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Conserved domains on  [gi|2130317402|gb|KAH7560493|]
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hypothetical protein JRO89_XS10G0030700 [Xanthoceras sorbifolium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03109 PLN03109
ETHYLENE-INSENSITIVE3-like3 protein; Provisional
 2286-2886 0e+00

ETHYLENE-INSENSITIVE3-like3 protein; Provisional


:

Pssm-ID: 215581  Cd Length: 599  Bit Score: 1017.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2286 LAMKEEIVKSSSDIEVDDIRCGNIAEKDVSDEEIDSDELERRMWKDRIKLKRIKEREKLVAEQAAEKQKPKQTSDQARRK 2365
Cdd:PLN03109     4 LAILAAELGDSSDFEVDGIRCDNLTENDVSDEEIEAEDLERRMWKDRIKLKRIKERQKKLQQAALEKSKPKKISDQARRK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2366 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEAECLVMDKADSSRN 2445
Cdd:PLN03109    84 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGASDNIRAWWKEKVKFDKNGPAAIAKYEAECLAMGEAESSGN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2446 gNSQSILQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPTGNEDWWVKLGLPQGQSPPYKKPHDLKKMWKVGVL 2525
Cdd:PLN03109   164 -NSQHSLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPSGNEDWWVKLGLPKGQSPPYKKPHDLKKMWKVGVL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2526 TAVIKHMSPDISKIRRHVRQSKCLQDKMTAKESAIWLGVLSREESLIQQPSSDNGTSGITETLPGGPANKKQPAISSDSD 2605
Cdd:PLN03109   243 TAVIKHMSPDFDKIRRHVRQSKCLQDKMTAKESLIWLGVLNREESLIRQPSSDNGTSGITETPRGGHEDRNKDAISSDSD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2606 YDVDGIDDGVGSVSSKDDRRSQSLDV-EPVSSLRNATSRSVQDREQQDKKRRRKGPREKPSRADQHPYMSvNEHPQDEPR 2684
Cdd:PLN03109   323 YDVDGLEDAPGSVSSKDDRRNLQPVAqEPERARDDAPNQVVPDKEKTKKPRKRKRPRGRSTVAEQEVEVT-QEHPPAESR 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2685 QILPDINNTDVPLIDYNMHGNQLENNTATALRSLERVPEGQSQIAASDFKQFSTVAPANVISTqSTYMDGRPMLYPMVQN 2764
Cdd:PLN03109   402 NALPDMNHVDAQGMEYQITGTSHENDTVTALQALGNGQEGFHLLPPAEFNNYNSNPSANANPS-SIYVGGRPLLYPNNDN 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2765 TELHDGATY-NLYNPSLEFGHSHDGQDSQMDMNVSQVRP----------EDGVHVPALRRNENEITNGDLHHYMKDTFPS 2833
Cdd:PLN03109   481 SELHSGNSYpGFYNPSSVYQHNPDKQPLPLSIMDHQVPPpgtgaladssSYRLHILGLSGNSNTIVGGELQQLMSDPFPG 560

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2130317402 2834 DqdrpvdnQFGSPLGSFAMDFGDFSSPFnlgmsgtSTYEELWAEEDLIEYFGA 2886
Cdd:PLN03109   561 E-------QDGSPFEGLPFDYGGFSSPF-------PDIDDLLDDDDLIQYFGA 599
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 507-1074 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: 583.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  507 RVTQNKTLYTWINEEGAVVSRRTYRELHANASLISHKLLtsekPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVL 586
Cdd:cd05931      4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ----AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  587 PPdplqRGGQALLKIENIAKSCNAVAILSTVGYHSAVRAGSVknlilltgkngkTTGRWPNLPWLHTDswikysknLQAE 666
Cdd:cd05931     80 PP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVD--------LLPD 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  667 NKADS---AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVS 743
Cdd:cd05931    136 TSAADwppPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYS 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 GGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstARNYDLSSMIFLMVAAEPVRQITLKRFIE 823
Cdd:cd05931    216 GGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDED--LEGLDLSSWRVALNGAEPVRPATLRRFAE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  824 LTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFV-------------------DWQGRVCCGYVdpnDPDVDIRIAN 884
Cdd:cd05931    294 AFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVD 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  885 PETGEEIkESGKEGEIWISSSSAGIGYWGREELSQKTFKNELPDyPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRN 964
Cdd:cd05931    371 PETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRN 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  965 IYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEV--RDAKTVDKEVVEKIKTRVAEEHGV 1042
Cdd:cd05931    449 HYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGV 515

                          570       580       590
                   ....*....|....*....|....*....|..
gi 2130317402 1043 TVASVKLIKPRTISKTTSGKIKRFECLKQFVD 1074
Cdd:cd05931    516 APADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
catalase_like super family cl09506
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 1699-2032 5.61e-129

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.


The actual alignment was detected with superfamily member cd08151:

Pssm-ID: 471888  Cd Length: 328  Bit Score: 408.74  E-value: 5.61e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1699 EEMDMKYKKIVGNLSANLAATTLKVKSRYFHRIGVGGKGQLKIYDKIQgLPDHNIFHPGKSYPVIVRHSNSLSADDDARI 1778
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1779 DARGAAIRILSDDVGSggstPPLLDLTLKTGKAFYARTIADFATWLVCGLAAREEHVKRV-PRVRDAVWMSL-RNADSFT 1856
Cdd:cd08151     80 DGRGAALRFLNAGDDD----AGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYT 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1857 ELHYYSNICRLFRFTDGQEMYVKFKLRPFDETISEDSGKVEPVGILPPDTGAIPRDENDTRPLLFLADDFKRRVESPtGV 1936
Cdd:cd08151    156 DLHYYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GV 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1937 RYIFQLQVQPVPQDEatRDIALDCTKPWDETEFPYIDIGEISIDQNLTKEESEKMEFNPYvRCHEIDVIPASSCSQ-SAS 2015
Cdd:cd08151    235 RYRLQIQLREVSDDA--TAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNPG-NTPESLGLPLAYCADdYAS 311

                          330
                   ....*....|....*..
gi 2130317402 2016 IDHGRSLIYEICQHLRN 2032
Cdd:cd08151    312 LGHLRSLVYEISQRLRK 328
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1271-1681 7.40e-22

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: 103.68  E-value: 7.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1271 GYPWLdymfSLAFAPLTWILCIFSTCISITFFGNSF------------LRPNytlspEVSIWSADFVKWWALYKAHEISS 1338
Cdd:TIGR02353   24 GYNWL----YEALDDVSWLYLRAVALVFAVPVGRLGfaiaakwllvgrWKPG-----TYPIWGSTYLRFWTVKRLVDAAP 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1339 kvfAVYLRGTVFLNCWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGVLVQGHEVRNGVLSFLPIRIGRNSSV 1416
Cdd:TIGR02353   95 ---TVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1417 GPFAVIQKGSIIGDEA--DAGAAVQ-NEAI---YHFIGIymvsflstlAAAIIYFLYIRVAEK--PTSPqhfAFLCISGA 1488
Cdd:TIGR02353  170 GTRSTLDIDTSIGDGAqlGHGSALQgGQSIpdgERWHGS---------PAQKTGADYRKVQPArpYTVR---RRLYVAGA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1489 FHWMPFTMIAYATMFAnVPSNPAYFAISVSIAYLLHG----LVLSFLTS---IVAQFLAgkqdekqSQMKTWLSN----- 1556
Cdd:TIGR02353  238 LFVVFVLLPPLAFLFA-IPVAITFDEIDWTLGPDMVGfilaLVLTFVALagfIAYTVLL-------LAAVRLLLNlvlkp 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1557 -RITIACHLRFAK---------------LLSGTEAFCMYFRLLGAEVGKHCSIRAINpVSCPKQISIGAGVHLGDFSRII 1620
Cdd:TIGR02353  310 gRYYVHSGFYYQAwtvqqlmdnsrvllfPLYASSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGLLMG 388

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1621 SGFYSSTGFISGKVEVQENSVIGSQSLILPNSVVQKDVILGALSVAPAHSVLQQGGVYVGS 1681
Cdd:TIGR02353  389 NARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 6.89e-15

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 71.41  E-value: 6.89e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402   26 IVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSAPVIFDLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN super family cl34196
Monoamine oxidase [Amino acid transport and metabolism];
21-265 1.74e-14

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: 78.81  E-value: 1.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLE-------KFHTVSGmcesvEIEGKMYDLGGQVLAANSaPVIFDLAKET 93
Cdd:COG1231      7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   94 GSELEEM-DAHKLALIDASTGEYQDNKVADDYVSVISLTLELQDKAKDSGRIGVHAVSDIasDLTP--TYLESHGLKSVP 170
Cdd:COG1231     80 GLPLEPFpNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  171 KSVAYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRFKGGYMNFWRKLSEYLPIEVHCNTEVLAIRRnSATN 243
Cdd:COG1231    158 RRLLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQ-DGDG 231

                          250       260
                   ....*....|....*....|..
gi 2130317402  244 VSVDVknvnGECEVMEFDKIII 265
Cdd:COG1231    232 VTVTT----DDGGTVRADAVIV 249
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2090-2293 4.12e-11

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: 68.62  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2090 LLQTILPyFLMGLVIFPPLNCLLFLKETKKLPLHWLLPLF----WLSSGLLAALACVVAKWVLVGKKKENETvKIWSAGV 2165
Cdd:TIGR02353  484 NLRIILP-FLLVQWAMLFALVVLDLQALDDYTEWGAVALLaaliLMAVGVGAFLILVERKWLVFGRLKPQEH-PLWSPFV 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2166 FV-DTTWQAFRTLVGDYFMEITGGSFLFMVWMKLMGSEIDldqGGGYVDSmgaVLNPE--MVEIERGGCVGREALLFGHI 2242
Cdd:TIGR02353  562 WLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKIG---RGVYIDG---TDLTErdLVTIGDDSTLNEGSVIQTHL 635

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 2243 YEgdDGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMKEEIV 2293
Cdd:TIGR02353  636 FE--DRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1126-1187 5.53e-09

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: 54.49  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1126 EFLIRLVSEQTGIPSSNISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISD 1187
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
PLN03109 PLN03109
ETHYLENE-INSENSITIVE3-like3 protein; Provisional
 2286-2886 0e+00

ETHYLENE-INSENSITIVE3-like3 protein; Provisional


Pssm-ID: 215581  Cd Length: 599  Bit Score: 1017.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2286 LAMKEEIVKSSSDIEVDDIRCGNIAEKDVSDEEIDSDELERRMWKDRIKLKRIKEREKLVAEQAAEKQKPKQTSDQARRK 2365
Cdd:PLN03109     4 LAILAAELGDSSDFEVDGIRCDNLTENDVSDEEIEAEDLERRMWKDRIKLKRIKERQKKLQQAALEKSKPKKISDQARRK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2366 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEAECLVMDKADSSRN 2445
Cdd:PLN03109    84 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGASDNIRAWWKEKVKFDKNGPAAIAKYEAECLAMGEAESSGN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2446 gNSQSILQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPTGNEDWWVKLGLPQGQSPPYKKPHDLKKMWKVGVL 2525
Cdd:PLN03109   164 -NSQHSLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPSGNEDWWVKLGLPKGQSPPYKKPHDLKKMWKVGVL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2526 TAVIKHMSPDISKIRRHVRQSKCLQDKMTAKESAIWLGVLSREESLIQQPSSDNGTSGITETLPGGPANKKQPAISSDSD 2605
Cdd:PLN03109   243 TAVIKHMSPDFDKIRRHVRQSKCLQDKMTAKESLIWLGVLNREESLIRQPSSDNGTSGITETPRGGHEDRNKDAISSDSD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2606 YDVDGIDDGVGSVSSKDDRRSQSLDV-EPVSSLRNATSRSVQDREQQDKKRRRKGPREKPSRADQHPYMSvNEHPQDEPR 2684
Cdd:PLN03109   323 YDVDGLEDAPGSVSSKDDRRNLQPVAqEPERARDDAPNQVVPDKEKTKKPRKRKRPRGRSTVAEQEVEVT-QEHPPAESR 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2685 QILPDINNTDVPLIDYNMHGNQLENNTATALRSLERVPEGQSQIAASDFKQFSTVAPANVISTqSTYMDGRPMLYPMVQN 2764
Cdd:PLN03109   402 NALPDMNHVDAQGMEYQITGTSHENDTVTALQALGNGQEGFHLLPPAEFNNYNSNPSANANPS-SIYVGGRPLLYPNNDN 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2765 TELHDGATY-NLYNPSLEFGHSHDGQDSQMDMNVSQVRP----------EDGVHVPALRRNENEITNGDLHHYMKDTFPS 2833
Cdd:PLN03109   481 SELHSGNSYpGFYNPSSVYQHNPDKQPLPLSIMDHQVPPpgtgaladssSYRLHILGLSGNSNTIVGGELQQLMSDPFPG 560

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2130317402 2834 DqdrpvdnQFGSPLGSFAMDFGDFSSPFnlgmsgtSTYEELWAEEDLIEYFGA 2886
Cdd:PLN03109   561 E-------QDGSPFEGLPFDYGGFSSPF-------PDIDDLLDDDDLIQYFGA 599
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 507-1074 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: 583.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  507 RVTQNKTLYTWINEEGAVVSRRTYRELHANASLISHKLLtsekPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVL 586
Cdd:cd05931      4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ----AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  587 PPdplqRGGQALLKIENIAKSCNAVAILSTVGYHSAVRAGSVknlilltgkngkTTGRWPNLPWLHTDswikysknLQAE 666
Cdd:cd05931     80 PP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVD--------LLPD 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  667 NKADS---AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVS 743
Cdd:cd05931    136 TSAADwppPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYS 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 GGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstARNYDLSSMIFLMVAAEPVRQITLKRFIE 823
Cdd:cd05931    216 GGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDED--LEGLDLSSWRVALNGAEPVRPATLRRFAE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  824 LTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFV-------------------DWQGRVCCGYVdpnDPDVDIRIAN 884
Cdd:cd05931    294 AFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVD 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  885 PETGEEIkESGKEGEIWISSSSAGIGYWGREELSQKTFKNELPDyPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRN 964
Cdd:cd05931    371 PETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRN 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  965 IYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEV--RDAKTVDKEVVEKIKTRVAEEHGV 1042
Cdd:cd05931    449 HYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGV 515

                          570       580       590
                   ....*....|....*....|....*....|..
gi 2130317402 1043 TVASVKLIKPRTISKTTSGKIKRFECLKQFVD 1074
Cdd:cd05931    516 APADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
EIN3 pfam04873
Ethylene insensitive 3; Ethylene insensitive 3 (EIN3) proteins are a family of plant ...
 2322-2569 1.22e-163

Ethylene insensitive 3; Ethylene insensitive 3 (EIN3) proteins are a family of plant DNA-binding proteins that regulate transcription in response to the gaseous plant hormone ethylene, and are essential for ethylene-mediated responses including the triple response, cell growth inhibition, and accelerated senescence.


Pssm-ID: 398508  Cd Length: 252  Bit Score: 504.68  E-value: 1.22e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2322 DELERRMWKDRIKLKRIKEREK---LVAEQAAEKQKPKQTSDQARRKKMSRAQDGILKYMLKLMEVCKARGFVYGIIPEK 2398
Cdd:pfam04873    1 EDLEKRMWKDRMLLKRLKERQKgglGAQLASLGKSKPKQPSEQARRKKMSRAQDGILKYMLKMMEVCNAQGFVYGIIPEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2399 GKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEAECLVMDKADSSRNGNSQSILQDLQDATLGSLLSSLMQHCDPPQRKY 2478
Cdd:pfam04873   81 GKPVSGSSDNLRAWWKEKVRFDRNGPAAIAKYQADNLLAGGSSPRAGCSGPHSLHELQDTTLGSLLSALMQHCDPPQRRF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2479 PLEKGVPPPWWPTGNEDWWVKLGLPQGQS-PPYKKPHDLKKMWKVGVLTAVIKHMSPDISKIRRHVRQSKCLQDKMTAKE 2557
Cdd:pfam04873  161 PLEKGVPPPWWPTGKELWWGQLGLPKDQGpPPYRKPHDLKKAWKVSVLTAVIKHMSPDISKIRKLVRQSKCLQDKMTAKE 240

                          250
                   ....*....|..
gi 2130317402 2558 SAIWLGVLSREE 2569
Cdd:pfam04873  241 SDTWLAVLNQEE 252
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1699-2032 5.61e-129

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: 408.74  E-value: 5.61e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1699 EEMDMKYKKIVGNLSANLAATTLKVKSRYFHRIGVGGKGQLKIYDKIQgLPDHNIFHPGKSYPVIVRHSNSLSADDDARI 1778
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1779 DARGAAIRILSDDVGSggstPPLLDLTLKTGKAFYARTIADFATWLVCGLAAREEHVKRV-PRVRDAVWMSL-RNADSFT 1856
Cdd:cd08151     80 DGRGAALRFLNAGDDD----AGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYT 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1857 ELHYYSNICRLFRFTDGQEMYVKFKLRPFDETISEDSGKVEPVGILPPDTGAIPRDENDTRPLLFLADDFKRRVESPtGV 1936
Cdd:cd08151    156 DLHYYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GV 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1937 RYIFQLQVQPVPQDEatRDIALDCTKPWDETEFPYIDIGEISIDQNLTKEESEKMEFNPYvRCHEIDVIPASSCSQ-SAS 2015
Cdd:cd08151    235 RYRLQIQLREVSDDA--TAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNPG-NTPESLGLPLAYCADdYAS 311

                          330
                   ....*....|....*..
gi 2130317402 2016 IDHGRSLIYEICQHLRN 2032
Cdd:cd08151    312 LGHLRSLVYEISQRLRK 328
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 511-1072 6.64e-93

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 314.57  E-value: 6.64e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  511 NKTLYTWINEE---GAVVSRRTYRELHANASLISHKLLTsekpVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpVPVLP 587
Cdd:PRK05850    16 DDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRR----HGSTGDRAVILAPQGLEYIVAFLGALQA----GLIAV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  588 PDPLQRGGQALLKIENIAKSCNAVAILSTvgyhSAVrAGSVknlilltGKNGKTTGRWPNLPWLHTDSWikyskNLQAEN 667
Cdd:PRK05850    88 PLSVPQGGAHDERVSAVLRDTSPSVVLTT----SAV-VDDV-------TEYVAPQPGQSAPPVIEVDLL-----DLDSPR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  668 KADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY------RSTSNTILVSWLPQYHDMGLIGGLFTAL 741
Cdd:PRK05850   151 GSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPI 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLeSDKSTArNYDLSSMIFLMVAAEPVRQITLKRF 821
Cdd:PRK05850   231 LGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKT-SDDDMA-GLDLGGVLGIISGSERVHPATLKRF 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 IELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDWQ------GRV--C--------CGYVDPNDPDVdiRIANP 885
Cdd:PRK05850   309 ADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPPESVRFDyeklsaGHAkrCetgggtplVSYGSPRSPTV--RIVDP 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  886 ETGEEIKeSGKEGEIWISSSSAGIGYWGREELSQKTFKNEL----PDYPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVA 961
Cdd:PRK05850   387 DTCIECP-AGTVGEIWVHGDNVAAGYWQKPEETERTFGATLvdpsPGTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVD 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  962 GRNIYSADIEKTVEsssELLRpGCCAVVGVPEevlstkgisvsDSSDQvgLVVIAEVRDAKTVDKEVVEK---IKTRVA- 1037
Cdd:PRK05850   466 GRNHYPDDIEATIQ---EITG-GRVAAISVPD-----------DGTEK--LVAIIELKKRGDSDEEAMDRlrtVKREVTs 528

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 2130317402 1038 ---EEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQF 1072
Cdd:PRK05850   529 aisKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 488-1077 5.98e-86

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: 296.25  E-value: 5.98e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  488 VEFPDLSSLDGYLKHWGthRVTQNKTLYTWIN---EEGAVVSRRTYRELHANASLISHKLltseKPVIKPGDRVLLVYVP 564
Cdd:NF038339    12 IRFPDGATLVDHVERNA--RERADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRVAILAPQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  565 GLDFVDCFFGCLRARVLPVPVLPPDPLQRGGqallKIENIAKSCNAVAILSTVGYHSAVR-------AGSVKNLILLTGk 637
Cdd:NF038339    86 GLDYVVSFFAAIYAGNIAVPLFDPDEPGHTD----RLHAVLGDCKPSAILTATSSAEGVRkffrslpAKERPRVIAVDA- 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  638 ngkttgrwpnLPWLHTDSWIKysknlqaenkadsAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTS 717
Cdd:NF038339   161 ----------VPDSVGSTWVR-------------PDADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDE 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  718 NTILVSWLPQYHDMGLIGGLFTALvsGGSSVLF-SPMTFIKNPLLWLETM---SKYQATHSAGPNFAFE-LMLRRLESDK 792
Cdd:NF038339   218 NSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWIRELaavSDGAGTFAAAPNFAFEhAAARGLPKEG 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  793 STarnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKP--IFVDW----QGR- 865
Cdd:NF038339   296 EP---LDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReelnAGRi 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  866 -------------VCCGYVDPNDPDVdirIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNEL------ 926
Cdd:NF038339   373 vevdpdapnavaqVSCGYVARSQWAV---IVDPETGTELPD-GQVGEIWLHGNNIGTGYWGRPEETEETFHNKLksrlee 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  927 -------PDypGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGV-----PEE 994
Cdd:NF038339   449 gshaegaPE--DANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVpanqlPAE 526

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  995 VL--STKGISVS--DSSDQvgLVVIAEvRDA---KTVDKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFE 1067
Cdd:NF038339   527 VFenSHSGLKYDadDSSEQ--LVIVAE-RAPgagKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRA 603

                          650
                   ....*....|
gi 2130317402 1068 CLKQFVDGTL 1077
Cdd:NF038339   604 CKAAYIDGTL 613
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 654-1074 4.04e-84

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: 290.40  E-value: 4.04e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSKNLQAENKADSAEPET-DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMG 732
Cdd:NF040633   177 ESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMG 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  733 LIGGLFtALVSGGSSVLFSPMTFIKNPLLWLETMSKYQ---ATHSAGPNFAFELMLRRleSDKSTARNYDLSSMIFLMVA 809
Cdd:NF040633   257 IILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSRREddvNVYTVVPNFALELAARY--ANPEEGEDLDLSAVDGIIIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDW------QGRVCCgyVDPNDPDV----- 878
Cdd:NF040633   334 SEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFdrealaEGRAVE--VAEDSENAvpfas 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 --------DIRIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNELP----------DYPGRIYTRTGDL 940
Cdd:NF040633   412 ngqvvrpqVLAIVDPETGQELPD-GTVGEIWVHGDNMAAGYLDREEETAETFRNTLGerlaensraeGAPEDNWMATGDL 490

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  941 GRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEVRD 1020
Cdd:NF040633   491 GVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPGD-------------DVEKLVILAERDD 557

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402 1021 AKTV--DKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQFVD 1074
Cdd:NF040633   558 EADEsgDAEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 527-1078 1.04e-81

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: 277.85  E-value: 1.04e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGQA-----LLKI 601
Cdd:COG0318     24 RLTYAELDARARRLAAALRALG---VGPGDRVALLLPNSPEFVVAFLAALRA---------------GAVVvplnpRLTA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  602 ENIAkscnavAILStvgyHSAVRAgsvknliLLTgkngkttgrwpnlpwlhtdswikysknlqaenkadsaepetddlCF 681
Cdd:COG0318     86 EELA------YILE----DSGARA-------LVT--------------------------------------------AL 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMtfikNPLL 761
Cdd:COG0318    105 ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF----DPER 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  762 WLETMSKYQATHSAGPNFAFELMLRRLEsdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLsqeVMAPGYGL 841
Cdd:COG0318    181 VLELIERERVTVLFGVPTMLARLLRHPE-----FARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYGL 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  842 AENCVFVSCAYGQGKPIFVDWQGRVCcgyvdpndPDVDIRIANPEtGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKT 921
Cdd:COG0318    250 TETSPVVTVNPEDPGERRPGSVGRPL--------PGVEVRIVDED-GRELPP-GEVGEIVVRGPNVMKGYWNDPEATAEA 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  922 FKNElpdypgriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVLstkg 1000
Cdd:COG0318    320 FRDG--------WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKW---- 384

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1001 isvsdssDQVGLVVIAeVRDAKTVD-KEVVEKIKTRVAeEHGVtvasvklikPRTIS------KTTSGKIKRFECLKQFV 1073
Cdd:COG0318    385 -------GERVVAFVV-LRPGAELDaEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGKIDRRALRERYA 446


                   ....*
gi 2130317402 1074 DGTLN 1078
Cdd:COG0318    447 AGALE 451
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
660-1072 3.78e-72

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 254.41  E-value: 3.78e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  660 SKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSN------TILVSWLPQYHDMGL 733
Cdd:NF038337   146 SLDLDGPNSPSIRISDAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGL 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  734 IGGLFTALVSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRlESDKSTArNYDLSSMIFLMVAAEPV 813
Cdd:NF038337   226 VLGVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRK-TTDADLA-GLDLGNVIGIVSGAERI 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  814 RQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDWQ----------------GRVCCGYVDPNDPD 877
Cdd:NF038337   304 HPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEpeklsegsaqrceartGSPLLSYGTPTSPT 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  878 VdiRIANPETGEEIKeSGKEGEIWISSSSAGIGYWGREELSQKTFKNEL----PDYPGRIYTRTGDLGRIIDGKLFITGR 953
Cdd:NF038337   384 V--RIVDPDTCIECP-AGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLanpsPGTPEGPWLRTGDLGFISEDEMFIVGR 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  954 IKDLIIVAGRNIYSADIEKTVESsselLRPGCCAVVGVPeevlstkgisvSDSSDQvgLVVIAEVRDAKTVDKEVVEK-- 1031
Cdd:NF038337   461 MKDLLIVYGRNHYPEDIESTVQE----ITGGRVAAISVP-----------VDETEK--LVTIIELKKRGDSDEEAMRKld 523

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2130317402 1032 -----IKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQF 1072
Cdd:NF038337   524 avknnVTAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQY 569
AMP-binding pfam00501
AMP-binding enzyme;
527-961 3.99e-63

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 222.57  E-value: 3.99e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLtseKPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQRggqallkIENIAK 606
Cdd:pfam00501   21 RLTYRELDERANRLAAGLR---ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE-------LAYILE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  607 SCNAVAILstvgyhsAVRAGSVKNLILLTGKNGKTTGRwpnlPWLHTDSWIKYSKNLQAENKADSAEPET-----DDLCF 681
Cdd:pfam00501   91 DSGAKVLI-------TDDALKLEELLEALGKLEVVKLV----LVLDRDPVLKEEPLPEEAKPADVPPPPPpppdpDDLAY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRS----TSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTFiK 757
Cdd:pfam00501  160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-L 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  758 NPLLWLETMSKYQATHSAGPNFAFELMLrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELtLPFGLSQevmap 837
Cdd:pfam00501  239 DPAALLELIERYKVTVLYGVPTLLNMLL-----EAGAPKRALLSSLRLVLSGGAPLPPELARRFREL-FGGALVN----- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  838 GYGLAENCVFVSCAYgqgkPIFVDWQGRVCCGYVDPNdpdVDIRIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREEL 917
Cdd:pfam00501  308 GYGLTETTGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPVPP-GEPGELCVRGPGVMKGYLNDPEL 379

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2130317402  918 SQKTFKnelpdyPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVA 961
Cdd:pfam00501  380 TAEAFD------EDGWY-RTGDLGRRDeDGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 529-971 2.93e-29

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: 123.14  E-value: 2.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLTSEKpvIKPGDRVLlVYVP-GLDFVDCFFGCLRArvlpvpvlppdplqrgGQALL-------- 599
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKA----------------GAAYVpldpaypa 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 -KIENIAKSCNAVAILSTVGyHSAVRAGSVKNLILLTGKNGKTTGRWPNLPWLhtdswikysknlqaenkadSAEPETDD 678
Cdd:TIGR01733   62 eRLAFILEDAGARLLLTDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------DAPSGPDD 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  679 LCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIgGLFTALVSGGSSVLFSPMTFIKN 758
Cdd:TIGR01733  122 LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDD 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  759 PLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARnydlssmiFLMVAAEPVRQITLKRFIELtlpfgLSQEVMAPG 838
Cdd:TIGR01733  201 AALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLR--------LVILGGEALTPALVDRWRAR-----GPGARLINL 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  839 YGLAENCVFVSCAYGQGKPifVDWQGRVCCGY---------VDPNDPDVDIrianpetgeeikesGKEGEIWISSSSAGI 909
Cdd:TIGR01733  268 YGPTETTVWSTATLVDPDD--APRESPVPIGRplantrlyvLDDDLRPVPV--------------GVVGELYIGGPGVAR 331

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  910 GYWGREELSQKTFKNE--LPDYPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:TIGR01733  332 GYLNRPELTAERFVPDpfAGGDGARLY-RTGDLVRYLpDGNLEFLGRIDDQVKIRGYRIELGEIE 395
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1271-1681 7.40e-22

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: 103.68  E-value: 7.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1271 GYPWLdymfSLAFAPLTWILCIFSTCISITFFGNSF------------LRPNytlspEVSIWSADFVKWWALYKAHEISS 1338
Cdd:TIGR02353   24 GYNWL----YEALDDVSWLYLRAVALVFAVPVGRLGfaiaakwllvgrWKPG-----TYPIWGSTYLRFWTVKRLVDAAP 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1339 kvfAVYLRGTVFLNCWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGVLVQGHEVRNGVLSFLPIRIGRNSSV 1416
Cdd:TIGR02353   95 ---TVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1417 GPFAVIQKGSIIGDEA--DAGAAVQ-NEAI---YHFIGIymvsflstlAAAIIYFLYIRVAEK--PTSPqhfAFLCISGA 1488
Cdd:TIGR02353  170 GTRSTLDIDTSIGDGAqlGHGSALQgGQSIpdgERWHGS---------PAQKTGADYRKVQPArpYTVR---RRLYVAGA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1489 FHWMPFTMIAYATMFAnVPSNPAYFAISVSIAYLLHG----LVLSFLTS---IVAQFLAgkqdekqSQMKTWLSN----- 1556
Cdd:TIGR02353  238 LFVVFVLLPPLAFLFA-IPVAITFDEIDWTLGPDMVGfilaLVLTFVALagfIAYTVLL-------LAAVRLLLNlvlkp 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1557 -RITIACHLRFAK---------------LLSGTEAFCMYFRLLGAEVGKHCSIRAINpVSCPKQISIGAGVHLGDFSRII 1620
Cdd:TIGR02353  310 gRYYVHSGFYYQAwtvqqlmdnsrvllfPLYASSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGLLMG 388

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1621 SGFYSSTGFISGKVEVQENSVIGSQSLILPNSVVQKDVILGALSVAPAHSVLQQGGVYVGS 1681
Cdd:TIGR02353  389 NARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 6.89e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 71.41  E-value: 6.89e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402   26 IVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSAPVIFDLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
21-265 1.74e-14

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 78.81  E-value: 1.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLE-------KFHTVSGmcesvEIEGKMYDLGGQVLAANSaPVIFDLAKET 93
Cdd:COG1231      7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   94 GSELEEM-DAHKLALIDASTGEYQDNKVADDYVSVISLTLELQDKAKDSGRIGVHAVSDIasDLTP--TYLESHGLKSVP 170
Cdd:COG1231     80 GLPLEPFpNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  171 KSVAYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRFKGGYMNFWRKLSEYLPIEVHCNTEVLAIRRnSATN 243
Cdd:COG1231    158 RRLLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQ-DGDG 231

                          250       260
                   ....*....|....*....|..
gi 2130317402  244 VSVDVknvnGECEVMEFDKIII 265
Cdd:COG1231    232 VTVTT----DDGGTVRADAVIV 249
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 22-94 7.87e-14

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: 76.79  E-value: 7.87e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402   22 TRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSaPVIFDLAKETG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2090-2293 4.12e-11

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: 68.62  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2090 LLQTILPyFLMGLVIFPPLNCLLFLKETKKLPLHWLLPLF----WLSSGLLAALACVVAKWVLVGKKKENETvKIWSAGV 2165
Cdd:TIGR02353  484 NLRIILP-FLLVQWAMLFALVVLDLQALDDYTEWGAVALLaaliLMAVGVGAFLILVERKWLVFGRLKPQEH-PLWSPFV 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2166 FV-DTTWQAFRTLVGDYFMEITGGSFLFMVWMKLMGSEIDldqGGGYVDSmgaVLNPE--MVEIERGGCVGREALLFGHI 2242
Cdd:TIGR02353  562 WLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKIG---RGVYIDG---TDLTErdLVTIGDDSTLNEGSVIQTHL 635

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 2243 YEgdDGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMKEEIV 2293
Cdd:TIGR02353  636 FE--DRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
PRK07233 PRK07233
hypothetical protein; Provisional
 23-270 1.92e-10

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 66.06  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEG----KMYdlggQVLAANSAPvIFDLAKETGSEle 98
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGGlpieRFY----HHIFKSDEA-LLELLDELGLE-- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   99 emdaHKLALIDASTGEYQDNKvaddyvsVISLT----------LELQDKAkdsgRIGVHAV-SDIASDLTP-------TY 160
Cdd:PRK07233    73 ----DKLRWRETKTGYYVDGK-------LYPLGtplellrfphLSLIDKF----RLGLLTLlARRIKDWRAldkvpaeEW 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  161 LESHGLKSVPKSV-------AYGYTASgygfvqDMPYAYI------HEFTRTSMAGKIR-RFKGGYMNFWRKLSEYLPI- 225
Cdd:PRK07233   138 LRRWSGEGVYEVFwepllesKFGDYAD------DVSAAWLwsrikrRGNRRYSLFGEKLgYLEGGFATLIDALAEAIEAr 211

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2130317402  226 --EVHCNTEVLAIRRNSATnvsvdVKNVNGECEVMEFDKIIISGSFP 270
Cdd:PRK07233   212 ggEIRLGTPVTSVVIDGGG-----VTGVEVDGEEEDFDAVISTAPPP 253
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1126-1187 5.53e-09

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: 54.49  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1126 EFLIRLVSEQTGIPSSNISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISD 1187
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 32-283 9.35e-09

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: 60.58  E-value: 9.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   32 SGLSAAYALTKLGyRNVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLaANSAPVIFDLAKETGSELEE--MDAHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGLEDRLvlPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  110 ASTGEYQDNKVADDYVSVISL-----TLELQDKAKDSGRIGVHAVSDIASDLTPTYLES---HGLKSVPKSVAYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRLGLAALASDALDEFDLDDFSLAESllfLGRRGPGDVEVWDRLIDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRFKGGYMNFWRKLSEYLPI-EVHCNTEVLAIRRNSATnV 244
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLGgDVRLNTRVRSIDREGDG-V 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2130317402  245 SVDVKNvngeCEVMEFDKIIISGSFPMRNGKIYRLPLSK 283
Cdd:pfam01593  238 TVTLTD----GEVIEADAVIVTVPLGVLKRILFTPPLPP 272
PRK07208 PRK07208
hypothetical protein; Provisional
 26-75 1.94e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 59.52  E-value: 1.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2130317402   26 IVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVSGMCESVEIEGKMYDLGG 75
Cdd:PRK07208     9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1584-1671 4.90e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 54.11  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSIRAINPVSCPKQISIGAGVHLGDFSRIISGFY-----SSTGFISGKVEVQENSVIGSQSLILPNSVVQKDV 1658
Cdd:COG0110     27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGA 106

                           90
                   ....*....|....*..
gi 2130317402 1659 ILGALSVA----PAHSV 1671
Cdd:COG0110    107 VVGAGSVVtkdvPPYAI 123
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1119-1191 1.29e-07

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: 51.01  E-value: 1.29e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130317402 1119 MSNKDIVEFLIRLVSEQTGIPSSNISATGSLVS-YGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISDLANF 1191
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADY 74
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1586-1671 1.28e-06

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: 49.38  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1586 EVGKHCSIRAINPVSCPKQISIGAGVHLGDFSRIISGFYS--------STGFISGKVEVQENSVIGSQSLILPNSVVQKD 1657
Cdd:cd04647      3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                           90
                   ....*....|....*...
gi 2130317402 1658 VILGALSVA----PAHSV 1671
Cdd:cd04647     83 AVVGAGSVVtkdvPPNSI 100
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 2612-2850 1.71e-05

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 50.28  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2612 DDGVGSVSSKDDRRSQSLDVEpVSSLRNATSRSVQDREQQDKKRRRKGPREKPS----RADQHPYMSVNEHPQDEPRqil 2687
Cdd:TIGR01642   68 YSSVRRSRDRPRRRSRSVRSI-EQHRRRLRDRSPSNQWRKDDKKRSLWDIKPPGyelvTADQAKASQVFSVPGTAPR--- 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2688 PDINNTDVPLIDYNMHG----NQLENNTATALRSL--ERVPEGQSQIAASDF--KQFSTVA-----PANVISTQSTYMDG 2754
Cdd:TIGR01642  144 PAMTDPEKLLAEGSIITplpvLPYQQQATRQARRLyvGGIPPEFVEEAVVDFfnDLMIATGyhkaeDGKHVSSVNINKEK 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2755 RPMLYPM--VQNTELH---DGATYNlyNPSLEFGHSHDGQDS-QMDMNVSQVRPEDGVHVPALRRN-------ENEITNG 2821
Cdd:TIGR01642  224 NFAFLEFrtVEEATFAmalDSIIYS--NVFLKIRRPHDYIPVpQITPEVSQKNPDDNAKNVEKLVNsttvldsKDRIYIG 301

                          250       260
                   ....*....|....*....|....*....
gi 2130317402 2822 DLHHYMKDtfpsDQDRPVDNQFGsPLGSF 2850
Cdd:TIGR01642  302 NLPLYLGE----DQIKELLESFG-DLKAF 325
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
2218-2289 2.24e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.79  E-value: 2.24e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402 2218 VLNPEMVEIERGGCVGREALLFGHIYEGDD---GKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMK 2289
Cdd:COG0110     42 IDDPGGITIGDNVLIGPGVTILTGNHPIDDpatFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTK 116
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 21-96 7.11e-05

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: 48.29  E-value: 7.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYR---NVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSaPVIFDLAKETGSE 96
Cdd:TIGR00562    2 KKHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLGLE 79
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 2219-2312 2.19e-04

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 42.98  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2219 LNPEMVEIERGGCVGREALLFG--HIYEGDDGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMKeeivkss 2296
Cdd:cd05825     19 YNLAPVTIGSDACISQGAYLCTgsHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVR------- 91

                           90
                   ....*....|....*.
gi 2130317402 2297 sDIEVDDIRCGNIAEK 2312
Cdd:cd05825     92 -DLPAWTVYAGNPAVP 106
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1124-1191 1.53e-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: 39.93  E-value: 1.53e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  1124 IVEFLIRLVSEQTGIPSSN-ISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISDLANF 1191
Cdd:smart00823   13 LLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1379-1445 2.81e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 2.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402 1379 VSIGDGAVIAEGVlvqghevrngvlsflpiRIGRNSSVGPFAVIQKGSIIGDEADAGAAVqneAIYH 1445
Cdd:PRK00892   119 VSIGPNAVIGAGV-----------------VIGDGVVIGAGAVIGDGVKIGADCRLHANV---TIYH 165
 
Name Accession Description Interval E-value
PLN03109 PLN03109
ETHYLENE-INSENSITIVE3-like3 protein; Provisional
 2286-2886 0e+00

ETHYLENE-INSENSITIVE3-like3 protein; Provisional


Pssm-ID: 215581  Cd Length: 599  Bit Score: 1017.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2286 LAMKEEIVKSSSDIEVDDIRCGNIAEKDVSDEEIDSDELERRMWKDRIKLKRIKEREKLVAEQAAEKQKPKQTSDQARRK 2365
Cdd:PLN03109     4 LAILAAELGDSSDFEVDGIRCDNLTENDVSDEEIEAEDLERRMWKDRIKLKRIKERQKKLQQAALEKSKPKKISDQARRK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2366 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEAECLVMDKADSSRN 2445
Cdd:PLN03109    84 KMSRAQDGILKYMLKLMEVCKARGFVYGIIPEKGKPVSGASDNIRAWWKEKVKFDKNGPAAIAKYEAECLAMGEAESSGN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2446 gNSQSILQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPTGNEDWWVKLGLPQGQSPPYKKPHDLKKMWKVGVL 2525
Cdd:PLN03109   164 -NSQHSLQDLQDATLGSLLSSLMQHCDPPQRKYPLEKGVPPPWWPSGNEDWWVKLGLPKGQSPPYKKPHDLKKMWKVGVL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2526 TAVIKHMSPDISKIRRHVRQSKCLQDKMTAKESAIWLGVLSREESLIQQPSSDNGTSGITETLPGGPANKKQPAISSDSD 2605
Cdd:PLN03109   243 TAVIKHMSPDFDKIRRHVRQSKCLQDKMTAKESLIWLGVLNREESLIRQPSSDNGTSGITETPRGGHEDRNKDAISSDSD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2606 YDVDGIDDGVGSVSSKDDRRSQSLDV-EPVSSLRNATSRSVQDREQQDKKRRRKGPREKPSRADQHPYMSvNEHPQDEPR 2684
Cdd:PLN03109   323 YDVDGLEDAPGSVSSKDDRRNLQPVAqEPERARDDAPNQVVPDKEKTKKPRKRKRPRGRSTVAEQEVEVT-QEHPPAESR 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2685 QILPDINNTDVPLIDYNMHGNQLENNTATALRSLERVPEGQSQIAASDFKQFSTVAPANVISTqSTYMDGRPMLYPMVQN 2764
Cdd:PLN03109   402 NALPDMNHVDAQGMEYQITGTSHENDTVTALQALGNGQEGFHLLPPAEFNNYNSNPSANANPS-SIYVGGRPLLYPNNDN 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2765 TELHDGATY-NLYNPSLEFGHSHDGQDSQMDMNVSQVRP----------EDGVHVPALRRNENEITNGDLHHYMKDTFPS 2833
Cdd:PLN03109   481 SELHSGNSYpGFYNPSSVYQHNPDKQPLPLSIMDHQVPPpgtgaladssSYRLHILGLSGNSNTIVGGELQQLMSDPFPG 560

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2130317402 2834 DqdrpvdnQFGSPLGSFAMDFGDFSSPFnlgmsgtSTYEELWAEEDLIEYFGA 2886
Cdd:PLN03109   561 E-------QDGSPFEGLPFDYGGFSSPF-------PDIDDLLDDDDLIQYFGA 599
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 507-1074 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: 583.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  507 RVTQNKTLYTWINEEGAVVSRRTYRELHANASLISHKLLtsekPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVL 586
Cdd:cd05931      4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ----AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  587 PPdplqRGGQALLKIENIAKSCNAVAILSTVGYHSAVRAGSVknlilltgkngkTTGRWPNLPWLHTDswikysknLQAE 666
Cdd:cd05931     80 PP----TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVD--------LLPD 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  667 NKADS---AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVS 743
Cdd:cd05931    136 TSAADwppPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYS 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 GGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstARNYDLSSMIFLMVAAEPVRQITLKRFIE 823
Cdd:cd05931    216 GGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDED--LEGLDLSSWRVALNGAEPVRPATLRRFAE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  824 LTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFV-------------------DWQGRVCCGYVdpnDPDVDIRIAN 884
Cdd:cd05931    294 AFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVD 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  885 PETGEEIkESGKEGEIWISSSSAGIGYWGREELSQKTFKNELPDyPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRN 964
Cdd:cd05931    371 PETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT-DEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRN 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  965 IYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEV--RDAKTVDKEVVEKIKTRVAEEHGV 1042
Cdd:cd05931    449 HYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGV 515

                          570       580       590
                   ....*....|....*....|....*....|..
gi 2130317402 1043 TVASVKLIKPRTISKTTSGKIKRFECLKQFVD 1074
Cdd:cd05931    516 APADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
EIN3 pfam04873
Ethylene insensitive 3; Ethylene insensitive 3 (EIN3) proteins are a family of plant ...
 2322-2569 1.22e-163

Ethylene insensitive 3; Ethylene insensitive 3 (EIN3) proteins are a family of plant DNA-binding proteins that regulate transcription in response to the gaseous plant hormone ethylene, and are essential for ethylene-mediated responses including the triple response, cell growth inhibition, and accelerated senescence.


Pssm-ID: 398508  Cd Length: 252  Bit Score: 504.68  E-value: 1.22e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2322 DELERRMWKDRIKLKRIKEREK---LVAEQAAEKQKPKQTSDQARRKKMSRAQDGILKYMLKLMEVCKARGFVYGIIPEK 2398
Cdd:pfam04873    1 EDLEKRMWKDRMLLKRLKERQKgglGAQLASLGKSKPKQPSEQARRKKMSRAQDGILKYMLKMMEVCNAQGFVYGIIPEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2399 GKPVSGSSDNIRAWWKEKVKFDKNGPAAIAKYEAECLVMDKADSSRNGNSQSILQDLQDATLGSLLSSLMQHCDPPQRKY 2478
Cdd:pfam04873   81 GKPVSGSSDNLRAWWKEKVRFDRNGPAAIAKYQADNLLAGGSSPRAGCSGPHSLHELQDTTLGSLLSALMQHCDPPQRRF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2479 PLEKGVPPPWWPTGNEDWWVKLGLPQGQS-PPYKKPHDLKKMWKVGVLTAVIKHMSPDISKIRRHVRQSKCLQDKMTAKE 2557
Cdd:pfam04873  161 PLEKGVPPPWWPTGKELWWGQLGLPKDQGpPPYRKPHDLKKAWKVSVLTAVIKHMSPDISKIRKLVRQSKCLQDKMTAKE 240

                          250
                   ....*....|..
gi 2130317402 2558 SAIWLGVLSREE 2569
Cdd:pfam04873  241 SDTWLAVLNQEE 252
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1699-2032 5.61e-129

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: 408.74  E-value: 5.61e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1699 EEMDMKYKKIVGNLSANLAATTLKVKSRYFHRIGVGGKGQLKIYDKIQgLPDHNIFHPGKSYPVIVRHSNSLSADDDARI 1778
Cdd:cd08151      1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1779 DARGAAIRILSDDVGSggstPPLLDLTLKTGKAFYARTIADFATWLVCGLAAREEHVKRV-PRVRDAVWMSL-RNADSFT 1856
Cdd:cd08151     80 DGRGAALRFLNAGDDD----AGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYT 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1857 ELHYYSNICRLFRFTDGQEMYVKFKLRPFDETISEDSGKVEPVGILPPDTGAIPRDENDTRPLLFLADDFKRRVESPtGV 1936
Cdd:cd08151    156 DLHYYSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GV 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1937 RYIFQLQVQPVPQDEatRDIALDCTKPWDETEFPYIDIGEISIDQNLTKEESEKMEFNPYvRCHEIDVIPASSCSQ-SAS 2015
Cdd:cd08151    235 RYRLQIQLREVSDDA--TAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNPG-NTPESLGLPLAYCADdYAS 311

                          330
                   ....*....|....*..
gi 2130317402 2016 IDHGRSLIYEICQHLRN 2032
Cdd:cd08151    312 LGHLRSLVYEISQRLRK 328
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 511-1072 6.64e-93

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 314.57  E-value: 6.64e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  511 NKTLYTWINEE---GAVVSRRTYRELHANASLISHKLLTsekpVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpVPVLP 587
Cdd:PRK05850    16 DDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRR----HGSTGDRAVILAPQGLEYIVAFLGALQA----GLIAV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  588 PDPLQRGGQALLKIENIAKSCNAVAILSTvgyhSAVrAGSVknlilltGKNGKTTGRWPNLPWLHTDSWikyskNLQAEN 667
Cdd:PRK05850    88 PLSVPQGGAHDERVSAVLRDTSPSVVLTT----SAV-VDDV-------TEYVAPQPGQSAPPVIEVDLL-----DLDSPR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  668 KADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY------RSTSNTILVSWLPQYHDMGLIGGLFTAL 741
Cdd:PRK05850   151 GSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPI 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLeSDKSTArNYDLSSMIFLMVAAEPVRQITLKRF 821
Cdd:PRK05850   231 LGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKT-SDDDMA-GLDLGGVLGIISGSERVHPATLKRF 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 IELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDWQ------GRV--C--------CGYVDPNDPDVdiRIANP 885
Cdd:PRK05850   309 ADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPPESVRFDyeklsaGHAkrCetgggtplVSYGSPRSPTV--RIVDP 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  886 ETGEEIKeSGKEGEIWISSSSAGIGYWGREELSQKTFKNEL----PDYPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVA 961
Cdd:PRK05850   387 DTCIECP-AGTVGEIWVHGDNVAAGYWQKPEETERTFGATLvdpsPGTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVD 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  962 GRNIYSADIEKTVEsssELLRpGCCAVVGVPEevlstkgisvsDSSDQvgLVVIAEVRDAKTVDKEVVEK---IKTRVA- 1037
Cdd:PRK05850   466 GRNHYPDDIEATIQ---EITG-GRVAAISVPD-----------DGTEK--LVAIIELKKRGDSDEEAMDRlrtVKREVTs 528

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 2130317402 1038 ---EEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQF 1072
Cdd:PRK05850   529 aisKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 488-1077 1.13e-89

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 307.04  E-value: 1.13e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  488 VEFPDLSSLDGYLKHWGthRVTQNKTLYTWIN---EEGAVVSRRTYRELHANASLISHKLltseKPVIKPGDRVLLVYVP 564
Cdd:PRK07769    15 IRFPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  565 GLDFVDCFFGCLRARVLPVPVLPPDPLQRGGqallKIENIAKSCNAVAILSTVGyhsavRAGSVKNLIlltgkNGKTTGR 644
Cdd:PRK07769    89 NLDYLIAFFGALYAGRIAVPLFDPAEPGHVG----RLHAVLDDCTPSAILTTTD-----SAEGVRKFF-----RARPAKE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  645 WPN------LPWLHTDSWIKysknlqaenkadsAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSN 718
Cdd:PRK07769   155 RPRviavdaVPDEVGATWVP-------------PEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  719 TILVSWLPQYHDMGLIGGLFTALVsGGSSVLFSPMTFIKNPLLWLETMSKYQA----THSAGPNFAFEL-MLRRLESDKS 793
Cdd:PRK07769   222 DRGVSWLPFFHDMGLITVLLPALL-GHYITFMSPAAFVRRPGRWIRELARKPGgtggTFSAAPNFAFEHaAARGLPKDGE 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  794 TArnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKP--IFVDWQ----GR-- 865
Cdd:PRK07769   301 PP--LDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRfv 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  866 ------------VCCGYVDPNDPDVdirIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNEL------- 926
Cdd:PRK07769   379 evpadapnavaqVSAGKVGVSEWAV---IVDPETASELPD-GQIGEIWLHGNNIGTGYWGKPEETAATFQNILksrlses 454

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  927 -----PDypGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGVP-----EEVL 996
Cdd:PRK07769   455 haegaPD--DALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPanqlpQVVF 532

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  997 --STKGISV--SDSSDQvgLVVIAEvRDA---KTVDKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECL 1069
Cdd:PRK07769   533 ddSHAGLKFdpEDTSEQ--LVIVAE-RAPgahKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACR 609


                   ....*...
gi 2130317402 1070 KQFVDGTL 1077
Cdd:PRK07769   610 AAYLDGSL 617
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 488-1077 5.98e-86

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: 296.25  E-value: 5.98e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  488 VEFPDLSSLDGYLKHWGthRVTQNKTLYTWIN---EEGAVVSRRTYRELHANASLISHKLltseKPVIKPGDRVLLVYVP 564
Cdd:NF038339    12 IRFPDGATLVDHVERNA--RERADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRVAILAPQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  565 GLDFVDCFFGCLRARVLPVPVLPPDPLQRGGqallKIENIAKSCNAVAILSTVGYHSAVR-------AGSVKNLILLTGk 637
Cdd:NF038339    86 GLDYVVSFFAAIYAGNIAVPLFDPDEPGHTD----RLHAVLGDCKPSAILTATSSAEGVRkffrslpAKERPRVIAVDA- 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  638 ngkttgrwpnLPWLHTDSWIKysknlqaenkadsAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTS 717
Cdd:NF038339   161 ----------VPDSVGSTWVR-------------PDADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDE 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  718 NTILVSWLPQYHDMGLIGGLFTALvsGGSSVLF-SPMTFIKNPLLWLETM---SKYQATHSAGPNFAFE-LMLRRLESDK 792
Cdd:NF038339   218 NSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWIRELaavSDGAGTFAAAPNFAFEhAAARGLPKEG 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  793 STarnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKP--IFVDW----QGR- 865
Cdd:NF038339   296 EP---LDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReelnAGRi 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  866 -------------VCCGYVDPNDPDVdirIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNEL------ 926
Cdd:NF038339   373 vevdpdapnavaqVSCGYVARSQWAV---IVDPETGTELPD-GQVGEIWLHGNNIGTGYWGRPEETEETFHNKLksrlee 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  927 -------PDypGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGV-----PEE 994
Cdd:NF038339   449 gshaegaPE--DANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVpanqlPAE 526

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  995 VL--STKGISVS--DSSDQvgLVVIAEvRDA---KTVDKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFE 1067
Cdd:NF038339   527 VFenSHSGLKYDadDSSEQ--LVIVAE-RAPgagKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRA 603

                          650
                   ....*....|
gi 2130317402 1068 CLKQFVDGTL 1077
Cdd:NF038339   604 CKAAYIDGTL 613
PRK05691 PRK05691
peptide synthase; Validated
 519-1195 1.29e-84

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 312.10  E-value: 1.29e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  519 NEEGAVVSrrtYRELHANASLISHKLLTSekpvIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQRGGQA- 597
Cdd:PRK05691    35 PGEGVVLS---YRDLDLRARTIAAALQAR----ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQEr 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  598 LLKIENIAKScnavAILSTVgyhsAVRAGSVKNLILLTGKNGKttgrwpnlPWLHTDSwikysknLQAENKADSAEP--E 675
Cdd:PRK05691   108 LLSIIADAEP----RLLLTV----ADLRDSLLQMEELAAANAP--------ELLCVDT-------LDPALAEAWQEPalQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  676 TDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNT--ILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPM 753
Cdd:PRK05691   165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPA 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLeSDKSTARnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQE 833
Cdd:PRK05691   245 YFLERPLRWLEAISEYGGTISGGPDFAYRLCSERV-SESALER-LDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 VMAPGYGLAENCVFVSCAY-GQGKPIF-VDWQG-------------RVCCGYVDPNDPdvdIRIANPETGEEIKEsGKEG 898
Cdd:PRK05691   323 SFFASYGLAEATLFVSGGRrGQGIPALeLDAEAlarnraepgtgsvLMSCGRSQPGHA---VLIVDPQSLEVLGD-NRVG 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  899 EIWISSSSAGIGYWGREELSQKTFKNelpdYPGRIYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSS 978
Cdd:PRK05691   399 EIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  979 ELLRPGCCAVVGVPEEVLSTKGISVsDSSDQVGLVVIAEvrdaktvdkEVVEKIKTRVAEEHGVTVASVKLIKPRTISKT 1058
Cdd:PRK05691   475 EVVRKGRVAAFAVNHQGEEGIGIAA-EISRSVQKILPPQ---------ALIKSIRQAVAEACQEAPSVVLLLNPGALPKT 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1059 TSGKIKRFECLKQFVDGTLNivPEPLFkkktfvrsfttgtcregktprPQLVSSPLPSPKMSNKDIVEFLIRLVSEQTGI 1138
Cdd:PRK05691   545 SSGKLQRSACRLRLADGSLD--SYALF---------------------PALQAVEAAQTAASGDELQARIAAIWCEQLKV 601

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402 1139 PSsnISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTAtciSDLANFSENL 1195
Cdd:PRK05691   602 EQ--VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEA---PTLAAFSAAV 653
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 654-1074 4.04e-84

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: 290.40  E-value: 4.04e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSKNLQAENKADSAEPET-DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMG 732
Cdd:NF040633   177 ESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMG 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  733 LIGGLFtALVSGGSSVLFSPMTFIKNPLLWLETMSKYQ---ATHSAGPNFAFELMLRRleSDKSTARNYDLSSMIFLMVA 809
Cdd:NF040633   257 IILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSRREddvNVYTVVPNFALELAARY--ANPEEGEDLDLSAVDGIIIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDW------QGRVCCgyVDPNDPDV----- 878
Cdd:NF040633   334 SEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFdrealaEGRAVE--VAEDSENAvpfas 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 --------DIRIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNELP----------DYPGRIYTRTGDL 940
Cdd:NF040633   412 ngqvvrpqVLAIVDPETGQELPD-GTVGEIWVHGDNMAAGYLDREEETAETFRNTLGerlaensraeGAPEDNWMATGDL 490

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  941 GRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEVRD 1020
Cdd:NF040633   491 GVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPGD-------------DVEKLVILAERDD 557

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402 1021 AKTV--DKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQFVD 1074
Cdd:NF040633   558 EADEsgDAEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 527-1078 1.04e-81

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: 277.85  E-value: 1.04e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGQA-----LLKI 601
Cdd:COG0318     24 RLTYAELDARARRLAAALRALG---VGPGDRVALLLPNSPEFVVAFLAALRA---------------GAVVvplnpRLTA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  602 ENIAkscnavAILStvgyHSAVRAgsvknliLLTgkngkttgrwpnlpwlhtdswikysknlqaenkadsaepetddlCF 681
Cdd:COG0318     86 EELA------YILE----DSGARA-------LVT--------------------------------------------AL 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMtfikNPLL 761
Cdd:COG0318    105 ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF----DPER 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  762 WLETMSKYQATHSAGPNFAFELMLRRLEsdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLsqeVMAPGYGL 841
Cdd:COG0318    181 VLELIERERVTVLFGVPTMLARLLRHPE-----FARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYGL 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  842 AENCVFVSCAYGQGKPIFVDWQGRVCcgyvdpndPDVDIRIANPEtGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKT 921
Cdd:COG0318    250 TETSPVVTVNPEDPGERRPGSVGRPL--------PGVEVRIVDED-GRELPP-GEVGEIVVRGPNVMKGYWNDPEATAEA 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  922 FKNElpdypgriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVLstkg 1000
Cdd:COG0318    320 FRDG--------WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKW---- 384

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1001 isvsdssDQVGLVVIAeVRDAKTVD-KEVVEKIKTRVAeEHGVtvasvklikPRTIS------KTTSGKIKRFECLKQFV 1073
Cdd:COG0318    385 -------GERVVAFVV-LRPGAELDaEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGKIDRRALRERYA 446


                   ....*
gi 2130317402 1074 DGTLN 1078
Cdd:COG0318    447 AGALE 451
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 672-1080 6.17e-80

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 278.16  E-value: 6.17e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  672 AEPETDDLCFLQFTSGSTGDAKGVMITHGG-------LIHNVKLMQRRYRStsntilVSWLPQYHDMGLIGGLFTAlVSG 744
Cdd:PRK12476   188 VELDTDDVSHLQYTSGSTRPPVGVEITHRAvgtnlvqMILSIDLLDRNTHG------VSWLPLYHDMGLSMIGFPA-VYG 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLFSPMTFIKNPLLWLETMS---KYQATHSAGPNFAFELMLRR-LESDKSTArnyDLSSMIfLMVAAEPVRQITLKR 820
Cdd:PRK12476   261 GHSTLMSPTAFVRRPQRWIKALSegsRTGRVVTAAPNFAYEWAAQRgLPAEGDDI---DLSNVV-LIIGSEPVSIDAVTT 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  821 FIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKP--IFVDWQ----GR--------------VCCGYVDPNDPDVdi 880
Cdd:PRK12476   337 FNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPsvVYLDREqlgaGRavrvaadapnavahVSCGQVARSQWAV-- 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  881 rIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNEL----PD-------YPGRIYTRTGDLGRIIDGKLF 949
Cdd:PRK12476   415 -IVDPDTGAELPD-GEVGEIWLHGDNIGRGYWGRPEETERTFGAKLqsrlAEgshadgaADDGTWLRTGDLGVYLDGELY 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  950 ITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEvRDAKTVDKE-- 1027
Cdd:PRK12476   493 ITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAE-------------DNERLVIVAE-RAAGTSRADpa 558

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2130317402 1028 -VVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQFVDGTLNIV 1080
Cdd:PRK12476   559 pAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGVH 612
PRK09192 PRK09192
fatty acyl-AMP ligase;
522-1076 1.22e-74

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 261.48  E-value: 1.22e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  522 GAVVSRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLqrGGQA--LL 599
Cdd:PRK09192    44 GQLEEALPYQTLRARAEAGARRLLALG---LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGF--GGREsyIA 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 KIENIAKSCNAVAILSTVGYHSAVRAGSvknlillTGKNGKTTGRWPNLpwlhtdswikyskNLQAENKADSAEPETDDL 679
Cdd:PRK09192   119 QLRGMLASAQPAAIITPDELLPWVNEAT-------HGNPLLHVLSHAWF-------------KALPEADVALPRPTPDDI 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  680 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRryrstsNTILV-------SWLPQYHDMGLIGGLFTALVSGGSSVLFSP 752
Cdd:PRK09192   179 AYLQYSSGSTRFPRGVIITHRALMANLRAISH------DGLKVrpgdrcvSWLPFYHDMGLVGFLLTPVATQLSVDYLPT 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 MTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESdkSTARNYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQ 832
Cdd:PRK09192   253 RDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNS--KDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDD 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVMAPGYGLAENCVFVSCA-YGQG-------------KPIFVDWQGR-------VCCGyvdPNDPDVDIRIANpETGEEI 891
Cdd:PRK09192   331 KAFMPSYGLAEATLAVSFSpLGSGivveevdrdrleyQGKAVAPGAEtrrvrtfVNCG---KALPGHEIEIRN-EAGMPL 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  892 KESGKeGEIWISSSSAGIGYWGREElSQKTFKnelPDypGriYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:PRK09192   407 PERVV-GHICVRGPSLMSGYFRDEE-SQDVLA---AD--G--WLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIE 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  972 KTVESSSElLRPGCCAVVGVPEEvlstkgisvsdssDQVGLVVIAEVRDAKTVDKE-VVEKIKTRVAEEHGVTVaSVKLI 1050
Cdd:PRK09192   478 WIAEQEPE-LRSGDAAAFSIAQE-------------NGEKIVLLVQCRISDEERRGqLIHALAALVRSEFGVEA-AVELV 542

                          570       580
                   ....*....|....*....|....*.
gi 2130317402 1051 KPRTISKTTSGKIKRFECLKQFVDGT 1076
Cdd:PRK09192   543 PPHSLPRTSSGKLSRAKAKKRYLSGA 568
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
660-1072 3.78e-72

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 254.41  E-value: 3.78e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  660 SKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSN------TILVSWLPQYHDMGL 733
Cdd:NF038337   146 SLDLDGPNSPSIRISDAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGL 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  734 IGGLFTALVSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRlESDKSTArNYDLSSMIFLMVAAEPV 813
Cdd:NF038337   226 VLGVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRK-TTDADLA-GLDLGNVIGIVSGAERI 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  814 RQITLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDWQ----------------GRVCCGYVDPNDPD 877
Cdd:NF038337   304 HPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEpeklsegsaqrceartGSPLLSYGTPTSPT 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  878 VdiRIANPETGEEIKeSGKEGEIWISSSSAGIGYWGREELSQKTFKNEL----PDYPGRIYTRTGDLGRIIDGKLFITGR 953
Cdd:NF038337   384 V--RIVDPDTCIECP-AGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLanpsPGTPEGPWLRTGDLGFISEDEMFIVGR 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  954 IKDLIIVAGRNIYSADIEKTVESsselLRPGCCAVVGVPeevlstkgisvSDSSDQvgLVVIAEVRDAKTVDKEVVEK-- 1031
Cdd:NF038337   461 MKDLLIVYGRNHYPEDIESTVQE----ITGGRVAAISVP-----------VDETEK--LVTIIELKKRGDSDEEAMRKld 523

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2130317402 1032 -----IKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQF 1072
Cdd:NF038337   524 avknnVTAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQY 569
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 663-1065 4.24e-72

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 252.99  E-value: 4.24e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNT-ILVSWLPQYHDMGLIGGLFTAL 741
Cdd:PRK07768   138 LLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTVPM 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESdKSTARNYDLSSMIFLMVAAEPVRQITLKRF 821
Cdd:PRK07768   218 YFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRR-QAKPGAFDLSSLRFALNGAEPIDPADVEDL 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 IELTLPFGLSQEVMAPGYGLAENCVFVScaygqgkpiFVDW-QGRVccgyVDPNDPDV--DIRIANPETGEEIK------ 892
Cdd:PRK07768   297 LDAGARFGLRPEAILPAYGMAEATLAVS---------FSPCgAGLV----VDEVDADLlaALRRAVPATKGNTRrlatlg 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  893 ------------ESGKE------GEIWISSSSAGIGYwgreelsqKTFKNELPDYPGRIYTRTGDLGRIID-GKLFITGR 953
Cdd:PRK07768   364 pplpglevrvvdEDGQVlpprgvGVIELRGESVTPGY--------LTMDGFIPAQDADGWLDTGDLGYLTEeGEVVVCGR 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  954 IKDLIIVAGRNIYSADIEKTVeSSSELLRPGCCAVVGVPeevlstkgisvSDSSDQvGLVVIAEVRDAKtvDKEVVEKIK 1033
Cdd:PRK07768   436 VKDVIIMAGRNIYPTDIERAA-ARVEGVRPGNAVAVRLD-----------AGHSRE-GFAVAVESNAFE--DPAEVRRIR 500

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2130317402 1034 TRVAE----EHGVTVASVKLIKPRTISKTTSGKIKR 1065
Cdd:PRK07768   501 HQVAHevvaEVGVRPRNVVVLGPGSIPKTPSGKLRR 536
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 515-1075 1.03e-71

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: 251.82  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  515 YTWINEEGAVVsRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQRG 594
Cdd:cd05906     28 ITYIDADGSEE-FQSYQDLLEDARRLAAGLRQLG---LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  595 GQALLKIENIAKSCNAVAILSTVGYHSAVRagsvknlilltgkngKTTGRWPNLPWlhtdSWIKYSKNLQAENKADSAEP 674
Cdd:cd05906    104 NARLRKLRHIWQLLGSPVVLTDAELVAEFA---------------GLETLSGLPGI----RVLSIEELLDTAADHDLPQS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMT 754
Cdd:cd05906    165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEE 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  755 FIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKStaRNYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQEV 834
Cdd:cd05906    245 ILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  835 MAPGYGLAENC------------------VFVSCaygqGKPIfvdwqgrvccgyvdpndPDVDIRIANPETgeEIKESGK 896
Cdd:cd05906    323 IRPAFGMTETCsgviysrsfptydhsqalEFVSL----GRPI-----------------PGVSMRIVDDEG--QLLPEGE 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  897 EGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVES 976
Cdd:cd05906    380 VGRLQVRGPVVTKGYYNNPEANAEAFTED-----G--WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  977 SSElLRPGCCAVVGVPEEvlstkgisvSDSSDQVGLV-VIAEVRDAKTVdkEVVEKIKTRVAEEHGVTVASVKLIKPRTI 1055
Cdd:cd05906    453 VPG-VEPSFTAAFAVRDP---------GAETEELAIFfVPEYDLQDALS--ETLRAIRSVVSREVGVSPAYLIPLPKEEI 520

                          570       580
                   ....*....|....*....|
gi 2130317402 1056 SKTTSGKIKRFECLKQFVDG 1075
Cdd:cd05906    521 PKTSLGKIQRSKLKAAFEAG 540
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 678-1064 3.54e-66

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: 228.71  E-value: 3.54e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHdMGLIGGLFTALVSGGSSVLFSPmtfiK 757
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPK----F 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  758 NPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLsqeVMAP 837
Cdd:cd04433     76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAG-----YDLSSLRALVSGGAPLPPELLERFEEA---PGI---KLVN 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  838 GYGLAENCVFVSCAYGQGKPIFVDWQGRVCcgyvdpndPDVDIRIANPETGEeiKESGKEGEIWISSSSAGIGYWGREEL 917
Cdd:cd04433    145 GYGLTETGGTVATGPPDDDARKPGSVGRPV--------PGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGYWNNPEA 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  918 SQKTFKNelpdypgrIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVL 996
Cdd:cd04433    215 TAAVDED--------GWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPDPEW 283

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  997 stkgisvsdsSDQVGLVViaEVRDAKTVDKevvEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIK 1064
Cdd:cd04433    284 ----------GERVVAVV--VLRPGADLDA---EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
AMP-binding pfam00501
AMP-binding enzyme;
527-961 3.99e-63

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 222.57  E-value: 3.99e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLtseKPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQRggqallkIENIAK 606
Cdd:pfam00501   21 RLTYRELDERANRLAAGLR---ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE-------LAYILE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  607 SCNAVAILstvgyhsAVRAGSVKNLILLTGKNGKTTGRwpnlPWLHTDSWIKYSKNLQAENKADSAEPET-----DDLCF 681
Cdd:pfam00501   91 DSGAKVLI-------TDDALKLEELLEALGKLEVVKLV----LVLDRDPVLKEEPLPEEAKPADVPPPPPpppdpDDLAY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRS----TSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTFiK 757
Cdd:pfam00501  160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-L 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  758 NPLLWLETMSKYQATHSAGPNFAFELMLrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELtLPFGLSQevmap 837
Cdd:pfam00501  239 DPAALLELIERYKVTVLYGVPTLLNMLL-----EAGAPKRALLSSLRLVLSGGAPLPPELARRFREL-FGGALVN----- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  838 GYGLAENCVFVSCAYgqgkPIFVDWQGRVCCGYVDPNdpdVDIRIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREEL 917
Cdd:pfam00501  308 GYGLTETTGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPVPP-GEPGELCVRGPGVMKGYLNDPEL 379

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2130317402  918 SQKTFKnelpdyPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVA 961
Cdd:pfam00501  380 TAEAFD------EDGWY-RTGDLGRRDeDGYLEIVGRKKDQIKLG 417
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 677-1075 6.15e-63

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: 225.06  E-value: 6.15e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTFI 756
Cdd:cd05908    106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFI 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 KNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstARNYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQEVMA 836
Cdd:cd05908    186 RRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK--ANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAIL 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  837 PGYGLAENCVFVsCAYGQGKPIF-----------------VDWQGRVCCGYVDPNDP--DVDIRIANPEtgEEIKESGKE 897
Cdd:cd05908    264 PVYGLAEASVGA-SLPKAQSPFKtitlgrrhvthgepepeVDKKDSECLTFVEVGKPidETDIRICDED--NKILPDGYI 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWISSSSAGIGYWGREELSQKTFKnelPDYpgriYTRTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKT-VES 976
Cdd:cd05908    341 GHIQIRGKNVTPGYYNNPEATAKVFT---DDG----WLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIaEEL 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  977 SSELLrpGCCAVVGVPEEvlstkgisvSDSSDQvglvVIAEVRDAKTVDK--EVVEKIKTRVAEEHGVTVASVKLIkpRT 1054
Cdd:cd05908    414 EGVEL--GRVVACGVNNS---------NTRNEE----IFCFIEHRKSEDDfyPLGKKIKKHLNKRGGWQINEVLPI--RR 476

                          410       420
                   ....*....|....*....|.
gi 2130317402 1055 ISKTTSGKIKRFECLKQFVDG 1075
Cdd:cd05908    477 IPKTTSGKVKRYELAQRYQSG 497
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
674-1076 4.80e-54

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 199.61  E-value: 4.80e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNT-ILVSWLPQYHDMGLIGGLFTALvsGGSSVLFSP 752
Cdd:PRK05851   149 PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAFLLTAAL--AGAPLWLAP 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 MT-FIKNPLLWLETMSKYQATHSAGPNFAFELM---LRRLesdkstaRNYDLSSMIFLMVAAEPVRQITLKRFIELTLPF 828
Cdd:PRK05851   227 TTaFSASPFRWLSWLSDSRATLTAAPNFAYNLIgkyARRV-------SDVDLGALRVALNGGEPVDCDGFERFATAMAPF 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  829 GLSQEVMAPGYGLAENcvfvSCAYGQGKP---------IFVDWQGRVCCGYVDPNDPDVDIRIANPEtgEEIKESGKE-G 898
Cdd:PRK05851   300 GFDAGAAAPSYGLAES----TCAVTVPVPgiglrvdevTTDDGSGARRHAVLGNPIPGMEVRISPGD--GAAGVAGREiG 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  899 EIWISSSSAGIGYWGREEL-SQKTFKnelpdypgriytrTGDLGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKtVESS 977
Cdd:PRK05851   374 EIEIRGASMMSGYLGQAPIdPDDWFP-------------TGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER-VAAQ 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  978 SELLRPGCCAVVGVPEevlstkgisvsdSSDQVGLVVIAEVR--DAKTVDKEVVEkiktRVAEEHGVTVASVKLIKPRTI 1055
Cdd:PRK05851   440 VRGVREGAVVAVGTGE------------GSARPGLVIAAEFRgpDEAGARSEVVQ----RVASECGVVPSDVVFVAPGSL 503

                          410       420
                   ....*....|....*....|.
gi 2130317402 1056 SKTTSGKIKRFECLKQFVDGT 1076
Cdd:PRK05851   504 PRTSSGKLRRLAVKRSLEAAD 524
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 514-1081 1.73e-53

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: 199.11  E-value: 1.73e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  514 LYTWINEEGAVVSRRTYRELHANASLISHKLLtsEKPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQR 593
Cdd:cd05905      1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQ--KKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  594 GGqALLKIENIAKSCNAVAILstvgyhsavRAGSVKNLILLTGKNGKTTGRWPNLPWLHTdswIKYSKNLQAENKADSAE 673
Cdd:cd05905     79 LG-FLLGTCKVRVALTVEACL---------KGLPKKLLKSKTAAEIAKKKGWPKILDFVK---IPKSKRSKLKKWGPHPP 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPM 753
Cdd:cd05905    146 TRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPE 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARNYD--LSSMIFLMVAAE-PVRQITLKRFIELTLPFGL 830
Cdd:cd05905    226 LMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDvnLSSLRMCMVPCEnRPRISSCDSFLKLFQTLGL 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 SQEVMAPGYGlaenCVFVScaygqgkpiFVDWQG-------RVccgYVDPND--------------------------PD 877
Cdd:cd05905    306 SPRAVSTEFG----TRVNP---------FICWQGtsgpepsRV---YLDMRAlrhgvvrlderdkpnslplqdsgkvlPG 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  878 VDIRIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNELPDYPGRI-----YTRTGDLGRIIDGK----- 947
Cdd:cd05905    370 AQVAIVNPETKGLCKD-GEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGitnnsYARTGLLGFLRPTKctdln 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  948 ------LFITGRIKDLIIVAGRNIYSADIEKTVEsSSELLRPGCCavvgvpeeVLSTKGIsvsdssdqvgLVVIAEVRDA 1021
Cdd:cd05905    449 veehdlLFVVGSIDETLEVRGLRHHPSDIEATVM-RVHPYRGRCA--------VFSITGL----------VVVVAEQPPG 509

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1022 KTVDK-EVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFECLKQFVDGTLNIVP 1081
Cdd:cd05905    510 SEEEAlDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIY 570
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 527-1065 2.74e-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: 175.06  E-value: 2.74e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGQA-----LLK- 600
Cdd:cd05936     24 KLTYRELDALAEAFAAGLQNLG---VQPGDRVALMLPNCPQFPIAYFGALKA---------------GAVVvplnpLYTp 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  601 --IENIAKSCNAVAILSTVGYHSAVRAGsvknlilltgkngKTTGRWPnlpwlhtdswikysknlqaenkadsaEPETDD 678
Cdd:cd05936     86 reLEHILNDSGAKALIVAVSFTDLLAAG-------------APLGERV--------------------------ALTPED 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  679 LCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY--RSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSPM 753
Cdd:cd05936    127 VAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLiprFRPI 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFiknpllwLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVRQITLKRFIELTlpfglsQE 833
Cdd:cd05936    207 GV-------LKEIRKHRVTIFPGVPTMYIALLNAPEFKK-----RDFSSLRLCISGGAPLPVEVAERFEELT------GV 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 VMAPGYGLAENCVFVSC--AYGQGKPifvdwqgrvccGYVDPNDPDVDIRIANPETGEEikESGKEGEIWISSSSAGIGY 911
Cdd:cd05936    269 PIVEGYGLTETSPVVAVnpLDGPRKP-----------GSIGIPLPGTEVKIVDDDGEEL--PPGEVGELWVRGPQVMKGY 335

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 WGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVessseLLRPGC--CAV 988
Cdd:cd05936    336 WNRPEETAEAFVDG--------WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVL-----YEHPAVaeAAV 402

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  989 VGVPEEvlsTKGISVsdssdqVGLVVIAEvrDAKTVDKEVVEKIKTRvaeehgvtVASVKLikPRTIS------KTTSGK 1062
Cdd:cd05936    403 VGVPDP---YSGEAV------KAFVVLKE--GASLTEEEIIAFCREQ--------LAGYKV--PRQVEfrdelpKSAVGK 461


                   ...
gi 2130317402 1063 IKR 1065
Cdd:cd05936    462 ILR 464
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
511-1075 1.59e-42

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 166.44  E-value: 1.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  511 NKTLYTWINEEGAVVsRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLvYVP-GLDFVDCFFGCLRArvlpvpvlppd 589
Cdd:COG0365     24 DKVALIWEGEDGEER-TLTYAELRREVNRFANALRALG---VKKGDRVAI-YLPnIPEAVIAMLACARI----------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  590 plqrGGQA-----LLKIENIA---KSCNAVAILSTVGYHSAVR--------------AGSVKNLILLTGKNGKTtgRWPN 647
Cdd:COG0365     88 ----GAVHspvfpGFGAEALAdriEDAEAKVLITADGGLRGGKvidlkekvdealeeLPSLEHVIVVGRTGADV--PMEG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  648 LPWLHTdswikysknlQAENKADSAEPET---DDLCFLQFTSGSTGDAKGVMITHGG-LIHNVKLMQR--------RYRS 715
Cdd:COG0365    162 DLDWDE----------LLAAASAEFEPEPtdaDDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYvldlkpgdVFWC 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  716 TSNtilVSWLpqyhdMGLIGGLFTALVSGGSSVLF--SPMTfiKNPLLWLETMSKYQATHsagpnF-----AFELMLRrl 788
Cdd:COG0365    232 TAD---IGWA-----TGHSYIVYGPLLNGATVVLYegRPDF--PDPGRLWELIEKYGVTV-----FftaptAIRALMK-- 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  789 eSDKSTARNYDLSSMIFLMVAAEP--------VRQITLKRFIEltlpfglsqevmapGYGLAE-NCVFVSCAYGQ----- 854
Cdd:COG0365    295 -AGDEPLKKYDLSSLRLLGSAGEPlnpevwewWYEAVGVPIVD--------------GWGQTEtGGIFISNLPGLpvkpg 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  855 --GKPIFvdwqgrvccGYvdpndpdvDIRIANpETGEEIkESGKEGEIWISSSSAG--IGYWGREELSQKTFKNELPDYp 930
Cdd:COG0365    360 smGKPVP---------GY--------DVAVVD-EDGNPV-PPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGRFPGW- 419

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  931 griYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVlstKGISVsdssdq 1009
Cdd:COG0365    420 ---Y-RTGDGARRDeDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE---AAVVGVPDEI---RGQVV------ 483

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1010 VGLVVIaevRDAKTVDKEVVEKIKTRVAEEhgvtVASVKliKPRTIS------KTTSGKIKRFEcLKQFVDG 1075
Cdd:COG0365    484 KAFVVL---KPGVEPSDELAKELQAHVREE----LGPYA--YPREIEfvdelpKTRSGKIMRRL-LRKIAEG 545
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 677-1063 4.69e-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: 158.93  E-value: 4.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNV--KLMQRRYRSTSNTILVswLPQYHDMGLIGGLFTALVSGGSSVL---FS 751
Cdd:cd17631     98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAvnALAALDLGPDDVLLVV--APLFHIGGLGVFTLPTLLRGGTVVIlrkFD 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PMTFiknpllwLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFglS 831
Cdd:cd17631    176 PETV-------LDLIERHRVTSFFLVPTMIQALLQHPRFAT-----TDLSSLRAVIYGGAPMPERLLRALQARGVKF--V 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  832 QevmapGYGLAENC-------------VFVSCaygqGKPIFvdwqgrvccgyvdpndpDVDIRIANPEtGEEIKEsGKEG 898
Cdd:cd17631    242 Q-----GYGMTETSpgvtflspedhrrKLGSA----GRPVF-----------------FVEVRIVDPD-GREVPP-GEVG 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  899 EIWISSSSAGIGYWGREELSQKTFKNelpdypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESS 977
Cdd:cd17631    294 EIVVRGPHVMAGYWNRPEATAAAFRD------G--WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEH 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  978 SELLRpgcCAVVGVPEEvlstkgisvsdssdQVGLVVIAEV--RDAKTVD-KEVVEKIKTRvaeehgvtVASVKLikPRT 1054
Cdd:cd17631    366 PAVAE---VAVIGVPDE--------------KWGEAVVAVVvpRPGAELDeDELIAHCRER--------LARYKI--PKS 418

                          410
                   ....*....|....*
gi 2130317402 1055 I------SKTTSGKI 1063
Cdd:cd17631    419 VefvdalPRNATGKI 433
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 529-1063 2.34e-40

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: 158.14  E-value: 2.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtseKPVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGqallkienIAKSC 608
Cdd:cd05911     12 TYAQLRTLSRRLAAGLR---KLGLKKGDVVGIISPNSTYYPPVFLGCLFA---------------GG--------IFSAA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  609 NAVAILSTVGYH---------------------SAVRAGSVKNLILLTGKNGKTTGRWPNLPWLHTDSwikysKNLQAEN 667
Cdd:cd05911     66 NPIYTADELAHQlkiskpkviftdpdglekvkeAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEE-----DEDLPPP 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  668 KADSAepetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRST--SNTILVSWLPQYHDMGLIgGLFTALVSGG 745
Cdd:cd05911    141 LKDGK----DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLF-TTLASLLNGA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  746 SSVLFSPMtfikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVrqitLKRFIELt 825
Cdd:cd05911    216 TVIIMPKF----DSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDK-----YDLSSLRVILSGGAPL----SKELQEL- 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  826 LPFGLSQEVMAPGYGLAENCVFVSCAygqgkPIFVDWQGrvCCGYVDPNdpdVDIRIANPETGEEIKEsGKEGEIWISSS 905
Cdd:cd05911    282 LAKRFPNATIKQGYGMTETGGILTVN-----PDGDDKPG--SVGRLLPN---VEAKIVDDDGKDSLGP-NEPGEICVRGP 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  906 SAGIGYWGREELSQKTFknelpDYPGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvesssELLR-- 982
Cdd:cd05911    351 QVMKGYYNNPEATKETF-----DEDG--WLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELE-------AVLLeh 416

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  983 PGC--CAVVGVPEEVlstkgisvsdSSDQ-VGLVVIAEvrDAKTVDKEVVEKIKTRVAEEH----GVTVASvklikprTI 1055
Cdd:cd05911    417 PGVadAAVIGIPDEV----------SGELpRAYVVRKP--GEKLTEKEVKDYVAKKVASYKqlrgGVVFVD-------EI 477


                   ....*...
gi 2130317402 1056 SKTTSGKI 1063
Cdd:cd05911    478 PKSASGKI 485
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 527-1075 1.59e-38

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 153.42  E-value: 1.59e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQAL------LK 600
Cdd:PRK06187    31 RTTYAELDERVNRLANALRALG---VKKGDRVAVFDWNSHEYLEAYFAVPKI----------------GAVLhpinirLK 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  601 ---IENIAKSCNAVAIL---STVGYHSAVRA--GSVKNLILLTGKNGKTTGrwpnLPWLHTDSWIKysknlQAENKADSA 672
Cdd:PRK06187    92 peeIAYILNDAEDRVVLvdsEFVPLLAAILPqlPTVRTVIVEGDGPAAPLA----PEVGEYEELLA-----AASDTFDFP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  673 EPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLigGL-FTALVSGGSSVLfs 751
Cdd:PRK06187   163 DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLpYLALMAGAKQVI-- 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PMTFIKNPLLwlETMSKYQATHSAGPNFAFELMLRRLEsdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLS 831
Cdd:PRK06187   239 PRRFDPENLL--DLIETERVTFFFAVPTIWQMLLKAPR-----AYFVDFSSLRLVIYGGAALPPALLREFKEK---FGID 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  832 qevMAPGYGLAENCVFVSCAY----GQGKPIFVDWQGRVCCGyvdpndpdVDIRIANPEtGEEIKESGKE-GEIWISSSS 906
Cdd:PRK06187   309 ---LVQGYGMTETSPVVSVLPpedqLPGQWTKRRSAGRPLPG--------VEARIVDDD-GDELPPDGGEvGEIIVRGPW 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  907 AGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR-PG 984
Cdd:PRK06187   377 LMQGYWNRPEATAETIDGG--------WLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYPRELE------DALYGhPA 442

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  985 C--CAVVGVPEEvlstkgisvsdSSDQVGLVVIaEVRDAKTVD-KEVVEKIKTRVAEEhgvtvasvKLikPRTIS----- 1056
Cdd:PRK06187   443 VaeVAVIGVPDE-----------KWGERPVAVV-VLKPGATLDaKELRAFLRGRLAKF--------KL--PKRIAfvdel 500

                          570       580
                   ....*....|....*....|
gi 2130317402 1057 -KTTSGKIKRFECLKQFVDG 1075
Cdd:PRK06187   501 pRTSVGKILKRVLREQYAEG 520
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 529-1065 2.90e-37

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: 149.00  E-value: 2.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLltsEKPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPpdplqrggqALLKIE---NIA 605
Cdd:cd05926     16 TYADLAELVDDLARQL---AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP---------AYKKAEfefYLA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  606 KSCNAVAILSTVGYHSAVRAGSVKNLILLtgkngkttgrwpNLPWLHTDSWIKYSK----NLQAENKADSAE--PETDDL 679
Cdd:cd05926     84 DLGSKLVLTPKGELGPASRAASKLGLAIL------------ELALDVGVLIRAPSAeslsNLLADKKNAKSEgvPLPDDL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  680 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSPMTFi 756
Cdd:cd05926    152 ALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFSASTF- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 knpllWLEtMSKYQAT-HSAGPNFaFELMLRRLESDKSTArnydLSSMIFLMVAAEPVRQITLKRfieltlpfgLSQEVM 835
Cdd:cd05926    231 -----WPD-VRDYNATwYTAVPTI-HQILLNRPEPNPESP----PPKLRFIRSCSASLPPAVLEA---------LEATFG 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  836 AP---GYGLAENCVFVSC---AYGQGKPIFVdwqGRvccgyvdpndPD-VDIRIANpETGeEIKESGKEGEIWISSSSAG 908
Cdd:cd05926    291 APvleAYGMTEAAHQMTSnplPPGPRKPGSV---GK----------PVgVEVRILD-EDG-EILPPGVVGEICLRGPNVT 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  909 IGYWGREELSQK-TFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTvessseLLR-PGC 985
Cdd:cd05926    356 RGYLNNPEANAEaAFKDG--------WFRTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGV------LLShPAV 421

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  986 --CAVVGVPEEVLstkgisvsdsSDQVGLVVIAevRDAKTVDK-EVVEKIKTRVAEehgVTVASvKLIKPRTISKTTSGK 1062
Cdd:cd05926    422 leAVAFGVPDEKY----------GEEVAAAVVL--REGASVTEeELRAFCRKHLAA---FKVPK-KVYFVDELPKTATGK 485


                   ...
gi 2130317402 1063 IKR 1065
Cdd:cd05926    486 IQR 488
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 677-1067 1.49e-35

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: 140.11  E-value: 1.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPmTFi 756
Cdd:cd05917      2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP-SF- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 kNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDkstarNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLSQEVMA 836
Cdd:cd05917     80 -DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFD-----KFDLSSLRTGIMAGAPCPPELMKRVIEV---MNMKDVTIA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  837 pgYGLAENCVfVSCAYGQGKPIFVDWQ--GRVCcgyvdpndPDVDIRIANPETGEEIKeSGKEGEIWISSSSAGIGYWGR 914
Cdd:cd05917    151 --YGMTETSP-VSTQTRTDDSIEKRVNtvGRIM--------PHTEAKIVDPEGGIVPP-VGVPGELCIRGYSVMKGYWND 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  915 EELSQKTFKNELpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPE 993
Cdd:cd05917    219 PEKTAEAIDGDG-------WLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSD---VQVVGVPD 288

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402  994 EVLstkgisvsdssdqvGLVVIAEVR---DAKTVDKEVVEKIKTRVAeeHGVTVASVKLIKprTISKTTSGKIKRFE 1067
Cdd:cd05917    289 ERY--------------GEEVCAWIRlkeGAELTEEDIKAYCKGKIA--HYKVPRYVFFVD--EFPLTVSGKIQKFK 347
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 665-1037 3.57e-32

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: 132.60  E-value: 3.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  665 AENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSG 744
Cdd:cd05935     72 SGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLFSpmtfIKNPLLWLETMSKYQATHS-AGPNFAFELMlrrlesdkSTARN--YDLSSMIFLMVAAEPVRQITLKRF 821
Cdd:cd05935    152 GTYVLMA----RWDRETALELIEKYKVTFWtNIPTMLVDLL--------ATPEFktRDLSSLKVLTGGGAPMPPAVAEKL 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 IELTlpfGLSqevMAPGYGLAENCVFV----------SCaygQGKPIFvdwqgrvccgyvdpndpDVDIRIANPETGEEI 891
Cdd:cd05935    220 LKLT---GLR---FVEGYGLTETMSQThtnpplrpklQC---LGIP*F-----------------GVDARVIDIETGREL 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  892 kESGKEGEIWISSSSAGIGYWGREELSQKTFKnelpDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADI 970
Cdd:cd05935    274 -PPNEVGEIVVRGPQIFKGYWNRPEETEESFI----EIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEV 348

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  971 EKTVESSSELLRpgcCAVVGVPEEvlstkgisvsDSSDQV-GLVVIAEVRDAKTVDKEVVEKIKTRVA 1037
Cdd:cd05935    349 EAKLYKHPAI*E---VCVISVPDE----------RVGEEVkAFIVLRPEYRGKVTEEDIIEWAREQMA 403
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 529-971 1.30e-31

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 132.78  E-value: 1.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLltSEKPVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrggQALL--------- 599
Cdd:PRK08314    37 SYRELLEEAERLAGYL--QQECGVRKGDRVLLYMQNSPQFVIAYYAILRA-----------------NAVVvpvnpmnre 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 -KIENIAKSCNAVAILSTVGYHS----AVRAGSVKNLIL------LTGKNGKTTGRW----PNLPWLHTDSWIKYSKNLQ 664
Cdd:PRK08314    98 eELAHYVTDSGARVAIVGSELAPkvapAVGNLRLRHVIVaqysdyLPAEPEIAVPAWlraePPLQALAPGGVVAWKEALA 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  665 AENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSG 744
Cdd:PRK08314   178 AGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAG 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLfspMTfiknplLW-----LETMSKYQATH-SAGPNFAFELMLR-RLESdkstarnYDLSSMIFLMVAAEPVRQIT 817
Cdd:PRK08314   258 ATVVL---MP------RWdreaaARLIERYRVTHwTNIPTMVVDFLASpGLAE-------RDLSSLRYIGGGGAAMPEAV 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  818 LKRFIELT-LPFglsQEvmapGYGLAENCVFV----------SCAygqGKPIFvdwqgrvccgyvdpndpDVDIRIANPE 886
Cdd:PRK08314   322 AERLKELTgLDY---VE----GYGLTETMAQThsnppdrpklQCL---GIPTF-----------------GVDARVIDPE 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  887 TGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKnELpdyPGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNI 965
Cdd:PRK08314   375 TLEELPP-GEVGEIVVHGPQVFKGYWNRPEATAEAFI-EI---DGKRFFRTGDLGRMdEEGYFFITDRLKRMINASGFKV 449


                   ....*.
gi 2130317402  966 YSADIE 971
Cdd:PRK08314   450 WPAEVE 455
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 637-1067 2.88e-31

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 132.43  E-value: 2.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  637 KNGKTTGRWPN-LPWlhtdSWIKYSKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNvkLMQRR--- 712
Cdd:PRK05605   182 ARAALTGPAPGtVPW----ETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAN--AAQGKawv 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  713 --YRSTSNTILVSwLPQYHDMGLIGGLFTALVSGGSSVLFsPMTFIknPLLwLETMSKYQATHSAG-PNFAFELMlrrle 789
Cdd:PRK05605   256 pgLGDGPERVLAA-LPMFHAYGLTLCLTLAVSIGGELVLL-PAPDI--DLI-LDAMKKHPPTWLPGvPPLYEKIA----- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  790 sDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELTlpFGLSQEvmapGYGLAENCVFVScaygqGKPIFVDWQGrvccG 869
Cdd:PRK05605   326 -EAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLT--GGLLVE----GYGLTETSPIIV-----GNPMSDDRRP----G 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  870 YVDPNDPDVDIRIANPETGEEIKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKL 948
Cdd:PRK05605   390 YVGVPFPDTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMeEDGFI 461

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  949 FITGRIKDLIIVAGRNIYSADIEktvesssELLR--PGC--CAVVGVPEEvlstkgisvsDSSDQVGLVVIAEvrDAKTV 1024
Cdd:PRK05605   462 RIVDRIKELIITGGFNVYPAEVE-------EVLRehPGVedAAVVGLPRE----------DGSEEVVAAVVLE--PGAAL 522

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2130317402 1025 DKevvEKIKTRVAEEhgVTVASVklikPRTI------SKTTSGKIKRFE 1067
Cdd:PRK05605   523 DP---EGLRAYCREH--LTRYKV----PRRFyhvdelPRDQLGKVRRRE 562
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 674-1067 6.24e-31

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: 129.25  E-value: 6.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---- 749
Cdd:cd05907     84 EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFassa 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 ---------FSPMTFIKNPLLWlETMSKyQATHSAGPNFAFELMLRRLesdkstarnydLSSMIFLMVAAEPVRQITLKR 820
Cdd:cd05907    164 etllddlseVRPTVFLAVPRVW-EKVYA-AIKVKAVPGLKRKLFDLAV-----------GGRLRFAASGGAPLPAELLHF 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  821 FIELTLPFGLsqevmapGYGLAENCVFVSCAYGQ-------GKPIfvdwqgrvccgyvdpndPDVDIRIANpetgeeike 893
Cdd:cd05907    231 FRALGIPVYE-------GYGLTETSAVVTLNPPGdnrigtvGKPL-----------------PGVEVRIAD--------- 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  894 sgkEGEIWISSSSAGIGYWGREElsqKTFKNELPDypGRIytRTGDLGRI-IDGKLFITGRIKDLIIVA-GRNIYSADIE 971
Cdd:cd05907    278 ---DGEILVRGPNVMLGYYKNPE---ATAEALDAD--GWL--HTGDLGEIdEDGFLHITGRKKDLIITSgGKNISPEPIE 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  972 KTVESS---SELL-----RPGCCAVVGVPEEVLS-------TKGISVSDSSDQVGlvVIAEVRDAktvdkevVEKIKTRV 1036
Cdd:cd05907    348 NALKASpliSQAVvigdgRPFLVALIVPDPEALEawaeehgIAYTDVAELAANPA--VRAEIEAA-------VEAANARL 418

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2130317402 1037 AeehgvTVASVK----LIKPRTIS---KTTSGKIKRFE 1067
Cdd:cd05907    419 S-----RYEQIKkfllLPEPFTIEngeLTPTLKLKRPV 451
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 523-994 1.51e-29

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: 124.95  E-value: 1.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVVSRR---TYRELHANASLISHKLLtsEKPViKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQALL 599
Cdd:cd05930      5 AVVDGDqslTYAELDARANRLARYLR--ERGV-GPGDLVAVLLERSLEMVVAILAVLKA----------------GAAYV 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 ---------KIENIAKSCNAVAILstvgyhsavragsvknlilltgkngkttgrwpnlpwlhTDSwikysknlqaenkad 670
Cdd:cd05930     66 pldpsypaeRLAYILEDSGAKLVL--------------------------------------TDP--------------- 92

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 saepetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlIGGLFTALVSGGSSVLF 750
Cdd:cd05930     93 ------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVL 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 SPMTfIKNPLLWLETMSKYQATHSAGPNFAFELMLrrlesdkSTARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpfgL 830
Cdd:cd05930    166 PEEV-RKDPEALADLLAEEGITVLHLTPSLLRLLL-------QELELAALPSLRLVLVGGEALPPDLVRRWREL-----L 232

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 SQEVMAPGYGLAENCVFVSC--------AYGQ---GKPIFvDWQGRVccgyVDPNDPDVDIrianpetgeeikesGKEGE 899
Cdd:cd05930    233 PGARLVNLYGPTEATVDATYyrvppddeEDGRvpiGRPIP-NTRVYV----LDENLRPVPP--------------GVPGE 293

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  900 IWISSSSAGIGYWGREELSQKTFkNELPDYPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESS 977
Cdd:cd05930    294 LYIGGAGLARGYLNRPELTAERF-VPNPFGPGeRMY-RTGDLVRWLpDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAH 371

                          490
                   ....*....|....*..
gi 2130317402  978 SELLRpgcCAVVGVPEE 994
Cdd:cd05930    372 PGVRE---AAVVAREDG 385
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 529-971 2.93e-29

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: 123.14  E-value: 2.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLTSEKpvIKPGDRVLlVYVP-GLDFVDCFFGCLRArvlpvpvlppdplqrgGQALL-------- 599
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKA----------------GAAYVpldpaypa 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 -KIENIAKSCNAVAILSTVGyHSAVRAGSVKNLILLTGKNGKTTGRWPNLPWLhtdswikysknlqaenkadSAEPETDD 678
Cdd:TIGR01733   62 eRLAFILEDAGARLLLTDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------DAPSGPDD 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  679 LCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIgGLFTALVSGGSSVLFSPMTFIKN 758
Cdd:TIGR01733  122 LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDD 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  759 PLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARnydlssmiFLMVAAEPVRQITLKRFIELtlpfgLSQEVMAPG 838
Cdd:TIGR01733  201 AALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLR--------LVILGGEALTPALVDRWRAR-----GPGARLINL 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  839 YGLAENCVFVSCAYGQGKPifVDWQGRVCCGY---------VDPNDPDVDIrianpetgeeikesGKEGEIWISSSSAGI 909
Cdd:TIGR01733  268 YGPTETTVWSTATLVDPDD--APRESPVPIGRplantrlyvLDDDLRPVPV--------------GVVGELYIGGPGVAR 331

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  910 GYWGREELSQKTFKNE--LPDYPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:TIGR01733  332 GYLNRPELTAERFVPDpfAGGDGARLY-RTGDLVRYLpDGNLEFLGRIDDQVKIRGYRIELGEIE 395
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 677-1065 3.53e-29

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: 124.65  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTS---NTILVSwLPQYHDMGLiGGLFTALVSGGSSVLFSPM 753
Cdd:cd05904    158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdseDVFLCV-LPMFHIYGL-SSFALGLLRLGATVVVMPR 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFIKNpllWLETMSKYQATH-SAGPNFAFELmlrrleSDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIEltlPFGLSQ 832
Cdd:cd05904    236 FDLEE---LLAAIERYKVTHlPVVPPIVLAL------VKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRA---KFPNVD 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVMapGYGLAE-NCVFVSCAYGQGKPIfvdwqGRVCCGYVDPNdpdVDIRIANPETGEEIKeSGKEGEIWISSSSAGIGY 911
Cdd:cd05904    304 LGQ--GYGMTEsTGVVAMCFAPEKDRA-----KYGSVGRLVPN---VEAKIVDPETGESLP-PNQTGELWIRGPSIMKGY 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 WGREELSQKTFKNElpdypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVG 990
Cdd:cd05904    373 LNNPEATAATIDKE-----G--WLHTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD---AAVIP 442

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  991 VPEEvlstkgisvsdssdQVGLVVIA-EVRDAKTVDKEvvEKIKTRVAEEhgvtVASVKLIKPRT----ISKTTSGKIKR 1065
Cdd:cd05904    443 YPDE--------------EAGEVPMAfVVRKPGSSLTE--DEIMDFVAKQ----VAPYKKVRKVAfvdaIPKSPSGKILR 502
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 523-1065 1.07e-27

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 120.39  E-value: 1.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVVS---RRTYREL-----HANASLISHKlltsekpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrg 594
Cdd:PRK07656    23 AYVFgdqRLTYAELnarvrRAAAALAALG--------IGKGDRVAIWAPNSPHWVIAALGALKA---------------- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  595 GQALLKIENIAKSCNAVAILSTVG--------------YHSAVRAGSVKNLILLTGKNGKTTGRwPNLPWlhtDSWIKys 660
Cdd:PRK07656    79 GAVVVPLNTRYTADEAAYILARGDakalfvlglflgvdYSATTRLPALEHVVICETEEDDPHTE-KMKTF---TDFLA-- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  661 knlQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTA 740
Cdd:PRK07656   153 ---AGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  741 LVSGGSsVLFSPmTFikNPLLWLETMSKYQATHSAGPNFAFELMLrrlesDKSTARNYDLSSmIFLMV---AAEPVRQIt 817
Cdd:PRK07656   230 LMRGAT-ILPLP-VF--DPDEVFRLIETERITVLPGPPTMYNSLL-----QHPDRSAEDLSS-LRLAVtgaASMPVALL- 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  818 lKRFiELTLPFglsqEVMAPGYGLAENCVFVsCAYGQGKPiFVDWQGrvCCGyvdPNDPDVDIRIANPEtGEEIkESGKE 897
Cdd:PRK07656   299 -ERF-ESELGV----DIVLTGYGLSEASGVT-TFNRLDDD-RKTVAG--TIG---TAIAGVENKIVNEL-GEEV-PVGEV 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWISSSSAGIGYWGREELSQKTFKNElpdypGRIYTrtGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTves 976
Cdd:PRK07656   364 GELLVRGPNVMKGYYDDPEATAAAIDAD-----GWLHT--GDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEV--- 433

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  977 sseLLR-PGC--CAVVGVPEEVLstkgisvsdssdqvGLVVIAevrdaktvdkEVVEKIKTRVAEEHGVTVASVKLIK-- 1051
Cdd:PRK07656   434 ---LYEhPAVaeAAVIGVPDERL--------------GEVGKA----------YVVLKPGAELTEEELIAYCREHLAKyk 486

                          570       580
                   ....*....|....*....|.
gi 2130317402 1052 -PRTIS------KTTSGKIKR 1065
Cdd:PRK07656   487 vPRSIEfldelpKNATGKVLK 507
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 669-1037 1.97e-27

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: 118.55  E-value: 1.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSV 748
Cdd:cd05941     81 TDSEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVE 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 L---FSPMTFIKNPLLWLETM-----------SKYQATHSAGPNFAFELMLRRLEsdkstarnydlssmifLMV---AAE 811
Cdd:cd05941    161 FlpkFDPKEVAISRLMPSITVfmgvptiytrlLQYYEAHFTDPQFARAAAAERLR----------------LMVsgsAAL 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  812 PVRqiTLKRFIELTLPFGLSQevmapgYGLAENCVFVSCAY-GQGKPifvdwqgrvccGYVDPNDPDVDIRIANPETGEE 890
Cdd:cd05941    225 PVP--TLEEWEAITGHTLLER------YGMTEIGMALSNPLdGERRP-----------GTVGMPLPGVQARIVDEETGEP 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  891 IKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRI-IDGKLFITGRIKDLII-VAGRNIYSA 968
Cdd:cd05941    286 LPR-GEVGEIQVRGPSVFKEYWNKPEATKEEFTDD-----G--WFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSAL 357

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402  969 DIEKTVESssellRPGC--CAVVGVPEEVLstkGISVsdssdqVGLVVIAEVRDAKTVDkEVVEKIKTRVA 1037
Cdd:cd05941    358 EIERVLLA-----HPGVseCAVIGVPDPDW---GERV------VAVVVLRAGAAALSLE-ELKEWAKQRLA 413
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 675-1066 9.95e-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: 116.77  E-value: 9.95e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLfspMT 754
Cdd:cd05914     87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVF---LD 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  755 FIKNPLlwLETMSKYQATHSAGPNFAFELMLRRLesdKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELTLPFG----- 829
Cdd:cd05914    164 KIPSAK--IIALAFAQVTPTLGVPVPLVIEKIFK---MDIIPKLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFGgnike 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 -------LSQEV----------MAPGYGLAENCVFVScaYGQGKPIFVDWQGRVCcgyvdpndPDVDIRIANPETGEEik 892
Cdd:cd05914    239 fviggakINPDVeeflrtigfpYTIGYGMTETAPIIS--YSPPNRIRLGSAGKVI--------DGVEVRIDSPDPATG-- 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  893 esgkEGEIWISSSSAGIGYWGREELSQKTFknelpDYPGriYTRTGDLGRI-IDGKLFITGRIKDLIIV-AGRNIYSADI 970
Cdd:cd05914    307 ----EGEIIVRGPNVMKGYYKNPEATAEAF-----DKDG--WFHTGDLGKIdAEGYLYIRGRKKEMIVLsSGKNIYPEEI 375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  971 EKTVESSSELLRpgccAVVGVPEEVLSTKGISVSDSSDQVGLVViaeVRDAKTVDKEVVEKIKTRVAEEHgvTVASVKLI 1050
Cdd:cd05914    376 EAKINNMPFVLE----SLVVVQEKKLVALAYIDPDFLDVKALKQ---RNIIDAIKWEVRDKVNQKVPNYK--KISKVKIV 446

                          410
                   ....*....|....*.
gi 2130317402 1051 KpRTISKTTSGKIKRF 1066
Cdd:cd05914    447 K-EEFEKTPKGKIKRF 461
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 527-1067 3.68e-26

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: 114.40  E-value: 3.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLlVYVPG-LDFVDCFFGCLRArvlpvpvlppdplqrgGQALLKIENIA 605
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALG---VGPGDVVA-FQLPNwWEFAVLYLACLRI----------------GAVTNPILPFF 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  606 KSCNAVAILSTvgyhsavraGSVKNLIlltgkngkTTGRWpnlpwlhtdswikysknlqaenKADSAEPETDDLCFLQFT 685
Cdd:cd05903     61 REHELAFILRR---------AKAKVFV--------VPERF----------------------RQFDPAAMPDAVALLLFT 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  686 SGSTGDAKGVMITHGGLIHNVKLMQRRYRST-SNTILVSwLPQYHDMGLIGGLFTALVSGGSSVLFSpmtfIKNPLLWLE 764
Cdd:cd05903    102 SGTTGEPKGVMHSHNTLSASIRQYAERLGLGpGDVFLVA-SPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALA 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  765 TMSKYQATHSAG-PNFAFELMLRRLESDKstarnyDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLsqeVMAPGYGLAE 843
Cdd:cd05903    177 LMREHGVTFMMGaTPFLTDLLNAVEEAGE------PLSRLRTFVCGGATVPRSLARRAAEL---LGA---KVCSAYGSTE 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  844 ncvfvscaygqgkpifvdwqgrvCCGYVDPNDPDVDIRIA----NPETGEEIK---------ESGKEGEIWISSSSAGIG 910
Cdd:cd05903    245 -----------------------CPGAVTSITPAPEDRRLytdgRPLPGVEIKvvddtgatlAPGVEGELLSRGPSVFLG 301

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  911 YWGREELSQKtfknelpDYPGRIYtRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR-PGC--C 986
Cdd:cd05903    302 YLDRPDLTAD-------AAPEGWF-RTGDLARLDEdGYLRITGRSKDIIIRGGENIPVLEVE------DLLLGhPGVieA 367

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  987 AVVGVPEEVLSTK--GISVSDSSDQVGLVVIAEVRDAKTVDKevvEKIKtrvaeEHGVTVASVklikPRtiskTTSGKIK 1064
Cdd:cd05903    368 AVVALPDERLGERacAVVVTKSGALLTFDELVAYLDRQGVAK---QYWP-----ERLVHVDDL----PR----TPSGKVQ 431


                   ...
gi 2130317402 1065 RFE 1067
Cdd:cd05903    432 KFR 434
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
649-1065 5.79e-26

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 115.97  E-value: 5.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  649 PWLHT-DSWIKYSKNLQAENKADS--AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWL 725
Cdd:COG1022    152 PRLLSlDELLALGREVADPAELEArrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFL 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  726 PQYHDMGLIGGLFtaLVSGGSSVLF--SPMTFIKN------------PLLWlETM-SKYQATHSAGP-------NFAFEL 783
Cdd:COG1022    232 PLAHVFERTVSYY--ALAAGATVAFaeSPDTLAEDlrevkptfmlavPRVW-EKVyAGIQAKAEEAGglkrklfRWALAV 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  784 ---MLRRLESDKSTARNYDLSSMIFLMVAAEPVRQIT---LKRFI--------ELTLPF---GLsqeVMAPGYGLAENCV 846
Cdd:COG1022    309 grrYARARLAGKSPSLLLRLKHALADKLVFSKLREALggrLRFAVsggaalgpELARFFralGI---PVLEGYGLTETSP 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  847 FVSC-AYGQ------GKPIfvdwqgrvccgyvdpndPDVDIRIANpetgeeikesgkEGEIWISSSSAGIGYWGREELSQ 919
Cdd:COG1022    386 VITVnRPGDnrigtvGPPL-----------------PGVEVKIAE------------DGEILVRGPNVMKGYYKNPEATA 436

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  920 KTFKnelPDypGriYTRTGDLGRII-DGKLFITGRIKDLIIVA-GRNIYSADIEKTVESS---SELL-----RPGCCAVV 989
Cdd:COG1022    437 EAFD---AD--G--WLHTGDIGELDeDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASpliEQAVvvgdgRPFLAALI 509

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  990 gVP-----EEVLSTKGISVSDSSDqvgLVVIAEVRDAktVDKEvVEKIKTRVAEEHgvTVASVKLI-KPRTISK---TTS 1060
Cdd:COG1022    510 -VPdfealGEWAEENGLPYTSYAE---LAQDPEVRAL--IQEE-VDRANAGLSRAE--QIKRFRLLpKEFTIENgelTPT 580


                   ....*
gi 2130317402 1061 GKIKR 1065
Cdd:COG1022    581 LKLKR 585
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 663-1065 8.52e-26

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: 113.31  E-value: 8.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKAD---SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLiGGLFT 739
Cdd:TIGR01923   94 IEAAGRYEtslSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFR 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  740 ALVSGGSSVLFSPmtfiKNPLLwlETMSKYQATH-SAGPNfafelMLRRLEsdKSTARNYDLSSmifLMVAAEPVRQITL 818
Cdd:TIGR01923  173 WLIEGATLRIVDK----FNQLL--EMIANERVTHiSLVPT-----QLNRLL--DEGGHNENLRK---ILLGGSAIPAPLI 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  819 KRFIELTLPFGLsqevmapGYGLAENCVFVSCAYGQGKPifvdwqGRVCCGYVDPNdpdVDIRIANPETGEEikesgkeG 898
Cdd:TIGR01923  237 EEAQQYGLPIYL-------SYGMTETCSQVTTATPEMLH------ARPDVGRPLAG---REIKIKVDNKEGH-------G 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  899 EIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESS 977
Cdd:TIGR01923  294 EIMVKGANLMKGYLYQGELTPAFEQQG--------WFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  978 SELLRpgcCAVVGVPEevlstkgisvsdssDQVGLVVIAEVRDAKTVDKEVVEKIKTRVAEEHGVTVASVKLikpRTISK 1057
Cdd:TIGR01923  366 PGIQE---AVVVPKPD--------------AEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKL---DELPY 425


                   ....*...
gi 2130317402 1058 TTSGKIKR 1065
Cdd:TIGR01923  426 NASGKILR 433
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 678-1067 4.05e-25

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: 111.23  E-value: 4.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSPMT 754
Cdd:cd05934     82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlprFSASR 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  755 FiknpllWLEtMSKYQAT--HSAGpnfafeLMLRRLesdKSTARNYDLSSMIFLMVAAEPVRQITLKRFIEltlPFGLsq 832
Cdd:cd05934    162 F------WSD-VRRYGATvtNYLG------AMLSYL---LAQPPSPDDRAHRLRAAYGAPNPPELHEEFEE---RFGV-- 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 eVMAPGYGLAENCVFVSCAYGQGKPIFvdwqgrvCCGYVDPndpDVDIRIANPETGEeiKESGKEGEIWISSSSAGI--- 909
Cdd:cd05934    221 -RLLEGYGMTETIVGVIGPRDEPRRPG-------SIGRPAP---GYEVRIVDDDGQE--LPAGEPGELVIRGLRGWGffk 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  910 GYWGREELSQKTFKNelpdypgrIYTRTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAV 988
Cdd:cd05934    288 GYYNMPEATAEAMRN--------GWFHTGDLGyRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE---AAV 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  989 VGVPEEVlstkgisvsdSSDQVGLVVIaeVRDAKTVD-KEVVEKIKTRVAeehgvtvasvKLIKPRTIS------KTTSG 1061
Cdd:cd05934    357 VAVPDEV----------GEDEVKAVVV--LRPGETLDpEELFAFCEGQLA----------YFKVPRYIRfvddlpKTPTE 414


                   ....*.
gi 2130317402 1062 KIKRFE 1067
Cdd:cd05934    415 KVAKAQ 420
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
675-1067 7.72e-25

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 112.07  E-value: 7.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK--------LMQRRYRstsntILVSWLPQYHDMGLIGG--LFTALvsG 744
Cdd:PRK08974   204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqakaaygpLLHPGKE-----LVVTALPLYHIFALTVNclLFIEL--G 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLfspmtfIKNPL---LWLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVRQITLKRF 821
Cdd:PRK08974   277 GQNLL------ITNPRdipGFVKELKKYPFTAITGVNTLFNALLNNEEFQE-----LDFSSLKLSVGGGMAVQQAVAERW 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 IELTLPFGLSqevmapGYGLAENCVFVSCAygqgkPI-FVDWQGRVccGYVDPNdpdVDIRIANPEtGEEIkESGKEGEI 900
Cdd:PRK08974   346 VKLTGQYLLE------GYGLTECSPLVSVN-----PYdLDYYSGSI--GLPVPS---TEIKLVDDD-GNEV-PPGEPGEL 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  901 WISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEKTVESSSE 979
Cdd:PRK08974   408 WVKGPQVMLGYWQRPEATDEVIKDG--------WLATGDIAVMDEeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  980 LLRpgcCAVVGVPEEVlstkgisvsdSSDQVGLVVIAevRDAKTVDKEVVEKIKtrvaeEH--GVTVAsvKLIKPRT-IS 1056
Cdd:PRK08974   480 VLE---VAAVGVPSEV----------SGEAVKIFVVK--KDPSLTEEELITHCR-----RHltGYKVP--KLVEFRDeLP 537

                          410
                   ....*....|.
gi 2130317402 1057 KTTSGKIKRFE 1067
Cdd:PRK08974   538 KSNVGKILRRE 548
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 529-982 1.50e-24

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: 109.71  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtseKPVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQALLKIENIAKSC 608
Cdd:cd17653     24 TYGELDAASNALANRLL---QLGVVPGDVVPLLSDRSLEMLVAILAILKA----------------GAAYVPLDAKLPSA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  609 NAVAILSTVGyhsavragsvKNLILLTgkngkttgrwpnlpwlhtdswikysknlqaenkaDSAepetDDLCFLQFTSGS 688
Cdd:cd17653     85 RIQAILRTSG----------ATLLLTT----------------------------------DSP----DDLAYIIFTSGS 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  689 TGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlIGGLFTALVSGGSSVLfspmtfiKNPLLWLETMSK 768
Cdd:cd17653    117 TGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDAC-IGEIFSTLCNGGTLVL-------ADPSDPFAHVAR 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  769 YQATHSAGPNFafelmLRRLEsdkstARNYDLSSMIFLmvAAEPVRQITLKRFIEltlpfglsQEVMAPGYGLAEnCVfV 848
Cdd:cd17653    189 TVDALMSTPSI-----LSTLS-----PQDFPNLKTIFL--GGEAVPPSLLDRWSP--------GRRLYNAYGPTE-CT-I 246

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  849 SCAYGQGKPIfvdwqGRVCCGYVDPNdpdVDIRIANPETgEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNElPD 928
Cdd:cd17653    247 SSTMTELLPG-----QPVTIGKPIPN---STCYILDADL-QPVPE-GVVGEICISGVQVARGYLGNPALTASKFVPD-PF 315

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402  929 YPG-RIYtRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLR 982
Cdd:cd17653    316 WPGsRMY-RTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 675-1067 2.37e-24

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: 109.09  E-value: 2.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY-RSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPM 753
Cdd:cd05919     89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 tfiKNPLLWLETMSKYQATHSAG-PNFaFELMLRrlESDKSTArnyDLSSMIFLMVAAEPvrqitlkrfieltLPFGLSQ 832
Cdd:cd05919    169 ---PTAERVLATLARFRPTVLYGvPTF-YANLLD--SCAGSPD---ALRSLRLCVSAGEA-------------LPRGLGE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVMA-------PGYGLAENC-VFVSCAYGQGKPifvDWQGRVCCGYvdpndpdvDIRIANPEtGEEIkESGKEGEIWISS 904
Cdd:cd05919    227 RWMEhfggpilDGIGATEVGhIFLSNRPGAWRL---GSTGRPVPGY--------EIRLVDEE-GHTI-PPGEEGDLLVRG 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  905 SSAGIGYWGREELSQKTFKNElpdypgriYTRTGDL-GRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVesssellrp 983
Cdd:cd05919    294 PSAAVGYWNNPEKSRATFNGG--------WYRTGDKfCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI--------- 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  984 gcCAVVGVPEEVLstkgISVSDSSDQVGLVVIAEVRDAKTVDKEVVEKIKTRVAEehgvTVASVKLikPRTIS------K 1057
Cdd:cd05919    357 --IQHPAVAEAAV----VAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLE----RLSAHKV--PRRIAfvdelpR 424

                          410
                   ....*....|
gi 2130317402 1058 TTSGKIKRFE 1067
Cdd:cd05919    425 TATGKLQRFK 434
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 523-996 3.18e-24

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: 109.85  E-value: 3.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVVS---RRTYRELHANASLISHKLLTSEkpvIKPGDRVLlVYVP-GLDFVDCFFGCLRArvlpvpvlppdplqrgG--- 595
Cdd:COG1021     43 AVVDgerRLSYAELDRRADRLAAGLLALG---LRPGDRVV-VQLPnVAEFVIVFFALFRA----------------Gaip 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  596 -QAL-----LKIENIAKSCNAVAILST--------VGYHSAVRAG--SVKNLILLTgkngkttgrwpnlpwlHTDSWIKY 659
Cdd:COG1021    103 vFALpahrrAEISHFAEQSEAVAYIIPdrhrgfdyRALARELQAEvpSLRHVLVVG----------------DAGEFTSL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  660 SKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIG-GLF 738
Cdd:COG1021    167 DALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  739 TALVSGGSSVL---FSPMTFiknpllwLETMSKYQATHSA-GPnfafELMLRRLESdkSTARNYDLSSMIFLMV-----A 809
Cdd:COG1021    247 GVLYAGGTVVLapdPSPDTA-------FPLIERERVTVTAlVP----PLALLWLDA--AERSRYDLSSLRVLQVggaklS 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQItlkrfiELTLPFGLsQEVmapgYGLAE---NC--------VFVSCaygQGKPIfvdwqgrvccgyvdpnDPDV 878
Cdd:COG1021    314 PELARRV------RPALGCTL-QQV----FGMAEglvNYtrlddpeeVILTT---QGRPI----------------SPDD 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 DIRIANPEtGEEIKEsGKEGEIW------ISsssagiGYWGREELSQKTFkneLPDypGriYTRTGDLGRII-DGKLFIT 951
Cdd:COG1021    364 EVRIVDED-GNPVPP-GEVGELLtrgpytIR------GYYRAPEHNARAF---TPD--G--FYRTGDLVRRTpDGYLVVE 428

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2130317402  952 GRIKDLIIVAGRNIYSADIEktvessSELLR-PGC--CAVVGVPEEVL 996
Cdd:COG1021    429 GRAKDQINRGGEKIAAEEVE------NLLLAhPAVhdAAVVAMPDEYL 470
catalase_like cd08150
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 1726-2031 4.22e-24

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: 104.95  E-value: 4.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1726 RYFHRIGVGGKGQLKIYDKIQGLPDHNIFHPGKSYPVIVRHSNSLSADDDARiDARGAAIRI-LSDDVGsggstppLLDL 1804
Cdd:cd08150      3 RGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKP-DIRGFAIKFtGVADAG-------TLDF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1805 TLKTGKAFYARTIADFATWLV---------CGLAAREEHVKRVPR-VRDAVWMSLRNADSFTELHYYSNICRLFRFTDGQ 1874
Cdd:cd08150     75 VLNNTPVFFIRNTSDYEDFVAefarsargePPLDFIAWYVEKRPEdLPNLLGARSQVPDSYAAARYFSQVTFAFINGAGK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1875 EMYVKFKLRPFDETISEDSgkvepvgilppdtgaiprDENDTRPLLFLADDFKRRVE-SPtgVRYIFQLQVQPvPQDEAT 1953
Cdd:cd08150    155 YRVVRSKDNPVDGIPSLED------------------HELEARPPDYLREELTERLQrGP--VVYDFRIQLND-DTDATT 213

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402 1954 RDialDCTKPWDeTEFPYIDIGEISIDQNLTKEESEKMEFNPYVRCHEIDVIPASScsqsaSIDHGRSLIYEICQHLR 2031
Cdd:cd08150    214 ID---NPTILWP-TEHPVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLG-----PILEVRRRVYTSSQGLR 282
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 675-1063 8.13e-24

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: 108.19  E-value: 8.13e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL-FSPM 753
Cdd:cd05909    145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFhPNPL 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFIKNPllwlETMSKYQATHSAG-PNFaFELMLRRlesdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLsq 832
Cdd:cd05909    225 DYKKIP----ELIYDKKATILLGtPTF-LRGYARA-------AHPEDFSSLRLVVAGAEKLKDTLRQEFQEK---FGI-- 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 eVMAPGYGLAENCVFVSCAYGQ--------GKPIfvdwqgrvccgyvdpndPDVDIRIANPETGEEIkESGKEGEIWISS 904
Cdd:cd05909    288 -RILEGYGTTECSPVISVNTPQspnkegtvGRPL-----------------PGMEVKIVSVETHEEV-PIGEGGLLLVRG 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  905 SSAGIGYWGREELSQKTFknelpdypGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvESSSELLRP 983
Cdd:cd05909    349 PNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIE---DILSEILPE 417

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  984 -GCCAVVGVPEEvlsTKGisvsdssDQVGLVVIAEVRDAKTVdkevvekikTRVAEEHGVTvasvKLIKPRTISKTT--- 1059
Cdd:cd05909    418 dNEVAVVSVPDG---RKG-------EKIVLLTTTTDTDPSSL---------NDILKNAGIS----NLAKPSYIHQVEeip 474


                   ....*..
gi 2130317402 1060 ---SGKI 1063
Cdd:cd05909    475 llgTGKP 481
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 672-1067 7.13e-23

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 106.00  E-value: 7.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  672 AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNvkLMQRRYRSTSN-----TILVSWLPQYHDMGLIGGLFTALVSGGS 746
Cdd:PRK05677   202 ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN--MLQCRALMGSNlnegcEILIAPLPLYHIYAFTFHCMAMMLIGNH 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  747 SVLfspmtfIKNPL---LWLETMSKYQATHSAGPNFAFELMLRRlesdkSTARNYDLSSMIFLMVAAEPVRQITLKRFIE 823
Cdd:PRK05677   280 NIL------ISNPRdlpAMVKELGKWKFSGFVGLNTLFVALCNN-----EAFRKLDFSALKLTLSGGMALQLATAERWKE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  824 LTlpfGLSqevMAPGYGLAENCVFVScaygqGKPIfvdwqGRVCCGYVDPNDPDVDIRIANPEtGEEIKeSGKEGEIWIS 903
Cdd:PRK05677   349 VT---GCA---ICEGYGMTETSPVVS-----VNPS-----QAIQVGTIGIPVPSTLCKVIDDD-GNELP-LGEVGELCVK 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  904 SSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLR 982
Cdd:PRK05677   411 GPQVMKGYWQRPEATDEILDSD-----G--WLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  983 pgcCAVVGVPEEvlstkgisvsDSSDQVGLVVIaeVRDAKTVDKE-VVEKIKTRVAeehGVTVAsvKLIKPR-TISKTTS 1060
Cdd:PRK05677   484 ---CAAIGVPDE----------KSGEAIKVFVV--VKPGETLTKEqVMEHMRANLT---GYKVP--KAVEFRdELPTTNV 543


                   ....*..
gi 2130317402 1061 GKIKRFE 1067
Cdd:PRK05677   544 GKILRRE 550
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 525-1066 7.34e-23

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: 105.53  E-value: 7.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  525 VSRRTYRELHANASLISHKLLTSekpVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQRGGQALlkieni 604
Cdd:cd05959     27 AGSLTYAELEAEARRVAGALRAL---GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL------ 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  605 AKSCNAVAILST----VGYHSAVRAGSVKNLILLTGKNGKTTGRwpnlPWLhTDSWIKYSKNLQAenkadsAEPETDDLC 680
Cdd:cd05959     98 EDSRARVVVVSGelapVLAAALTKSEHTLVVLIVSGGAGPEAGA----LLL-AELVAAEAEQLKP------AATHADDPA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  681 FLQFTSGSTGDAKGVMITHGGLIHNVKLMQRR-YRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLfspMTFIKNP 759
Cdd:cd05959    167 FWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVL---MPERPTP 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  760 LLWLETMSKYQATHSAGPNFAFELMLRrleSDKSTARnyDLSSMIFLMVAAEPVRQITLKRFIELtlpFGLSqevMAPGY 839
Cdd:cd05959    244 AAVFKRIRRYRPTVFFGVPTLYAAMLA---APNLPSR--DLSSLRLCVSAGEALPAEVGERWKAR---FGLD---ILDGI 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  840 GLAENC-VFVSCAYGQGKPifvDWQGRVCCGYvdpndpdvDIRIANpETGEEIKEsGKEGEIWISSSSAGIGYWGREELS 918
Cdd:cd05959    313 GSTEMLhIFLSNRPGRVRY---GTTGKPVPGY--------EVELRD-EDGGDVAD-GEPGELYVRGPSSATMYWNNRDKT 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  919 QKTFKNElpdypgriYTRTGD-LGRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVLS 997
Cdd:cd05959    380 RDTFQGE--------WTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGVEDEDGL 448

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402  998 TKgisvsdssdQVGLVVIAEVRDAKTVD-KEVVEKIKTRvaeehgvtVASVKLikPRTI------SKTTSGKIKRF 1066
Cdd:cd05959    449 TK---------PKAFVVLRPGYEDSEALeEELKEFVKDR--------LAPYKY--PRWIvfvdelPKTATGKIQRF 505
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 677-1067 2.36e-22

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 104.33  E-value: 2.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQ-------RRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL 749
Cdd:PRK07059   204 DDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpafEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNIL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 fspmtfIKNPL---LWLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFL----MVAAEPVRqitlKRFI 822
Cdd:PRK07059   284 ------IPNPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDK-----LDFSKLIVAngggMAVQRPVA----ERWL 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  823 ELTlpfGLSqevMAPGYGLAENCVFVSCaygqgKPIFVD-WQGrvCCGYVDPNDpDVDIRianPETGEEIKeSGKEGEIW 901
Cdd:PRK07059   349 EMT---GCP---ITEGYGLSETSPVATC-----NPVDATeFSG--TIGLPLPST-EVSIR---DDDGNDLP-LGEPGEIC 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  902 ISSSSAGIGYWGREElsqKTFKNELPDypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSEL 980
Cdd:PRK07059   411 IRGPQVMAGYWNRPD---ETAKVMTAD--G--FFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGV 483

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  981 LRpgcCAVVGVPEEvlstkgisvsDSSDQVGLVVIAevRDAKTVDKEVVEKIKTRVAeehGVTVAsvKLIKPRT-ISKTT 1059
Cdd:PRK07059   484 LE---VAAVGVPDE----------HSGEAVKLFVVK--KDPALTEEDVKAFCKERLT---NYKRP--KFVEFRTeLPKTN 543


                   ....*...
gi 2130317402 1060 SGKIKRFE 1067
Cdd:PRK07059   544 VGKILRRE 551
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 684-1065 2.50e-22

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: 101.18  E-value: 2.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  684 FTSGSTGDAKGVMITHGGLI-HNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLfTALVSGGSSVLFSPMTFIKNPLLW 762
Cdd:cd17635      8 FTSGTTGEPKAVLLANKTFFaVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTTYKSLFKI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  763 LETmskYQAThsaGPNFAFELMLRRLESDKSTarNYDLSSMIFLMVAAEPVRQITlKRFIELtlpFGLSQEVMApgYGLA 842
Cdd:cd17635     87 LTT---NAVT---TTCLVPTLLSKLVSELKSA--NATVPSLRLIGYGGSRAIAAD-VRFIEA---TGLTNTAQV--YGLS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  843 ENcvfvscaygqgkpifvdwqGRVCC-----GYVDPND-----PDVDIRIANPETGEEIkeSGKEGEIWISSSSAGIGYW 912
Cdd:cd17635    153 ET-------------------GTALClptddDSIEINAvgrpyPGVDVYLAATDGIAGP--SASFGTIWIKSPANMLGYW 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  913 GREELSQKTFKNElpdypgriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVEsssELLRPGCCAVVGV 991
Cdd:cd17635    212 NNPERTAEVLIDG--------WVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAE---GVSGVQECACYEI 280

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130317402  992 PEEVLstkgisvsdssdqvGLVVIAEVRDAKTVDKEVVEKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKR 1065
Cdd:cd17635    281 SDEEF--------------GELVGLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 523-954 3.42e-22

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: 105.71  E-value: 3.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVVSRR---TYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGqALL 599
Cdd:COG1020    494 AVVFGDqslTYAELNARANRLAHHLRALG---VGPGDLVGVCLERSLEMVVALLAVLKA---------------GA-AYV 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 KI------ENIAkscnavAILStvgyHSAVRagsvknlILLTgkNGKTTGRWP--NLPWLHTDSwikysknlQAENKADS 671
Cdd:COG1020    555 PLdpaypaERLA------YMLE----DAGAR-------LVLT--QSALAARLPelGVPVLALDA--------LALAAEPA 607

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  672 AEPET----DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlIGGLFTALVSGGSS 747
Cdd:COG1020    608 TNPPVpvtpDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATL 686

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 VLFSPMTfIKNPLLWLETMSKYQATHSagpNF---AFELMLRRLESdkstarnyDLSSMIFLMVAAEPVRQITLKRFIEL 824
Cdd:COG1020    687 VLAPPEA-RRDPAALAELLARHRVTVL---NLtpsLLRALLDAAPE--------ALPSLRLVLVGGEALPPELVRRWRAR 754

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 tlpfgLSQEVMAPGYGLAENCVFVSCAYGQ-----------GKPIfvdWQGRVccgYV-DPNDPDVDIrianpetgeeik 892
Cdd:COG1020    755 -----LPGARLVNLYGPTETTVDSTYYEVTppdadggsvpiGRPI---ANTRV---YVlDAHLQPVPV------------ 811

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402  893 esGKEGEIWISSSSAGIGYWGREELSQKTFkneLPD---YPG-RIYtRTGDLGRII-DGKLFITGRI 954
Cdd:COG1020    812 --GVPGELYIGGAGLARGYLNRPELTAERF---VADpfgFPGaRLY-RTGDLARWLpDGNLEFLGRA 872
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1271-1681 7.40e-22

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: 103.68  E-value: 7.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1271 GYPWLdymfSLAFAPLTWILCIFSTCISITFFGNSF------------LRPNytlspEVSIWSADFVKWWALYKAHEISS 1338
Cdd:TIGR02353   24 GYNWL----YEALDDVSWLYLRAVALVFAVPVGRLGfaiaakwllvgrWKPG-----TYPIWGSTYLRFWTVKRLVDAAP 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1339 kvfAVYLRGTVFLNCWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGVLVQGHEVRNGVLSFLPIRIGRNSSV 1416
Cdd:TIGR02353   95 ---TVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFI 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1417 GPFAVIQKGSIIGDEA--DAGAAVQ-NEAI---YHFIGIymvsflstlAAAIIYFLYIRVAEK--PTSPqhfAFLCISGA 1488
Cdd:TIGR02353  170 GTRSTLDIDTSIGDGAqlGHGSALQgGQSIpdgERWHGS---------PAQKTGADYRKVQPArpYTVR---RRLYVAGA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1489 FHWMPFTMIAYATMFAnVPSNPAYFAISVSIAYLLHG----LVLSFLTS---IVAQFLAgkqdekqSQMKTWLSN----- 1556
Cdd:TIGR02353  238 LFVVFVLLPPLAFLFA-IPVAITFDEIDWTLGPDMVGfilaLVLTFVALagfIAYTVLL-------LAAVRLLLNlvlkp 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1557 -RITIACHLRFAK---------------LLSGTEAFCMYFRLLGAEVGKHCSIRAINpVSCPKQISIGAGVHLGDFSRII 1620
Cdd:TIGR02353  310 gRYYVHSGFYYQAwtvqqlmdnsrvllfPLYASSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGLLMG 388

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1621 SGFYSSTGFISGKVEVQENSVIGSQSLILPNSVVQKDVILGALSVAPAHSVLQQGGVYVGS 1681
Cdd:TIGR02353  389 NARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 678-1000 1.40e-21

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: 98.73  E-value: 1.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHgglIHNVKLMQR-----RYRSTSNTILVSwlPQYHDMGLIGGLFTALVSGGSSVlfsP 752
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAH---RQTLRAAAAwadcaDLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGATVV---P 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 MTfIKNPLLWLETMSKYQATHSAGPNFAFELMLrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRfIELTLPFglsq 832
Cdd:cd17638     73 VA-VFDVDAILEAIERERITVLPGPPTLFQSLL-----DHPGRKKFDLSSLRAAVTGAATVPVELVRR-MRSELGF---- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVMAPGYGLAENCVFVSCAYGQGKPIFVDWQGRVCcgyvdpndPDVDIRIANPetgeeikesgkeGEIWISSSSAGIGYW 912
Cdd:cd17638    142 ETVLTAYGLTEAGVATMCRPGDDAETVATTCGRAC--------PGFEVRIADD------------GEVLVRGYNVMQGYL 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  913 GREELSQKTFknelpDYPGriYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEKTVessSELLRPGCCAVVGV 991
Cdd:cd17638    202 DDPEATAEAI-----DADG--WLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGAL---AEHPGVAQVAVIGV 271


                   ....*....
gi 2130317402  992 PEEVLSTKG 1000
Cdd:cd17638    272 PDERMGEVG 280
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 664-1065 1.52e-21

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 101.59  E-value: 1.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  664 QAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNV--KLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTAL 741
Cdd:PLN02330   171 RAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATL 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVL---FSPMTFIkNPLLWLETmskyqathSAGPnFAFELMLRRLESdkSTARNYDLSSMIF--LMVAAEPVRQI 816
Cdd:PLN02330   251 RNKGKVVVmsrFELRTFL-NALITQEV--------SFAP-IVPPIILNLVKN--PIVEEFDLSKLKLqaIMTAAAPLAPE 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  817 TLKRFiELTLPFGLSQEvmapGYGLAE-NCVFVScaygQGKPifVDWQG---RVCCGYVDPNdpdVDIRIANPETGEEIK 892
Cdd:PLN02330   319 LLTAF-EAKFPGVQVQE----AYGLTEhSCITLT----HGDP--EKGHGiakKNSVGFILPN---LEVKFIDPDTGRSLP 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  893 ESgKEGEIWISSSSAGIGYWGREELSQKTFknelpDYPGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:PLN02330   385 KN-TPGELCVRSQCVMQGYYNNKEETDRTI-----DEDG--WLHTGDIGYIDdDGDIFIVDRIKELIKYKGFQVAPAELE 456

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  972 KTVessseLLRPGC--CAVVGVPEEvlstkgisvsdSSDQVGLVVIAEVRDAKTVDKEVVEKIKTRVAeeHGVTVASVKL 1049
Cdd:PLN02330   457 AIL-----LTHPSVedAAVVPLPDE-----------EAGEIPAACVVINPKAKESEEDILNFVAANVA--HYKKVRVVQF 518

                          410
                   ....*....|....*.
gi 2130317402 1050 IKprTISKTTSGKIKR 1065
Cdd:PLN02330   519 VD--SIPKSLSGKIMR 532
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 671-994 1.59e-21

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: 100.81  E-value: 1.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTS--NTILVSWLpqYHDMGlIGGLFTALVSGGSSV 748
Cdd:cd12114    120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPddRVLALSSL--SFDLS-VYDIFGALSAGATLV 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LFSPMTfIKNPLLWLETMSKYQATHSagpNFA---FELMLRRLESDKSTARNydlssmiflmvaaepVRQITLK-RFIEL 824
Cdd:cd12114    197 LPDEAR-RRDPAHWAELIERHGVTLW---NSVpalLEMLLDVLEAAQALLPS---------------LRLVLLSgDWIPL 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 TLPFGLSQ-----EVMAPGyGLAENCVF-------------VSCAYGQ---GKPIFV-DWQGRVCcgyvdpndPDvdiri 882
Cdd:cd12114    258 DLPARLRAlapdaRLISLG-GATEASIWsiyhpidevppdwRSIPYGRplaNQRYRVlDPRGRDC--------PD----- 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  883 anpetgeeikesGKEGEIWISSSSAGIGYWGREELSQKTFkneLPDYPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIV 960
Cdd:cd12114    324 ------------WVPGELWIGGRGVALGYLGDPELTAARF---VTHPDGeRLY-RTGDLGRYRpDGTLEFLGRRDGQVKV 387

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2130317402  961 AGRNIYSADIEKTVESSSELLRpGCCAVVGVPEE 994
Cdd:cd12114    388 RGYRIELGEIEAALQAHPGVAR-AVVVVLGDPGG 420
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 677-992 2.84e-21

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 100.34  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSsvlfspMTFI 756
Cdd:PRK07514   156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGAS------MIFL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 K--NPLLWLETMSkyQATHSAG-PNFaFELMLRRLESDKSTARNYDLssmiFLMVAAePVRQITLKRFIELTlpfglsqe 833
Cdd:PRK07514   230 PkfDPDAVLALMP--RATVMMGvPTF-YTRLLQEPRLTREAAAHMRL----FISGSA-PLLAETHREFQERT-------- 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 vmapG------YGLAENCVFVSCAYgQGKpifvdwqgRVCcGYVDPNDPDVDIRIANPETGEEIkESGKEGEIWISSSSA 907
Cdd:PRK07514   294 ----GhailerYGMTETNMNTSNPY-DGE--------RRA-GTVGFPLPGVSLRVTDPETGAEL-PPGEIGMIEVKGPNV 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  908 GIGYWGREElsqKTfKNEL-PDypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEK-------TVESss 978
Cdd:PRK07514   359 FKGYWRMPE---KT-AEEFrAD--G--FFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGeidelpgVVES-- 428

                          330
                   ....*....|....
gi 2130317402  979 ellrpgccAVVGVP 992
Cdd:PRK07514   429 --------AVIGVP 434
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 676-1075 4.37e-21

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: 100.85  E-value: 4.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  676 TDDLCFLqFTSGSTGDAKGVMITHGGliHNVKL---MQRRYRSTSNTilVSWLPQyhDMGLIGG----LFTALVSGGSSV 748
Cdd:cd05967    230 TDPLYIL-YTSGTTGKPKGVVRDNGG--HAVALnwsMRNIYGIKPGD--VWWAAS--DVGWVVGhsyiVYGPLLHGATTV 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LFS--PmTFIKNPLLWLETMSKYQATH--SAgPNfAFElMLRRLESDKSTARNYDLSSMIFLMVAAEPVRQITLKrFIEL 824
Cdd:cd05967    303 LYEgkP-VGTPDPGAFWRVIEKYQVNAlfTA-PT-AIR-AIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLE-WAEN 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 TLPfglsqevmAP----------GYGLAENCVFVSC----AYGQGKPIFvdwqgrvccGYvdpndpdvDIRIANpETGEE 890
Cdd:cd05967    378 TLG--------VPvidhwwqtetGWPITANPVGLEPlpikAGSPGKPVP---------GY--------QVQVLD-EDGEP 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  891 IKeSGKEGEIWIS---SSSAGIGYWGREELSQKTFkneLPDYPGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIY 966
Cdd:cd05967    432 VG-PNELGNIVIKlplPPGCLLTLWKNDERFKKLY---LSKFPG--YYDTGDAGYKdEDGYLFIMGRTDDVINVAGHRLS 505

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  967 SADIEKTVessseLLRPGC--CAVVGVPEEvlsTKGisvsdsSDQVGLVVIAEvrDAKTVDKEVVEKIKTRVAEEHGvTV 1044
Cdd:cd05967    506 TGEMEESV-----LSHPAVaeCAVVGVRDE---LKG------QVPLGLVVLKE--GVKITAEELEKELVALVREQIG-PV 568

                          410       420       430
                   ....*....|....*....|....*....|..
gi 2130317402 1045 ASVKL-IKPRTISKTTSGKIKRfECLKQFVDG 1075
Cdd:cd05967    569 AAFRLvIFVKRLPKTRSGKILR-RTLRKIADG 599
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 677-1067 5.32e-21

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: 98.56  E-value: 5.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHgglihnvklmqrRYRSTSNTILVSWLP-QYHDM-----------GLIGGLFTALVSG 744
Cdd:cd05972     81 EDPALIYFTSGTTGLPKGVLHTH------------SYPLGHIPTAAYWLGlRPDDIhwniadpgwakGAWSSFFGPWLLG 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLFSPMTFikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESdkstarNYDLSSMIFLMVAAEPVRQITLKRFIEl 824
Cdd:cd05972    149 ATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS------SYKFSHLRLVVSAGEPLNPEVIEWWRA- 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 tlPFGLSqevMAPGYGLAENCVFVSCAYGQ-------GKPIfvdwqgrvccgyvdpndPDVDIRIANPEtGEEIKEsGKE 897
Cdd:cd05972    220 --ATGLP---IRDGYGQTETGLTVGNFPDMpvkpgsmGRPT-----------------PGYDVAIIDDD-GRELPP-GEE 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWISSSSAGI--GYWGREELSQKTFKNElpdypgriYTRTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEktv 974
Cdd:cd05972    276 GDIAIKLPPPGLflGYVGDPEKTEASIRGD--------YYLTGDRAyRDEDGYFWFVGRADDIIKSSGYRIGPFEVE--- 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  975 essSELLR-PGC--CAVVGVPEEVlstkgisvsdssdqVGLVVIAEV--RDAKTVDKEVVEKIKTRVAEEHGVTVASVKL 1049
Cdd:cd05972    345 ---SALLEhPAVaeAAVVGSPDPV--------------RGEVVKAFVvlTSGYEPSEELAEELQGHVKKVLAPYKYPREI 407

                          410
                   ....*....|....*...
gi 2130317402 1050 IKPRTISKTTSGKIKRFE 1067
Cdd:cd05972    408 EFVEELPKTISGKIRRVE 425
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
526-1067 7.29e-21

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 99.44  E-value: 7.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  526 SRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLvYVPGL-DFVDCFFGCLRARVLPVPVLPPDPLQRGGQALLKieni 604
Cdd:PRK06087    48 ASYTYSALDHAASRLANWLLAKG---IEPGDRVAF-QLPGWcEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNK---- 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  605 aksCNAVAILSTVGYHS--------AVRAgSVKNL--ILLTGKNGKTTgrwpnlpwlhtdSWIKYSKNLQA-ENKADSAE 673
Cdd:PRK06087   120 ---CQAKMFFAPTLFKQtrpvdlilPLQN-QLPQLqqIVGVDKLAPAT------------SSLSLSQIIADyEPLTTAIT 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSpm 753
Cdd:PRK06087   184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD-- 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 tfIKNPLLWLETMSKYQATHSAGPN-FAFELmLRRLESDKstarnYDLSSMIFLMVAAEPVRqitlKRFIELTLPFGLsq 832
Cdd:PRK06087   262 --IFTPDACLALLEQQRCTCMLGATpFIYDL-LNLLEKQP-----ADLSALRFFLCGGTTIP----KKVARECQQRGI-- 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 eVMAPGYGLAENC--VFVScaygQGKPI--FVDWQGRVCCGyvdpndpdVDIRIANpetgEEIKE--SGKEGEiwisSSS 906
Cdd:PRK06087   328 -KLLSVYGSTESSphAVVN----LDDPLsrFMHTDGYAAAG--------VEIKVVD----EARKTlpPGCEGE----EAS 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  907 AG----IGYWGREELSQKTFKNElpdypGRIYtrTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVessSELL 981
Cdd:PRK06087   387 RGpnvfMGYLDEPELTARALDEE-----GWYY--SGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDIL---LQHP 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  982 RPGCCAVVGVPEEVLSTKGISvsdssdqvgLVVIAEVRDAKTVDkEVVE-----KIKTRVAEEHGVTVASvklikprtIS 1056
Cdd:PRK06087   457 KIHDACVVAMPDERLGERSCA---------YVVLKAPHHSLTLE-EVVAffsrkRVAKYKYPEHIVVIDK--------LP 518

                          570
                   ....*....|.
gi 2130317402 1057 KTTSGKIKRFE 1067
Cdd:PRK06087   519 RTASGKIQKFL 529
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 622-1037 9.39e-21

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: 98.86  E-value: 9.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  622 AVRAGSVKNLILLTGKNGKTTGRWPNlpWLHTDSWIkysknlqAENKADSAEPETD--DLCFLQFTSGSTGDAKGVMITH 699
Cdd:cd12119    115 APRLPTVEHVVVMTDDAAMPEPAGVG--VLAYEELL-------AAESPEYDWPDFDenTAAAICYTSGTTGNPKGVVYSH 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  700 GGLI-HNVKLMQR--RYRSTSNTILVSwLPQYHDMGLigGL-FTALVSGGSSVLFSPMTfikNPLLWLETMSKYQATHSA 775
Cdd:cd12119    186 RSLVlHAMAALLTdgLGLSESDVVLPV-VPMFHVNAW--GLpYAAAMVGAKLVLPGPYL---DPASLAELIEREGVTFAA 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  776 GPNFAFELMLRRLEsdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELTLPfglsqeVMApGYGLAENCVFVSCAY--- 852
Cdd:cd12119    260 GVPTVWQGLLDHLE-----ANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR------VIH-AWGMTETSPLGTVARpps 327

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  853 -GQGKPIFVDW-----QGRVCCGyvdpndpdVDIRIANPEtGEEIKESGKE-GEI-----WISSSsagigYWGREELSQK 920
Cdd:cd12119    328 eHSNLSEDEQLalrakQGRPVPG--------VELRIVDDD-GRELPWDGKAvGELqvrgpWVTKS-----YYKNDEESEA 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  921 TFKNelpdypGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEE----- 994
Cdd:cd12119    394 LTED------G--WLRTGDVATIDeDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE---AAVIGVPHPkwger 462

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2130317402  995 -VLstkgisvsdssdqvgLVVIAEvrDAKTVDKEVVEKIKTRVA 1037
Cdd:cd12119    463 pLA---------------VVVLKE--GATVTAEELLEFLADKVA 489
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 527-1065 9.49e-21

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 99.24  E-value: 9.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgG------QALLK 600
Cdd:PRK08316    36 SWTYAELDAAVNRVAAALLDLG---LKKGDRVAALGHNSDAYALLWLACARA----------------GavhvpvNFMLT 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  601 IENIA---KSCNAVAILSTVGYHSAVRAGSVKNLILLTGKNGKTTGRWPNLPWLHTDSWIkysknLQAENKADSAEPETD 677
Cdd:PRK08316    97 GEELAyilDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWA-----EAGSVAEPDVELADD 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNvklmqrrYRST-------SNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLF 750
Cdd:PRK08316   172 DLAQILYTSGTESLPKGAMLTHRALIAE-------YVSCivagdmsADDIPLHALPLYHCAQLDVFLGPYLYVGATNVIL 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 -SPmtfikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSM--IFLMVAAEPVRqiTLKRFIElTLP 827
Cdd:PRK08316   245 dAP-----DPELILRTIEAERITSFFAPPTVWISLLRHPDFDT-----RDLSSLrkGYYGASIMPVE--VLKELRE-RLP 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  828 -------FGlsQEVMAPgygLAEncvfV-----------SCaygqGKPIFvdwqgrvccgyvdpndpDVDIRIANpETGE 889
Cdd:PRK08316   312 glrfyncYG--QTEIAP---LAT----VlgpeehlrrpgSA----GRPVL-----------------NVETRVVD-DDGN 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  890 EIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNelpdypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSA 968
Cdd:PRK08316   361 DVAP-GEVGEIVHRSPQLMLGYWDDPEKTAEAFRG------G--WFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASR 431

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  969 DIEKTV---ESSSELlrpgccAVVGVPEEvlstKGIsvsdssDQVGLVVIaeVRDAKTVD-KEVVEKIKTRvaeehgvtV 1044
Cdd:PRK08316   432 EVEEALythPAVAEV------AVIGLPDP----KWI------EAVTAVVV--PKAGATVTeDELIAHCRAR--------L 485

                          570       580
                   ....*....|....*....|....*...
gi 2130317402 1045 ASVKLikPRTI------SKTTSGKI-KR 1065
Cdd:PRK08316   486 AGFKV--PKRVifvdelPRNPSGKIlKR 511
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 650-1065 1.98e-20

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: 97.51  E-value: 1.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  650 WLHTDSWIkysknlQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYH 729
Cdd:cd05922     96 VLDADGIR------AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  730 DMGLiGGLFTALVSGGSSVLfsPMTFIKNPLLWlETMSKYQATHSAGPNFAFElMLRRLESDKSTarnydLSSMIFLMVA 809
Cdd:cd05922    170 DYGL-SVLNTHLLRGATLVL--TNDGVLDDAFW-EDLREHGATGLAGVPSTYA-MLTRLGFDPAK-----LPSLRYLTQA 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQITLKRFIELtLPfGLSQEVMapgYGLAEncVFVSCAY-----------GQGKPIfvdwqgrvccgyvdpndPDV 878
Cdd:cd05922    240 GGRLPQETIARLREL-LP-GAQVYVM---YGQTE--ATRRMTYlpperilekpgSIGLAI-----------------PGG 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 DIRIANPETGEEikESGKEGEIWISSSSAGIGYWGRE-ELSQKTFKNelpdypGRIYtrTGDLGRI-IDGKLFITGRIKD 956
Cdd:cd05922    296 EFEILDDDGTPT--PPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGG------GVLH--TGDLARRdEDGFLFIVGRRDR 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  957 LIIVAGRNIYSADIEKTVESSSELlrpGCCAVVGVPEevlstkgisvsDSSDQVGLVViaeVRDAKTVDKEVvekikTRV 1036
Cdd:cd05922    366 MIKLFGNRISPTEIEAAARSIGLI---IEAAAVGLPD-----------PLGEKLALFV---TAPDKIDPKDV-----LRS 423

                          410       420       430
                   ....*....|....*....|....*....|
gi 2130317402 1037 AEEHGVTVASVKLIKP-RTISKTTSGKIKR 1065
Cdd:cd05922    424 LAERLPPYKVPATVRVvDELPLTASGKVDY 453
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 677-1063 2.06e-20

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: 95.63  E-value: 2.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTFi 756
Cdd:cd05944      2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 KNPLL----WlETMSKYQATH-SAGPNFAFELMLRRLesdkstarNYDLSSMIFLMVAAEPVRQITLKRFIELTlpfGLS 831
Cdd:cd05944     81 RNPGLfdnfW-KLVERYRITSlSTVPTVYAALLQVPV--------NADISSLRFAMSGAAPLPVELRARFEDAT---GLP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  832 qevMAPGYGLAENCVFVSCAY--GQGKPifvdwqGRVccGYVDPNdPDVDIRIANPETGEEIKESGKE-GEIWISSSSAG 908
Cdd:cd05944    149 ---VVEGYGLTEATCLVAVNPpdGPKRP------GSV--GLRLPY-ARVRIKVLDGVGRLLRDCAPDEvGEICVAGPGVF 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  909 IGYWgREELSQKTFKNELpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELlrpGCCA 987
Cdd:cd05944    217 GGYL-YTEGNKNAFVADG-------WLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV---AFAG 285

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402  988 VVGVPEEvlstkgisvsdSSDQVGLVVIAEVRDAKTVDKEVVEKIKTRVAEEHGVTVAsVKLIKPrtISKTTSGKI 1063
Cdd:cd05944    286 AVGQPDA-----------HAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAVPKH-IEVLEE--LPVTAVGKV 347
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 669-992 2.32e-20

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: 96.93  E-value: 2.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPET-----DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLiGGLFTALVS 743
Cdd:cd05945     84 LDAAKPALliadgDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALAS 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 GGSSVLFsPMTFIKNPLLWLETMSKYQAT--HSAgPNFAfeLMLRRLESDKStARNYDLSSMIFlmvAAEPvrqitlkrf 821
Cdd:cd05945    163 GATLVPV-PRDATADPKQLFRFLAEHGITvwVST-PSFA--AMCLLSPTFTP-ESLPSLRHFLF---CGEV--------- 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  822 ieltLPFGLSQEVM--APG------YGLAENCvfVSCAYGQGKPIFVDWQGRVCCGYVdpnDPDVDIRIANpETGEEIKE 893
Cdd:cd05945    226 ----LPHKTARALQqrFPDariyntYGPTEAT--VAVTYIEVTPEVLDGYDRLPIGYA---KPGAKLVILD-EDGRPVPP 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  894 sGKEGEIWISSSSAGIGYWGREELSQKTFkneLPDYPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEK 972
Cdd:cd05945    296 -GEKGELVISGPSVSKGYLNNPEKTAAAF---FPDEGQRAY-RTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEA 370

                          330       340
                   ....*....|....*....|
gi 2130317402  973 TVESSSELlrpGCCAVVGVP 992
Cdd:cd05945    371 ALRQVPGV---KEAVVVPKY 387
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 677-994 4.23e-20

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 97.20  E-value: 4.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNvklMQRRYRSTSNT-------------ILVSWLPQYHDMGLIGGLFTALVS 743
Cdd:PRK12492   207 DDIAVLQYTGGTTGLAKGAMLTHGNLVAN---MLQVRACLSQLgpdgqplmkegqeVMIAPLPLYHIYAFTANCMCMMVS 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 GGSSVLfspmtfIKNPLL---WLETMSKYQATHSAGPNFAF-ELMlrrlesDKSTARNYDLSSM--------IFLMVAAE 811
Cdd:PRK12492   284 GNHNVL------ITNPRDipgFIKELGKWRFSALLGLNTLFvALM------DHPGFKDLDFSALkltnsggtALVKATAE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  812 PVRQITLKRFIEltlpfglsqevmapGYGLAEnCVFVSCA--YGQgkpifvdwQGRVccGYVDPNDPDVDIRIANPEtGE 889
Cdd:PRK12492   352 RWEQLTGCTIVE--------------GYGLTE-TSPVASTnpYGE--------LARL--GTVGIPVPGTALKVIDDD-GN 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  890 EIKeSGKEGEIWISSSSAGIGYWGREELSQktfknELPDYPGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSA 968
Cdd:PRK12492   406 ELP-LGERGELCIKGPQVMKGYWQQPEATA-----EALDAEG--WFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPN 477

                          330       340
                   ....*....|....*....|....*.
gi 2130317402  969 DIEKTVESSSELlrpGCCAVVGVPEE 994
Cdd:PRK12492   478 EIEDVVMAHPKV---ANCAAIGVPDE 500
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 677-994 1.22e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 96.00  E-value: 1.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFtALVSGGSSVLFSPMTFi 756
Cdd:PRK12583   201 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANL-GCMTVGACLVYPNEAF- 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 kNPLLWLETMSKYQAT--HSAGPNFAFELmlrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRFI-ELTLPfglsqE 833
Cdd:PRK12583   279 -DPLATLQAVEEERCTalYGVPTMFIAEL-------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMdEMHMA-----E 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 VMApGYGLAENCVfVSCAYGQGKPIfvdwQGRVCCgyVDPNDPDVDIRIANPEtGEEIKeSGKEGEIWISSSSAGIGYWG 913
Cdd:PRK12583   346 VQI-AYGMTETSP-VSLQTTAADDL----ERRVET--VGRTQPHLEVKVVDPD-GATVP-RGEIGELCTRGYSVMKGYWN 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  914 REELSQKTFknelpDYPGRIYtrTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVP 992
Cdd:PRK12583   416 NPEATAESI-----DEDGWMH--TGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD---VQVFGVP 485


                   ..
gi 2130317402  993 EE 994
Cdd:PRK12583   486 DE 487
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 654-971 1.83e-19

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: 94.70  E-value: 1.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSKNLQAENKADsaepetdDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRST--SNTILVSwlPQYHDM 731
Cdd:cd17655    121 TIYHEESENLEPVSKSD-------DLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGehLRVALFA--SISFDA 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  732 GlIGGLFTALVSGGSSVLFSPMTFIKNPLLwLETMSKYQATHSAGPnfafELMLRRL-ESDKSTArnydlSSMIFLMVAA 810
Cdd:cd17655    192 S-VTEIFASLLSGNTLYIVRKETVLDGQAL-TQYIRQNRITIIDLT----PAHLKLLdAADDSEG-----LSLKHLIVGG 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  811 EPVRQITLKRFIELtlpFGLSQEVMApGYGLAENCvfVSCAYGQGKPIfVDWQGRVCCGyvdpnDPDVDIRIANPETGEE 890
Cdd:cd17655    261 EALSTELAKKIIEL---FGTNPTITN-AYGPTETT--VDASIYQYEPE-TDQQVSVPIG-----KPLGNTRIYILDQYGR 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  891 IKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElPDYPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSA 968
Cdd:cd17655    329 PQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDD-PFVPGeRMY-RTGDLARWLpDGNIEFLGRIDHQVKIRGYRIELG 406


                   ...
gi 2130317402  969 DIE 971
Cdd:cd17655    407 EIE 409
PRK07529 PRK07529
AMP-binding domain protein; Validated
 624-992 2.34e-19

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 95.41  E-value: 2.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  624 RAGSVKNLILLTGKNGKTTGRWPNLPWLHTDSWIKYsKNLQAENKADSAE-------PETDDLCFLQFTSGSTGDAKGVM 696
Cdd:PRK07529   154 ALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARI-LDFDAELARQPGDrlfsgrpIGPDDVAAYFHTGGTTGMPKLAQ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  697 ITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTF-----IKNplLWlETMSKYQA 771
Cdd:PRK07529   233 HTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYrgpgvIAN--FW-KIVERYRI 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  772 TH-SAGPNFAFELMLRRLESdkstarnYDLSSMIFLMVAAEPVRQITLKRFIELTlpfGLSqevMAPGYGLAENCVFVSC 850
Cdd:PRK07529   310 NFlSGVPTVYAALLQVPVDG-------HDISSLRYALCGAAPLPVEVFRRFEAAT---GVR---IVEGYGLTEATCVSSV 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  851 AygqgkpiFVDWQGRVccGYVDPNDPDVDIRIAN-PETGEEIKES--GKEGEIWISSSSAGIGYWGREelsqktfKNELP 927
Cdd:PRK07529   377 N-------PPDGERRI--GSVGLRLPYQRVRVVIlDDAGRYLRDCavDEVGVLCIAGPNVFSGYLEAA-------HNKGL 440

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  928 DYPGRiYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTvessseLLR-P--GCCAVVGVP 992
Cdd:PRK07529   441 WLEDG-WLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEA------LLRhPavALAAAVGRP 502
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
665-1037 2.56e-19

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 94.57  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  665 AENKADSAEPE--TDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALV 742
Cdd:PRK05852   162 TEPTPATSTPEglRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  743 SGGSSVL-----FSPMTFiknpllWlETMSKYQAT-HSAGPNFaFELMLRRLESDKSTARNYDLSsmiFLMVAAEPVRQI 816
Cdd:PRK05852   242 SGGAVLLpargrFSAHTF------W-DDIKAVGATwYTAVPTI-HQILLERAATEPSGRKPAALR---FIRSCSAPLTAE 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  817 TLKrfieltlpfGLSQEVMAPgyglaencvfVSCAYG------QGKPIFVDWQGR-----VCCGYVDPNDpDVDIRIANP 885
Cdd:PRK05852   311 TAQ---------ALQTEFAAP----------VVCAFGmteathQVTTTQIEGIGQtenpvVSTGLVGRST-GAQIRIVGS 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  886 ETGEeiKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRN 964
Cdd:PRK05852   371 DGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG--------WLRTGDLGSLsAAGDLSIRGRIKELINRGGEK 440

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402  965 IYSADIEKTVESSSELLRpgcCAVVGVPEEVLstkgisvsdsSDQVGLVVIAEVRDAKTVDkEVVEKIKTRVA 1037
Cdd:PRK05852   441 ISPERVEGVLASHPNVME---AAVFGVPDQLY----------GEAVAAVIVPRESAPPTAE-ELVQFCRERLA 499
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1231-1670 2.82e-19

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: 95.20  E-value: 2.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1231 GIWMFQLLALTYVLAIMifPAYLsvcAFIQLVSATHTLTDGYPWLDYMFSLAFAPLT-WILCIFSTCISITFFGNSFLRP 1309
Cdd:TIGR02353  235 AGALFVVFVLLPPLAFL--FAIP---VAITFDEIDWTLGPDMVGFILALVLTFVALAgFIAYTVLLLAAVRLLLNLVLKP 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1310 N--YTLSpevsiwsadfvkwWALYKAHEIS-----SKVFAVYLRGTVFLNCWFEMLGARIGSSVLLDTVDITDPSLVSIG 1382
Cdd:TIGR02353  310 GryYVHS-------------GFYYQAWTVQqlmdnSRVLLFPLYASSYIPHWYRALGAKIGKVAEISSAQHEVPDLTDIG 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1383 DGAVIAEGVLVQGHEVRNGVLSFLPIRIGRNSSVGPFAVIQKGSIIGDE----------ADAGAA--------------- 1437
Cdd:TIGR02353  377 EETFIADGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNvllgvlsmtpKDGKVRegvgwlgsppfelpr 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1438 VQNEAIYHFIGIYMVSFLSTLAAAIIYFLYIrvaekptspqhFAFLCISGAFHWMPFTMI-----AYATMFANVPSNPAY 1512
Cdd:TIGR02353  457 RVNRDDELEALTFEPDPRRRLARKNVENLRI-----------ILPFLLVQWAMLFALVVLdlqalDDYTEWGAVALLAAL 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1513 FAISVSiayllhglVLSFLTSIVAQFLA-GKQdekQSQMKT------WLSNRIT----IACHLRFAKLLSGTEAFCMYFR 1581
Cdd:TIGR02353  526 ILMAVG--------VGAFLILVERKWLVfGRL---KPQEHPlwspfvWLHELHWklyeSVAVPNFLRPFRGTPFLPAILR 594

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1582 LLGAEVGKHCSIRA--INPVSCpkqISIGAGVHLGDFSRIISGFYSSTGFISGKVEVQENSVIGSQSLILPNSVVQKDVI 1659
Cdd:TIGR02353  595 LLGVKIGRGVYIDGtdLTERDL---VTIGDDSTLNEGSVIQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSV 671

                          490
                   ....*....|....*..
gi 2130317402 1660 LGALSVA------PAHS 1670
Cdd:TIGR02353  672 LGPDSLVmkgeevPAHT 688
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 490-1063 3.80e-19

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: 94.57  E-value: 3.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  490 FPDLS------SLDGYLKHWGthrvtqNKTLYTWINEEGAVVSRRTYRELHANASLISHKLLTSEkpvIKPGDRVLlVYV 563
Cdd:cd17634     47 FEDATlnlaanALDRHLRENG------DRTAIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLG---VKKGDRVA-IYM 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  564 PGL-DFVDCFFGCLRARVLPVPVLppdplqrGGQALLKIENIAKSCNAVAILSTVGYHSAVR---------------AGS 627
Cdd:cd17634    117 PMIpEAAVAMLACARIGAVHSVIF-------GGFAPEAVAGRIIDSSSRLLITADGGVRAGRsvplkknvddalnpnVTS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  628 VKNLILL--TGKN-GKTTGRWPnlpWLHTdswikysknlQAENKADSAEPE---TDDLCFLQFTSGSTGDAKGVMITHGG 701
Cdd:cd17634    190 VEHVIVLkrTGSDiDWQEGRDL---WWRD----------LIAKASPEHQPEamnAEDPLFILYTSGTTGKPKGVLHTTGG 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  702 liHNVKLMQR-RYRSTSNTILVSWLpqYHDMGLIGG----LFTALVSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSag 776
Cdd:cd17634    257 --YLVYAATTmKYVFDYGPGDIYWC--TADVGWVTGhsylLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNIL-- 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  777 pnFAFELMLRRL--ESDKSTARnYDLSSMIFLMVAAEPVRQITLKRFIELTlpfglsqevmapgyglaencvfvscaYGQ 854
Cdd:cd17634    331 --YTAPTAIRALmaAGDDAIEG-TDRSSLRILGSVGEPINPEAYEWYWKKI--------------------------GKE 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  855 GKPIFVDWQGRVCCGYVDPNDPDVDIRIA----NPETGEEIK---------ESGKEGEIWISSSSAG--IGYWGR----E 915
Cdd:cd17634    382 KCPVVDTWWQTETGGFMITPLPGAIELKAgsatRPVFGVQPAvvdneghpqPGGTEGNLVITDPWPGqtRTLFGDherfE 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  916 ELSQKTFKNelpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEE 994
Cdd:cd17634    462 QTYFSTFKG---------MYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE---AAVVGIPHA 529

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  995 VlstKGISVsdssdqVGLVVI-AEVRDAKTVDKEVVEkiktRVAEEHGVTVASVKLIKPRTISKTTSGKI 1063
Cdd:cd17634    530 I---KGQAP------YAYVVLnHGVEPSPELYAELRN----WVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 672-994 5.98e-19

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 94.99  E-value: 5.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  672 AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFS 751
Cdd:PRK08633   777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP 856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 pmtfikNPLLWL---ETMSKYQATHSAG-PNFaFELMLRRLESDKStarnyDLSSMIFLMVAAEPVRQITLKRFIEltlP 827
Cdd:PRK08633   857 ------DPTDALgiaKLVAKHRATILLGtPTF-LRLYLRNKKLHPL-----MFASLRLVVAGAEKLKPEVADAFEE---K 921

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  828 FGLsqEVMApGYGLAENC--VFVSCaygqgkPIFVDWQGRVCC----GYVDPNDPDVDIRIANPETGEEIKEsGKEGEIW 901
Cdd:PRK08633   922 FGI--RILE-GYGATETSpvASVNL------PDVLAADFKRQTgskeGSVGMPLPGVAVRIVDPETFEELPP-GEDGLIL 991

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  902 ISSSSAGIGYWGREELSQKTFKnelpDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvESSSEL 980
Cdd:PRK08633   992 IGGPQVMKGYLGDPEKTAEVIK----DIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIGGEMVPLGAVE---EELAKA 1064

                          330
                   ....*....|....*.
gi 2130317402  981 L--RPGCCAVVGVPEE 994
Cdd:PRK08633  1065 LggEEVVFAVTAVPDE 1080
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 673-1065 7.29e-19

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 93.56  E-value: 7.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  673 EPEtDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKL-MQRRYRSTS-NTILVSWLPQYHDMGLIGGLFTALVSGGSSVLF 750
Cdd:PRK06710   203 DPE-NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 sPMTFIKnplLWLETMSKYQATHSAG-PNFAFELMlrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELTlpfg 829
Cdd:PRK06710   282 -PKFDMK---MVFEAIKKHKVTLFPGaPTIYIALL------NSPLLKEYDISSIRACISGSAPLPVEVQEKFETVT---- 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 lsQEVMAPGYGLAENCVFVSCAYgqgkpifvDWQGRVcCGYVDPNDPDVDIRIANPETGEEIKeSGKEGEIWISSSSAGI 909
Cdd:PRK06710   348 --GGKLVEGYGLTESSPVTHSNF--------LWEKRV-PGSIGVPWPDTEAMIMSLETGEALP-PGEIGEIVVKGPQIMK 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  910 GYWGREELSQKTFKNElpdypgriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAV 988
Cdd:PRK06710   416 GYWNKPEETAAVLQDG--------WLHTGDVGYMDeDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE---VVT 484

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  989 VGVPEEVlstKGISVSdssdqvGLVVIAEvrdaktvDKEVVEKIKTRVAEEHGVTVASVKLIKPRT-ISKTTSGKIKR 1065
Cdd:PRK06710   485 IGVPDPY---RGETVK------AFVVLKE-------GTECSEEELNQFARKYLAAYKVPKVYEFRDeLPKTTVGKILR 546
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 677-1073 1.14e-18

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: 92.22  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNT-IL--------VSwlpqyhdmglIGGLFTALVSGGSs 747
Cdd:cd05918    106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVS----------ILEIFTTLAAGGC- 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 vLFSP-----MTFIknpllwLETMSKYQATHsAG--PNFAfelmlRRLESDkstarnyDLSSMIFLMVAAEPVRQITLKR 820
Cdd:cd05918    175 -LCIPseedrLNDL------AGFINRLRVTW-AFltPSVA-----RLLDPE-------DVPSLRTLVLGGEALTQSDVDT 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  821 FIELTlpfglsqEVMApGYGLAENCVFVSCaygqgKPIFVDWQGR-------VCCGYVDPNDPDvdiRIAnPetgeeike 893
Cdd:cd05918    235 WADRV-------RLIN-AYGPAECTIAATV-----SPVVPSTDPRnigrplgATCWVVDPDNHD---RLV-P-------- 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  894 SGKEGEIWISSSSAGIGYWGREELSQKTF-------KNELPDYPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNI 965
Cdd:cd05918    290 IGAVGELLIEGPILARGYLNDPEKTAAAFiedpawlKQEGSGRGRRLY-RTGDLVRYNpDGSLEYVGRKDTQVKIRGQRV 368

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  966 YSADIEKTVESSSELLRPgCCAVVGVPeevlstkgisvSDSSDQVGLVVIAEVRDAKTVDKEVVEKIktrvAEEHGVTVA 1045
Cdd:cd05918    369 ELGEIEHHLRQSLPGAKE-VVVEVVKP-----------KDGSSSPQLVAFVVLDGSSSGSGDGDSLF----LEPSDEFRA 432

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2130317402 1046 SVKLIKPR------------------TISKTTSGKIKRfECLKQFV 1073
Cdd:cd05918    433 LVAELRSKlrqrlpsymvpsvflplsHLPLTASGKIDR-RALRELA 477
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 670-1071 1.86e-18

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: 90.87  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  670 DSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHdmglIGGL---FTALVSGGS 746
Cdd:cd05912     70 KDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLsilMRSVIYGMT 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  747 SVLFSPMtfikNPLLWLETMSKYQATH-SAGPNfafelMLRRLESDKSTARNYDLSSMiflMVAAEPVRQITLKRFIELT 825
Cdd:cd05912    146 VYLVDKF----DAEQVLHLINSGKVTIiSVVPT-----MLQRLLEILGEGYPNNLRCI---LLGGGPAPKPLLEQCKEKG 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  826 LPFGLSqevmapgYGLAENC---VFVSCAYGQ------GKPIFvdwqgrvccgyvdpndpDVDIRIANPETGEEikesgK 896
Cdd:cd05912    214 IPVYQS-------YGMTETCsqiVTLSPEDALnkigsaGKPLF-----------------PVELKIEDDGQPPY-----E 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  897 EGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVE 975
Cdd:cd05912    265 VGEILLKGPNVTKGYLNRPDATEESFENG--------WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  976 SssellRPGC--CAVVGVPEevlstkgisvsdssDQVGLVVIAEVRDAKTVDKEVVEKIktrvAEEHgvtVASVKLikPR 1053
Cdd:cd05912    337 S-----HPAIkeAGVVGIPD--------------DKWGQVPVAFVVSERPISEEELIAY----CSEK---LAKYKV--PK 388

                          410       420
                   ....*....|....*....|....
gi 2130317402 1054 TI------SKTTSGKIKRFEcLKQ 1071
Cdd:cd05912    389 KIyfvdelPRTASGKLLRHE-LKQ 411
PRK08315 PRK08315
AMP-binding domain protein; Validated
 677-995 3.42e-18

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 91.41  E-value: 3.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPmTFi 756
Cdd:PRK08315   199 DDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGE-GF- 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 kNPLLWLETMSKYQATHSAG-PN-FAFELMLRRLESdkstarnYDLSSM---IflMVAAE-PVRqiTLKRFIELtlpFGL 830
Cdd:PRK08315   277 -DPLATLAAVEEERCTALYGvPTmFIAELDHPDFAR-------FDLSSLrtgI--MAGSPcPIE--VMKRVIDK---MHM 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 SQEVMApgYGLAEnCVFVSCAYGQGKPI--FVDWQGRVccgyvdpnDPDVDIRIANPETGEEIkESGKEGEIWISSSSAG 908
Cdd:PRK08315   342 SEVTIA--YGMTE-TSPVSTQTRTDDPLekRVTTVGRA--------LPHLEVKIVDPETGETV-PRGEQGELCTRGYSVM 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  909 IGYWGREElsqKTfkNELPDYPGriYTRTGDLGrIID--GKLFITGRIKDLIIVAGRNIYSADIEktvesssELLR--PG 984
Cdd:PRK08315   410 KGYWNDPE---KT--AEAIDADG--WMHTGDLA-VMDeeGYVNIVGRIKDMIIRGGENIYPREIE-------EFLYthPK 474

                          330
                   ....*....|....*...
gi 2130317402  985 C--CAVVGVP-----EEV 995
Cdd:PRK08315   475 IqdVQVVGVPdekygEEV 492
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
529-1067 6.60e-18

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 90.32  E-value: 6.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLTSEKpvIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQR--------GGQALLK 600
Cdd:PRK08751    52 TYREADQLVEQFAAYLLGELQ--LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRElkhqlidsGASVLVV 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  601 IENIAKSCNAV--------AILSTVGYHSAVRAGSVKNLILLTGKNgkttgrwpNLPWLHTDSWIKYSKNLQAENK--AD 670
Cdd:PRK08751   130 IDNFGTTVQQViadtpvkqVITTGLGDMLGFPKAALVNFVVKYVKK--------LVPEYRINGAIRFREALALGRKhsMP 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNvklMQR--RYRSTSNTI------LVSWLPQYHDMGLIG-GLFTAL 741
Cdd:PRK08751   202 TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAN---MQQahQWLAGTGKLeegcevVITALPLYHIFALTAnGLVFMK 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLFSPM---TFIKNpllwletMSKYQATHSAGPNFAFELMLRRLESDKstarnYDLSSMIFLMVAAEPVRQITL 818
Cdd:PRK08751   279 IGGCNHLISNPRdmpGFVKE-------LKKTRFTAFTGVNTLFNGLLNTPGFDQ-----IDFSSLKMTLGGGMAVQRSVA 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  819 KRFIELTlpfGLSqevMAPGYGLAENcvfvscaygqgkpifvdwQGRVCCGYVDPNDPDVDIRIANPETGEEIKES---- 894
Cdd:PRK08751   347 ERWKQVT---GLT---LVEAYGLTET------------------SPAACINPLTLKEYNGSIGLPIPSTDACIKDDagtv 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  895 ---GKEGEIWISSSSAGIGYWGREELSQKTFknelpDYPGriYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADI 970
Cdd:PRK08751   403 laiGEIGELCIKGPQVMKGYWKRPEETAKVM-----DADG--WLHTGDIARMDEqGFVYIVDRKKDMILVSGFNVYPNEI 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  971 EKTVESSSELLRpgcCAVVGVPEEvlstkgisvsdSSDQVGLVVIAEvRDAKTVDKEVVEKIKTRVAEEHGVTVASVKli 1050
Cdd:PRK08751   476 EDVIAMMPGVLE---VAAVGVPDE-----------KSGEIVKVVIVK-KDPALTAEDVKAHARANLTGYKQPRIIEFR-- 538

                          570
                   ....*....|....*..
gi 2130317402 1051 kpRTISKTTSGKIKRFE 1067
Cdd:PRK08751   539 --KELPKTNVGKILRRE 553
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 675-1067 7.11e-18

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: 89.41  E-value: 7.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLI-H--NVKLMQRRYRSTSNtilVSWLPQyhDMGLIGGLFTALVSG---GSSV 748
Cdd:cd05971     86 GSDDPALIIYTSGTTGPPKGALHAHRVLLgHlpGVQFPFNLFPRDGD---LYWTPA--DWAWIGGLLDVLLPSlyfGVPV 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LFSPMT-FikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARNydlssMIFLMVAAEPVRQitlkrfiELTL- 826
Cdd:cd05971    161 LAHRMTkF--DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK-----LRAIATGGESLGE-------ELLGw 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 ---PFGLSqevMAPGYGLAE-NCVFVSCAY-------GQGKPIfvdwqgrvccgyvdpndPDVDIRIANPEtGEEIKEsG 895
Cdd:cd05971    227 areQFGVE---VNEFYGQTEcNLVIGNCSAlfpikpgSMGKPI-----------------PGHRVAIVDDN-GTPLPP-G 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 KEGEIWIS--SSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEK 972
Cdd:cd05971    285 EVGEIAVElpDPVAFLGYWNNPSATEKKMAGD--------WLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  973 TVESSSELLRpgcCAVVGVPEEVlstKGISVSdssdqvGLVVIAE-VRDAKTVDKEVVEKIKTRV-AEEHGVTVASVKli 1050
Cdd:cd05971    357 CLLKHPAVLM---AAVVGIPDPI---RGEIVK------AFVVLNPgETPSDALAREIQELVKTRLaAHEYPREIEFVN-- 422

                          410
                   ....*....|....*..
gi 2130317402 1051 kprTISKTTSGKIKRFE 1067
Cdd:cd05971    423 ---ELPRTATGKIRRRE 436
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 669-994 8.77e-18

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 89.66  E-value: 8.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEP-------ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHdmglIGGLFTA- 740
Cdd:PRK06188   153 AAKFGPaplvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AGGAFFLp 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  741 -LVSGGSSVL---FSPMTFiknpllwLETMSKYQATHSagpnFAFELMLRRLeSDKSTARNYDLSSMIFLMVAAEPVRQI 816
Cdd:PRK06188   229 tLLRGGTVIVlakFDPAEV-------LRAIEEQRITAT----FLVPTMIYAL-LDHPDLRTRDLSSLETVYYGASPMSPV 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  817 TLKRFIELtlpFGlsqEVMAPGYGLAEnCVFVSCAYGQGKPIFVDWQGRVCCGYVDPNdpdVDIRIANPEtGEEIKeSGK 896
Cdd:PRK06188   297 RLAEAIER---FG---PIFAQYYGQTE-APMVITYLRKRDHDPDDPKRLTSCGRPTPG---LRVALLDED-GREVA-QGE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  897 EGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVE 975
Cdd:PRK06188   365 VGEICVRGPLVMDGYWNRPEETAEAFRDG--------WLHTGDVAREdEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA 436

                          330
                   ....*....|....*....
gi 2130317402  976 SSSELlrpGCCAVVGVPEE 994
Cdd:PRK06188   437 EHPAV---AQVAVIGVPDE 452
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 662-1065 1.56e-17

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 88.71  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  662 NLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTAL 741
Cdd:PRK09088   120 SADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVL 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSsVLFSPMTFIKNPLLWLETMSkYQATHSAG-PNFAfeLMLRRLESDKSTArnydLSSMIFLMVAAEPVRQITLKR 820
Cdd:PRK09088   200 AVGGS-ILVSNGFEPKRTLGRLGDPA-LGITHYFCvPQMA--QAFRAQPGFDAAA----LRHLTALFTGGAPHAAEDILG 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  821 FIELTLPfglsqevMAPGYGLAE-NCVF---VSCAYGQGKpifvdwqgrvcCGYVDPNDPDVDIRIANpETGEEIkESGK 896
Cdd:PRK09088   272 WLDDGIP-------MVDGFGMSEaGTVFgmsVDCDVIRAK-----------AGAAGIPTPTVQTRVVD-DQGNDC-PAGV 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  897 EGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVE 975
Cdd:PRK09088   332 PGELLLRGPNLSPGYWRRPQATARAFTGD-----G--WFRTGDIArRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLA 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  976 SSSELLRpgcCAVVGVPEEVLStkgisvsdssdQVGLVVIAeVRDAKTVD-KEVVEKIKTRVAE----EHGVTVASVkli 1050
Cdd:PRK09088   405 DHPGIRE---CAVVGMADAQWG-----------EVGYLAIV-PADGAPLDlERIRSHLSTRLAKykvpKHLRLVDAL--- 466

                          410
                   ....*....|....*
gi 2130317402 1051 kPRtiskTTSGKIKR 1065
Cdd:PRK09088   467 -PR----TASGKLQK 476
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 649-994 1.59e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 89.33  E-value: 1.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  649 PWLHTDSWIKYSKNLQAENKADSAE-PETDDLCFLQFTSGSTGDAKGVMITHGGLIH----NVKLMQRRyrsTSNTILVS 723
Cdd:PRK06178   180 PRLAAAGAIDLLPALRACTAPVPLPpPALDALAALNYTGGTTGMPKGCEHTQRDMVYtaaaAYAVAVVG---GEDSVFLS 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  724 WLPQY----HDMGLIGGLFtalvSGGSSVLFSPMtfikNPLLWLETMSKYQATHSAGP-NFAFELMlrrlesDKSTARNY 798
Cdd:PRK06178   257 FLPEFwiagENFGLLFPLF----SGATLVLLARW----DAVAFMAAVERYRVTRTVMLvDNAVELM------DHPRFAEY 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  799 DLSSMIFLMVAAEpVRQITL---KRFIELTlpfglsQEVMAPG-YGLAENCVFVSCAYGQ--------GKPIFvdwqgrv 866
Cdd:PRK06178   323 DLSSLRQVRVVSF-VKKLNPdyrQRWRALT------GSVLAEAaWGMTETHTCDTFTAGFqdddfdllSQPVF------- 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  867 cCGY-VdpndPDVDIRIANPETGEEIKeSGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGrIID 945
Cdd:PRK06178   389 -VGLpV----PGTEFKICDFETGELLP-LGAEGEIVVRTPSLLKGYWNKPEATAEALRDG--------WLHTGDIG-KID 453

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402  946 GKLFI--TGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEE 994
Cdd:PRK06178   454 EQGFLhyLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG---SAVVGRPDP 501
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 670-1066 1.87e-17

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 88.96  E-value: 1.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  670 DSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL 749
Cdd:PRK13295   190 ARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVL 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 FSpmtfIKNPLLWLETMSKYQATHSAGPN-FAFELmlrrleSDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpF 828
Cdd:PRK13295   270 QD----IWDPARAAELIRTEGVTFTMASTpFLTDL------TRAVKESGRPVSSLRTFLCAGAPIPGALVERARAA---L 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  829 GLSqevMAPGYGLAENcvfvscaygqgkpifvdwqGRVCCGYVDPND-----------PDVDIRIANPEtGEEIKeSGKE 897
Cdd:PRK13295   337 GAK---IVSAWGMTEN-------------------GAVTLTKLDDPDerasttdgcplPGVEVRVVDAD-GAPLP-AGQI 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWISSSSAGIGYWGREELSqktfkneLPDYPGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVES 976
Cdd:PRK13295   393 GRLQVRGCSNFGGYLKRPQLN-------GTDADG--WFDTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYR 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  977 SSELLRpgcCAVVGVPEEVLSTKGISVsdssdqvglVVIaevRDAKTVDKEVVekikTRVAEEHGVTVASV--KLIKPRT 1054
Cdd:PRK13295   464 HPAIAQ---VAIVAYPDERLGERACAF---------VVP---RPGQSLDFEEM----VEFLKAQKVAKQYIpeRLVVRDA 524

                          410
                   ....*....|..
gi 2130317402 1055 ISKTTSGKIKRF 1066
Cdd:PRK13295   525 LPRTPSGKIQKF 536
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 527-996 2.34e-17

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: 88.15  E-value: 2.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLlVYVP-GLDFVDCFFGCLRArvlpvpvlppdplqrggqallkienia 605
Cdd:cd05920     40 RLTYRELDRRADRLAAGLRGLG---IRPGDRVV-VQLPnVAEFVVLFFALLRL--------------------------- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  606 kscNAVAILSTVGYHSA-----VRAGSVKNLILltgkngktTGRWPNLpwlhtdswikYSKNLQAENKADSAEPetddlC 680
Cdd:cd05920     89 ---GAVPVLALPSHRRSelsafCAHAEAVAYIV--------PDRHAGF----------DHRALARELAESIPEV-----A 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  681 FLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIG-GLFTALVSGGSSVLFSPmtfiKNP 759
Cdd:cd05920    143 LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPD----PSP 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  760 LLWLETMSKYQATHSA-GPNFAfelmlrRLESDKSTARNYDLSSMIFLMVAAEPVRQiTLKRFIELTLPFGLsQEVmapg 838
Cdd:cd05920    219 DAAFPLIEREGVTVTAlVPALV------SLWLDAAASRRADLSSLRLLQVGGARLSP-ALARRVPPVLGCTL-QQV---- 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  839 YGLAENCVfvsCAYGQGKP--IFVDWQGRvccgyvdPNDPDVDIRIANPEtGEEIKEsGKEGEIWISSSSAGIGYWGREE 916
Cdd:cd05920    287 FGMAEGLL---NYTRLDDPdeVIIHTQGR-------PMSPDDEIRVVDEE-GNPVPP-GEEGELLTRGPYTIRGYYRAPE 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  917 LSQKTFKnelPDypGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR-PGC--CAVVGVP 992
Cdd:cd05920    355 HNARAFT---PD--G--FYRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVE------NLLLRhPAVhdAAVVAMP 421


                   ....
gi 2130317402  993 EEVL 996
Cdd:cd05920    422 DELL 425
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
656-994 5.44e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 87.22  E-value: 5.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  656 WIKYSKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGL----IHNVKLMQRRYRSTSNTILvswlPQYHDM 731
Cdd:PRK06839   128 SITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMfwnaLNNTFAIDLTMHDRSIVLL----PLFHIG 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  732 GLigGLFT--ALVSGGSSVLfsPMTFikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKStarnyDLSSMIFLMVA 809
Cdd:PRK06839   204 GI--GLFAfpTLFAGGVIIV--PRKF--EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETT-----NLQSVRWFYNG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQITLKRFIELTLPFGlsqevmaPGYGLAENC--VFvscaygqgkpIFVDWQGRVCCGYVDPNDPDVDIRIANPET 887
Cdd:PRK06839   273 GAPCPEELMREFIDRGFLFG-------QGFGMTETSptVF----------MLSEEDARRKVGSIGKPVLFCDYELIDENK 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  888 GEeiKESGKEGEIWISSSSAGIGYWGREELSQKTFKNelpdypGRIYtrTGDLGRII-DGKLFITGRIKDLIIVAGRNIY 966
Cdd:PRK06839   336 NK--VEVGEVGELLIRGPNVMKEYWNRPDATEETIQD------GWLC--TGDLARVDeDGFVYIVGRKKEMIISGGENIY 405

                          330       340
                   ....*....|....*....|....*...
gi 2130317402  967 SADIEKTVESSSELLRpgcCAVVGVPEE 994
Cdd:PRK06839   406 PLEVEQVINKLSDVYE---VAVVGRQHV 430
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 678-994 7.34e-17

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: 84.30  E-value: 7.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTilvSWL---PQYHdmglIGGLFTA---LVSGGSSVLFS 751
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD---SWLlslPLYH----VGGLAILvrsLLAGAELVLLE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PmtfikNPLLwLETMSKYQATH-SAGPNfafelMLRR-LESDKSTArnyDLSSMIFLMVAAEPVRQITLKRFIELTLPfg 829
Cdd:cd17630     74 R-----NQAL-AEDLAPPGVTHvSLVPT-----QLQRlLDSGQGPA---ALKSLRAVLLGGAPIPPELLERAADRGIP-- 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 lsqevMAPGYGLAEncvFVSCAYGQGKPIFVDwqgrvccGYVDPNDPDVDIRIANPetgeeikesgkeGEIWISSSSAGI 909
Cdd:cd17630    138 -----LYTTYGMTE---TASQVATKRPDGFGR-------GGVGVLLPGRELRIVED------------GEIWVGGASLAM 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  910 GYWGREelsqktfknELPDYPGRIYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAV 988
Cdd:cd17630    191 GYLRGQ---------LVPEFNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD---AFV 258


                   ....*.
gi 2130317402  989 VGVPEE 994
Cdd:cd17630    259 VGVPDE 264
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 674-1039 3.42e-16

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: 84.44  E-value: 3.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYH-------DMG-LIGGLFTALVSGG 745
Cdd:cd05932    134 RFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHvtervfvEGGsLYGGVLVAFAESL 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  746 SSVL-----FSPMTFIKNPLLWletmSKYQ-ATHSAGPNFAFELMLR-----RLESDKsTARNYDLSSMIFLMVAAEPVR 814
Cdd:cd05932    214 DTFVedvqrARPTLFFSVPRLW----TKFQqGVQDKIPQQKLNLLLKipvvnSLVKRK-VLKGLGLDQCRLAGCGSAPVP 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  815 QITLKRFIELTLPfglsqevMAPGYGLAENCvfvscAYGQgkpifVDWQGRVCCGYVDPNDPDVDIRIanpetgeeikes 894
Cdd:cd05932    289 PALLEWYRSLGLN-------ILEAYGMTENF-----AYSH-----LNYPGRDKIGTVGNAGPGVEVRI------------ 339

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  895 GKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVA-GRNIYSADIEK 972
Cdd:cd05932    340 SEDGEILVRSPALMMGYYKDPEATAEAFTAD-----G--FLRTGDKGELdADGNLTITGRVKDIFKTSkGKYVAPAPIEN 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  973 ------TVE----SSSELLRPGCCAV---VGVPEEVLSTKGI-------------SVSDSSDQVGLVVIaeVRDAKTVDK 1026
Cdd:cd05932    413 klaehdRVEmvcvIGSGLPAPLALVVlseEARLRADAFARAEleaslrahlarvnSTLDSHEQLAGIVV--VKDPWSIDN 490

                          410
                   ....*....|....*.
gi 2130317402 1027 EVVE---KIKTRVAEE 1039
Cdd:cd05932    491 GILTptlKIKRNVLEK 506
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 657-958 3.47e-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: 84.57  E-value: 3.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  657 IKYSKNlQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRR---YRSTSNTILvSWLPQYHDM-- 731
Cdd:cd17639     69 LIHSLN-ETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvpeLLGPDDRYL-AYLPLAHIFel 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  732 ----------GLIG-----GLFTALVSG--GSSVLFSPMTFIKNPLLWlETMSK-YQATHSAGP-------NFAFELMLR 786
Cdd:cd17639    147 aaenvclyrgGTIGygsprTLTDKSKRGckGDLTEFKPTLMVGVPAIW-DTIRKgVLAKLNPMGglkrtlfWTAYQSKLK 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  787 RLESDKSTARnydLSSMIFlmvaaEPVRQITLKRfIELTLPFG--LS---QEVM-------APGYGLAENCvfvscaygq 854
Cdd:cd17639    226 ALKEGPGTPL---LDELVF-----KKVRAALGGR-LRYMLSGGapLSadtQEFLnivlcpvIQGYGLTETC--------- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  855 gkpifvdwqgrvCCGYV-DPNDPDVDiRIANPETGEEIK----ESGK--------EGEIWISSSSAGIGYWGREELSQKT 921
Cdd:cd17639    288 ------------AGGTVqDPGDLETG-RVGPPLPCCEIKlvdwEEGGystdkpppRGEILIRGPNVFKGYYKNPEKTKEA 354

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2130317402  922 FKnelpdyPGRiYTRTGDLGRII-DGKLFITGRIKDLI 958
Cdd:cd17639    355 FD------GDG-WFHTGDIGEFHpDGTLKIIDRKKDLV 385
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 654-1067 5.47e-16

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: 84.08  E-value: 5.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSKNLQA-----ENKADSAEPETDDLCFLQFTSGSTGDAKgvMITH------GGLI-----HNVKLMQRRYrSTS 717
Cdd:cd05970    157 EGWIDFRKLIKNaspdfERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVtakywQNVREGGLHL-TVA 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  718 NTilvSWlpqyhDMGLIGGLFTALVSGGSSVLFSPMTFIknPLLWLETMSKYQATHSAGPNFAFELMLRRLESDkstarn 797
Cdd:cd05970    234 DT---GW-----GKAVWGKIYGQWIAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR------ 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  798 YDLSSMIFLMVAAEPVRQITLKRFIELTlpfGLSqevMAPGYGLAENCVFVSCAYG-QGKPifvdwqgrvccGYVDPNDP 876
Cdd:cd05970    298 YDLSSLRYCTTAGEALNPEVFNTFKEKT---GIK---LMEGFGQTETTLTIATFPWmEPKP-----------GSMGKPAP 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  877 DVDIRIANPEtGEEIkESGKEGEIWISSSSA---GI--GYWGREELSQKTFKNElpdypgriYTRTGDLG-RIIDGKLFI 950
Cdd:cd05970    361 GYEIDLIDRE-GRSC-EAGEEGEIVIRTSKGkpvGLfgGYYKDAEKTAEVWHDG--------YYHTGDAAwMDEDGYLWF 430

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  951 TGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVlstKGISVsdssdQVGLVVIAEVRDAKTVDKEVVE 1030
Cdd:cd05970    431 VGRTDDLIKSSGYRIGPFEVESALIQHPAVLE---CAVTGVPDPI---RGQVV-----KATIVLAKGYEPSEELKKELQD 499

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2130317402 1031 KIKtRVAeehgvtvASVKLikPRTIS------KTTSGKIKRFE 1067
Cdd:cd05970    500 HVK-KVT-------APYKY--PRIVEfvdelpKTISGKIRRVE 532
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 669-971 5.66e-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: 83.29  E-value: 5.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSV 748
Cdd:cd17650     85 AKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLV 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LfSPMTFIKNPLLWLETMSKYQAT-HSAGPNFAFELMlrrlesdKSTARN-YDLSSMIFLMVAAEPVrqiTLKRFIELTL 826
Cdd:cd17650    165 I-CPDEVKLDPAALYDLILKSRITlMESTPALIRPVM-------AYVYRNgLDLSAMRLLIVGSDGC---KAQDFKTLAA 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 PFGLSQEVMApGYGLAENCvfVSCAYGQGKPIFVDWQGRVCCGYVDPNdpdVDIRIANPEtgEEIKESGKEGEIWISSSS 906
Cdd:cd17650    234 RFGQGMRIIN-SYGVTEAT--IDSTYYEEGRDPLGDSANVPIGRPLPN---TAMYVLDER--LQPQPVGVAGELYIGGAG 305

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402  907 AGIGYWGREELSQKTFkNELPDYPG-RIYtRTGDLGR-IIDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:cd17650    306 VARGYLNRPELTAERF-VENPFAPGeRMY-RTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIE 370
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 677-977 9.56e-16

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: 82.79  E-value: 9.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFtaLVSGGSSVLFSPMTFI 756
Cdd:cd17640     88 DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF--IFACGCSQAYTSIRTL 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 KN-------------PLLWLETMSKYQATHSAGPnfAFELMLRRlesdkstarnydlssmiFLMVAAEPVRQIT------ 817
Cdd:cd17640    166 KDdlkrvkphyivsvPRLWESLYSGIQKQVSKSS--PIKQFLFL-----------------FFLSGGIFKFGISgggalp 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  818 --LKRFIELTlpfGLSqevMAPGYGLAENCVFVSCaygqGKPifvdwqGRVCCGYVDPNDPDVDIRIANPETGEEIKESG 895
Cdd:cd17640    227 phVDTFFEAI---GIE---VLNGYGLTETSPVVSA----RRL------KCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGE 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 KeGEIWISSSSAGIGYWGREE-----LSQKTFKNelpdypgriytrTGDLGRI-IDGKLFITGRIKDLIIVA-GRNIYSA 968
Cdd:cd17640    291 K-GIVWVRGPQVMKGYYKNPEatskvLDSDGWFN------------TGDLGWLtCGGELVLTGRAKDTIVLSnGENVEPQ 357


                   ....*....
gi 2130317402  969 DIEKTVESS 977
Cdd:cd17640    358 PIEEALMRS 366
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 529-1066 9.64e-16

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: 82.53  E-value: 9.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtsEKPVIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrggqallkieniaksc 608
Cdd:cd05958     12 TYRDLLALANRIANVLV--GELGIVPGNRVLLRGSNSPELVACWFGIQKA------------------------------ 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  609 NAVAilstVGYHSAVRAGsvknlilltgkngkttgrwpnlpwlhtdswiKYSKNLQAENKA----DSAEPETDDLCFLQF 684
Cdd:cd05958     60 GAIA----VATMPLLRPK-------------------------------ELAYILDKARITvalcAHALTASDDICILAF 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  685 TSGSTGDAKGVMITHggliHNVKLMQRRY-----RSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLFSPMTfiknP 759
Cdd:cd05958    105 TSGTTGAPKATMHFH----RDPLASADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT----P 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  760 LLWLETMSKYQATHSAGPNFAFELMLrrlesDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELTlpfGLsqEVMaPGY 839
Cdd:cd05958    177 DLLLSAIARYKPTVLFTAPTAYRAML-----AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT---GI--PII-DGI 245

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  840 GLAENC-VFVSCAYGQGKPifvDWQGRVCCGYvdpndpdvdirianpeTGEEIKESGKE---GEIWISSSSAGIGYWGRE 915
Cdd:cd05958    246 GSTEMFhIFISARPGDARP---GATGKPVPGY----------------EAKVVDDEGNPvpdGTIGRLAVRGPTGCRYLA 306

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  916 ELSQKTFKNELPDYPGRIYTRTGDlgriidGKLFITGRIKDLIIVAGRNIYSADIEKTVessseLLRPGC--CAVVGVPe 993
Cdd:cd05958    307 DKRQRTYVQGGWNITGDTYSRDPD------GYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVaeCAVVGHP- 374

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  994 evlstkgisvsdssDQVGLVVIAE---VRDAKTVDKEVVEKIKTRVAEEhgvtVASVKliKPRTIS------KTTSGKIK 1064
Cdd:cd05958    375 --------------DESRGVVVKAfvvLRPGVIPGPVLARELQDHAKAH----IAPYK--YPRAIEfvtelpRTATGKLQ 434


                   ..
gi 2130317402 1065 RF 1066
Cdd:cd05958    435 RF 436
PLN02246 PLN02246
4-coumarate--CoA ligase
 652-1065 1.70e-15

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 82.72  E-value: 1.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  652 HTDSWIKYSKNLQA-ENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKlmQR-------RYRSTSNTILVS 723
Cdd:PLN02246   153 PPEGCLHFSELTQAdENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA--QQvdgenpnLYFHSDDVILCV 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  724 wLPQYHdmglIGGLFTALVSG---GSSVLFSPmTFIKNPLlwLETMSKYQAThsAGPnFAFELMLRRLESDksTARNYDL 800
Cdd:PLN02246   231 -LPMFH----IYSLNSVLLCGlrvGAAILIMP-KFEIGAL--LELIQRHKVT--IAP-FVPPIVLAIAKSP--VVEKYDL 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  801 SSMIFLMVAAEPvrqitLKRFIELTLPFGLSQEVMAPGYGLAENCVFVSCAYGQGKPIFVDWQGrvCCGYVDPNdpdVDI 880
Cdd:PLN02246   298 SSIRMVLSGAAP-----LGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSG--SCGTVVRN---AEL 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  881 RIANPETGEEIKEsGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRI-IDGKLFITGRIKDLII 959
Cdd:PLN02246   368 KIVDPETGASLPR-NQPGEICIRGPQIMKGYLNDPEATANTIDKD-----G--WLHTGDIGYIdDDDELFIVDRLKELIK 439

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  960 VAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVlstkgisvsdssdqVGLVVIAEVrdAKTVDKEVVE-KIKTRVAE 1038
Cdd:PLN02246   440 YKGFQVAPAELEALLISHPSIAD---AAVVPMKDEV--------------AGEVPVAFV--VRSNGSEITEdEIKQFVAK 500

                          410       420       430
                   ....*....|....*....|....*....|.
gi 2130317402 1039 EhgvtVASVKLIKP----RTISKTTSGKIKR 1065
Cdd:PLN02246   501 Q----VVFYKRIHKvffvDSIPKAPSGKILR 527
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 527-1066 1.89e-15

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 82.50  E-value: 1.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRarvLPVPVLPPDPLQRGGQallkIENIAK 606
Cdd:PRK06155    46 RWTYAEAARAAAAAAHALAAAG---VKRGDRVALMCGNRIEFLDVFLGCAW---LGAIAVPINTALRGPQ----LEHILR 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  607 SCNAVAILSTVGYHSAVRA-----GSVKNLILLTGKNGkttGRWPnLPWlhtdswiKYSKNLQAENKADSAEPETDDLCF 681
Cdd:PRK06155   116 NSGARLLVVEAALLAALEAadpgdLPLPAVWLLDAPAS---VSVP-AGW-------STAPLPPLDAPAPAAAVQPGDTAA 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGL----IHNVKLMQRRyrstSNTILVSWLPQYHDMGLiGGLFTALVSGGSSVL---FSPMT 754
Cdd:PRK06155   185 ILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLEIG----ADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLeprFSASG 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  755 FiknpllWLEtMSKYQAThsagpnFAFEL--MLRRLESDKSTARNYDLSSMIFLM--VAAEPVRQITLKrfieltlpFGL 830
Cdd:PRK06155   260 F------WPA-VRRHGAT------VTYLLgaMVSILLSQPARESDRAHRVRVALGpgVPAALHAAFRER--------FGV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 SqevMAPGYGLAENCVFVSCAYGQGKPifvDWQGRVCCGYvdpndpdvDIRIANpETGEEIkESGKEGEIWISSSSAGI- 909
Cdd:PRK06155   319 D---LLDGYGSTETNFVIAVTHGSQRP---GSMGRLAPGF--------EARVVD-EHDQEL-PDGEPGELLLRADEPFAf 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  910 --GYWGREELSQKTFKNelpdypgrIYTRTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcC 986
Cdd:PRK06155   383 atGYFGMPEKTVEAWRN--------LWFHTGDRVvRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA---A 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  987 AVVGVPEEVlstkgisvsdSSDQVGLVVIaeVRDAKTVD-KEVVEKIKTRVAeehgvtvasvKLIKPRTIS------KTT 1059
Cdd:PRK06155   452 AVFPVPSEL----------GEDEVMAAVV--LRDGTALEpVALVRHCEPRLA----------YFAVPRYVEfvaalpKTE 509


                   ....*..
gi 2130317402 1060 SGKIKRF 1066
Cdd:PRK06155   510 NGKVQKF 516
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
26-92 6.89e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 71.41  E-value: 6.89e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402   26 IVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSAPVIFDLAKE 92
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
21-265 1.74e-14

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 78.81  E-value: 1.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLE-------KFHTVSGmcesvEIEGKMYDLGGQVLAANSaPVIFDLAKET 93
Cdd:COG1231      7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   94 GSELEEM-DAHKLALIDASTGEYQDNKVADDYVSVISLTLELQDKAKDSGRIGVHAVSDIasDLTP--TYLESHGLKSVP 170
Cdd:COG1231     80 GLPLEPFpNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAEL--DRESlaEWLRRNGASPSA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  171 KSVAYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRFKGGYMNFWRKLSEYLPIEVHCNTEVLAIRRnSATN 243
Cdd:COG1231    158 RRLLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQ-DGDG 231

                          250       260
                   ....*....|....*....|..
gi 2130317402  244 VSVDVknvnGECEVMEFDKIII 265
Cdd:COG1231    232 VTVTT----DDGGTVRADAVIV 249
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 677-1067 2.26e-14

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 79.12  E-value: 2.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLM------QRRYRSTSNTILVSwLPQYHDMGLigGLF-TALVSGGSSVL 749
Cdd:PLN02574   198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeasQYEYPGSDNVYLAA-LPMFHIYGL--SLFvVGLLSLGSTIV 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 ----FSPMTFIKnpllwleTMSKYQATHsagpnFAF--ELMLRRLESDKSTARNyDLSSMIFLMVAAEPVRQITLKRFIE 823
Cdd:PLN02574   275 vmrrFDASDMVK-------VIDRFKVTH-----FPVvpPILMALTKKAKGVCGE-VLKSLKQVSCGAAPLSGKFIQDFVQ 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  824 lTLP-FGLSQevmapGYGLAEncvfvSCAYGQGKPIFVDWQGRVCCGYVDPNdpdVDIRIANPETGEEIKeSGKEGEIWI 902
Cdd:PLN02574   342 -TLPhVDFIQ-----GYGMTE-----STAVGTRGFNTEKLSKYSSVGLLAPN---MQAKVVDWSTGCLLP-PGNCGELWI 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  903 SSSSAGIGYWGREELSQKTFKNELpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELL 981
Cdd:PLN02574   407 QGPGVMKGYLNNPKATQSTIDKDG-------WLRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEII 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  982 RpgcCAVVGVPEEvlstkgisvsdssdQVGLVVIAEV--RDAKTVDKE-VVEKIKTRVAEEHGVTvasvKLIKPRTISKT 1058
Cdd:PLN02574   480 D---AAVTAVPDK--------------ECGEIPVAFVvrRQGSTLSQEaVINYVAKQVAPYKKVR----KVVFVQSIPKS 538


                   ....*....
gi 2130317402 1059 TSGKIKRFE 1067
Cdd:PLN02574   539 PAGKILRRE 547
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 680-974 2.27e-14

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: 79.32  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  680 CFLQFTSGSTGDAKGVMITHGGL----IHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSsVLFS---- 751
Cdd:cd05933    153 CTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQ-VYFAqpda 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 -------------PMTFIKNPLLW-----------------------------LETMSKYQATHSagPNFAFELMLRRLE 789
Cdd:cd05933    232 lkgtlvktlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGES--PSPLFYRLAKKLV 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  790 SDKSTARnYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGlsqevmaPGYGLAEN--CVFVSC--AYGQGKpifvdwQGR 865
Cdd:cd05933    310 FKKVRKA-LGLDRCQKFFTGAAPISRETLEFFLSLNIPIM-------ELYGMSETsgPHTISNpqAYRLLS------CGK 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  866 VCcgyvdpndPDVDIRIANPEtgeeikeSGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRI-I 944
Cdd:cd05933    376 AL--------PGCKTKIHNPD-------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDED-----G--WLHSGDLGKLdE 433

                          330       340       350
                   ....*....|....*....|....*....|.
gi 2130317402  945 DGKLFITGRIKDLIIVA-GRNIYSADIEKTV 974
Cdd:cd05933    434 DGFLYITGRIKELIITAgGENVPPVPIEDAV 464
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 680-1055 6.37e-14

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: 75.80  E-value: 6.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  680 CFLQFTSGSTGDAKGVMITHGGLI-HNVKLMQRRyRSTSNTILVSWLPQYHdMGLIGGLFTALVSGGSSVlFSPMTfikN 758
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQ-AIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNV-FVRRV---D 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  759 PLLWLETMSKYQATHS--AGPNFAfelMLRRLESDkstaRNYDLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQ-EVM 835
Cdd:cd17636     77 AEEVLELIEAERCTHAflLPPTID---QIVELNAD----GLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGGYGQtEVM 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  836 A----PGYGlaencvfVSCAYGQGKPifvdwqgrvccgyvdpnDPDVDIRIANPEtGEEIKeSGKEGEIWISSSSAGIGY 911
Cdd:cd17636    150 GlatfAALG-------GGAIGGAGRP-----------------SPLVQVRILDED-GREVP-DGEVGEIVARGPTVMAGY 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 WGREELSQKTFKNElpdypgriYTRTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTVESssellRPGC--CAV 988
Cdd:cd17636    204 WNRPEVNARRTRGG--------WHHTNDLGrREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-----HPAVadAAV 270

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  989 VGVPEEVL--STKGIsvsdssdqvglVVIAEvrDAKTVDKEVVEKIKTRvaeehgvtVASVKliKPRTI 1055
Cdd:cd17636    271 IGVPDPRWaqSVKAI-----------VVLKP--GASVTEAELIEHCRAR--------IASYK--KPKSV 316
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 520-991 7.08e-14

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 77.48  E-value: 7.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  520 EEGAVVSrrtYRELHANASLISHKLLtseKPVIKPGDRVLLVYVPGLDFVDCFFGCLRARVLPVPVLPPDPLQ------- 592
Cdd:PRK06164    31 DEDRPLS---RAELRALVDRLAAWLA---AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHevahilg 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  593 RGGQALLKIENIAKSCNAVAILSTVGyHSAVRAgsVKNLILLTGKNGKTTGRWP----NLPWLHtdswikysknLQAENK 668
Cdd:PRK06164   105 RGRARWLVVWPGFKGIDFAAILAAVP-PDALPP--LRAIAVVDDAADATPAPAPgarvQLFALP----------DPAPPA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLCFLQFT-SGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLftALVSGGSS 747
Cdd:PRK06164   172 AAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL--GALAGGAP 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 VLFSPmTFIKNPLLWLetMSKYQATHSAGPNFAFELMLRRL--ESDKSTARNYDLSSmiFLMVAAEpVRQITLKRFIELT 825
Cdd:PRK06164   250 LVCEP-VFDAARTARA--LRRHRVTHTFGNDEMLRRILDTAgeRADFPSARLFGFAS--FAPALGE-LAALARARGVPLT 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  826 LPFGlSQEVMApgyglaencvFVSCaygqgKPIFVDWQGRVCCGYVdPNDPDVDIRIANPETGeEIKESGKEGEIWISSS 905
Cdd:PRK06164   324 GLYG-SSEVQA----------LVAL-----QPATDPVSVRIEGGGR-PASPEARVRARDPQDG-ALLPDGESGEIEIRAP 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  906 SAGIGYWGREELSQKTFKnelPDypGriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESssellRPG 984
Cdd:PRK06164   386 SLMRGYLDNPDATARALT---DD--G--YFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA-----LPG 453


                   ....*....
gi 2130317402  985 C--CAVVGV 991
Cdd:PRK06164   454 VaaAQVVGA 462
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 22-94 7.87e-14

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: 76.79  E-value: 7.87e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402   22 TRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSaPVIFDLAKETG 94
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 682-992 1.87e-13

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 76.21  E-value: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGlihnvklmqrRYRSTSNTIlVSW-----------LPQYHDMGLIGGLFTAlVSGGSSVLf 750
Cdd:PLN03102   191 LNYTSGTTADPKGVVISHRG----------AYLSTLSAI-IGWemgtcpvylwtLPMFHCNGWTFTWGTA-ARGGTSVC- 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 spMTFIKNPLLWlETMSKYQATHSAGPNFAFELMLRRLESDKSTArnydlSSMIFLMVAAEPVRQITLKRFIELTLpfgl 830
Cdd:PLN03102   258 --MRHVTAPEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPR-----SGPVHVLTGGSPPPAALVKKVQRLGF---- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 sqEVMApGYGLAEncvfvscayGQGKPIFVDWQG-------------RVCCGYVDPNDPDVDIRiaNPETGEEIKESGKE 897
Cdd:PLN03102   326 --QVMH-AYGLTE---------ATGPVLFCEWQDewnrlpenqqmelKARQGVSILGLADVDVK--NKETQESVPRDGKT 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 -GEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVE 975
Cdd:PLN03102   392 mGEIVIKGSSIMKGYLKNPKATSEAFKHG--------WLNTGDVGVIhPDGHVEIKDRSKDIIISGGENISSVEVENVLY 463

                          330
                   ....*....|....*..
gi 2130317402  976 SSSELLRpgcCAVVGVP 992
Cdd:PLN03102   464 KYPKVLE---TAVVAMP 477
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 655-957 2.06e-13

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: 75.71  E-value: 2.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  655 SWIKYSKnLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNV----KLMQRRYRSTSNTILVSWLPQYHd 730
Cdd:cd05927     93 SLEEFEK-LGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAH- 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  731 mgliggLFTALV-----SGGSSVLF---------------SPMTFIKNPLLWLETMSKYQATHSAGP-------NFAFEL 783
Cdd:cd05927    171 ------IFERVVealflYHGAKIGFysgdirlllddikalKPTVFPGVPRVLNRIYDKIFNKVQAKGplkrklfNFALNY 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  784 MLRRLESDKSTARNYdLSSMIF-------------LMVAAEPVRQITLKrFIELTLPFGLSQevmapGYGLAENCVfvsc 850
Cdd:cd05927    245 KLAELRSGVVRASPF-WDKLVFnkikqalggnvrlMLTGSAPLSPEVLE-FLRVALGCPVLE-----GYGQTECTA---- 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  851 aygqgkPIFVDWQGRVCCGYVDPNDPDVDIRIAN-PETGEEIKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdy 929
Cdd:cd05927    314 ------GATLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED---- 383

                          330       340
                   ....*....|....*....|....*....
gi 2130317402  930 pGriYTRTGDLGRII-DGKLFITGRIKDL 957
Cdd:cd05927    384 -G--WLHTGDIGEWLpNGTLKIIDRKKNI 409
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 678-1065 2.36e-13

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: 73.98  E-value: 2.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIH----NVKLMqrrYRSTSNTILVSWlPQYHDMGLIGGLFtALVSGGSSVLFSpm 753
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIEsfvcNEDLF---NISGEDAILAPG-PLSHSLFLYGAIS-ALYLGGTFIGQR-- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFikNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDkSTARNYDLSSMIFLMVAAEPVRQITLKrfIELTLPFGLSQE 833
Cdd:cd17633     74 KF--NPKSWIRKINQYNATVIYLVPTMLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIFPK--ANLIEFYGTSEL 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 vmapgyglaeNCVFVSCAYGQGKPIFVdwqGRVCcgyvdpndPDVDIRIANpetgeeiKESGKEGEIWISSSSAGIGYWG 913
Cdd:cd17633    149 ----------SFITYNFNQESRPPNSV---GRPF--------PNVEIEIRN-------ADGGEIGKIFVKSEMVFSGYVR 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  914 REELSqktfknelpdyPGRIYTrTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGccaVVGVP 992
Cdd:cd17633    201 GGFSN-----------PDGWMS-VGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI---VVGIP 265

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402  993 EEvlstkgisvsdssdQVGLVVIAEVRDAKTVDKEVVEKIKTRVAEEHgvtVASvKLIKPRTISKTTSGKIKR 1065
Cdd:cd17633    266 DA--------------RFGEIAVALYSGDKLTYKQLKRFLKQKLSRYE---IPK-KIIFVDSLPYTSSGKIAR 320
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 685-992 2.39e-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: 73.84  E-value: 2.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  685 TSGSTGDAKGVMITHGGLIH-NVKLMQRrYRSTSNTILVSWLPQYHDMGLiGGLFTALVSGGSSVLFSPMtfikNPLLWL 763
Cdd:cd17637      8 TAAVAGRPRGAVLSHGNLIAaNLQLIHA-MGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKF----DPAEAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  764 ETMSKYQATHSagpnFAFELMLRRLEsDKSTARNYDLSSMiflmvaaepvRQI-------TLKRFIELTLPFGLSqevma 836
Cdd:cd17637     82 ELIEEEKVTLM----GSFPPILSNLL-DAAEKSGVDLSSL----------RHVlgldapeTIQRFEETTGATFWS----- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  837 pGYGLAENCVFVSCAYGQGKPIFVdwqGRVCcgyvdpndPDVDIRIANpETGEEIkESGKEGEIWISSSSAGIGYWGREE 916
Cdd:cd17637    142 -LYGQTETSGLVTLSPYRERPGSA---GRPG--------PLVRVRIVD-DNDRPV-PAGETGEIVVRGPLVFQGYWNLPE 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  917 LSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRI--KDLIIVAGRNIYSADIEKTVessseLLRPGCCAVV--GV 991
Cdd:cd17637    208 LTAYTFRNG--------WHHTGDLGRFdEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVI-----LEHPAIAEVCviGV 274


                   .
gi 2130317402  992 P 992
Cdd:cd17637    275 P 275
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 664-991 3.04e-13

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: 74.80  E-value: 3.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  664 QAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYhdmgligGLFTALVs 743
Cdd:cd05910     72 EAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPAL- 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  744 gGSSVLFSPMTFIK----NPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTarnydLSSMIFLMVAAEPVRQITLK 819
Cdd:cd05910    144 -GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT-----LPSLRRVLSAGAPVPIALAA 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  820 RFIELTLPfglSQEVMAPgYGLAEN---CVFVSCAYGQGKPIFVDWQGRVCCGYVDPNdpdVDIRIAnPETGEEIKE--- 893
Cdd:cd05910    218 RLRKMLSD---EAEILTP-YGATEAlpvSSIGSRELLATTTAATSGGAGTCVGRPIPG---VRVRII-EIDDEPIAEwdd 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  894 -----SGKEGEIWISSSSAGIGYWGREelsQKTFKNELPDYPGRIYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYS 967
Cdd:cd05910    290 tlelpRGEIGEITVTGPTVTPTYVNRP---VATALAKIDDNSEGFWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYT 366

                          330       340
                   ....*....|....*....|....
gi 2130317402  968 ADIEKTVESSSELLRpgcCAVVGV 991
Cdd:cd05910    367 EPVERVFNTHPGVRR---SALVGV 387
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 668-1003 6.65e-13

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 74.31  E-value: 6.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  668 KADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLI-----HNVKLM---QRRYRStsntILVSwlPQYHDMGlIGGLfT 739
Cdd:PRK07470   154 RVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAfvitnHLADLMpgtTEQDAS----LVVA--PLSHGAG-IHQL-C 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  740 ALVSGGSSVL-----FSPMTFiknpllWlETMSKYQATHSagpnFAFELMLRRLESDKSTARnYDLSSMIFLMVAAEPVR 814
Cdd:PRK07470   226 QVARGAATVLlpserFDPAEV------W-ALVERHRVTNL----FTVPTILKMLVEHPAVDR-YDHSSLRYVIYAGAPMY 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  815 QITLKRFIELTLPfglsqeVMAPGYGLAE--NCVFVSCAYGQgkpifvdwqgrvccgyvDPND-PDVDIRIAN-PETGEE 890
Cdd:PRK07470   294 RADQKRALAKLGK------VLVQYFGLGEvtGNITVLPPALH-----------------DAEDgPDARIGTCGfERTGME 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  891 IK---------ESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIV 960
Cdd:PRK07470   351 VQiqddegrelPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG--------WFRTGDLGHLdARGFLYITGRASDMYIS 422

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2130317402  961 AGRNIYSADIEKTVessseLLRPGC--CAVVGVPEEVLSTKGISV 1003
Cdd:PRK07470   423 GGSNVYPREIEEKL-----LTHPAVseVAVLGVPDPVWGEVGVAV 462
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 523-1065 1.26e-12

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: 73.15  E-value: 1.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVVS---RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQALL 599
Cdd:cd17651     13 ALVAegrRLTYAELDRRANRLAHRLRARG---VGPGDLVALCARRSAELVVALLAILKA----------------GAAYV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 KIE---------NIAKSCNAVAILStvgyHSAVRAGSvknlilltgkngkttgrwpnLPWLHTDSWIKYSKNLQAENKAD 670
Cdd:cd17651     74 PLDpaypaerlaFMLADAGPVLVLT----HPALAGEL--------------------AVELVAVTLLDQPGAAAGADAEP 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLiGGLFTALVSGGSSVL- 749
Cdd:cd17651    130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLp 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 -----FSPMTFiknpLLWLETmskYQATHSAGPNFAFELMLrrLESDKSTARNYDLSSMIflmVAAEPVRQITLKRFIEL 824
Cdd:cd17651    209 peevrTDPPAL----AAWLDE---QRISRVFLPTVALRALA--EHGRPLGVRLAALRYLL---TGGEQLVLTEDLREFCA 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 TLPFGLsqevMAPGYGLAENCVfVSCAYGQGKPifVDWQGRVCCGYVDPNdpdVDIRIANPetGEEIKESGKEGEIWISS 904
Cdd:cd17651    277 GLPGLR----LHNHYGPTETHV-VTALSLPGDP--AAWPAPPPIGRPIDN---TRVYVLDA--ALRPVPPGVPGELYIGG 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  905 SSAGIGYWGREELSQKTFKnELPDYPGRIYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR- 982
Cdd:cd17651    345 AGLARGYLNRPELTAERFV-PDPFVPGARMYRTGDLARWLpDGELEFLGRADDQVKIRGFRIELGEIE------AALARh 417

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  983 PGCCAVVGVPEEvlstkgisvsDSSDQVGLVVIAEVRDAKTVDkevVEKIKTRVAE---EHGVTVASVKLikpRTISKTT 1059
Cdd:cd17651    418 PGVREAVVLARE----------DRPGEKRLVAYVVGDPEAPVD---AAELRAALAThlpEYMVPSAFVLL---DALPLTP 481


                   ....*.
gi 2130317402 1060 SGKIKR 1065
Cdd:cd17651    482 NGKLDR 487
srpA_like cd08153
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ...
 1757-1995 2.38e-12

Catalase-like heme-binding proteins similar to the uncharacterized srpA; 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 the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.


Pssm-ID: 163709  Cd Length: 295  Bit Score: 70.34  E-value: 2.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1757 GKSYPVIVRHSNS--LSADDDARIDARGAAIRILSDDvgsGGSTppllDLTLKTGKAFYARTIADFATWLVCGL------ 1828
Cdd:cd08153     45 GGSVPVTGRFSLGggNPKAPDDAANPRGMALKFRLPD---GEQW----RMVMNSFPVFPVRTPEEFLALLKAIApdatgk 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1829 ---AAREEHVKRVPRVRDAV-WM-SLRNADSFTELHYYS-NIcrlFRFTD--GQEMYVKFKLRPfdetisedsgkVEPVG 1900
Cdd:cd08153    118 pdpAKLKAFLAAHPEAAAFLaWIkTAPPPASFANTTYYGvNA---FYFTNanGKRQPVRWRFVP-----------EDGVK 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1901 ILPPDTGAiPRDENdtrpllFLADDFKRRVESPTgVRYIFQLQVqPVPQDEATrdialDCTKPWDETEfPYIDIGEISID 1980
Cdd:cd08153    184 YLSDEEAA-KLGPD------FLFDELAQRLAQGP-VRWDLVLQL-AEPGDPTD-----DPTKPWPADR-KEVDAGTLTIT 248

                          250
                   ....*....|....*..
gi 2130317402 1981 QNLTKEE--SEKMEFNP 1995
Cdd:cd08153    249 KVAPDQGgaCRDINFDP 265
PRK09274 PRK09274
peptide synthase; Provisional
 526-1053 3.56e-12

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 71.85  E-value: 3.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  526 SRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFgclrarvlpvpvlppdplqrggqALLKIenia 605
Cdd:PRK09274    40 DELSFAELDARSDAIAHGLNAAG---IGRGMRAVLMVTPSLEFFALTF-----------------------ALFKA---- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  606 kscNAVAIL--STVGY--------HSAVRA------------------GSVKNLIlltgkngkTTGR--WPNLPWLHTDS 655
Cdd:PRK09274    90 ---GAVPVLvdPGMGIknlkqclaEAQPDAfigipkahlarrlfgwgkPSVRRLV--------TVGGrlLWGGTTLATLL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  656 WIKYSKNLQAenkadsAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILvswLPQYHDMGLIG 735
Cdd:PRK09274   159 RDGAAAPFPM------ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEID---LPTFPLFALFG 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  736 glfTALvsGGSSVLfSPMTFIK----NPLLWLETMSKYQATHSAGpNFAfelMLRRLeSDKSTARNYDLSSMIFLMVAAE 811
Cdd:PRK09274   230 ---PAL--GMTSVI-PDMDPTRpatvDPAKLFAAIERYGVTNLFG-SPA---LLERL-GRYGEANGIKLPSLRRVISAGA 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  812 PVRQITLKRFIELtLPFGLsqEVMAPgYGLAEncVFVSCAYGQGKPIFVDWQ-----GRVCCGYVDPndpDVDIRI---- 882
Cdd:PRK09274   299 PVPIAVIERFRAM-LPPDA--EILTP-YGATE--ALPISSIESREILFATRAatdngAGICVGRPVD---GVEVRIiais 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  883 ANP-ETGEEIKE--SGKEGEIWISSSSAGIGYWGREElsqKTFKNELPDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLI 958
Cdd:PRK09274   370 DAPiPEWDDALRlaTGEIGEIVVAGPMVTRSYYNRPE---ATRLAKIPDGQGDVWHRMGDLGYLdAQGRLWFCGRKAHRV 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  959 IVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPeevlsTKGisvsdssDQVGLVVIaEVRDAKTVDKEVVEKIKTRVAE 1038
Cdd:PRK09274   447 ETAGGTLYTIPCERIFNTHPGVKR---SALVGVG-----VPG-------AQRPVLCV-ELEPGVACSKSALYQELRALAA 510

                          570
                   ....*....|....*..
gi 2130317402 1039 EHGVTvASVK--LIKPR 1053
Cdd:PRK09274   511 AHPHT-AGIErfLIHPS 526
PRK12467 PRK12467
peptide synthase; Provisional
 654-973 4.27e-12

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 72.89  E-value: 4.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSknlqAENKADSAEPetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGl 733
Cdd:PRK12467   639 DLLCGYS----GHNPEVALDP--DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG- 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  734 IGGLFTALVSGGSSVLFSPMTfIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARNYdlssmifLMVAAEPV 813
Cdd:PRK12467   712 VTELFGALASGATLHLLPPDC-ARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRA-------LVCGGEAL 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  814 RQITLKRFIELTLPFGLSQEvmapgYGLAENCVFVS---CAyGQGKPIFVDWQGRVCcgyvdpndPDVDIRI----ANPE 886
Cdd:PRK12467   784 QVDLLARVRALGPGARLINH-----YGPTETTVGVStyeLS-DEERDFGNVPIGQPL--------ANLGLYIldhyLNPV 849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  887 TGeeikesGKEGEIWISSSSAGIGYWGREELSQKTFkneLPDyP-----GRIYtRTGDLGR-IIDGKLFITGRIKDLIIV 960
Cdd:PRK12467   850 PV------GVVGELYIGGAGLARGYHRRPALTAERF---VPD-PfgadgGRLY-RTGDLARyRADGVIEYLGRMDHQVKI 918

                          330
                   ....*....|...
gi 2130317402  961 AGRNIYSADIEKT 973
Cdd:PRK12467   919 RGFRIELGEIEAR 931
y4iL_like cd08152
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ...
 1736-1995 4.65e-12

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: 69.60  E-value: 4.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1736 KGQLKIYDkiqGLPDH---NIFHPGKSYPVIVRHSNSLSADDDARI-DARGAAIRILsddvGSGGstPPLL--------D 1803
Cdd:cd08152     16 KAEFTVLD---DLPPElaqGLFAEPGTYPAVIRFSNAPGDILDDSVpDPRGMAIKVL----GVPG--EKLLpeedattqD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1804 LTLKTGKAFYARTIADFA--TWLVCGLAAREEHVKRVP----RVRDAVWMSLRNADSFTELH-----------YYSniCR 1866
Cdd:cd08152     87 FVLVNHPVFFARDAKDYLalLKLLARTTSLPDGAKAALsaplRGALRVLEAAGGESPTLKLGghppahplgetYWS--QA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1867 LFRFTDGqemYVKFKLRPfdetiseDSGKVEPvgiLPPDTGAIPRDENDTRPLLflADDFKRRvesptGVRYIFQLQVQp 1946
Cdd:cd08152    165 PYRFGDY---VAKYSVVP-------ASPALPA---LTGKELDLTDDPDALREAL--ADFLAEN-----DAEFEFRIQLC- 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402 1947 vpQDEATRDIAlDCTKPWDETEFPYIDIGEISID-QNLTKEES-----EKMEFNP 1995
Cdd:cd08152    224 --TDLEKMPIE-DASVEWPEALSPFVPVATITIPpQDFDSPARqrafdDNLSFNP 275
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 671-994 6.74e-12

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: 70.78  E-value: 6.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIgGLFTALVSGGSSVLF 750
Cdd:cd12116    120 RTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIA 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 SPMTfIKNPLLWLETMSKYQATH-SAGPNFaFELMLRRLESDKSTARnydlssmifLMVAAEPvrqitlkrfieltLPFG 829
Cdd:cd12116    199 PRET-QRDPEALARLIEAHSITVmQATPAT-WRMLLDAGWQGRAGLT---------ALCGGEA-------------LPPD 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 LSQEVMAPG------YGLAENCVFVSCAYGQ--------GKPIfvdWQGRVccgYVdpndpdVDIRIANPETGEeikesg 895
Cdd:cd12116    255 LAARLLSRVgslwnlYGPTETTIWSTAARVTaaagpipiGRPL---ANTQV---YV------LDAALRPVPPGV------ 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 kEGEIWISSSSAGIGYWGREELSQKTFkneLPD-YPG---RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADI 970
Cdd:cd12116    317 -PGELYIGGDGVAQGYLGRPALTAERF---VPDpFAGpgsRLY-RTGDLVRRRaDGRLEYLGRADGQVKIRGHRIELGEI 391

                          330       340
                   ....*....|....*....|....*..
gi 2130317402  971 EktvessSELLR-PGC--CAVVGVPEE 994
Cdd:cd12116    392 E------AALAAhPGVaqAAVVVREDG 412
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 523-971 6.88e-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: 70.77  E-value: 6.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  523 AVV---SRRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQALL 599
Cdd:cd17646     16 AVVdegRTLTYRELDERANRLAHLLRARG---VGPEDRVAVLLPRSADLVVALLAVLKA----------------GAAYL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 ---------KIENIAKSCNAVAILSTvgyhSAVRAGSVKNLILLTGKNGKTTGRWPNLPWlhtdswikysknlqaenkad 670
Cdd:cd17646     77 pldpgypadRLAYMLADAGPAVVLTT----ADLAARLPAGGDVALLGDEALAAPPATPPL-------------------- 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 sAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlIGGLFTALVSGGSSVLF 750
Cdd:cd17646    133 -VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVA 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 SPMTFiKNPLLWLETMSKYQAT--HsagpnFaFELMLRRL--ESDKSTARnydlsSMIFLMVAAEPVRQITLKRFIELtl 826
Cdd:cd17646    211 RPGGH-RDPAYLAALIREHGVTtcH-----F-VPSMLRVFlaEPAAGSCA-----SLRRVFCSGEALPPELAARFLAL-- 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 pFGLSqevMAPGYGLAENCVFVScaygqgkpifvDWQgrvccgyVDPNDPDVDIRIANPETGEEI---------KESGKE 897
Cdd:cd17646    277 -PGAE---LHNLYGPTEAAIDVT-----------HWP-------VRGPAETPSVPIGRPVPNTRLyvlddalrpVPVGVP 334

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  898 GEIWISSSSAGIGYWGREELSQKTFkneLPDY--PG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:cd17646    335 GELYLGGVQLARGYLGRPALTAERF---VPDPfgPGsRMY-RTGDLARWRpDGALEFLGRSDDQVKIRGFRVEPGEIE 408
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 665-996 7.25e-12

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: 70.48  E-value: 7.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  665 AENKADSAEPETDDLC---FLQFTSGSTGDAKGVMITH-GGLIHNVKLMQRRYRS--TSNTILVSWLPQYHDMGLIGgLF 738
Cdd:cd05929    110 EAAEGGSPETPIEDEAagwKMLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRW-SM 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  739 TALVSGGSSVL---FSPMTFiknpllwLETMSKYQATHSagpNFAFELMLRRLESDKSTARNYDLSSMIFLMVAAEP--- 812
Cdd:cd05929    189 TALFMGGTLVLmekFDPEEF-------LRLIERYRVTFA---QFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcpp 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  813 -VRQITLK----RFIELtlpfglsqevmapgYGLAEnCVFVSCAYGQ---------GKPIfvdwQGRVCCgyVDPNDPDV 878
Cdd:cd05929    259 wVKEQWIDwggpIIWEY--------------YGGTE-GQGLTIINGEewlthpgsvGRAV----LGKVHI--LDEDGNEV 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 dirianpETGEEikesgkeGEIWISSSSAgigywgreelsqKTFKN----ELPDYPGRIYTRTGDLGRI-IDGKLFITGR 953
Cdd:cd05929    318 -------PPGEI-------GEVYFANGPG------------FEYTNdpekTAAARNEGGWSTLGDVGYLdEDGYLYLTDR 371

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2130317402  954 IKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVL 996
Cdd:cd05929    372 RSDMIISGGVNIYPQEIENALIAHPKVLD---AAVVGVPDEEL 411
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 675-971 7.39e-12

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: 70.41  E-value: 7.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTIlvsWLpQYHDMGL---IGGLFTALVSGGSSVLFS 751
Cdd:cd17643     91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFdfsVWEIWGALLHGGRLVVVP 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PMTFIKNPLLWL----ETMSKYQATHSAgpnfafelMLRRLESDKSTARnyDLSSMIFLMVAAEPVRQITLKRFIEltlP 827
Cdd:cd17643    167 YEVARSPEDFARllrdEGVTVLNQTPSA--------FYQLVEAADRDGR--DPLALRYVIFGGEALEAAMLRPWAG---R 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  828 FGLSQEVMAPGYGLAENCVFVSC-------AYGQ-----GKPIfVDWQGRVccgyVDPNDPDVdirianpetgeeikESG 895
Cdd:cd17643    234 FGLDRPQLVNMYGITETTVHVTFrpldaadLPAAaaspiGRPL-PGLRVYV----LDADGRPV--------------PPG 294

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402  896 KEGEIWISSSSAGIGYWGREELSQKTFKNELPDYPGRIYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:cd17643    295 VVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLpDGELEYLGRADEQVKIRGFRIELGEIE 371
PRK05857 PRK05857
fatty acid--CoA ligase;
671-1065 9.99e-12

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 70.42  E-value: 9.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPE--TDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQ----RRYRSTSNTILVSWLPQYHdmglIGGLF---TAL 741
Cdd:PRK05857   161 AGNADqgSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQkeglNWVTWVVGETTYSPLPATH----IGGLWwilTCL 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLFSPMTFIKNPLLwletMSKYQATHSAGPNfafelMLRRLESD-KSTArnYDLSSMIFLMVAAEpvRQITLK- 819
Cdd:PRK05857   237 MHGGLCVTGGENTTSLLEIL----TTNAVATTCLVPT-----LLSKLVSElKSAN--ATVPSLRLVGYGGS--RAIAADv 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  820 RFIELTlpfGLSQevmAPGYGLAENCVFVSCAYGQGKPIfvdwqGRVCCGYVDPNDPDVDIRIANPETGE----EIKESG 895
Cdd:PRK05857   304 RFIEAT---GVRT---AQVYGLSETGCTALCLPTDDGSI-----VKIEAGAVGRPYPGVDVYLAATDGIGptapGAGPSA 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 KEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDL-GRIIDGKLFITGRIKDLIIVAGRNIYSADIEKTV 974
Cdd:PRK05857   373 SFGTLWIKSPANMLGYWNNPERTAEVLIDG--------WVNTGDLlERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIA 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  975 ESSSELLRPGCcavVGVPEEVLSTkgisvsdssdQVGLVVIAevrdAKTVDKEVVEKIKTRVAEEHGVTVASV----KLI 1050
Cdd:PRK05857   445 EGVSGVREAAC---YEIPDEEFGA----------LVGLAVVA----SAELDESAARALKHTIAARFRRESEPMarpsTIV 507

                          410
                   ....*....|....*
gi 2130317402 1051 KPRTISKTTSGKIKR 1065
Cdd:PRK05857   508 IVTDIPRTQSGKVMR 522
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 643-995 1.61e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 69.71  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  643 GRWPNLPWLHTDSwIKYSKNLQ--AENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGL-IHNVKLMQRRYRSTSNT 719
Cdd:PRK07867   117 GLDPGVRVINVDS-PAWADELAahRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRFGLGPDDV 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  720 ILVSwLPQYHDMGLIGGLFTALVSGGSSVL---FSPMTFiknpllwLETMSKYQATHS--AGPNFAFELMLRRLESDKS- 793
Cdd:PRK07867   196 CYVS-MPLFHSNAVMAGWAVALAAGASIALrrkFSASGF-------LPDVRRYGATYAnyVGKPLSYVLATPERPDDADn 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  794 TARnydlssMIFLMVAAEPvrqiTLKRFIEltlPFGLsqeVMAPGYGLAENCvfVSCAYGQGKPifvdwqgrvcCGYVDP 873
Cdd:PRK07867   268 PLR------IVYGNEGAPG----DIARFAR---RFGC---VVVDGFGSTEGG--VAITRTPDTP----------PGALGP 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  874 NDPDVDIRiaNPETGEE-----IKESGKE------GEIwISSSSAGI--GYWGREELSQKTFKNelpdypGRIYtrTGDL 940
Cdd:PRK07867   320 LPPGVAIV--DPDTGTEcppaeDADGRLLnadeaiGEL-VNTAGPGGfeGYYNDPEADAERMRG------GVYW--SGDL 388

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  941 G-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTvessseLLR-PGC--CAVVGVPEEV 995
Cdd:PRK07867   389 AyRDADGYAYFAGRLGDWMRVDGENLGTAPIERI------LLRyPDAteVAVYAVPDPV 441
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 668-994 1.74e-11

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: 69.46  E-value: 1.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  668 KADSAEPETDDLCFlqFTSGSTGDAKGVMITHGGLIHNVKLM--QRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGG 745
Cdd:cd05923    143 EDPPREPEQPAFVF--YTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDG 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  746 SSVL---FSPmtfiKNPLLWLEtmsKYQATHSagpnFAFELMLRRLESdKSTARNYDLSSMIFLMVAAEPVRQITLKRfI 822
Cdd:cd05923    221 TYVVveeFDP----ADALKLIE---QERVTSL----FATPTHLDALAA-AAEFAGLKLSSLRHVTFAGATMPDAVLER-V 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  823 ELTLPfGLSQEVmapgYGLAE--NCVFVSCAY--GQGKPIFVDwqgrvccgyvdpndpdvDIRIAN-PETGEEIKESGKE 897
Cdd:cd05923    288 NQHLP-GEKVNI----YGTTEamNSLYMRDARtgTEMRPGFFS-----------------EVRIVRiGGSPDEALANGEE 345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWI--SSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTV 974
Cdd:cd05923    346 GELIVaaAADAAFTGYLNQPEATAKKLQDG--------WYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVL 417

                          330       340
                   ....*....|....*....|..
gi 2130317402  975 EssselLRPGC--CAVVGVPEE 994
Cdd:cd05923    418 S-----RHPGVteVVVIGVADE 434
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 669-1066 2.49e-11

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: 68.70  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILvsWlpQYHDMGLIGGLFTALVS----G 744
Cdd:cd05973     80 AANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--W--NAADPGWAYGLYYAITGplalG 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVL----FSPmtfiknPLLWlETMSKYQATHSAGPNFAFelmlRRLESDKSTARNYDLSSMIFLMVAAEPVRQITLKR 820
Cdd:cd05973    156 HPTILleggFSV------ESTW-RVIERLGVTNLAGSPTAY----RLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRW 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  821 F-IELTLPfglsqevMAPGYGLAENCVFVSCAYGQGKPIFVDWQGRVCCGY-VDPNDPDVDirianpETGEeikesGKEG 898
Cdd:cd05973    225 FdAALGVP-------IHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWrVAVLDDDGD------ELGP-----GEPG 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  899 EIWISSSSAGI----GYWGREElsqktfknelPDYPGRIYtRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEkt 973
Cdd:cd05973    287 RLAIDIANSPLmwfrGYQLPDT----------PAIDGGYY-LTGDTVEFdPDGSFSFIGRADDVITMSGYRIGPFDVE-- 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  974 vesSSELLRPGC--CAVVGVPE----EVLStkgisvsdssdqvGLVVIAEVRDAKT-VDKEVVEKIKTRVAeEHGvtvas 1046
Cdd:cd05973    354 ---SALIEHPAVaeAAVIGVPDpertEVVK-------------AFVVLRGGHEGTPaLADELQLHVKKRLS-AHA----- 411

                          410       420
                   ....*....|....*....|....*.
gi 2130317402 1047 vkliKPRTIS------KTTSGKIKRF 1066
Cdd:cd05973    412 ----YPRTIHfvdelpKTPSGKIQRF 433
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 670-1066 2.84e-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: 68.55  E-value: 2.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  670 DSAEPETddLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDmGLIGGLFTALVSGGSSVL 749
Cdd:cd17649     89 LTHHPRQ--LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVL 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 fspmtfiKNPLLWLETMSKYQATHSAGPNFAfelmlrrlesDKSTARNYDLSSmifLMVAAEPVRQITLKRFI---ELTL 826
Cdd:cd17649    166 -------RPDELWASADELAEMVRELGVTVL----------DLPPAYLQQLAE---EADRTGDGRPPSLRLYIfggEALS 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 PFGLSQEVMAP-----GYGLAENCVFVS---CAYGQGK-----PIfvdwqGRVCCGYVdpndpdvdIRIANPETGEeiKE 893
Cdd:cd17649    226 PELLRRWLKAPvrlfnAYGPTEATVTPLvwkCEAGAARagasmPI-----GRPLGGRS--------AYILDADLNP--VP 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  894 SGKEGEIWISSSSAGIGYWGREELSQKTFkneLPD---YPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSA 968
Cdd:cd17649    291 VGVTGELYIGGEGLARGYLGRPELTAERF---VPDpfgAPGsRLY-RTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELG 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  969 DIEKTVESSSELLRpgcCAVVGVPeevlstkgisvSDSSDQVGLVVIAEVRDAKTVDKevvEKIKTRVAE---EHGVTVA 1045
Cdd:cd17649    367 EIEAALLEHPGVRE---AAVVALD-----------GAGGKQLVAYVVLRAAAAQPELR---AQLRTALRAslpDYMVPAH 429

                          410       420
                   ....*....|....*....|.
gi 2130317402 1046 SVKLIKprtISKTTSGKIKRF 1066
Cdd:cd17649    430 LVFLAR---LPLTPNGKLDRK 447
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
527-954 3.10e-11

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 68.77  E-value: 3.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEKPVIKPgdrvLLVYvPGLDF--VDCFFGCLRARVLPVPVLPPDPLQRggqaLLKIENI 604
Cdd:PRK04813    27 KLTYGQLKEDSDALAAFIDSLKLPDKSP----IIVF-GHMSPemLATFLGAVKAGHAYIPVDVSSPAER----IEMIIEV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  605 AKscnAVAILSTVGyhsavragsvknlilltgkngkttgrwpnLPWLHTDSWIKYSKNLQAENKADSAEPET-----DDL 679
Cdd:PRK04813    98 AK---PSLIIATEE-----------------------------LPLEILGIPVITLDELKDIFATGNPYDFDhavkgDDN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  680 CFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNtilVSWLPQ--YH-DMGLIGgLFTALVSGGSsvLFS-PMTF 755
Cdd:PRK04813   146 YYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEG---PQFLNQapYSfDLSVMD-LYPTLASGGT--LVAlPKDM 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  756 IKNPLLWLETMSKYQ-ATHSAGPNFAfELMLrrLESDKSTARNYDLSSMIFlmvAAE--PVR--QITLKRFieltlPfgl 830
Cdd:PRK04813   220 TANFKQLFETLPQLPiNVWVSTPSFA-DMCL--LDPSFNEEHLPNLTHFLF---CGEelPHKtaKKLLERF-----P--- 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 sQEVMAPGYGLAENCVFVS--------CAYGQGKPIfvdwqgrvccGYVDPndpDVDIRIANpETGEEIKEsGKEGEIWI 902
Cdd:PRK04813   286 -SATIYNTYGPTEATVAVTsieitdemLDQYKRLPI----------GYAKP---DSPLLIID-EEGTKLPD-GEQGEIVI 349

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2130317402  903 SSSSAGIGYWGREELSQKTFK--NELPDYpgriytRTGDLGRIIDGKLFITGRI 954
Cdd:PRK04813   350 SGPSVSKGYLNNPEKTAEAFFtfDGQPAY------HTGDAGYLEDGLLFYQGRI 397
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 685-1067 4.01e-11

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 67.87  E-value: 4.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  685 TSGSTGDAKGVMITHGGLIHNVKLMQRRYRS---TSNTILVswlpqyhdMGLIGGLFTA---LVSG----GSSVLfsPMT 754
Cdd:COG1541     91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAagvRPGDRVQ--------NAFGYGLFTGglgLHYGaerlGATVI--PAG 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  755 FIkNPLLWLETMSKYQATHSAG-PNFAFeLMLRRLESDKSTARNYDLSSMIFlmvAAEPVRQITLKRFIELtlpFGLsqE 833
Cdd:COG1541    161 GG-NTERQLRLMQDFGPTVLVGtPSYLL-YLAEVAEEEGIDPRDLSLKKGIF---GGEPWSEEMRKEIEER---WGI--K 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 VMApGYGLAE--NCVFVSCAYGQGkpiFVDWQGRVccgYVDpndpdvdirIANPETGEEIKEsGKEGEIWISSssagigy 911
Cdd:COG1541    231 AYD-IYGLTEvgPGVAYECEAQDG---LHIWEDHF---LVE---------IIDPETGEPVPE-GEEGELVVTT------- 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 wgreelsqkTFKNELPdypgRI-YtRTGDLGRIIDGK----------LFITGRIKDLIIVAGRNIYSADIEKTVESSSEL 980
Cdd:COG1541    287 ---------LTKEAMP----LIrY-RTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  981 lrpGCCAVVGVPEEvlstkgisvsDSSDQvgLVVIAEVRDAKTVDkEVVEKIKTRVAEEHGVTVAsVKLIKPRTISKTTs 1060
Cdd:COG1541    353 ---GPEYQIVVDRE----------GGLDE--LTVRVELAPGASLE-ALAEAIAAALKAVLGLRAE-VELVEPGSLPRSE- 414


                   ....*..
gi 2130317402 1061 GKIKRFE 1067
Cdd:COG1541    415 GKAKRVI 421
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2090-2293 4.12e-11

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: 68.62  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2090 LLQTILPyFLMGLVIFPPLNCLLFLKETKKLPLHWLLPLF----WLSSGLLAALACVVAKWVLVGKKKENETvKIWSAGV 2165
Cdd:TIGR02353  484 NLRIILP-FLLVQWAMLFALVVLDLQALDDYTEWGAVALLaaliLMAVGVGAFLILVERKWLVFGRLKPQEH-PLWSPFV 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2166 FV-DTTWQAFRTLVGDYFMEITGGSFLFMVWMKLMGSEIDldqGGGYVDSmgaVLNPE--MVEIERGGCVGREALLFGHI 2242
Cdd:TIGR02353  562 WLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKIG---RGVYIDG---TDLTErdLVTIGDDSTLNEGSVIQTHL 635

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 2243 YEgdDGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMKEEIV 2293
Cdd:TIGR02353  636 FE--DRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 500-1065 4.52e-11

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: 68.67  E-value: 4.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  500 LKHWGTHRVTQnkTLYTWINEEGAVVSRrTYRELHANASLISHKLltsEKPVIKPGDRVLLvYVP-GLDFVDCFFGCLRA 578
Cdd:cd05968     67 LDKWLADTRTR--PALRWEGEDGTSRTL-TYGELLYEVKRLANGL---RALGVGKGDRVGI-YLPmIPEIVPAFLAVARI 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  579 rvlpvpvlppdplqrgGQALLKI------ENIA---KSCNAVAILSTVGY--------------HSAVRAGSVKNLILLT 635
Cdd:cd05968    140 ----------------GGIVVPIfsgfgkEAAAtrlQDAEAKALITADGFtrrgrevnlkeeadKACAQCPTVEKVVVVR 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  636 GkngktTGRwPNLPWLHTDSWikySKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLihNVKLMQRRYR- 714
Cdd:cd05968    204 H-----LGN-DFTPAKGRDLS---YDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGF--PLKAAQDMYFq 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  715 -STSNTILVSWLPqyhDMGLIGG---LFTALVSGGSSVLF--SPmTFIKNPLLWlETMSKYQATH-SAGPNFAFELMLRR 787
Cdd:cd05968    273 fDLKPGDLLTWFT---DLGWMMGpwlIFGGLILGATMVLYdgAP-DHPKADRLW-RMVEDHEITHlGLSPTLIRALKPRG 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  788 LESdkstARNYDLSSMIFLMVAAEPVRQITLKRFIELTLpfglsqevmapgyglAENCVFvsCAYGQGKPIFvdwQGRVC 867
Cdd:cd05968    348 DAP----VNAHDLSSLRVLGSTGEPWNPEPWNWLFETVG---------------KGRNPI--INYSGGTEIS---GGILG 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  868 CGYVDPNDPdVDIRIANP--------ETGEEIkeSGKEGEIWISSSSAGI--GYWGREELSQKTFKNELPDypgrIYTRt 937
Cdd:cd05968    404 NVLIKPIKP-SSFNGPVPgmkadvldESGKPA--RPEVGELVLLAPWPGMtrGFWRDEDRYLETYWSRFDN----VWVH- 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  938 GDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVLSTKgisvsdssdqvgLVVIA 1016
Cdd:cd05968    476 GDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE---SAAIGVPHPVKGEA------------IVCFV 540

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402 1017 EVRDAKTVDKEVVEKIKTRVAEEHGvtvasvKLIKPRTI------SKTTSGKIKR 1065
Cdd:cd05968    541 VLKPGVTPTEALAEELMERVADELG------KPLSPERIlfvkdlPKTRNAKVMR 589
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 529-976 5.28e-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: 68.00  E-value: 5.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtsEKPViKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrGGQAL--------LK 600
Cdd:cd12117     24 TYAELNERANRLARRLR--AAGV-GPGDVVGVLAERSPELVVALLAVLKA---------------GAAYVpldpelpaER 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  601 IENIAKSCNAVAILSTvgyhsavragsvknlilltgknGKTTGRWPNLPwlhTDSWIkysknLQAENKADSAEPET---- 676
Cdd:cd12117     86 LAFMLADAGAKVLLTD----------------------RSLAGRAGGLE---VAVVI-----DEALDAGPAGNPAVpvsp 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGG---LIHNVKLM----QRRYRSTSNtilVSWlpqyhDMGLIGgLFTALVSGGSSVL 749
Cdd:cd12117    136 DDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTNYVtlgpDDRVLQTSP---LAF-----DASTFE-IWGALLNGARLVL 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 FSPMTfiknpLLWLETMSKYQATHsaGPNFAFelmlrrlesdkstarnydLSSMIF-LMVAAEPVRQITLKRFIeltlpF 828
Cdd:cd12117    207 APKGT-----LLDPDALGALIAEE--GVTVLW------------------LTAALFnQLADEDPECFAGLRELL-----T 256

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  829 GlsQEVMAP-----------------GYGLAENCVFvSCAY---------GQ---GKPIfvdwQGRVCcgYVdpndPDVD 879
Cdd:cd12117    257 G--GEVVSPphvrrvlaacpglrlvnGYGPTENTTF-TTSHvvteldevaGSipiGRPI----ANTRV--YV----LDED 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  880 IRIANPetgeeikesGKEGEIWISSSSAGIGYWGREELSQKTFKnELPDYPG-RIYtRTGDLGRII-DGKLFITGRIKDL 957
Cdd:cd12117    324 GRPVPP---------GVPGELYVGGDGLALGYLNRPALTAERFV-ADPFGPGeRLY-RTGDLARWLpDGRLEFLGRIDDQ 392

                          490
                   ....*....|....*....
gi 2130317402  958 IIVAGRNIYSADIEKTVES 976
Cdd:cd12117    393 VKIRGFRIELGEIEAALRA 411
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
663-1071 7.84e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 67.29  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKADSAEPETDDLCF---LQFTSGSTGDAKGVMITHG-------GLIHNVKLmqrryrsTSNTilvSWL---PQYH 729
Cdd:PRK03640   124 LMNGPKEEAEIQEEFDLDEvatIMYTSGTTGKPKGVIQTYGnhwwsavGSALNLGL-------TEDD---CWLaavPIFH 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  730 dmglIGGL---FTALVSGGSSVL---FSPmTFIKNpllWLE-----TMSKYQAthsagpnfafelMLRRLESDKSTAR-N 797
Cdd:PRK03640   194 ----ISGLsilMRSVIYGMRVVLvekFDA-EKINK---LLQtggvtIISVVST------------MLQRLLERLGEGTyP 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  798 YDLSSMiflMVAAEPVRQITLKRFIELTLPFGLSqevmapgYGLAENC---VFVSCAYGQ------GKPIFvdwqgrvcc 868
Cdd:PRK03640   254 SSFRCM---LLGGGPAPKPLLEQCKEKGIPVYQS-------YGMTETAsqiVTLSPEDALtklgsaGKPLF--------- 314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  869 gyvdpndpDVDIRIANpetGEEIKESGKEGEIWISSSSAGIGYWGREELSQKTFKNelpdypGRIYTrtGDLGRI-IDGK 947
Cdd:PRK03640   315 --------PCELKIEK---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD------GWFKT--GDIGYLdEEGF 375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  948 LFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPGccaVVGVPEEvlstkgisvsdssdQVGLVVIAEVRDAKTVDKE 1027
Cdd:PRK03640   376 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAG---VVGVPDD--------------KWGQVPVAFVVKSGEVTEE 438

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1028 VVEKIktrvAEEHgvtVASVKLIK--------PRtiskTTSGKIKRFEcLKQ 1071
Cdd:PRK03640   439 ELRHF----CEEK---LAKYKVPKrfyfveelPR----NASGKLLRHE-LKQ 478
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 677-971 1.49e-10

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: 66.12  E-value: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNtilvSWLPQYHDMGLIGG---LFTALVSGGSSVLFSPM 753
Cdd:cd17652     93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG----SRVLQFASPSFDASvweLLMALLAGATLVLAPAE 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFIKNPLLwLETMSKYQATHSAGPNFAfelmLRRLESDkstarnyDLSSMIFLMVAAEPVrqitlkrfieltlPFGLSQE 833
Cdd:cd17652    169 ELLPGEPL-ADLLREHRITHVTLPPAA----LAALPPD-------DLPDLRTLVVAGEAC-------------PAELVDR 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  834 -----VMAPGYGLAENCVFVSCAY----GQGKPIFVDWQGRVCcgYV-DPNDPDVDIrianpetgeeikesGKEGEIWIS 903
Cdd:cd17652    224 wapgrRMINAYGPTETTVCATMAGplpgGGVPPIGRPVPGTRV--YVlDARLRPVPP--------------GVPGELYIA 287

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402  904 SSSAGIGYWGREELSQKTFkneLPD---YPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:cd17652    288 GAGLARGYLNRPGLTAERF---VADpfgAPGsRMY-RTGDLARWRaDGQLEFLGRADDQVKIRGFRIELGEVE 356
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 666-1065 1.67e-10

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: 65.99  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  666 ENKADSAEPEtdDLCFLQFTSGSTGDAKGVmithgglIHNVKLMQRRYRSTSntilvsWLPQYHD-------------MG 732
Cdd:cd05969     80 EELYERTDPE--DPTLLHYTSGTTGTPKGV-------LHVHDAMIFYYFTGK------YVLDLHPddiywctadpgwvTG 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  733 LIGGLFTALVSGGSSVL----FSPMTfiknpllWLETMSKYQAT-HSAGPNfAFELMLRrleSDKSTARNYDLSSMIFLM 807
Cdd:cd05969    145 TVYGIWAPWLNGVTNVVyegrFDAES-------WYGIIERVKVTvWYTAPT-AIRMLMK---EGDELARKYDLSSLRFIH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  808 VAAEPvrqitlkrfieltlpfgLSQEVMAPGYGlaencVFvscaygqGKPIFVDWQGRVCCGYVDPNDPDVDIRIAN--- 884
Cdd:cd05969    214 SVGEP-----------------LNPEAIRWGME-----VF-------GVPIHDTWWQTETGSIMIANYPCMPIKPGSmgk 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  885 ----------PETGEEIkESGKEGEIWISSS--SAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFIT 951
Cdd:cd05969    265 plpgvkaavvDENGNEL-PPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG--------WYLTGDLAYRdEDGYFWFV 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  952 GRIKDLIIVAGRNIYSADIEKTVESSSELLRPGccaVVGVPEEVLstkgisvsdssdqvGLVVIAEV--RDAKTVDKEVV 1029
Cdd:cd05969    336 GRADDIIKTSGHRVGPFEVESALMEHPAVAEAG---VIGKPDPLR--------------GEIIKAFIslKEGFEPSDELK 398

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2130317402 1030 EKIKTRVAEEHGVTVAsvklikPRTIS------KTTSGKIKR 1065
Cdd:cd05969    399 EEIINFVRQKLGAHVA------PREIEfvdnlpKTRSGKIMR 434
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 876-1065 1.75e-10

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: 66.43  E-value: 1.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  876 PDVDIRIANPETGEEikESGKEGEIWISSSSAGI--GYWGREELSQKTFkneLPDYPGriYTRTGDLGRI-IDGKLFITG 952
Cdd:cd05966    417 FGIEPAILDEEGNEV--EGEVEGYLVIKRPWPGMarTIYGDHERYEDTY---FSKFPG--YYFTGDGARRdEDGYYWITG 489

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  953 RIKDLIIVAGRNIYSADIEktvesSSELLRPGC--CAVVGVPEEVlstKGISVsdssdqVGLVViaeVRDAKTVDKEVVE 1030
Cdd:cd05966    490 RVDDVINVSGHRLGTAEVE-----SALVAHPAVaeAAVVGRPHDI---KGEAI------YAFVT---LKDGEEPSDELRK 552

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2130317402 1031 KIKTRVAEEHGvtvasvKLIKPRTI------SKTTSGKIKR 1065
Cdd:cd05966    553 ELRKHVRKEIG------PIATPDKIqfvpglPKTRSGKIMR 587
PRK07233 PRK07233
hypothetical protein; Provisional
 23-270 1.92e-10

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 66.06  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEG----KMYdlggQVLAANSAPvIFDLAKETGSEle 98
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGGlpieRFY----HHIFKSDEA-LLELLDELGLE-- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   99 emdaHKLALIDASTGEYQDNKvaddyvsVISLT----------LELQDKAkdsgRIGVHAV-SDIASDLTP-------TY 160
Cdd:PRK07233    73 ----DKLRWRETKTGYYVDGK-------LYPLGtplellrfphLSLIDKF----RLGLLTLlARRIKDWRAldkvpaeEW 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  161 LESHGLKSVPKSV-------AYGYTASgygfvqDMPYAYI------HEFTRTSMAGKIR-RFKGGYMNFWRKLSEYLPI- 225
Cdd:PRK07233   138 LRRWSGEGVYEVFwepllesKFGDYAD------DVSAAWLwsrikrRGNRRYSLFGEKLgYLEGGFATLIDALAEAIEAr 211

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2130317402  226 --EVHCNTEVLAIRRNSATnvsvdVKNVNGECEVMEFDKIIISGSFP 270
Cdd:PRK07233   212 ggEIRLGTPVTSVVIDGGG-----VTGVEVDGEEEDFDAVISTAPPP 253
PRK12316 PRK12316
peptide synthase; Provisional
 662-971 2.60e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 66.90  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  662 NLQAENKADSAEPEtdDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDmGLIGGLFTAL 741
Cdd:PRK12316  3183 NYAEANPAIRTMPE--NLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPL 3259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLfspmtfiKNPLLWLETMSKYQATHSAGPNF--AFELMLRRLESDKSTARNYDLSSMIFLMVAaepvrqitlk 819
Cdd:PRK12316  3260 MSGARVVL-------AGPEDWRDPALLVELINSEGVDVlhAYPSMLQAFLEEEDAHRCTSLKRIVCGGEA---------- 3322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  820 rfieltLPFGLSQEVMAPGYglaencvfVSCAYGQGKPifVDWQGRVCCGYVDPNDPDVDIRIANP-----ETGEEIKES 894
Cdd:PRK12316  3323 ------LPADLQQQVFAGLP--------LYNLYGPTEA--TITVTHWQCVEEGKDAVPIGRPIANRacyilDGSLEPVPV 3386

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  895 GKEGEIWISSSSAGIGYWGREELSQKTFKNElPDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:PRK12316  3387 GALGELYLGGEGLARGYHNRPGLTAERFVPD-PFVPGERLYRTGDLARYrADGVIEYIGRVDHQVKIRGFRIELGEIE 3463
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 677-995 1.07e-09

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: 64.09  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIhnVKLMQRRYRSTSNTI-----LVSWLPQYHDMGLIGGLFTALVsgGSSVLFS 751
Cdd:cd17642    184 EQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNQIipdtaILTVIPFHHGFGMFTTLGYLIC--GFRVVLM 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PmTFIKNplLWLETMSKY--QATHSAGPNFAFelmlrrleSDKSTARN-YDLSSMIFLMVAAEP----VRQITLKRFiel 824
Cdd:cd17642    260 Y-KFEEE--LFLRSLQDYkvQSALLVPTLFAF--------FAKSTLVDkYDLSNLHEIASGGAPlskeVGEAVAKRF--- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 TLPFglsqevMAPGYGLAENCvfvscaygqgKPIFVDWQGRVCCGYVDPNDPDVDIRIANPETGEEIKeSGKEGEIWISS 904
Cdd:cd17642    326 KLPG------IRQGYGLTETT----------SAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLG-PNERGELCVKG 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  905 SSAGIGYWGREELSQktfknELPDYPGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRP 983
Cdd:cd17642    389 PMIMKGYVNNPEATK-----ALIDKDG--WLHSGDIAYYdEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDA 461

                          330
                   ....*....|..
gi 2130317402  984 GccaVVGVPEEV 995
Cdd:cd17642    462 G---VAGIPDED 470
PRK12316 PRK12316
peptide synthase; Provisional
 653-971 1.18e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 64.59  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  653 TDSWIKYSknlqAENKADSAEPetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDmG 732
Cdd:PRK12316  4676 DEDWEGFP----AHDPAVRLHP--DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-G 4748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  733 LIGGLFTALVSGGSSVlfspmtfIKNPLLWLETmSKYQATHSAG---PNFAfELMLRRLESDksTARNYDLSSMIFLMVA 809
Cdd:PRK12316  4749 SHEGLYHPLINGASVV-------IRDDSLWDPE-RLYAEIHEHRvtvLVFP-PVYLQQLAEH--AERDGEPPSLRVYCFG 4817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  810 AEPVRQITLKRFIELTLPFGLSQevmapGYGLAENCVFVSCaygqgkpifvdwqgRVCCGYVDPNDPDVDIRIANPETGE 889
Cdd:PRK12316  4818 GEAVAQASYDLAWRALKPVYLFN-----GYGPTETTVTVLL--------------WKARDGDACGAAYMPIGTPLGNRSG 4878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  890 EIKES-------GKEGEIWISSSSAGIGYWGREELSQKTFKNELPDYPG-RIYtRTGDLGRI-IDGKLFITGRIKDLIIV 960
Cdd:PRK12316  4879 YVLDGqlnplpvGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGgRLY-RTGDLARYrADGVIDYLGRVDHQVKI 4957

                          330
                   ....*....|.
gi 2130317402  961 AGRNIYSADIE 971
Cdd:PRK12316  4958 RGFRIELGEIE 4968
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 651-996 1.56e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 63.09  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  651 LHTDSWIKYsknlqaenkadsAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHD 730
Cdd:PRK07787   114 LHARSWHRY------------PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHV 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  731 MGLIGGLFTALVSGGSSV---LFSPmtfiknpllwletmSKYQATHSAGPN--FAFELMLRRLESDKSTARNydLSSMIF 805
Cdd:PRK07787   182 HGLVLGVLGPLRIGNRFVhtgRPTP--------------EAYAQALSEGGTlyFGVPTVWSRIAADPEAARA--LRGARL 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  806 LM--VAAEPV------RQITLKRFIELtlpfglsqevmapgYGLAENCVFVSC-AYGQGKPifvdwqgrvccGYVDPNDP 876
Cdd:PRK07787   246 LVsgSAALPVpvfdrlAALTGHRPVER--------------YGMTETLITLSTrADGERRP-----------GWVGLPLA 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  877 DVDIRIANpETGEEIKESGKE-GEIWISSSSAGIGYWGREELSQKTFkneLPDypGriYTRTGDLGRI-IDGKLFITGRI 954
Cdd:PRK07787   301 GVETRLVD-EDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAF---TAD--G--WFRTGDVAVVdPDGMHRIVGRE 372

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2130317402  955 K-DLIIVAGRNIYSADIEKTVessseLLRPGC--CAVVGVPEEVL 996
Cdd:PRK07787   373 StDLIKSGGYRIGAGEIETAL-----LGHPGVreAAVVGVPDDDL 412
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 685-994 2.14e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 63.02  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  685 TSGSTGDAKGVMITH-------GGLIHNVKLmqrryRSTSNTILVSwlPQYHDMGL-IGGLFTALvsgGSSVLFsPMTFi 756
Cdd:PRK07788   215 TSGTTGTPKGAPRPEpsplaplAGLLSRVPF-----RAGETTLLPA--PMFHATGWaHLTLAMAL---GSTVVL-RRRF- 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 kNPLLWLETMSKYQATH-SAGPnfafeLMLRR-LESDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIELtlpFGlsqEV 834
Cdd:PRK07788   283 -DPEATLEDIAKHKATAlVVVP-----VMLSRiLDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEA---FG---PV 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  835 MAPGYGLAEnCVFVSCAYGQgkpifvDWQ------GRVCCGyvdpndpdVDIRIANpETGEEIKEsGKEGEIWISSSSAG 908
Cdd:PRK07788   351 LYNLYGSTE-VAFATIATPE------DLAeapgtvGRPPKG--------VTVKILD-ENGNEVPR-GVVGRIFVGNGFPF 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  909 IGYWGreelsqktfknelPDYPGRI--YTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvesssELL--RP 983
Cdd:PRK07788   414 EGYTD-------------GRDKQIIdgLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVE-------DLLagHP 473

                          330
                   ....*....|...
gi 2130317402  984 GC--CAVVGVPEE 994
Cdd:PRK07788   474 DVveAAVIGVDDE 486
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2099-2292 2.92e-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: 62.85  E-value: 2.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2099 LMGLVIFPPLNCLLFLKETKK-LPLHWLL-----PLFWLSSGLLAALACVV--------AKWVLVGKKKEnETVKIWSAG 2164
Cdd:TIGR02353    1 VCQTLQLIPIVTLSGLQWLAPlLGYNWLYealddVSWLYLRAVALVFAVPVgrlgfaiaAKWLLVGRWKP-GTYPIWGST 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2165 VFvdtTWQAFRTLVGDYFMEITGGSFLFMVWMKLMGSEI--DLDQGGGYVDSMGavlnpeMVEIERGGCVGREALLFGHI 2242
Cdd:TIGR02353   80 YL---RFWTVKRLVDAAPTVLLSGSPLYSLYLRALGAKIgkGVDIGSLPPVCTD------LLTIGAGTIVRKEVMLLGYR 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 2243 YEGddGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALS-LAMKEEI 2292
Cdd:TIGR02353  151 AER--GRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSaLQGGQSI 199
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 529-995 3.05e-09

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: 62.19  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtsEKPViKPGDRVLLVYVPGLDFVDCFFGCLRArvlpvpvlppdplqrgGQALLKIEniaksc 608
Cdd:cd17645     25 TYKQLNEKANQLARHLR--GKGV-KPDDQVGIMLDKSLDMIAAILGVLKA----------------GGAYVPID------ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  609 navailstvgyhsavragsvknlilltgkngkttgrwPNLPwlhtDSWIKYsknLQAENKADSAEPETDDLCFLQFTSGS 688
Cdd:cd17645     80 -------------------------------------PDYP----GERIAY---MLADSSAKILLTNPDDLAYVIYTSGS 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  689 TGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDmGLIGGLFTALVSGGSSVLFSPMTfiknpLLWLETMSK 768
Cdd:cd17645    116 TGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFD-ASAWEIFPHLTAGAALHVVPSER-----RLDLDALND 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  769 YQATHSAGPNFafelmLRRLESDKSTArnYDLSSMIFLMVAAEpvrqiTLKRFIELtlPFGLSQevmapGYGLAENCVFV 848
Cdd:cd17645    190 YFNQEGITISF-----LPTGAAEQFMQ--LDNQSLRVLLTGGD-----KLKKIERK--GYKLVN-----NYGPTENTVVA 250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  849 SCA-----YGQ---GKPIfvdwqgrvccgyvdpndpdVDIRIANPETGEEIKESGKEGEIWISSSSAGIGYWGREELSQK 920
Cdd:cd17645    251 TSFeidkpYANipiGKPI-------------------DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  921 TFKNElPDYPGRIYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELL------------RPGCCA 987
Cdd:cd17645    312 KFIVH-PFVPGERMYRTGDLAKFLpDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIElaavlakedadgRKYLVA 390


                   ....*...
gi 2130317402  988 VVGVPEEV 995
Cdd:cd17645    391 YVTAPEEI 398
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 677-1084 3.57e-09

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 62.12  E-value: 3.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHN--VKLMQRRYrsTSNTILVSWLPQYHdmglIGGLFTAL--VSGGSSVLFSP 752
Cdd:PLN02860   172 DDAVLICFTSGTTGRPKGVTISHSALIVQslAKIAIVGY--GEDDVYLHTAPLCH----IGGLSSALamLMVGACHVLLP 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 mtfiknpllwletmsKYQAThsagpnFAFELMlrrlesdkstaRNYDLSSMIFL--MVA--AEPVR-QITLKRFIELT-- 825
Cdd:PLN02860   246 ---------------KFDAK------AALQAI-----------KQHNVTSMITVpaMMAdlISLTRkSMTWKVFPSVRki 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  826 ------LPFGLSQEV--------MAPGYGLAENC---VFVS-------------CAYGQGKPIFVDWQGRVCCGYVDPNd 875
Cdd:PLN02860   294 lngggsLSSRLLPDAkklfpnakLFSAYGMTEACsslTFMTlhdptlespkqtlQTVNQTKSSSVHQPQGVCVGKPAPH- 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  876 pdVDIRIANPEtgeeikeSGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgrIYTRTGDLGRIID-GKLFITGRI 954
Cdd:PLN02860   373 --VELKIGLDE-------SSRVGRILTRGPHVMLGYWGQNSETASVLSND-------GWLDTGDIGWIDKaGNLWLIGRS 436

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  955 KDLIIVAGRNIYSADIEKTVessseLLRPGC--CAVVGVPEEVLSTKGISV---------SDSSDQvglvviaEVRDAKT 1023
Cdd:PLN02860   437 NDRIKTGGENVYPEEVEAVL-----SQHPGVasVVVVGVPDSRLTEMVVACvrlrdgwiwSDNEKE-------NAKKNLT 504

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1024 VDKEVVeKIKTRVAEEHGVTVASVKLIKPRTISKTTSGKIKRFEcLKQFVDGTLNIVPEPL 1084
Cdd:PLN02860   505 LSSETL-RHHCREKNLSRFKIPKLFVQWRKPFPLTTTGKIRRDE-VRREVLSHLQSLPSNL 563
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 682-994 4.82e-09

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 61.84  E-value: 4.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVM--ITHG----GLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLfTALVSGGSSVL---FSP 752
Cdd:PRK08276   145 MLYSSGTTGRPKGIKrpLPGLdpdeAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGM-SALALGGTVVVmekFDA 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 MTFiknpllwLETMSKYQATHSAGPNFAFELMLRRLESdkstARN-YDLSSMIFLMVAAEPVRQITLKRFIELTLPfgls 831
Cdd:PRK08276   224 EEA-------LALIERYRVTHSQLVPTMFVRMLKLPEE----VRArYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP---- 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  832 qeVMAPGYGLAENC--VFVSCAYGQGKPIFVD--WQGRvccgyvdpndpdvdIRIANpETGEEIKeSGKEGEIWISSSSA 907
Cdd:PRK08276   289 --IIHEYYASSEGGgvTVITSEDWLAHPGSVGkaVLGE--------------VRILD-EDGNELP-PGEIGTVYFEMDGY 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  908 GIGYWGREElsqKTFKNELPdypgRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR-PGC 985
Cdd:PRK08276   351 PFEYHNDPE---KTAAARNP----HGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIE------NLLVThPKV 417

                          330
                   ....*....|.
gi 2130317402  986 --CAVVGVPEE 994
Cdd:PRK08276   418 adVAVFGVPDE 428
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1126-1187 5.53e-09

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: 54.49  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1126 EFLIRLVSEQTGIPSSNISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISD 1187
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK12316 PRK12316
peptide synthase; Provisional
 677-971 5.72e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 62.28  E-value: 5.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDmGLIGGLFTALVSgGSSVLFSPMTfi 756
Cdd:PRK12316  2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD-GAHEQWFHPLLN-GARVLIRDDE-- 2221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 knplLWL-----ETMSKYQATHSAGPNFAFELMLRRLESDKST--ARNYdlssmiflMVAAEPVRQITLKRFIEltlpfG 829
Cdd:PRK12316  2222 ----LWDpeqlyDEMERHGVTILDFPPVYLQQLAEHAERDGRPpaVRVY--------CFGGEAVPAASLRLAWE-----A 2284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 LSQEVMAPGYGLAENCVFVSCaygqgkpifvdWQgrvcCGYVDPND---PDVDIRIANP-----ETGEEIKESGKEGEIW 901
Cdd:PRK12316  2285 LRPVYLFNGYGPTEAVVTPLL-----------WK----CRPQDPCGaayVPIGRALGNRrayilDADLNLLAPGMAGELY 2349

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402  902 ISSSSAGIGYWGREELSQKTFkneLPDyP-----GRIYtRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:PRK12316  2350 LGGEGLARGYLNRPGLTAERF---VPD-PfsasgERLY-RTGDLARYrADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 527-994 5.84e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 61.44  E-value: 5.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  527 RRTYRELHANASLISHKLLTSEkpvIKPGDRVLLVYVPGLDFVDCFFGCLRARvlpvpvlppdplqrggqALL------- 599
Cdd:PRK07798    28 RLTYAELEERANRLAHYLIAQG---LGPGDHVGIYARNRIEYVEAMLGAFKAR-----------------AVPvnvnyry 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  600 ---KIENIAKSCNAVAILstvgYHSAVrAGSVKNLIlltgkngkttgrwPNLPWLHT-------------DSWIKYSKNL 663
Cdd:PRK07798    88 vedELRYLLDDSDAVALV----YEREF-APRVAEVL-------------PRLPKLRTlvvvedgsgndllPGAVDYEDAL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  664 -QAENKADSAEPETDDLCFLqFTSGSTGDAKGVMITH--------GGL-------IHNVKLMQRRYRSTSNTILVSWLPQ 727
Cdd:PRK07798   150 aAGSPERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQedifrvllGGRdfatgepIEDEEELAKRAAAGPGMRRFPAPPL 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  728 YHDMGLIGGlFTALVSGGSSVLFSPMTFikNPLLWLETMSKYQAT-------HSAGPnfafelMLRRLEsdksTARNYDL 800
Cdd:PRK07798   229 MHGAGQWAA-FAALFSGQTVVLLPDVRF--DADEVWRTIEREKVNvitivgdAMARP------LLDALE----ARGPYDL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  801 SSMIFLMVAAEPVRQITLKRFIELtLPfglsQEVMAPGYGLAE--NCVFVSCAYGQ---GKPIFvdwqgrvccgyvdpnD 875
Cdd:PRK07798   296 SSLFAIASGGALFSPSVKEALLEL-LP----NVVLTDSIGSSEtgFGGSGTVAKGAvhtGGPRF---------------T 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  876 PDVDIRIANPETGEEIKESGKEGeiWISSSsaG---IGYWGREELSQKTFknelPDYPGRIYTRTGDLGRI-IDGKLFIT 951
Cdd:PRK07798   356 IGPRTVVLDEDGNPVEPGSGEIG--WIARR--GhipLGYYKDPEKTAETF----PTIDGVRYAIPGDRARVeADGTITLL 427

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2130317402  952 GRIKDLIIVAGRNIYSADIEktvesssELLR--PGC--CAVVGVPEE 994
Cdd:PRK07798   428 GRGSVCINTGGEKVFPEEVE-------EALKahPDVadALVVGVPDE 467
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 684-1065 6.52e-09

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 61.25  E-value: 6.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  684 FTSGSTGDAKGVMITHGGLIHNVKLMQRR---YRSTSNTILVSWLPQYHDMGLIGGLFtALVSGGSSVL---FSPMTFik 757
Cdd:PRK12406   159 YTSGTTGHPKGVRRAAPTPEQAAAAEQMRaliYGLKPGIRALLTGPLYHSAPNAYGLR-AGRLGGVLVLqprFDPEEL-- 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  758 npllwLETMSKYQATHSagpnFAFELMLRRL-ESDKSTARNYDLSSMIFLMVAAEPV-RQItlKR-FIELTLPfglsqeV 834
Cdd:PRK12406   236 -----LQLIERHRITHM----HMVPTMFIRLlKLPEEVRAKYDVSSLRHVIHAAAPCpADV--KRaMIEWWGP------V 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  835 MAPGYGLAENCVFVSCAYGQ--GKPIFVdwqGRVCcgyvdpndPDVDIRIANpETGEEIkESGKEGEIWisSSSAGIG-- 910
Cdd:PRK12406   299 IYEYYGSTESGAVTFATSEDalSHPGTV---GKAA--------PGAELRFVD-EDGRPL-PQGEIGEIY--SRIAGNPdf 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  911 -YWGREElsqktfKNELPDYPGRIytRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEktvessSELLR-PGC-- 985
Cdd:PRK12406   364 tYHNKPE------KRAEIDRGGFI--TSGDVGYLdADGYLFLCDRKRDMVISGGVNIYPAEIE------AVLHAvPGVhd 429

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  986 CAVVGVPEEVLSTkgisvsdssdqvGLVVIAEVRDAKTVDKEVVEK-IKTRVAeehGVTVASVKLIKPRtISKTTSGKI- 1063
Cdd:PRK12406   430 CAVFGIPDAEFGE------------ALMAVVEPQPGATLDEADIRAqLKARLA---GYKVPKHIEIMAE-LPREDSGKIf 493


                   ..
gi 2130317402 1064 KR 1065
Cdd:PRK12406   494 KR 495
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 32-283 9.35e-09

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: 60.58  E-value: 9.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   32 SGLSAAYALTKLGyRNVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLaANSAPVIFDLAKETGSELEE--MDAHKLALID 109
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGLEDRLvlPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  110 ASTGEYQDNKVADDYVSVISL-----TLELQDKAKDSGRIGVHAVSDIASDLTPTYLES---HGLKSVPKSVAYGYTASG 181
Cdd:pfam01593   80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRLGLAALASDALDEFDLDDFSLAESllfLGRRGPGDVEVWDRLIDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRFKGGYMNFWRKLSEYLPI-EVHCNTEVLAIRRNSATnV 244
Cdd:pfam01593  160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLGgDVRLNTRVRSIDREGDG-V 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2130317402  245 SVDVKNvngeCEVMEFDKIIISGSFPMRNGKIYRLPLSK 283
Cdd:pfam01593  238 TVTLTD----GEVIEADAVIVTVPLGVLKRILFTPPLPP 272
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 673-994 9.52e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 60.86  E-value: 9.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  673 EPETDDLcflQFTSGSTGDAKGVM--ITHGGLIHNVKL---MQRRYRSTSNTILVSWLPQYHDMGLiggLFTALV--SGG 745
Cdd:PRK13391   153 ESLGTDM---LYSSGTTGRPKGIKrpLPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHSAPQ---RAVMLVirLGG 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  746 SSVL---FSPMTFiknpllwLETMSKYQATHSAGPNFAFELMLRRLESDKSTarnYDLSSMIFLMVAAEPVRQITLKRFI 822
Cdd:PRK13391   227 TVIVmehFDAEQY-------LALIEEYGVTHTQLVPTMFSRMLKLPEEVRDK---YDLSSLEVAIHAAAPCPPQVKEQMI 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  823 ELTLPfglsqeVMAPGYGLAENCVFVSCAYGQ--GKPIFVdwqGRVCCGyvdpndpdvDIRIANpETGEEIKeSGKEGEI 900
Cdd:PRK13391   297 DWWGP------IIHEYYAATEGLGFTACDSEEwlAHPGTV---GRAMFG---------DLHILD-DDGAELP-PGEPGTI 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  901 WISSSSAgIGYWGREElsqKTFKNELPDyPGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSE 979
Cdd:PRK13391   357 WFEGGRP-FEYLNDPA---KTAEARHPD-GT--WSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPK 429

                          330
                   ....*....|....*
gi 2130317402  980 LLRpgcCAVVGVPEE 994
Cdd:PRK13391   430 VAD---AAVFGVPNE 441
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 23-60 1.09e-08

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: 60.15  E-value: 1.09e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGM 60
Cdd:COG0493    123 KVAVVGSGPAGLAAAYQLARAGHE-VTVFEALDKPGGL 159
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 654-1071 1.88e-08

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: 59.79  E-value: 1.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  654 DSWIKYSKNLQ-AENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRS-TSNTIlvSWlpQYHDM 731
Cdd:cd05928    150 DGWLNFKELLNeASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDlTASDI--MW--NTSDT 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  732 GLIGGLFTALVSG---GSSVLFSPMTFIkNPLLWLETMSKYQATHSAGPNFAFELMLRRlesdkstarnyDLSSMIF--- 805
Cdd:cd05928    226 GWIKSAWSSLFEPwiqGACVFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQ-----------DLSSYKFpsl 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  806 --LMVAAEPVRQITLKRFIELTlpfGLSqevMAPGYGLAEncVFVSCAYGQG---KPifvdwqgrvccGYVDPNDPDVDI 880
Cdd:cd05928    294 qhCVTGGEPLNPEVLEKWKAQT---GLD---IYEGYGQTE--TGLICANFKGmkiKP-----------GSMGKASPPYDV 354

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  881 RIANpETGEeIKESGKEGEIWISSSSAG-----IGYWGREELSQKTFKnelpdypGRIYTrTGDLGRI-IDGKLFITGRI 954
Cdd:cd05928    355 QIID-DNGN-VLPPGTEGDIGIRVKPIRpfglfSGYVDNPEKTAATIR-------GDFYL-TGDRGIMdEDGYFWFMGRA 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  955 KDLIIVAGRNIYSADIEKT-------VESssellrpgccAVVGVPEEVlstKGISVSdssdqvGLVVIA---EVRDAKTV 1024
Cdd:cd05928    425 DDVINSSGYRIGPFEVESAliehpavVES----------AVVSSPDPI---RGEVVK------AFVVLApqfLSHDPEQL 485

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2130317402 1025 DKEVVEKIKTrvaeehgvTVASVKLikPRTIS------KTTSGKIKRFECLKQ 1071
Cdd:cd05928    486 TKELQQHVKS--------VTAPYKY--PRKVEfvqelpKTVTGKIQRNELRDK 528
PRK07208 PRK07208
hypothetical protein; Provisional
 26-75 1.94e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 59.52  E-value: 1.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2130317402   26 IVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVSGMCESVEIEGKMYDLGG 75
Cdd:PRK07208     9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 671-994 2.94e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 59.44  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  671 SAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGL-IGGLFTALVsgGSSVL 749
Cdd:PRK06334   177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLS--GVPVV 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 FSpmtfiKNPLL---WLETMSKYQATHSAGPNFAFELMLRRLESDKSTarnydLSSMIFLMVAAE----PVRQITLKRFI 822
Cdd:PRK06334   255 FA-----YNPLYpkkIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESC-----LPSLRFVVIGGDafkdSLYQEALKTFP 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  823 ELTLpfglsqevmAPGYGLAEnCVFVSCAYGQGKPifvdwQGRVCCGYvdPNDpDVDIRIANPETGEEIkESGKEGEIWI 902
Cdd:PRK06334   325 HIQL---------RQGYGTTE-CSPVITINTVNSP-----KHESCVGM--PIR-GMDVLIVSEETKVPV-SSGETGLVLT 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  903 SSSSAGIGYWGREelsqktFKNELPDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIysadiekTVESSSELL 981
Cdd:PRK06334   386 RGTSLFSGYLGED------FGQGFVELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMV-------SLEALESIL 452

                          330
                   ....*....|...
gi 2130317402  982 RPGCcavvGVPEE 994
Cdd:PRK06334   453 MEGF----GQNAA 461
PRK12316 PRK12316
peptide synthase; Provisional
 666-971 3.38e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 59.97  E-value: 3.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  666 ENKADSAEPEtdDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY-RSTSNTILVSwLPQYHDMGlIGGLFTALVSG 744
Cdd:PRK12316   646 ENPGTELNPE--NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYgLGVGDTVLQK-TPFSFDVS-VWEFFWPLMSG 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  745 GSSVLFSPMTFiKNPLLWLETMskyqATHSAGPNFAFELMLRRLESDKSTArnyDLSSMIFLMVAAEPVRQITLKRFIEL 824
Cdd:PRK12316   722 ARLVVAAPGDH-RDPAKLVELI----NREGVDTLHFVPSMLQAFLQDEDVA---SCTSLRRIVCSGEALPADAQEQVFAK 793

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  825 tlpfgLSQEVMAPGYGLAENCVFVSC---------AYGQGKPIfvdwqGRVCCGYVDPNDPDVDIRIAnpetgeeikesg 895
Cdd:PRK12316   794 -----LPQAGLYNLYGPTEAAIDVTHwtcveeggdSVPIGRPI-----ANLACYILDANLEPVPVGVL------------ 851

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 keGEIWISSSSAGIGYWGREELSQKTFkneLPDYPG---RIYtRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:PRK12316   852 --GELYLAGRGLARGYHGRPGLTAERF---VPSPFVageRMY-RTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIE 925
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 806-1067 4.30e-08

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: 58.40  E-value: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  806 LMVAAEPVRQITLKRfIELTLP------FGLSqEVMAPGYGLaencvfvSCAYGQGKPIFVDwqgrvcCGYVDpndpdvd 879
Cdd:cd05913    203 GIFGAEPWTEEMRKR-IERRLGikaydiYGLT-EIIGPGVAF-------ECEEKDGLHIWED------HFIPE------- 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  880 irIANPETGEEIKEsGKEGEIWISSssagigyWGREELsqktfknelpdyPGRIYtRTGDLGRIIDGK----------LF 949
Cdd:cd05913    261 --IIDPETGEPVPP-GEVGELVFTT-------LTKEAM------------PLIRY-RTRDITRLLPGPcpcgrthrriDR 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  950 ITGRIKDLIIVAGRNIYSADIEKTVessseLLRPGCCA----VVGVPE--EVLSTKgISVSDSSDqvglvviaEVRDAKT 1023
Cdd:cd05913    318 ITGRSDDMLIIRGVNVFPSQIEDVL-----LKIPGLGPhyqlILTRQEhlDELTIK-VEVRPEAD--------DDEKLEA 383

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2130317402 1024 VDKEVVEKIKTRVaeehGVTVAsVKLIKPRTISKTTsGKIKRFE 1067
Cdd:cd05913    384 LKQRLERHIKSVL----GVTVE-VELVEPGSLPRSE-GKAKRVI 421
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 663-958 4.78e-08

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 58.97  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK-LMQRRYRSTSNTILVSWLPQYHDMGLIGGlfTAL 741
Cdd:PLN02387   236 LGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgVMTVVPKLGKNDVYLAYLPLAHILELAAE--SVM 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  742 VSGGSSVLF-SPMTFIknpllwlETMSKYQ------ATH------SAGP-------------------------NFAFEl 783
Cdd:PLN02387   314 AAVGAAIGYgSPLTLT-------DTSNKIKkgtkgdASAlkptlmTAVPaildrvrdgvrkkvdakgglakklfDIAYK- 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  784 mlRRLES-DKSTARNYDLSSMIFLMVAAEPVRQI-----------------TLKRFIELTLPFGLSQevmapGYGLAEnc 845
Cdd:PLN02387   386 --RRLAAiEGSWFGAWGLEKLLWDALVFKKIRAVlggrirfmlsggaplsgDTQRFINICLGAPIGQ-----GYGLTE-- 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  846 vfvSCAYGQgkpiFVDWQGrVCCGYVDPNDPDVDIRIAN-PETGEEIKESG-KEGEIWISSSSAGIGYWGREELSQKTFK 923
Cdd:PLN02387   457 ---TCAGAT----FSEWDD-TSVGRVGPPLPCCYVKLVSwEEGGYLISDKPmPRGEIVIGGPSVTLGYFKNQEKTDEVYK 528

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2130317402  924 NelpDYPGRIYTRTGDLGRI-IDGKLFITGRIKDLI 958
Cdd:PLN02387   529 V---DERGMRWFYTGDIGQFhPDGCLEIIDRKKDIV 561
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1584-1671 4.90e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 54.11  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSIRAINPVSCPKQISIGAGVHLGDFSRIISGFY-----SSTGFISGKVEVQENSVIGSQSLILPNSVVQKDV 1658
Cdd:COG0110     27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGA 106

                           90
                   ....*....|....*..
gi 2130317402 1659 ILGALSVA----PAHSV 1671
Cdd:COG0110    107 VVGAGSVVtkdvPPYAI 123
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 652-1035 5.26e-08

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: 58.59  E-value: 5.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  652 HTDSWIKYSKNLQAENKA-DSAEPET----------DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTI 720
Cdd:cd17641    122 YDDPRLISFEDVVALGRAlDRRDPGLyerevaagkgEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDE 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  721 LVSWLPQYHDMGLIGGLFTALVSG-------------------GSSVLFSPmtfiknPLLWLETMSKYQATHS-AGP--N 778
Cdd:cd17641    202 YVSVLPLPWIGEQMYSVGQALVCGfivnfpeepetmmedlreiGPTFVLLP------PRVWEGIAADVRARMMdATPfkR 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  779 FAFEL-------MLRRLESDKSTARNYDLSSMIFLMVAAEPVR-QITLKRF-IELTLPFGLSQEVM----APG------Y 839
Cdd:cd17641    276 FMFELgmklglrALDRGKRGRPVSLWLRLASWLADALLFRPLRdRLGFSRLrSAATGGAALGPDTFrffhAIGvplkqlY 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  840 GLAENCVFvscaygqgkpIFVDWQGRVCCGYVDPNDPDVDIRIANpetgeeikesgkEGEIWISSSSAGIGYWGREELSQ 919
Cdd:cd17641    356 GQTELAGA----------YTVHRDGDVDPDTVGVPFPGTEVRIDE------------VGEILVRSPGVFVGYYKNPEATA 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  920 KTFKNElpdypGriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSAD-IEKTVESSSELL--------RPGCCAVV 989
Cdd:cd17641    414 EDFDED-----G--WLHTGDAGYFkENGHLVVIDRAKDVGTTSDGTRFSPQfIENKLKFSPYIAeavvlgagRPYLTAFI 486

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  990 GVPEEVLST----KGISVSDSSD-----QVGLVVIAEVRdakTVDKEVVEKIKTR 1035
Cdd:cd17641    487 CIDYAIVGKwaeqRGIAFTTYTDlasrpEVYELIRKEVE---KVNASLPEAQRIR 538
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 678-961 6.25e-08

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 58.49  E-value: 6.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRS-----TSNTILVSWLPQYHDMGLIggLFTALVSGGSSVLF-- 750
Cdd:PLN02614   224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanaalTVKDVYLSYLPLAHIFDRV--IEECFIQHGAAIGFwr 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 -------------SPMTFIKNPLLWLETMSKYQATHSAG---PNFAFELMLRRLESDKSTARNYDLSSMIFLMVAAEPVR 814
Cdd:PLN02614   302 gdvklliedlgelKPTIFCAVPRVLDRVYSGLQKKLSDGgflKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  815 Q-------------ITLKRFIELTLPFGLSQEVMApGYGLAENC--VFVScaygqgkpiFVDWQGRVccGYVDPNDPDVD 879
Cdd:PLN02614   382 QglggnvriilsgaAPLASHVESFLRVVACCHVLQ-GYGLTESCagTFVS---------LPDELDML--GTVGPPVPNVD 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  880 IRIAN-PETGEEIKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDL 957
Cdd:PLN02614   450 IRLESvPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWqPNGSMKIIDRKKNI 521


                   ....
gi 2130317402  958 IIVA 961
Cdd:PLN02614   522 FKLS 525
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 657-996 8.17e-08

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 58.19  E-value: 8.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  657 IKYSKnLQAENKADSAE---PETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQ---YHD 730
Cdd:PLN02736   199 VTYSK-LLAQGRSSPQPfrpPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLahiYER 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  731 MGLIgglftALVSGGSSVLF---------------SPMTFIKNPLLWLETMSKYQAT-HSAGP------NFAFELMLRRL 788
Cdd:PLN02736   278 VNQI-----VMLHYGVAVGFyqgdnlklmddlaalRPTIFCSVPRLYNRIYDGITNAvKESGGlkerlfNAAYNAKKQAL 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  789 ESDKSTARNYDlsSMIFLMVAAEPVRQItlkRFIeLTLPFGLSQEVM-----------APGYGLAE-NCVFVSCAygqgk 856
Cdd:PLN02736   353 ENGKNPSPMWD--RLVFNKIKAKLGGRV---RFM-SSGASPLSPDVMeflricfggrvLEGYGMTEtSCVISGMD----- 421

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  857 pifvdwQGRVCCGYVDPNDPDVDIRIAN-PETGEEIKESG-KEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriY 934
Cdd:PLN02736   422 ------EGDNLSGHVGSPNPACEVKLVDvPEMNYTSEDQPyPRGEICVRGPIIFKGYYKDEVQTREVIDED-----G--W 488

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130317402  935 TRTGDLGR-IIDGKLFITGRIKDLIIVA-GRNIYSADIEKTVESS---------SELLRPGCCAVVGVPEEVL 996
Cdd:PLN02736   489 LHTGDIGLwLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCkfvaqcfvyGDSLNSSLVAVVVVDPEVL 561
PRK12467 PRK12467
peptide synthase; Provisional
 663-971 1.13e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 58.25  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKADSAEPET--------DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlI 734
Cdd:PRK12467  1696 LDQEDDWLEGYSDSnpavnlapQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS-V 1774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  735 GGLFTALVSGGSSVLFSPMTFiKNPLLWLETMSKYQATHSAGPNFAFELMlrrLESDKSTARNYDLSSMIFlmvAAEPVR 814
Cdd:PRK12467  1775 WELFWPLINGARLVIAPPGAH-RDPEQLIQLIERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVC---GGEALE 1847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  815 QITLKRFIELTLPFGLSQevmapGYGLAENCVFVS---CAYGqgkpifvDWQGRVCcgyvdpndpdVDIRIANPETGEEI 891
Cdd:PRK12467  1848 VEALRPWLERLPDTGLFN-----LYGPTETAVDVThwtCRRK-------DLEGRDS----------VPIGQPIANLSTYI 1905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  892 KES-------GKEGEIWISSSSAGIGYWGREELSQKTF-KNELPDYPGRIYtRTGDLGRI-IDGKLFITGRIKDLIIVAG 962
Cdd:PRK12467  1906 LDAslnpvpiGVAGELYLGGVGLARGYLNRPALTAERFvADPFGTVGSRLY-RTGDLARYrADGVIEYLGRIDHQVKIRG 1984


                   ....*....
gi 2130317402  963 RNIYSADIE 971
Cdd:PRK12467  1985 FRIELGEIE 1993
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1119-1191 1.29e-07

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: 51.01  E-value: 1.29e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130317402 1119 MSNKDIVEFLIRLVSEQTGIPSSNISATGSLVS-YGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISDLANF 1191
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADY 74
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1352-1438 1.40e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 52.95  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1352 NCWFEMLGARIGSSVLLDT-VDITDPSLVSIGDGAVIAEGVLV--QGHEVRN---GVLSFLPIRIGRNSSVGPFAVIQKG 1425
Cdd:COG0110     20 GVRIYGGNITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWIGAGATILPG 99

                           90
                   ....*....|....*
gi 2130317402 1426 SIIGDEA--DAGAAV 1438
Cdd:COG0110    100 VTIGDGAvvGAGSVV 114
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 672-1025 3.16e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 55.80  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  672 AEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL-- 749
Cdd:PRK13388   145 REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALpa 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  750 -FSPMTFiknpllwLETMSKYQATH--SAGPNFAFELMLRRLESDKSTArnydlssmifLMVA----AEPvRQITlkrfi 822
Cdd:PRK13388   225 kFSASGF-------LDDVRRYGATYfnYVGKPLAYILATPERPDDADNP----------LRVAfgneASP-RDIA----- 281

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  823 ELTLPFGLSqevMAPGYGLAENCVFVSCAYGQGKPIFvdwqGRvccgyvdpndPDVDIRIANPETGEE-----IKESGKE 897
Cdd:PRK13388   282 EFSRRFGCQ---VEDGYGSSEGAVIVVREPGTPPGSI----GR----------GAPGVAIYNPETLTEcavarFDAHGAL 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 -------GEIWISSSSAGI-GYWGREELSQKTFKNelpdypGRIYtrTGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSA 968
Cdd:PRK13388   345 lnadeaiGELVNTAGAGFFeGYYNNPEATAERMRH------GMYW--SGDLAyRDADGWIYFAGRTADWMRVDGENLSAA 416

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  969 DIEKTvessseLLR-PGC--CAVVGVPEEVlstkgisvsdSSDQVGLVViaEVRDAKTVD 1025
Cdd:PRK13388   417 PIERI------LLRhPAInrVAVYAVPDER----------VGDQVMAAL--VLRDGATFD 458
PRK12467 PRK12467
peptide synthase; Provisional
 651-971 3.36e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 56.71  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  651 LHTDSWIKYSKNlqaeNKADSAEPEtdDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHD 730
Cdd:PRK12467  3217 LDRLDLNGYSEN----NPSTRVMGE--NLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD 3290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  731 mGLIGGLFTALVSGGSSVlfspmtfIKNPLLW--LETMSKYQATHSAGPNFAfELMLRRLESDKSTARNYDLSSMIFLMV 808
Cdd:PRK12467  3291 -GAQERFLWTLICGGCLV-------VRDNDLWdpEELWQAIHAHRISIACFP-PAYLQQFAEDAGGADCASLDIYVFGGE 3361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  809 AAEPVRQITLKRFIE---LTLPFGLSQEVMAPgygLAENCVFVSCAYGQGKPIFVDWQGRVCcgYV-DPNdpdvdiriAN 884
Cdd:PRK12467  3362 AVPPAAFEQVKRKLKprgLTNGYGPTEAVVTV---TLWKCGGDAVCEAPYAPIGRPVAGRSI--YVlDGQ--------LN 3428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  885 PETgeeikeSGKEGEIWISSSSAGIGYWGREELSQKTF-KNELPDYPGRIYtRTGDLGRI-IDGKLFITGRIKDLIIVAG 962
Cdd:PRK12467  3429 PVP------VGVAGELYIGGVGLARGYHQRPSLTAERFvADPFSGSGGRLY-RTGDLARYrADGVIEYLGRIDHQVKIRG 3501


                   ....*....
gi 2130317402  963 RNIYSADIE 971
Cdd:PRK12467  3502 FRIELGEIE 3510
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 669-1064 8.44e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 54.63  E-value: 8.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLC--FLQFTSGSTGDAKGVMITHGGLIHN------VKLMQRRYRSTSNTILVSWLPQYHDMGL-IGGLFT 739
Cdd:PRK13390   138 AGAGPRLTEQPCgaVMLYSSGTTGFPKGIQPDLPGRDVDapgdpiVAIARAFYDISESDIYYSSAPIYHAAPLrWCSMVH 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  740 ALvsgGSSVLFSPMTFIKNPLLWLEtmsKYQATHSagpNFAFELMLRRLESDKSTARNYDLSSMIFLMVAAEP----VRQ 815
Cdd:PRK13390   218 AL---GGTVVLAKRFDAQATLGHVE---RYRITVT---QMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKH 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  816 ITLKRFIELTLPFGLSQEVmapgYGLAencvFVSCAYGQGKPIFVdwqGRVCCGYVDPNDPDvdirianpetGEEIKeSG 895
Cdd:PRK13390   289 AMIDWLGPIVYEYYSSTEA----HGMT----FIDSPDWLAHPGSV---GRSVLGDLHICDDD----------GNELP-AG 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  896 KEGEIWISSSSAGIGYWGREElsqKTFKNELPDYPgrIYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEKTV 974
Cdd:PRK13390   347 RIGTVYFERDRLPFRYLNDPE---KTAAAQHPAHP--FWTTVGDLGSVDEdGYLYLADRKSFMIISGGVNIYPQETENAL 421

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  975 EssselLRPGC--CAVVGVPEevlstkgisvSDSSDQVGLVV--IAEVRDAKTVDKEVVEKIKTRVAeeHGVTVASVKLI 1050
Cdd:PRK13390   422 T-----MHPAVhdVAVIGVPD----------PEMGEQVKAVIqlVEGIRGSDELARELIDYTRSRIA--HYKAPRSVEFV 484

                          410
                   ....*....|....*..
gi 2130317402 1051 K--PRT-ISKTTSGKIK 1064
Cdd:PRK13390   485 DelPRTpTGKLVKGLLR 501
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 659-773 9.88e-07

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 54.50  E-value: 9.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  659 YSKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITH----------GGLIhnvklmqrryRSTSNTILVSWLPQY 728
Cdd:PRK08279   181 AAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLL----------RLTPDDVLYCCLPLY 250

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2130317402  729 HDMGLIGGLFTALVSGGSSVL---FSPMTFiknpllWLEtMSKYQATH 773
Cdd:PRK08279   251 HNTGGTVAWSSVLAAGATLALrrkFSASRF------WDD-VRRYRATA 291
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 678-772 1.05e-06

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: 53.90  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSPMT 754
Cdd:cd05940     82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASN 161

                           90
                   ....*....|....*...
gi 2130317402  755 FiknpllWLETMsKYQAT 772
Cdd:cd05940    162 F------WDDIR-KYQAT 172
PRK13382 PRK13382
bile acid CoA ligase;
674-994 1.11e-06

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 53.99  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  674 PETDDLCFLqfTSGSTGDAKGVMITHGGLIHNVKLMQRR--YRSTSNTILVSwlPQYHDMGLIGGLFTALVSggssvlfS 751
Cdd:PRK13382   195 GRKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRtpWRAEEPTVIVA--PMFHAWGFSQLVLAASLA-------C 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  752 PMTFIK--NPLLWLETMSKYQATHSAgpnfAFELMLRRLESDKSTARN-YDLSSMIFLMVAAEPVRQITLKRFIEltlPF 828
Cdd:PRK13382   264 TIVTRRrfDPEATLDLIDRHRATGLA----VVPVMFDRIMDLPAEVRNrYSGRSLRFAAASGSRMRPDVVIAFMD---QF 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  829 GlsqEVMAPGYGLAEnCVFVSCAYGQGKPIFVDWQGRVCCGyvdpndpdVDIRIANPEtGEEIKEsGKEGEIWISSSSAG 908
Cdd:PRK13382   337 G---DVIYNNYNATE-AGMIATATPADLRAAPDTAGRPAEG--------TEIRILDQD-FREVPT-GEVGTIFVRNDTQF 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  909 IGYwgrEELSQKTFKNElpdypgriYTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCA 987
Cdd:PRK13382   403 DGY---TSGSTKDFHDG--------FMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE---AA 468


                   ....*..
gi 2130317402  988 VVGVPEE 994
Cdd:PRK13382   469 VIGVDDE 475
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 673-973 1.17e-06

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: 53.98  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  673 EPEtdDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGlIGGLFTALVSGGSSVLfSP 752
Cdd:cd17644    104 QPE--NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVL-RP 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  753 MTFIKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTArnydLSSMIFLMVAAEPVRQITLKRFIELTLPFGLSQ 832
Cdd:cd17644    180 EEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDL----PSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLI 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVmapgYGLAENCVFVSC----AYGQ--------GKPIfVDWQGRVCCGYVDPNDPDVdirianpetgeeikesgkEGEI 900
Cdd:cd17644    256 NV----YGPTEATIAATVcrltQLTErnitsvpiGRPI-ANTQVYILDENLQPVPVGV------------------PGEL 312

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402  901 WISSSSAGIGYWGREELSQKTF-KNELPDYPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKT 973
Cdd:cd17644    313 HIGGVGLARGYLNRPELTAEKFiSHPFNSSESeRLY-KTGDLARYLpDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1586-1671 1.28e-06

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: 49.38  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1586 EVGKHCSIRAINPVSCPKQISIGAGVHLGDFSRIISGFYS--------STGFISGKVEVQENSVIGSQSLILPNSVVQKD 1657
Cdd:cd04647      3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                           90
                   ....*....|....*...
gi 2130317402 1658 VILGALSVA----PAHSV 1671
Cdd:cd04647     83 AVVGAGSVVtkdvPPNSI 100
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 23-59 1.30e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 53.64  E-value: 1.30e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSG 59
Cdd:PRK11749   142 KVAVIGAGPAGLTAAHRLARKGYD-VTIFEARDKAGG 177
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
677-843 1.36e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 54.20  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLF-SPMTF 755
Cdd:PRK06814   793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYpSPLHY 872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  756 IKNPLLWLETmskyQATHSAGPNFaFelmlrrLESDKSTARNYDLSSMIFLMVAAEPVRQITLKRFIEltlPFGLSqevM 835
Cdd:PRK06814   873 RIIPELIYDT----NATILFGTDT-F------LNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWME---KFGIR---I 935


                   ....*...
gi 2130317402  836 APGYGLAE 843
Cdd:PRK06814   936 LEGYGVTE 943
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 836-1065 1.37e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 53.84  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  836 APGYGLAENCVFVsCAYGQGKpiFvdWQGRVCCGYVDPNdpdVDIRIANPETGEeikesgkegeIWISSSSAGIGYWGRE 915
Cdd:PRK07445   258 APTYGMTETASQI-ATLKPDD--F--LAGNNSSGQVLPH---AQITIPANQTGN----------ITIQAQSLALGYYPQI 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  916 ELSQKTFKnelpdypgriytrTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEkTVESSSELLRPGCcaVVGVPEE 994
Cdd:PRK07445   320 LDSQGIFE-------------TDDLGYLDaQGYLHILGRNSQKIITGGENVYPAEVE-AAILATGLVQDVC--VLGLPDP 383

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  995 vlstkgisvsdssdQVGLVVIAEVRDAKTVDKevVEKIKTRVAEEhgvtVASVKL----IKPRTISKTTSGKIKR 1065
Cdd:PRK07445   384 --------------HWGEVVTAIYVPKDPSIS--LEELKTAIKDQ----LSPFKQpkhwIPVPQLPRNPQGKINR 438
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 677-1037 1.46e-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: 53.15  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLcFLQFTSGSTGDAKGVMITH--------GGLIH------NVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGlfTALV 742
Cdd:cd05924      4 DDL-YILYTGGTTGMPKGVMWRQedifrmlmGGADFgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTA--FGGL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  743 SGGSSVLFSPMTFikNPLLWLETMSKYQATHSAgpnFAFELMLRRLESDKSTARNYDLSSMIFLMVAAEP----VRQITL 818
Cdd:cd05924     81 LGGQTVVLPDDRF--DPEEVWRTIEKHKVTSMT---IVGDAMARPLIDALRDAGPYDLSSLFAISSGGALlspeVKQGLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  819 KRFIELTLPFGL-SQEVMAPGYGlaencvfVSCAYGQGKPIFVDWQGRVCcgyvdpndpdvdirIANPETGEEIKESGKE 897
Cdd:cd05924    156 ELVPNITLVDAFgSSETGFTGSG-------HSAGSGPETGPFTRANPDTV--------------VLDDDGRVVPPGSGGV 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GeiWISSSS-AGIGYWGREELSQKTFknelPDYPGRIYTRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVE 975
Cdd:cd05924    215 G--WIARRGhIPLGYYGDEAKTAETF----PEVDGVRYAVPGDRATVEaDGTVTLLGRGSVCINTGGEKVFPEEVEEALK 288

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  976 SssellRPGC--CAVVGVPEEVLSTKgisvsdssdqvgLVVIAEVRDAKTVD-KEVVEKIKTRVA 1037
Cdd:cd05924    289 S-----HPAVydVLVVGRPDERWGQE------------VVAVVQLREGAGVDlEELREHCRTRIA 336
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
677-753 1.57e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 53.95  E-value: 1.57e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVLF-SPM 753
Cdd:PRK08043   365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPL 442
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 677-976 2.06e-06

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: 53.09  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLihnVKLMQRRYRSTSNTILVSWL---PQYHDMGlIGGLFTALVSGGSSVLfspm 753
Cdd:cd12115    105 DDLAYVIYTSGSTGRPKGVAIEHRNA---AAFLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVVL---- 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 tfIKNPLLWLETMSKYQATH-SAGPNFAFELMlrRLESDKSTARNYDLssmiflmvAAEPVRQITLKRFIELtlpfgLSQ 832
Cdd:cd12115    177 --ADNVLALPDLPAAAEVTLiNTVPSAAAELL--RHDALPASVRVVNL--------AGEPLPRDLVQRLYAR-----LQV 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 EVMAPGYGLAEncvfvSCAYGQGKPIFVDWQGRVCCGYVDPND-PDVDIRIANPETgeeikeSGKEGEIWISSSSAGIGY 911
Cdd:cd12115    240 ERVVNLYGPSE-----DTTYSTVAPVPPGASGEVSIGRPLANTqAYVLDRALQPVP------LGVPGELYIGGAGVARGY 308

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  912 WGREELSQKTFkneLPD--YPG-RIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVES 976
Cdd:cd12115    309 LGRPGLTAERF---LPDpfGPGaRLY-RTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRS 373
PRK05691 PRK05691
peptide synthase; Validated
 651-971 2.78e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 53.63  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  651 LHTDSWIKYSKNLQAENkadsaepetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHD 730
Cdd:PRK05691  1256 LHLDSWPSQAPGLHLHG---------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD 1326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  731 MGlIGGLFTALVSGGSSVLFSPMTFiKNPLLWLETMSKYQAT--HSAGPnfafelmLRRLESDKSTARNydLSSMIFLMV 808
Cdd:PRK05691  1327 VS-VWECFWPLITGCRLVLAGPGEH-RDPQRIAELVQQYGVTtlHFVPP-------LLQLFIDEPLAAA--CTSLRRLFS 1395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  809 AAEPVRQITLKRFIELtlpfgLSQEVMAPGYGLAENCVFVS---C--AYGQGKPIfvdwqGR----VCCgyvdpndpdvd 879
Cdd:PRK05691  1396 GGEALPAELRNRVLQR-----LPQVQLHNRYGPTETAINVThwqCqaEDGERSPI-----GRplgnVLC----------- 1454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  880 iRIANPETgeEIKESGKEGEIWISSSSAGIGYWGREELSQKTFkneLPDYPG----RIYtRTGDLGRI-IDGKLFITGRI 954
Cdd:PRK05691  1455 -RVLDAEL--NLLPPGVAGELCIGGAGLARGYLGRPALTAERF---VPDPLGedgaRLY-RTGDRARWnADGALEYLGRL 1527

                          330
                   ....*....|....*..
gi 2130317402  955 KDLIIVAGRNIYSADIE 971
Cdd:PRK05691  1528 DQQVKLRGFRVEPEEIQ 1544
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 21-103 3.30e-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: 51.86  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSG-------MCESVEIegkMYDLG-GQVLAANSAPV----IFD 88
Cdd:COG0654      3 RTDVLIVGGGPAGLALALALARAGIR-VTVVERAPPPRPdgrgialSPRSLEL---LRRLGlWDRLLARGAPIrgirVRD 78

                           90
                   ....*....|....*
gi 2130317402   89 laKETGSELEEMDAH 103
Cdd:COG0654     79 --GSDGRVLARFDAA 91
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 675-974 3.64e-06

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: 52.48  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLmQRRY--RSTSNTIL----VSWLPQYHDmgliggLFTALVSGGSSV 748
Cdd:cd17656    126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF-EREKtnINFSDKVLqfatCSFDVCYQE------IFSTLLSGGTLY 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LFSpmtfiKNPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKSTARnyDLSSMIFLMVAAEPVRQITlKRFIELTLPF 828
Cdd:cd17656    199 IIR-----EETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFIN--RFPTCVKHIITAGEQLVIT-NEFKEMLHEH 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  829 GLSqevMAPGYGLAENCVFVSCAYGQGKPIfvdwqgrvccgyvdPNDP-------DVDIRIANPEtgEEIKESGKEGEIW 901
Cdd:cd17656    271 NVH---LHNHYGPSETHVVTTYTINPEAEI--------------PELPpigkpisNTWIYILDQE--QQLQPQGIVGELY 331

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130317402  902 ISSSSAGIGYWGREELSQKTFKNELPDYPGRIYtRTGDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTV 974
Cdd:cd17656    332 ISGASVARGYLNRQELTAEKFFPDPFDPNERMY-RTGDLARYLpDGNIEFLGRADHQVKIRGYRIELGEIEAQL 404
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 681-1065 4.54e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 52.44  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  681 FLQFTSGSTGDAKGVMITHGGlihNVKLMQRRYRSTSNTILVSWLPQYHDMGLI---GGLFTALVSGGSSVLFSpMTFIK 757
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSLSLGNTFVMFE-GGIIK 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  758 NPL----LWlETMSKYQATHSagpnFAFELMLRRLESDKSTARN----YDLSSMIFLMVAAEPVRQiTLKRFIELTLPFG 829
Cdd:PTZ00237   334 NKHieddLW-NTIEKHKVTHT----LTLPKTIRYLIKTDPEATIirskYDLSNLKEIWCGGEVIEE-SIPEYIENKLKIK 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  830 LSQevmapGYGLAE-NCVFVSCAYGQGKPIFVdwqgrvcCGYvdpndPDVDIR--IANPEtGEEIKESgKEGEIWIS--- 903
Cdd:PTZ00237   408 SSR-----GYGQTEiGITYLYCYGHINIPYNA-------TGV-----PSIFIKpsILSED-GKELNVN-EIGEVAFKlpm 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  904 SSSAGIGYWGREELsqktFKNELPDYPGriYTRTGDLGRIIDGKLF-ITGRIKDLIIVAGRNIYSADIEKTVESSSELLR 982
Cdd:PTZ00237   469 PPSFATTFYKNDEK----FKQLFSKFPG--YYNSGDLGFKDENGYYtIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  983 pgCCAVvgvpeevlstkGISVSDSSDQ-VGLVVIAEVRDAKTVD----KEVVEKIKTRVAEEHgvTVASVKLIKPRtISK 1057
Cdd:PTZ00237   543 --CCSI-----------GIYDPDCYNVpIGLLVLKQDQSNQSIDlnklKNEINNIITQDIESL--AVLRKIIIVNQ-LPK 606


                   ....*...
gi 2130317402 1058 TTSGKIKR 1065
Cdd:PTZ00237   607 TKTGKIPR 614
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 663-954 4.78e-06

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: 52.05  E-value: 4.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  663 LQAENKADSAEPetDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQ--RRYRSTSNTILVSWLPQYHDMGLIGGLFTA 740
Cdd:cd05921    153 AAVDAAFAAVGP--DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqtYPFFGEEPPVLVDWLPWNHTFGGNHNFNLV 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  741 LVSGGSSVLFS--PM-----TFIKNpllWLETMSKYQATHSAGpnfaFELMLRRLESDKSTARNYdLSSMIFLMVAAEPV 813
Cdd:cd05921    231 LYNGGTLYIDDgkPMpggfeETLRN---LREISPTVYFNVPAG----WEMLVAALEKDEALRRRF-FKRLKLMFYAGAGL 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  814 RQITLKRFIELTLPFGLSQEVMAPGYGLAENcvfvscaygqgkpifvdwqGRVCCGYVDPNDPDVDIRIanPETGEEIK- 892
Cdd:cd05921    303 SQDVWDRLQALAVATVGERIPMMAGLGATET-------------------APTATFTHWPTERSGLIGL--PAPGTELKl 361

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  893 -ESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYTRTGDLGRIIDGK-----LFITGRI 954
Cdd:cd05921    362 vPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEE-----G--FYCLGDAAKLADPDdpakgLVFDGRV 422
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
897-1080 5.05e-06

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 52.09  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  897 EGEIWISSSSAGIGYW----GREELSQKTFKNELPDYPGRIYT-----RTGDLGRII-DGKLFITGRIKDLIIVAGRNIY 966
Cdd:PRK05620   385 EGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFTadgwlRTGDVGSVTrDGFLTIHDRARDVIRSGGEWIY 464

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  967 SADIEKTVESSSELLRpgcCAVVGVPEEVLSTKGISVSdssdqvglVVIAEVRDAKTVDKEVVEKIKTRV----AEEHGV 1042
Cdd:PRK05620   465 SAQLENYIMAAPEVVE---CAVIGYPDDKWGERPLAVT--------VLAPGIEPTRETAERLRDQLRDRLpnwmLPEYWT 533

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2130317402 1043 TVASvklikprtISKTTSGKIKRFECLKQFVDGTLNIV 1080
Cdd:PRK05620   534 FVDE--------IDKTSVGKFDKKDLRQHLADGDFEII 563
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 677-947 6.21e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 51.77  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNV----KLMQRRYRS-TSNTILVSWLPQYHDMGLIGGlfTALVSGGSSVLF- 750
Cdd:PLN02861   220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVlstdHLLKVTDRVaTEEDSYFSYLPLAHVYDQVIE--TYCISKGASIGFw 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  751 --------------SPMTFIKNPLLWLETMSKYQATHSAGP-------NFAFELMLRRLE----SDKSTARnydLSSMIF 805
Cdd:PLN02861   298 qgdirylmedvqalKPTIFCGVPRVYDRIYTGIMQKISSGGmlrkklfDFAYNYKLGNLRkglkQEEASPR---LDRLVF 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  806 -------------LMVAAEPV-RQItlKRFIELTlpfglSQEVMAPGYGLAENCVFVSCAYGQGKPIFvdwqgrvccGYV 871
Cdd:PLN02861   375 dkikeglggrvrlLLSGAAPLpRHV--EEFLRVT-----SCSVLSQGYGLTESCGGCFTSIANVFSMV---------GTV 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  872 DPNDPDVDIRIAN-PETGEEIKESGKEGEIWISSSSAGIGYWGREELSQKTFKNElpdypgriYTRTGDLG--------R 942
Cdd:PLN02861   439 GVPMTTIEARLESvPEMGYDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDG--------WFHTGDIGewqpngamK 510


                   ....*
gi 2130317402  943 IIDGK 947
Cdd:PLN02861   511 IIDRK 515
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 684-994 6.67e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 51.54  E-value: 6.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  684 FTSGSTGDAKGVM---ITHGGLIHNVKLMQRRYRSTSNTILVSwLPQYHDMGLigGLFTALVSGGSSVLfSPMTFIKNPL 760
Cdd:PRK13383   181 LTSGTTGKPKGVPrapQLRSAVGVWVTILDRTRLRTGSRISVA-MPMFHGLGL--GMLMLTIALGGTVL-THRHFDAEAA 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  761 LWLETMskyqatHSAGPNFAFELMLRRLES--DKSTARNyDLSSMIFLMVAAEPVRQITLKRFIEltlPFGlsqEVMAPG 838
Cdd:PRK13383   257 LAQASL------HRADAFTAVPVVLARILElpPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMD---TYG---DILYNG 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  839 YGLAEncvfVSCAYGQGKPIFVDWQ---GRVCCG----YVDPNDPDVDIRIAnpetgeeikesgkeGEIWISSSSAGIGY 911
Cdd:PRK13383   324 YGSTE----VGIGALATPADLRDAPetvGKPVAGcpvrILDRNNRPVGPRVT--------------GRIFVGGELAGTRY 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 WGReelSQKTFKNELpdypgriyTRTGDLGRIID-GKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRPgccAVVG 990
Cdd:PRK13383   386 TDG---GGKAVVDGM--------TSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN---AVIG 451


                   ....
gi 2130317402  991 VPEE 994
Cdd:PRK13383   452 VPDE 455
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 660-972 8.27e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 51.03  E-value: 8.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  660 SKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK----LMQRryrSTSNTILVSwLPQYHDMGLiG 735
Cdd:PRK09029   118 SLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEgvlsLMPF---TAQDSWLLS-LPLFHVSGQ-G 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  736 GLFTALVSGGSSVLFSPMTFiknpllwletmskYQA----TH-SAGPNfafelMLRRLESDKSTArnydLSSMIFL---- 806
Cdd:PRK09029   193 IVWRWLYAGATLVVRDKQPL-------------EQAlagcTHaSLVPT-----QLWRLLDNRSEP----LSLKAVLlgga 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  807 MVAAEPVRQITlKRFIELTLpfglsqevmapGYGLAEncvFVS--CAY------GQGKPIfvdwQGRvccgyvdpndpdv 878
Cdd:PRK09029   251 AIPVELTEQAE-QQGIRCWC-----------GYGLTE---MAStvCAKradglaGVGSPL----PGR------------- 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  879 DIRIANpetgeeikesgkeGEIWISSSSAGIGYWGREELsqktfkNELPDYPGRIYTRtgDLGRIIDGKLFITGRIKDLI 958
Cdd:PRK09029   299 EVKLVD-------------GEIWLRGASLALGYWRQGQL------VPLVNDEGWFATR--DRGEWQNGELTILGRLDNLF 357

                          330
                   ....*....|....
gi 2130317402  959 IVAGRNIYSADIEK 972
Cdd:PRK09029   358 FSGGEGIQPEEIER 371
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 1584-1681 9.57e-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: 49.02  E-value: 9.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSI--RAInpvscpkqisIGAGVHLGDFSRIisgfysSTG-FISGKVEVQENSVIGSQSLILPNSVVQKDVIL 1660
Cdd:cd03360    114 DARIGDNVIIntGAV----------IGHDCVIGDFVHI------APGvVLSGGVTIGEGAFIGAGATIIQGVTIGAGAII 177

                           90       100
                   ....*....|....*....|....
gi 2130317402 1661 GALSVapahsVLQ---QGGVYVGS 1681
Cdd:cd03360    178 GAGAV-----VTKdvpDGSVVVGN 196
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 912-1065 1.12e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 50.91  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  912 WGREELSQKTFkneLPDYPGRIYTrtGDlGRIID--GKLFITGRIKDLIIVAGRNIYSADIEKTV---ESSSEllrpgcC 986
Cdd:PRK00174   467 YGDHERFVKTY---FSTFKGMYFT--GD-GARRDedGYYWITGRVDDVLNVSGHRLGTAEIESALvahPKVAE------A 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  987 AVVGVPEEVlstKGISVsdssdqVGLVVIaevRDAKTVDKEVVEKIKTRVAEEHGvtvasvKLIKPRTIS------KTTS 1060
Cdd:PRK00174   535 AVVGRPDDI---KGQGI------YAFVTL---KGGEEPSDELRKELRNWVRKEIG------PIAKPDVIQfapglpKTRS 596


                   ....*
gi 2130317402 1061 GKIKR 1065
Cdd:PRK00174   597 GKIMR 601
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 21-74 1.40e-05

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 50.62  E-value: 1.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEGKMYDLG 74
Cdd:COG1233      3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTFERPGFRFDVG 55
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 2612-2850 1.71e-05

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 50.28  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2612 DDGVGSVSSKDDRRSQSLDVEpVSSLRNATSRSVQDREQQDKKRRRKGPREKPS----RADQHPYMSVNEHPQDEPRqil 2687
Cdd:TIGR01642   68 YSSVRRSRDRPRRRSRSVRSI-EQHRRRLRDRSPSNQWRKDDKKRSLWDIKPPGyelvTADQAKASQVFSVPGTAPR--- 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2688 PDINNTDVPLIDYNMHG----NQLENNTATALRSL--ERVPEGQSQIAASDF--KQFSTVA-----PANVISTQSTYMDG 2754
Cdd:TIGR01642  144 PAMTDPEKLLAEGSIITplpvLPYQQQATRQARRLyvGGIPPEFVEEAVVDFfnDLMIATGyhkaeDGKHVSSVNINKEK 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2755 RPMLYPM--VQNTELH---DGATYNlyNPSLEFGHSHDGQDS-QMDMNVSQVRPEDGVHVPALRRN-------ENEITNG 2821
Cdd:TIGR01642  224 NFAFLEFrtVEEATFAmalDSIIYS--NVFLKIRRPHDYIPVpQITPEVSQKNPDDNAKNVEKLVNsttvldsKDRIYIG 301

                          250       260
                   ....*....|....*....|....*....
gi 2130317402 2822 DLHHYMKDtfpsDQDRPVDNQFGsPLGSF 2850
Cdd:TIGR01642  302 NLPLYLGE----DQIKELLESFG-DLKAF 325
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
2218-2289 2.24e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.79  E-value: 2.24e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402 2218 VLNPEMVEIERGGCVGREALLFGHIYEGDD---GKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMK 2289
Cdd:COG0110     42 IDDPGGITIGDNVLIGPGVTILTGNHPIDDpatFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTK 116
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 684-954 2.31e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 50.04  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  684 FTSGSTGDAKGVMITHGGLIHNVKLMQ---RRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSsvLF----SPMtfi 756
Cdd:PRK12582   227 FTSGSTGMPKAVINTQRMMCANIAMQEqlrPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGT--LYiddgKPL--- 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  757 knPLLWLETMskyQATHSAGPNF------AFELMLRRLESDKSTARNYdLSSMIFLMVAAEPVRQITLKRFIELTLPFGL 830
Cdd:PRK12582   302 --PGMFEETI---RNLREISPTVygnvpaGYAMLAEAMEKDDALRRSF-FKNLRLMAYGGATLSDDLYERMQALAVRTTG 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  831 SQEVMAPGYGLAENcvfvscaygQGKPIFVDWqgrvccgyvdpnDPDVDIRIANPETGEEIK--ESGKEGEIWISSSSAG 908
Cdd:PRK12582   376 HRIPFYTGYGATET---------APTTTGTHW------------DTERVGLIGLPLPGVELKlaPVGDKYEVRVKGPNVT 434

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130317402  909 IGYWGREELSQKTFKNElpdypGriYTRTGDLGRIIDGK-----LFITGRI 954
Cdd:PRK12582   435 PGYHKDPELTAAAFDEE-----G--FYRLGDAARFVDPDdpekgLIFDGRV 478
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 13-60 2.69e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.87  E-value: 2.69e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2130317402   13 KLHPCLPVT-TRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGM 60
Cdd:PRK12771   128 KFPAPAPDTgKRVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGM 175
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1584-1681 2.83e-05

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: 46.64  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSIRA-INPvscpkqISIGAGVHLGDFSRIisgfYSSTGF---ISGKV-----------EVQENSVIGSQSLI 1648
Cdd:cd04645     23 GSSVWFGAVLRGdVNP------IRIGERTNIQDGSVL----HVDPGYptiIGDNVtvghgavlhgcTIGDNCLIGMGAII 92

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2130317402 1649 LPNSVVQKDVILGALSVAPAHSVLQQGGVYVGS 1681
Cdd:cd04645     93 LDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 655-729 2.92e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 49.81  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  655 SWIKYSKnLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVK-----LMQRRYRSTSNTILVSWLPQYH 729
Cdd:PLN02430   199 SWIDFLH-MGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlfMEQFEDKMTHDDVYLSFLPLAH 277
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 1379-1439 3.40e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 46.81  E-value: 3.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130317402 1379 VSIGDGAVIAEGVLVQGhevrngvlsflPIRIGRNSSVGPFAVIQKGSIIGDEADAGAAVQ 1439
Cdd:cd05636     18 VWIGEGAIVRSGAYIEG-----------PVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVE 67
prpE PRK10524
propionyl-CoA synthetase; Provisional
 670-1065 3.73e-05

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 49.18  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  670 DSAEPEtddlcFLQFTSGSTGDAKGVMITHGGliHNVKLMQ-----------RRYRSTSntilvswlpqyhDMGLIGG-- 736
Cdd:PRK10524   231 ESNEPS-----YILYTSGTTGKPKGVQRDTGG--YAVALATsmdtifggkagETFFCAS------------DIGWVVGhs 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  737 --LFTALVSGGSSVLFSPMTFIKNPLLWLETMSKYQATHSagpnFAFELMLRRLE-SDKSTARNYDLSSMIFLMVAAEPV 813
Cdd:PRK10524   292 yiVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRM----FSAPTAIRVLKkQDPALLRKHDLSSLRALFLAGEPL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  814 RQITlKRFIELTLpfglsqevmapgyglaencvfvscaygqGKPIfVD--WQ------------------------GRVC 867
Cdd:PRK10524   368 DEPT-ASWISEAL----------------------------GVPV-IDnyWQtetgwpilaiargvedrptrlgspGVPM 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  868 CGYvdpndpdvDIRIANPETGEEIkESGKEGEIWIssssagigywgreelsqktfknELPDYPGRIYTRTGDLGRII--- 944
Cdd:PRK10524   418 YGY--------NVKLLNEVTGEPC-GPNEKGVLVI----------------------EGPLPPGCMQTVWGDDDRFVkty 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  945 -------------------DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVlstKGisvsd 1005
Cdd:PRK10524   467 wslfgrqvystfdwgirdaDGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE---VAVVGVKDAL---KG----- 535

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1006 ssdQVGlVVIAEVRDAKTVDKE------------VVEKIKTRVAEEHGVTVASVklikprtISKTTSGKIKR 1065
Cdd:PRK10524   536 ---QVA-VAFVVPKDSDSLADRearlalekeimaLVDSQLGAVARPARVWFVSA-------LPKTRSGKLLR 596
PLN02654 PLN02654
acetate-CoA ligase
 675-1065 4.30e-05

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 49.13  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  675 ETDDLCFLQFTSGSTGDAKGVMITHGG-LIHNVKLMQRR--YRSTSntilVSWLPQyhDMGLIGG----LFTALVSGGSS 747
Cdd:PLN02654   273 DAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAfdYKPTD----VYWCTA--DCGWITGhsyvTYGPMLNGATV 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 VLFSPMTFIKNPLLWLETMSKYQAT-HSAGPNFAFELMLrrlESDKSTARnYDLSSMIFLMVAAEPVRQITLKRFIELTl 826
Cdd:PLN02654   347 LVFEGAPNYPDSGRCWDIVDKYKVTiFYTAPTLVRSLMR---DGDEYVTR-HSRKSLRVLGSVGEPINPSAWRWFFNVV- 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 pfGLSQEVMAPGYGLAENCVF----VSCAYGQgKPifvdwqGRVCCGYVDPNDPDVDirianpETGEEIkESGKEGEIWI 902
Cdd:PLN02654   422 --GDSRCPISDTWWQTETGGFmitpLPGAWPQ-KP------GSATFPFFGVQPVIVD------EKGKEI-EGECSGYLCV 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  903 SSSSAGI--GYWGREELSQKTFkneLPDYPGriYTRTGD-LGRIIDGKLFITGRIKDLIIVAGRNIYSADIEktvesSSE 979
Cdd:PLN02654   486 KKSWPGAfrTLYGDHERYETTY---FKPFAG--YYFSGDgCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE-----SAL 555

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  980 LLRPGC--CAVVGVPEEVlstKGisvsdssdqVGLVVIAEVRDAKTVDKEVVEKIKTRVAEEHGVTVASVKLIKPRTISK 1057
Cdd:PLN02654   556 VSHPQCaeAAVVGIEHEV---KG---------QGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623


                   ....*...
gi 2130317402 1058 TTSGKIKR 1065
Cdd:PLN02654   624 TRSGKIMR 631
PLN03000 PLN03000
amine oxidase
 3-97 4.42e-05

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 49.25  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402    3 LGKSIGDQFsklhPCLPVTTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIE----GKMYDLGGQVL 78
Cdd:PLN03000   170 IAQAIKDKF----PAQSSKSSVVIVGAGLSGLAAARQLMRFGFK-VTVLEGRKRPGGRVYTKKMEanrvGAAADLGGSVL 244

                           90
                   ....*....|....*....
gi 2130317402   79 AANSAPVIFDLAKETGSEL 97
Cdd:PLN03000   245 TGTLGNPLGIIARQLGSSL 263
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 21-96 7.11e-05

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: 48.29  E-value: 7.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYR---NVTVLEKFHTVSGMCESVEIEGKMYDLGGQVLAANSaPVIFDLAKETGSE 96
Cdd:TIGR00562    2 KKHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLGLE 79
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 677-957 7.18e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.43  E-value: 7.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRS-----TSNTILVSWLPQYHDMGL-IGGLFTA---LVSGGSS 747
Cdd:PTZ00216   264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligppEEDETYCSYLPLAHIMEFgVTNIFLArgaLIGFGSP 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 --------------VLFSPMTFIKNPLLWlETMSKyqATHSAGP----------NFAFELMLRRLESDKST--------- 794
Cdd:PTZ00216   344 rtltdtfarphgdlTEFRPVFLIGVPRIF-DTIKK--AVEAKLPpvgslkrrvfDHAYQSRLRALKEGKDTpywnekvfs 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  795 -ARnYDLSSMIFLMVAA-EPVRQITlKRFIELTlpFGLsqevMAPGYGLAENcvfvscaygqgkpifvdwqgrVCC---- 868
Cdd:PTZ00216   421 aPR-AVLGGRVRAMLSGgGPLSAAT-QEFVNVV--FGM----VIQGWGLTET---------------------VCCggiq 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  869 --GYVDPNDpdvdirIANPETGEEIK----ESGK-------EGEIWISSSSAGIGYWGREELSQKTFKNElpdypGriYT 935
Cdd:PTZ00216   472 rtGDLEPNA------VGQLLKGVEMKlldtEEYKhtdtpepRGEILLRGPFLFKGYYKQEELTREVLDED-----G--WF 538

                          330       340
                   ....*....|....*....|...
gi 2130317402  936 RTGDLGRI-IDGKLFITGRIKDL 957
Cdd:PTZ00216   539 HTGDVGSIaANGTLRIIGRVKAL 561
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 682-1067 7.18e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 48.40  E-value: 7.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  682 LQFTSGSTGDAKGVMITHGGLIHNvklmqrryrSTSNTIlvSW-----------LPQYHdmgLIGGLF--TALVSGGSSV 748
Cdd:PRK08162   187 LNYTSGTTGNPKGVVYHHRGAYLN---------ALSNIL--AWgmpkhpvylwtLPMFH---CNGWCFpwTVAARAGTNV 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  749 LFSPMTfiknPLLWLETMSKYQATHSAGPNFAFELMLRRLESDKStARNYDLSSMIflMVAAEPVRQI--TLKRFIELTL 826
Cdd:PRK08162   253 CLRKVD----PKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRA-GIDHPVHAMV--AGAAPPAAVIakMEEIGFDLTH 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  827 PFGLSqEVmapgYGLAencvfVSCAYGQG---KPI-----FVDWQGrVCCGYVDpndpdvDIRIANPETGEEIKESGKE- 897
Cdd:PRK08162   326 VYGLT-ET----YGPA-----TVCAWQPEwdaLPLderaqLKARQG-VRYPLQE------GVTVLDPDTMQPVPADGETi 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  898 GEIWISSSSAGIGYWGREELSQKTFKNelpdypGRIYTrtGDLG-RIIDGKLFITGRIKDLIIVAGRNIYSADIEKTves 976
Cdd:PRK08162   389 GEIMFRGNIVMKGYLKNPKATEEAFAG------GWFHT--GDLAvLHPDGYIKIKDRSKDIIISGGENISSIEVEDV--- 457

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  977 sseLLR-PGC--CAVVGVPEEvlstkgisvsdssdQVGLVVIA--EVRDAKTVDK-EVVEKIKTRVAeehGVTVAsvKLI 1050
Cdd:PRK08162   458 ---LYRhPAVlvAAVVAKPDP--------------KWGEVPCAfvELKDGASATEeEIIAHCREHLA---GFKVP--KAV 515

                          410
                   ....*....|....*..
gi 2130317402 1051 KPRTISKTTSGKIKRFE 1067
Cdd:PRK08162   516 VFGELPKTSTGKIQKFV 532
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 669-747 8.68e-05

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: 48.22  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  669 ADSAEPETDDLCFLQFTSGSTGDAKGVMITHggliHNVKLMQRRYRST-----SNTILVSWLPQYHDMGLIgGLFTALVS 743
Cdd:cd17632    215 LFRPEPDDDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIqdirpPASITLNFMPMSHIAGRI-SLYGTLAR 289


                   ....
gi 2130317402  744 GGSS 747
Cdd:cd17632    290 GGTA 293
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 684-994 9.53e-05

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 47.85  E-value: 9.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  684 FTSGSTGDAKGVMITHGGLIHNVKLMQRRYR-STSNTILVSWLPQYHDMGLiGGLFTALVSGGSSVLFSPMTFikNPLLW 762
Cdd:PRK07786   181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGaDINSDVGFVGVPLFHIAGI-GSMLPGLLLGAPTVIYPLGAF--DPGQL 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  763 LETMSKYQATHSagpnFAFELMLRRLESDKsTARNYDLSsMIFLMVAAEPVRQITLKRFIElTLP-------FGlsQEVM 835
Cdd:PRK07786   258 LDVLEAEKVTGI----FLVPAQWQAVCAEQ-QARPRDLA-LRVLSWGAAPASDTLLRQMAA-TFPeaqilaaFG--QTEM 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  836 APgyglaencvfVSCAY-GQ---------GKPIfVDWQGRVccgyVDPNDPDVDIrianpetgeeikesGKEGEIWISSS 905
Cdd:PRK07786   329 SP----------VTCMLlGEdairklgsvGKVI-PTVAARV----VDENMNDVPV--------------GEVGEIVYRAP 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  906 SAGIGYWGREELSQKTFKNElpdypgriYTRTGDLGRI-IDGKLFITGRIKDLIIVAGRNIYSADIEKTVESSSELLRpg 984
Cdd:PRK07786   380 TLMSGYWNNPEATAEAFAGG--------WFHSGDLVRQdEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVE-- 449

                          330
                   ....*....|
gi 2130317402  985 cCAVVGVPEE 994
Cdd:PRK07786   450 -VAVIGRADE 458
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1379-1438 1.40e-04

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: 44.71  E-value: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1379 VSIGDGAVIAEGVLVQGHEVRNGVLsflpirIGRNSSVGPFAVIQKGSIIGdeadAGAAV 1438
Cdd:cd04645     61 TIIGDNVTVGHGAVLHGCTIGDNCL------IGMGAIILDGAVIGKGSIVA----AGSLV 110
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 2219-2312 2.19e-04

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 42.98  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 2219 LNPEMVEIERGGCVGREALLFG--HIYEGDDGKVKFGKIRIGEGGFVGSRAVAMPGVRVETGGSLAALSLAMKeeivkss 2296
Cdd:cd05825     19 YNLAPVTIGSDACISQGAYLCTgsHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVR------- 91

                           90
                   ....*....|....*.
gi 2130317402 2297 sDIEVDDIRCGNIAEK 2312
Cdd:cd05825     92 -DLPAWTVYAGNPAVP 106
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 26-53 2.42e-04

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: 46.39  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*...
gi 2130317402   26 IVGAGPSGLSAAYALTKLGyRNVTVLEK 53
Cdd:COG2072     11 VIGAGQAGLAAAYHLRRAG-IDFVVLEK 37
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1585-1681 2.50e-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: 44.71  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1585 AEVGKHCSIRAinpvscpkQISIGAGVHLGDFSRIISGfysstgfisgkVEVQENSVIGSQSLILPNSVVQKDVILGals 1664
Cdd:cd03352      2 AKIGENVSIGP--------NAVIGEGVVIGDGVVIGPG-----------VVIGDGVVIGDDCVIHPNVTIYEGCIIG--- 59

                           90
                   ....*....|....*..
gi 2130317402 1665 vapAHSVLQQGGVyVGS 1681
Cdd:cd03352     60 ---DRVIIHSGAV-IGS 72
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1373-1430 2.77e-04

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: 42.44  E-value: 2.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130317402 1373 ITDPSLVSIGDGAVIAEGVLVQGH--------EVRNGVLSFLPIRIGRNSSVGPFAVIQKGSIIGD 1430
Cdd:cd04647     16 ISAGGGITIGDNVLIGPNVTIYDHnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
23-53 2.84e-04

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 46.26  E-value: 2.84e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEK 53
Cdd:COG2509     32 DVVIVGAGPAGLFAALELAEAGLK-PLVLER 61
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 16-60 2.93e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 46.26  E-value: 2.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2130317402   16 PCLPVT-TRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGM 60
Cdd:PRK12814   187 ERAPKSgKKVAIIGAGPAGLTAAYYLLRKGHD-VTIFDANEQAGGM 231
PRK13984 PRK13984
putative oxidoreductase; Provisional
 16-60 3.16e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 46.30  E-value: 3.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2130317402   16 PCLPVTTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGM 60
Cdd:PRK13984   278 EPEKKNKKVAIVGSGPAGLSAAYFLATMGYE-VTVYESLSKPGGV 321
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 22-81 3.17e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 45.78  E-value: 3.17e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   22 TRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKfHTVSGMCESveiegkmYDLGGQVLAAN 81
Cdd:PRK12409     2 SHIAVIGAGITGVTTAYALAQRGYQ-VTVFDR-HRYAAMETS-------FANGGQLSASN 52
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1377-1438 3.23e-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: 41.47  E-value: 3.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402 1377 SLVSIGDGAVIAEGVLVQGHEVRNGVL---SFLPIRIGRNSSVGPFAVIQKGSIIGDEA--DAGAAV 1438
Cdd:cd00208     11 PKAVIRGPVVIGDNVNIGPGAVIGAATgpnEKNPTIIGDNVEIGANAVIHGGVKIGDNAviGAGAVV 77
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 21-96 3.59e-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: 46.00  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSGMCESVEIEgkmyDLG-----GQ--VLAANSApvIFDLAKET 93
Cdd:COG3349      3 PPRVVVVGGGLAGLAAAVELAEAGFR-VTLLEARPRLGGRARSFPDP----DTGlpidnGQhvLLGCYRN--TLDLLRRI 75


                   ...
gi 2130317402   94 GSE 96
Cdd:COG3349     76 GAA 78
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
643-1189 3.69e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 46.19  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  643 GRWPNLPWLHTDSwikYSKNLQAENKADSAEPETDDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILV 722
Cdd:PRK10252   567 PRFADVPDLTSLC---YNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVL 643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  723 SWLPQYHDMGlIGGLFTALVSGGSSVLFSPMTFiKNPllwletmskyqathsagpnfafeLMLRRLESDKSTARNYDLSS 802
Cdd:PRK10252   644 QKTPCSFDVS-VWEFFWPFIAGAKLVMAEPEAH-RDP-----------------------LAMQQFFAEYGVTTTHFVPS 698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  803 MIFLMVAAEPVRQI-----TLKRFI---ElTLPFGLSQE----VMAP---GYGLAENCVFVScaygqGKPIFVDWQGRVc 867
Cdd:PRK10252   699 MLAAFVASLTPEGArqscaSLRQVFcsgE-ALPADLCREwqqlTGAPlhnLYGPTEAAVDVS-----WYPAFGEELAAV- 771

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  868 cgyvdPNDPdvdIRIANP--ETGEEIKES-------GKEGEIWISSSSAGIGYWGREELSQKTFKNElPDYPG-RIYtRT 937
Cdd:PRK10252   772 -----RGSS---VPIGYPvwNTGLRILDArmrpvppGVAGDLYLTGIQLAQGYLGRPDLTASRFIAD-PFAPGeRMY-RT 841

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  938 GDLGRII-DGKLFITGRIKDLIIVAGRNIYSADIEKTVESSsellrPGcCAVVGVPEEVLSTKGISVSDSSDQVGLVVIA 1016
Cdd:PRK10252   842 GDVARWLdDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQAL-----PD-VEQAVTHACVINQAAATGGDARQLVGYLVSQ 915

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1017 EVRDAKTVDkevvekIKTRVAE---EHGVTVASVKLikpRTISKTTSGKIKRfeclkqfvdgtlNIVPEPLFKKKTfvrs 1093
Cdd:PRK10252   916 SGLPLDTSA------LQAQLRErlpPHMVPVVLLQL---DQLPLSANGKLDR------------KALPLPELKAQV---- 970

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1094 fttgtcrEGKTPRPQLVSSplpspkmsnkdivefLIRLVSEQTGIPSSNISAtgSLVSYGIDSIGVVRAAQKLSEFLGVP 1173
Cdd:PRK10252   971 -------PGRAPKTGTETI---------------IAAAFSSLLGCDVVDADA--DFFALGGHSLLAMKLAAQLSRQFARQ 1026

                          570
                   ....*....|....*.
gi 2130317402 1174 VGAVDIFTATCISDLA 1189
Cdd:PRK10252  1027 VTPGQVMVASTVAKLA 1042
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 877-1071 3.70e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 45.93  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  877 DVDIRIANpETGEEIkESGKEGEIWISSSSAGIGYWGREELSQKtfknelPDYPGriYTRTGDLGRI-IDGKLFITGRIK 955
Cdd:PRK07638   315 NVQVRICN-EAGEEV-QKGEIGTVYVKSPQFFMGYIIGGVLARE------LNADG--WMTVRDVGYEdEEGFIYIVGREK 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  956 DLIIVAGRNIYSADIEKTVESSSELLRpgcCAVVGVPEEVLSTKGISVSDSSdqvglvviaevrdaktvdkEVVEKIKTR 1035
Cdd:PRK07638   385 NMILFGGINIFPEEIESVLHEHPAVDE---IVVIGVPDSYWGEKPVAIIKGS-------------------ATKQQLKSF 442

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2130317402 1036 VAEEhgvtVASVKLIKP----RTISKTTSGKIKRFECLKQ 1071
Cdd:PRK07638   443 CLQR----LSSFKIPKEwhfvDEIPYTNSGKIARMEAKSW 478
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
20-59 3.79e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 45.67  E-value: 3.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2130317402   20 VTTRIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTVSG 59
Cdd:COG0665      1 ATADVVVIGGGIAGLSTAYHLARRGLD-VTVLERGRPGSG 39
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 23-98 4.50e-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: 45.08  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEKFHTV--------SGMCESVEIEGKMYDLGGqvLAANSAPVIFDLAKETG 94
Cdd:pfam01266    1 DVVVIGGGIVGLSTAYELARRGLS-VTLLERGDDPgsgasgrnAGLIHPGLRYLEPSELAR--LALEALDLWEELEEELG 77


                   ....
gi 2130317402   95 SELE 98
Cdd:pfam01266   78 IDCG 81
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 13-59 8.79e-04

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 45.12  E-value: 8.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2130317402   13 KLHPCLPVTT-----RIGIVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVSG 59
Cdd:PRK12778   418 SGNISVPEVAekngkKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 23-53 8.94e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 44.77  E-value: 8.94e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLEK 53
Cdd:PRK12810   145 KVAVVGSGPAGLAAADQLARAGHK-VTVFER 174
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1124-1191 1.53e-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: 39.93  E-value: 1.53e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130317402  1124 IVEFLIRLVSEQTGIPSSN-ISATGSLVSYGIDSIGVVRAAQKLSEFLGVPVGAVDIFTATCISDLANF 1191
Cdd:smart00823   13 LLDLVREQVAAVLGHAAAEaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 677-971 1.58e-03

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; 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. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 43.96  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  677 DDLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSPM 753
Cdd:cd05937     87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsrkFSAS 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  754 TFiknpllWLETMSKyQATHSAgpnFAFELMLRRLESDKSTarnYDLSSMIfLMVAAEPVRQITLKRFIEltlPFGLSQ- 832
Cdd:cd05937    167 QF------WKDVRDS-GATIIQ---YVGELCRYLLSTPPSP---YDRDHKV-RVAWGNGLRPDIWERFRE---RFNVPEi 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  833 -EVMAPGYGLAENCVFVSCAYGQGKPIFVDWQGRVCCGY------VDPNDPDVdirIANPETG--EEIKeSGKEGE---- 899
Cdd:cd05937    230 gEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENqvvlvkMDPETDDP---IRDPKTGfcVRAP-VGEPGEmlgr 305

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402  900 IWISSSSAGIGYWGREELSQKTFkneLPDY--PGRIYTRTGD-LGRIIDGKLFITGRIKDLIIVAGRNIYSADIE 971
Cdd:cd05937    306 VPFKNREAFQGYLHNEDATESKL---VRDVfrKGDIYFRTGDlLRQDADGRWYFLDRLGDTFRWKSENVSTTEVA 377
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 678-989 1.76e-03

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: 43.54  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  678 DLCFLQFTSGSTGDAKGVMITHGGLIHNVKLMQRRY----------RSTSNTILVSWLPQYHDmGLIGGlfTALVSGGSS 747
Cdd:cd17648     95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYfgrdngdeavLFFSNYVFDFFVEQMTL-ALLNG--QKLVVPPDE 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  748 VLFSPMTFIknpllwlETMSKYQATH-SAGPNFAFELMLRRLESDKS-TARNYDLSSMIFlmvaaEPVRQitlkRFIELT 825
Cdd:cd17648    172 MRFDPDRFY-------AYINREKVTYlSGTPSVLQQYDLARLPHLKRvDAAGEEFTAPVF-----EKLRS----RFAGLI 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  826 LpfglsqevmaPGYGLAENCVfvscaYGQGKPIFVDWQGRVCCGYVDPNdpdVDIRIANPETgeEIKESGKEGEIWISSS 905
Cdd:cd17648    236 I----------NAYGPTETTV-----TNHKRFFPGDQRFDKSLGRPVRN---TKCYVLNDAM--KRVPVGAVGELYLGGD 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  906 SAGIGYWGREELSQKTF--------KNELPDYPGRIYtRTGDLGRII-DGKLFITGRiKDL-IIVAGRNIYSADIEKTVE 975
Cdd:cd17648    296 GVARGYLNRPELTAERFlpnpfqteQERARGRNARLY-KTGDLVRWLpSGELEYLGR-NDFqVKIRGQRIEPGEVEAALA 373

                          330
                   ....*....|....
gi 2130317402  976 SSSELLRpgcCAVV 989
Cdd:cd17648    374 SYPGVRE---CAVV 384
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1360-1430 1.88e-03

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: 42.01  E-value: 1.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1360 ARIGSSVLLDtvditdpSLVSIGDGAVIAEGVLVQ-GHEVRNGVlsflpiRIGRNSSVGPFAVIQKGSIIGD 1430
Cdd:cd03352      2 AKIGENVSIG-------PNAVIGEGVVIGDGVVIGpGVVIGDGV------VIGDDCVIHPNVTIYEGCIIGD 60
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 529-755 2.12e-03

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: 43.43  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  529 TYRELHANASLISHKLLtsEKPVIKPGDRVLLVYVPGLDFVDCFFGclrarvlpvpvlppdplqrggqallkienIAKSC 608
Cdd:cd05938      7 TYRDVDRRSNQAARALL--AHAGLRPGDTVALLLGNEPAFLWIWLG-----------------------------LAKLG 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  609 NAVAILSTvgyhsAVRAGSVKNLILLTGKNGKTTGR------WPNLPWLHTDS---WIKYS-------KNLQAENKADSA 672
Cdd:cd05938     56 CPVAFLNT-----NIRSKSLLHCFRCCGAKVLVVAPelqeavEEVLPALRADGvsvWYLSHtsntegvISLLDKVDAASD 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  673 EPETDDL---------CFLQFTSGSTGDAKGVMITHggliHNVKLMQRRYRS---TSNTILVSWLPQYHDMGLIGGLFTA 740
Cdd:cd05938    131 EPVPASLrahvtikspALYIYTSGTTGLPKAARISH----LRVLQCSGFLSLcgvTADDVIYITLPLYHSSGFLLGIGGC 206

                          250
                   ....*....|....*...
gi 2130317402  741 LVSGGSSVL---FSPMTF 755
Cdd:cd05938    207 IELGATCVLkpkFSASQF 224
PRK12831 PRK12831
putative oxidoreductase; Provisional
 23-59 2.47e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 43.08  E-value: 2.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVSG 59
Cdd:PRK12831   142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGG 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1379-1445 2.81e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 2.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402 1379 VSIGDGAVIAEGVlvqghevrngvlsflpiRIGRNSSVGPFAVIQKGSIIGDEADAGAAVqneAIYH 1445
Cdd:PRK00892   119 VSIGPNAVIGAGV-----------------VIGDGVVIGAGAVIGDGVKIGADCRLHANV---TIYH 165
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1095-1189 2.91e-03

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 42.43  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1095 TTGTCREGKTPRPQLVSSPLPSPKMSN----KDIVEFLIRLVSEQTGIPSSNISATGSLVSYGIDSIGVVRAAQKLSEfL 1170
Cdd:COG3433    187 LALKVVARAAPALAAAEALLAAASPAPaletALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRK-A 265

                           90
                   ....*....|....*....
gi 2130317402 1171 GVPVGAVDIFTATCISDLA 1189
Cdd:COG3433    266 GLDVSFADLAEHPTLAAWW 284
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1379-1430 3.01e-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: 42.70  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2130317402 1379 VSIGDGAVIAEGVlvqghevrngvlsflpiRIGRNSSVGPFAVIQKGSIIGD 1430
Cdd:COG1044    115 VSIGPFAVIGAGV-----------------VIGDGVVIGPGVVIGDGVVIGD 149
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1379-1445 3.12e-03

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: 41.62  E-value: 3.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130317402 1379 VSIGDGAVIAEGVlvqghevrngvlsflpiRIGRNSSVGPFAVIQKGSIIGDEADAGAAVqneAIYH 1445
Cdd:cd03352      8 VSIGPNAVIGEGV-----------------VIGDGVVIGPGVVIGDGVVIGDDCVIHPNV---TIYE 54
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 1584-1671 3.16e-03

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 39.35  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSIR------AINPVSCPKQISIGAGVHLGDFSRIIsgfysstgfisGKVEVQENSVIGsqslilPNSVVQKD 1657
Cdd:cd03354     28 TAVIGDNCTIYqgvtlgGKGKGGGKRHPTIGDNVVIGAGAKIL-----------GNITIGDNVKIG------ANAVVTKD 90

                           90
                   ....*....|....
gi 2130317402 1658 VilgalsvaPAHSV 1671
Cdd:cd03354     91 V--------PANST 96
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1585-1665 3.18e-03

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: 38.77  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1585 AEVGKHCSIraiNP-VSCPKQISIGAGVHLGDFSRIISGFYsstGFISGKVEVQENSVIGSQSLILPNSVVQKDVILGAL 1663
Cdd:cd00208      1 VFIGEGVKI---HPkAVIRGPVVIGDNVNIGPGAVIGAATG---PNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAG 74


                   ..
gi 2130317402 1664 SV 1665
Cdd:cd00208     75 AV 76
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 23-52 3.38e-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: 38.72  E-value: 3.38e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYRnVTVLE 52
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGSK-VTVVE 29
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1586-1682 3.77e-03

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.78  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1586 EVGKHCSI------RA-INPvscpkqISIGAGVHLGDFSRI-ISGFYSSTgfISGKV-----------EVQENSVIGSQS 1646
Cdd:COG0663     30 TIGEDVSVwpgavlRGdVGP------IRIGEGSNIQDGVVLhVDPGYPLT--IGDDVtighgailhgcTIGDNVLIGMGA 101

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2130317402 1647 LILPNSVVQKDVILGALSVAPAHSVLQQGGVYVGSQ 1682
Cdd:COG0663    102 IVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSP 137
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 681-746 4.09e-03

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 42.56  E-value: 4.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130317402  681 FLqFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNT--ILVSWLPQYHDMGLIGGLFTALVSGGS 746
Cdd:PRK08180   214 FL-FTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGT 280
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 1584-1681 4.72e-03

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: 40.94  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1584 GAEVGKHCSIraiNPVScpkqiSIGAGVHLGDFSRIISGfysstGFISGKVEVQENSVIGSQSLILPN------------ 1651
Cdd:TIGR03570  117 DVRIGDNVII---NTGA-----IVEHDCVIGDFVHIAPG-----VTLSGGVVIGEGVFIGAGATIIQGvtigagaivgag 183

                           90       100       110
                   ....*....|....*....|....*....|
gi 2130317402 1652 SVVQKDVilgalsvapahsvlQQGGVYVGS 1681
Cdd:TIGR03570  184 AVVTKDI--------------PDGGVVVGV 199
PLN02576 PLN02576
protoporphyrinogen oxidase
 21-82 4.96e-03

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 42.31  E-value: 4.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130317402   21 TTRIGIVGAGPSGLSAAYALTKLGYRNVTVLEKFHTVSGMCESVEIEGKMYDLGgqvlaANS 82
Cdd:PLN02576    12 SKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEG-----PNS 68
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
29-59 5.16e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 41.49  E-value: 5.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2130317402   29 AGPSGLSAAYALTKLGYRnVTVLEK-----FHTVSG 59
Cdd:COG0644      1 AGPAGSAAARRLARAGLS-VLLLEKgsfpgDKICGG 35
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1343-1438 5.84e-03

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 41.94  E-value: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1343 VYLRGTVFL--------NCWFEmlGA-RIGSSVLL--DTVdITDpslVSIGDGAVIAEGVLVQGHevrngvlsflpirIG 1411
Cdd:COG1207    261 TYIDGDVEIgrdvvidpNVILE--GKtVIGEGVVIgpNCT-LKD---STIGDGVVIKYSVIEDAV-------------VG 321

                           90       100
                   ....*....|....*....|....*..
gi 2130317402 1412 RNSSVGPFAVIQKGSIIGDEADAGAAV 1438
Cdd:COG1207    322 AGATVGPFARLRPGTVLGEGVKIGNFV 348
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 24-60 6.26e-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: 6.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2130317402   24 IGIVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVSGM 60
Cdd:PRK12779   309 IAVVGSGPSGLINAYLLAVEGF-PVTVFEAFHDLGGV 344
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 1352-1436 6.81e-03

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 38.74  E-value: 6.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402 1352 NCWfemlgarIGSSVLLDTVDitdpsLVSIGDGAVIAEGVLVQG--HEVRNGVLSFL--PIRIGRNSSVGPFAVIQKGSI 1427
Cdd:cd05825      9 NSW-------IGEGVWIYNLA-----PVTIGSDACISQGAYLCTgsHDYRSPAFPLItaPIVIGDGAWVAAEAFVGPGVT 76


                   ....*....
gi 2130317402 1428 IGDEADAGA 1436
Cdd:cd05825     77 IGEGAVVGA 85
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 676-772 7.79e-03

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports 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 FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 41.64  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402  676 TDDLCFLqFTSGSTGDAKGVMITHGGLIHNVKLMQRRYRSTSNTILVSWLPQYHDMGLIGGLFTALVSGGSSVL---FSP 752
Cdd:cd05939    104 RDKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIrkkFSA 182

                           90       100
                   ....*....|....*....|
gi 2130317402  753 MTFiknpllWLETMsKYQAT 772
Cdd:cd05939    183 SNF------WDDCV-KYNCT 195
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 23-94 7.91e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 41.37  E-value: 7.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYR-NVTVLEKFHTVSGMCESVEIEGKMYDLG--GQVLAANSAPvifDLAKETG 94
Cdd:PRK11883     2 KVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFPIELGpeSFLARKPSAP---ALVKELG 73
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 24-101 9.03e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 40.53  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130317402   24 IGIVGAGPSGLSAAYALTKLGYRNVTVLEKfhtvsgmceSVEIEGKMYdLGGQVLaanSAPVIFDLAK----ETGSELEE 99
Cdd:pfam01946   20 VVIVGAGSSGLTAAYYLAKNRGLKVAIIER---------SVSPGGGAW-LGGQLF---SAMVVRKPAHlfldEFGIPYED 86


                   ..
gi 2130317402  100 MD 101
Cdd:pfam01946   87 EG 88
PRK06753 PRK06753
hypothetical protein; Provisional
 23-58 9.89e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 41.21  E-value: 9.89e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2130317402   23 RIGIVGAGPSGLSAAYALTKLGYrNVTVLEKFHTVS 58
Cdd:PRK06753     2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNESVK 36
 
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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