|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
61-461 |
1.03e-170 |
|
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: 493.35 E-value: 1.03e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQEICRLlecaGQDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLAL----GKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLagqeyvellspvvrklgvpllplppavyngaaeehgvrelperdwrdRGAMIIYTSGTTGRPKGVLS 220
Cdd:cd05941 77 EYVITDSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWekfLSSETPRINVFMAVP 300
Cdd:cd05941 110 THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMGVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 301 TIYTKLMDYYDKHFTQPhvqDFVRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTvAARL 380
Cdd:cd05941 187 TIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLD-GERR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 381 PGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrvtPGFKEKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFK 460
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEETGE-------------------PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
.
gi 946754379 461 T 461
Cdd:cd05941 324 T 324
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
55-461 |
1.96e-85 |
|
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: 274.38 E-value: 1.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPG-----DRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAgqeyvellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGR 214
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 215 PKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRIN 294
Cdd:COG0318 115 PKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELI---ERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 295 VFMAVPTIYTKLMDYYDKHFTQPHvqdfvravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALS-NP 373
Cdd:COG0318 192 VLFGVPTMLARLLRHPEFARYDLS-----------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTvNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 374 LTVAARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAF 453
Cdd:COG0318 261 EDPGERRPGSVGRPLPGVEVRIVDE-------------DGRE----LPPG---EVGEIVVRGPNVMKGYWNDPEATAEAF 320
|
....*...
gi 946754379 454 tSDGWFKT 461
Cdd:COG0318 321 -RDGWLRT 327
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-461 |
3.36e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 251.46 E-value: 3.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRALAFGDRVALVDQHGVH-TYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVP 130
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRlTYRELDERANRLA----AGLRALGVG-KGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 131 LFRKHPQADLEYFIQDSRSSVVLAGQEYVelLSPVVRKLGVPLLPLPPAVYNGAAE------------EHGVRELPERDW 198
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALK--LEELLEALGKLEVVKLVLVLDRDPVlkeeplpeeakpADVPPPPPPPPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 RDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL----VHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP 274
Cdd:pfam00501 154 PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 EFSAQLVWEKFLSSETPRINVFMAVPTIYTKLMDyydkhftqphvQDFVRAVCEEKIRLMVSGSAALPLPVLEKWKNITG 354
Cdd:pfam00501 234 GFPALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HTLLERYGMTE--IGMALSNPLTVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaEGNEkdtrVTPGfkeKEGELL 432
Cdd:pfam00501 303 GALVNGYGLTEttGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDE------------TGEP----VPPG---EPGELC 363
|
410 420
....*....|....*....|....*....
gi 946754379 433 VRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:pfam00501 364 VRGPGVMKGYLNDPELTAEAFDEDGWYRT 392
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-461 |
1.61e-71 |
|
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: 238.23 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRALA-FGDRVALVDQHGVHTYKDLYcrslRLSQEICRLLECAGqdLQE-ERISFMCSNDVSYVVAQWASWMSGGIAV 129
Cdd:cd05936 4 LLEEAARrFPDKTALIFMGRKLTYRELD----ALAEAFAAGLQNLG--VQPgDRVALMLPNCPQFPIAYFGALKAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 130 PLfrkHPQ---ADLEYFIQDSRSSVVLAGQEYVELLSPvvrklgvpllplppavyngaaeEHGVRELPERDwRDRGAMII 206
Cdd:cd05936 78 PL---NPLytpRELEHILNDSGAKALIVAVSFTDLLAA----------------------GAPLGERVALT-PEDVAVLQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 207 YTSGTTGRPKGVLSTHHNIRAVVTGLvhkWAWTK-----DDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLV 281
Cdd:cd05936 132 YTSGTTGVPKGAMLTHRNLVANALQI---KAWLEdllegDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 WEKFlssETPRINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERY 361
Cdd:cd05936 209 LKEI---RKHRVTIFPGVPTMYIALLNAPEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEIG-MALSNPLTVAARlPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVFR 440
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRK-PGSIGIPLPGTEVKIVDD-------------DGEE----LPPG---EVGELWVRGPQVMK 333
|
410 420
....*....|....*....|.
gi 946754379 441 EYWGKPEETKKAFTsDGWFKT 461
Cdd:cd05936 334 GYWNRPEETAEAFV-DGWLRT 353
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
49-461 |
1.36e-67 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 228.61 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 49 SAPVFTR---ALAFGDRVALVDQHG-VHTYKDLycrsLRLSQEICRLLecAGQDLQE-ERISFMCSNDVSYVVAQWASWM 123
Cdd:PRK07514 2 NNNLFDAlraAFADRDAPFIETPDGlRYTYGDL----DAASARLANLL--VALGVKPgDRVAVQVEKSPEALALYLATLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 124 SGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDWRDRG- 202
Cdd:PRK07514 76 AGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVPRGa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 ---AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQ 279
Cdd:PRK07514 156 ddlAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 280 LVWEKFlssetPRINVFMAVPTIYTKLMDyyDKHFTQPHVQdfvravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLE 359
Cdd:PRK07514 236 AVLALM-----PRATVMMGVPTFYTRLLQ--EPRLTREAAA---------HMRLFISGSAPLLAETHREFQERTGHAILE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 360 RYGMTEIGMALSNPLtVAARLPGSVGTPLPGVEVQIVSENPQKEgCPyilhaegnekdtrvtpgfKEKEGELLVRGPTVF 439
Cdd:PRK07514 300 RYGMTETNMNTSNPY-DGERRAGTVGFPLPGVSLRVTDPETGAE-LP------------------PGEIGMIEVKGPNVF 359
|
410 420
....*....|....*....|..
gi 946754379 440 REYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK07514 360 KGYWRMPEKTAEEFRADGFFIT 381
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
36-461 |
1.42e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 203.68 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 36 RPLHVALAARSDKSAPvftrALAFGDRVAlvdqhgvhTYKDLYCRSLRLSQEIcrllecAGQDlqeeRISFMCSNDVSYV 115
Cdd:PRK07787 2 ASLNPAAVAAAADIAD----AVRIGGRVL--------SRSDLAGAATAVAERV------AGAR----RVAVLATPTLATV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 116 VAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAG--QEYVELlsPVVrklgvpllplppAVYNGAAEEHGVREL 193
Cdd:PRK07787 60 LAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPapDDPAGL--PHV------------PVRLHARSWHRYPEP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 194 PErdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML 273
Cdd:PRK07787 126 DP----DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 274 PEFSAQLVWEKFLSSETprinVFMAVPTIYTKLMDyydkhftqphVQDFVRAVceEKIRLMVSGSAALPLPVLEKWKNIT 353
Cdd:PRK07787 202 GRPTPEAYAQALSEGGT----LYFGVPTVWSRIAA----------DPEAARAL--RGARLLVSGSAALPVPVFDRLAALT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 354 GHTLLERYGMTEIGMALSNpLTVAARLPGSVGTPLPGVEVQIVSENpqkeGCPyiLHAEGnekdtrvtpgfkEKEGELLV 433
Cdd:PRK07787 266 GHRPVERYGMTETLITLST-RADGERRPGWVGLPLAGVETRLVDED----GGP--VPHDG------------ETVGELQV 326
|
410 420
....*....|....*....|....*...
gi 946754379 434 RGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK07787 327 RGPTLFDGYLNRPDATAAAFTADGWFRT 354
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
55-461 |
2.59e-56 |
|
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: 196.68 E-value: 2.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL-FR 133
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKG-----DRVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPqADLEYFIQDSRSSVVLagqeyvellspvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGTTG 213
Cdd:cd17631 79 LTP-PEVAYILADSGAKVLF----------------------------------------------DDLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAqlvwEKFLS-SETPR 292
Cdd:cd17631 112 RPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDP----ETVLDlIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 293 INVFMAVPTIYTKLMDYYDkhFTQPhvqDFVRavceekIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGM-ALS 371
Cdd:cd17631 188 VTSFFLVPTMIQALLQHPR--FATT---DLSS------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPgVTF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 372 NPLTVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKK 451
Cdd:cd17631 256 LSPEDHRRKLGSAGRPVFFVEVRIVDPD-------------GRE----VPPG---EVGEIVVRGPHVMAGYWNRPEATAA 315
|
410
....*....|
gi 946754379 452 AFtSDGWFKT 461
Cdd:cd17631 316 AF-RDGWFHT 324
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
58-461 |
6.71e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 197.72 E-value: 6.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 58 AFGDRVALVDQHGVHTYKDLYCRSLRLSQEicrLLEC---AGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPL-FR 133
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRLANA---LRALgvkKGD-----RVAVFDWNSHEYLEAYFAVPKIGAVLHPInIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQaDLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVP--------LLPLPPAVYNGAAEEHGVRELPERDWRDRG--- 202
Cdd:PRK06187 90 LKPE-EIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVrtvivegdGPAAPLAPEVGEYEELLAAASDTFDFPDIDend 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 -AMIIYTSGTTGRPKGVLSTHHNIRAVVTGlVHKW-AWTKDDVILHVLPLHHVHG----VVnkllcPLWVGATCVMLPEF 276
Cdd:PRK06187 169 aAAMLYTSGTTGHPKGVVLSHRNLFLHSLA-VCAWlKLSRDDVYLVIVPMFHVHAwglpYL-----ALMAGAKQVIPRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 277 SAQLVWEKFlssETPRINVFMAVPTIYTKLMDYYDKHFtqphvQDFVRavceekIRLMVSGSAALPLPVLEKWKNITGHT 356
Cdd:PRK06187 243 DPENLLDLI---ETERVTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKFGID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 357 LLERYGMTEIGmalsnPLTVAARLP----------GSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGFKE 426
Cdd:PRK06187 309 LVQGYGMTETS-----PVVSVLPPEdqlpgqwtkrRSAGRPLPGVEARIVDD-------------DGDE----LPPDGGE 366
|
410 420 430
....*....|....*....|....*....|....*
gi 946754379 427 KeGELLVRGPTVFREYWGKPEETKKAFTsDGWFKT 461
Cdd:PRK06187 367 V-GEIIVRGPWLMQGYWNRPEATAETID-GGWLHT 399
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
60-461 |
9.70e-56 |
|
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: 196.82 E-value: 9.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 60 GDRVALVDQHGVHTYKDLYCRSLRLSQEICRL-LEcagqdlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQA 138
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALgVK------REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 139 DLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPpaVYNGAAEEHGVREL------------PERDWRDRGAMII 206
Cdd:cd05959 92 DYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLI--VSGGAGPEAGALLLaelvaaeaeqlkPAATHADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 207 YTSGTTGRPKGVLSTHHNIRAV-------VTGLvhkwawTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SA 278
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTaelyarnVLGI------REDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 QLVWEKFlssETPRINVFMAVPTIYTKLMDYYDkhftqPHVQDFVRavceekIRLMVSGSAALPLPVLEKWKNITGHTLL 358
Cdd:cd05959 244 AAVFKRI---RRYRPTVFFGVPTLYAAMLAAPN-----LPSRDLSS------LRLCVSAGEALPAEVGERWKARFGLDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 359 ERYGMTEIG-MALSNplTVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEkdtrVTPGfkeKEGELLVRGPT 437
Cdd:cd05959 310 DGIGSTEMLhIFLSN--RPGRVRYGTTGKPVPGYEVELRDED-------------GGD----VADG---EPGELYVRGPS 367
|
410 420
....*....|....*....|....
gi 946754379 438 VFREYWGKPEETKKAFTSdGWFKT 461
Cdd:cd05959 368 SATMYWNNRDKTRDTFQG-EWTRT 390
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
73-461 |
4.96e-55 |
|
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: 194.45 E-value: 4.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYcrslRLSQEICRLLECAGQDLQEeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05926 16 TYADLA----ELVDDLARQLAALGIKKGD-RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 L------------AGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDwRDRGAMIIYTSGTTGRPKGVLS 220
Cdd:cd05926 91 LtpkgelgpasraASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPL-PDDLALILHTSGTTGRPKGVPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRINVFMAVP 300
Cdd:cd05926 170 THRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDV---RDYNATWYTAVP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 301 TIYTKLMDYYDKHFTQPHVqdfvravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MAlSNPLTVAA 378
Cdd:cd05926 247 TIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPLPPGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 379 RLPGSVGTPLpGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGW 458
Cdd:cd05926 316 RKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVGEICLRGPNVTRGYLNNPEANAEAAFKDGW 374
|
...
gi 946754379 459 FKT 461
Cdd:cd05926 375 FRT 377
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
52-461 |
9.71e-54 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 193.39 E-value: 9.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRALAFGDRVALVDQHG----VHTYKDLYcrslrlsQEICRLleCAG-QDL---QEERISFMCSNDVSYVVAQWASWM 123
Cdd:COG1022 17 LRRRAARFPDRVALREKEDgiwqSLTWAEFA-------ERVRAL--AAGlLALgvkPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 124 SGGIAVPLFRKHPQADLEYFIQDSRSSVVLAG-QEYVELLSPVVRKLGvplLPLPPAVYNGAAEEHGVRELPERDWRDRG 202
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELP---SLRHIVVLDPRGLRDDPRLLSLDELLALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 ---------------------AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLL 261
Cdd:COG1022 165 revadpaelearraavkpddlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 262 CpLWVGATCV----------MLPEFSAQL------VWEKFLSS------ETPRI-----NVFMAVPTIYtklMDYYDKHF 314
Cdd:COG1022 245 A-LAAGATVAfaespdtlaeDLREVKPTFmlavprVWEKVYAGiqakaeEAGGLkrklfRWALAVGRRY---ARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 315 TQPHVQDFVRAVCEE------------KIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEI-GMALSNPLTvaARLP 381
Cdd:COG1022 321 SPSLLLRLKHALADKlvfsklrealggRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPG--DNRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 382 GSVGTPLPGVEVQIvsenpqkegcpyilhAEgnekdtrvtpgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:COG1022 398 GTVGPPLPGVEVKI---------------AE---------------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHT 447
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
203-461 |
4.05e-53 |
|
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: 185.18 E-value: 4.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQLVW 282
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 EKFlssETPRINVFMAVPTIYTKLMDYYDKHftqPHVQDFVRAVCeekirlmvSGSAALPLPVLEKWKNITGHTLLERYG 362
Cdd:cd04433 82 ELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 363 MTEIG-MALSNPLTVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaegnekDTRVTPGFkekEGELLVRGPTVFRE 441
Cdd:cd04433 148 LTETGgTVATGPPDDDARKPGSVGRPVPGVEVRIVDPD-----------------GGELPPGE---IGELVVRGPSVMKG 207
|
250 260
....*....|....*....|
gi 946754379 442 YWGKPEETkKAFTSDGWFKT 461
Cdd:cd04433 208 YWNNPEAT-AAVDEDGWYRT 226
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
73-461 |
8.24e-50 |
|
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: 180.10 E-value: 8.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSqeiCRLLECAGQdlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05911 12 TYAQLRTLSRRLA---AGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYVELLSPVVRKLG--------------VPLLPLPPAVYNGAAEEHGVRELPERDwrDRGAMIIYTSGTTGRPKGV 218
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGpkdkiivlddkpdgVLSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 219 LSTHHNIRAVV--TGLVHKWAWTKDDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAqlvwEKFLSS-ETPRINV 295
Cdd:cd05911 165 CLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDS----ELFLDLiEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 296 FMAVPTIYTKLmdyydkhFTQPHVQDFVRAvceeKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALS-NP 373
Cdd:cd05911 240 LYLVPPIAAAL-------AKSPLLDKYDLS----SLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTvNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 374 LTVAarLPGSVGTPLPGVEVQIVSENPQKEGCPyilhaegNEkdtrvtpgfkekEGELLVRGPTVFREYWGKPEETKKAF 453
Cdd:cd05911 309 DGDD--KPGSVGRLLPNVEAKIVDDDGKDSLGP-------NE------------PGEICVRGPQVMKGYYNNPEATKETF 367
|
....*...
gi 946754379 454 TSDGWFKT 461
Cdd:cd05911 368 DEDGWLHT 375
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
203-461 |
6.81e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 176.73 E-value: 6.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRA-VVTGLvhkwAWT-----KDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 276
Cdd:PRK05605 222 ALILYTSGTTGKPKGAQLTHRNLFAnAAQGK----AWVpglgdGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 277 SAQLVWeKFLSSETPrinVFM-AVPTIYTKLMDYYDKHftqphvqdfvrAVCEEKIRLMVSGSAALPLPVLEKWKNITGH 355
Cdd:PRK05605 298 DIDLIL-DAMKKHPP---TWLpGVPPLYEKIAEAAEER-----------GVDLSGVRNAFSGAMALPVSTVELWEKLTGG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 356 TLLERYGMTEIG-MALSNPLTvAARLPGSVGTPLPGVEVQIVS-ENPQKEgcpyilhaegnekdtrVTPGfkeKEGELLV 433
Cdd:PRK05605 363 LLVEGYGLTETSpIIVGNPMS-DDRRPGYVGVPFPDTEVRIVDpEDPDET----------------MPDG---EEGELLV 422
|
250 260
....*....|....*....|....*...
gi 946754379 434 RGPTVFREYWGKPEETKKAFTsDGWFKT 461
Cdd:PRK05605 423 RGPQVFKGYWNRPEETAKSFL-DGWFRT 449
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
56-461 |
2.87e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 173.55 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKH 135
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAA----AALAALGIG-KGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 136 PQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVynGAAEEHGVRELPERDWRDRG------------- 202
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICET--EEDDPHTEKMKTFTDFLAAGdpaerapevdpdd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 -AMIIYTSGTTGRPKGVLSTHHNIravvTGLVHKWA----WTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 277
Cdd:PRK07656 168 vADILFTSGTTGRPKGAMLTHRQL----LSNAADWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVwekFLSSETPRINVFMAVPTIYTKLMDYYDKHFTqphvqDFvravceEKIRLMVSGSAALPLPVLEKWKNITG-HT 356
Cdd:PRK07656 244 PDEV---FRLIETERITVLPGPPTMYNSLLQHPDRSAE-----DL------SSLRLAVTGAASMPVALLERFESELGvDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 357 LLERYGMTE-IGMALSNPL-TVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEKDTRVTpgfkekeGELLVR 434
Cdd:PRK07656 310 VLTGYGLSEaSGVTTFNRLdDDRKTVAGTIGTAIAGVENKIVNEL-------------GEEVPVGEV-------GELLVR 369
|
410 420
....*....|....*....|....*..
gi 946754379 435 GPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK07656 370 GPNVMKGYYDDPEATAAAIDADGWLHT 396
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
102-461 |
1.10e-46 |
|
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: 170.85 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAgqeyvellspvvrklgvpllplppavy 181
Cdd:cd05907 31 DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV--------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 182 ngaaeehgvrelperDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLL 261
Cdd:cd05907 84 ---------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 262 CPLWVGATCVMLPEfsaqlvwEKFLSSETPRI--NVFMAVPTIytklmdyYDKHFTQPHVQD--------FVRAVCeEKI 331
Cdd:cd05907 149 VPLLAGARIYFASS-------AETLLDDLSEVrpTVFLAVPRV-------WEKVYAAIKVKAvpglkrklFDLAVG-GRL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 332 RLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALS-NPLTvaARLPGSVGTPLPGVEVQIVSenpqkegcpyilh 410
Cdd:cd05907 214 RFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTlNPPG--DNRIGTVGKPLPGVEVRIAD------------- 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 946754379 411 aegnekdtrvtpgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05907 278 -----------------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHT 311
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
73-461 |
2.24e-45 |
|
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: 167.23 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQeicrLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVP-LFRKHPQaDLEYFIQDSRSSV 151
Cdd:cd05914 9 TYKDLADNIAKFAL----LLKINGVG-TGDRVALMGENRPEWGIAFFAIWTYGAIAVPiLAEFTAD-EVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 152 VLAGQEyvellspvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTG 231
Cdd:cd05914 83 IFVSDE------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 232 LVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQL-----------------VWE---KFLSSETP 291
Cdd:cd05914 121 VKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKiialafaqvtptlgvpvPLViekIFKMDIIP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 292 RINV-----FMAVP--------TIYTKLMDYYDKHFtqphvqdfvravceekiRLMVSGSAALPLPVLEKWKNItGHTLL 358
Cdd:cd05914 201 KLTLkkfkfKLAKKinnrkirkLAFKKVHEAFGGNI-----------------KEFVIGGAKINPDVEEFLRTI-GFPYT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 359 ERYGMTEIGMALSNPLTVAARLpGSVGTPLPGVEVQIVSENPQKEgcpyilhaegnekdtrvtpgfkekEGELLVRGPTV 438
Cdd:cd05914 263 IGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPDPATG------------------------EGEIIVRGPNV 317
|
410 420
....*....|....*....|...
gi 946754379 439 FREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHT 340
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
60-461 |
2.27e-43 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 163.74 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 60 GDRVAL--VDQHGVH---TYKDLYcrslrlsQEICRLlecAG--QDL---QEERISFMCSNDVSYVVAQWASWMSGGIAV 129
Cdd:COG0365 23 GDKVALiwEGEDGEErtlTYAELR-------REVNRF---ANalRALgvkKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 130 P---LFRKHpqaDLEYFIQDSRSSVVLAGQEYVELLSP---------------------VVRKLGVPLLPLPPAVYNGAA 185
Cdd:COG0365 93 PvfpGFGAE---ALADRIEDAEAKVLITADGGLRGGKVidlkekvdealeelpslehviVVGRTGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 186 EEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIrAVVTGLVHKWAW--TKDDVILHVLPLHHVHGVVNKLLCP 263
Cdd:COG0365 170 AAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY-LVHAATTAKYVLdlKPGDVFWCTADIGWATGHSYIVYGP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 264 LWVGATCVML---PEF-SAQLVW---EKFlssetpRINVFMAVPTIYTKLMDYYDKHFTQPhvqDFVRavceekIRLMVS 336
Cdd:COG0365 249 LLNGATVVLYegrPDFpDPGRLWeliEKY------GVTVFFTAPTAIRALMKAGDEPLKKY---DLSS------LRLLGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 337 GSAALPLPVLEKWKNITGHTLLERYGMTEIGMA-LSNPLTVAARlPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNE 415
Cdd:COG0365 314 AGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVK-PGSMGKPVPGYDVAVVDE-------------DGNP 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 946754379 416 kdtrVTPGfkeKEGELLVRG--PTVFREYWGKPEETKKAF--TSDGWFKT 461
Cdd:COG0365 380 ----VPPG---EEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRT 422
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
56-461 |
5.56e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 162.44 E-value: 5.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVDQHGVHTYKDLYCRSLRLsqeicrllecAGQdLQEE-------RISFMCSNDVSYVVAQWASWMSGGIA 128
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERL----------AGY-LQQEcgvrkgdRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 129 VPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVP-----------LLPLPPAVYNGAAEEHGVRELPERD 197
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvivaqysdylPAEPEIAVPAWLRAEPPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 198 W-------------------RDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVN 258
Cdd:PRK08314 169 VvawkealaaglappphtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 259 KLLCPLWVGATCVMLP----EFSAQLVwekflssETPRINVFMAVPTIytkLMDYydkhFTQPHVQDFvravCEEKIRLM 334
Cdd:PRK08314 249 SMNAPIYAGATVVLMPrwdrEAAARLI-------ERYRVTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 VSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSNPLtvAARLPGSVGTPLPGVEVQIVSENPQKEgcpyilhaeg 413
Cdd:PRK08314 311 GGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPP--DRPKLQCLGIPTFGVDARVIDPETLEE---------- 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 946754379 414 nekdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAF-TSDG--WFKT 461
Cdd:PRK08314 379 ------LPPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRT 420
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
73-461 |
4.56e-41 |
|
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: 154.56 E-value: 4.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKG-----DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYVELlspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL 232
Cdd:cd05935 78 VVGSELDDL-----------------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 233 VHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRINVFMAVPTIYTKLMdyydk 312
Cdd:cd05935 117 AVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLL----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 313 hfTQPHVQDFvravCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE-IGMALSNPLTVAARlpGSVGTPLPGV 391
Cdd:cd05935 189 --ATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKL--QCLGIP*FGV 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946754379 392 EVQIVSENPQKEgcpyilhaegnekdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDG---WFKT 461
Cdd:cd05935 261 DARVIDIETGRE----------------LPPN---EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRT 314
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
52-461 |
5.05e-39 |
|
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: 150.46 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRALAFGDRVALVDQHG--VHTYKDLycrsLRLSQEICRLLECAGqdLQEERISFMCS-NDVSYVVAQWASWMSGGIA 128
Cdd:cd05904 11 SFLFASAHPSRPALIDAATgrALTYAEL----ERRVRRLAAGLAKRG--GRKGDVVLLLSpNSIEFPVAFLAVLSLGAVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 129 VPLfrkHP---QADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVP--LLPLPPAVYNGAAEEHGVRELPERDWRDRGA 203
Cdd:cd05904 85 TTA---NPlstPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLdsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWT--KDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAqlv 281
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDL--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 wEKFLSS-ETPRINVFMAVPTIYTKLMDyydkhftQPHVQDFVRAvceeKIRLMVSGSAALPLPVLEKWKNITGHT-LLE 359
Cdd:cd05904 239 -EELLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKELIEAFRAKFPNVdLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 360 RYGMTE---IGMALSNPLTVAARlPGSVGTPLPGVEVQIVS-ENPQKEGcpyilhaegnekdtrvtPGfkeKEGELLVRG 435
Cdd:cd05904 307 GYGMTEstgVVAMCFAPEKDRAK-YGSVGRLVPNVEAKIVDpETGESLP-----------------PN---QTGELWIRG 365
|
410 420
....*....|....*....|....*.
gi 946754379 436 PTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHT 391
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
55-464 |
3.63e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 147.70 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAgqdlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVK----KGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVynGAAEEHGVRELPERDwRDRGAMIIYTSGTTGR 214
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSL--KEIEDRKIDNFVEKN-ESASFIICYTSGTTGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 215 PKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNKLLCPLWVGATCVML-----PEFSAQLVwekflssE 289
Cdd:PRK06839 164 PKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVprkfePTKALSMI-------E 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 290 TPRINVFMAVPTIYTKLMDYYDkhFTQPHVQdfvravceeKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE---- 365
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSK--FETTNLQ---------SVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtspt 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 366 IGMALSNPltvAARLPGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrVTPGfkeKEGELLVRGPTVFREYWGK 445
Cdd:PRK06839 304 VFMLSEED---ARRKVGSIGKPVLFCDYELIDENKNK-----------------VEVG---EVGELLIRGPNVMKEYWNR 360
|
410
....*....|....*....
gi 946754379 446 PEETKKAFtSDGWFKTACL 464
Cdd:PRK06839 361 PDATEETI-QDGWLCTGDL 378
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
102-462 |
1.61e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 147.10 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQ---------------EYV------- 159
Cdd:PRK06710 75 DRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDlvfprvtnvqsatkiEHVivtriad 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 160 ------ELLSPVVRK-----LGVPLLPLPPAVYNGAAEEH--GVREL--PERDWrdrgAMIIYTSGTTGRPKGVLSTHHN 224
Cdd:PRK06710 155 flpfpkNLLYPFVQKkqsnlVVKVSESETIHLWNSVEKEVntGVEVPcdPENDL----ALLQYTGGTTGFPKGVMLTHKN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 225 IRAVVTGLVHkWAWT---KDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRINVFMAVPT 301
Cdd:PRK06710 231 LVSNTLMGVQ-WLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAI---KKHKVTLFPGAPT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 302 IYTKLMDyydkhftQPHVQDFVRAvceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmalSNPLTVA---- 377
Cdd:PRK06710 307 IYIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTE-----SSPVTHSnflw 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 378 -ARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaegnEKDTRVTPGfkeKEGELLVRGPTVFREYWGKPEETkKAFTSD 456
Cdd:PRK06710 371 eKRVPGSIGVPWPDTEAMIMSL----------------ETGEALPPG---EIGEIVVKGPQIMKGYWNKPEET-AAVLQD 430
|
....*.
gi 946754379 457 GWFKTA 462
Cdd:PRK06710 431 GWLHTG 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
72-461 |
2.64e-37 |
|
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: 143.97 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 72 HTYKDLycrsLRLSQEICRLLECAGqDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSV 151
Cdd:cd05934 4 WTYAEL----LRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 152 VLAgqeyvellSPvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLSTHHNIRAVVTG 231
Cdd:cd05934 79 VVV--------DP--------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 232 LVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSetpRINVFMAVPTIYTKLMDyyd 311
Cdd:cd05934 113 SARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRY---GATVTNYLGAMLSYLLA--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 312 khfTQPHVQDfvravCEEKIRLmVSGSAALPLpVLEKWKNITGHTLLERYGMTEIGMALSNPLtVAARLPGSVGTPLPGV 391
Cdd:cd05934 187 ---QPPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVIGPR-DEPRRPGSIGRPAPGY 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946754379 392 EVQIVSEnpqkegcpyilhaegnekDTRVTPgfKEKEGELLVR---GPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05934 256 EVRIVDD------------------DGQELP--AGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHT 307
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
61-474 |
1.87e-36 |
|
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: 141.90 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLA----RYLRERGVG-PGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDL-------------------------------------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEF----SAQLVweKFLSSEtpRINVF 296
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEEvrkdPEALA--DLLAEE--GITVL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 297 MAVPTIYTKLMDYYDkhftqphvqdfvRAVCeEKIRLMVSGSAALPLPVLEKW-KNITGHTLLERYGMTEI-GMALSNPL 374
Cdd:cd05930 189 HLTPSLLRLLLQELE------------LAAL-PSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEAtVDATYYRV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 375 TVAARLPGSV--GTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKA 452
Cdd:cd05930 256 PPDDEEDGRVpiGRPIPNTRV-------------YVLDENLRP----VPPG---VPGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430
....*....|....*....|....*....|..
gi 946754379 453 FTSDGWFKTACL-----LVTRTP-----FLRR 474
Cdd:cd05930 316 FVPNPFGPGERMyrtgdLVRWLPdgnleFLGR 347
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
73-469 |
4.64e-36 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 140.09 E-value: 4.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEIcRLLECAGQDlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:TIGR01733 1 TYRELDERANRLARHL-RAAGGVGPG---DRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHgvreLPERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL 232
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLDPLELAALDDAPAPPP----PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 233 VHKWAWTKDDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPEfSAQLVWEKFLSS--ETPRINVFMAVPTIYTKLMDyy 310
Cdd:TIGR01733 153 ARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAALLAAliAEHPVTVLNLTPSLLALLAA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 311 DKHFTQPHVqdfvravceekiRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSN------PLTVAARLPgs 383
Cdd:TIGR01733 229 ALPPALASL------------RLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTAtlvdpdDAPRESPVP-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 384 VGTPLPGVEVqivsenpqkegcpYILHAEGNEKDTRVTpgfkekeGELLVRGPTVFREYWGKPEETKKAFTSDGWFKTAC 463
Cdd:TIGR01733 295 IGRPLANTRL-------------YVLDDDLRPVPVGVV-------GELYIGGPGVARGYLNRPELTAERFVPDPFAGGDG 354
|
....*.
gi 946754379 464 LLVTRT 469
Cdd:TIGR01733 355 ARLYRT 360
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
73-461 |
3.01e-34 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 135.20 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPG-----DVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYvellspvvrklgvpllplppavyngaaEEHGVRELPerdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL 232
Cdd:cd05903 78 VVPERF---------------------------RQFDPAAMP-----DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 233 VHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEkflSSETPRINVFMAVPTIYTKLMDyydk 312
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA---LMREHGVTFMMGATPFLTDLLN---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 313 hftqpHVQDFVRAVCEekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSN-PLTVAARLPGSVGTPLPGV 391
Cdd:cd05903 199 -----AVEEAGEPLSR--LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSiTPAPEDRRLYTDGRPLPGV 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 392 EVQIVSENPQKegcpyilhaegnekdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05903 272 EIKVVDDTGAT-----------------LAPG---VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRT 320
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
39-459 |
3.24e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 133.90 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 39 HVALAARSDKSAPVFTRALA-FGDRVALVDQHGVHTYkdlycrslrlsQEICRLLECAGQDLQE------ERISFMCSND 111
Cdd:PRK08316 3 ERSTRARRQTIGDILRRSARrYPDKTALVFGDRSWTY-----------AELDAAVNRVAAALLDlglkkgDRVAALGHNS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 112 VSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEhgvR 191
Cdd:PRK08316 72 DAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG---G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 192 ELPERDWRDRG--------------AMIIYTSGTTGRPKGVLSTHhniRAVV---TGLVHKWAWTKDDVILHVLPLHHVH 254
Cdd:PRK08316 149 WLDFADWAEAGsvaepdveladddlAQILYTSGTESLPKGAMLTH---RALIaeyVSCIVAGDMSADDIPLHALPLYHCA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 255 GVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRINVFMAVPTIYTKLMDYYDkhFTQPHVQDFVRAvceekirlm 334
Cdd:PRK08316 226 QLDVFLGPYLYVGATNVILDAPDPELILRTI---EAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKG--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 VSGSAALPLPVLEKwknitghtLLER---------YGMTEIGmalsnPL-TV-----AARLPGSVGTPLPGVEVQIVSEn 399
Cdd:PRK08316 292 YYGASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLaTVlgpeeHLRRPGSAGRPVLNVETRVVDD- 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 400 pqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWF 459
Cdd:PRK08316 358 ------------DGND----VAPG---EVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWF 397
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
55-461 |
6.58e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 132.39 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSlrlsQEICRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAV----VSVAGKLAALGVK-KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRklgvpllplppAVYNGAAEEHGVRELPERDWR-DRGAMIIYTSGTTG 213
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGIS-----------VKFAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWEkflSSETPRI 293
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISG-LSILMRSVIYGMRVVLVEKFDAEKINK---LLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVFMAVPTIYTKLmdyydkhftqphVQDFVRAVCEEKIRLMVSGSAALPLPVLE--KWKNItghTLLERYGMTEIG---M 368
Cdd:PRK03640 231 TIISVVSTMLQRL------------LERLGEGTYPSSFRCMLLGGGPAPKPLLEqcKEKGI---PVYQSYGMTETAsqiV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 369 ALSnPLTVAARLpGSVGTPLPGVEVQIvsenpqkegcpyilhaegnEKDTRVTPGFkeKEGELLVRGPTVFREYWGKPEE 448
Cdd:PRK03640 296 TLS-PEDALTKL-GSAGKPLFPCELKI-------------------EKDGVVVPPF--EEGEIVVKGPNVTKGYLNREDA 352
|
410
....*....|...
gi 946754379 449 TKKAFtSDGWFKT 461
Cdd:PRK03640 353 TRETF-QDGWFKT 364
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
72-461 |
6.68e-33 |
|
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: 132.75 E-value: 6.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 72 HTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL-FRKHPQaDLEYFIQDSRSS 150
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPG-----DRVATLAWNTHRHLELYYAVPGMGAVLHTInPRLFPE-QIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 151 VVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVREL----------PERDWRD----RGAMIIYTSGTTGRPK 216
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLayeellaaesPEYDWPDfdenTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 217 GVLSTHhniRAVV-----------TGLVHKwawtkdDVILHVLPLHHVH--GVvnkllcP---LWVGATCV-----MLPE 275
Cdd:cd12119 180 GVVYSH---RSLVlhamaalltdgLGLSES------DVVLPVVPMFHVNawGL------PyaaAMVGAKLVlpgpyLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 276 FSAQLvwekfLSSETPRINVfmAVPTIYTKLMDYYDKHftqPHVQDFVRAVceekirlmVSGSAALPLPVLEKWKNItGH 355
Cdd:cd12119 245 SLAEL-----IEREGVTFAA--GVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 356 TLLERYGMTEIGmalsnPLTVAARLPGSV---------------GTPLPGVEVQIVSEnpqkegcpyilhaegnekDTRV 420
Cdd:cd12119 306 RVIHAWGMTETS-----PLGTVARPPSEHsnlsedeqlalrakqGRPVPGVELRIVDD------------------DGRE 362
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 946754379 421 TPGFKEKEGELLVRGPTVFREYWGKPEETkKAFTSDGWFKT 461
Cdd:cd12119 363 LPWDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRT 402
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
73-461 |
8.34e-33 |
|
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: 131.71 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSqeicrlleCAGQDL---QEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRS 149
Cdd:cd17640 7 TYKDLYQEILDFA--------AGLRSLgvkAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 150 SVVLagqeyvellspvvrklgvpllplppaVYNGAaeehgvrelperdwrDRGAMIIYTSGTTGRPKGVLSTHHNIravV 229
Cdd:cd17640 79 VALV--------------------------VENDS---------------DDLATIIYTSGTTGNPKGVMLTHANL---L 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 230 TGLVHKWAWTK---DDVILHVLPLHHVHGVVNKLLCPLWvGATCVmlpeFSAQlvweKFLSSETPRIN--VFMAVP---- 300
Cdd:cd17640 115 HQIRSLSDIVPpqpGDRFLSILPIWHSYERSAEYFIFAC-GCSQA----YTSI----RTLKDDLKRVKphYIVSVPrlwe 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 301 TIYTKLmdyYDKHFTQPHVQDFV--RAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEIGmalsnPLTVAA 378
Cdd:cd17640 186 SLYSGI---QKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETS-----PVVSAR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 379 RLP----GSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEkdtrVTPgfKEKEGELLVRGPTVFREYWGKPEETKKAFT 454
Cdd:cd17640 257 RLKcnvrGSVGRPLPGTEIKIVDPE-------------GNV----VLP--PGEKGIVWVRGPQVMKGYYKNPEATSKVLD 317
|
....*..
gi 946754379 455 SDGWFKT 461
Cdd:cd17640 318 SDGWFNT 324
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
73-461 |
2.52e-32 |
|
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: 129.39 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEICRLlecagQDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVv 152
Cdd:cd05912 3 TFAELFEEVSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 lagqeyvellspvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL 232
Cdd:cd05912 77 -----------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 233 VHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSetpRINVFMAVPTIYTKLMDYYDK 312
Cdd:cd05912 110 ALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSG---KVTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 313 HftqphvqdfvravCEEKIRLMVSGSAALPLPVLE--KWKNItghTLLERYGMTEIG--MALSNPLTVAARLpGSVGTPL 388
Cdd:cd05912 186 G-------------YPNNLRCILLGGGPAPKPLLEqcKEKGI---PVYQSYGMTETCsqIVTLSPEDALNKI-GSAGKPL 248
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946754379 389 PGVEVQIVSENPQKEGcpyilhaegnekdtrvtpgfkekEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05912 249 FPVELKIEDDGQPPYE-----------------------VGEILLKGPNVTKGYLNRPDATEESF-ENGWFKT 297
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
73-461 |
1.27e-31 |
|
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: 127.45 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLycrsLRLSQEICRLLECAGqdLQE-ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSV 151
Cdd:cd05972 2 SFREL----KRESAKAANVLAKLG--LRKgDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 152 VLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLSTHhniRAVVTG 231
Cdd:cd05972 76 IVTDAEDP-------------------------------------------ALIYFTSGTTGLPKGVLHTH---SYPLGH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 232 LVHKWAWT---KDDVILHVLPLHHVHGVVNKLLCPLWVGATCVM--LPEFSAQLVWEKfLSSEtpRINVFMAVPTIYTKL 306
Cdd:cd05972 110 IPTAAYWLglrPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILEL-LERY--GVTSFCGPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 307 MDYYDKHFTQPHVQDFVravceekirlmvsgSAALPL--PVLEKWKNITGHTLLERYGMTEIGMALSNPLTVAARlPGSV 384
Cdd:cd05972 187 IKQDLSSYKFSHLRLVV--------------SAGEPLnpEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVK-PGSM 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946754379 385 GTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTV--FREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05972 252 GRPTPGYDVAIIDD-------------DGRE----LPPG---EEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLT 309
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
62-461 |
1.66e-31 |
|
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: 127.58 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 62 RVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLE 141
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSG-----DRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 142 YFIQDSRSSVVLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLST 221
Cdd:cd05919 76 YIARDCEARLVVTSADDI-------------------------------------------AYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 222 HHNIRAVVTGLVHKW-AWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SAQLVWEKfLSSETPRinVFMAV 299
Cdd:cd05919 113 HRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLAT-LARFRPT--VLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 300 PTIYTKLMDYYDKHftqphvQDFVRAvceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MALSNplTVAA 378
Cdd:cd05919 190 PTFYANLLDSCAGS------PDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSN--RPGA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 379 RLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGW 458
Cdd:cd05919 257 WRLGSTGRPVPGYEIRLVDE-------------EGHT----IPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGW 315
|
...
gi 946754379 459 FKT 461
Cdd:cd05919 316 YRT 318
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
203-461 |
1.09e-30 |
|
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: 126.18 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVH---KWAwTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefsaq 279
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvpELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSP----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 280 lvweKFLSSETPR-----INVF-----MAVP----TIYTKLMD----------------YYDKHFTQPHVQD-------- 321
Cdd:cd17639 165 ----RTLTDKSKRgckgdLTEFkptlmVGVPaiwdTIRKGVLAklnpmgglkrtlfwtaYQSKLKALKEGPGtplldelv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 322 F--VRAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEI--GMALSNPltvAARLPGSVGTPLPGVEVQIVS 397
Cdd:cd17639 241 FkkVRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDP---GDLETGRVGPPLPCCEIKLVD 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946754379 398 enpQKEGcpyilhaeGNEKDTrvtpgfKEKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd17639 317 ---WEEG--------GYSTDK------PPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHT 363
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
55-461 |
4.00e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 124.71 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALA-FGDRVALVDQHGVHTYKDLycrSLRLSQEIcRLLECAGQDLQEeRISFMCSNDVSYVVAQWASWMSGGIAVPLfr 133
Cdd:PRK06188 20 SALKrYPDRPALVLGDTRLTYGQL---ADRISRYI-QAFEALGLGTGD-AVALLSLNRPEVLMAIGAAQLAGLRRTAL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 kHPQADLE---YFIQDSRSSV-VLAGQEYVE----LL--SPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDWRDRGA 203
Cdd:PRK06188 93 -HPLGSLDdhaYVLEDAGISTlIVDPAPFVEralaLLarVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvnKLLCPLWVGATCVMLPEFSAqlvwE 283
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDP----A 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KFLSS-ETPRINVFMAVPTIYTKLMDYYDkhftqPHVQDFvravceEKIRLMVSGSAALpLPV-LEKWKNITGHTLLERY 361
Cdd:PRK06188 246 EVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPM-SPVrLAEAIERFGPIFAQYY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEIGMALS------NPLTVAARLpGSVGTPLPGVEVQivsenpqkegcpyILHAEGNEkdtrVTPGfkeKEGELLVRG 435
Cdd:PRK06188 314 GQTEAPMVITylrkrdHDPDDPKRL-TSCGRPTPGLRVA-------------LLDEDGRE----VAQG---EVGEICVRG 372
|
410 420
....*....|....*....|....*.
gi 946754379 436 PTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK06188 373 PLVMDGYWNRPEETAEAF-RDGWLHT 397
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
203-461 |
8.64e-30 |
|
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: 123.21 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-----EFS 277
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPnpldyKKI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVWEKflssetpRINVFMAVPTiytkLMDYYDKhftQPHVQDFvravceEKIRLMVSGSAALPLPVLEKWKNITGHTL 357
Cdd:cd05909 230 PELIYDK-------KATILLGTPT----FLRGYAR---AAHPEDF------SSLRLVVAGAEKLKDTLRQEFQEKFGIRI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 358 LERYGMTEIGMALSNPLTVAARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrvtPGFKEKEGELLVRGPT 437
Cdd:cd05909 290 LEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSV-------------ETHE------EVPIGEGGLLLVRGPN 350
|
250 260
....*....|....*....|....
gi 946754379 438 VFREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05909 351 VMLGYLNEPELTSFAF-GDGWYDT 373
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
54-459 |
1.84e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.93 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 54 TRALAFGDRVALVDQHGV-HTYKDLYCRSLRLSQeicRLLECAGQDLqeERISFMCSNDVSYVVAQWASWMSGGIAVPLF 132
Cdd:PRK06087 31 QTARAMPDKIAVVDNHGAsYTYSALDHAASRLAN---WLLAKGIEPG--DRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 133 RKHPQADLEYFIQDSRSSVVLA-----GQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDW--------- 198
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEplttaitth 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 RDRGAMIIYTSGTTGRPKGVLSTHHNI----RAVVTGLvhkwAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP 274
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNIlaseRAYCARL----NLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 EFSAQLVWEKFlssETPRINVFM-AVPTIYTKLmdyydKHFTQPHVqDFvravceEKIRLMVSGSAALPLPVLEKWKNiT 353
Cdd:PRK06087 262 IFTPDACLALL---EQQRCTCMLgATPFIYDLL-----NLLEKQPA-DL------SALRFFLCGGTTIPKKVARECQQ-R 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 354 GHTLLERYGMTE-IGMALSNPLTVAARLPGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrVTPGfkeKEGELL 432
Cdd:PRK06087 326 GIKLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-----------------LPPG---CEGEEA 385
|
410 420
....*....|....*....|....*..
gi 946754379 433 VRGPTVFREYWGKPEETKKAFTSDGWF 459
Cdd:PRK06087 386 SRGPNVFMGYLDEPELTARALDEEGWY 412
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
40-464 |
1.93e-29 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 122.69 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 40 VALAARSDKSAPvftrALAF-GDRVALvdqhgvhTYKDLycrsLRLSQEICRLLECAGQdLQEERISFMCSNDVSYVVAQ 118
Cdd:PRK05852 22 VEVAATRLPEAP----ALVVtADRIAI-------SYRDL----ARLVDDLAGQLTRSGL-LPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 119 WASWMSGGIAVPLFRKHPQADleyfiQDSRSSVVLAGQEYVELLSPVVRKLGV--------------PLLPLPPAVYNGA 184
Cdd:PRK05852 86 LAASRADLVVVPLDPALPIAE-----QRVRSQAAGARVVLIDADGPHDRAEPTtrwwpltvnvggdsGPSGGTLSVHLDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 185 AEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPL 264
Cdd:PRK05852 161 ATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 265 WVGATcVMLP---EFSAQLVWEKFLSSETpriNVFMAVPTIYTKLMDyydkhftQPHVQDFVRAvcEEKIRLMVSGSAAL 341
Cdd:PRK05852 241 ASGGA-VLLPargRFSAHTFWDDIKAVGA---TWYTAVPTIHQILLE-------RAATEPSGRK--PAALRFIRSCSAPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 342 PLPVLEKWKNITGHTLLERYGMTEIGMALSnpltvAARLPGSVGTPLPGVEVQIV--SENPQKEgcpyILHAEGNEkdtr 419
Cdd:PRK05852 308 TAETAQALQTEFAAPVVCAFGMTEATHQVT-----TTQIEGIGQTENPVVSTGLVgrSTGAQIR----IVGSDGLP---- 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 946754379 420 VTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTsDGWFKTACL 464
Cdd:PRK05852 375 LPAG---AVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDL 415
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
102-461 |
4.53e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.07 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLaGQEYVELLSPVVRKLgvpllplppAVY 181
Cdd:PRK09088 48 ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL-GDDAVAAGRTDVEDL---------AAF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 182 NGAAEEHGVRELPERDwRDRGAMIIYTSGTTGRPKGVLSTHHNIRAV-----VTGLVhkwawTKDDVILHVLPLHHVHGV 256
Cdd:PRK09088 118 IASADALEPADTPSIP-PERVSLILFTSGTSGQPKGVMLSERNLQQTahnfgVLGRV-----DAHSSFLCDAPMFHIIGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 257 VNKLLCPLWVGATCVMLPEFSAQ--LVWekfLSSETPRINVFMAVPTIYTKLMDyydkhftQPhvqDFVRAVCEeKIRLM 334
Cdd:PRK09088 192 ITSVRPVLAVGGSILVSNGFEPKrtLGR---LGDPALGITHYFCVPQMAQAFRA-------QP---GFDAAALR-HLTAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 VSGSAALPLPVLEKWKNiTGHTLLERYGMTEIGMALSNPL---TVAARLpGSVGTPLPGVEVQIVSENpqkegcpyilha 411
Cdd:PRK09088 258 FTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVdcdVIRAKA-GAAGIPTPTVQTRVVDDQ------------ 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 946754379 412 egnekDTRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK09088 324 -----GNDCPAG---VPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRT 365
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
203-461 |
5.30e-29 |
|
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: 121.55 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKW----AWTKDDVILHVLPLHHV--HGVVNKLLC-----PLWVGATCV 271
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 272 MLPEFSAqlvwekfLSsetPRInvFMAVPTIYTKL----------------------MDYYDKHFTQPHVQ-----DF-- 322
Cdd:cd05927 197 LLDDIKA-------LK---PTV--FPGVPRVLNRIydkifnkvqakgplkrklfnfaLNYKLAELRSGVVRaspfwDKlv 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 323 ---VRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI--GMALSNPltvAARLPGSVGTPLPGVEVQIVS 397
Cdd:cd05927 265 fnkIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP---GDTSVGHVGGPLPCAEVKLVD 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946754379 398 EnPQKEgcpYilHAEGNEKdtrvtpgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05927 342 V-PEMN---Y--DAKDPNP-----------RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHT 388
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
204-461 |
1.10e-28 |
|
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: 116.99 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWE 283
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KflsSETPRINVFMAVPTIYTKLMDYYDKHFTQPhvqDFVRAVceekirlmvsgsAALPLP-VLEKWKNITGHTLLERYG 362
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 363 MTEIgmalSNPLTVA--ARLPGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGfkeKEGELLVRGPTVFR 440
Cdd:cd17637 145 QTET----SGLVTLSpyRERPGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETGEIVVRGPLVFQ 200
|
250 260
....*....|....*....|.
gi 946754379 441 EYWGKPEETKKAFtSDGWFKT 461
Cdd:cd17637 201 GYWNLPELTAYTF-RNGWHHT 220
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
103-461 |
2.23e-28 |
|
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: 119.11 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 103 RISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQ-EYVELLSPVVRKLGVPLLPLPPAVY 181
Cdd:cd05932 33 KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKlDDWKAMAPGVPEGLISISLPPPSAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 182 N-----------GAAEEHGVRELPERDwrdrgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPL 250
Cdd:cd05932 113 NcqyqwddliaqHPPLEERPTRFPEQL-----ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 251 HHVHGVVNKLLCPLWVGATcVMLPE----FSAQLvwekflssETPRINVFMAVPTIYTKL-MDYYDKHFTQ--------P 317
Cdd:cd05932 188 AHVTERVFVEGGSLYGGVL-VAFAEsldtFVEDV--------QRARPTLFFSVPRLWTKFqQGVQDKIPQQklnlllkiP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 318 HVQDFVR-----AVCEEKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEiGMALSNPLTVAARLPGSVGTPLPGVE 392
Cdd:cd05932 259 VVNSLVKrkvlkGLGLDQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTE-NFAYSHLNYPGRDKIGTVGNAGPGVE 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946754379 393 VQIvsenpqkegcpyilhaegnekdtrvtpgfkEKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05932 337 VRI------------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRT 375
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
55-461 |
5.17e-28 |
|
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: 118.50 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALV---DQHGV---HTYKDLYCRSLRLSQEICRLLECAgqdlqeERISFMCSNDVSYVVAQWASWMSGGIA 128
Cdd:cd05931 2 RAAARPDRPAYTfldDEGGReetLTYAELDRRARAIAARLQAVGKPG------DRVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 129 VPLF---RKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNgaaeehgVRELPERDWRDRG--- 202
Cdd:cd05931 76 VPLPpptPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDL-------LPDTSAADWPPPSpdp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 ---AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSaq 279
Cdd:cd05931 149 ddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 280 lvwekflssetprinvFMAVPTIYTKLMDYYDKHFTQphVQDF-----VRAVCEEKI--------RLMVSGSAalplPVL 346
Cdd:cd05931 227 ----------------FLRRPLRWLRLISRYRATISA--APNFaydlcVRRVRDEDLegldlsswRVALNGAE----PVR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 347 EKwkniTGHTLLER--------------YGMTEIGMALS-----NPLTV----AARLPG----------------SVGTP 387
Cdd:cd05931 285 PA----TLRRFAEAfapfgfrpeafrpsYGLAEATLFVSggppgTGPVVlrvdRDALAGravavaaddpaarelvSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 388 LPGVEVQIVSENPQKEgCPyilhaegnekDTRVtpgfkekeGELLVRGPTVFREYWGKPEETKKAF------TSDGWFKT 461
Cdd:cd05931 361 LPDQEVRIVDPETGRE-LP----------DGEV--------GEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRT 421
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
55-453 |
5.36e-28 |
|
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: 120.35 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQeicRLLEC-AGQdlqEERISFMCSNDVSYVVAQWASWMSGGIAVPLFR 133
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAH---HLRALgVGP---GDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLgVPLLPLPPAVYNGAAEEHGVRElperdwrDRGAMIIYTSGTTG 213
Cdd:COG1020 559 AYPAERLAYMLEDAGARLVLTQSALAARLPELGVPV-LALDALALAAEPATNPPVPVTP-------DDLAYVIYTSGSTG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQ--LVWEKFLSSEtp 291
Cdd:COG1020 631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE-IFGALLSGATLVLAPPEARRdpAALAELLARH-- 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 292 RINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravceekiRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE--IGm 368
Cdd:COG1020 708 RVTVLNLTPSLLRALLDAAPEALPSL--------------RLVLVGGEALPPELVRRWRARLPGArLVNLYGPTEttVD- 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 369 ALSNPLTVAARLPGSV--GTPLPGVEVQIVSE--NPQKEGCPyilhaegnekdtrvtpgfkekeGELLVRGPTVFREYWG 444
Cdd:COG1020 773 STYYEVTPPDADGGSVpiGRPIANTRVYVLDAhlQPVPVGVP----------------------GELYIGGAGLARGYLN 830
|
....*....
gi 946754379 445 KPEETKKAF 453
Cdd:COG1020 831 RPELTAERF 839
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
61-461 |
8.87e-28 |
|
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: 116.58 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGD-----PVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAgqeyvellspvvrklgvpllplppavyngaaEEHGVrelperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd05945 81 REILDAAKPALLIA-------------------------------DGDDN------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLH---HVHGvvnkLLCPLWVGATCVMLPEfsAQLVWEKFLSSETPR--INV 295
Cdd:cd05945 118 SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD----LYPALASGATLVPVPR--DATADPKQLFRFLAEhgITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 296 FMAVPTIYTKLMdyYDKHFTQPHVQDfvravceekIRLMVSGSAALPLPVLEKWKNIT-GHTLLERYGMTEIGMALS--- 371
Cdd:cd05945 192 WVSTPSFAAMCL--LSPTFTPESLPS---------LRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTyie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 372 ---NPLTVAARLPgsVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEE 448
Cdd:cd05945 261 vtpEVLDGYDRLP--IGYAKPGAKLVILDE-------------DGRP----VPPG---EKGELVISGPSVSKGYLNNPEK 318
|
410
....*....|....*.
gi 946754379 449 TKKAFTSD---GWFKT 461
Cdd:cd05945 319 TAAAFFPDegqRAYRT 334
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
200-461 |
2.53e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 116.32 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRavVTGLVHKW--AWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 277
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVWEKFLSSetpRINVFMAVPTIYTKLMdyydkhfTQPhVQDFVRAVCeekIRLMVsgsAALPLPVLEKWKNIT--GH 355
Cdd:PRK08008 251 ARAFWGQVCKY---RATITECIPMMIRTLM-------VQP-PSANDRQHC---LREVM---FYLNLSDQEKDAFEErfGV 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 356 TLLERYGMTE-IGMALSNPLTVAARLPgSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEkdtrVTPGfkeKEGELLVR 434
Cdd:PRK08008 314 RLLTSYGMTEtIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDH-------------NRP----LPAG---EIGEICIK 372
|
250 260 270
....*....|....*....|....*....|
gi 946754379 435 ---GPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK08008 373 gvpGKTIFKEYYLDPKATAKVLEADGWLHT 402
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-461 |
9.15e-27 |
|
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: 111.99 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNI--RAVVTGlvHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML-PEFSAQLV 281
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnNGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 wekFLSSETPRINVFMAVPTIYTKLMDYYDKHFTQPHvqdfvravceeKIRLMVSGSAALPLPVLEKwknitghtLLERY 361
Cdd:cd05917 85 ---LEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLS-----------SLRTGIMAGAPCPPELMKR--------VIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEI----GMALSNPLTVAARLP-------GSVGTPLPGVEVQIVsenpqkegcpyilhaegnEKDTRVTPGFKEKeGE 430
Cdd:cd05917 143 NMKDVtiayGMTETSPVSTQTRTDdsiekrvNTVGRIMPHTEAKIV------------------DPEGGIVPPVGVP-GE 203
|
250 260 270
....*....|....*....|....*....|.
gi 946754379 431 LLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05917 204 LCIRGYSVMKGYWNDPEKTAEAIDGDGWLHT 234
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
199-461 |
9.68e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 114.77 E-value: 9.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 RDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVtgLVHKWAW-----TKDDVILHVLPLHHVHGV-VNKLLCpLWVGATCVM 272
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHIFALtVNCLLF-IELGGQNLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 273 ------LPEFSAQLVWEKFLSsetprinvFMAVPTIYTKLMDyyDKHFTQphvQDFvravceEKIRLMVSGSAALPLPVL 346
Cdd:PRK08974 282 itnprdIPGFVKELKKYPFTA--------ITGVNTLFNALLN--NEEFQE---LDF------SSLKLSVGGGMAVQQAVA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 347 EKWKNITGHTLLERYGMTEigmalSNPLTVA-----ARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVT 421
Cdd:PRK08974 343 ERWVKLTGQYLLEGYGLTE-----CSPLVSVnpydlDYYSGSIGLPVPSTEIKLVDD-------------DGNE----VP 400
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 946754379 422 PGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK08974 401 PG---EPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLAT 436
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
61-461 |
1.54e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 113.99 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVH------TYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL--- 131
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAALVDRVAVGLARLGVGRG-----DVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 132 FRKHpqaDLEYFIQDSRSSVVLAGQEY--------VELLSPVVRKLgvpllpLPPAVYNGAAEEHGVRELPERDW----- 198
Cdd:PRK13295 114 FRER---ELSFMLKHAESKVLVVPKTFrgfdhaamARRLRPELPAL------RHVVVVGGDGADSFEALLITPAWeqepd 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 ------RDRG-----AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVG 267
Cdd:PRK13295 185 apailaRLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 ATCVMlpefsaQLVWEKFLSSE---TPRINVFMAvptiytklmdyydkhfTQPHVQDFVRAVCEE-----KIRLMVSGSA 339
Cdd:PRK13295 265 ATAVL------QDIWDPARAAElirTEGVTFTMA----------------STPFLTDLTRAVKESgrpvsSLRTFLCAGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 340 ALPLPVLEKWKNITGHTLLERYGMTEIGMA-LSNPLTVAARLPGSVGTPLPGVEVQIVSenpqkegcpyilhAEGNEkdt 418
Cdd:PRK13295 323 PIPGALVERARAALGAKIVSAWGMTENGAVtLTKLDDPDERASTTDGCPLPGVEVRVVD-------------ADGAP--- 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 946754379 419 rVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtsDGWFKT 461
Cdd:PRK13295 387 -LPAG---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDT 423
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
200-461 |
2.24e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.02 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 274
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdptda 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 EFSAQLVwEKFlssetpRINVFMAVPT---IYTKlmdyydkhFTQPHVQDFvravceEKIRLMVSGSAALPLPVLEKWKN 351
Cdd:PRK08633 862 LGIAKLV-AKH------RATILLGTPTflrLYLR--------NKKLHPLMF------ASLRLVVAGAEKLKPEVADAFEE 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 352 ITGHTLLERYGMTEigmaLSNPLTV-------------AARLPGSVGTPLPGVEVQIVSENPQKEgcpyilhaegnekdt 418
Cdd:PRK08633 921 KFGIRILEGYGATE----TSPVASVnlpdvlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETFEE--------------- 981
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 946754379 419 rVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFT---SDGWFKT 461
Cdd:PRK08633 982 -LPPG---EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVT 1023
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
203-461 |
2.56e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 113.58 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVV--TGLVHKWAWTKDD-----VILHVLPLHHVHGV-VNKLLcPLWVGATCVMLP 274
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVANVlqMEAWLQPAFEKKPrpdqlNFVCALPLYHIFALtVCGLL-GMRTGGRNILIP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 E------FSAQLvwEKFlssetpRINVFMAVPTIYTKLMDYYDkhFTQphvQDFvravceEKIRLMVSGSAALPLPVLEK 348
Cdd:PRK07059 286 NprdipgFIKEL--KKY------QVHIFPAVNTLYNALLNNPD--FDK---LDF------SKLIVANGGGMAVQRPVAER 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 349 WKNITGHTLLERYGMTEIG-MALSNPLTVAArLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeK 427
Cdd:PRK07059 347 WLEMTGCPITEGYGLSETSpVATCNPVDATE-FSGTIGLPLPSTEVSIRDD-------------DGND----LPLG---E 405
|
250 260 270
....*....|....*....|....*....|....
gi 946754379 428 EGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK07059 406 PGEICIRGPQVMAGYWNRPDETAKVMTADGFFRT 439
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
56-461 |
2.80e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 112.78 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKH 135
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGD-----TVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 136 PQADLEYFIQDSRSSVVLAGQE--YVELLSpvvrklgvpllplppavyngaaeehgvRELPERDWR---DRGAMII--YT 208
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREfeYEDLLA---------------------------EGDPDFEWIppaDEWDPIAlnYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 209 SGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnklLCPLW----VGATCVMLPEFSAQLVWEk 284
Cdd:cd12118 142 SGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYD- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 285 flSSETPRINVFMAVPTIYTKLMDYydkhftqphvQDFVRAVCEEKIRLMVSGSAAlPLPVLEKWKNItGHTLLERYGMT 364
Cdd:cd12118 216 --LIEKHKVTHFCGAPTVLNMLANA----------PPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL-GFDVTHVYGLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 365 EIgmalSNPLTVAARLPGSVGTPLpgvEVQIVSENPQkeGCPYILHAEGNEKDT---RVTPGFKEKEGELLVRGPTVFRE 441
Cdd:cd12118 282 ET----YGPATVCAWKPEWDELPT---EERARLKARQ--GVRYVGLEEVDVLDPetmKPVPRDGKTIGEIVFRGNIVMKG 352
|
410 420
....*....|....*....|
gi 946754379 442 YWGKPEETKKAFtSDGWFKT 461
Cdd:cd12118 353 YLKNPEATAEAF-RGGWFHS 371
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
59-461 |
3.12e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.83 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 59 FGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL-FRKHPq 137
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKG-----DRILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQTP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 138 ADLEYFIQDSRSSVVLAG---QEYVEL---LSPVVRKLGVPLLPLPPAVYNGAAEEH-GVRELPERDWRDRGAMIIYTSG 210
Cdd:PRK07470 94 DEVAYLAEASGARAMICHadfPEHAAAvraASPDLTHVVAIGGARAGLDYEALVARHlGARVANAAVDHDDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 211 TTGRPKGVLSTHHNIRAVVT--------GLvhkwawTKDDVILHVLPLHHVHGVvnKLLCPLWVGATCVMLP--EFSAQL 280
Cdd:PRK07470 174 TTGRPKAAVLTHGQMAFVITnhladlmpGT------TEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 281 VWEKFlssETPRINVFMAVPTIyTKLM------DYYDkHFTQPHV---------QDFVRAvceekirlmvsgsaalpLPV 345
Cdd:PRK07470 246 VWALV---ERHRVTNLFTVPTI-LKMLvehpavDRYD-HSSLRYViyagapmyrADQKRA-----------------LAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 346 LekwknitGHTLLERYGMTEIgmalSNPLTV------------AARLpGSVGTPLPGVEVQivsenpqkegcpyILHAEG 413
Cdd:PRK07470 304 L-------GKVLVQYFGLGEV----TGNITVlppalhdaedgpDARI-GTCGFERTGMEVQ-------------IQDDEG 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 946754379 414 NEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK07470 359 RE----LPPG---ETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRT 398
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
55-481 |
4.33e-26 |
|
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: 112.55 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeiCRLLEcagQDLQ-EERISFMCSNDVSYVVAQWASWMSGgiAVPLF- 132
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLA---AGLLA---LGLRpGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 133 -RKHPQADLEYFIQDSRSSVVLA-----GQEYVELLSPVVRKLgvpLLPLPPAVYNGAAEEHGVRELPE--RDWRDRG-- 202
Cdd:COG1021 106 lPAHRRAEISHFAEQSEAVAYIIpdrhrGFDYRALARELQAEV---PSLRHVLVVGDAGEFTSLDALLAapADLSEPRpd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 ----AMIIYTSGTTGRPKGVLSTH----HNIRAvvtgLVHKWAWTKDDVILHVLPLHH--------VHGVvnkllcpLWV 266
Cdd:COG1021 183 pddvAFFQLSGGTTGLPKLIPRTHddylYSVRA----SAEICGLDADTVYLAALPAAHnfplsspgVLGV-------LYA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 267 GATCVMLPEFSAQ----LVwekflssETPRINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravceEKIRLMVSGSAALP 342
Cdd:COG1021 252 GGTVVLAPDPSPDtafpLI-------ERERVTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 343 LPVLEKWKNITGHTLLERYGMTEiGM----ALSNPLTVAARlpgSVGTPL-PGVEVQIVSEnpqkegcpyilhaEGNEkd 417
Cdd:COG1021 314 PELARRVRPALGCTLQQVFGMAE-GLvnytRLDDPEEVILT---TQGRPIsPDDEVRIVDE-------------DGNP-- 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946754379 418 trVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKTAClLVTRTPflRRHSHVQGR 481
Cdd:COG1021 375 --VPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGD-LVRRTP--DGYLVVEGR 430
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
73-461 |
5.58e-26 |
|
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: 112.38 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL-------FRKHPQADLEYFIQ 145
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPG-----DSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 146 DSRSSVVLAGQEYVELLSPV--VRKLGVPLLPLPPAVYNGAAEEHGVRELPerdwrDRGAMIIYTSGTTGRPKGVLSTHH 223
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLetLSGLPGIRVLSIEELLDTAADHDLPQSRP-----DDLALLMLTSGSTGFPKAVPLTHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 224 NIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP--EFSAQ-LVWEKFLssETPRINVFMAVP 300
Cdd:cd05906 191 NILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPteEILADpLRWLDLI--DRYRVTITWAPN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 301 TIYTKLMDYYDKHFTQPHvqDFVRavceekIRLMVSGSAALPLPVLEKWKNitghtLLERY-----------GMTEI--G 367
Cdd:cd05906 269 FAFALLNDLLEEIEDGTW--DLSS------LRYLVNAGEAVVAKTIRRLLR-----LLEPYglppdairpafGMTETcsG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 368 MALSNPLTVAARLPG----SVGTPLPGVEVQIVSENPQkegcpyilhaegnekdtrVTPgfKEKEGELLVRGPTVFREYW 443
Cdd:cd05906 336 VIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQ------------------LLP--EGEVGRLQVRGPVVTKGYY 395
|
410
....*....|....*...
gi 946754379 444 GKPEETKKAFTSDGWFKT 461
Cdd:cd05906 396 NNPEANAEAFTEDGWFRT 413
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
200-461 |
1.51e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.59 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHN--IRAVVTGLVHKWawTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML---- 273
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHGNevANAWLGALLLGL--GPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqg 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 274 ---PEFSAQLvWEKFlssETPRINVFMAVPTIYTKLMDyydkhftQPhvqdfVRAVCEEKIRLMVSGSAALPLPVLEKWK 350
Cdd:PRK07529 291 yrgPGVIANF-WKIV---ERYRINFLSGVPTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 351 NITGHTLLERYGMTEiGMALS--NPLTVAARlPGSVGTPLPGVEVQIVSENPQKegcPYILHAEGNEkdtrvtpgfkekE 428
Cdd:PRK07529 355 AATGVRIVEGYGLTE-ATCVSsvNPPDGERR-IGSVGLRLPYQRVRVVILDDAG---RYLRDCAVDE------------V 417
|
250 260 270
....*....|....*....|....*....|...
gi 946754379 429 GELLVRGPTVFREYWgKPEETKKAFTSDGWFKT 461
Cdd:PRK07529 418 GVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNT 449
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
205-461 |
2.13e-25 |
|
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: 107.59 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHhniRAVVtGLVHKWA----WTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQL 280
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAH---RQTL-RAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 281 VWEKFlssETPRINVFMAVPTIYTKLMDYydkhftqPHVQDFVRAvceeKIRLMVSGSAALPLPVLEKWKNITG-HTLLE 359
Cdd:cd17638 81 ILEAI---ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 360 RYGMTEIGMA-LSNPLTVAARLPGSVGTPLPGVEVQIVSenpqkegcpyilhaegnekdtrvtpgfkekEGELLVRGPTV 438
Cdd:cd17638 147 AYGLTEAGVAtMCRPGDDAETVATTCGRACPGFEVRIAD------------------------------DGEVLVRGYNV 196
|
250 260
....*....|....*....|...
gi 946754379 439 FREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd17638 197 MQGYLDDPEATAEAIDADGWLHT 219
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-461 |
2.23e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 110.68 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRAL-AFGDRVALVDQHGVHTYKDLYcrslRLSQEICRLLECAGQDLQEERISFMCSNDVSYVVAQWASWMSGGIAV- 129
Cdd:PRK12492 29 VFERSCkKFADRPAFSNLGVTLSYAELE----RHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 130 --PL-----------------------FRKH-----PQADLEYFIQDSRSSVVLAGQEYveLLSPVVRKLG--VPLLPLP 177
Cdd:PRK12492 105 tnPLytaremrhqfkdsgaralvylnmFGKLvqevlPDTGIEYLIEAKMGDLLPAAKGW--LVNTVVDKVKkmVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 178 PAV--YNGAAEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDD----------VIL 245
Cdd:PRK12492 183 QAVpfKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 246 HVLPLHHVHGVVNKLLCPLWVGATCVML------PEFSAQLVWEKFlssetpriNVFMAVPTIYTKLMDYYDkhFTQphv 319
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMMVSGNHNVLItnprdiPGFIKELGKWRF--------SALLGLNTLFVALMDHPG--FKD--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 320 QDFVRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MALSNPLTVAARLpGSVGTPLPGVEVQIVSE 398
Cdd:PRK12492 330 LDFSA------LKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARL-GTVGIPVPGTALKVIDD 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946754379 399 npqkegcpyilhaEGNEKDtrvtpgFKEKeGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK12492 403 -------------DGNELP------LGER-GELCIKGPQVMKGYWQQPEATAEALDAEGWFKT 445
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
62-461 |
3.13e-25 |
|
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: 108.72 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 62 RVALVDQHGVHTYKDLycrsLRLSQEICRLLECAGQDLQEERISFMCSNDVSYVVAQWASWMSGGIAV---PLFRKhpqA 138
Cdd:cd05958 1 RTCLRSPEREWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVatmPLLRP---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 139 DLEYFIQDSRSSVVLAGQeyvellspvvrklgvpllplppavyngaAEEHgvrelperdwRDRGAMIIYTSGTTGRPKGV 218
Cdd:cd05958 74 ELAYILDKARITVALCAH----------------------------ALTA----------SDDICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 219 LSTHHNIRAVVTGL-VHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVwekFLSSETPRINVFM 297
Cdd:cd05958 116 MHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL---LSAIARYKPTVLF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 298 AVPTIYTKLMDYYDkhFTQPHVQdfvravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTVA 377
Cdd:cd05958 193 TAPTAYRAMLAHPD--AAGPDLS---------SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 378 ARlPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGPTVfreYWGKPEETKKAFTSDG 457
Cdd:cd05958 262 AR-PGATGKPVPGYEAKVVDD-------------EGNP----VPDG---TIGRLAVRGPTG---CRYLADKRQRTYVQGG 317
|
....
gi 946754379 458 WFKT 461
Cdd:cd05958 318 WNIT 321
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
60-456 |
4.49e-25 |
|
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: 108.92 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 60 GDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPG-----DRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAGQEyveLLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRElperdwrDRGAMIIYTSGTTGRPKGVL 219
Cdd:cd12116 76 LRYILEDAEPALVLTDDA---LPDRLPAGLPVLLLALAAAAAAPAAPRTPVSP-------DDLAYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLP-------LhhvhgvvnKLLCPLWVGATCVML-------PEFSAQLVwekf 285
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAVTTyafdislL--------ELLLPLLAGARVVIApretqrdPEALARLI---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 286 lssETPRINVFMAVPTIYTKLMDyydkhfTQPHVQDFVRAVCeekirlmvsGSAALPlPVLEKWKNITGHTLLERYGMTE 365
Cdd:cd12116 214 ---EAHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 366 IGM-ALSNPLTVAARlPGSVGTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrVTPGFKekeGELLVRGPTVFREYWG 444
Cdd:cd12116 275 TTIwSTAARVTAAAG-PIPIGRPLANTQV-------------YVLDAALRP----VPPGVP---GELYIGGDGVAQGYLG 333
|
410
....*....|..
gi 946754379 445 KPEETKKAFTSD 456
Cdd:cd12116 334 RPALTAERFVPD 345
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
61-453 |
5.59e-25 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 109.10 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPL--FRKHPQa 138
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGLGLARG-----ERVAIYLDKRLETVTAMFGAALAGGVFVPInpLLKAEQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 139 dLEYFIQDSRSSVVLAGQEYVELLSPV------VRKLGVPLLPLPPAVYNGAAEEHGVREL--------PERDWRDRGAM 204
Cdd:TIGR03098 89 -VAHILADCNVRLLVTSSERLDLLHPAlpgchdLRTLIIVGDPAHASEGHPGEEPASWPKLlalgdadpPHPVIDSDMAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWEk 284
Cdd:TIGR03098 168 ILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLPRDVLK- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 285 flSSETPRINVFMAVPTIYTKLMDYYDKHFTQPHvqdfvravceekIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGM 363
Cdd:TIGR03098 246 --ALEKHGITGLAAVPPLWAQLAQLDWPESAAPS------------LRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 364 TEIGMALSNPLTVAARLPGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGfkeKEGELLVRGPTVFREYW 443
Cdd:TIGR03098 312 TEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVL-----------------REDGSECAPG---EEGELVHRGALVAMGYW 371
|
410
....*....|
gi 946754379 444 GKPEETKKAF 453
Cdd:TIGR03098 372 NDPEKTAERF 381
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
72-461 |
5.84e-25 |
|
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: 107.97 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 72 HTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSV 151
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKG-----DRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 152 VLAGQEYVELLSPvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGTTGRPKGVLSTHHN-IRAVVT 230
Cdd:cd05969 76 LITTEELYERTDP-----------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAmIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 231 GlvhKWAW--TKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQlVWEKFLSSEtpRINVFMAVPTIYTKLM 307
Cdd:cd05969 121 G---KYVLdlHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAE-SWYGIIERV--KVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 308 DYYDkhftqphvqDFVRAVCEEKIRLMVSGSAALPlPVLEKW-KNITGHTLLERYGMTEIG-MALSNPLTVAARlPGSVG 385
Cdd:cd05969 195 KEGD---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIK-PGSMG 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 946754379 386 TPLPGVEVQIVSENpqkegcpyilhaeGNEkdtrVTPGfkeKEGELLVRG--PTVFREYWGKPEETKKAFTsDGWFKT 461
Cdd:cd05969 264 KPLPGVKAAVVDEN-------------GNE----LPPG---TKGILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLT 320
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
55-456 |
5.86e-25 |
|
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: 108.52 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDLqEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLA----HLLRARGVGP-EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAGqeyvELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPerdwrDRGAMIIYTSGTTGR 214
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT----ADLAARLPAGGDVALLGDEALAAPPATPPLVPPRP-----DNLAYVIYTSGSTGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 215 PKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhhvhGV---VNKLLCPLWVGATCVML-------PEFSAQLVWEK 284
Cdd:cd17646 153 PKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 285 flssetprinvfmAVPTIytklmdyydkHFTQPHVQDFVRAVCEEK---IRLMVSGSAALPLPVLEKWKNITGHTLLERY 361
Cdd:cd17646 229 -------------GVTTC----------HFVPSMLRVFLAEPAAGScasLRRVFCSGEALPPELAARFLALPGAELHNLY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTE--IGMALSNPLTVAARLPGSVGTPLPGVEVqivsenpqkegcpYILHAEGNekdtRVTPGFkekEGELLVRGPTVF 439
Cdd:cd17646 286 GPTEaaIDVTHWPVRGPAETPSVPIGRPVPNTRL-------------YVLDDALR----PVPVGV---PGELYLGGVQLA 345
|
410
....*....|....*..
gi 946754379 440 REYWGKPEETKKAFTSD 456
Cdd:cd17646 346 RGYLGRPALTAERFVPD 362
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
203-461 |
1.23e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 108.31 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNI-------RAVVTGLVHKWAwtkdDVILHVLPLHHVHGVVNKLLCPLWVGATCVM--- 272
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNEGC----EILIAPLPLYHIYAFTFHCMAMMLIGNHNILisn 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 273 ---LPEFSAQLVWEKFLSsetprinvFMAVPTIYTKLMdyydkhftqpHVQDFvRAVCEEKIRLMVSGSAALPLPVLEKW 349
Cdd:PRK05677 286 prdLPAMVKELGKWKFSG--------FVGLNTLFVALC----------NNEAF-RKLDFSALKLTLSGGMALQLATAERW 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 350 KNITGHTLLERYGMTEIG-MALSNPltVAARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKE 428
Cdd:PRK05677 347 KEVTGCAICEGYGMTETSpVVSVNP--SQAIQVGTIGIPVPSTLCKVIDD-------------DGNE----LPLG---EV 404
|
250 260 270
....*....|....*....|....*....|...
gi 946754379 429 GELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEATDEILDSDGWLKT 437
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
200-461 |
2.14e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 107.58 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHhniRAVVTGLVHKWA---WTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEF 276
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISH---SALIVQSLAKIAivgYGEDDVYLHTAPLCHIGG-LSSALAMLMVGACHVLLPKF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 277 SAQLVWEKFlssETPRINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravCEEKIRLMVSGSAALPLPVLEKWKNITGHT 356
Cdd:PLN02860 248 DAKAALQAI---KQHNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 357 -LLERYGMTEIGMALSNpLTVAARLPGSVGTPLPGVEVQIVSENPQKEG-C-----PYIlhaegnekDTRVTPGFKEKEG 429
Cdd:PLN02860 316 kLFSAYGMTEACSSLTF-MTLHDPTLESPKQTLQTVNQTKSSSVHQPQGvCvgkpaPHV--------ELKIGLDESSRVG 386
|
250 260 270
....*....|....*....|....*....|..
gi 946754379 430 ELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PLN02860 387 RILTRGPHVMLGYWGQNSETASVLSNDGWLDT 418
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
203-461 |
8.14e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 105.73 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGlVHKWAWTKD------DVILHVLPLHHVHGVVNKLLCPLWVGAtCVML--- 273
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGG-CNHLisn 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 274 ----PEFSAQLvwekflssETPRINVFMAVPTIYTKLMDyyDKHFTQphvQDFvravceEKIRLMVSGSAALPLPVLEKW 349
Cdd:PRK08751 289 prdmPGFVKEL--------KKTRFTAFTGVNTLFNGLLN--TPGFDQ---IDF------SSLKMTLGGGMAVQRSVAERW 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 350 KNITGHTLLERYGMTEIG-MALSNPLTVAaRLPGSVGTPLPGVEVQIVSENPQKEGCPYIlhaegnekdtrvtpgfkeke 428
Cdd:PRK08751 350 KQVTGLTLVEAYGLTETSpAACINPLTLK-EYNGSIGLPIPSTDACIKDDAGTVLAIGEI-------------------- 408
|
250 260 270
....*....|....*....|....*....|...
gi 946754379 429 GELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETAKVMDADGWLHT 441
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-464 |
1.06e-23 |
|
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: 102.94 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML-PE-FS 277
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgPAgYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVWEKFLS-SETPRINVFMAVPTIYTKLMdyydkhfTQPHVQDFvravceEKIRLMVSGSAALPLPVLEKWKNITGHT 356
Cdd:cd05944 82 NPGLFDNFWKlVERYRITSLSTVPTVYAALL-------QVPVNADI------SSLRFAMSGAAPLPVELRARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 357 LLERYGMTEIGMALSNPLTVAARLPGSVGTPLPGVEVQIVSENPQKEgcpYILHAEGNEKdtrvtpgfkekeGELLVRGP 436
Cdd:cd05944 149 VVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGR---LLRDCAPDEV------------GEICVAGP 213
|
250 260
....*....|....*....|....*...
gi 946754379 437 TVFREYWgKPEETKKAFTSDGWFKTACL 464
Cdd:cd05944 214 GVFGGYL-YTEGNKNAFVADGWLNTGDL 240
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
42-459 |
1.13e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 105.24 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 42 LAARSDKSAPVFTRALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWAS 121
Cdd:PRK07786 13 LARRQNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFG-----DRVLILMLNRTEFVESVLAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 122 WMSGGIAVPL-FRKHPqADLEYFIQDSRSSVVL----------AGQEYVELLSPVVRKLGVPLLPLPP--AVYNGAAEEH 188
Cdd:PRK07786 88 NMLGAIAVPVnFRLTP-PEIAFLVSDCGAHVVVteaalapvatAVRDIVPLLSTVVVAGGSSDDSVLGyeDLLAEAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 189 GVRELPErdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKW-AWTKDDVILHVLPLHHVHGVVNkLLCPLWVG 267
Cdd:PRK07786 167 APVDIPN----DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNgADINSDVGFVGVPLFHIAGIGS-MLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 ATCVMLP--EFSA-QL--VWEKflssetPRINVFMAVPTIYtklmdyydkhftqphvqdfvRAVCEE--------KIRLM 334
Cdd:PRK07786 242 APTVIYPlgAFDPgQLldVLEA------EKVTGIFLVPAQW--------------------QAVCAEqqarprdlALRVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 VSGSAALPLPVL-EKWKNITGHTLLERYGMTEIgmalsNPLTV------AARLPGSVGTPLPGVEVQIVSENPQKegcpy 407
Cdd:PRK07786 296 SWGAAPASDTLLrQMAATFPEAQILAAFGQTEM-----SPVTCmllgedAIRKLGSVGKVIPTVAARVVDENMND----- 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 946754379 408 ilhaegnekdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWF 459
Cdd:PRK07786 366 ------------VPVG---EVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWF 401
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
203-461 |
4.01e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 104.03 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGatcVMLPEFSAQLVw 282
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYG---VAVGFYQGDNL- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 eKFLSS-ETPRINVFMAVPTIYTKLMD--------------------YYDK-----HFTQPH------VQDFVRAVCEEK 330
Cdd:PLN02736 299 -KLMDDlAALRPTIFCSVPRLYNRIYDgitnavkesgglkerlfnaaYNAKkqaleNGKNPSpmwdrlVFNKIKAKLGGR 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 331 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNpLTVAARLPGSVGTPLPGVEVQIVS---ENPQKEGCPY 407
Cdd:PLN02736 378 VRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG-MDEGDNLSGHVGSPNPACEVKLVDvpeMNYTSEDQPY 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 946754379 408 ilhaegnekdtrvtpgfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PLN02736 457 -------------------PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHT 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
61-456 |
2.46e-22 |
|
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: 100.07 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLA----RTLRAEGVG-PGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLagqeyVELLSPvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd17643 77 AFILADSGPSLLL-----TDPDDL--------------------------------------AYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVilhVLPLHH---------VHGvvnkllcPLWVGATCVML-------PEFSAQLVWEK 284
Cdd:cd17643 114 SHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVpyevarsPEDFARLLRDE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 285 flssetpRINVFMAVPTIYTKLMDYYDKHFTQPHvqdfvravceeKIRLMVSGSAALPLPVLEKWKNITGH---TLLERY 361
Cdd:cd17643 184 -------GVTVLNQTPSAFYQLVEAADRDGRDPL-----------ALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEIGMALSNPLTVAARLPGS----VGTPLPGVEVQIVSENPQkegcpyilhaegnekdtRVTPGfkeKEGELLVRGPT 437
Cdd:cd17643 246 GITETTVHVTFRPLDAADLPAAaaspIGRPLPGLRVYVLDADGR-----------------PVPPG---VVGELYVSGAG 305
|
410
....*....|....*....
gi 946754379 438 VFREYWGKPEETKKAFTSD 456
Cdd:cd17643 306 VARGYLGRPELTAERFVAN 324
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
41-461 |
3.97e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 100.60 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 41 ALAARSDKSAPVFTRALA---------FGDRVALVDQHGVHTYKDLYCRSLRLSQeicrLLECAGQDlQEERISFMCSND 111
Cdd:PRK06155 7 GLAARAVDPLPPSERTLPamlarqaerYPDRPLLVFGGTRWTYAEAARAAAAAAH----ALAAAGVK-RGDRVALMCGNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 112 VSYV-VAQWASWMsGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVvrKLGVPLLPLP----PAVYNGAAE 186
Cdd:PRK06155 82 IEFLdVFLGCAWL-GAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--DPGDLPLPAVwlldAPASVSVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 187 EHGVRELPERDWR---------DRGAmIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvV 257
Cdd:PRK06155 159 GWSTAPLPPLDAPapaaavqpgDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNA-L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 258 NKLLCPLWVGATCVMLPEFSAQLVWEKFLSSETPRINVFMAVPTIYTKlmdyydkhftQPHVQDfvravcEEKIRLMVSG 337
Cdd:PRK06155 237 NAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLS----------QPARES------DRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 338 SAALPLPVLEKWKNITGHTLLERYGMTEIGMALSnpLTVAARLPGSVGTPLPGVEVQIVSENpqkegcpyilhaegnekD 417
Cdd:PRK06155 301 GPGVPAALHAAFRERFGVDLLDGYGSTETNFVIA--VTHGSQRPGSMGRLAPGFEARVVDEH-----------------D 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 946754379 418 TRVTPGfkeKEGELLVRG--PTVFRE-YWGKPEETKKAFtSDGWFKT 461
Cdd:PRK06155 362 QELPDG---EPGELLLRAdePFAFATgYFGMPEKTVEAW-RNLWFHT 404
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
61-456 |
4.46e-22 |
|
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: 99.71 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGqdLQEERI-SFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLA----RTLREKG--VGPDTIvGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAGQEyvelLSPVVRKLGVPLLPLPPAVYNGAAEEhgvreLPERDWRDRGAMIIYTSGTTGRPKGVL 219
Cdd:cd17655 86 IQYILEDSGADILLTQSH----LQPPIAFIGLIDLLDEDTIYHEESEN-----LEPVSKSDDLAYVIYTSGSTGKPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAqlvwekflssetprinvfmav 299
Cdd:cd17655 157 IEHRGVVNLVEWANKVIYQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVRKETV--------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 300 pTIYTKLMDYYDKH------FTQPHVQ--DFVRAVCEEKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGM- 368
Cdd:cd17655 215 -LDGQALTQYIRQNritiidLTPAHLKllDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVd 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 369 ALSNPLTVAARLPGSV--GTPLPGVEVQIVSEN--PQKEGCPyilhaegnekdtrvtpgfkekeGELLVRGPTVFREYWG 444
Cdd:cd17655 294 ASIYQYEPETDQQVSVpiGKPLGNTRIYILDQYgrPQPVGVA----------------------GELYIGGEGVARGYLN 351
|
410
....*....|..
gi 946754379 445 KPEETKKAFTSD 456
Cdd:cd17655 352 RPELTAEKFVDD 363
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
52-461 |
5.32e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.05 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 52 VFTRALAFGDRVALVD-QHG-VHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGI-- 127
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGrVYTYADVELLSRRVAAGLHKLGIRQG-----DVVMLLLPNCPEFVLAFLGASRRGAVtt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 128 -AVPLFrkhPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYN--------GAAEEhgvrELPERDW 198
Cdd:PLN02246 104 tANPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGclhfseltQADEN----ELPEVEI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 R-DRGAMIIYTSGTTGRPKGVLSTHhniRAVVTGLVHK-------WAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATC 270
Cdd:PLN02246 177 SpDDVVALPYSSGTTGLPKGVMLTH---KGLVTSVAQQvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VMLPEFSAQLVWEKFlssETPRINVFMAVPTIYTKL-----MDYYDKhftqphvqdfvravceEKIRLMVSGSAAL---- 341
Cdd:PLN02246 254 LIMPKFEIGALLELI---QRHKVTIAPFVPPIVLAIakspvVEKYDL----------------SSIRMVLSGAAPLgkel 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 342 ------PLPvlekwknitGHTLLERYGMTEIGMALS-------NPLTVAarlPGSVGTPLPGVEVQIVsenpqkegcpyi 408
Cdd:PLN02246 315 edafraKLP---------NAVLGQGYGMTEAGPVLAmclafakEPFPVK---SGSCGTVVRNAELKIV------------ 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 946754379 409 lhaegnEKDTRVTPGfKEKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PLN02246 371 ------DPETGASLP-RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHT 416
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
183-461 |
7.95e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 100.05 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 183 GAAEEHGVReLPERDwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWA-----WTKDDVILHVLPLHHV--HG 255
Cdd:PTZ00216 250 SAGSHHPLN-IPENN--DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNdligpPEEDETYCSYLPLAHImeFG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 256 VVNKLL---CPLWVGATCVMLPEFS---AQLV-WEKFLSSETPRI------NVFMAVP-------TIYTK--------LM 307
Cdd:PTZ00216 327 VTNIFLargALIGFGSPRTLTDTFArphGDLTeFRPVFLIGVPRIfdtikkAVEAKLPpvgslkrRVFDHayqsrlraLK 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 308 DYYDKHFTQPHVQDFVRAVCEEKIRLMVSGSAALPLPVLEkWKNITGHTLLERYGMTEI----GMALSNPLTvaarlPGS 383
Cdd:PTZ00216 407 EGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTETvccgGIQRTGDLE-----PNA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 384 VGTPLPGVEVQIVSenpqkegcpyilhaegnekdtrvTPGFK-----EKEGELLVRGPTVFREYWGKPEETKKAFTSDGW 458
Cdd:PTZ00216 481 VGQLLKGVEMKLLD-----------------------TEEYKhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGW 537
|
...
gi 946754379 459 FKT 461
Cdd:PTZ00216 538 FHT 540
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
54-481 |
1.15e-21 |
|
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: 98.55 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 54 TRALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeiCRLlecAGQDLQE-ERISFMCSNDVSYVVAQWASWMSGGIAVPLF 132
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLA---AGL---RGLGIRPgDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 133 RKHPQADLEYFIQDSRSSVVLAGQEYVELLSpvvRKLgvpllplppavyngAAEEHgvRELPERdwrdrgAMIIYTSGTT 212
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDRHAGFDH---RAL--------------ARELA--ESIPEV------ALFLLSGGTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 213 GRPKGVLSTH----HNIRAVVtglvhKWAW-TKDDVILHVLPLHHvhgvvN-KLLCP-----LWVGATCVMLPEFSAQLV 281
Cdd:cd05920 152 GTPKLIPRTHndyaYNVRASA-----EVCGlDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 wekFLSSETPRINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERY 361
Cdd:cd05920 222 ---FPLIEREGVTVTALVPALVSLWLDAAASRRADL-----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEiGM----ALSNPltvAARLPGSVGTPL-PGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRGP 436
Cdd:cd05920 288 GMAE-GLlnytRLDDP---DEVIIHTQGRPMsPDDEIRVVDE-------------EGNP----VPPG---EEGELLTRGP 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 946754379 437 TVFREYWGKPEETKKAFTSDGWFKTAClLVTRTPflRRHSHVQGR 481
Cdd:cd05920 344 YTIRGYYRAPEHNARAFTPDGFYRTGD-LVRRTP--DGYLVVEGR 385
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
55-461 |
2.30e-21 |
|
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: 97.98 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQH-GVH-TYKDLYCRSLRLSQEICRLlecaGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLF 132
Cdd:cd17642 26 RYASVPGTIAFTDAHtGVNySYAEYLEMSVRLAEALKKY----GLK-QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 133 RKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPlppAVYNGAAEEHGVREL------------------- 193
Cdd:cd17642 101 DIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTI---IILDSKEDYKGYQCLytfitqnlppgfneydfkp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 194 PERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIravVTGLVHK------WAWTKDDVILHVLPLHHVHGVVNkLLCPLWVG 267
Cdd:cd17642 178 PSFDRDEQVALIMNSSGSTGLPKGVQLTHKNI---VARFSHArdpifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLICG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 ATCVMLPEFSAQLvwekFLSS-ETPRINVFMAVPTiytkLMDYYDKHftqPHVQDFvravceEKIRLMVSGSAALPLpvl 346
Cdd:cd17642 254 FRVVLMYKFEEEL----FLRSlQDYKVQSALLVPT----LFAFFAKS---TLVDKY------DLSNLHEIASGGAPL--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 347 ekwKNITGHTLLERYGMTEI--GMALSNplTVAARL--------PGSVGTPLPGVEVQIVsenpqkegcpyilhaegnEK 416
Cdd:cd17642 314 ---SKEVGEAVAKRFKLPGIrqGYGLTE--TTSAILitpegddkPGAVGKVVPFFYAKVV------------------DL 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 946754379 417 DTRVTPGFKEKeGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd17642 371 DTGKTLGPNER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHS 414
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
71-459 |
7.50e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 96.13 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 71 VHTYKDLYCRSLRLSQeicrLLECAGqdLQE-ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRS 149
Cdd:PRK08276 11 VVTYGELEARSNRLAH----GLRALG--LREgDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 150 SVVLAGQEYVELLSPVVRKLGvpLLPLPPAVYNGAAEehGVRELPErdWRD-----------RGAMIIYTSGTTGRPKGV 218
Cdd:PRK08276 85 KVLIVSAALADTAAELAAELP--AGVPLLLVVAGPVP--GFRSYEE--ALAaqpdtpiadetAGADMLYSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 219 LS--THHNIRA---VVTGLVHKWAWTKDD-VILHVLPLHHV-----HGVVNKLlcplwvGATCVMLPEFSAqlvwEKFLS 287
Cdd:PRK08276 159 KRplPGLDPDEapgMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDA----EEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 288 S-ETPRINVFMAVPTIYTKLMdyydkhftqpHVQDFVRAVCE-EKIRLMVSGSAALPLPVleKWKNIT--GHTLLERYGM 363
Cdd:PRK08276 229 LiERYRVTHSQLVPTMFVRML----------KLPEEVRARYDvSSLRVAIHAAAPCPVEV--KRAMIDwwGPIIHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 364 TE-IGMALSNPLTVAARlPGSVGTPLPGvEVQIVSENpqkegcpyilhaeGNEkdtrVTPGfkeKEGELLVRGPTVFREY 442
Cdd:PRK08276 297 SEgGGVTVITSEDWLAH-PGSVGKAVLG-EVRILDED-------------GNE----LPPG---EIGTVYFEMDGYPFEY 354
|
410
....*....|....*..
gi 946754379 443 WGKPEETKKAFTSDGWF 459
Cdd:PRK08276 355 HNDPEKTAAARNPHGWV 371
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
61-461 |
1.46e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.49 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYcrslRLSQEICRLLECAGQdLQEERISFMCSNDVSYVVAQWASWMSGGIAVP---LFRKHpq 137
Cdd:PRK06178 48 QRPAIIFYGHVITYAELD----ELSDRFAALLRQRGV-GAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 138 aDLEYFIQDSRSSVVLAgqeyVELLSPVVRKlgVPLLPLPPAVYNGAAEE----HGVRELPE---------RDWRD---- 200
Cdd:PRK06178 121 -ELSYELNDAGAEVLLA----LDQLAPVVEQ--VRAETSLRHVIVTSLADvlpaEPTLPLPDslraprlaaAGAIDllpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 201 -RG---------------AMIIYTSGTTGRPKGVLSTHHNI---RAVVTGLVHkwAWTKDDVILHVLPLHHVHGVVNKLL 261
Cdd:PRK06178 194 lRActapvplpppaldalAALNYTGGTTGMPKGCEHTQRDMvytAAAAYAVAV--VGGEDSVFLSFLPEFWIAGENFGLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 262 CPLWVGATCVMLPEFSAQLVWEkflSSETPRINV-FMAVPTiYTKLMDY-----YD-KHFTQPHVQDFVRAVCEEkIRlm 334
Cdd:PRK06178 272 FPLFSGATLVLLARWDAVAFMA---AVERYRVTRtVMLVDN-AVELMDHprfaeYDlSSLRQVRVVSFVKKLNPD-YR-- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 vsgsaalplpvlEKWKNITGHTLLE-RYGMTEIGMalSNPLTVAARL--------PGSVGTPLPGVEVQIVSEnpqkegc 405
Cdd:PRK06178 345 ------------QRWRALTGSVLAEaAWGMTETHT--CDTFTAGFQDddfdllsqPVFVGLPVPGTEFKICDF------- 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 946754379 406 pyilhaegnekDTRVTPGFKEkEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK06178 404 -----------ETGELLPLGA-EGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHT 446
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
203-465 |
2.34e-20 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 92.71 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLV-HKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAQLV 281
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 WEKFLssETPRINVFMAVPTIYTKLMDYYdkhftqphvQDFVRAVceEKIRLMVSGSAalpLPVLEKWKNI--TGHT-LL 358
Cdd:cd17635 83 LFKIL--TTNAVTTTCLVPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS---RAIAADVRFIeaTGLTnTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 359 ERYGMTEIGMALSNPLTVAARLPGSVGTPLPGVEVQIvsenpqkegcpyilhaegneKDTRVTPGFKEKEGELLVRGPTV 438
Cdd:cd17635 147 QVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYL--------------------AATDGIAGPSASFGTIWIKSPAN 206
|
250 260
....*....|....*....|....*..
gi 946754379 439 FREYWGKPEETKKAFTsDGWFKTACLL 465
Cdd:cd17635 207 MLGYWNNPERTAEVLI-DGWVNTGDLG 232
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-456 |
2.14e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.30 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQeicRLLEcAGQdLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAH---VLIA-AGV-GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLaGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEH-GVRELPerdwrDRGAMIIYTSGTTGRPKGVL 219
Cdd:PRK12467 602 AYMLDDSGVRLLL-TQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNpEVALDP-----DNLAYVIYTSGSTGQPKGVA 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSETPRINVFMAV 299
Cdd:PRK12467 676 ISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 300 PTIYTKLMdyydkhftqphvQDFVRAVCEEKIRLMVSGSaALPLPVLEKWKNIT-GHTLLERYGMTEIGMALSN-PLTVA 377
Cdd:PRK12467 755 PSHLQALL------------QASRVALPRPQRALVCGGE-ALQVDLLARVRALGpGARLINHYGPTETTVGVSTyELSDE 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 378 ARLPGSV--GTPLPGVEVQIV--SENPQKEGCPyilhaegnekdtrvtpgfkekeGELLVRGPTVFREYWGKPEETKKAF 453
Cdd:PRK12467 822 ERDFGNVpiGQPLANLGLYILdhYLNPVPVGVV----------------------GELYIGGAGLARGYHRRPALTAERF 879
|
...
gi 946754379 454 TSD 456
Cdd:PRK12467 880 VPD 882
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
182-458 |
4.17e-19 |
|
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: 90.99 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 182 NGAAEEHGVRELPERDwrdrgAMIIY-TSGTTGRPKGVLSTH--HNIRAVVTGlvHKW-AWTKDDVILHVLPLHHVHGVV 257
Cdd:cd05928 160 NEASTEHHCVETGSQE-----PMAIYfTSGTTGSPKMAEHSHssLGLGLKVNG--RYWlDLTASDIMWNTSDTGWIKSAW 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 258 NKLLCPlWVGATCVM---LPEFSAQLVWEKFlsSETPrINVFMAVPTIYTKLmdyydkhftqphVQDFVRAVCEEKIRLM 334
Cdd:cd05928 233 SSLFEP-WIQGACVFvhhLPRFDPLVILKTL--SSYP-ITTFCGAPTVYRML------------VQQDLSSYKFPSLQHC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 335 VSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIVSENpqkegcpyilhaeGN 414
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIK-PGSMGKASPPYDVQIIDDN-------------GN 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 946754379 415 ekdtrVTPgfKEKEGELLVR-GPT----VFREYWGKPEETKKAFTSDGW 458
Cdd:cd05928 363 -----VLP--PGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFY 404
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
120-452 |
1.04e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 89.04 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 120 ASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDWr 199
Cdd:cd05922 41 AGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 drgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFS-A 278
Cdd:cd05922 120 ---ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVlD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 QLVWEKFlssETPRINVFMAVPTIYTKL--MDYYD------KHFTQ-----PhvQDFVRAVCEekirlmvsgsaALPlpv 345
Cdd:cd05922 196 DAFWEDL---REHGATGLAGVPSTYAMLtrLGFDPaklpslRYLTQaggrlP--QETIARLRE-----------LLP--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 346 lekwknitGHTLLERYGMTEIGMALSN-PLTVAARLPGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGf 424
Cdd:cd05922 257 --------GAQVYVMYGQTEATRRMTYlPPERILEKPGSIGLAIPGGEFEIL-----------------DDDGTPTPPG- 310
|
330 340
....*....|....*....|....*...
gi 946754379 425 keKEGELLVRGPTVFREYWGKPEETKKA 452
Cdd:cd05922 311 --EPGEIVHRGPNVMKGYWNDPPYRRKE 336
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
61-456 |
1.85e-18 |
|
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: 88.19 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQdLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLA----HRLRALGV-GPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAgqeyvellspvvrklgvpllplppavyngaaeeHGVRELperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd17649 77 RYMLEDSGAGLLLT---------------------------------HHPRQL---------AYVIYTSGSTGTPKGVAV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSETPRINVfMAVP 300
Cdd:cd17649 115 SHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV-LDLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 301 TIY-TKLMDYYDKHFTQPHVqdfvravceeKIRLMVSGSAALPLPVLEKWKnITGHTLLERYGMTE--IGMALSNPLTVA 377
Cdd:cd17649 193 PAYlQQLAEEADRTGDGRPP----------SLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEatVTPLVWKCEAGA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 378 ARLPGSV--GTPLPGVEVqivsenpqkegcpYILHAEGNEKDTRVTpgfkekeGELLVRGPTVFREYWGKPEETKKAFTS 455
Cdd:cd17649 262 ARAGASMpiGRPLGGRSA-------------YILDADLNPVPVGVT-------GELYIGGEGLARGYLGRPELTAERFVP 321
|
.
gi 946754379 456 D 456
Cdd:cd17649 322 D 322
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
61-461 |
3.93e-18 |
|
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: 87.71 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGqdLQE-ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVA----GALKAAG--VRPgDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPllplppavynGAAEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVL 219
Cdd:cd12114 76 REAILADAGARLVLTDGPDAQLDVAVFDVLILD----------LDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQ--LVWEKFLssETPRINVFM 297
Cdd:cd12114 146 ISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEARRRdpAHWAELI--ERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 298 AVPTIYTKLMDYYDKHFTQPHVQdfvRAVceekirlMVSG---SAALPLPVLEKWKNITGHTLlerYGMTEiGMALSN-- 372
Cdd:cd12114 223 SVPALLEMLLDVLEAAQALLPSL---RLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATE-ASIWSIyh 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 373 PLTVAARLPGSV--GTPLPGVEVQIVseNPQKEGCPyilhaegnekdtrvtPGFkekEGELLVRGPTVFREYWGKPEETK 450
Cdd:cd12114 289 PIDEVPPDWRSIpyGRPLANQRYRVL--DPRGRDCP---------------DWV---PGELWIGGRGVALGYLGDPELTA 348
|
410
....*....|....*
gi 946754379 451 KAFTSDG----WFKT 461
Cdd:cd12114 349 ARFVTHPdgerLYRT 363
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
203-457 |
4.75e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 87.65 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVnkllcplwVGATCVmLPEFS----A 278
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMDptrpA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 QLVWEKFLSS-ETPRINVFMAVPTIYTKLMDYydkhftqphvqdfvravCEEK------IRLMVSGSAALPLPVLEKWKN 351
Cdd:PRK09274 248 TVDPAKLFAAiERYGVTNLFGSPALLERLGRY-----------------GEANgiklpsLRRVISAGAPVPIAVIERFRA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 352 ITGHT--LLERYGMTE------IGM--ALSNPLTVAARLPGS-VGTPLPGVEVQI--VSENPQKEGcpyilhaegnEKDT 418
Cdd:PRK09274 311 MLPPDaeILTPYGATEalpissIESreILFATRAATDNGAGIcVGRPVDGVEVRIiaISDAPIPEW----------DDAL 380
|
250 260 270
....*....|....*....|....*....|....*....
gi 946754379 419 RVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDG 457
Cdd:PRK09274 381 RLATG---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDG 416
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
61-461 |
6.03e-18 |
|
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: 87.18 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVH--TYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQA 138
Cdd:cd05923 16 DACAIADPARGLrlTYSELRARIEAVAARLHARGLRPGQ-----RVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 139 DLEYFIQ--DSRSSVVLAGQEYVellsPVVRKLGVPLLPLPPAVYNGAAEEHGvRELPERDWR-DRGAMIIYTSGTTGRP 215
Cdd:cd05923 91 ELAELIErgEMTAAVIAVDAQVM----DAIFQSGVRVLALSDLVGLGEPESAG-PLIEDPPREpEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 216 KGVLSTHHNIRAVVTGLVHK--WAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFlssETPRI 293
Cdd:cd05923 166 KGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLI---EQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVFMAVPTIYTKLMdyydkhftqpHVQDFVRAVCEEKIRLMVSGsAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNP 373
Cdd:cd05923 243 TSLFATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 374 ltvAARlPGSVGTPLPGVEVQIVSenpqkegcpyilhaEGNEKDTRVTPGfkeKEGELLVR--GPTVFREYWGKPEETKK 451
Cdd:cd05923 312 ---DAR-TGTEMRPGFFSEVRIVR--------------IGGSPDEALANG---EEGELIVAaaADAAFTGYLNQPEATAK 370
|
410
....*....|
gi 946754379 452 AFtSDGWFKT 461
Cdd:cd05923 371 KL-QDGWYRT 379
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
56-466 |
9.77e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.54 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVdqHG--VHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFR 133
Cdd:PRK08162 28 AEVYPDRPAVI--HGdrRRTWAETYARCRRLASALARRGIGRG-----DTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPL---PPAVYnGAAEEHGVREL--------PERDWR--- 199
Cdd:PRK08162 101 RLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvDDPEY-PGGRFIGALDYeaflasgdPDFAWTlpa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMII--YTSGTTGRPKGVLsTHHN---IRAVVTGLVhkWAWTKDDVILHVLPLHHVHGvvnklLCPLW----VGATC 270
Cdd:PRK08162 180 DEWDAIAlnYTSGTTGNPKGVV-YHHRgayLNALSNILA--WGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VMLPEFSAQLVWEKFlssETPRINVFMAVPTIYTKLMdyydkhftqpHVQDFVRAVCEEKIRLMVSGsAALPLPVLEKWK 350
Cdd:PRK08162 252 VCLRKVDPKLIFDLI---REHGVTHYCGAPIVLSALI----------NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKME 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 351 NItGHTLLERYGMTEIgmalSNPLTVAARLPGSVGTPLPGvEVQIVSenpqKEGCPYILHAEGN--EKDT-RVTPGFKEK 427
Cdd:PRK08162 318 EI-GFDLTHVYGLTET----YGPATVCAWQPEWDALPLDE-RAQLKA----RQGVRYPLQEGVTvlDPDTmQPVPADGET 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 946754379 428 EGELLVRGPTVFREYWGKPEETKKAFtSDGWFKTACLLV 466
Cdd:PRK08162 388 IGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAV 425
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
102-461 |
1.08e-17 |
|
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: 86.71 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAG-QEYVELLSPV--------------- 165
Cdd:cd17641 37 DVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEdEEQVDKLLEIadripsvryviycdp 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 166 --VRK------LGVPLLPLPPAVYNGAAEEHGVRELPERDWRDRgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWA 237
Cdd:cd17641 117 rgMRKyddprlISFEDVVALGRALDRRDPGLYEREVAAGKGEDV-AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 238 WTKDDVILHVLPLHHVHGVVNKLLCPLWVGaTCVMLPE-----------------FSAQLVWEKFLS------SETPRIN 294
Cdd:cd17641 196 LGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreigptfvLLPPRVWEGIAAdvrarmMDATPFK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 295 VFMavptiYTKLMDY------YDKHFTQPHVQDFVRAVCEEKI--------------RLMVSGSAALPLPVLEKWKNItG 354
Cdd:cd17641 275 RFM-----FELGMKLglraldRGKRGRPVSLWLRLASWLADALlfrplrdrlgfsrlRSAATGGAALGPDTFRFFHAI-G 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HTLLERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIvsenpqkegcpyilhaegnekdtrvtpgfkEKEGELLVR 434
Cdd:cd17641 349 VPLKQLYGQTELAGAYTVHRDGDVD-PDTVGVPFPGTEVRI------------------------------DEVGEILVR 397
|
410 420
....*....|....*....|....*..
gi 946754379 435 GPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd17641 398 SPGVFVGYYKNPEATAEDFDEDGWLHT 424
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-456 |
1.83e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 4 DAAVPPRVVMTFQRLVCALASRQLAPIrhgGSRPL--------HVALAARSDKSAP--------VFTRALAFGDRVALVD 67
Cdd:PRK12316 4496 DAATIERLARHLTNLLEAMAEDPQRRL---GELQLlekaeqqrIVALWNRTDAGYPatrcvhqlVAERARMTPDAVAVVF 4572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 68 QHGVHTYKDLYCRSLRLSQeicRLLECA-GQDLqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQD 146
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAH---ALIARGvGPEV---LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMED 4646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 147 SRSSVVLAGQEYVELLsPVvrklgvpllplppavyngAAEEHGVRELPERDWRDRG-------------AMIIYTSGTTG 213
Cdd:PRK12316 4647 SGAALLLTQSHLLQRL-PI------------------PDGLASLALDRDEDWEGFPahdpavrlhpdnlAYVIYTSGSTG 4707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVM------LPEFSAQLVWEKfls 287
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLYAEIHEH--- 4783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 288 setpRINVFMAVPTIYtklmdyydkhftQPHVQDFVRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEi 366
Cdd:PRK12316 4784 ----RVTVLVFPPVYL------------QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTE- 4846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 367 gmALSNPLTVAAR---LPGS----VGTPLPGVEVqivsenpqkegcpYILHAEGNEKDTRVTpgfkekeGELLVRGPTVF 439
Cdd:PRK12316 4847 --TTVTVLLWKARdgdACGAaympIGTPLGNRSG-------------YVLDGQLNPLPVGVA-------GELYLGGEGVA 4904
|
490
....*....|....*..
gi 946754379 440 REYWGKPEETKKAFTSD 456
Cdd:PRK12316 4905 RGYLERPALTAERFVPD 4921
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
55-458 |
2.59e-17 |
|
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: 84.95 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLA----RRLRAAGVG-PGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAGqeyvellspvvRKLGVPLLPLPPAVYNGAAEEHGVRELPERDWR-DRGAMIIYTSGTTG 213
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTD-----------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSpDDLAYVMYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNiravVTGLVHKWAW---TKDDVILHVLPL------HHVHGvvnkllcPLWVGATCVMLP--EFSAQLVW 282
Cdd:cd12117 150 RPKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPkgTLLDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 EKFLSSEtpRINVFMAVPTIYTKLMDyydkhftqphvqdfVRAVCEEKIRLMVSGSAALPLPVLEKWKNITGH-TLLERY 361
Cdd:cd12117 219 GALIAEE--GVTVLWLTAALFNQLAD--------------EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTE-IGMALSNPLTVAARLPGSV--GTPLPGVEVQIVSEN--PQKEGCPyilhaegnekdtrvtpgfkekeGELLVRGP 436
Cdd:cd12117 283 GPTEnTTFTTSHVVTELDEVAGSIpiGRPIANTRVYVLDEDgrPVPPGVP----------------------GELYVGGD 340
|
410 420
....*....|....*....|..
gi 946754379 437 TVFREYWGKPEETKKAFTSDGW 458
Cdd:cd12117 341 GLALGYLNRPALTAERFVADPF 362
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
58-466 |
6.76e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 84.05 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 58 AFGDRVALVDQHGV--HTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKH 135
Cdd:PRK12583 30 RFPDREALVVRHQAlrYTWRQLADAVDRLARGLLALGVQPG-----DRVGIWAPNCAEWLLTQFATARIGAILVNINPAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 136 PQADLEYFIQDSRSSVVLA-----GQEYVELLSPVVRKLGVPLLPLPP---------AVYNGAAEEHGV----------- 190
Cdd:PRK12583 105 RASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALAcerlpelrgVVSLAPAPPPGFlawhelqarge 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 191 ----RELPERDW---RDRGAMIIYTSGTTGRPKGVLSTHHNI--RAVVTGlvHKWAWTKDDVILHVLPLHHVHGVVNKLL 261
Cdd:PRK12583 185 tvsrEALAERQAsldRDDPINIQYTSGTTGFPKGATLSHHNIlnNGYFVA--ESLGLTEHDRLCVPVPLYHCFGMVLANL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 262 CPLWVGAtCVMLP--EFSAQLVWEkflSSETPRINVFMAVPTIYTKLMDYYD-KHFtqphvqDFvravceEKIRLMVSGS 338
Cdd:PRK12583 263 GCMTVGA-CLVYPneAFDPLATLQ---AVEEERCTALYGVPTMFIAELDHPQrGNF------DL------SSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 339 AALPLPVLEKwknitghtLLERYGMTEI----GMALSNPLT----VAARLP---GSVGTPLPGVEVQIVsenpqkegcpy 407
Cdd:PRK12583 327 APCPIEVMRR--------VMDEMHMAEVqiayGMTETSPVSlqttAADDLErrvETVGRTQPHLEVKVV----------- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 946754379 408 ilHAEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKTACLLV 466
Cdd:PRK12583 388 --DPDGAT----VPRG---EIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLAT 437
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
199-461 |
8.52e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 83.79 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 RDRGAMIIYTSGTTGRPKGVLSTHhniRAVVTglvHkWAWTKddvilHVLPLHH------------VHGVVNKLLCPLWV 266
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLHVH---NAMLQ---H-YQTGK-----YVLDLHEddvywctadpgwVTGTSYGIFAPWLN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 267 GATCVML-PEFSAQlVWEKFLSSEtpRINVFMAVPTIYTKLMDYYDKHFTQ---PHVQdFVRAVCE----EKIRLmvsGS 338
Cdd:PRK04319 272 GATNVIDgGRFSPE-RWYRILEDY--KVTVWYTAPTAIRMLMGAGDDLVKKydlSSLR-HILSVGEplnpEVVRW---GM 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 339 AALPLPVLEKWknitghtlleryGMTEIG-MALSNPLTVAARlPGSVGTPLPGVEVQIVSENpqkegcpyilhaeGNEkd 417
Cdd:PRK04319 345 KVFGLPIHDNW------------WMTETGgIMIANYPAMDIK-PGSMGKPLPGIEAAIVDDQ-------------GNE-- 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 946754379 418 trVTPGfkeKEGELLVRG--PTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK04319 397 --LPPN---RMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVS 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
201-461 |
1.46e-16 |
|
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: 81.22 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 201 RGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAQL 280
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 281 VwekflSSETPRINVFMAVPTIYTKLMDYydkHFTQPHVqdfvravceEKIRLMVSGSAALPLPVLEKWKNiTGHTLLER 360
Cdd:cd17630 80 E-----DLAPPGVTHVSLVPTQLQRLLDS---GQGPAAL---------KSLRAVLLGGAPIPPELLERAAD-RGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTEIGMALSNpLTVAARLPGSVGTPLPGVEVQIVSenpqkegcpyilhaegnekdtrvtpgfkekEGELLVRGPTVFR 440
Cdd:cd17630 142 YGMTETASQVAT-KRPDGFGRGGVGVLLPGRELRIVE------------------------------DGEIWVGGASLAM 190
|
250 260
....*....|....*....|.
gi 946754379 441 EYWGKPEEtkKAFTSDGWFKT 461
Cdd:cd17630 191 GYLRGQLV--PEFNEDGWFTT 209
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
203-461 |
1.57e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.00 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDD--VILHVLPLHHVHGVVNKLLCPLWVGATCVM-----LPE 275
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 276 FSAQLVweKFLSSETPriNVFMAVPTIYTKLMDYYDkhftqphvQDfvRAVCE---EKIRLMVSGSAALPLPVLEKWKNI 352
Cdd:PRK08180 292 GFDETL--RNLREISP--TVYFNVPKGWEMLVPALE--------RD--AALRRrffSRLKLLFYAGAALSQDVWDRLDRV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 353 TGHTLLER------YGMTEIGMALSNpLTVAARLPGSVGTPLPGVEVQIVsenpqkegcPYilhaegnekDTRVtpgfke 426
Cdd:PRK08180 358 AEATCGERirmmtgLGMTETAPSATF-TTGPLSRAGNIGLPAPGCEVKLV---------PV---------GGKL------ 412
|
250 260 270
....*....|....*....|....*....|....*
gi 946754379 427 kegELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK08180 413 ---EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRS 444
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
110-461 |
1.71e-16 |
|
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: 82.79 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 110 NDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV-----------LAGQEYVELLSPVVrKLGVPLLPLPP 178
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILvvenqkqlqkiLQIQDKLPHLKAII-QYKEPLKEKEP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 179 AVYNGAAEEHGVRELPERDWRDR--------GAMIIYTSGTTGRPKGVLSTHHNI----RAVVTGLVHKWAWTKDDVILH 246
Cdd:cd05933 121 NLYSWDEFMELGRSIPDEQLDAIissqkpnqCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 247 VLPLHHVHGVVNKLLCPLWVGAtCVMLPEFSAqLVWEKFLSSETPRINVFMAVPTIYTKLMD----------YYDK---- 312
Cdd:cd05933 201 YLPLSHIAAQILDIWLPIKVGG-QVYFAQPDA-LKGTLVKTLREVRPTAFMGVPRVWEKIQEkmkavgaksgTLKRkias 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 313 ----------------HFTQPHVQDFVRAVCEEKIRLMV---------SGSAALPLPVLEKW--KNItghTLLERYGMTE 365
Cdd:cd05933 279 wakgvgletnlklmggESPSPLFYRLAKKLVFKKVRKALgldrcqkffTGAAPISRETLEFFlsLNI---PIMELYGMSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 366 IgmalSNPLTV----AARLpGSVGTPLPGVEVQIvsENPQKEGcpyilhaegnekdtrvtpgfkekEGELLVRGPTVFRE 441
Cdd:cd05933 356 T----SGPHTIsnpqAYRL-LSCGKALPGCKTKI--HNPDADG-----------------------IGEICFWGRHVFMG 405
|
410 420
....*....|....*....|
gi 946754379 442 YWGKPEETKKAFTSDGWFKT 461
Cdd:cd05933 406 YLNMEDKTEEAIDEDGWLHS 425
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
53-458 |
1.73e-16 |
|
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: 82.39 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 53 FTR-ALAFGDRVALVDQHGVHTYKDLYCRSLRLSQeicRLLECAGQDlqEERISFMCSNDVSYVVAQWASWMSGGIAVPL 131
Cdd:cd17651 1 FERqAARTPDAPALVAEGRRLTYAELDRRANRLAH---RLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 132 FRKHPQADLEYFIQDSRSSVVLAGQEYVELLsPVVRKLGVPLLPLPPAVYNGAAEEhgvrelPERDwRDRGAMIIYTSGT 211
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGEL-AVELVAVTLLDQPGAAAGADAEPD------PALD-ADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 212 TGRPKGVLSTHhnirAVVTGLVhkwAWtkDDVILHVLPLHHVHGV--------VNKLLCPLWVGATCVMLPE-------- 275
Cdd:cd17651 148 TGRPKGVVMPH----RSLANLV---AW--QARASSLGPGARTLQFaglgfdvsVQEIFSTLCAGATLVLPPEevrtdppa 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 276 FSAQLvwekflssETPRIN-VFMavPTIytklmdyydkhftqphvqdFVRAVCEEKIR----------LMVSGSAALPLP 344
Cdd:cd17651 219 LAAWL--------DEQRISrVFL--PTV-------------------ALRALAEHGRPlgvrlaalryLLTGGEQLVLTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 345 VLEKW-KNITGHTLLERYGMTE--IGMALSNPLTVAAR-LPGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrV 420
Cdd:cd17651 270 DLREFcAGLPGLRLHNHYGPTEthVVTALSLPGDPAAWpAPPPIGRPIDNTRVYVLDAALRP-----------------V 332
|
410 420 430
....*....|....*....|....*....|....*...
gi 946754379 421 TPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGW 458
Cdd:cd17651 333 PPG---VPGELYIGGAGLARGYLNRPELTAERFVPDPF 367
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
61-456 |
1.85e-16 |
|
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: 81.92 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQeicRLLEC-AGQdlqEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLAR---LLAARgVGP---ERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAgqeyvellSPvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGTTGRPKGVL 219
Cdd:cd17652 76 IAYMLADARPALLLT--------TP-----------------------------------DNLAYVIYTSGSTGRPKGVV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAQlvwekflssetprinvfmAV 299
Cdd:cd17652 113 VTHRGLANLAAAQIAAFDVGPGSRVLQFASP-SFDASVWELLMALLAGATLVLAPAEELL------------------PG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 300 PTIYTKLMDYYDKHFTQ-PHVQDFVRAVCEEKIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTE--IGMALSNPLTV 376
Cdd:cd17652 174 EPLADLLREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTEttVCATMAGPLPG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 377 AARLPgsVGTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrVTPGFKekeGELLVRGPTVFREYWGKPEETKKAFTSD 456
Cdd:cd17652 252 GGVPP--IGRPVPGTRV-------------YVLDARLRP----VPPGVP---GELYIAGAGLARGYLNRPGLTAERFVAD 309
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
100-461 |
2.51e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.20 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 100 QEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPvvrkLGVPLLPLPPA 179
Cdd:PLN02574 91 QGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP----LGVPVIGVPEN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 180 VY--NGAAEEHGVRELPERDW---------RDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAW-----TKDDV 243
Cdd:PLN02574 167 YDfdSKRIEFPKFYELIKEDFdfvpkpvikQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASqyeypGSDNV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 244 ILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQlvwEKFLSSETPRINVFMAVPTIYTKLMdyydkHFTQPhvqdfV 323
Cdd:PLN02574 247 YLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAS---DMVKVIDRFKVTHFPVVPPILMALT-----KKAKG-----V 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 324 RAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE---IGMALSNplTVAARLPGSVGTPLPGVEVQIVSen 399
Cdd:PLN02574 314 CGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEstaVGTRGFN--TEKLSKYSSVGLLAPNMQAKVVD-- 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946754379 400 pQKEGCpyilhaegnekdtRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PLN02574 390 -WSTGC-------------LLPPG---NCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRT 434
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
61-456 |
2.77e-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: 81.74 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQEICRLlecAGQdlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGL---GVA--PGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd17650 77 QYMLEDSGAKLLLTQPEDL-------------------------------------------AYVIYTSGTTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIravvTGLVHKWawtKDDVILHVLPLHHVHGV-------VNKLLCPLWVGATCVMLPE---FSAQLVWEKFLSSet 290
Cdd:cd17650 114 EHRNV----AHAAHAW---RREYELDSFPVRLLQMAsfsfdvfAGDFARSLLNGGTLVICPDevkLDPAALYDLILKS-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 291 pRINVFMAVPTIYTKLMDYYDKHFTQPhvqdfvravceEKIRLMVSGSAALPLpvleKWKNitghTLLER---------- 360
Cdd:cd17650 185 -RITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDFK----TLAARfgqgmriins 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTEIGMALSNPLTVAARLPGS----VGTPLPGVEVQIVSE--NPQKEGCpyilhaegnekdtrvtpgfkekEGELLVR 434
Cdd:cd17650 245 YGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDErlQPQPVGV----------------------AGELYIG 302
|
410 420
....*....|....*....|..
gi 946754379 435 GPTVFREYWGKPEETKKAFTSD 456
Cdd:cd17650 303 GAGVARGYLNRPELTAERFVEN 324
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-456 |
2.99e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQeicRLLEC-AGQDLqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAH---RLIALgVGPEV---LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAGQEYVELLsPVVRKLGVPLLPLPPAVYNGAAEEH-GVRELPerdwrDRGAMIIYTSGTTGRPKGV 218
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARL-PLPDGLRSLVLDQEDDWLEGYSDSNpAVNLAP-----QNLAYVIYTSGSTGRPKGA 1736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 219 LSTHHNIRAVVTGLVHKWAWTKDDVILHVLPlHHVHGVVNKLLCPLWVGATCVMLPeFSAQLVWEKFLSS-ETPRINVFM 297
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQLIQLiERQQVTTLH 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 298 AVPTIYTKLMDyYDKHFTQPhvqdfvravceEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSNPLTV 376
Cdd:PRK12467 1815 FVPSMLQQLLQ-MDEQVEHP-----------LSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDVTHWTCR 1882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 377 AARLPGS----VGTPLPGVEVQIVSE--NPQKEGCPyilhaegnekdtrvtpgfkekeGELLVRGPTVFREYWGKPEETK 450
Cdd:PRK12467 1883 RKDLEGRdsvpIGQPIANLSTYILDAslNPVPIGVA----------------------GELYLGGVGLARGYLNRPALTA 1940
|
....*.
gi 946754379 451 KAFTSD 456
Cdd:PRK12467 1941 ERFVAD 1946
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
55-458 |
3.99e-16 |
|
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: 81.20 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGD-----VVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVlagqeyvellspvvrklgvpllplppaVYNGAAEEhgvrelperdwrdrGAMIIYTSGTTGR 214
Cdd:cd17653 81 LPSARIQAILRTSGATLL---------------------------LTTDSPDD--------------LAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 215 PKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVmLPEFSAQlvwekfLSSETPRIN 294
Cdd:cd17653 120 PKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDAC-IGEIFSTLCNGGTLV-LADPSDP------FAHVARTVD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 295 VFMAVPTIYTKLmdyydkhftqpHVQDFVRavceekIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTEIGMAlsnpL 374
Cdd:cd17653 192 ALMSTPSILSTL-----------SPQDFPN------LKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTIS----S 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 375 TVAARLPG---SVGTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKK 451
Cdd:cd17653 249 TMTELLPGqpvTIGKPIPNSTC-------------YILDADLQP----VPEG---VVGEICISGVQVARGYLGNPALTAS 308
|
....*..
gi 946754379 452 AFTSDGW 458
Cdd:cd17653 309 KFVPDPF 315
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
30-468 |
4.35e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 81.59 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 30 IRHGGSRPLHVALAaRSDKsapvfTRALAFGDRVALVDQHGVHtykdlycrsLRlsqeicrllecAGQDLQEERISFMCS 109
Cdd:PRK05857 21 FEQARQQPEAIALR-RCDG-----TSALRYRELVAEVGGLAAD---------LR-----------AQSVSRGSRVLVISD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 110 NDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHG 189
Cdd:PRK05857 75 NGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 190 vrelPERDW--------RDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHK---WA-WTKDDVILHVLPLHHVHGVV 257
Cdd:PRK05857 155 ----LDAASlagnadqgSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnWVtWVVGETTYSPLPATHIGGLW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 258 NKLLCpLWVGATCVMLPEFSAQLVweKFLSSEtpRINVFMAVPTIYTKLMdyYDKHFTqphvqdfvrAVCEEKIRLMV-S 336
Cdd:PRK05857 231 WILTC-LMHGGLCVTGGENTTSLL--EILTTN--AVATTCLVPTLLSKLV--SELKSA---------NATVPSLRLVGyG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 337 GSAALPLPVleKWKNITGHTLLERYGMTEIG-MALSNPL---TVAARLPGSVGTPLPGVEVQIVSENpqkEGCPyilhae 412
Cdd:PRK05857 295 GSRAIAADV--RFIEATGVRTAQVYGLSETGcTALCLPTddgSIVKIEAGAVGRPYPGVDVYLAATD---GIGP------ 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 946754379 413 gNEKDTRVTPGFkekeGELLVRGPTVFREYWGKPEETKKAFTsDGWFKTACLLVTR 468
Cdd:PRK05857 364 -TAPGAGPSASF----GTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERR 413
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
203-461 |
4.62e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.63 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVL---PLHHVHGvVNKLLCP-LWVGATCVM-----L 273
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMG-GNANFNGlLWGGGTLYIddgkpL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 274 PEFSAQLVweKFLSSETPRinVFMAVPTIYTKLMDYYDKhftqphvQDFVRAVCEEKIRLMVSGSAALPLPVLEKWK--- 350
Cdd:PRK12582 302 PGMFEETI--RNLREISPT--VYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQala 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 351 -NITGH--TLLERYGMTEIGmalsnPLTV----AARLPGSVGTPLPGVEVQIVSenpqkEGCPYilhaegnekdtrvtpg 423
Cdd:PRK12582 371 vRTTGHriPFYTGYGATETA-----PTTTgthwDTERVGLIGLPLPGVELKLAP-----VGDKY---------------- 424
|
250 260 270
....*....|....*....|....*....|....*...
gi 946754379 424 fkekegELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK12582 425 ------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRL 456
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
200-461 |
6.38e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 81.23 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHK-WAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP---- 274
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSapvt 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 EFSAQLVWEKFLSSetprinVFMAVPTIYTKLMDYYDKhftqphvqDFVRAVceekiRLMVSGSAALPLPVLEKWKNITG 354
Cdd:PRK06060 225 PEAAAILSARFGPS------VLYGVPNFFARVIDSCSP--------DSFRSL-----RCVVSAGEALELGLAERLMEFFG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HT-LLERYGMTEIGMA-LSNplTVAARLPGSVGTPLPGVEVQIVSENPQKEGcpyilhaegnekdtrvtPGFkekEGELL 432
Cdd:PRK06060 286 GIpILDGIGSTEVGQTfVSN--RVDEWRLGTLGRVLPPYEIRVVAPDGTTAG-----------------PGV---EGDLW 343
|
250 260
....*....|....*....|....*....
gi 946754379 433 VRGPTVFREYWGKPEETkkaFTSDGWFKT 461
Cdd:PRK06060 344 VRGPAIAKGYWNRPDSP---VANEGWLDT 369
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
25-442 |
7.67e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 80.74 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 25 RQLAPIRHGGSRPLHVALAARSDksapvftralafGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERI 104
Cdd:PRK07788 40 RLAADIRRYGPFAGLVAHAARRA------------PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAG-----DGV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 105 SFMCSNDVSYVVAQWASWMSGGIAVPL---FRKhPQadLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPL--LPLPPA 179
Cdd:PRK07788 103 AVLARNHRGFVLALYAAGKVGARIILLntgFSG-PQ--LAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRawGGNPDD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 180 VYNGAAEEHGVRELPERD-------WRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHH 252
Cdd:PRK07788 180 DEPSGSTDETLDDLIAGSstaplpkPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 253 VHGVVNKLLCpLWVGATCVMLPEFSAQLVWEkflSSETPRINVFMAVPTIYTKLMDYYDKHFTQPHVQdfvravceeKIR 332
Cdd:PRK07788 260 ATGWAHLTLA-MALGSTVVLRRRFDPEATLE---DIAKHKATALVVVPVMLSRILDLGPEVLAKYDTS---------SLK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 333 LMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMAlsnplTVA-----ARLPGSVGTPLPGVEVQIVSENpqkegcpy 407
Cdd:PRK07788 327 IIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFA-----TIAtpedlAEAPGTVGRPPKGVTVKILDEN-------- 393
|
410 420 430
....*....|....*....|....*....|....*
gi 946754379 408 ilhaegnekDTRVTPGfkeKEGELLVRGPTVFREY 442
Cdd:PRK07788 394 ---------GNEVPRG---VVGRIFVGNGFPFEGY 416
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
73-461 |
7.81e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 80.17 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05971 8 TFKELKTASNRFA----NVLKEIGLE-KGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAgqeyvellspvvrklgvpllplppavyngaaeehgvrelperDWRDRGAMIIYTSGTTGRPKGVLSTHHNI--RAVVT 230
Cdd:cd05971 83 VT------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLlgHLPGV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 231 GLVHK--------------WAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQlvwekflssetpriNVF 296
Cdd:cd05971 121 QFPFNlfprdgdlywtpadWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVT--------------TAF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 297 MavPTIYTKLMdyydkHFTQPHVQDFVRavceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTV 376
Cdd:cd05971 187 L--PPTALKMM-----RQQGEQLKHAQV-----KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 377 AARLPGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGfkeKEGELLVR--GPTVFREYWGKPEETKKAFT 454
Cdd:cd05971 255 FPIKPGSMGKPIPGHRVAIV-----------------DDNGTPLPPG---EVGEIAVElpDPVAFLGYWNNPSATEKKMA 314
|
....*..
gi 946754379 455 SDgWFKT 461
Cdd:cd05971 315 GD-WLLT 320
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
61-456 |
8.11e-16 |
|
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: 80.17 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQeicrLLECAGqdLQEERISFMC-SNDVSYVVAQWASWMSGGIAVPLFRKHPQAD 139
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAH----YLQSLG--VKSESLVGICvERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 140 LEYFIQDSRSSVVLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVL 219
Cdd:cd17644 89 LTYILEDAQISVLLTQPENL-------------------------------------------AYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 STHHNIRAVVTGLVHKWAWTKDDVILHVLPLhhVHGVVNKLLCPLWV-GATCVMLPE---FSAQLVWEKflsSETPRINV 295
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTLLsGATLVLRPEemrSSLEDFVQY---IQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 296 FmAVPTIYTKLMdyydkhftqphVQDFVRAVCE--EKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTE--IGMA 369
Cdd:cd17644 201 L-SLPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEatIAAT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 370 LSNP--LTVAARLPGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrVTPGFKekeGELLVRGPTVFREYWGKPE 447
Cdd:cd17644 269 VCRLtqLTERNITSVPIGRPIANTQVYILDENLQP-----------------VPVGVP---GELHIGGVGLARGYLNRPE 328
|
....*....
gi 946754379 448 ETKKAFTSD 456
Cdd:cd17644 329 LTAEKFISH 337
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
205-461 |
9.13e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 80.32 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEk 284
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 285 flSSETPRINVFMAVPTIYTKLM-----DYYDKhftqphvqdfvravceEKIRLMVSGSAALP-LPVLEKWKNITGHTLL 358
Cdd:PRK06145 233 --AIERHRLTCAWMAPVMLSRVLtvpdrDRFDL----------------DSLAWCIGGGEKTPeSRIRDFTRVFTRARYI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 359 ERYGMTEigMALSNPLTVAAR---LPGSVGTPLPGVEVQIVSEnpqkegcpyilhaegnekDTRVTPgfKEKEGELLVRG 435
Cdd:PRK06145 295 DAYGLTE--TCSGDTLMEAGReieKIGSTGRALAHVEIRIADG------------------AGRWLP--PNMKGEICMRG 352
|
250 260
....*....|....*....|....*.
gi 946754379 436 PTVFREYWGKPEETKKAFTsDGWFKT 461
Cdd:PRK06145 353 PKVTKGYWKDPEKTAEAFY-GDWFRS 377
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
61-458 |
9.30e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 80.21 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYcrslRLSQEICRLLEcaGQDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWF----ESVCKVANWLN--EKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGQEYVELLSpvvrklGVPLLPLPPAVYNGAAEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLS 220
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLP------DEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVH---GVVNKllcpLWVGATCVMLPEFSAQLVWEKFlssETPRINVFM 297
Cdd:PRK07638 164 AQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAIST----LYVGQTVHLMRKFIPNQVLDKL---ETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 298 AVPTIYTKLMDyydkhftqphvqdfVRAVCEEKIRLMVSGsAALPLPVLEKWKNITGH-TLLERYGMTEIGMALSNPLTV 376
Cdd:PRK07638 237 TVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYGASELSFVTALVDEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 377 AARLPGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKaFTSD 456
Cdd:PRK07638 302 SERRPNSVGRPFHNVQVRIC-----------------NEAGEEVQKG---EIGTVYVKSPQFFMGYIIGGVLARE-LNAD 360
|
..
gi 946754379 457 GW 458
Cdd:PRK07638 361 GW 362
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
110-458 |
9.83e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 80.13 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 110 NDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAgqeYVELLSPV-------VRKLGVPLLPLPPAVYn 182
Cdd:PRK12406 45 NDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHGLasalpagVTVLSVPTPPEIAAAY- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 183 GAAEEHgvRELPE--RDWRD---------------RGAMIiYTSGTTGRPKGV---------LSTHHNIRAVVTGLvhkw 236
Cdd:PRK12406 121 RISPAL--LTPPAgaIDWEGwlaqqepydgppvpqPQSMI-YTSGTTGHPKGVrraaptpeqAAAAEQMRALIYGL---- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 237 awTKDDVILHVLPLHH----VHGVVNKLLcplwvGATCVMLPEFSAqlvwEKFLSS-ETPRI-NVFMaVPTIYTKLMDYY 310
Cdd:PRK12406 194 --KPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDP----EELLQLiERHRItHMHM-VPTMFIRLLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 311 DKhftqphvqdfVRAVCE-EKIRLMVSGSAALPLPV----LEKWknitGHTLLERYGMTEIGMALSNPLTVAARLPGSVG 385
Cdd:PRK12406 262 EE----------VRAKYDvSSLRHVIHAAAPCPADVkramIEWW----GPVIYEYYGSTESGAVTFATSEDALSHPGTVG 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 946754379 386 TPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGFKekeGELLVRGPTV--FrEYWGKPEEtKKAFTSDGW 458
Cdd:PRK12406 328 KAAPGAELRFVDE-------------DGRP----LPQGEI---GEIYSRIAGNpdF-TYHNKPEK-RAEIDRGGF 380
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
203-460 |
1.03e-15 |
|
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: 80.55 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDD--VILHVLPLHHVHGVVNKLLCPLWVGATCVM-----LPE 275
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkpMPG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 276 FSAQLVweKFLSSETPriNVFMAVPTIYTKLMDYYDKhftqphvQDFVRAVCEEKIRLMVSGSAALPLPVLEKWKNI--- 352
Cdd:cd05921 248 GFEETL--RNLREISP--TVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALava 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 353 -TGH--TLLERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtrvtpgfkekeg 429
Cdd:cd05921 317 tVGEriPMMAGLGATETAPTATFTHWPTER-SGLIGLPAPGTELKLVPSGGKY--------------------------- 368
|
250 260 270
....*....|....*....|....*....|.
gi 946754379 430 ELLVRGPTVFREYWGKPEETKKAFTSDGWFK 460
Cdd:cd05921 369 EVRVKGPNVTPGYWRQPELTAQAFDEEGFYC 399
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
73-462 |
1.05e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.83 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEicrLLECAGQDlqEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:PLN02614 81 TYQEVYDIVIKLGNS---LRSVGVKD--EAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYV-----------ELLSPVVRKLGVPLLPLPPAVYNGAA----------EEHGVRELPERDWRDRgAMIIYTSGT 211
Cdd:PLN02614 156 FVEEKKIselfktcpnstEYMKTVVSFGGVSREQKEEAETFGLViyawdeflklGEGKQYDLPIKKKSDI-CTIMYTSGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 212 TGRPKGVLSTHHNIRAVVTGLVH-----KWAWTKDDVILHVLPLHHVHGVVNKlLCPLWVGATcVMLPEFSAQLVWEKfL 286
Cdd:PLN02614 235 TGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDRVIE-ECFIQHGAA-IGFWRGDVKLLIED-L 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 287 SSETPRInvFMAVP----TIYT----KLMD-------YYDKHFT---------QPHVQ----------DFVRAVCEEKIR 332
Cdd:PLN02614 312 GELKPTI--FCAVPrvldRVYSglqkKLSDggflkkfVFDSAFSykfgnmkkgQSHVEasplcdklvfNKVKQGLGGNVR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 333 LMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTVAARLPGSVGTPLPGVEVQIvsenpqkEGCPyilhaE 412
Cdd:PLN02614 390 IILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRL-------ESVP-----E 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 946754379 413 GNEKDTRVTPgfkekEGELLVRGPTVFREYWGKPEETKKAFTsDGWFKTA 462
Cdd:PLN02614 458 MEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTG 501
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
61-459 |
1.17e-15 |
|
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: 79.67 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSQEicrlLECAGQdLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAAR----LRAAGV-GPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGqeyvellspvvrklgvpllplppavyngaaeehgvrelperdwRDRGAMIIYTSGTTGRPKGVLS 220
Cdd:cd12115 89 RFILEDAQARLVLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVtglvhKWAwtkddviLHVLPLHHVHGV-----------VNKLLCPLWVGATCVM------LPEFSAQlvwe 283
Cdd:cd12115 126 EHRNAAAFL-----QWA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVLadnvlaLPDLPAA---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 kflsSETPRINvfmAVPTIYTKLMDyydkhftQPHVQDFVRAVCeekirlmvsgSAALPLP---VLEKWKNITGHTLLER 360
Cdd:cd12115 190 ----AEVTLIN---TVPSAAAELLR-------HDALPASVRVVN----------LAGEPLPrdlVQRLYARLQVERVVNL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTE-IGMALSNPLTVAARLPGSVGTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrVTPGFKekeGELLVRGPTVF 439
Cdd:cd12115 246 YGPSEdTTYSTVAPVPPGASGEVSIGRPLANTQA-------------YVLDRALQP----VPLGVP---GELYIGGAGVA 305
|
410 420
....*....|....*....|
gi 946754379 440 REYWGKPEETKKAFTSDGWF 459
Cdd:cd12115 306 RGYLGRPGLTAERFLPDPFG 325
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
192-461 |
2.81e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 79.12 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 192 ELPERDwRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVH-----KWAWTKDDVILHVLPLHHVHGVVNKLLCpLWV 266
Cdd:PLN02861 213 ELPPKQ-KTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 267 GATCVMlpefsaqlvWE---KFLSSETPRI--NVFMAVPTIY------------------TKLMDY--------YDKHFT 315
Cdd:PLN02861 291 GASIGF---------WQgdiRYLMEDVQALkpTIFCGVPRVYdriytgimqkissggmlrKKLFDFaynyklgnLRKGLK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 316 QPHVQDFVRAVCEEKI--------RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNPLTVAARLPGSVGTP 387
Cdd:PLN02861 362 QEEASPRLDRLVFDKIkeglggrvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVP 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946754379 388 LPGVEVQIVSenpqkegCPYIlhaeGNEKDTRVtpgfkeKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PLN02861 442 MTTIEARLES-------VPEM----GYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHT 497
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
56-468 |
3.27e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 78.63 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFG--DRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFR 133
Cdd:PRK06164 18 AHARArpDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGD-----RVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQADLEYFIQDSRSSVV--------------LAGQEYVELLS----PVVRKLGVPLLPLPPAVYNGAAEEHGVRELP- 194
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLvvwpgfkgidfaaiLAAVPPDALPPlraiAVVDDAADATPAPAPGARVQLFALPDPAPPAa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 195 ---ERDWRDRGAMIIYTSGTTGRPKGVLsthHNIRAVVTglvHKWA------WTKDDVILHVLPLHHVHGvVNKLLCPLW 265
Cdd:PRK06164 173 ageRAADPDAGALLFTTSGTTSGPKLVL---HRQATLLR---HARAiaraygYDPGAVLLAALPFCGVFG-FSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 266 VGATCVMLPEFSAQLVWEKFLSSetpRINVFMAVPTIYTKLMDyydkhfTQPHVQDFVRAvceekiRLMVSGSAALPLPV 345
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRH---RVTHTFGNDEMLRRILD------TAGERADFPSA------RLFGFASFAPALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 346 LEKWKNITGHTLLERYGMTE-IGMALSNPLT--VAARLPGSvGTPL-PGVEVQIVseNPQKEG-CPyilhaegnekdtrv 420
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEvQALVALQPATdpVSVRIEGG-GRPAsPEARVRAR--DPQDGAlLP-------------- 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 946754379 421 tPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKTACLLVTR 468
Cdd:PRK06164 374 -DG---ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTR 417
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
192-458 |
2.48e-14 |
|
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: 75.49 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 192 ELPERDWRdrGAMIIYTSGTTGRPKGVLStHHNIRAVVTGLVHKWA----WTKDDVILHVLPLHHV--HGVVNKllcPLW 265
Cdd:cd05929 119 TPIEDEAA--GWKMLYSGGTTGRPKGIKR-GLPGGPPDNDTLMAAAlgfgPGADSVYLSPAPLYHAapFRWSMT---ALF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 266 VGATCVMLPEFSAqlvwEKFLSS-ETPRINVFMAVPTIYTKLMDYYDKhftQPHVQDFvravceEKIRLMVSGSAALPLP 344
Cdd:cd05929 193 MGGTLVLMEKFDP----EEFLRLiERYRVTFAQFVPTMFVRLLKLPEA---VRNAYDL------SSLKRVIHAAAPCPPW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 345 VLEKWKNITGHTLLERYGMTE-IGMALSNP---LTvaarLPGSVGTPLPGvEVQIVSENpqkegcpyilhaeGNEKDTRV 420
Cdd:cd05929 260 VKEQWIDWGGPIIWEYYGGTEgQGLTIINGeewLT----HPGSVGRAVLG-KVHILDED-------------GNEVPPGE 321
|
250 260 270
....*....|....*....|....*....|....*...
gi 946754379 421 TpgfkekeGELLVRGPTVFrEYWGKPEETKKAFTSDGW 458
Cdd:cd05929 322 I-------GEVYFANGPGF-EYTNDPEKTAAARNEGGW 351
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-283 |
5.15e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.92 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 58 AFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDLQEeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQ 137
Cdd:PRK07798 15 AVPDRVALVCGDRRLTYAELEERANRLA----HYLIAQGLGPGD-HVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 138 ADLEYFIQDSRSSVVLAGQEYVELLSPVVRKL-----------GVPLLPLPPAV-YNGA-AEEHGVRELPERDWRDRgaM 204
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREFAPRVAEVLPRLpklrtlvvvedGSGNDLLPGAVdYEDAlAAGSPERDFGERSPDDL--Y 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAV-------VTG--------LVHKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGAT 269
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIFRVllggrdfATGepiedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAA-LFSGQT 246
|
250
....*....|....*.
gi 946754379 270 CVMLP--EFSAQLVWE 283
Cdd:PRK07798 247 VVLLPdvRFDADEVWR 262
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
5-457 |
7.81e-14 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 74.41 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 5 AAVPPRVVMTFQRLVCALASRQLAPIRhgGSRPLHVALAARSDKSAPvfTRALAFG-----DRVALVDQHGVHTYKDLYC 79
Cdd:PRK13382 1 AGIKDRLRDTLGLIATLRRAGLIAPMR--PDRYLRIVAAMRREGMGP--TSGFAIAaqrcpDRPGLIDELGTLTWRELDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 80 RSLRLSQEICRLlecagQDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYV 159
Cdd:PRK13382 77 RSDALAAALQAL-----PIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 160 ELLS------PVVRKLGVPLLPLPPAVYNGAAEEHGVRELPERDwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLV 233
Cdd:PRK13382 152 ATVDraladcPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTG--RKGRVILLTSGTTGTPKGARRSGPGGIGTLKAIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 234 HKWAWTKDDVILHVLPLHHVHGVVNkLLCPLWVGATCVML----PEFSAQLVwekflssETPRINVFMAVPTIYTKLMDY 309
Cdd:PRK13382 230 DRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRrrfdPEATLDLI-------DRHRATGLAVVPVMFDRIMDL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 310 ydkhftqphVQDFVRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGM-ALSNPLTVAARlPGSVGTPL 388
Cdd:PRK13382 302 ---------PAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMiATATPADLRAA-PDTAGRPA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 389 PGVEVQivsenpqkegcpyILHAEGNEkdtrVTPGfkeKEGELLVRGPTVFREYW-GKPEETKKAFTSDG 457
Cdd:PRK13382 372 EGTEIR-------------ILDQDFRE----VPTG---EVGTIFVRNDTQFDGYTsGSTKDFHDGFMASG 421
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
205-461 |
9.00e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 74.47 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTGL-----VHKWAWTKDDVILHVLPLHHV-------------------HGVVNKL 260
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 261 LCPLWvgatcVMLPEFSAQL--VWEKF-------LSSETP-RINVFMAVPTIYTKLMDYYDKHFTQPHVQDF-----VRA 325
Cdd:PLN02430 305 RDDLM-----ELKPTLLAGVprVFERIhegiqkaLQELNPrRRLIFNALYKYKLAWMNRGYSHKKASPMADFlafrkVKA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 326 VCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI--GMALSNPLTVAarLPGSVGTPLPGVEVQIvSENPQKE 403
Cdd:PLN02430 380 KLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFPDEMC--MLGTVGAPAVYNELRL-EEVPEMG 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 946754379 404 GCPYilhaeGNekdtrvtpgfkEKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PLN02430 457 YDPL-----GE-----------PPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHT 497
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
200-442 |
1.22e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 73.98 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 274
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 275 EFSAQLVWEKflssetpRINVFMAVPTIytkLMDYydKHFTQPHvqDFVRavceekIRLMVSGSAALPLPVLEKWKNITG 354
Cdd:PRK08043 445 RIVPELVYDR-------NCTVLFGTSTF---LGNY--ARFANPY--DFAR------LRYVVAGAEKLQESTKQLWQDKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HTLLERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIVSenpqkegcpyilhaegnekdtrvTPGFkEKEGELLVR 434
Cdd:PRK08043 505 LRILEGYGVTECAPVVSINVPMAAK-PGTVGRILPGMDARLLS-----------------------VPGI-EQGGRLQLK 559
|
....*...
gi 946754379 435 GPTVFREY 442
Cdd:PRK08043 560 GPNIMNGY 567
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
203-461 |
1.24e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 73.63 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHN--IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQ 279
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 280 LVWEkFLSSEtpRINVFMAVPTIYTKLMDYYDKH-FTQPHvqdfvravceekIRLMVSGSAALPLPVLEKWKNItGHTLL 358
Cdd:PRK06018 259 SVYE-LLDTE--KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDM-GVEVR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 359 ERYGMTEIgmalsNPLTVAARLPGsvgtPLPGVEVQIVSENPQKEG-CPYILHAEGNEKDTRVTPGFKEKEGELLVRGPT 437
Cdd:PRK06018 323 HAWGMTEM-----SPLGTLAALKP----PFSKLPGDARLDVLQKQGyPPFGVEMKITDDAGKELPWDGKTFGRLKVRGPA 393
|
250 260
....*....|....*....|....
gi 946754379 438 VFREYWGkpeETKKAFTSDGWFKT 461
Cdd:PRK06018 394 VAAAYYR---VDGEILDDDGFFDT 414
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
73-461 |
1.32e-13 |
|
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: 73.68 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLrlsQEICRLLECAGQDLQEerISFMCSNDVSYVVAQWASWMSGGIAVPLfrkhpqadleyfiqdsrssVV 152
Cdd:cd05908 17 SYRHLREEAL---GYLGALQELGIKPGQE--VVFQITHNNKFLYLFWACLLGGMIAVPV-------------------SI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEYVELLSPVVRKLGVPLLPlppavyngaAEEHGVRELPerdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL 232
Cdd:cd05908 73 GSNEEHKLKLNKVWNTLKNPYLI---------TEEEVLCELA-----DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 233 VHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefsaqlvwekflssetprINVFMAVPTIYTKLMDYYD- 311
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP------------------TRLFIRRPILWLKKASEHKa 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 312 -----KHFTQPHVQDFVRAVCEEK-----IRLMVSGSAALPLPVLEKW-KNITGHTL-----LERYGMTEIGMALSNP-- 373
Cdd:cd05908 201 tivssPNFGYKYFLKTLKPEKANDwdlssIRMILNGAEPIDYELCHEFlDHMSKYGLkrnaiLPVYGLAEASVGASLPka 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 374 -------------LTVAARLPG------------SVGTPLPGVEVQIVSEnpQKEGCP--YILHAEGNEKDtrVTPGfke 426
Cdd:cd05908 281 qspfktitlgrrhVTHGEPEPEvdkkdsecltfvEVGKPIDETDIRICDE--DNKILPdgYIGHIQIRGKN--VTPG--- 353
|
410 420 430
....*....|....*....|....*....|....*
gi 946754379 427 kegellvrgptvfreYWGKPEETKKAFTSDGWFKT 461
Cdd:cd05908 354 ---------------YYNNPEATAKVFTDDGWLKT 373
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-456 |
1.34e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.61 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSQeicRLLECA-GQDLQeerISFMCSNDVSYVVAQWASWMSGGIAVPLFR 133
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAH---RLIERGvGPDVL---VGVAVERSLEMVVGLLAILKAGGAYVPLDP 3139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLplppavyngaAEEHGVRELPERDWRDRGAMIIYTSGTTG 213
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRG----------DENYAEANPAIRTMPENLAYVIYTSGSTG 3209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSETPRI 293
Cdd:PRK12316 3210 KPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGV 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVFMAVPTIYTKLmdyydkhFTQPHVQDFVravceeKIRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGMAlSNP 373
Cdd:PRK12316 3289 DVLHAYPSMLQAF-------LEEEDAHRCT------SLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATIT-VTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 374 LTVAARLPGS--VGTPLPGVEVqivsenpqkegcpYILhaegnekDTRVTPGFKEKEGELLVRGPTVFREYWGKPEETKK 451
Cdd:PRK12316 3353 WQCVEEGKDAvpIGRPIANRAC-------------YIL-------DGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAE 3412
|
....*
gi 946754379 452 AFTSD 456
Cdd:PRK12316 3413 RFVPD 3417
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-456 |
1.62e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVAlvdqhgvhTYKDLYCRSLRLSQeicRLLECA-GQDLqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:PRK12316 529 ALAFGEETL--------DYAELNRRANRLAH---ALIERGvGPDV---LVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAgQEYVELLSPVVRKLGVPLLPLPPAVYNGAAEEHGVREL-PERDwrdrgAMIIYTSGTTG 213
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLLS-QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELnPENL-----AYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPE---FSAQLVWEkflSSET 290
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPgdhRDPAKLVE---LINR 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 291 PRINVFMAVPTIytklmdyydkhfTQPHVQDFVRAVCEEkIRLMVSGSAALPLPVLEK--WKNITGHtLLERYGMTE--I 366
Cdd:PRK12316 745 EGVDTLHFVPSM------------LQAFLQDEDVASCTS-LRRIVCSGEALPADAQEQvfAKLPQAG-LYNLYGPTEaaI 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 367 GMALSNPLTVAARLPgSVGTPLPGVevqivsenpqkeGCpYILHAEGNEKDTRVTpgfkekeGELLVRGPTVFREYWGKP 446
Cdd:PRK12316 811 DVTHWTCVEEGGDSV-PIGRPIANL------------AC-YILDANLEPVPVGVL-------GELYLAGRGLARGYHGRP 869
|
410
....*....|
gi 946754379 447 EETKKAFTSD 456
Cdd:PRK12316 870 GLTAERFVPS 879
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
56-461 |
2.18e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.92 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVDQHgvhtykdlycRSLRLS----QEICRLLECA--------GqdlqeERISFMCSNDVSYVVAQWASWM 123
Cdd:PRK08315 26 AARYPDREALVYRD----------QGLRWTyrefNEEVDALAKGllalgiekG-----DRVGIWAPNVPEWVLTQFATAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 124 SGGIAV---PLFRKHpqaDLEYFIQDSRSS-VVLAGQ----EYVELLSPVVRKLGVPLLPLPPA---------VYNGAAE 186
Cdd:PRK08315 91 IGAILVtinPAYRLS---ELEYALNQSGCKaLIAADGfkdsDYVAMLYELAPELATCEPGQLQSarlpelrrvIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 187 EHGVRELPErdWRDRGAM--------------------IIYTSGTTGRPKGVLSTHHNI--------RAVvtGLVHKwaw 238
Cdd:PRK08315 168 HPGMLNFDE--LLALGRAvddaelaarqatldpddpinIQYTSGTTGFPKGATLTHRNIlnngyfigEAM--KLTEE--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 239 tkDDVILHVlPLHHVHGVVNKLLCPLWVGATCV-MLPEFSAQLVWEkflSSETPRINVFMAVPTIYTKLMDYYD-KHFtq 316
Cdd:PRK08315 241 --DRLCIPV-PLYHCFGMVLGNLACVTHGATMVyPGEGFDPLATLA---AVEEERCTALYGVPTMFIAELDHPDfARF-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 317 phvqDFVRavceekIRLMVSGSAALPLPVLEKwknitghtLLERYGMTEI----GMALSNPLTVAARL--P-----GSVG 385
Cdd:PRK08315 313 ----DLSS------LRTGIMAGSPCPIEVMKR--------VIDKMHMSEVtiayGMTETSPVSTQTRTddPlekrvTTVG 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 946754379 386 TPLPGVEVQIVSEnpqkegcpyilhAEGNEkdtrVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK08315 375 RALPHLEVKIVDP------------ETGET----VPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHT 431
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
55-464 |
3.29e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.28 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALV------DQHGVHTYKDLYCRSlrlsqeicRLLECAGQDLQE--ERISFMCSNDVSYVVAQWASWMSGG 126
Cdd:PRK05691 18 RAAQTPDRLALRfladdpGEGVVLSYRDLDLRA--------RTIAAALQARASfgDRAVLLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 127 IAVPLF-----RKHPQADLEYFIQDSRSSVVLAgqeyVELLSPVVRKLGVPLLPlppavynGAAEEHGVRELPE---RDW 198
Cdd:PRK05691 90 IAVPAYppesaRRHHQERLLSIIADAEPRLLLT----VADLRDSLLQMEELAAA-------NAPELLCVDTLDPalaEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 199 R------DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWA--WTKDDVILHVLPLHHVHGVVNKLLCPLWVGATC 270
Cdd:PRK05691 159 QepalqpDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 V-MLPEFsaqlvwekflssetprinvFMAVPTIYTKLMDYYDKhfTQPHVQDFVRAVCEEKI-------------RLMVS 336
Cdd:PRK05691 239 VlMSPAY-------------------FLERPLRWLEAISEYGG--TISGGPDFAYRLCSERVsesalerldlsrwRVAYS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 337 GSAALPLPVLEKWKN------ITGHTLLERYGMTEIGMALSN--------PLTVAARL-------PG------SVGTPLP 389
Cdd:PRK05691 298 GSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGgrrgqgipALELDAEAlarnraePGtgsvlmSCGRSQP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 946754379 390 GVEVQIVsENPQKEGCPyilhaegnekDTRVtpgfkekeGELLVRGPTVFREYWGKPEETKKAFTS-DG--WFKTACL 464
Cdd:PRK05691 378 GHAVLIV-DPQSLEVLG----------DNRV--------GEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDL 436
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
144-283 |
5.57e-13 |
|
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: 71.55 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 144 IQDSRSSVVLAG---QEYVELLSPVVRKLGVPLLplppaVYNGAAEEHGVR-----------ELPERDWRDR-----GAM 204
Cdd:cd05938 74 FRCCGAKVLVVApelQEAVEEVLPALRADGVSVW-----YLSHTSNTEGVIslldkvdaasdEPVPASLRAHvtiksPAL 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVvTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWE 283
Cdd:cd05938 149 YIYTSGTTGLPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD 226
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
73-461 |
5.86e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 71.65 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSqeicRLLECAGqdLQE-ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSV 151
Cdd:PRK13391 26 TYRELDERSNRLA----HLFRSLG--LKRgDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 152 VL---AGQEYVELLS---PVVRKLGVPLLPLPPAVYNGAAEehGVRELPERDWRD--RGAMIIYTSGTTGRPKGVL---- 219
Cdd:PRK13391 100 LItsaAKLDVARALLkqcPGVRHRLVLDGDGELEGFVGYAE--AVAGLPATPIADesLGTDMLYSSGTTGRPKGIKrplp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 220 ----STHHNIRAVVTGLvhkWAWTKDDVILHVLPLHHVH-----GVVNKLlcplwvGATCVMLPEFSAqlvwEKFLSS-E 289
Cdd:PRK13391 178 eqppDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHFDA----EQYLALiE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 290 TPRINVFMAVPTIYTKLM-------DYYDkhftqphVQDFVRAVceekirlmvsgSAALPLPVLEKWKNIT--GHTLLER 360
Cdd:PRK13391 245 EYGVTHTQLVPTMFSRMLklpeevrDKYD-------LSSLEVAI-----------HAAAPCPPQVKEQMIDwwGPIIHEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTE-IGMALSNPLTVAARlPGSVGTPLPGVevqivsenpqkegcPYILHAEGNEkdtrVTPGfkeKEGELLVRGPTVF 439
Cdd:PRK13391 307 YAATEgLGFTACDSEEWLAH-PGTVGRAMFGD--------------LHILDDDGAE----LPPG---EPGTIWFEGGRPF 364
|
410 420
....*....|....*....|..
gi 946754379 440 rEYWGKPEETKKAFTSDGWFKT 461
Cdd:PRK13391 365 -EYLNDPAKTAEARHPDGTWST 385
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
51-404 |
6.52e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 71.57 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 51 PVFTRALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGQdlqeeRISFMCSNDVSYVVAQWASWMSGGIAVP 130
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGR-----AVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 131 LFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPpavyngAAEEHGVRELPERDwrdrGAMIIYTSG 210
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATA------GAEESGGRPAVAAP----GRIVLLTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 211 TTGRPKGVLSthhniRAVVTGLVHKWAWTKDDVILHV-------LPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQlvwE 283
Cdd:PRK13383 185 TTGKPKGVPR-----APQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLG-LGMLMLTIALGGTVLTHRHFDAE---A 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KFLSSETPRINVFMAVPTIYTKLMDYYDKhftqphvqdfVRAVCE-EKIRLMVSGSAALPLPVLEKWKNITGHTLLERYG 362
Cdd:PRK13383 256 ALAQASLHRADAFTAVPVVLARILELPPR----------VRARNPlPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYG 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 946754379 363 MTEIGM-ALSNPLTVaARLPGSVGTPLPGVEVQIVSENPQKEG 404
Cdd:PRK13383 326 STEVGIgALATPADL-RDAPETVGKPVAGCPVRILDRNNRPVG 367
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
204-461 |
1.01e-12 |
|
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: 69.64 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNI--RAVVTGLVHkwAWTKDDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQLV 281
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALlaQALVLAVLQ--AIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 WEkFLSSETPRiNVFMAVPTIytklmdyydkhftqphvqDFVRAVCEEKIRLMVSGSAALPLPvlEKWKNITGHTLLER- 360
Cdd:cd17636 81 LE-LIEAERCT-HAFLLPPTI------------------DQIVELNADGLYDLSSLRSSPAAP--EWNDMATVDTSPWGr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 ----YGMTEI-GMALSNPLTVAARlpGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEkdtrVTPGfkeKEGELLVRG 435
Cdd:cd17636 139 kpggYGQTEVmGLATFAALGGGAI--GGAGRPSPLVQVRILDE-------------DGRE----VPDG---EVGEIVARG 196
|
250 260
....*....|....*....|....*.
gi 946754379 436 PTVFREYWGKPEETKKAFTsDGWFKT 461
Cdd:cd17636 197 PTVMAGYWNRPEVNARRTR-GGWHHT 221
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
55-473 |
1.05e-12 |
|
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: 70.65 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGqdLQEERISFMC---SNDVsyVVAQWASWMSGGIAVPL 131
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLA----HHLRSLG--VGPGVFVPLCfekSKWA--VVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 132 FRKHPQADLEYFIQDSRSSVVLAGQEyvellspvvrklgvpllplppavyngaaeehgvrelperdwrDRGAMIIYTSGT 211
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLTSSP------------------------------------------SDAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 212 TGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVlpLHHVHGV-VNKLLCPLWVGAT-CVM--------LPEFSAQLv 281
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQF--ASYTFDVsILEIFTTLAAGGClCIPseedrlndLAGFINRL- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 wekflssetpRINVFMAVPTIyTKLMDyydkhftqPhvQDFVRavceekIRLMVSGSAALPLPVLEKWknITGHTLLERY 361
Cdd:cd05918 195 ----------RVTWAFLTPSV-ARLLD--------P--EDVPS------LRTLVLGGEALTQSDVDTW--ADRVRLINAY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 GMTEIGMALSNPLTVAARLPGSVGTPLPGVevqivsenpqkegcPYILHAEGNEKdtRVTPGFkekEGELLVRGPTVFRE 441
Cdd:cd05918 246 GPAECTIAATVSPVVPSTDPRNIGRPLGAT--------------CWVVDPDNHDR--LVPIGA---VGELLIEGPILARG 306
|
410 420 430
....*....|....*....|....*....|..
gi 946754379 442 YWGKPEETKKAFTSDGWFKTACLLVTRTPFLR 473
Cdd:cd05918 307 YLNDPEKTAAAFIEDPAWLKQEGSGRGRRLYR 338
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
192-475 |
1.25e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 70.58 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 192 ELPERDwrdrGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGL--VHKWAWTKDDVILHVLPLHHV--HGVvnkllcPL--W 265
Cdd:PRK05620 177 ELDETT----AAAICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 266 VGATCVMLP--EFSAQLVwEKFLSSETPRinVFMAVPTIYTKLMDYYDKHftQPhvqdfvravceEKIRL--MVSGSAAL 341
Cdd:PRK05620 247 MSGTPLVFPgpDLSAPTL-AKIIATAMPR--VAHGVPTLWIQLMVHYLKN--PP-----------ERMSLqeIYVGGSAV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 342 PLPVLEKWKnitghtllERYGMTEI---GMALSNPLTVAARLPGSV------------GTPLPGVEVQIVSenpqkegcp 406
Cdd:PRK05620 311 PPILIKAWE--------ERYGVDVVhvwGMTETSPVGTVARPPSGVsgearwayrvsqGRFPASLEYRIVN--------- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 407 yilhaegnekDTRVTPGFKEKEGELLVRGPTVFREYWGKP----------------EETKKAFTSDGWFKTACL-LVTRT 469
Cdd:PRK05620 374 ----------DGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVgSVTRD 443
|
....*.
gi 946754379 470 PFLRRH 475
Cdd:PRK05620 444 GFLTIH 449
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
204-461 |
3.49e-12 |
|
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: 67.82 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWE 283
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLF-LYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KFlssETPRINVFMAVPTIYTKLMDYYDKHftqphvqdfvravceEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYG 362
Cdd:cd17633 83 KI---NQYNATVIYLVPTMLQALARTLEPE---------------SKIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 363 MTEIGMALSNpLTVAARLPGSVGTPLPGVEVqivsenpqkegcpYILHAEGNEkdtrvtpgfkekEGELLVRGPTVFREY 442
Cdd:cd17633 145 TSELSFITYN-FNQESRPPNSVGRPFPNVEI-------------EIRNADGGE------------IGKIFVKSEMVFSGY 198
|
250
....*....|....*....
gi 946754379 443 WGKPEETKkaftsDGWFKT 461
Cdd:cd17633 199 VRGGFSNP-----DGWMSV 212
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
61-456 |
3.97e-12 |
|
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: 68.65 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQdLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLA----RFLREKGV-KKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGQEYVELLSpvvrKLGVPLLPLPPAVYNGAAEEhgvreLPERDWRDRGAMIIYTSGTTGRPKGVLS 220
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKSKLS----FNKSTILLEDPSISQEDTSN-----IDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIravvTGLV-----HKWAWTKDDVILHVLPLHHV--HGVVNKLLcplwVGATCVMLPEFSAQLVWEKFLSSETPRI 293
Cdd:cd17656 149 EHKNM----VNLLhfereKTNINFSDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFDLVKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVfMAVPTIYTKLMdYYDKHFTQPhVQDFVRAVCEEKIRLMVSGsaalPLPVLEKWKNITGHTlleRYGMTE---IGMAL 370
Cdd:cd17656 221 EV-VFLPVAFLKFI-FSEREFINR-FPTCVKHIITAGEQLVITN----EFKEMLHEHNVHLHN---HYGPSEthvVTTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 371 SNPLTVAARLPgSVGTPLPGVEVQIVSENPQKEGCPYIlhaegnekdtrvtpgfkekeGELLVRGPTVFREYWGKPEETK 450
Cdd:cd17656 291 INPEAEIPELP-PIGKPISNTWIYILDQEQQLQPQGIV--------------------GELYISGASVARGYLNRQELTA 349
|
....*.
gi 946754379 451 KAFTSD 456
Cdd:cd17656 350 EKFFPD 355
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
207-461 |
6.51e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 68.19 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 207 YTSGTTGRPKGVLSTHHN--IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQLVWE 283
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KFlssETPRINVFMAVPTIYTKLMDYydkhfTQPHVQDFvravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGM 363
Cdd:PRK07008 262 LI---EAERVTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 364 TEIgmalsNPLTVAARL-------PGSV--------GTPLPGVEVQIVSEnpqkegcpyilhaegnekDTRVTPGFKEKE 428
Cdd:PRK07008 328 TEM-----SPLGTLCKLkwkhsqlPLDEqrkllekqGRVIYGVDMKIVGD------------------DGRELPWDGKAF 384
|
250 260 270
....*....|....*....|....*....|...
gi 946754379 429 GELLVRGPTVFREYWGKPEETkkafTSDGWFKT 461
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASP----LVDGWFPT 413
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
191-442 |
6.58e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.84 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 191 RELPERDWRDRgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATC 270
Cdd:PRK06814 785 VYFCNRDPDDP-AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VMLPefsaqlvwekflsseTP---RInvfmaVPT-IY-----------TKLMDYYDkhftQPHVQDFVRavceekIRLMV 335
Cdd:PRK06814 864 FLYP---------------SPlhyRI-----IPElIYdtnatilfgtdTFLNGYAR----YAHPYDFRS------LRYVF 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 336 SGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MALSNPLtvaARLPGSVGTPLPGVEVQIvsenpqkegcpyilhaeg 413
Cdd:PRK06814 914 AGAEKVKEETRQTWMEKFGIRILEGYGVTETApvIALNTPM---HNKAGTVGRLLPGIEYRL------------------ 972
|
250 260
....*....|....*....|....*....
gi 946754379 414 nEKdtrvTPGFKEKeGELLVRGPTVFREY 442
Cdd:PRK06814 973 -EP----VPGIDEG-GRLFVRGPNVMLGY 995
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
120-461 |
1.09e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.40 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 120 ASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELL---SPVVRKLGVPLLPLPPAVyngaAEEHGVRELPER 196
Cdd:PRK07867 73 AAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdglDPGVRVINVDSPAWADEL----AAHRDAEPPFRV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 197 DWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 276
Cdd:PRK07867 149 ADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 277 SAQlvweKFLssetPRINVFMAVPTIYT-KLMDYYdkhFTQPHVQDfvraVCEEKIRLMVsGSAALPlPVLEKWKNITGH 355
Cdd:PRK07867 229 SAS----GFL----PDVRRYGATYANYVgKPLSYV---LATPERPD----DADNPLRIVY-GNEGAP-GDIARFARRFGC 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 356 TLLERYGMTEIGMALS-NPLTVaarlPGSVGTPLPGVEVQivseNPQK-EGCPyilhaEGNEKDTRVTPGfKEKEGELL- 432
Cdd:PRK07867 292 VVVDGFGSTEGGVAITrTPDTP----PGALGPLPPGVAIV----DPDTgTECP-----PAEDADGRLLNA-DEAIGELVn 357
|
330 340
....*....|....*....|....*....
gi 946754379 433 VRGPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK07867 358 TAGPGGFEGYYNDPEADAERM-RGGVYWS 385
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-456 |
4.20e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 4 DAAVPPRVVMTFQRLV---CALASRQLA--PIRHGGSRPLHVALAARSDKSAP--------VFTRALAFGDRVALVDQHG 70
Cdd:PRK12316 1948 DAAAIERLDRHLLHLLeqmAEDAQAALGelALLDAGERQRILADWDRTPEAYPrgpgvhqrIAEQAARAPEAIAVVFGDQ 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 71 VHTYKDLYCRSLRLSQeicRLLECAGQdlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSS 150
Cdd:PRK12316 2028 HLSYAELDSRANRLAH---RLRARGVG--PEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAA 2102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 151 VVLAGQEYVELLSPV--VRKLGVPLLplppAVYNGAAEEHGVRELPERDWrdrgAMIIYTSGTTGRPKGVLSTHHNIRAV 228
Cdd:PRK12316 2103 LLLTQRHLLERLPLPagVARLPLDRD----AEWADYPDTAPAVQLAGENL----AYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 229 VTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEfsaqlvwEKFLSSETPRINVFMAVPTIytklmd 308
Cdd:PRK12316 2175 CQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGARVLIRDD-------ELWDPEQLYDEMERHGVTIL------ 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 309 yydkHFTQPHVQDFV----RAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEigmALSNPLTVAARLPGS 383
Cdd:PRK12316 2241 ----DFPPVYLQQLAehaeRDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLLWKCRPQDP 2313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 946754379 384 VGTPLPGVEVQIVSENpqkegcPYILHAEGNEKDTRVTpgfkekeGELLVRGPTVFREYWGKPEETKKAFTSD 456
Cdd:PRK12316 2314 CGAAYVPIGRALGNRR------AYILDADLNLLAPGMA-------GELYLGGEGLARGYLNRPGLTAERFVPD 2373
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
61-453 |
1.09e-10 |
|
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: 63.96 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDLQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLA----HYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGqeyvellspvvrklgvpllplppavyngaaeehgVRELperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd17648 78 QFILEDTGARVVITN----------------------------------STDL---------AYAIYTSGTTGKPKGVLV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNIRAVVTGLVHKW--AWTKDDVIL----HVLPLHhvhgvVNKLLCPLWVGATCVMLPEfSAQLVWEKFLS-SETPRI 293
Cdd:cd17648 115 EHGSVVNLRTSLSERYfgRDNGDEAVLffsnYVFDFF-----VEQMTLALLNGQKLVVPPD-EMRFDPDRFYAyINREKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVFMAVPTIyTKLMDYYdkhfTQPHVQdfvravceekiRLMVSGSaALPLPVLEKWKNITGHTLLERYGMTEIGM-ALSN 372
Cdd:cd17648 189 TYLSGTPSV-LQQYDLA----RLPHLK-----------RVDAAGE-EFTAPVFEKLRSRFAGLIINAYGPTETTVtNHKR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 373 PLTVAARLPGSVGTPLPGVEVQIVSENPQkegcpyilhaegnekdtRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKA 452
Cdd:cd17648 252 FFPGDQRFDKSLGRPVRNTKCYVLNDAMK-----------------RVPVG---AVGELYLGGDGVARGYLNRPELTAER 311
|
.
gi 946754379 453 F 453
Cdd:cd17648 312 F 312
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
204-399 |
1.68e-10 |
|
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: 63.31 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQLVW 282
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 EKFlssETPRINVFMAVPTIYTKLMdyydkhftqphvQDFVRAVCEEKIRLMVSGSAALPL-PVLEKWKNIT-GHTLLER 360
Cdd:cd05973 172 RVI---ERLGVTNLAGSPTAYRLLM------------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDH 236
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTEIGMALSNPLTVAARL-PGSVGTPLPGVEVQIVSEN 399
Cdd:cd05973 237 YGQTELGMVLANHHALEHPVhAGSAGRAMPGWRVAVLDDD 276
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
207-461 |
1.84e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.84 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 207 YTSGTTGRPKGVLSTHHNIravVTGLVHKWAWTKDDVI-----LHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLV 281
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNL---VANLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 WEKFLSSEtprINVFMAVPTIYTKLMdyydkhfTQPHVQDFvrAVCEEKIRLMVSGSAALPLPVLEKWKN-ITGHTLLER 360
Cdd:PLN02330 268 LNALITQE---VSFAPIVPPIILNLV-------KNPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEAkFPGVQVQEA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 361 YGMTE---IGMALSNPLT---VAARlpGSVGTPLPGVEVQIVsenpqkegcpyilhaegNEKDTRVTPgfKEKEGELLVR 434
Cdd:PLN02330 336 YGLTEhscITLTHGDPEKghgIAKK--NSVGFILPNLEVKFI-----------------DPDTGRSLP--KNTPGELCVR 394
|
250 260
....*....|....*....|....*..
gi 946754379 435 GPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PLN02330 395 SQCVMQGYYNNKEETDRTIDEDGWLHT 421
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
55-461 |
4.32e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.58 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 55 RALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLecAGQDLQE-ERISFMCSNDVSYVVAqWASWMSGGIAVPLFR 133
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNARANRYA----HWA--AARGVGKgDVVALLMENRPEYLAA-WLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQAD-LEYFIQDSRSSVVLAGQEYVELLSPVvRKLGVPLLPLPPAVYNGAAEEHGVREL-------PERDWRDRGAMI 205
Cdd:PRK08279 119 TQQRGAvLAHSLNLVDAKHLIVGEELVEAFEEA-RADLARPPRLWVAGGDTLDDPEGYEDLaaaaagaPTTNPASRSGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 206 -------IYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSA 278
Cdd:PRK08279 198 akdtafyIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 QLVWE---KFlssetpRINVFMAVPTIYTKLMDYYDKHFTQPHvqdfvravceeKIRLMVsGSAALPlPVLEKWKNITG- 354
Cdd:PRK08279 278 SRFWDdvrRY------RATAFQYIGELCRYLLNQPPKPTDRDH-----------RLRLMI-GNGLRP-DIWDEFQQRFGi 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HTLLERYGMTEIGMALSNPLTV---AARLPGSVGTPLPGVEVQIVSENPqkegcpyILHAEGNEkdTRVTPGfkeKEGEL 431
Cdd:PRK08279 339 PRILEFYAASEGNVGFINVFNFdgtVGRVPLWLAHPYAIVKYDVDTGEP-------VRDADGRC--IKVKPG---EVGLL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 946754379 432 LV----RGPtvfreYWG--KPEETKK-----AFT-SDGWFKT 461
Cdd:PRK08279 407 IGritdRGP-----FDGytDPEASEKkilrdVFKkGDAWFNT 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-456 |
6.60e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 17 RLVCALASRQLAPIRHGGSRPLHVALAARSDKsapvftRALAFGDRVALVDQHGVHTYKDLYCRSLRLSQeicRLLECA- 95
Cdd:PRK05691 1108 QLLDAAERAQLAQWGQAPCAPAQAWLPELLNE------QARQTPERIALVWDGGSLDYAELHAQANRLAH---YLRDKGv 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 96 GQDLqeeRISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLP 175
Cdd:PRK05691 1179 GPDV---CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDS 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 176 LPPAVYNGAA---EEHGvrelperdwrDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhH 252
Cdd:PRK05691 1256 LHLDSWPSQApglHLHG----------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI-S 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 253 VHGVVNKLLCPLWVGATCVML-------PEFSAQLVWEKflssetprinvfmAVPTIytklmdyydkHFTQPHVQDFVR- 324
Cdd:PRK05691 1325 FDVSVWECFWPLITGCRLVLAgpgehrdPQRIAELVQQY-------------GVTTL----------HFVPPLLQLFIDe 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 325 ---AVCeEKIRLMVSGSAALPLP----VLEKWKNITGHTlleRYGMTEIGMALSNPLTVAA---RLPgsVGTPLPGVevq 394
Cdd:PRK05691 1382 plaAAC-TSLRRLFSGGEALPAElrnrVLQRLPQVQLHN---RYGPTETAINVTHWQCQAEdgeRSP--IGRPLGNV--- 1452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946754379 395 ivsenpqkegCPYILHAEGNEkdtrVTPGFKekeGELLVRGPTVFREYWGKPEETKKAFTSD 456
Cdd:PRK05691 1453 ----------LCRVLDAELNL----LPPGVA---GELCIGGAGLARGYLGRPALTAERFVPD 1497
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
184-461 |
6.80e-10 |
|
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: 62.09 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 184 AAEEHGVRELP---ERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAvvtglvhkwAWTKDD----------VILHVLPL 250
Cdd:cd17632 204 AVRGRDLPPAPlfrPEPDDDPLALLIYTSGSTGTPKGAMYTERLVAT---------FWLKVSsiqdirppasITLNFMPM 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 251 HHVHGvVNKLLCPLWVGATCVMLPEFSAQLVWEKFlsSETPRINVFMaVPTIYTKLMDYY----DKHFTQPHVQDF---- 322
Cdd:cd17632 275 SHIAG-RISLYGTLARGGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCDMLFQRYqaelDRRSVAGADAETlaer 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 323 VRAVCEEKI---RLM--VSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSNpltvaarlpGSVGTPlPGVEVQIVS 397
Cdd:cd17632 351 VKAELRERVlggRLLaaVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILD---------GVIVRP-PVLDYKLVD 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 946754379 398 enpqkegCPYIlhaeGNEKDTRVTPgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:cd17632 421 -------VPEL----GYFRTDRPHP-----RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRT 468
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
116-461 |
1.21e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.17 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 116 VAQwASWMSGGIAVPLFRKHPQADLEYFIQDSR-------SSVVLAGQEYvELLSPVVRKLGVPLLPLPPAVyngAAEEH 188
Cdd:PRK07768 70 TAQ-GLWMRGASLTMLHQPTPRTDLAVWAEDTLrvigmigAKAVVVGEPF-LAAAPVLEEKGIRVLTVADLL---AADPI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 189 GVRELPERDWrdrgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKD-DVILHVLPLHHVHGVVNKLLCPLWVG 267
Cdd:PRK07768 145 DPVETGEDDL----ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 ATCVMLpefsaqlvwekflsseTPriNVFMAVPTIYTKLMDYYDKHFTQ-PH-----VQDFVRAVCEEK------IRLMV 335
Cdd:PRK07768 221 AELVKV----------------TP--MDFLRDPLLWAELISKYRGTMTAaPNfayalLARRLRRQAKPGafdlssLRFAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 336 SGSAALPLPVLEKWKNITG------HTLLERYGMTEIGMALS-----NPLTV---------------------AARLPgS 383
Cdd:PRK07768 283 NGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSfspcgAGLVVdevdadllaalrravpatkgnTRRLA-T 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 384 VGTPLPGVEVQIVSENpqkegcpyilhaeGNEKDTRvtpgfkeKEGELLVRGPTVFREYW--GKPEETKKAftsDGWFKT 461
Cdd:PRK07768 362 LGPPLPGLEVRVVDED-------------GQVLPPR-------GVGVIELRGESVTPGYLtmDGFIPAQDA---DGWLDT 418
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
56-456 |
1.25e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.72 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVAlvdqhgvhTYKDLYCRSLRLSQeicRLLEC-AGQDLQeerISFMCSNDVSYVVAQWASWMSGGIAVPLFRK 134
Cdd:PRK12467 3113 ALVFGDQQL--------SYAELNRRANRLAH---RLIAIgVGPDVL---VGVAVERSVEMIVALLAVLKAGGAYVPLDPE 3178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 135 HPQADLEYFIQDSRSSVVLAGQEYVELLsPVVRklGVPLLPLPPAVYNGAAEEH-GVRELPERDwrdrgAMIIYTSGTTG 213
Cdd:PRK12467 3179 YPRERLAYMIEDSGVKLLLTQAHLLEQL-PAPA--GDTALTLDRLDLNGYSENNpSTRVMGENL-----AYVIYTSGSTG 3250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 214 RPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVMlpefSAQLVWEkflssetpri 293
Cdd:PRK12467 3251 KPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVV----RDNDLWD---------- 3315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 nvfmavPTIYTKLMDYYD---KHFTQPHVQDFV----RAVCeEKIRLMVSGSAALPLPVLEKWKN-ITGHTLLERYGMTE 365
Cdd:PRK12467 3316 ------PEELWQAIHAHRisiACFPPAYLQQFAedagGADC-ASLDIYVFGGEAVPPAAFEQVKRkLKPRGLTNGYGPTE 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 366 IGMAL------SNPLTVAARLPgsVGTPLPGVEVqivsenpqkegcpYILHAEGNEKDTRVTpgfkekeGELLVRGPTVF 439
Cdd:PRK12467 3389 AVVTVtlwkcgGDAVCEAPYAP--IGRPVAGRSI-------------YVLDGQLNPVPVGVA-------GELYIGGVGLA 3446
|
410
....*....|....*..
gi 946754379 440 REYWGKPEETKKAFTSD 456
Cdd:PRK12467 3447 RGYHQRPSLTAERFVAD 3463
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
203-461 |
3.53e-09 |
|
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: 59.43 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTH-HNIRAVVTGLVhkWAWTKDDVI-LHVLPLHHVHGVVNKLLCPlWVGATCVML---PEFS 277
Cdd:cd05970 188 LLVYFSSGTTGMPKMVEHDFtYPLGHIVTAKY--WQNVREGGLhLTVADTGWGKAVWGKIYGQ-WIAGAAVFVydyDKFD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVWEKFlssETPRINVFMAVPTIY-----TKLMDYydkhftqphvqDFvravceEKIRLMVSGSAALPLPVLEKWKNI 352
Cdd:cd05970 265 PKALLEKL---SKYGVTTFCAPPTIYrflirEDLSRY-----------DL------SSLRYCTTAGEALNPEVFNTFKEK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 353 TGHTLLERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEKDTrvtpgfkEKEGELL 432
Cdd:cd05970 325 TGIKLMEGFGQTETTLTIATFPWMEPK-PGSMGKPAPGYEIDLIDR-------------EGRSCEA-------GEEGEIV 383
|
250 260 270
....*....|....*....|....*....|....
gi 946754379 433 VR---GPTV--FREYWGKPEETKKAFtSDGWFKT 461
Cdd:cd05970 384 IRtskGKPVglFGGYYKDAEKTAEVW-HDGYYHT 416
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
203-461 |
3.58e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 59.75 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTG---LVHKWAwtKDDVILHVLPLHHVhgvvnkllcpLWVGATCVMLPEFSA- 278
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGvmtVVPKLG--KNDVYLAYLPLAHI----------LELAAESVMAAVGAAi 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 ----QLVwekfLSSETPRI-------------NVFMAVPTIYTKLMD--------------------YY----------- 310
Cdd:PLN02387 321 gygsPLT----LTDTSNKIkkgtkgdasalkpTLMTAVPAILDRVRDgvrkkvdakgglakklfdiaYKrrlaaiegswf 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 311 -----DKHFTQPHVQDFVRAVCEEKIRLMVSGSAALPlPVLEKWKNIT-GHTLLERYGMTEI--GMALSNPLTVAArlpG 382
Cdd:PLN02387 397 gawglEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLS-GDTQRFINIClGAPIGQGYGLTETcaGATFSEWDDTSV---G 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 383 SVGTPLPGVEVQIVSenpqkegcpyilHAEGNEKDT-RVTPgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDG---- 457
Cdd:PLN02387 473 RVGPPLPCCYVKLVS------------WEEGGYLISdKPMP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmr 535
|
....
gi 946754379 458 WFKT 461
Cdd:PLN02387 536 WFYT 539
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
203-464 |
6.79e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 58.67 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpeFSAQLVW 282
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV----FAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 EKFLSS--ETPRINVFMAVPTIYTKLMDYYDKHFTqphvqdfvravCEEKIRLMVSGSAALPLPVLEKWKNITGH-TLLE 359
Cdd:PRK06334 262 PKKIVEmiDEAKVTFLGSTPVFFDYILKTAKKQES-----------CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 360 RYGMTEIGMALSNPLTVAARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaegnEKDTRVTPGfkeKEGELLVRGPTVF 439
Cdd:PRK06334 331 GYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSE----------------ETKVPVSSG---ETGLVLTRGTSLF 391
|
250 260
....*....|....*....|....*...
gi 946754379 440 REYWGkpEETKKAFTS---DGWFKTACL 464
Cdd:PRK06334 392 SGYLG--EDFGQGFVElggETWYVTGDL 417
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
205-457 |
9.21e-09 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 58.41 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTH--HNIRAVVTglvHKWAW-TKDDVIL-----------HVlplHHVHGvvnkllcPLWVGATC 270
Cdd:TIGR02188 242 ILYTSGSTGKPKGVLHTTggYLLYAAMT---MKYVFdIKDGDIFwctadvgwitgHS---YIVYG-------PLANGATT 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VML---PEF-SAQLVWEKFlssETPRINVFMAVPTIYTKLMDYYDkhftqphvqDFVRAVCEEKIRLMvsGSAALPL-Pv 345
Cdd:TIGR02188 309 VMFegvPTYpDPGRFWEII---EKHKVTIFYTAPTAIRALMRLGD---------EWVKKHDLSSLRLL--GSVGEPInP- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 346 lEKWK---NITGHT---LLERYGMTEIGMALSNPLTVAARL-PGSVGTPLPGVEVQIVSEnpqkegcpyilhaEGNEKDT 418
Cdd:TIGR02188 374 -EAWMwyyKVVGKErcpIVDTWWQTETGGIMITPLPGATPTkPGSATLPFFGIEPAVVDE-------------EGNPVEG 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 946754379 419 rvtpgfKEKEGELLVRG--PTVFREYWGKPE---ET------KKAFTSDG 457
Cdd:TIGR02188 440 ------PGEGGYLVIKQpwPGMLRTIYGDHErfvDTyfspfpGYYFTGDG 483
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
205-461 |
9.79e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 58.58 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTGLvHKWAWTKD---DVILHVLPLHHVHGVVNKLLCpLWVGATCVmlpefsaqlV 281
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKynpKTHLSYLPISHIYERVIAYLS-FMLGGTIN---------I 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 282 WEK---FLSSE--TPRINVFMAVPT----IYTKLMDYYDK----------------------HFTQ-----PHVQDFVRA 325
Cdd:PTZ00342 378 WSKdinYFSKDiyNSKGNILAGVPKvfnrIYTNIMTEINNlpplkrflvkkilslrksnnngGFSKflegiTHISSKIKD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 326 VCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGmalsNPLTVAARL---PGSVGTPL-PGVEVQIVSENPQ 401
Cdd:PTZ00342 458 KVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETT----GPIFVQHADdnnTESIGGPIsPNTKYKVRTWETY 533
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 402 KEgcpyilhaegneKDTrvTPgfkekEGELLVRGPTVFREYWGKPEETKKAFTSDGWFKT 461
Cdd:PTZ00342 534 KA------------TDT--LP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
203-282 |
1.19e-08 |
|
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: 57.75 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHniRAV-VTGLVHKWAWTKD-DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQL 280
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHR--RAWrGGAFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
..
gi 946754379 281 VW 282
Cdd:cd05940 162 FW 163
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-457 |
1.26e-08 |
|
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: 57.47 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVnkllcplwVGATCV---MLPEF 276
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPA--------LGLTSVipdMDPTR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 277 SAQLVWEKFLSS-ETPRINVFMAVPTIYTKLMDYYDKH-FTQPHVqdfvravceekiRLMVSGSAALPLPVLEKWKNITG 354
Cdd:cd05910 157 PARADPQKLVGAiRQYGVSIVFGSPALLERVARYCAQHgITLPSL------------RRVLSAGAPVPIALAARLRKMLS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 HT--LLERYGMTE---IGMALSNPLTVAARLPGS------VGTPLPGVEVQIVSENPQKegcpyiLHAEGNEKdtRVTPG 423
Cdd:cd05910 225 DEaeILTPYGATEalpVSSIGSRELLATTTAATSggagtcVGRPIPGVRVRIIEIDDEP------IAEWDDTL--ELPRG 296
|
250 260 270
....*....|....*....|....*....|....
gi 946754379 424 fkeKEGELLVRGPTVFREYWGKPEETKKAFTSDG 457
Cdd:cd05910 297 ---EIGEITVTGPTVTPTYVNRPVATALAKIDDN 327
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-456 |
2.48e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 57.36 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 115 VVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVVLAGQEYVELLsPVVRKLGVPLLPLPPAVYNGAAEehgVRELP 194
Cdd:PRK10252 522 TLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF-ADVPDLTSLCYNAPLAPQGAAPL---QLSQP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 195 erdwrDRGAMIIYTSGTTGRPKGVLSTHhniRAVVTGLV---HKWAWTKDDVILHVLPL-HHVHgvVNKLLCPLWVGATC 270
Cdd:PRK10252 598 -----HHTAYIIFTSGSTGRPKGVMVGQ---TAIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKL 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VMLPEFS----AQLvwEKFLSSEtpRINVFMAVPTIYTKlmdyydkhFTQPHVQDFVRAVCEEKIRLMVSGSaALPLPVL 346
Cdd:PRK10252 668 VMAEPEAhrdpLAM--QQFFAEY--GVTTTHFVPSMLAA--------FVASLTPEGARQSCASLRQVFCSGE-ALPADLC 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 347 EKWKNITGHTLLERYGMTEIGMALSnpltvaarlpgsvGTPLPGVEVQIVSENPQKEGCP------YILHAEGNEkdtrV 420
Cdd:PRK10252 735 REWQQLTGAPLHNLYGPTEAAVDVS-------------WYPAFGEELAAVRGSSVPIGYPvwntglRILDARMRP----V 797
|
330 340 350
....*....|....*....|....*....|....*.
gi 946754379 421 TPGFKekeGELLVRGPTVFREYWGKPEETKKAFTSD 456
Cdd:PRK10252 798 PPGVA---GDLYLTGIQLAQGYLGRPDLTASRFIAD 830
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
56-466 |
9.50e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 54.85 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 56 ALAFGDRVALVDQHGVHTYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKH 135
Cdd:PLN02479 30 AVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPG-----STVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 136 PQADLEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPL-------------------PPAVYNGAAEEHGVREL--P 194
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSfkppllivigdptcdpkslQYALGKGAIEYEKFLETgdP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 195 ERDWR---DRGAMII--YTSGTTGRPKGVLSTHHN--IRAVVTGLVhkWAWTKDDVILHVLPLHHVHGvvnklLCPLWVG 267
Cdd:PLN02479 185 EFAWKppaDEWQSIAlgYTSGTTASPKGVVLHHRGayLMALSNALI--WGMNEGAVYLWTLPMFHCNG-----WCFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 A----TCVMLPEFSAQLVWEKFLSSetpRINVFMAVPTIYTKLMDY--YDKHFTQPHVqdfvravceekIRLMVSGSAal 341
Cdd:PLN02479 258 AalcgTNICLRQVTAKAIYSAIANY---GVTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 342 PLPVLEKWKNITGHTLLERYGMTEIgmalSNPLTVAARLPGSVGTPLpgvEVQivSENPQKEGCPYIlHAEG----NEKD 417
Cdd:PLN02479 322 PPPSVLFAMSEKGFRVTHTYGLSET----YGPSTVCAWKPEWDSLPP---EEQ--ARLNARQGVRYI-GLEGldvvDTKT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 946754379 418 TRVTPGFKEKEGELLVRGPTVFREYWGKPEETKKAFtSDGWFKTACLLV 466
Cdd:PLN02479 392 MKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGV 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
54-272 |
1.03e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 54 TRALAFGDRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDLQEeRISFMCSNDVSYVVAQWASWMSGGIAVPLFR 133
Cdd:PRK05691 2196 AQAARTPQAPALTFAGQTLSYAELDARANRLA----RALRERGVGPQV-RVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 134 KHPQADLEYFIQDSRSSVVLAGQEYVELLSPV---VRKLGVPLLPLPPAVYNGAaeehgvrELPERDWRDRGAMIIYTSG 210
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEALGELpagVARWCLEDDAAALAAYSDA-------PLPFLSLPQHQAYLIYTSG 2343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946754379 211 TTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNKLLCPLWVGATCVM 272
Cdd:PRK05691 2344 STGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL 2404
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
61-456 |
1.10e-07 |
|
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: 54.48 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 61 DRVALVDQHGVHTYKDLYCRSLRLSqeicRLLECAGQDlQEERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADL 140
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLA----RHLRGKGVK-PDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 141 EYFIQDSRSSVVLAGQEYVellspvvrklgvpllplppavyngaaeehgvrelperdwrdrgAMIIYTSGTTGRPKGVLS 220
Cdd:cd17645 88 AYMLADSSAKILLTNPDDL-------------------------------------------AYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 221 THHNiravvtgLVHKWAW-------TKDDVILhVLPLHHVHGVVNKLLCPLWVGATCVMLPEfsaqlvwekflssETpRI 293
Cdd:cd17645 125 EHHN-------LVNLCEWhrpyfgvTPADKSL-VYASFSFDASAWEIFPHLTAGAALHVVPS-------------ER-RL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVfmavptiyTKLMDYYDKH-----FTQPHVQDFVRAVCEEKIRLMVSGSaalplPVLEKWKNiTGHTLLERYGMTEIG- 367
Cdd:cd17645 183 DL--------DALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGG-----DKLKKIER-KGYKLVNNYGPTENTv 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 368 MALSNPLTVA-ARLPgsVGTPLPGVEVQIVSENPQkegcpyiLHAEGnekdtrvtpgfkeKEGELLVRGPTVFREYWGKP 446
Cdd:cd17645 249 VATSFEIDKPyANIP--IGKPIDNTRVYILDEALQ-------LQPIG-------------VAGELCIAGEGLARGYLNRP 306
|
410
....*....|
gi 946754379 447 EETKKAFTSD 456
Cdd:cd17645 307 ELTAEKFIVH 316
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
205-414 |
1.11e-07 |
|
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: 54.87 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIrAVVTGLVHKWA---------WTKDDV--------IlhvlplhhVHGvvnkllcPLWVG 267
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGY-LLYAATTFKYVfdyhpddiyWCTADIgwitghsyI--------VYG-------PLANG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 268 ATCVML------PEFSAqlVWEKFlssETPRINVFMAVPTIYTKLMDYYDkhftqphvqDFVRAVCEEKIRLMvsGSAAL 341
Cdd:cd05966 300 ATTVMFegtptyPDPGR--YWDIV---EKHKVTIFYTAPTAIRALMKFGD---------EWVKKHDLSSLRVL--GSVGE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 342 PL-PvlEKWK---NITGH---TLLERYGMTEIGMALSNPLTVAARL-PGSVGTPLPGVEVQIVSENPQKEGcpyiLHAEG 413
Cdd:cd05966 364 PInP--EAWMwyyEVIGKercPIVDTWWQTETGGIMITPLPGATPLkPGSATRPFFGIEPAILDEEGNEVE----GEVEG 437
|
.
gi 946754379 414 N 414
Cdd:cd05966 438 Y 438
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
104-390 |
1.20e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.63 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 104 ISFMCSNDVSYVVAQWASWMSGgIAVPLFRKH---PQADleYFIQDSRSSVVLAGQEY----VELLSPVVRKLGVPLLPL 176
Cdd:PRK13390 52 VALLSDNSPEALVVLWAALRSG-LYITAINHHltaPEAD--YIVGDSGARVLVASAALdglaAKVGADLPLRLSFGGEID 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 177 PPAVYNGAAEEHGVReLPERDWrdrGAMIIYTSGTTGRPKG---------VLSTHHNIRAVVTGLvhkWAWTKDDVILHV 247
Cdd:PRK13390 129 GFGSFEAALAGAGPR-LTEQPC---GAVMLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 248 LPLHHVH-----GVVNKLlcplwvGATCVMLPEFSAQLVW---EKFlssetpRINVFMAVPTIYTKLMDYYDKHFTQPHV 319
Cdd:PRK13390 202 APIYHAAplrwcSMVHAL------GGTVVLAKRFDAQATLghvERY------RITVTQMVPTMFVRLLKLDADVRTRYDV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 946754379 320 qdfvravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI-GMALSNPLTVAARlPGSVGTPLPG 390
Cdd:PRK13390 270 ---------SSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAhGMTFIDSPDWLAH-PGSVGRSVLG 331
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
71-461 |
1.28e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 54.63 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 71 VHTYKDLYCRSLRLSqeiCRLLecaGQDLQ-EERISFMCSNDVSYVVAQWASWMSGGIAVPLF-------RKHPQADLEY 142
Cdd:PRK09192 49 ALPYQTLRARAEAGA---RRLL---ALGLKpGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 143 FIQDSRSSVVLAGQEYVELLSPVVRKLGvpllplppAVYNGAAEEHGVRE-----LPERDwRDRGAMIIYTSGTTGRPKG 217
Cdd:PRK09192 123 MLASAQPAAIITPDELLPWVNEATHGNP--------LLHVLSHAWFKALPeadvaLPRPT-PDDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 218 VLSTHHNIRAVVTGLVHKWAWTKD-DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP--EFSAQ-LVWEKFLSSETPRI 293
Cdd:PRK09192 194 VIITHRALMANLRAISHDGLKVRPgDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFARRpLQWLDLISRNRGTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 294 NVfmaVPT----IYTKLMDyydkhfTQPHVQ-DFVRAvceekiRLMVSGSAALPLPVLEKW------KNITGHTLLERYG 362
Cdd:PRK09192 274 SY---SPPfgyeLCARRVN------SKDLAElDLSCW------RVAGIGADMIRPDVLHQFaeafapAGFDDKAFMPSYG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 363 MTEIGMALSNP--------LTV-AARLPGS------------------VGTPLPGVEVQIVSENpqkegcpyilhaeGNE 415
Cdd:PRK09192 339 LAEATLAVSFSplgsgivvEEVdRDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEA-------------GMP 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 946754379 416 KDTRVTpgfkekeGELLVRGPTVFREYWGKpEETKKAFTSDGWFKT 461
Cdd:PRK09192 406 LPERVV-------GHICVRGPSLMSGYFRD-EESQDVLAADGWLDT 443
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
191-423 |
1.34e-07 |
|
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: 54.51 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 191 RELPERDWRDRGAMIIYTSGTTGRPKGVLSTH--HNIRAvVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGA 268
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYA-ATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 269 TCVMlpeFSAQLVWekflssetprinvfmavPTIyTKLMDYYDKH-----FTQPHVQDFVRAVCEEKIR------LMVSG 337
Cdd:cd17634 302 TTLL---YEGVPNW-----------------PTP-ARMWQVVDKHgvnilYTAPTAIRALMAAGDDAIEgtdrssLRILG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 338 SAALPL---PVLEKWKNITGH--TLLERYGMTEIGMALSNPLTVAARL-PGSVGTPLPGVEVQIVSEnpqkEGCPYILHA 411
Cdd:cd17634 361 SVGEPInpeAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPLPGAIELkAGSATRPVFGVQPAVVDN----EGHPQPGGT 436
|
250
....*....|..
gi 946754379 412 EGNEKDTRVTPG 423
Cdd:cd17634 437 EGNLVITDPWPG 448
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
197-461 |
2.25e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 53.72 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 197 DWR-DRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnklLCPLW----VGATCV 271
Cdd:PRK09029 131 AWQpQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG-----QGIVWrwlyAGATLV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 272 mLPEFsaqlvwEKFLSSetprinVFMA-----VPTIYTKLMDYYDKHFTQPHVqdfvravceekirLMvsGSAALPlpvl 346
Cdd:PRK09029 206 -VRDK------QPLEQA------LAGCthaslVPTQLWRLLDNRSEPLSLKAV-------------LL--GGAAIP---- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 347 ekwknitgHTLLER-----------YGMTEigMAlSnplTVAAR----LPGsVGTPLPGVEVQIVsenpqkegcpyilha 411
Cdd:PRK09029 254 --------VELTEQaeqqgircwcgYGLTE--MA-S---TVCAKradgLAG-VGSPLPGREVKLV--------------- 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 946754379 412 egnekdtrvtpgfkekEGELLVRGPTVFREYW--GKPeetkKAFT-SDGWFKT 461
Cdd:PRK09029 304 ----------------DGEIWLRGASLALGYWrqGQL----VPLVnDEGWFAT 336
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
102-480 |
2.48e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFrkHPQAD-----LEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPL 176
Cdd:PRK07769 80 DRVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAEPghvgrLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERPR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 177 PPAVyNGAAEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGV 256
Cdd:PRK07769 158 VIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 257 VNKLLCPLWVGATCVMLPefsAQLV-----WEKFLSS-ETPRINVFMAVPtiytklmdyydkHFTQPHVQdfVRAVCEE- 329
Cdd:PRK07769 237 ITVLLPALLGHYITFMSP---AAFVrrpgrWIRELARkPGGTGGTFSAAP------------NFAFEHAA--ARGLPKDg 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 330 -------KIRLMVSGSAALPLPVLEKWKNITGHTLLER------YGMTEIGMALSN-PLTVAARLPGSVGTPLPG---VE 392
Cdd:PRK07769 300 eppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTtPMDEEPTVIYVDRDELNAgrfVE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 393 VQIVSEN--PQKeGCPYILHAE-----GNEKDTRVTPGfkeKEGELLVRGPTVFREYWGKPEETKKAFTSdgwfktacLL 465
Cdd:PRK07769 380 VPADAPNavAQV-SAGKVGVSEwavivDPETASELPDG---QIGEIWLHGNNIGTGYWGKPEETAATFQN--------IL 447
|
410
....*....|....*
gi 946754379 466 VTRTPflrrHSHVQG 480
Cdd:PRK07769 448 KSRLS----ESHAEG 458
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
204-404 |
3.67e-07 |
|
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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 52.96 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHhniRAVVTGLVHKWAWT---KDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML--PEFSA 278
Cdd:cd05974 89 LLYFTSGTTSKPKLVEHTH---RSYPVGHLSTMYWIglkPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 279 QLVWEKFlssETPRINVFMAVPTIYTKLMDyydkhftqphvQDFVRAvcEEKIRLMVSGSAALPLPVLEKWKNITGHTLL 358
Cdd:cd05974 166 KRVLAAL---VRYGVTTLCAPPTVWRMLIQ-----------QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 946754379 359 ERYGMTEIGMALSNPLTVAARlPGSVGTPLPGVEVQIVSE--NPQKEG 404
Cdd:cd05974 230 DGYGQTETTALVGNSPGQPVK-AGSMGRPLPGYRVALLDPdgAPATEG 276
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
203-399 |
1.26e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 51.32 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 203 AMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEfSAQLVW 282
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 283 EKFLSS--ETPRINVFMAVPTIYtklmdyydKHFTQPHVQDFVRAVcEEKIRLMVSGSAALP-LPVLEKWKNITGHT-LL 358
Cdd:cd17654 199 SKLADIlfKRHRITVLQATPTLF--------RRFGSQSIKSTVLSA-TSSLRVLALGGEPFPsLVILSSWRGKGNRTrIF 269
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 946754379 359 ERYGMTEIGM-ALSNPLTVaARLPGSVGTPLPGVEVQIVSEN 399
Cdd:cd17654 270 NIYGITEVSCwALAYKVPE-EDSPVQLGSPLLGTVIEVRDQN 310
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
202-435 |
1.44e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.81 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 202 GAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVML----PEFS 277
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIItnknPKFA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVwekflsSETPRiNVFMAVPTIYTKLmdyydKHFTQPHVQDFvravceekiRLMVSGsAALPLPVLEKWKNITGHtL 357
Cdd:PRK08308 183 LNIL------RNTPQ-HILYAVPLMLHIL-----GRLLPGTFQFH---------AVMTSG-TPLPEAWFYKLRERTTY-M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 358 LERYGMTEIG-MALSNPLtvaaRLPGSVGTPLPGVEVQIVS--ENPQKegcpYILHAEGNEKDTRvTPGFKEKEGELLVR 434
Cdd:PRK08308 240 MQQYGCSEAGcVSICPDM----KSHLDLGNPLPHVSVSAGSdeNAPEE----IVVKMGDKEIFTK-DLGYKSERGTLHFM 310
|
.
gi 946754379 435 G 435
Cdd:PRK08308 311 G 311
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
205-457 |
1.73e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.05 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLP-----EFsAQ 279
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPkdmtaNF-KQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 280 LvwekFLSSETPRINVFMAVPTiytkLMD--YYDKHFTQ---PHVQDFVraVCEEkirlmvsgsaALPLPVLEKwknitg 354
Cdd:PRK04813 226 L----FETLPQLPINVWVSTPS----FADmcLLDPSFNEehlPNLTHFL--FCGE----------ELPHKTAKK------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 355 htLLER---------YGMTEIGMALS------NPLTVAARLPgsVGTPLPGVEVQIVSENPQKegcpyilhaegnekdtr 419
Cdd:PRK04813 280 --LLERfpsatiyntYGPTEATVAVTsieitdEMLDQYKRLP--IGYAKPDSPLLIIDEEGTK----------------- 338
|
250 260 270
....*....|....*....|....*....|....*....
gi 946754379 420 VTPGfkeKEGELLVRGPTVFREYWGKPEETKKAF-TSDG 457
Cdd:PRK04813 339 LPDG---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDG 374
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
200-466 |
1.81e-06 |
|
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: 50.89 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 200 DRGAMIIYTSGTTGRPKGVLSThhNIRAVVTG-LVHKWAWTKD-DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 277
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAIS--WRRTLVTSnLLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 278 AQLVWEKFLSSETPRI-------NVFMAVPTiytklmDYYDKhftqphvqdfvravcEEKIRlMVSGSAALPlPVLEKWK 350
Cdd:cd05937 165 ASQFWKDVRDSGATIIqyvgelcRYLLSTPP------SPYDR---------------DHKVR-VAWGNGLRP-DIWERFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 351 nitghtllERYGMTEIG---------MALSN----PLTVAA-RLPGSVGTPLPGVEVQIVSENPQKEGCPYilhaegnek 416
Cdd:cd05937 222 --------ERFNVPEIGefyaategvFALTNhnvgDFGAGAiGHHGLIRRWKFENQVVLVKMDPETDDPIR--------- 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 946754379 417 dtRVTPGF-----KEKEGELLVRGP----TVFREYWGKPEETKKAFTS------DGWFKTACLLV 466
Cdd:cd05937 285 --DPKTGFcvrapVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLR 347
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
193-282 |
1.98e-06 |
|
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: 50.50 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 193 LPERDWRDRgAMIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHH----VHGVVNKLLcplwVGA 268
Cdd:cd05939 98 QDDVNFRDK-LFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGS 172
|
90
....*....|....
gi 946754379 269 TCVMLPEFSAQLVW 282
Cdd:cd05939 173 TVVIRKKFSASNFW 186
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-457 |
2.74e-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: 50.07 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSTHHNIRAVVTG--------------LVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATC 270
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgeftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 271 VMLPEFSAQLVWEkflSSETPRINVFMAVPTIYTK-LMDYYDKhftqPHVQDFvravceEKIRLMVSGSAALPLPVLEKW 349
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 350 KNITGH-TLLERYGMTEIGMALSNplTVAARLPGSVGTPLPGVEVQIVSEnpqkegcpyilhaegnekDTRVTPGFKEKE 428
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFTGSG--HSAGSGPETGPFTRANPDTVVLDD------------------DGRVVPPGSGGV 214
|
250 260 270
....*....|....*....|....*....|
gi 946754379 429 GELLVRGpTVFREYWGKPEETKKAF-TSDG 457
Cdd:cd05924 215 GWIARRG-HIPLGYYGDEAKTAETFpEVDG 243
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
204-461 |
2.89e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.41 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 204 MIIYTSGTTGRPKGVLSTHHNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQlvwe 283
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSAS---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 KFLssetPRINVFMAVptiytkLMDYYDKHFT----QPHVQDfvravcEEKIRLMVS-GSAALPlpvlekwKNIT----- 353
Cdd:PRK13388 230 GFL----DDVRRYGAT------YFNYVGKPLAyilaTPERPD------DADNPLRVAfGNEASP-------RDIAefsrr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 354 -GHTLLERYGMTEIGMALSNPLTVAarlPGSVGTPLPGVEvqIVSENPQKEGCPYILHAEGnekdtRVTpGFKEKEGELL 432
Cdd:PRK13388 287 fGCQVEDGYGSSEGAVIVVREPGTP---PGSIGRGAPGVA--IYNPETLTECAVARFDAHG-----ALL-NADEAIGELV 355
|
250 260 270
....*....|....*....|....*....|
gi 946754379 433 VR-GPTVFREYWGKPEETKKAFtSDGWFKT 461
Cdd:PRK13388 356 NTaGAGFFEGYYNNPEATAERM-RHGMYWS 384
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
205-405 |
3.62e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.14 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 205 IIYTSGTTGRPKGVLSThhniravvTG--LV-----HKWA---------WTKDDV--------IlhvlplhhVHGvvnkl 260
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHT--------TGgyLVyaamtMKYVfdykdgdvyWCTADVgwvtghsyI--------VYG----- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 261 lcPLWVGATCVML---PEFSAQLVW----EKFlssetpRINVFMAVPTIYTKLMDYYDKHFTQPHVqdfvravceEKIRL 333
Cdd:PRK00174 309 --PLANGATTLMFegvPNYPDPGRFweviDKH------KVTIFYTAPTAIRALMKEGDEHPKKYDL---------SSLRL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 334 MvsGSAALPL-PvlEKW----KNITGhtllER------YGMTEIGMALSNPLTVAARL-PGSVGTPLPGVEVQIVSE--N 399
Cdd:PRK00174 372 L--GSVGEPInP--EAWewyyKVVGG----ERcpivdtWWQTETGGIMITPLPGATPLkPGSATRPLPGIQPAVVDEegN 443
|
....*.
gi 946754379 400 PQKEGC 405
Cdd:PRK00174 444 PLEGGE 449
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
73-447 |
4.58e-06 |
|
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: 49.80 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 73 TYKDLYCRSLRLSQEICRLLECAGqdlqeERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQADLEYFIQDSRSSVV 152
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKG-----DRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 153 LAGQEY------VELLSP---------------VVRKLG--VPLLPLPPAVYNGAAEEHGVRelPERDWRDRGAMIIYTS 209
Cdd:cd05968 168 ITADGFtrrgreVNLKEEadkacaqcptvekvvVVRHLGndFTPAKGRDLSYDEEKETAGDG--AERTESEDPLMIIYTS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 210 GTTGRPKGVLSTHHN--IRAVVTgLVHKWAWTKDDVILHVLPLHHVHGVVnKLLCPLWVGATCVM---LPEF-SAQLVWE 283
Cdd:cd05968 246 GTTGKPKGTVHVHAGfpLKAAQD-MYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHpKADRLWR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 284 kflSSETPRINVFMAVPTIYTKLMdyydkhftqPHVQDFVRAvcEEKIRLMVSGSAALPLPvLEKWKNITGHTLLERY-- 361
Cdd:cd05968 324 ---MVEDHEITHLGLSPTLIRALK---------PRGDAPVNA--HDLSSLRVLGSTGEPWN-PEPWNWLFETVGKGRNpi 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 362 ----GMTEI-GMALSNPLtVAARLPGSVGTPLPGVEVQIVSEnpqkEGCPyilhaegnekdtrvtpgFKEKEGELLVRGP 436
Cdd:cd05968 389 inysGGTEIsGGILGNVL-IKPIKPSSFNGPVPGMKADVLDE----SGKP-----------------ARPEVGELVLLAP 446
|
410
....*....|...
gi 946754379 437 TV--FREYWGKPE 447
Cdd:cd05968 447 WPgmTRGFWRDED 459
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
102-300 |
1.28e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.20 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 102 ERISFMCSNDVSYVVAQWASWMSGGIAVPLFRKHPQAD---LEYFIQDSRSSVVLAGQEYVELLSPVVRKLGVPLLPLPP 178
Cdd:PRK12476 93 DRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHaerLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRPRVI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 179 AVyNGAAEEHGVRELPERDWRDRGAMIIYTSGTTGRPKGVLSTHhniRAVVTGLV-------------HKWAWtkddvil 245
Cdd:PRK12476 173 AI-DAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITH---RAVGTNLVqmilsidlldrntHGVSW------- 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 946754379 246 hvLPLHHVHGVVNKLLCPLWVGATCVMLPefsAQLV-----WEKFLSSETPRINVFMAVP 300
Cdd:PRK12476 242 --LPLYHDMGLSMIGFPAVYGGHSTLMSP---TAFVrrpqrWIKALSEGSRTGRVVTAAP 296
|
|
| |
