|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-657 |
0e+00 |
|
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: 1004.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 87 GAQRFSYAEAERESNRIARAFLRargwtggrrgsgrgsteegarvappagdaaargttAPPLAPGATVALLLPAGPDFLW 166
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLA-----------------------------------HAGLRPGDTVALLLGNEPAFLW 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 167 IWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAA 246
Cdd:cd05938 47 IWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 247 DQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGC 326
Cdd:cd05938 127 AASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGC 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 327 LGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQIL 406
Cdd:cd05938 207 IELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 407 ETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYA 486
Cdd:cd05938 287 EFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 487 GAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPG 566
Cdd:cd05938 367 GDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 567 HEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSVLSDPLYVLDQDI 646
Cdd:cd05938 447 HEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQ 526
|
570
....*....|.
gi 82581629 647 GAYLPLTPARY 657
Cdd:cd05938 527 KTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
62-666 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 639.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 62 ESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAflrargwtggrrgsgrgsteegarvappagdAAAR 141
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHW-------------------------------AAAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 142 GttappLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRA 221
Cdd:PRK08279 83 G-----VGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 222 MGLHLWATGPE-TNVAGISNLLSEAADQVDEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLKVLQC-QGFYH 297
Cdd:PRK08279 158 PPRLWVAGGDTlDDPEGYEDLAAAAAGAPTTN----PASRSGVTakDTAFYIYTSGTTGLPKAAVMSHMRWLKAmGGFGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 298 LCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECD 377
Cdd:PRK08279 234 LLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 378 HKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR-ASWLYKhifPFSLIRYDVMTGEPIRN 456
Cdd:PRK08279 314 HRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRvPLWLAH---PYAIVKYDVDTGEPVRD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 457 AQGHCMTTSPGEPGLLVAPVSQQSPFLGYAgAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKG 536
Cdd:PRK08279 391 ADGRCIKVKPGEVGLLIGRITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 537 ENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTE 616
Cdd:PRK08279 470 ENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTG 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 82581629 617 TFKQQKVRMANEGFDPSVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLR 666
Cdd:PRK08279 550 TFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFR 599
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
89-632 |
0e+00 |
|
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: 567.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 89 QRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLLPAGPDFLWIW 168
Cdd:cd05940 2 EALTYAELDAMANRYARWL-------------------------------KSLG-----LKPGDVVALFMENRPEYVLLW 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 169 FGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALvlatefleslepdlpalramglhlwatgpetnvagisnllseaadq 248
Cdd:cd05940 46 LGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL---------------------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 249 vdepvpgylsapqnIMDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCL 327
Cdd:cd05940 80 --------------VVDAALYIYTSGTTGLPKAAIISHRRAWRgGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACL 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 328 GIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILE 407
Cdd:cd05940 146 ASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 408 TYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAG 487
Cdd:cd05940 226 FYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTD 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 488 APELAKdKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGH 567
Cdd:cd05940 306 PAATEK-KILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGT 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 568 EGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDP 632
Cdd:cd05940 385 DGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
148-632 |
5.26e-164 |
|
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: 478.84 E-value: 5.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALV--LATEFLESLEPDLPALRAMGLH 225
Cdd:cd05939 25 YRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIfnLLDPLLTQSSTEPPSQDDVNFR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 lwatgpetnvagisnllseaadqvdepvpgylsapqnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQE 304
Cdd:cd05939 105 ---------------------------------------DKLFYIYTSGTTGLPKAAVIVHSRYYRiAAGAYYAFGMRPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 305 DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV 384
Cdd:cd05939 146 DVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTT 464
Cdd:cd05939 226 GNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 465 SPGEPGLLVAPVSQQSP---FLGYAGAPELAKdKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVAT 541
Cdd:cd05939 306 QPGEPGLLVGKIIQNDPlrrFDGYVNEGATNK-KIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVST 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 542 TEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALAlRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQ 621
Cdd:cd05939 385 TEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIV-DPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQ 463
|
490
....*....|.
gi 82581629 622 KVRMANEGFDP 632
Cdd:cd05939 464 KTDLQKEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
150-632 |
1.63e-134 |
|
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: 403.35 E-value: 1.63e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVlatefleslepdlpalramglhlwat 229
Cdd:cd05937 30 AGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI-------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 230 gpetnvagisnllseaadqVDEPVPgylsapqnimdtCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIY 308
Cdd:cd05937 84 -------------------VDPDDP------------AILIYTSGTTGLPKAAAISWRRTLVtSNLLSHDLNLKNGDRTY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 309 LALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGL 388
Cdd:cd05937 133 TCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 389 RPDTWERFLRRFGPLQILETYGMTEGNVATFNY-TG--RQGAVGRASWLYKHIF--PFSLIRYDVMTGEPIR-NAQGHCM 462
Cdd:cd05937 213 RPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGdfGAGAIGHHGLIRRWKFenQVVLVKMDPETDDPIRdPKTGFCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 463 TTSPGEPGLLVA--PVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVA 540
Cdd:cd05937 293 RAPVGEPGEMLGrvPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 541 TTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALR----PPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTE 616
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEessaVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTD 452
|
490
....*....|....*.
gi 82581629 617 TFKQQKVRMANEGFDP 632
Cdd:cd05937 453 NHKQQKGVLRDEGVDP 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-622 |
1.19e-87 |
|
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: 280.33 E-value: 1.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 88 AQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLLPAGPDFLWI 167
Cdd:cd05934 1 GRRWTYAELLRESARIAAAL-------------------------------AALG-----IRPGDRVALMLDNCPEFLFA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 168 WFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVlatefleslepdlpalramglhlwatgpetnvagisnllseaad 247
Cdd:cd05934 45 WFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 248 qvdepvpgylsapqniMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGC 326
Cdd:cd05934 81 ----------------VDPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAA 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 327 LGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQIL 406
Cdd:cd05934 145 LSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 407 ETYGMTEGNVATFN---YTGRQGAVGRASWLYKhifpfslIRydvmtgepIRNAQGHcmTTSPGEPG-LLVAPVSQQSPF 482
Cdd:cd05934 224 EGYGMTETIVGVIGprdEPRRPGSIGRPAPGYE-------VR--------IVDDDGQ--ELPAGEPGeLVIRGLRGWGFF 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 483 LGYAGAPElAKDKLLKdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGv 562
Cdd:cd05934 287 KGYYNMPE-ATAEAMR------NGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA- 358
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82581629 563 tVPGHEGR-AGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd05934 359 -VPDEVGEdEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
67-628 |
1.29e-84 |
|
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: 273.22 E-value: 1.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 67 LAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttap 146
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAAL-------------------------------RALG---- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 147 pLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVlatefleslepdlpalramglhl 226
Cdd:COG0318 46 -VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV----------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 227 watgpetnvagisnllseaadqvdepvpgylsapqnimdTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQED 305
Cdd:COG0318 102 ---------------------------------------TALILYTSGTTGRPKGVMLTHRNLLaNAAAIAAALGLTPGD 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 306 VIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV- 384
Cdd:COG0318 143 VVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVs 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 -GSGLRPDTWERFLRRFGPlQILETYGMTEGN-VATFN----YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQ 458
Cdd:COG0318 223 gGAPLPPELLERFEERFGV-RIVEGYGLTETSpVVTVNpedpGERRPGSVGRP-------LPGVEVR--------IVDED 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 459 GHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGEN 538
Cdd:COG0318 287 GR--ELPPGEVGEIV--VRGPNVMKGYWNDPEATAEAF-------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGEN 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 539 VATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETF 618
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASG 434
|
570
....*....|
gi 82581629 619 KQQKVRMANE 628
Cdd:COG0318 435 KIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
66-632 |
1.36e-67 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 230.80 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 66 SLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGtta 145
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHAL-------------------------------AAAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 146 ppLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGlH 225
Cdd:PRK06155 68 --VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLP-A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKvlqcqgFY-------HL 298
Cdd:PRK06155 145 VWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPG---DTAAILYTSGTTGPSKGVCCPHAQ------FYwwgrnsaED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 299 CGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDH 378
Cdd:PRK06155 216 LEIGADDVLYTTLPLFHTN-ALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 379 KVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNV--ATFNYTGRQGAVGRaswlykhifpfslirydVMTGEPIRN 456
Cdd:PRK06155 295 RVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNFviAVTHGSQRPGSMGR-----------------LAPGFEARV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 457 AQGHCMTTSPGEPGLLVAPVSQQSPFL-GYAGAPElakdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWK 535
Cdd:PRK06155 357 VDEHDQELPDGEPGELLLRADEPFAFAtGYFGMPE-------KTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 536 GENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:PRK06155 430 GENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKT 508
|
570
....*....|....*..
gi 82581629 616 ETFKQQKVRMANEGFDP 632
Cdd:PRK06155 509 ENGKVQKFVLREQGVTA 525
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
265-619 |
3.33e-64 |
|
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: 215.61 E-value: 3.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGNVATFNY 421
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsgGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 422 TG-----RQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKL 496
Cdd:cd04433 159 PPdddarKPGSVGRP-------VPGVEVR--------IVDPDGG--ELPPGEIGELV--VRGPSVMKGYWNNPEATAAVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 497 lkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 576
Cdd:cd04433 220 -------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 82581629 577 ALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd04433 292 VLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
75-535 |
9.71e-59 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 203.70 E-value: 9.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGA-QRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappLAPGAT 153
Cdd:pfam00501 5 AARTPDKTALEVGEgRRLTYRELDERANRLAAGLR-------------------------------ALG-----VGKGDR 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 154 VALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF-LESLEPDLPALRAMGLHLWATGPE 232
Cdd:pfam00501 49 VAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TNVAGISNLLSEAADQVDEPVPgylsaPQNIMDTCLYIFTSGTTGLPKAARISHL----KVLQCQGFYHLC-GVHQEDVI 307
Cdd:pfam00501 129 VLKEEPLPEEAKPADVPPPPPP-----PPDPDDLAYIIYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGfGLGPDDRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 308 YLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA---SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR--L 382
Cdd:pfam00501 204 LSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 383 AVGSGLRPDTWERFLRRFGPlQILETYGMTEGNVATFNY------TGRQGAVGRaswlykhifPFSLIRY---DVMTGEP 453
Cdd:pfam00501 284 SGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPlpldedLRSLGSVGR---------PLPGTEVkivDDETGEP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 454 IRnaqghcmttsPGEPGLLVapVSQQSPFLGYAGAPELAkdkllKDVFWSGDvFFNTGDLLVCDEQGFLHFHDRTGDTIR 533
Cdd:pfam00501 354 VP----------PGEPGELC--VRGPGVMKGYLNDPELT-----AEAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
..
gi 82581629 534 WK 535
Cdd:pfam00501 416 LG 417
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
131-660 |
2.85e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 199.91 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 131 VAPPAGDAAARGTTAPPLAPgATVALLLPAGPDFLwiwFGLAKAGLrTAFVPTAL---RRGPLL-------HClrscgas 200
Cdd:PRK07867 35 IRGSAARAAALRARLDPTRP-PHVGVLLDNTPEFS---LLLGAAAL-SGIVPVGLnptRRGAALardiahaDC------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 201 ALVLA-TEFLESLEPDLPALRAMglhlwatgpETNVAGISNLLSEAADqvDEPVPGYLSApqniMDTCLYIFTSGTTGLP 279
Cdd:PRK07867 103 QLVLTeSAHAELLDGLDPGVRVI---------NVDSPAWADELAAHRD--AEPPFRVADP----DDLFMLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 280 KAARISHLKV-----LQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT 354
Cdd:PRK07867 168 KAVRCTHRKVasagvMLAQRF----GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 355 VFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVAtFNYT--GRQGAVGRAs 432
Cdd:PRK07867 244 YANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFG-CVVVDGFGSTEGGVA-ITRTpdTPPGALGPL- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 433 wlykhifPFSLIRYDVMTGEPIRNAQ--GHCMTTSPGEPGLLVApVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFnt 510
Cdd:PRK07867 321 -------PPGVAIVDPDTGTECPPAEdaDGRLLNADEAIGELVN-TAGPGGFEGYYNDPEADAERMRGGVYWSGDLAY-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 511 gdllvCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQL- 589
Cdd:PRK07867 391 -----RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP-VVGDQVMAALVLAPGAKFDPDAFa 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82581629 590 -YSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDpsvLSDPLYvldqdigAYLPLTPARYSAL 660
Cdd:PRK07867 465 eFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD---CADPVW-------WIRRLTPSDYAAL 526
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
135-663 |
6.94e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 190.62 E-value: 6.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 135 AGDAAARGTTAPPLAPGAT---VALLLPAGPDFLwiwFGLAKAGLRTAFV----PTalRRGP-LLHCLRSCGASALVLAT 206
Cdd:PRK13388 33 LAEAAARAAALIALADPDRplhVGVLLGNTPEML---FWLAAAALGGYVLvglnTT--RRGAaLAADIRRADCQLLVTDA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 207 EFLESLEP-DLPALRAMglhlwatgpETNVAGISNLLSEAADQVDEPVPGylsapqnIMDTCLYIFTSGTTGLPKAARIS 285
Cdd:PRK13388 108 EHRPLLDGlDLPGVRVL---------DVDTPAYAELVAAAGALTPHREVD-------AMDPFMLIFTSGTTGAPKAVRCS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 286 HLKVLQCQgfYHLC---GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGEL 362
Cdd:PRK13388 172 HGRLAFAG--RALTerfGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 363 CRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVA-TFNYTGRQGAVGRAswlykhiFPf 441
Cdd:PRK13388 250 LAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIvVREPGTPPGSIGRG-------AP- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 442 SLIRYDVMTGEPirnaqghCMTTSPGEPGLLVAP-------VSQQ--SPFLGYAGAPELAKDKLLKDVFWSGDVFFNtgd 512
Cdd:PRK13388 321 GVAIYNPETLTE-------CAVARFDAHGALLNAdeaigelVNTAgaGFFEGYYNNPEATAERMRHGMYWSGDLAYR--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 513 llvcDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQL--Y 590
Cdd:PRK13388 391 ----DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE-RVGDQVMAALVLRDGATFDPDAFaaF 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82581629 591 SHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDpSVLSDPLYVLDQDiGAYLPLTPARYSALLSG 663
Cdd:PRK13388 466 LAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWA-TGDPVTLWVRRGG-PAYRLMSEPAKAALAAE 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
74-622 |
7.21e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 187.58 E-value: 7.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 74 LAREQPTHTFLIH-----GAQRFSYAEAERESNRIARAFLRArgwtggrrgsgrgsteeGARvappAGDaaargttappl 148
Cdd:PRK08008 16 LADVYGHKTALIFessggVVRRYSYLELNEEINRTANLFYSL-----------------GIR----KGD----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 149 apgaTVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWA 228
Cdd:PRK08008 64 ----KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 229 TGP----ETNVAGISNLLSEAADQVDEPVPgyLSAPqnimDTCLYIFTSGTTGLPKAARISHLKvLQCQGFYHL--CGVH 302
Cdd:PRK08008 140 TRValpaDDGVSSFTQLKAQQPATLCYAPP--LSTD----DTAEILFTSGTTSRPKGVVITHYN-LRFAGYYSAwqCALR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 303 QEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR- 381
Cdd:PRK08008 213 DDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRe 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 ----LAVGSGLRPDtwerFLRRFGpLQILETYGMTEGNVATFNYTG----RQGAVGRASWLYKhifpfslirydvmtgEP 453
Cdd:PRK08008 293 vmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTETIVGIIGDRPgdkrRWPSIGRPGFCYE---------------AE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 454 IRNAQGHCMttSPGEPG-LLVAPVSQQSPFLGYAGAPElAKDKLLkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTI 532
Cdd:PRK08008 353 IRDDHNRPL--PAGEIGeICIKGVPGKTIFKEYYLDPK-ATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMI 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 533 RWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEgRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:PRK08008 425 KRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD-EAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDL 503
|
570
....*....|
gi 82581629 613 ATTETFKQQK 622
Cdd:PRK08008 504 PRNCSGKIIK 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
67-619 |
1.06e-51 |
|
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: 185.84 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 67 LAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttap 146
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGL-------------------------------QNLG---- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 147 pLAPGATVALLLPAGPDFLWIWFGLAKAGLrtAFVPTALRRGP--LLHCLRSCGASALVLATEFLESLEPDLPALRAMGL 224
Cdd:cd05936 46 -VQPGDRVALMLPNCPQFPIAYFGALKAGA--VVVPLNPLYTPreLEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HlwatgPEtnvagisnllseaadqvdepvpgylsapqnimDTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCG 300
Cdd:cd05936 123 T-----PE--------------------------------DVAVLQYTSGTTGVPKGAMLTHrnlvANALQIKAWLEDLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 301 VHqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKV 380
Cdd:cd05936 166 EG-DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 381 RLAVGSG--LRPDTWERFLRRFGpLQILETYGMTE-GNVATFN-YTG--RQGAVGraswlykHIFPFSLIRydvmtgepI 454
Cdd:cd05936 245 RLCISGGapLPVEVAERFEELTG-VPIVEGYGLTEtSPVVAVNpLDGprKPGSIG-------IPLPGTEVK--------I 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 455 RNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPElAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRW 534
Cdd:cd05936 309 VDDDGE--ELPPGEVGELW--VRGPQVMKGYWNRPE-ETAEAFVD----G--WLRTGDIGYMDEDGYFFIVDRKKDMIIV 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 535 KGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLAT 614
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDP-YSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPK 456
|
....*
gi 82581629 615 TETFK 619
Cdd:cd05936 457 SAVGK 461
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
71-625 |
2.01e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 155.34 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsTEEGARvappagdaaargttapplaP 150
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANAL-----------------RALGVK-------------------K 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALVLATEF---LESLEPDLPALRamglH 225
Cdd:PRK06187 56 GDRVAVFDWNSHEYLEAYFAVPKIG--AVLHPINIRLKPeeIAYILNDAEDRVVLVDSEFvplLAAILPQLPTVR----T 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATGPETN------VAGISNLLSEAADQVDEPVPGylsapqnIMDTCLYIFTSGTTGLPKAARISH----LKVLQCQGF 295
Cdd:PRK06187 130 VIVEGDGPAaplapeVGEYEELLAAASDTFDFPDID-------ENDAAAMLYTSGTTGHPKGVVLSHrnlfLHSLAVCAW 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 YHLcgvHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE 375
Cdd:PRK06187 203 LKL---SRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 376 CDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY--------TGRQGAVGRAswlykhiFPFSLI 444
Cdd:PRK06187 279 DFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTEtSPVVSVLPpedqlpgqWTKRRSAGRP-------LPGVEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 445 RydvmtgepIRNAQGHCMTTSPGEPGLLVApvsqQSPFL--GYAGAPELAKDKLLKDvfWsgdvfFNTGDLLVCDEQGFL 522
Cdd:PRK06187 351 R--------IVDDDGDELPPDGGEVGEIIV----RGPWLmqGYWNRPEATAETIDGG--W-----LHTGDVGYIDEDGYL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 523 HFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYAR 602
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDE-KWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKL 490
|
570 580
....*....|....*....|...
gi 82581629 603 PRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK06187 491 PKRIAFVDELPRTSVGKILKRVL 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
258-622 |
3.12e-40 |
|
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: 153.21 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 258 SAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK 336
Cdd:cd05941 83 SEPSLVLDPALILYTSGTTGRPKGVVLTHANLAaNVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 337 PKFSASQFWDDCQKHRVTVFQ-----YIGELCRYLVNQPPSK---AECDHKVRLAV-GSG-LRPDTWERFLRRFGpLQIL 406
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMgvptiYTRLLQYYEAHFTDPQfarAAAAERLRLMVsGSAaLPVPTLEEWEAITG-HTLL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 407 ETYGMTEGNVATFN-YTG--RQGAVGRAswlykhiFPFSLIR-YDVMTGEPirnaqghcmtTSPGEPG-LLVApvsqqSP 481
Cdd:cd05941 242 ERYGMTEIGMALSNpLDGerRPGTVGMP-------LPGVQARiVDEETGEP----------LPRGEVGeIQVR-----GP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 482 --FLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTG-DTIRWKGENVATTEVAEVLETLDFLQEVN 558
Cdd:cd05941 300 svFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECA 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 559 IYGVTVPGHeGRAGMAALALRPP-QALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd05941 374 VIGVPDPDW-GERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
75-622 |
7.32e-40 |
|
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: 151.99 E-value: 7.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHAL-------------------------------RALG-----VAKGDRV 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALvlatefleslepdlpalramglhlwatgpe 232
Cdd:cd17631 49 AVLSKNSPEFLELLFAAARLG--AVFVPLNFRLTPpeVAYILADSGAKVL------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 tnvagisnllseaadqvdepvpgylsapqnIMDTCLYIFTSGTTGLPKAARISHLKVLqcqGFYHLCGVHQ----EDVIY 308
Cdd:cd17631 97 ------------------------------FDDLALLMYTSGTTGRPKGAMLTHRNLL---WNAVNALAALdlgpDDVLL 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 309 LALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF-----QYigelcrYLVNQPPSKAECDH-KVR- 381
Cdd:cd17631 144 VVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFflvptMI------QALLQHPRFATTDLsSLRa 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 LAVGSGLRPDTWERFLRRFGPlQILETYGMTE-GNVATFNYTGRQ----GAVGRASwlykhifPFSLIRydvmtgepIRN 456
Cdd:cd17631 218 VIYGGAPMPERLLRALQARGV-KFVQGYGMTEtSPGVTFLSPEDHrrklGSAGRPV-------FFVEVR--------IVD 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 457 AQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRW 534
Cdd:cd17631 282 PDGR--EVPPGEVGEIVV----RGPhvMAGYWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 535 KGENVATTEVAEVLETLDFLQEVNIYGvtVPgHE--GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:cd17631 349 GGENVYPAEVEDVLYEHPAVAEVAVIG--VP-DEkwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
570
....*....|
gi 82581629 613 ATTETFKQQK 622
Cdd:cd17631 426 PRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
70-612 |
1.37e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 149.67 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 70 RLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLA 149
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAAL-------------------------------AALG-----IG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAG-----LRTAFVPTA----LRRGpllhclrscGASALVLATEFLESLEP---DLP 217
Cdd:PRK07656 54 KGDRVAIWAPNSPHWVIAALGALKAGavvvpLNTRYTADEaayiLARG---------DAKALFVLGLFLGVDYSattRLP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 218 ALRamglHLWATGPETNVAGISNLLSE----AADQVDEPVPGYlsAPQNIMDTclyIFTSGTTGLPKAARISHLKVLQ-C 292
Cdd:PRK07656 125 ALE----HVVICETEEDDPHTEKMKTFtdflAAGDPAERAPEV--DPDDVADI---LFTSGTTGRPKGAMLTHRQLLSnA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 293 QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS 372
Cdd:PRK07656 196 ADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 373 KAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGN-VATFNYTGRQ-----GAVGRAswlykhifpfsli 444
Cdd:PRK07656 276 SAEDLSSLRLAVtgAASMPVALLERFESELGVDIVLTGYGLSEASgVTTFNRLDDDrktvaGTIGTA------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 445 rydvMTGEPIRNAQGHCMTTSPGEPG-LLVapvsqQSP--FLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGF 521
Cdd:PRK07656 343 ----IAGVENKIVNELGEEVPVGEVGeLLV-----RGPnvMKGYYDDPEATAAAI------DADGWLHTGDLGRLDEEGY 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 522 LHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPY 600
Cdd:PRK07656 408 LYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG--VPDERlGEVGKAYVVLKPGAELTEEELIAYCREHLAKY 485
|
570
....*....|..
gi 82581629 601 ARPRFLRLQESL 612
Cdd:PRK07656 486 KVPRSIEFLDEL 497
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
75-644 |
2.48e-37 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 146.80 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIH-----GAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLA 149
Cdd:COG0365 19 AEGRGDKVALIWegedgEERTLTYAELRREVNRFANAL-------------------------------RALG-----VK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLE-----SLEPDLPALRAMGL 224
Cdd:COG0365 63 KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRggkviDLKEKVDEALEELP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HLWA------TGPETNVAGISNLLSEAADQVDEPVPGYLSApqniMDTCLYIFTSGTTGLPKAARISH---LKVLQCQGF 295
Cdd:COG0365 143 SLEHvivvgrTGADVPMEGDLDWDELLAAASAEFEPEPTDA----DDPLFILYTSGTTGKPKGVVHTHggyLVHAATTAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 YHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFqyigelC------RY 365
Cdd:COG0365 219 YVL-DLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFpDPGRLWELIEKYGVTVF------FtaptaiRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 366 LVNQPPSKAEcDH---KVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTE--GNVATFNYTG--RQGAVGRaswlyk 436
Cdd:COG0365 292 LMKAGDEPLK-KYdlsSLRLLgsAGEPLNPEVWEWWYEAVG-VPIVDGWGQTEtgGIFISNLPGLpvKPGSMGK------ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 437 hifPFSLIRYDVM--TGEPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGD 512
Cdd:COG0365 364 ---PVPGYDVAVVdeDGNPVP----------PGEEGELVIKGPWPGMFRGYWNDPE-----RYRETYFGrfPGWYR-TGD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 513 LLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVniyGVT-VPgHEGRaGMAALA---LRPPQALN--L 586
Cdd:COG0365 425 GARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA---AVVgVP-DEIR-GQVVKAfvvLKPGVEPSdeL 499
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82581629 587 VQ-LYSHVSENLPPYARPRFLRLQESLATTETFKQQ-----KVRMANEGFDPSVLSDPlYVLDQ 644
Cdd:COG0365 500 AKeLQAHVREELGPYAYPREIEFVDELPKTRSGKIMrrllrKIAEGRPLGDTSTLEDP-EALDE 562
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
148-600 |
5.86e-37 |
|
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: 144.66 E-value: 5.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLepdLPALRAMGL--H 225
Cdd:cd05911 32 LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKV---KEAAKELGPkdK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATGPETN-VAGISNLLSEAADQVDEPVPGYLSAPQNimDTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCg 300
Cdd:cd05911 109 IIVLDDKPDgVLSIEDLLSPTLGEEDEDLPPPLKDGKD--DTAAILYSSGTTGLPKGVCLSHrnliANLSQVQTFLYGN- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 301 VHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHK 379
Cdd:cd05911 186 DGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPlLDKYDLSSL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 380 VRLAVGSG-LRPDTWERFLRRFGPLQILETYGMTEGNVATF---NYTGRQGAVGRaswlykhIFPFSLIRYDVMTGepiR 455
Cdd:cd05911 265 RVILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVGR-------LLPNVEAKIVDDDG---K 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 456 NAQGhcmttsPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWK 535
Cdd:cd05911 335 DSLG------PNEPGEIC--VRGPQVMKGYYNNPEATKETFDED----G--WLHTGDIGYFDEDGYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 536 GENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPY 600
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
137-627 |
7.19e-37 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 144.38 E-value: 7.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 137 DAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEfleSLEPDL 216
Cdd:cd05926 25 DDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKG---ELGPAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 PA-----LRAMGLHLWATGPETNVAG--ISNLLSEAADQVDEPVPgylSAPqnimDTCLYIFTSGTTGLPKAARISHLKV 289
Cdd:cd05926 102 RAasklgLAILELALDVGVLIRAPSAesLSNLLADKKNAKSEGVP---LPD----DLALILHTSGTTGRPKGVPLTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 290 lqCQGFYHLCGVHQ---EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYL 366
Cdd:cd05926 175 --AASATNITNTYKltpDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQIL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 367 VNQPPSKAEC-DHKVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTEgnvATFNYTGRQ--------GAVGRASwly 435
Cdd:cd05926 253 LNRPEPNPESpPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTE---AAHQMTSNPlppgprkpGSVGKPV--- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 436 khifpfslirydvmtGEPIR--NAQGHCMTtsPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDL 513
Cdd:cd05926 326 ---------------GVEVRilDEDGEILP--PGVVGEIC--LRGPNVTRGYLNNPEANAEAAFKD----G--WFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 514 LVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHV 593
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KYGEEVAAAVVLREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|....
gi 82581629 594 SENLPPYARPRFLRLQESLATTETFKQQKVRMAN 627
Cdd:cd05926 460 RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
75-612 |
2.38e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 125.82 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappLAPGATV 154
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-------------------------------DLG-----LKKGDRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGLrtAFVPT--ALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPE 232
Cdd:PRK08316 65 AALGHNSDAYALLWLACARAGA--VHVPVnfMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TNVAGISNLLSEAADQVDEPVPGylsAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLAL 311
Cdd:PRK08316 143 REAPGGWLDFADWAEAGSVAEPD---VELADDDLAQILYTSGTESLPKGAMLTHRALIaEYVSCIVAGDMSADDIPLHAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 312 PLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF-----QYIGelcryLVNQPpskaECDhKVRLavgS 386
Cdd:PRK08316 220 PLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFfapptVWIS-----LLRHP----DFD-TRDL---S 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 387 GLR---------P-DTWERFLRRFGPLQILETYGMTE-GNVATF----NYTGRQGAVGRASwlykhIFPFSLIRYDvmTG 451
Cdd:PRK08316 287 SLRkgyygasimPvEVLKELRERLPGLRFYNCYGQTEiAPLATVlgpeEHLRRPGSAGRPV-----LNVETRVVDD--DG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 452 EPIrnaqghcmttSPGEPGLLVApvsqQSPFL--GYAGAPELAkdkllKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTG 529
Cdd:PRK08316 360 NDV----------APGEVGEIVH----RSPQLmlGYWDDPEKT-----AEAFRGG--WFHSGDLGVMDEEGYITVVDRKK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 530 DTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 609
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP-KWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFV 497
|
...
gi 82581629 610 ESL 612
Cdd:PRK08316 498 DEL 500
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
74-622 |
1.64e-29 |
|
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: 122.86 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 74 LAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARgwtggrrgsgrgsteegarvappagdaaargttappLAPGAT 153
Cdd:cd05959 13 LNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALG------------------------------------VKREER 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 154 VALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPET 233
Cdd:cd05959 57 VLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 234 NVAGISNLlseaADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLC--------GVHQED 305
Cdd:cd05959 137 PEAGALLL----AELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH------ADIYWTAelyarnvlGIREDD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 306 VIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV 384
Cdd:cd05959 207 VCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 GSG--LRPDTWERFLRRFGpLQILETYGMTE-GNVATFNYTG--RQGAVGRASWLYKhifpfslIRydvmtgepIRNAQG 459
Cdd:cd05959 287 SAGeaLPAEVGERWKARFG-LDILDGIGSTEmLHIFLSNRPGrvRYGTTGKPVPGYE-------VE--------LRDEDG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 460 HcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENV 539
Cdd:cd05959 351 G--DVADGEPGELY--VRGPSSATMYWNNRDKTRDTFQGE--W-----TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 540 ATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRP---PQALNLVQLYSHVSENLPPYARPRFLRLQESLATTE 616
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KAFVVLRPgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTA 498
|
....*.
gi 82581629 617 TFKQQK 622
Cdd:cd05959 499 TGKIQR 504
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
305-666 |
5.64e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 123.67 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 305 DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV 384
Cdd:PRK07868 647 DTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTG-RQGAVGRAswlykhiFPFS----LIRYDVMTGEPIRNAQG 459
Cdd:PRK07868 727 GSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaKIGSKGRP-------LPGAgrveLAAYDPEHDLILEDDRG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 460 HCMTTSPGEPGLLvapvsqqspfLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENV 539
Cdd:PRK07868 800 FVRRAEVNEVGVL----------LARARGPIDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPV 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 540 ATTEVAEVLETLDFLQEVNIYGVTVPGHEgrAGMAALALRPPQALNLVQLYSHVSEnLPPYARPRFLRLQESLATTETFK 619
Cdd:PRK07868 870 YTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYR 946
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 82581629 620 QQKVRMANEGFdPSVLSDPLYvLDQDIGAYLPLTPARYSALLSGDLR 666
Cdd:PRK07868 947 PTVSALRAAGI-PKPGRQAWY-FDPETNRYRRLTPAVRAELTGGHRR 991
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-626 |
6.03e-28 |
|
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: 115.45 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVLQcQGFY--HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSA 341
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVN-NGYFigERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDCQKHRVTVFQ-----YIGELCRylvnqpPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTE 413
Cdd:cd05917 82 LAVLEAIEKEKCTALHgvptmFIAELEH------PDFDKFDlSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 GNVATFNYTG------RQGAVGRaswlykhIFPFSLIRYDVMTG--EPIRNAQGHCMTTspgepGLLVapvsqqspFLGY 485
Cdd:cd05917 156 TSPVSTQTRTddsiekRVNTVGR-------IMPHTEAKIVDPEGgiVPPVGVPGELCIR-----GYSV--------MKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 486 AGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVP 565
Cdd:cd05917 216 WNDPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VP 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82581629 566 GHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMA 626
Cdd:cd05917 288 DERyGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
265-623 |
2.44e-27 |
|
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: 115.13 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHlcGVHQEDVIY-LALP--LYHMSGSLLGIvgcLGIGATVVL--K 336
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLHTHsypLGHIPTAAYWL--GLRPDDIHWnIADPgwAKGAWSSFFGP---WLLGATVFVyeG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 337 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHkVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG 414
Cdd:cd05972 157 PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 415 NVATFNYTG---RQGAVGRASWLYKhifpFSLIRYDvmtGEPIrnaqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPEl 491
Cdd:cd05972 235 GLTVGNFPDmpvKPGSMGRPTPGYD----VAIIDDD---GREL----------PPGEEGDIAIKLPPPGLFLGYVGDPE- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 492 aKDKllkdVFWSGDVFFnTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLetldfLQ--EVNIYGVTVPGHEG 569
Cdd:cd05972 297 -KTE----ASIRGDYYL-TGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL-----LEhpAVAEAAVVGSPDPV 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 570 RAGM--AALALR----PPQALNLvQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKV 623
Cdd:cd05972 366 RGEVvkAFVVLTsgyePSEELAE-ELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
79-615 |
6.31e-27 |
|
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: 114.16 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgstEEGARvappagdaaargttapplaPGATVALLL 158
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-----------------ERGVG-------------------PGDLVAVLL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGLrtAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRamglhlwatgpetnvagI 238
Cdd:cd05930 45 ERSLEMVVAILAVLKAGA--AYVP-----------------------------LDPSYPAER-----------------L 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 239 SNLLSEAADQVdepVpgyLSAPQNIMdtclY-IFTSGTTGLPKAARISHlkvlqcQGFYHLCGVHQEDV------IYLAL 311
Cdd:cd05930 77 AYILEDSGAKL---V---LTDPDDLA----YvIYTSGSTGKPKGVMVEH------RGLVNLLLWMQEAYpltpgdRVLQF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 312 PLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG- 387
Cdd:cd05930 141 TSFSFDVSVWEIFGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGe 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 388 -LRPDTWERFLRRFGPLQILETYGMTEGNV-ATFnytgrqgavgraswlykHIFPFSLIRYDVMT-GEPIRNAQ-----G 459
Cdd:cd05930 219 aLPPDLVRRWRELLPGARLVNLYGPTEATVdATY-----------------YRVPPDDEEDGRVPiGRPIPNTRvyvldE 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 460 HCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENV 539
Cdd:cd05930 282 NLRPVPPGVPGELY--IGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82581629 540 ATTEVAEVLETLDFLQEVniygVTVPGHEGRAGM---AALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:cd05930 360 ELGEIEAALLAHPGVREA----AVVAREDGDGEKrlvAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
71-548 |
2.05e-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: 113.70 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappLAP 150
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLL-------------------------------ALG-----LRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLAT--------EFLESLEPDLPALRam 222
Cdd:COG1021 75 GDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVPSLR-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 223 glHLWATGPETNVAGISNLLSEAADqVDEPVPgylsAPQnimDTCLYIFTSGTTGLPK---------------AARIshl 287
Cdd:COG1021 153 --HVLVVGDAGEFTSLDALLAAPAD-LSEPRP----DPD---DVAFFQLSGGTTGLPKliprthddylysvraSAEI--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 288 kvlqcqgfyhlCGVHQEDViYL-ALPLYH-MSGSLLGIVGCLGIGATVVLKPKFSAsqfwDDC----QKHRVTVfqyIGe 361
Cdd:COG1021 220 -----------CGLDADTV-YLaALPAAHnFPLSSPGVLGVLYAGGTVVLAPDPSP----DTAfpliERERVTV---TA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 362 lcryLVnqPP-------SKAECDHKVR-LAV----GSGLRPDTWERFLRRFGP-LQilETYGMTEGNVatfNYTG----- 423
Cdd:COG1021 280 ----LV--PPlallwldAAERSRYDLSsLRVlqvgGAKLSPELARRVRPALGCtLQ--QVFGMAEGLV---NYTRlddpe 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 424 --RQGAVGRAswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPEL-AKdkllk 498
Cdd:COG1021 349 evILTTQGRP------ISPDDEVR--------IVDEDGN--PVPPGEVGELLT----RGPytIRGYYRAPEHnAR----- 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 82581629 499 dVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVL 548
Cdd:COG1021 404 -AF-TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL 451
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
140-548 |
2.80e-26 |
|
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: 113.10 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 140 ARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGlrtAFVPTA---LRRGPLLHCLRSCGASALVLATEFLESLEPDL 216
Cdd:cd05904 46 AAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG---AVVTTAnplSTPAEIAKQVKDSGAKLAFTTAELAEKLASLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 PALRAMGlhlwatGPETNVAGISNLLSEAaDQVDEPVPgylSAPQNimDTCLYIFTSGTTGLPKAARISHLK-VLQCQGF 295
Cdd:cd05904 123 LPVVLLD------SAEFDSLSFSDLLFEA-DEAEPPVV---VIKQD--DVAALLYSSGTTGRSKGVMLTHRNlIAMVAQF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 --YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFqyigelcrYLVnqPP-- 371
Cdd:cd05904 191 vaGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL--------PVV--PPiv 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 372 ---SKAECDHKVRLA----VGSG---LRPDTWERFLRRFGPLQILETYGMTE-GNVATFNYT-----GRQGAVGR--ASW 433
Cdd:cd05904 261 lalVKSPIVDKYDLSslrqIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApekdrAKYGSVGRlvPNV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 434 LYKHIfpfsliryDVMTGEPIrnaqghcmttSPGEPG-LLVapvsqQSPFL--GYAGAPELAKDKLLKDvfwsGdvFFNT 510
Cdd:cd05904 341 EAKIV--------DPETGESL----------PPNQTGeLWI-----RGPSImkGYLNNPEATAATIDKE----G--WLHT 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 82581629 511 GDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVL 548
Cdd:cd05904 392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
72-604 |
3.66e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 113.10 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 72 AYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappLAPG 151
Cdd:PRK07788 56 AHAARRAPDRAALIDERGTLTYAELDEQSNALARGLL-------------------------------ALG-----VRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 152 ATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF---LESLEPDLPALRAMGLHlwA 228
Cdd:PRK07788 100 DGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFtdlLSALPPDLGRLRAWGGN--P 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 229 TGPETNVAGISNLLSEAADQVDEPVPgylSAPQNimdTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVI 307
Cdd:PRK07788 178 DDDEPSGSTDETLDDLIAGSSTAPLP---KPPKP---GGIVILTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFRAGETT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 308 YLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP---SKAECDH-KVRLA 383
Cdd:PRK07788 252 LLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPevlAKYDTSSlKIIFV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 384 VGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATFnyTGRQ------GAVGRaswlykhifPFSLIR---YDvMTGEPI 454
Cdd:PRK07788 331 SGSALSPELATRALEAFGPV-LYNLYGSTEVAFATI--ATPEdlaeapGTVGR---------PPKGVTvkiLD-ENGNEV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 455 rnaqghcmttSPGEPGLLVapVSQQSPFLGYAGapelAKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTIRW 534
Cdd:PRK07788 398 ----------PRGVVGRIF--VGNGFPFEGYTD----GRDKQIIDGLLS------SGDVGYFDEDGLLFVDGRDDDMIVS 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82581629 535 KGENVATTEVAEVLETLDFLQEVNIYGVTVP--GHEGRagmAALALRPPQALNLVQLYSHVSENLPPYARPR 604
Cdd:PRK07788 456 GGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefGQRLR---AFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
216-604 |
1.05e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 112.02 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 216 LPALRAMGLHLwaTGPETNVAGISNLLSEAA----DQVDEPVPgylsAPQnimDTCLYIFTSGTTGLPKAARISH--LKV 289
Cdd:PRK05605 176 IPALRKARAAL--TGPAPGTVPWETLVDAAIggdgSDVSHPRP----TPD---DVALILYTSGTTGKPKGAQLTHrnLFA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 290 LQCQGFYHLCGV-HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 368
Cdd:PRK05605 247 NAAQGKAWVPGLgDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 369 QPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLqILETYGMTE------GNvaTFNYTGRQGAVGRAswlykhiFP 440
Cdd:PRK05605 327 AAEERGVDLSGVRNAFsgAMALPVSTVELWEKLTGGL-LVEGYGLTEtspiivGN--PMSDDRRPGYVGVP-------FP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 441 FSLIRydvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAKDKLLKDvfWsgdvfFNTGDLLVCDEQG 520
Cdd:PRK05605 397 DTEVR--------IVDPEDPDETMPDGEEGELLVRGPQV--FKGYWNRPEETAKSFLDG--W-----FRTGDVVVMEEDG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 521 FLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGRAGM-AALALRPPQALNLVQLYSHVSENLPP 599
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVvAAVVLEPGAALDPEGLRAYCREHLTR 537
|
....*
gi 82581629 600 YARPR 604
Cdd:PRK05605 538 YKVPR 542
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
60-604 |
8.97e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.59 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 60 SSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaA 139
Cdd:PRK07470 2 MSRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAAL-------------------------------A 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 140 ARGttappLAPGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALVLATEFLESLEpdlp 217
Cdd:PRK07470 51 ARG-----VRKGDRILVHSRNCNQMFESMFAAFRLG--AVWVPTNFRQTPdeVAYLAEASGARAMICHADFPEHAA---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 218 ALRAMGLHLwatgpeTNVAGISNllSEAADQVDEPVPGYLSAPQNIM-----DTCLYIFTSGTTGLPKAARISHLKVlqc 292
Cdd:PRK07470 120 AVRAASPDL------THVVAIGG--ARAGLDYEALVARHLGARVANAavdhdDPCWFFFTSGTTGRPKAAVLTHGQM--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 293 qGFY---HLC----GVHQEDVIYLALPLYHMSG--SLLGIVGclgiGATVVLKP--KFSASQFWDDCQKHRVTVFQYIGE 361
Cdd:PRK07470 189 -AFVitnHLAdlmpGTTEQDASLVVAPLSHGAGihQLCQVAR----GAATVLLPseRFDPAEVWALVERHRVTNLFTVPT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 362 LCRYLVnQPPSKAECDH-KVRLAVGSG---LRPDTwERFLRRFGPLqILETYGMTEgnvATFNYT--------------G 423
Cdd:PRK07470 264 ILKMLV-EHPAVDRYDHsSLRYVIYAGapmYRADQ-KRALAKLGKV-LVQYFGLGE---VTGNITvlppalhdaedgpdA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 424 RQGAVGRASwlykhifpfslirydvmTGE--PIRNAQGHCMttSPGEPGLLVapVSQQSPFLGYAGAPElAKDKLLKDvF 501
Cdd:PRK07470 338 RIGTCGFER-----------------TGMevQIQDDEGREL--PPGETGEIC--VIGPAVFAGYYNNPE-ANAKAFRD-G 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 502 WsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPP 581
Cdd:PRK07470 395 W-----FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVW-GEVGVAVCVARDG 468
|
570 580
....*....|....*....|...
gi 82581629 582 QALNLVQLYSHVSENLPPYARPR 604
Cdd:PRK07470 469 APVDEAELLAWLDGKVARYKLPK 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
75-603 |
1.95e-24 |
|
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: 107.29 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARRL-------------------------------RAAG-----VGPGDVV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALVlatefleslepDLPALRAmglhlWATGPE 232
Cdd:cd12117 51 GVLAERSPELVVALLAVLKAG--AAYVPLDPELPAerLAFMLADAGAKVLL-----------TDRSLAG-----RAGGLE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TNVagisnLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLcGVHQEDVIYLAL 311
Cdd:cd12117 113 VAV-----VIDEALDAGPAGNPAVPVSPD---DLAYVMYTSGSTGRPKGVAVTHRGVVRlVKNTNYV-TLGPDDRVLQTS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 312 PLyHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPskaECDHKVR--LAVGS 386
Cdd:cd12117 184 PL-AFDASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLADEDP---ECFAGLRelLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 387 GLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMTTS- 465
Cdd:cd12117 260 VVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGS---------------IPIGRPIANTRVYVLDEDg 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 466 ----PGEPGLLV---APVSqqspfLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGEN 538
Cdd:cd12117 325 rpvpPGVPGELYvggDGLA-----LGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 539 VATTEVAEVLETLDFLQEVniyGVTVpgHEGRAGMAALA--LRPPQALNLVQLYSHVSENLPPYARP 603
Cdd:cd12117 400 IELGEIEAALRAHPGVREA---VVVV--REDAGGDKRLVayVVAEGALDAAELRAFLRERLPAYMVP 461
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
82-626 |
2.02e-24 |
|
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: 106.79 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 82 TFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsTEEGARVappagdaaargttapplaPGATVALLLPAG 161
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVL-----------------VGELGIV------------------PGNRVLLRGSNS 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 162 PDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCgasalvlatefleslepdlpalramglhlwatgpETNVAgisnL 241
Cdd:cd05958 47 PELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA----------------------------------RITVA----L 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 242 LSEAADQVDepvpgylsapqnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGF-YHLCGVHQEDVIYLALPLYHMSGS 319
Cdd:cd05958 89 CAHALTASD--------------DICILAFTSGTTGAPKATMHFHRDPLAsADRYaVNVLRLREDDRFVGSPPLAFTFGL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 320 LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFL 397
Cdd:cd05958 155 GGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGeaLPAALHRAWK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 398 RRFGpLQILETYGMTEGNVATFNYTGRQGAVGRaswlykhifpfslirydvmTGEP-------IRNAQGHcmTTSPGEPG 470
Cdd:cd05958 235 EATG-IPIIDGIGSTEMFHIFISARPGDARPGA-------------------TGKPvpgyeakVVDDEGN--PVPDGTIG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 471 LLVApvsqQSPfLGYAGapeLAkDKLLKDVFwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLET 550
Cdd:cd05958 293 RLAV----RGP-TGCRY---LA-DKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQ 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82581629 551 LDFLQEVNIYGVTVPGhEGRAGMAALALRP---PQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMA 626
Cdd:cd05958 362 HPAVAECAVVGHPDES-RGVVVKAFVVLRPgviPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
66-612 |
4.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 106.51 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 66 SLAWRLAYLAREQPTHTFLIHGAQRFSYAEAEResnriaraflrargwtggrrgsgrgsteegaRVAPPAGDAAARGTTA 145
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQ-------------------------------RILQAAGMLHARGIGQ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 146 pplapGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALVLATEFleslepdlpalramg 223
Cdd:PRK06145 52 -----GDVVALLMKNSAAFLELAFAASYLG--AVFLPINYRLAAdeVAYILGDAGAKLLLVDEEF--------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 224 lhlwatgpETNVA-GISNLLSEAADQVD---------EPVPGYLSAPQNIMDtclYIFTSGTTGLPKAARISHLKVlQCQ 293
Cdd:PRK06145 110 --------DAIVAlETPKIVIDAAAQADsrrlaqgglEIPPQAAVAPTDLVR---LMYTSGTTDRPKGVMHSYGNL-HWK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 294 GFYHLC--GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIG-ELCRYLVNQP 370
Cdd:PRK06145 178 SIDHVIalGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPvMLSRVLTVPD 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 371 PSKAECDhKVRLAVGSGLRpdTWERFLRRFGPL----QILETYGMTEG-NVATFNYTGRQ----GAVGRAswlYKHIfpf 441
Cdd:PRK06145 258 RDRFDLD-SLAWCIGGGEK--TPESRIRDFTRVftraRYIDAYGLTETcSGDTLMEAGREiekiGSTGRA---LAHV--- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 442 slirydvmtgePIRNAQGHCMTTSPGEPG--LLVAPVSQQspflGYAGAPELAKDKLLKDVFWSGDVFFntgdllvCDEQ 519
Cdd:PRK06145 329 -----------EIRIADGAGRWLPPNMKGeiCMRGPKVTK----GYWKDPEKTAEAFYGDWFRSGDVGY-------LDEE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 520 GFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVtvpgHEGRAG---MAALALRPPQALNLVQLYSHVSEN 596
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGV----HDDRWGeriTAVVVLNPGATLTLEALDRHCRQR 462
|
570
....*....|....*.
gi 82581629 597 LPPYARPRFLRLQESL 612
Cdd:PRK06145 463 LASFKVPRQLKVRDEL 478
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-612 |
5.90e-24 |
|
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: 105.60 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAG--LRTAFVPT-ALRRGPLLHCLRSCGASALVLATEFLES-LE 213
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrLGLVFVPLnPTLKESVLRYLVADAGGRIVLADAGAADrLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 214 PDLPALRAMGLhlwatgpetnvagisNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-QC 292
Cdd:cd05922 85 DALPASPDPGT---------------VLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLaNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 293 QGFYHLCGVHQEDVIYLALPLYHMSG-SLLGIvgCLGIGATVVLKPKFSASQ-FWDDCQKHRVTVFQ---YIGELCRYLV 367
Cdd:cd05922 147 RSIAEYLGITADDRALTVLPLSYDYGlSVLNT--HLLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 368 NQPpskAECDHKVRLAVGSGLRPDTWERFLRRFGPL-QILETYGMTEgnvATFNYT--------GRQGAVGRAswlykhi 438
Cdd:cd05922 225 FDP---AKLPSLRYLTQAGGRLPQETIARLRELLPGaQVYVMYGQTE---ATRRMTylpperilEKPGSIGLA------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 439 FPFSLIRYDVMTGEPirnaqghcmtTSPGEPGLLVAPVSQQSpfLGYAGAP-ELAKDKLLKDVFWsgdvffnTGDLLVCD 517
Cdd:cd05922 292 IPGGEFEILDDDGTP----------TPPGEPGEIVHRGPNVM--KGYWNDPpYRRKEGRGGGVLH-------TGDLARRD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 518 EQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEgraGMAALALRPPQaLNLVQLYSHVSENL 597
Cdd:cd05922 353 EDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDK-IDPKDVLRSLAERL 428
|
490
....*....|....*
gi 82581629 598 PPYARPRFLRLQESL 612
Cdd:cd05922 429 PPYKVPATVRVVDEL 443
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
137-625 |
8.21e-24 |
|
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: 104.77 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 137 DAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFleslepdl 216
Cdd:cd05903 12 DRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERF-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 palRAMglhlwatgpetnvagisnllseaaDQVDEPVpgylsapqnimDTCLYIFTSGTTGLPKAARISH--LKVLQCQG 294
Cdd:cd05903 84 ---RQF------------------------DPAAMPD-----------AVALLLFTSGTTGEPKGVMHSHntLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 295 FYHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQ----YIGELCRYLVNQP 370
Cdd:cd05903 126 AERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTDLLNAVEEAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 371 PskAECDHKVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATFNYTgrQGAVGRASWLYKHIFPfslirydvmt 450
Cdd:cd05903 205 E--PLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAVTSIT--PAPEDRRLYTDGRPLP---------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 451 GEPIRNAQGHCMTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRT 528
Cdd:cd05903 270 GVEIKVVDDTGATLAPGVEGELLS----RGPsvFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 529 GDTIRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHE----GRAGMAALALRPPQALNLVQLYSHVS-ENLPPYARP 603
Cdd:cd05903 339 KDIIIRGGENIPVLEVEDLL-----LGHPGVIEAAVVALPderlGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWP 413
|
490 500
....*....|....*....|..
gi 82581629 604 RFLRLQESLATTETFKQQKVRM 625
Cdd:cd05903 414 ERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
137-625 |
1.47e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.14 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 137 DAAARGTTAPPLAPGATVALLLPAGpdflWIWFGLAKAGLRTAFVPTAL----RRGPLLHCLRSCGASALVLATEF---- 208
Cdd:PRK13295 66 DRVAVGLARLGVGRGDVVSCQLPNW----WEFTVLYLACSRIGAVLNPLmpifRERELSFMLKHAESKVLVVPKTFrgfd 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 209 ----LESLEPDLPALRamglHLWATGPETNVaGISNLLSEAADQVDEPVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAAR 283
Cdd:PRK13295 142 haamARRLRPELPALR----HVVVVGGDGAD-SFEALLITPAWEQEPDAPAILARLRpGPDDVTQLIYTSGTTGEPKGVM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 284 ISHLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTvFQ----- 357
Cdd:PRK13295 217 HTANTLMANIVPYaERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastp 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 358 YIGELCRYLVNQPPSKAECdhKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFNYTGRqgAVGRASWLYKH 437
Cdd:PRK13295 296 FLTDLTRAVKESGRPVSSL--RTFLCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVTLTKLDD--PDERASTTDGC 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 438 IFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDkllkdvfwSGDVFFNTGDLLVCD 517
Cdd:PRK13295 371 PLPGVEVR--------VVDADGA--PLPAGQIGRLQ--VRGCSNFGGYLKRPQLNGT--------DADGWFDTGDLARID 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 518 EQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPghEGRAGMAALA---LRPPQALNLVQLYSHV- 593
Cdd:PRK13295 431 ADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvPRPGQSLDFEEMVEFLk 506
|
490 500 510
....*....|....*....|....*....|..
gi 82581629 594 SENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK13295 507 AQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
150-548 |
1.56e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 105.42 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPtALRRGPLLHCLRSCGASALVLATEF--------LESLEPDLPALRA 221
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEAAGIANPINP-LLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkVAEVLAALPELRT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 222 M---GLHLWATGPETNV---------AGISNLLSEAADQvdePVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAARISHL- 287
Cdd:PRK07529 161 VvevDLARYLPGPKRLAvplirrkahARILDFDAELARQ---PGDRLFSGRPiGPDDVAAYFHTGGTTGMPKLAQHTHGn 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 288 KVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA------SQFWDDCQKHRVTVFQYIGE 361
Cdd:PRK07529 238 EVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYrgpgviANFWKIVERYRINFLSGVPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 362 LCRYLVNQPPSKAECDhKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTEGN-VATFNYTG---RQGAVGRAswly 435
Cdd:PRK07529 318 VYAALLQVPVDGHDIS-SLRYALcgAAPLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPDgerRIGSVGLR---- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 436 khiFPFSLIRydVMTGEPIRNAQGHCmttSPGEPGLLVapVSQQSPFLGYAgapELAKDKLLkdvfWSGDVFFNTGDLLV 515
Cdd:PRK07529 392 ---LPYQRVR--VVILDDAGRYLRDC---AVDEVGVLC--IAGPNVFSGYL---EAAHNKGL----WLEDGWLNTGDLGR 454
|
410 420 430
....*....|....*....|....*....|...
gi 82581629 516 CDEQGFLHFHDRTGDTIRWKGENVATTEVAEVL 548
Cdd:PRK07529 455 IDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
265-619 |
8.06e-23 |
|
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: 101.79 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAaNALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG-NVATFN 420
Cdd:cd05935 165 ALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 421 YTGRQgavgRASWLYKHIFPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDv 500
Cdd:cd05935 244 PPLRP----KLQCLGIP*FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQIFKGYWNRPEETEESFIEI- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 501 fwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALR 579
Cdd:cd05935 307 --KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV--ISVPDERvGEEVKAFIVLR 382
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 82581629 580 PPQALNLVQ--LYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd05935 383 PEYRGKVTEedIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
71-625 |
1.36e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.16 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQPTHTFLI--HGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGTTappl 148
Cdd:PRK12583 24 FDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLL-------------------------------ALGVQ---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 149 aPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF--------LESLEP------ 214
Cdd:PRK12583 69 -PGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFktsdyhamLQELLPglaegq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 215 -------DLPALRamGLHLWATGPETNVAGISNLLSEA---ADQVDEPVPGYLSA--PQNIMdtclyiFTSGTTGLPKAA 282
Cdd:PRK12583 148 pgalaceRLPELR--GVVSLAPAPPPGFLAWHELQARGetvSREALAERQASLDRddPINIQ------YTSGTTGFPKGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 283 RISHLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSASQFWDDCQKHRVTVFQ--- 357
Cdd:PRK12583 220 TLSHHNILNNGYFVaESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 358 --YIGELcrylvnQPPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTG------RQG 426
Cdd:PRK12583 300 tmFIAEL------DHPQRGNFDlSSLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAaddlerRVE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 427 AVGRaswlykhifpfSLIRYDVmtgePIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvfwSGDV 506
Cdd:PRK12583 374 TVGR-----------TQPHLEV----KVVDPDGA--TVPRGEIGELC--TRGYSVMKGYWNNPEATAESI------DEDG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 507 FFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNL 586
Cdd:PRK12583 429 WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY-GEEIVAWVRLHPGHAASE 507
|
570 580 590
....*....|....*....|....*....|....*....
gi 82581629 587 VQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK12583 508 EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
75-625 |
1.67e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 102.04 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIArAFLrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFA-ALL------------------------------RQRG-----VGAGDRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPTA--LRRGPLLHCLRSCGASALVLATEFLESLEPDLPALR-------AMGLH 225
Cdd:PRK06178 87 AVFLPNCPQFHIVFFGILKLG--AVHVPVSplFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSlrhvivtSLADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWAT----------GPETNVAGISNLLS--EAADQVDEPVPGYLSAPQNIMdtclyiFTSGTTGLPKAARISHLK-VLQC 292
Cdd:PRK06178 165 LPAEptlplpdslrAPRLAAAGAIDLLPalRACTAPVPLPPPALDALAALN------YTGGTTGMPKGCEHTQRDmVYTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 293 QGFYHLCGVHQEDVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVfqyigelCRYLVNQP- 370
Cdd:PRK06178 239 AAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTR-------TVMLVDNAv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 371 -----PSKAECDHKVRLAVGS-----GLRPDTWERFLRRFGPLQILETYGMTEGNVA-TFNyTGRQgaVGRASWLYKHIF 439
Cdd:PRK06178 312 elmdhPRFAEYDLSSLRQVRVvsfvkKLNPDYRQRWRALTGSVLAEAAWGMTETHTCdTFT-AGFQ--DDDFDLLSQPVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 440 -----PFSLIRY-DVMTGEPIrnaqghcmttsP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLkdvfwsgDVFFNTGD 512
Cdd:PRK06178 389 vglpvPGTEFKIcDFETGELL-----------PlGAEGEIV--VRTPSLLKGYWNKPEATAEALR-------DGWLHTGD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 513 LLVCDEQGFLHFHDRTGDTIRWKGENVATTEVaEVLetldFLQEVNIYGVTVPG----HEGRAGMAALALRPPQALNLVQ 588
Cdd:PRK06178 449 IGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV-EAL----LGQHPAVLGSAVVGrpdpDKGQVPVAFVQLKPGADLTAAA 523
|
570 580 590
....*....|....*....|....*....|....*..
gi 82581629 589 LYSHVSENLPPYARPRfLRLQESLATTETFKQQKVRM 625
Cdd:PRK06178 524 LQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
268-619 |
1.77e-22 |
|
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: 98.63 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYI-FTSGTTGLPKAARISH---LKVLQCQGfyHLCGVHQEDVIYLALPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSErswIESFVCNE--DLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQppskAECDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 421
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGqkLFESTKKKLKNIFPKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 422 TG---RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGhcmttspGEPGLLVApvsqQSP--FLGYAGAPELAKDKl 496
Cdd:cd17633 156 NQesrPPNSVGR-------PFPNVEIE--------IRNADG-------GEIGKIFV----KSEmvFSGYVRGGFSNPDG- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 497 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHEGRaGMAAL 576
Cdd:cd17633 209 -----W-----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP---DARF-GEIAV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 82581629 577 ALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd17633 275 ALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
89-619 |
2.08e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 101.13 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 89 QRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLLPAGPDFLWIW 168
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGL-------------------------------RALG-----LREGDVVAILLENNPEFFEVY 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 169 FGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPEtnVAGISNLLSEAADQ 248
Cdd:PRK08276 54 WAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGP--VPGFRSYEEALAAQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 249 VDEP----VPGYLsapqniMdtcLYifTSGTTGLPKAAR--ISHLKVLQCQG------FYHLCGVhqEDVIYLA-LPLYH 315
Cdd:PRK08276 132 PDTPiadeTAGAD------M---LY--SSGTTGRPKGIKrpLPGLDPDEAPGmmlallGFGMYGG--PDSVYLSpAPLYH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 316 mSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS-KAECD---HKVRLAVGSGLRPD 391
Cdd:PRK08276 199 -TAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvRARYDvssLRVAIHAAAPCPVE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 392 TWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAVGRAsWLYK-HIFPfslirydvMTGEPIrnaqghcmttSP 466
Cdd:PRK08276 278 VKRAMIDWWGPI-IHEYYASSEGGGVTVitseDWLAHPGSVGKA-VLGEvRILD--------EDGNEL----------PP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 467 GEPGLLVapVSQQSPFLGYAGAPELAKDKllkdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAE 546
Cdd:PRK08276 338 GEIGTVY--FEMDGYPFEYHNDPEKTAAA------RNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIEN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 547 VLETLDFLQEVNIYGV--------------TVPGHEGRAGMAAlalrppqalnlvQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:PRK08276 410 LLVTHPKVADVAVFGVpdeemgervkavvqPADGADAGDALAA------------ELIAWLRGRLAHYKCPRSIDFEDEL 477
|
....*..
gi 82581629 613 ATTETFK 619
Cdd:PRK08276 478 PRTPTGK 484
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
260-619 |
1.26e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 99.34 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 260 PQNimDTCLYIFTSGTTGLPKAARISHLKVLQCQgfyhLCGVH-------QEDVIYLALPLYHMSGslLGIVGCLGI--G 330
Cdd:PRK06710 204 PEN--DLALLQYTGGTTGFPKGVMLTHKNLVSNT----LMGVQwlynckeGEEVVLGVLPFFHVYG--MTAVMNLSImqG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 331 ATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV-GSGLRP-DTWERFLRRFGPlQILET 408
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPvEVQEKFETVTGG-KLVEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 409 YGMTEGNVAT---FNYTGR-QGAVGrASWLYKHIFPFSLirydvMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLG 484
Cdd:PRK06710 355 YGLTESSPVThsnFLWEKRvPGSIG-VPWPDTEAMIMSL-----ETGEALP----------PGEIGEIV--VKGPQIMKG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 485 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTV 564
Cdd:PRK06710 417 YWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 565 PgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:PRK06710 490 P-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGK 543
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
265-625 |
2.12e-21 |
|
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: 97.53 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLK-VLQCQGF-YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SA 341
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDpLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTEgNVATF 419
Cdd:cd05919 172 ERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATE-VGHIF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 420 --NYTG--RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDK 495
Cdd:cd05919 250 lsNRPGawRLGSTGR-------PVPGYEIR--------LVDEEGH--TIPPGEEGDLL--VRGPSAAVGYWNNPEKSRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 496 LLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTvPGHEGRAGMAA 575
Cdd:cd05919 311 FN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAF 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 82581629 576 LALRPPQALNLV---QLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:cd05919 383 VVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
151-628 |
2.85e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 97.34 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALramglhlwatg 230
Cdd:PRK03640 52 GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVK----------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 231 petnvagISNLLSEAADQVDEPVPGYLSAPQNIMdtclyiFTSGTTGLPKAarishlkVLQCQGfYHL---------CGV 301
Cdd:PRK03640 121 -------FAELMNGPKEEAEIQEEFDLDEVATIM------YTSGTTGKPKG-------VIQTYG-NHWwsavgsalnLGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 302 HQEDVIYLALPLYHMSG-SLLgiVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPsKAECDHKV 380
Cdd:PRK03640 180 TEDDCWLAAVPIFHISGlSIL--MRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLG-EGTYPSSF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 381 R-LAVGSGLRP-DTWERFLRRFGPlqILETYGMTE--GNVATFNYTGRQGAVGRASwlyKHIFPFSL-IRYDVMTGEPir 455
Cdd:PRK03640 257 RcMLLGGGPAPkPLLEQCKEKGIP--VYQSYGMTEtaSQIVTLSPEDALTKLGSAG---KPLFPCELkIEKDGVVVPP-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 456 NAQGHCMTTSPGepgllVAPvsqqspflGYagapeLAKDKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWK 535
Cdd:PRK03640 330 FEEGEIVVKGPN-----VTK--------GY-----LNREDATRETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 536 GENVATTEVAEVLETLDFLQEVNIYGVTvpghEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLAT 614
Cdd:PRK03640 390 GENIYPAEIEEVLLSHPGVAEAGVVGVP----DDKWGQVPVAfVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPR 465
|
490
....*....|....
gi 82581629 615 TETFKQQKVRMANE 628
Cdd:PRK03640 466 NASGKLLRHELKQL 479
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
75-623 |
4.53e-21 |
|
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: 97.18 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIH----GAQR-FSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLA 149
Cdd:cd05970 27 AKEYPDKLALVWcddaGEERiFTFAELADYSDKTANFF-------------------------------KAMG-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATE--FLESLEPDLPALRAMGLHLW 227
Cdd:cd05970 71 KGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 228 ATGPETNvaGISNLLSEAADQV-DEPVPGYLSAPQNiMDTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHLCgvhQ 303
Cdd:cd05970 151 VGDPVPE--GWIDFRKLIKNASpDFERPTANSYPCG-EDILLVYFSSGTTGMPKMVEHDFtypLGHIVTAKYWQNV---R 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 304 EDVIYLALP----LYHMSGSLLG--IVGClgigATVVLK-PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAEC 376
Cdd:cd05970 225 EGGLHLTVAdtgwGKAVWGKIYGqwIAGA----AVFVYDyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 377 DhKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEGNVATFNYTG---RQGAVGRASWLYkhifPFSLIRYD---V 448
Cdd:cd05970 301 S-SLRYCTTAGeaLNPEVFNTFKEKTG-IKLMEGFGQTETTLTIATFPWmepKPGSMGKPAPGY----EIDLIDREgrsC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 449 MTGEpirnaQGH-CMTTSPGEP-GLlvapvsqqspFLGYAGAPELAKDkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHD 526
Cdd:cd05970 375 EAGE-----EGEiVIRTSKGKPvGL----------FGGYYKDAEKTAE-----VWHDG--YYHTGDAAWMDEDGYLWFVG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 527 RTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALAL----RPPQALNlVQLYSHVSENLPPYAR 602
Cdd:cd05970 433 RTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDP-IRGQVVKATIVLakgyEPSEELK-KELQDHVKKVTAPYKY 510
|
570 580
....*....|....*....|.
gi 82581629 603 PRFLRLQESLATTETFKQQKV 623
Cdd:cd05970 511 PRIVEFVDELPKTISGKIRRV 531
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
148-628 |
7.95e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 96.74 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF--------LESLEPDLPAL 219
Cdd:PRK06087 71 IEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvdlILPLQNQLPQL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 220 RAMGLhLWATGPETNVAGISNLLSEAadqvdEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLKVLQCQGFYh 297
Cdd:PRK06087 151 QQIVG-VDKLAPATSSLSLSQIIADY-----EP----LTTAITTHgdELAAVLFTSGTEGLPKGVMLTHNNILASERAY- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 298 LCGVH--QEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT----VFQYIGELCRYLVNQPP 371
Cdd:PRK06087 220 CARLNltWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDLLNLLEKQPA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 372 SKAECdhKVRLAVGSGLRPDTWERFLRRfgPLQILETYGMTEGNVATF----NYTGRQGAV-GRAswlykhifpfsliry 446
Cdd:PRK06087 300 DLSAL--RFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAVvnldDPLSRFMHTdGYA--------------- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 447 dvMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAkDKLLKDVFWsgdvfFNTGDLLVCDEQGFLHFHD 526
Cdd:PRK06087 361 --AAGVEIKVVDEARKTLPPGCEGEEASRGPNV--FMGYLDEPELT-ARALDEEGW-----YYSGDLCRMDEAGYIKITG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 527 RTGDTIRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGH-EGRAG---MAALALRPP-QALNLVQLYSHVSEN-LPPY 600
Cdd:PRK06087 431 RKKDIIVRGGENISSREVEDIL-----LQHPKIHDACVVAMpDERLGersCAYVVLKAPhHSLTLEEVVAFFSRKrVAKY 505
|
490 500
....*....|....*....|....*...
gi 82581629 601 ARPRFLRLQESLATTETFKQQKVRMANE 628
Cdd:PRK06087 506 KYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
76-619 |
8.34e-21 |
|
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: 96.88 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 76 REQPTHTFLIH------GAQRFSYAEAERESNRIARAFLRArgwtggrrgsgrgSTEEGARVAppagdaaargtTAPPLA 149
Cdd:cd17634 64 RENGDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDL-------------GVKKGDRVA-----------IYMPMI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPA--GPDFLWIWFGLAKAGLRTAfvptalrrgpllhcLRSCGASALVLATEFLESLEP-DLPALRAMGLHL 226
Cdd:cd17634 120 PEAAVAMLACAriGAVHSVIFGGFAPEAVAGR--------------IIDSSSRLLITADGGVRAGRSvPLKKNVDDALNP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 227 WATGPETNVA----GISNLLSEAAD-----QVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH--LKVLQCQGF 295
Cdd:cd17634 186 NVTSVEHVIVlkrtGSDIDWQEGRDlwwrdLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFQYIGELCRYLVNQPP 371
Cdd:cd17634 266 KYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 372 SKAE----CDHKVRLAVGSGLRPDTWERFLRRFGPLQ--ILETYGMTEgnVATFNYTGRQGAVGRASWlyKHIFPFSLIR 445
Cdd:cd17634 346 DAIEgtdrSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE--TGGFMITPLPGAIELKAG--SATRPVFGVQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 446 YDVMtgepirNAQGHcmTTSPGEPGLLVAPVSQQSPFLGYAGAPelakDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFH 525
Cdd:cd17634 422 PAVV------DNEGH--PQPGGTEGNLVITDPWPGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWIT 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 526 DRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR----PPQALNlVQLYSHVSENLPPYA 601
Cdd:cd17634 490 GRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNhgvePSPELY-AELRNWVRKEIGPLA 567
|
570
....*....|....*...
gi 82581629 602 RPRFLRLQESLATTETFK 619
Cdd:cd17634 568 TPDVVHWVDSLPKTRSGK 585
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
265-622 |
1.69e-20 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 92.95 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLAL-PLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 421
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtgAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 422 TGRqgavgraswlykhifPFSLIRYDVmtGEPIRNAQGHCmttspGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvf 501
Cdd:cd17638 161 PGD---------------DAETVATTC--GRACPGFEVRI-----ADDGEVL--VRGYNVMQGYLDDPEATAEAI----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 502 wSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRP 580
Cdd:cd17638 212 -DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKAFVVARP 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 82581629 581 PQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd17638 289 GVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
270-622 |
1.95e-20 |
|
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: 94.34 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAarishlkVLQCQG--FYHL------CGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSA 341
Cdd:cd05912 83 MYTSGTTGKPKG-------VQQTFGnhWWSAigsalnLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPlqILETYGMTE--GNVATF 419
Cdd:cd05912 155 EQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIP--VYQSYGMTEtcSQIVTL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 420 NYT---GRQGAVGRASwlykhiFPFSLirydvmtgePIRNAQGhcmttSPGEPG--LLVAP-VSQqspflGYAGAPELAK 493
Cdd:cd05912 233 SPEdalNKIGSAGKPL------FPVEL---------KIEDDGQ-----PPYEVGeiLLKGPnVTK-----GYLNRPDATE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 494 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHE----G 569
Cdd:cd05912 288 E-----SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL-----LSHPAIKEAGVVGIPddkwG 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 82581629 570 RAGMAALALRPPqaLNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd05912 356 QVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
75-615 |
2.96e-20 |
|
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: 94.33 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGTtapplAPGATV 154
Cdd:cd17651 5 AARTPDAPALVAEGRRLTYAELDRRANRLAHRL-------------------------------RARGV-----GPGDLV 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGLrtAFVPT--ALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPE 232
Cdd:cd17651 49 ALCARRSAELVVALLAILKAGA--AYVPLdpAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TNvagisnllSEAADQVDEPVpgYLsapqnimdtclyIFTSGTTGLPKAARISHLKVL-----QCQGFyhlcGVHQED-V 306
Cdd:cd17651 127 AE--------PDPALDADDLA--YV------------IYTSGSTGRPKGVVMPHRSLAnlvawQARAS----SLGPGArT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 307 IYLALPLYHMsgSLLGIVGCLGIGATVVLKP---KFSASQFWDDCQKHRVT-------VFQYIGELCRYLVNQPPSKAE- 375
Cdd:cd17651 181 LQFAGLGFDV--SVQEIFSTLCAGATLVLPPeevRTDPPALAAWLDEQRISrvflptvALRALAEHGRPLGVRLAALRYl 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 376 CDHKVRLAVGSGLRpdtweRFLRRFGPLQILETYGMTEGNVATfnytgrqgavgraswlyKHIFPFSLIRYD--VMTGEP 453
Cdd:cd17651 259 LTGGEQLVLTEDLR-----EFCAGLPGLRLHNHYGPTETHVVT-----------------ALSLPGDPAAWPapPPIGRP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 454 IRNAQGHCMTTS-----PGEPG-LLVAPVSQQSpflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDR 527
Cdd:cd17651 317 IDNTRVYVLDAAlrpvpPGVPGeLYIGGAGLAR---GYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGR 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 528 TGDTIRWKGENVATTEVAEVLETLdflqeVNIYGVTVPGHEGRAGMAALA----LRPPQALNLVQLYSHVSENLPPYARP 603
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARH-----PGVREAVVLAREDRPGEKRLVayvvGDPEAPVDAAELRAALATHLPEYMVP 468
|
570
....*....|..
gi 82581629 604 RFLRLQESLATT 615
Cdd:cd17651 469 SAFVLLDALPLT 480
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
129-612 |
3.32e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 94.46 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 129 ARVAPPAGDAAARGTTApplapGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALV--- 203
Cdd:PRK07786 50 DRVAALAGALSRRGVGF-----GDRVLILMLNRTEFVESVLAANMLG--AIAVPVNFRLTPpeIAFLVSDCGAHVVVtea 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 204 ----LATEfLESLEPDLPALRAMGlhlwaTGPETNVAGISNLLSEAADQVdEPVPGYLSAPQNIMdtclyiFTSGTTGLP 279
Cdd:PRK07786 123 alapVATA-VRDIVPLLSTVVVAG-----GSSDDSVLGYEDLLAEAGPAH-APVDIPNDSPALIM------YTSGTTGRP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 280 KAARISHLKvLQCQGFYHLCGVH---QEDVIYLALPLYHMSGslLGIVGC-LGIGATVVLKP--KFSASQFWDDCQKHRV 353
Cdd:PRK07786 190 KGAVLTHAN-LTGQAMTCLRTNGadiNSDVGFVGVPLFHIAG--IGSMLPgLLLGAPTVIYPlgAFDPGQLLDVLEAEKV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 354 T-VFQYIGELCRYLVNQPPSKAECDHKVrLAVGSGLRPDTwerFLRR----FGPLQILETYGMTEGNVATFNYTG----- 423
Cdd:PRK07786 267 TgIFLVPAQWQAVCAEQQARPRDLALRV-LSWGAAPASDT---LLRQmaatFPEAQILAAFGQTEMSPVTCMLLGedair 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 424 RQGAVGRaswlykhIFPFSLIRY--DVMTGEPirnaqghcmttsPGEPGLLV--APVSQQspflGYAGAPELAkdkllKD 499
Cdd:PRK07786 343 KLGSVGK-------VIPTVAARVvdENMNDVP------------VGEVGEIVyrAPTLMS----GYWNNPEAT-----AE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 500 VFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHE--GRAGMAALA 577
Cdd:PRK07786 395 AFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA---DEkwGEVPVAVAA 469
|
490 500 510
....*....|....*....|....*....|....*.
gi 82581629 578 LRPPQA-LNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:PRK07786 470 VRNDDAaLTLEDLAEFLTDRLARYKHPKALEIVDAL 505
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
92-557 |
4.69e-20 |
|
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: 93.10 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 92 SYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLLPAGPDFL-WIWfG 170
Cdd:TIGR01733 1 TYRELDERANRLARHLR------------------------------AAGG-----VGPGDRVAVLLERSAELVvAIL-A 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 171 LAKAGlrTAFVP----TALRRgpLLHCLRSCGAsALVLATEFLESLEPDLPALRAMGLHLWatgpetnvagisnlLSEAA 246
Cdd:TIGR01733 45 VLKAG--AAYVPldpaYPAER--LAFILEDAGA-RLLLTDSALASRLAGLVLPVILLDPLE--------------LAALD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 247 DQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGSLLGIVG 325
Cdd:TIGR01733 106 DAPAPPPPDAPSGPD---DLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPDDRV-LQFASLSFDASVEEIFG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 326 CLGIGATVVL------KPKFSASQFWDDcqKHRVTVFQ---YIGELCrylvnqPPSKAECDHKVRLAVGSG--LRPDTWE 394
Cdd:TIGR01733 182 ALLAGATLVVppedeeRDDAALLAALIA--EHPVTVLNltpSLLALL------AAALPPALASLRLVILGGeaLTPALVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 395 RFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWlykhifpfslirydVMTGEPIRNAQ-----GHCMTTSPGEP 469
Cdd:TIGR01733 254 RWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP--------------VPIGRPLANTRlyvldDDLRPVPVGVV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 470 GLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGD--VFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEV 547
Cdd:TIGR01733 320 GELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
490
....*....|
gi 82581629 548 LETLDFLQEV 557
Cdd:TIGR01733 398 LLRHPGVREA 407
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-612 |
6.08e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.40 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFL-IHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALL 157
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLL-------------------------------VALG-----VKPGDRVAVQ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 158 LPAGPDFLWIWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGASALVLATEFLESLEPdlPALRAMGLHLwatgpET-N 234
Cdd:PRK07514 60 VEKSPEALALYLATLRAGA--VFLPlnTAYTLAELDYFIGDAEPALVVCDPANFAWLSK--IAAAAGAPHV-----ETlD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 235 VAGISNLLSEAADQVDEPVPgylsAPQNIMDTCLYIFTSGTTGLPKAARISH------LKVL-QCQGFyhlcgvHQEDVI 307
Cdd:PRK07514 131 ADGTGSLLEAAAAAPDDFET----VPRGADDLAAILYTSGTTGRSKGAMLSHgnllsnALTLvDYWRF------TPDDVL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 308 YLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDdcQKHRVTVFQ-----YIgelcRYLVNQPPSKAECDHkVRL 382
Cdd:PRK07514 201 IHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLA--LMPRATVMMgvptfYT----RLLQEPRLTREAAAH-MRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 383 AV-GSG-LRPDTWERFLRRFGpLQILETYGMTEGNVATFN-YTG--RQGAVGraswlykhiFPF---SLIRYDVMTGEPI 454
Cdd:PRK07514 274 FIsGSApLLAETHREFQERTG-HAILERYGMTETNMNTSNpYDGerRAGTVG---------FPLpgvSLRVTDPETGAEL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 455 rnaqghcmttSPGEPGLLvaPVSQQSPFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRW 534
Cdd:PRK07514 344 ----------PPGEIGMI--EVKGPNVFKGYWRMPEKTAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIIS 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 535 KGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:PRK07514 406 GGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDEL 482
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
128-625 |
1.04e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 92.84 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 128 GARVAPPAG-----DAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASAL 202
Cdd:PRK12406 8 GDRRRSFDElaqraARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 203 VLATEFLESLEPDLPAlrAMGLHLWATGPETNVA-GIS-NLLSEAADQVD---------EPVPGYLSAPQNImdtclyIF 271
Cdd:PRK12406 88 IAHADLLHGLASALPA--GVTVLSVPTPPEIAAAyRISpALLTPPAGAIDwegwlaqqePYDGPPVPQPQSM------IY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 272 TSGTTGLPKAARISHLKVLQCQGF----YHLCGVHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDD 347
Cdd:PRK12406 160 TSGTTGHPKGVRRAAPTPEQAAAAeqmrALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 348 CQKHRVTVFQYIGELCRYLVNQPPskaecdhKVRLAVG-SGLR----------PDTWERFLRRFGPLqILETYGMTEGNV 416
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPE-------EVRAKYDvSSLRhvihaaapcpADVKRAMIEWWGPV-IYEYYGSTESGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ATF----NYTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVAPVSQQSPFLgYAGAPElA 492
Cdd:PRK12406 311 VTFatseDALSHPGTVGKAA-------PGAELRFVDEDGRPL----------PQGEIGEIYSRIAGNPDFT-YHNKPE-K 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 493 KDKLLKDVF-WSGDVffntGDLlvcDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GR 570
Cdd:PRK12406 372 RAEIDRGGFiTSGDV----GYL---DADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 571 AGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK12406 443 ALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
75-610 |
2.77e-19 |
|
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: 91.57 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:cd17646 8 AARTPDAPAVVDEGRTLTYRELDERANRLAHLL-------------------------------RARG-----VGPEDRV 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVP--TALRRGPLLHCLRSCGAsALVLATEFLESLEPDLPALRAMGLHLWATGPE 232
Cdd:cd17646 52 AVLLPRSADLVVALLAVLKAG--AAYLPldPGYPADRLAYMLADAGP-AVVLTTADLAARLPAGGDVALLGDEALAAPPA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TnvagisnllseaadqvdepVPGYLSAPQNimdTCLYIFTSGTTGLPKAARISHL----KVLQCQGFYhlcGVHQEDVIY 308
Cdd:cd17646 129 T-------------------PPLVPPRPDN---LAYVIYTSGSTGRPKGVMVTHAgivnRLLWMQDEY---PLGPGDRVL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 309 LALPLyHMSGSLLGIVGCLGIGATVVL-------KPKFSASQFwddcQKHRVTVFQYIGELCRYLVNQPpsKAECDHKVR 381
Cdd:cd17646 184 QKTPL-SFDVSVWELFWPLVAGARLVVarpgghrDPAYLAALI----REHGVTTCHFVPSMLRVFLAEP--AAGSCASLR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 LAVGSG--LRPDTWERFLRRFG-PLQILetYGMTEGNVATFNYTGRQGAVGRAswlykhifpfslirydVMTGEPIRNAQ 458
Cdd:cd17646 257 RVFCSGeaLPPELAARFLALPGaELHNL--YGPTEAAIDVTHWPVRGPAETPS----------------VPIGRPVPNTR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 459 GHCMTTS-----PGEPGLLV---APVSQqspflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGD 530
Cdd:cd17646 319 LYVLDDAlrpvpVGVPGELYlggVQLAR-----GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 531 TIRWKGENVATTEVAEVLETLDflqEVNiyGVTVPGHEGRAGMAAL-----ALRPPQALNLVQLYSHVSENLPPYARP-R 604
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHP---AVT--HAVVVARAAPAGAARLvgyvvPAAGAAGPDTAALRAHLAERLPEYMVPaA 468
|
....*.
gi 82581629 605 FLRLQE 610
Cdd:cd17646 469 FVVLDA 474
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
148-622 |
2.92e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 91.68 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLAT---EFLESLEPDLPALRamgL 224
Cdd:PRK13391 46 LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAaklDVARALLKQCPGVR---H 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HLWATGPETnVAGISNLLSEAADQVDEPVPGylsapQNIMDTCLYifTSGTTGLPKAAR--ISHLKVLQCQGFYHLCGV- 301
Cdd:PRK13391 123 RLVLDGDGE-LEGFVGYAEAVAGLPATPIAD-----ESLGTDMLY--SSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQRl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 302 --HQEDVIYLA-LPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpskaecdH 378
Cdd:PRK13391 195 wgFRSDMVYLSpAPLYH-SAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP-------E 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 379 KVRLAVG-SGLR----------PDTWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAVGRAswlykhifpfsl 443
Cdd:PRK13391 267 EVRDKYDlSSLEvaihaaapcpPQVKEQMIDWWGPI-IHEYYAATEGLGFTAcdseEWLAHPGTVGRA------------ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 444 irydvMTGEP-IRNAQGHCMttSPGEPGLLVapVSQQSPFlGYAGAPELAKDKLLKDVFWSgdvffNTGDLLVCDEQGFL 522
Cdd:PRK13391 334 -----MFGDLhILDDDGAEL--PPGEPGTIW--FEGGRPF-EYLNDPAKTAEARHPDGTWS-----TVGDIGYVDEDGYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 523 HFHDRTGDTIRWKGENVATTEVAEVLETL--------------DFLQEVNIYGVTVPGHEGRAGMAAlalrppqalnlvQ 588
Cdd:PRK13391 399 YLTDRAAFMIISGGVNIYPQEAENLLITHpkvadaavfgvpneDLGEEVKAVVQPVDGVDPGPALAA------------E 466
|
490 500 510
....*....|....*....|....*....|....
gi 82581629 589 LYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:PRK13391 467 LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYK 500
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
66-540 |
3.10e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 91.70 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 66 SLAWRLAYLAREQPTHTFLIH----GAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaAR 141
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLL-------------------------------AL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 142 GttappLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF----LESLEPDLP 217
Cdd:COG1022 61 G-----VKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldkLLEVRDELP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 218 ALRamglHLW-----ATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL-Q 291
Cdd:COG1022 136 SLR----HIVvldprGLRDDPRLLSLDELLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLsN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 292 CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGiVGCLGIGATVVlkpkFSAS--QFWDDCQKHRVTVF------------- 356
Cdd:COG1022 212 ARALLERLPLGPGDRTLSFLPLAHVFERTVS-YYALAAGATVA----FAESpdTLAEDLREVKPTFMlavprvwekvyag 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 357 ------------------------QYIgelCRYLVNQPPSKAE------CD----HKVRLAVG-------SG---LRPDT 392
Cdd:COG1022 287 iqakaeeagglkrklfrwalavgrRYA---RARLAGKSPSLLLrlkhalADklvfSKLREALGgrlrfavSGgaaLGPEL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 393 wERFLRRFGpLQILETYGMTE-GNVATFNYTGRQ--GAVGRAswlykhiFPFSLIRydvmtgepIrnaqghcmttspGEP 469
Cdd:COG1022 364 -ARFFRALG-IPVLEGYGLTEtSPVITVNRPGDNriGTVGPP-------LPGVEVK--------I------------AED 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 470 G-LLVapvsqQSP--FLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTIrwK---GENVA 540
Cdd:COG1022 415 GeILV-----RGPnvMKGYYKNPEATAEAFDAD----G--WLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVA 478
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
265-622 |
3.26e-19 |
|
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: 89.63 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISH------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 338
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANktffavPDILQKEGL----NWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 339 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRP-DTWERFLRRFGPLQILETYGMTEGNVA 417
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 418 TFNYTGRQ----GAVGraswlykHIFP---FSLIRYDVMTGepIRNAQGHCMTTSPGEpgllvapvsqqspFLGYAGAPE 490
Cdd:cd17635 158 LCLPTDDDsieiNAVG-------RPYPgvdVYLAATDGIAG--PSASFGTIWIKSPAN-------------MLGYWNNPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 491 LAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGR 570
Cdd:cd17635 216 RTAEVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGEL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 82581629 571 AGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd17635 289 VGLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
271-562 |
5.38e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 90.88 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 271 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSllgIVGCL-----GIGATVVLKPKfSA 341
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTALPLYHIFAL---TVNCLlfielGGQNLLITNPR-DI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKaECD-HKVRLAVGSGLR-----PDTWERFLRRFgplqILETYGMTEGN 415
Cdd:PRK08974 289 PGFVKELKKYPFTAITGVNTLFNALLNNEEFQ-ELDfSSLKLSVGGGMAvqqavAERWVKLTGQY----LLEGYGLTECS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 416 ----VATFNYTGRQGAVGraswlykhiFPFSlirydvMTGEPIRNAQGHcmTTSPGEPGLLVAPVSQQspFLGYAGAPEl 491
Cdd:PRK08974 364 plvsVNPYDLDYYSGSIG---------LPVP------STEIKLVDDDGN--EVPPGEPGELWVKGPQV--MLGYWQRPE- 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82581629 492 AKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGV 562
Cdd:PRK08974 424 ATDEVIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
149-552 |
5.45e-19 |
|
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: 90.47 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 149 APGATVALLLPAGPDFLWIWFGLAKAGlrtaFVP-----TALRRGpLLHCLRSCGASALVLATEFLESL-EPDLPALRAM 222
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSG----KVPvmlnyTAGLRE-LRACIKLAGIKTVLTSKQFIEKLkLHHLFDVEYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 223 -------GLHLWATGPETNVAGISNLLSEAADQVDEPVpgylsAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL----Q 291
Cdd:cd05909 104 arivyleDLRAKISKADKCKAFLAGKFPPKWLLRIFGV-----APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanveQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 292 CQGFYHLcgvHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK-FSASQFWDDCQKHRVTVFQYIGELCRYLVNQp 370
Cdd:cd05909 179 ITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 371 pSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTEG----NVATFNYTGRQGAVGRaswlykhifPFSLI 444
Cdd:cd05909 255 -AHPEDFSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECspviSVNTPQSPNKEGTVGR---------PLPGM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 445 RY---DVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPElakdkllKDVFWSGDVFFNTGDLLVCDEQGF 521
Cdd:cd05909 324 EVkivSVETHEEV----------PIGEGGLLL--VRGPNVMLGYLNEPE-------LTSFAFGDGWYDTGDIGKIDGEGF 384
|
410 420 430
....*....|....*....|....*....|.
gi 82581629 522 LHFHDRTGDTIRWKGENVATTEVAEVLETLD 552
Cdd:cd05909 385 LTITGRLSRFAKIAGEMVSLEAIEDILSEIL 415
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-616 |
6.61e-19 |
|
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: 88.48 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAARISHLKVLQCQ-GFYHLCGVHQEDVIYLALPLYHMSG-SLLGIVGCLGiGATVVLkPKFSASQFWDD 347
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANlQLIHAMGLTEADVYLNMLPLFHIAGlNLALATFHAG-GANVVM-EKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 348 CQKHRVTVFqyiGELcrylvnqPP---SKAECDHKVRLAVGSgLR-------PDTWERFLRRfGPLQILETYGMTE-GNV 416
Cdd:cd17637 84 IEEEKVTLM---GSF-------PPilsNLLDAAEKSGVDLSS-LRhvlgldaPETIQRFEET-TGATFWSLYGQTEtSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ATFN-YTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIRnaqghcmttsPGEPGLLVApvsqQSP--FLGYAGAPELAK 493
Cdd:cd17637 152 VTLSpYRERPGSAGRPG-------PLVRVRIVDDNDRPVP----------AGETGEIVV----RGPlvFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 494 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTG--DTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRA 571
Cdd:cd17637 211 Y-----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP-KWGEG 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 82581629 572 GMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTE 616
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTA 327
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
148-627 |
7.14e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 90.30 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLrtAFVPTALRRGP--LLHCLRSCGASALVLATEFLESLEpDLPALRAMGLH 225
Cdd:PRK06839 50 VKKGERIAILSQNSLEYIVLLFAIAKVEC--IAVPLNIRLTEneLIFQLKDSGTTVLFVEKTFQNMAL-SMQKVSYVQRV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATGPetnvagiSNLLSEAADQVDEPvpgylsapqNIMDTCLYIFTSGTTGLPKAARIShlkvlQCQGFYHlcGVHQ-- 303
Cdd:PRK06839 127 ISITSL-------KEIEDRKIDNFVEK---------NESASFIICYTSGTTGKPKGAVLT-----QENMFWN--ALNNtf 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 304 ------EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECD 377
Cdd:PRK06839 184 aidltmHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 378 HKVRLAVGSG------LRPDTWERFLrRFGplqilETYGMTEGNVATF-----NYTGRQGAVGRaswlykhifPFSLIRY 446
Cdd:PRK06839 264 QSVRWFYNGGapcpeeLMREFIDRGF-LFG-----QGFGMTETSPTVFmlseeDARRKVGSIGK---------PVLFCDY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 447 DVmtgepIRNAQGHcmtTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHD 526
Cdd:PRK06839 329 EL-----IDENKNK---VEVGEVGELL--IRGPNVMKEYWNRPDATEETI-------QDGWLCTGDLARVDEDGFVYIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 527 RTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 606
Cdd:PRK06839 392 RKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHV-KWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEI 470
|
490 500
....*....|....*....|.
gi 82581629 607 RLQESLATTETFKQQKVRMAN 627
Cdd:PRK06839 471 VFLKELPKNATGKIQKAQLVN 491
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
138-638 |
1.32e-18 |
|
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: 89.86 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGASALVLATEFLE----- 210
Cdd:cd05968 103 RLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG--IVVPifSGFGKEAAATRLQDAEAKALITADGFTRrgrev 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 211 SLEPDL-PALRAMGL--------HLWATGPETNVAGISnllseAADQVDEPVPGYlsAPQNIMDTCLYIFTSGTTGLPKA 281
Cdd:cd05968 181 NLKEEAdKACAQCPTvekvvvvrHLGNDFTPAKGRDLS-----YDEEKETAGDGA--ERTESEDPLMIIYTSGTTGKPKG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 282 ARISH----LKVlqCQGFYHLCGVHQEDVIYLALPLYHMSGSLLgIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRV 353
Cdd:cd05968 254 TVHVHagfpLKA--AQDMYFQFDLKPGDLLTWFTDLGWMMGPWL-IFGGLILGATMVLydgAPDHpKADRLWRMVEDHEI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 354 TVFQYIGELCRYLV--NQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGplqiletygmtEGNVATFNYTG----RQ 425
Cdd:cd05968 331 THLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGepWNPEPWNWLFETVG-----------KGRNPIINYSGgteiSG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 426 GAVGraSWLYKHIFPFSL------IRYDVM--TGEPIRNAQGHCMTTSPGePGLlvapvsqQSPFLGyagapelaKDKLL 497
Cdd:cd05968 400 GILG--NVLIKPIKPSSFngpvpgMKADVLdeSGKPARPEVGELVLLAPW-PGM-------TRGFWR--------DEDRY 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 498 KDVFWSG-DVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 576
Cdd:cd05968 462 LETYWSRfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEAIVCFV 540
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 577 ALRP---PQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK--QQKVRMANEGFDP---SVLSDP 638
Cdd:cd05968 541 VLKPgvtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKvmRRVIRAAYLGKELgdlSSLENP 610
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
66-625 |
3.25e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 88.26 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 66 SLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGtta 145
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWL-------------------------------AAQG--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 146 ppLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF--------LESLEPD-L 216
Cdd:PRK06164 57 --VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFkgidfaaiLAAVPPDaL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 PALRAMGLhLWATGPETNvAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIF-TSGTTGLPKAARISHLKVL-QCQG 294
Cdd:PRK06164 135 PPLRAIAV-VDDAADATP-APAPGARVQLFALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLrHARA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 295 FYHLCGVHQEDVIYLALPlyhMSGS--LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS 372
Cdd:PRK06164 213 IARAYGYDPGAVLLAALP---FCGVfgFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 373 KAECDHKVRLAVGS--GLRPDTWERFLRRFGPLQILetYGMTE------GNVATFNYTGRQGAVGRAswlykhIFPFSLI 444
Cdd:PRK06164 290 RADFPSARLFGFASfaPALGELAALARARGVPLTGL--YGSSEvqalvaLQPATDPVSVRIEGGGRP------ASPEARV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 445 RY-DVMTGEPIrnaqghcmttSPGEPGLLvaPVSQQSPFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLH 523
Cdd:PRK06164 362 RArDPQDGALL----------PDGESGEI--EIRAPSLMRGYLDNPDATARAL------TDDGYFRTGDLGYTRGDGQFV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 524 FHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHEGRAGMAALALRPPQA-LNLVQLYSHVSENLPPYAR 602
Cdd:PRK06164 424 YQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT---RDGKTVPVAFVIPTDGAsPDEAGLMAACREALAGFKV 500
|
570 580
....*....|....*....|....*.
gi 82581629 603 PRFLRLQESLATTET---FKQQKVRM 625
Cdd:PRK06164 501 PARVQVVEAFPVTESangAKIQKHRL 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-626 |
4.32e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 86.38 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL------KP 337
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSnEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 338 KFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN-V 416
Cdd:cd05944 83 PGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATG-LPVVEGYGLTEATcL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ATFNYTG---RQGAVGRAswlykhiFPFSLIRYDVMTGEPirNAQGHCmttSPGEpgllVAPVSQQSPflgyaGAPELAK 493
Cdd:cd05944 162 VAVNPPDgpkRPGSVGLR-------LPYARVRIKVLDGVG--RLLRDC---APDE----VGEICVAGP-----GVFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 494 DKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGM 573
Cdd:cd05944 221 YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDA-HAGELPV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 574 AALALRPPQALNLVQLYSHVSENLPPYAR-PRFLRLQESLATT---ETFKQQKVRMA 626
Cdd:cd05944 300 AYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTavgKVFKPALRADA 356
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
137-615 |
5.94e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 87.63 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 137 DAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPllHCLRSCGASALVLATEFLESLEPDL 216
Cdd:PRK05852 54 DDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE--QRVRSQAAGARVVLIDADGPHDRAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 PALRAMGLHLWATGPETNVAGIsnlLSEAADQVDEPVPgYLSAPQNIM-DTCLYIFTSGTTGLPKAARISHLKVLQ---- 291
Cdd:PRK05852 132 PTTRWWPLTVNVGGDSGPSGGT---LSVHLDAATEPTP-ATSTPEGLRpDDAMIMFTGGTTGLPKMVPWTHANIASsvra 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 292 -CQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 368
Cdd:PRK05852 208 iITGY----RLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 369 QPPSKA--ECDHKVRL--AVGSGLRPDTWERFLRRFGPlQILETYGMTEG--NVATFNYTGRQ---------GAVGRAsw 433
Cdd:PRK05852 284 RAATEPsgRKPAALRFirSCSAPLTAETAQALQTEFAA-PVVCAFGMTEAthQVTTTQIEGIGqtenpvvstGLVGRS-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 434 lykhifpfslirydvmTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLkdvfwsgDVFFNTGDL 513
Cdd:PRK05852 361 ----------------TGAQIRIVGSDGLPLPAGAVGEVW--LRGTTVVRGYLGDPTITAANFT-------DGWLRTGDL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 514 LVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHV 593
Cdd:PRK05852 416 GSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLY-GEAVAAVIVPRESAPPTAEELVQFC 494
|
490 500
....*....|....*....|..
gi 82581629 594 SENLPPYARPRFLRLQESLATT 615
Cdd:PRK05852 495 RERLAAFEIPASFQEASGLPHT 516
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
58-619 |
7.07e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.86 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 58 PESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagd 137
Cdd:PRK12316 1996 PEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR----------------------------- 2046
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 aaARGttappLAPGATVALLLPAGPDFLWIWFGLAKAGlrTAFVP--TALRRGPLLHCLRSCGASALVLATEFLESLEPd 215
Cdd:PRK12316 2047 --ARG-----VGPEVRVAIAAERSFELVVALLAVLKAG--GAYVPldPNYPAERLAYMLEDSGAALLLTQRHLLERLPL- 2116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 216 lpalramglhlwatgpetnVAGISNLLSEAADQVDEpVPGYLSAPQNIMDTCLY-IFTSGTTGLPKAARISHLKVLQ-CQ 293
Cdd:PRK12316 2117 -------------------PAGVARLPLDRDAEWAD-YPDTAPAVQLAGENLAYvIYTSGSTGLPKGVAVSHGALVAhCQ 2176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 294 GFYHLCGVHQEDVIYLALPlYHMSGSLLGIVGCLGIGATVVLKPK--FSASQFWDDCQKHRVTV-------FQYIGELCR 364
Cdd:PRK12316 2177 AAGERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTIldfppvyLQQLAEHAE 2255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 365 YLVNQPPSKAECdhkvrlAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYT-GRQGAVGRASwlykhifpfsl 443
Cdd:PRK12316 2256 RDGRPPAVRVYC------FGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKcRPQDPCGAAY----------- 2318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 444 irydVMTGEPIRNAQGHCMTTS-----PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCD 517
Cdd:PRK12316 2319 ----VPIGRALGNRRAYILDADlnllaPGMAGELY--LGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYR 2392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 518 EQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENL 597
Cdd:PRK12316 2393 ADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARL 2470
|
570 580
....*....|....*....|..
gi 82581629 598 PPYARPRFLRLQESLATTETFK 619
Cdd:PRK12316 2471 PAYMVPAHWVVLERLPLNPNGK 2492
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
150-619 |
8.12e-18 |
|
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: 86.40 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAG-----LRTAFVPtalrrGPLLHCLRSCGASALVLATEFLESLEPDLPALramgL 224
Cdd:cd05969 24 KGDRVFVLSPRSPELYFSMLGIGKIGavicpLFSAFGP-----EAIRDRLENSEAKVLITTEELYERTDPEDPTL----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HlwatgpetnvagisnllseaadqvdepvpgylsapqnimdtclyiFTSGTTGLPKAARISHLKVLQ--CQGFYHLcGVH 302
Cdd:cd05969 95 H---------------------------------------------YTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 303 QEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSASQFWDDCQKHRVTVF----QYIGELCRYLVNQPPSKAECD 377
Cdd:cd05969 129 PDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVyEGRFDAESWYGIIERVKVTVWytapTAIRMLMKEGDELARKYDLSS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 378 HKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNYTG---RQGAVGRaswlykhifPFSLIRYDVMT--G 451
Cdd:cd05969 209 LRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSIMIANYPCmpiKPGSMGK---------PLPGVKAAVVDenG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 452 EPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPElakdkLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDT 531
Cdd:cd05969 279 NELP----------PGTKGILALKPGWPSMFRGIWNDEE-----RYKNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 532 IRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR----PPQALNlVQLYSHVSENLPPYARPRFLR 607
Cdd:cd05969 342 IKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGEIIKAFISLKegfePSDELK-EEIINFVRQKLGAHVAPREIE 419
|
490
....*....|..
gi 82581629 608 LQESLATTETFK 619
Cdd:cd05969 420 FVDNLPKTRSGK 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
148-619 |
1.58e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.47 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLE---PDLPALRAM-- 222
Cdd:PRK08751 73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqviADTPVKQVItt 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 223 GL-----------------HLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNImdtCLYIFTSGTTGLPKAARIS 285
Cdd:PRK08751 153 GLgdmlgfpkaalvnfvvkYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDI---AFLQYTGGTTGVAKGAMLT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 286 H----LKVLQCQGFYHLCGVHQE--DVIYLALPLYHM----SGSL--LGIVGClgigATVVLKPKfSASQFWDDCQKHRV 353
Cdd:PRK08751 230 HrnlvANMQQAHQWLAGTGKLEEgcEVVITALPLYHIfaltANGLvfMKIGGC----NHLISNPR-DMPGFVKELKKTRF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 354 TVFQYIGELCRYLVNQPpSKAECDH---KVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFnytgrqgavgr 430
Cdd:PRK08751 305 TAFTGVNTLFNGLLNTP-GFDQIDFsslKMTLGGGMAVQRSVAERWKQVTG-LTLVEAYGLTETSPAAC----------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 431 aswlykhIFPFSLIRYDVMTGEPI-------RNAQGHCMTTspGEPGLLVAPVSQQspFLGYAGAPELAKDKLlkdvfwS 503
Cdd:PRK08751 372 -------INPLTLKEYNGSIGLPIpstdaciKDDAGTVLAI--GEIGELCIKGPQV--MKGYWKRPEETAKVM------D 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 504 GDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGRAGMAALALRPPQA 583
Cdd:PRK08751 435 ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEKSGEIVKVVIVKKDPA 512
|
490 500 510
....*....|....*....|....*....|....*.
gi 82581629 584 LNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:PRK08751 513 LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGK 548
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
151-622 |
3.17e-17 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 84.81 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGaSALVLATEFLEslEPDLPALRAMglHLWATG 230
Cdd:TIGR01923 24 GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD-VQLLLTDSLLE--EKDFQADSLD--RIEAAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 231 PEtnvagisnllseaadqvdepvPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH-------LKVLQCQGFYhlcgvhQ 303
Cdd:TIGR01923 99 RY---------------------ETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFrnhyasaVGSKENLGFT------E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 304 EDVIYLALPLYHMSGslLGIV-GCLGIGATVVLKPKFSasQFWDDCQKHRVTVFQYI-GELCRYLvnQPPSKAECDHKVR 381
Cdd:TIGR01923 152 DDNWLLSLPLYHISG--LSILfRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVpTQLNRLL--DEGGHNENLRKIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 LavGSGLRPDTWERFLRRFGpLQILETYGMTE--GNVATFN--YTGRQGAVGRASwlykhifPFSLIRYDVmtgePIRNA 457
Cdd:TIGR01923 226 L--GGSAIPAPLIEEAQQYG-LPIYLSYGMTEtcSQVTTATpeMLHARPDVGRPL-------AGREIKIKV----DNKEG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 458 QGHCMTTSPGepgllvapvsqqsPFLGYAGAPELAkdKLLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGE 537
Cdd:TIGR01923 292 HGEIMVKGAN-------------LMKGYLYQGELT--PAFEQQGW-----FNTGDIGELDGEGFLYVLGRRDDLIISGGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 538 NVATTEVAEVLETLDFLQEVniygVTVPGHEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARP-RFLRLQEsLATT 615
Cdd:TIGR01923 352 NIYPEEIETVLYQHPGIQEA----VVVPKPDAEWGQVPVAyIVSESDISQAKLIAYLTEKLAKYKVPiAFEKLDE-LPYN 426
|
....*..
gi 82581629 616 ETFKQQK 622
Cdd:TIGR01923 427 ASGKILR 433
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
71-625 |
3.79e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 85.25 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQPTHTFLI--HGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappL 148
Cdd:PRK08315 22 LDRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLL-------------------------------ALG-----I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 149 APGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF--------LESLEPDL---- 216
Cdd:PRK08315 66 EKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyvamLYELAPELatce 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 ---------PALRA---MGlhlwatgpETNVAGISN---LLSEAADQVDEPVPGYLSA-----PQNIMdtclyiFTSGTT 276
Cdd:PRK08315 146 pgqlqsarlPELRRvifLG--------DEKHPGMLNfdeLLALGRAVDDAELAARQATldpddPINIQ------YTSGTT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 277 GLPKAARISHLKVL-------QCQGFYHlcgvhqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK-PKFSASQFWDDC 348
Cdd:PRK08315 212 GFPKGATLTHRNILnngyfigEAMKLTE------EDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPgEGFDPLATLAAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 349 QKHRVTVFQ-----YIGELcrylvnQPPSKAECDHkvrlavgSGLR---------P-DTWERFLRRFGPLQILETYGMTE 413
Cdd:PRK08315 286 EEERCTALYgvptmFIAEL------DHPDFARFDL-------SSLRtgimagspcPiEVMKRVIDKMHMSEVTIAYGMTE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 GN-VATFNYTG-----RQGAVGRAswlykhiFPFSLIR-YDVMTGEpirnaqghcmTTSPGEPGLLVApvSQQSPFLGYA 486
Cdd:PRK08315 353 TSpVSTQTRTDdplekRVTTVGRA-------LPHLEVKiVDPETGE----------TVPRGEQGELCT--RGYSVMKGYW 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 487 GAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 566
Cdd:PRK08315 414 NDPEKTAEAIDAD----G--WMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDE- 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 82581629 567 HEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK08315 487 KYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
125-562 |
3.94e-17 |
|
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: 84.87 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 125 TEEGARVAPPAGDAAARGttappLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVL 204
Cdd:cd05923 32 SELRARIEAVAARLHARG-----LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 205 ATEfleslEPDLPALRAMGLHLWATGPETNvagiSNLLSEAADQVDEPVPGylsaPQnimDTCLYIFTSGTTGLPKAARI 284
Cdd:cd05923 107 AVD-----AQVMDAIFQSGVRVLALSDLVG----LGEPESAGPLIEDPPRE----PE---QPAFVFYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 285 SH-------LKVLQCQGFYHlcGVHqEDVIYLaLPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQ 357
Cdd:cd05923 171 PQraaesrvLFMSTQAGLRH--GRH-NVVLGL-MPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 358 YIGELCRYLVN---QPPSKAECDHKVRLAVGSglRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWl 434
Cdd:cd05923 247 ATPTHLDALAAaaeFAGLKLSSLRHVTFAGAT--MPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGF- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 435 ykhifpFSLIRYDVMTGEPIRNAqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPELAKDKLLkdvfwsgDVFFNTGDLL 514
Cdd:cd05923 324 ------FSEVRIVRIGGSPDEAL-------ANGEEGELIVAAAADAAFTGYLNQPEATAKKLQ-------DGWYRTGDVG 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 82581629 515 VCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGV 562
Cdd:cd05923 384 YVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
71-625 |
4.81e-17 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 84.30 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsTEEGarvappagdaaargttappLAP 150
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGL-----------------RGLG-------------------IRP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLpalramglhlwatg 230
Cdd:cd05920 65 GDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRAL-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 231 petnvagisnllseaADQVDEPVPgylsapqnimDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYH-------LCGVHQ 303
Cdd:cd05920 131 ---------------ARELAESIP----------EVALFLLSGGTTGTPKLIPRTH------NDYAYnvrasaeVCGLDQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 304 EDVIYLALPLYH---MSGSllGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT--------VFQYIGELCRYlVNQPPS 372
Cdd:cd05920 180 DTVYLAVLPAAHnfpLACP--GVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTvtalvpalVSLWLDAAASR-RADLSS 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 373 kaecdHKVRLAVGSGLRPDTWERFLRRFGPlQILETYGMTEGNVatfNYT----------GRQGavgraswlyKHIFPFS 442
Cdd:cd05920 257 -----LRLLQVGGARLSPALARRVPPVLGC-TLQQVFGMAEGLL---NYTrlddpdeviiHTQG---------RPMSPDD 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 443 LIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDkllkdVFwSGDVFFNTGDLLVCDEQG 520
Cdd:cd05920 319 EIR--------VVDEEGN--PVPPGEEGELLT----RGPytIRGYYRAPEHNAR-----AF-TPDGFYRTGDLVRRTPDG 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 521 FLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALRPPQaLNLVQLYSHVSE-NLP 598
Cdd:cd05920 379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV--VAMPDELlGERSCAFVVLRDPP-PSAAQLRRFLRErGLA 455
|
570 580
....*....|....*....|....*..
gi 82581629 599 PYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:cd05920 456 AYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
75-413 |
5.19e-17 |
|
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: 85.68 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:COG1020 486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHL-------------------------------RALG-----VGPGDLV 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGASALVlaTEflESLEPDLPALRAMGLHL----WA 228
Cdd:COG1020 530 GVCLERSLEMVVALLAVLKAGA--AYVPldPAYPAERLAYMLEDAGARLVL--TQ--SALAARLPELGVPVLALdalaLA 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 229 TGPETNvagisnllseaadqvdepvPGYLSAPQNIMdtclY-IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDV 306
Cdd:COG1020 604 AEPATN-------------------PPVPVTPDDLA----YvIYTSGSTGRPKGVMVEHRALVNlLAWMQRRYGLGPGDR 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 307 IYLALPLyhmS--GSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQ----YIGELCRYLVNQPPSkaecd 377
Cdd:COG1020 661 VLQFASL---SfdASVWEIFGALLSGATLVLAPPearRDPAALAELLARHRVTVLNltpsLLRALLDAAPEALPS----- 732
|
330 340 350
....*....|....*....|....*....|....*...
gi 82581629 378 hkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 413
Cdd:COG1020 733 --LRLVLVGGeaLPPELVRRWRARLPGARLVNLYGPTE 768
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
63-648 |
1.12e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 63 SGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARG 142
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALI-------------------------------ARG 4597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 143 ttappLAPGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALR--RGPLLHCLRSCGASALVLATEFLeslePDLPAlr 220
Cdd:PRK12316 4598 -----VGPEVLVGIAMERSAEMMVGLLAVLKAG--GAYVPLDPEypRERLAYMMEDSGAALLLTQSHLL----QRLPI-- 4664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 221 AMGLHLWATGPETNVAGISnllseaadqvdEPVPGYLSAPQNImdtCLYIFTSGTTGLPKAARISHLKVLQcqgfyHLCG 300
Cdd:PRK12316 4665 PDGLASLALDRDEDWEGFP-----------AHDPAVRLHPDNL---AYVIYTSGSTGRPKGVAVSHGSLVN-----HLHA 4725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 301 VHQE-----DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPkfsaSQFWDDCQ------KHRVTVFQYIGELCRYLVNQ 369
Cdd:PRK12316 4726 TGERyeltpDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD----DSLWDPERlyaeihEHRVTVLVFPPVYLQQLAEH 4801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 370 PPSKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASwlYKHIfpfslirydv 448
Cdd:PRK12316 4802 AERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAA--YMPI---------- 4869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 449 mtGEPIRNAQGHCMTTSpGEPgllvAPVSQQSPFL--------GYAGAPELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQ 519
Cdd:PRK12316 4870 --GTPLGNRSGYVLDGQ-LNP----LPVGVAGELYlggegvarGYLERPALTAERFVPDPFGApGGRLYRTGDLARYRAD 4942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 520 GFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEvniygVTVPGHEGRAGMAALALRPPQALNLV-----------Q 588
Cdd:PRK12316 4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE-----AVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelrdE 5017
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82581629 589 LYSHVSENLPPYARPRFLRLQESLATTETFKQQkvRMANEGFDPSVLSD----PLYVLDQDIGA 648
Cdd:PRK12316 5018 LKAALRERLPEYMVPAHLVFLARMPLTPNGKLD--RKALPQPDASLLQQayvaPRSELEQQVAA 5079
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
265-576 |
1.30e-16 |
|
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: 82.64 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPkfSASQ 343
Cdd:cd05907 88 DLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAET 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHK---VRLAVGSGLR----------PDTwERFLRRFGpLQILETYG 410
Cdd:cd05907 166 LLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKrklFDLAVGGRLRfaasggaplpAEL-LHFFRALG-IPVYEGYG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 411 MTE-GNVATFNYTGRQ--GAVGRaswlykhifpfslirydVMTGEPIR-NAQGHCMTTSPgepgllvapvsqqSPFLGYA 486
Cdd:cd05907 244 LTEtSAVVTLNPPGDNriGTVGK-----------------PLPGVEVRiADDGEILVRGP-------------NVMLGYY 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 487 GAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRW-KGENVATTEVAEVLETLDFLQEVNIYGvtvp 565
Cdd:cd05907 294 KNPEATAEALDAD----G--WLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG---- 363
|
330
....*....|.
gi 82581629 566 ghEGRAGMAAL 576
Cdd:cd05907 364 --DGRPFLVAL 372
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
148-615 |
1.61e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 83.15 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFV-PTALRRgPLLHCLRSCGASALVLATEFLESLEPDLP--ALR---- 220
Cdd:PRK07059 70 LAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVnPLYTPR-ELEHQLKDSGAEAIVVLENFATTVQQVLAktAVKhvvv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 221 -AMGLHLWATG--------------PETNVAG---ISNLLSEAADQVDEPVPgylSAPQnimDTCLYIFTSGTTGLPKAA 282
Cdd:PRK07059 149 aSMGDLLGFKGhivnfvvrrvkkmvPAWSLPGhvrFNDALAEGARQTFKPVK---LGPD---DVAFLQYTGGTTGVSKGA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 283 RISH----LKVLQCQGFY---HLCGVHQEDVIYL-ALPLYHMSGslLGIVGCLGI--GATVVLKPK-FSASQFWDDCQKH 351
Cdd:PRK07059 223 TLLHrnivANVLQMEAWLqpaFEKKPRPDQLNFVcALPLYHIFA--LTVCGLLGMrtGGRNILIPNpRDIPGFIKELKKY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 352 RVTVFQYIGELCRYLVNQPP-SKAECDhKVRLAVGSGL---RPdTWERFLRRFGpLQILETYGMTEGN-VATFNytgrqg 426
Cdd:PRK07059 301 QVHIFPAVNTLYNALLNNPDfDKLDFS-KLIVANGGGMavqRP-VAERWLEMTG-CPITEGYGLSETSpVATCN------ 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 427 avgraswlykhifPFSLIRYDVMTGEP-------IRNAQGHCMttSPGEPGLLVAPVSQQSPflGYAGAP-ELAKdkllk 498
Cdd:PRK07059 372 -------------PVDATEFSGTIGLPlpstevsIRDDDGNDL--PLGEPGEICIRGPQVMA--GYWNRPdETAK----- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 499 dvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAgMAALAL 578
Cdd:PRK07059 430 --VMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDE-HSGEA-VKLFVV 505
|
490 500 510
....*....|....*....|....*....|....*..
gi 82581629 579 RPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:PRK07059 506 KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKT 542
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
190-615 |
2.52e-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: 82.10 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 190 LLHCLRSCGASALVLATEFLE-SLE---PDLPALRAMGLHLwATGPETNVAGISNLLSEAADQVdepvpgYLSAPQNImd 265
Cdd:cd17644 38 LAHYLQSLGVKSESLVGICVErSLEmiiGLLAILKAGGAYV-PLDPNYPQERLTYILEDAQISV------LLTQPENL-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 266 tcLY-IFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQEdvIYLALPLYHMSGSLLG-------IVGCLGIGATVVLKP 337
Cdd:cd17644 109 --AYvIYTSGSTGKPKGVMIEHQSLVN-----LSHGLIKE--YGITSSDRVLQFASIAfdvaaeeIYVTLLSGATLVLRP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 338 K---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQ-PPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPL-QILETYG 410
Cdd:cd17644 180 EemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLRLVIvgGEAVQPELVRQWQKNVGNFiQLINVYG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 411 MTEGNVATFnytgrqgavgraswLYKHIFPFSLIRYDVMTGEPIRNAQGHCM-----TTSPGEPG-LLVAPVSQQSpflG 484
Cdd:cd17644 260 PTEATIAAT--------------VCRLTQLTERNITSVPIGRPIANTQVYILdenlqPVPVGVPGeLHIGGVGLAR---G 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 485 YAGAPELAKDKLLKDVFWS--GDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEvniygV 562
Cdd:cd17644 323 YLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT-----A 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 563 TVPGHEGRAG----MAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:cd17644 398 VVIVREDQPGnkrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLT 454
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
75-615 |
4.16e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.90 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgstEEGarvappagdaaargttappLAPGATV 154
Cdd:PRK12467 522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLI-----------------AAG-------------------VGPDVLV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPTALR--RGPLLHCLRSCGAsALVLATEFLESLEPDLPALRAMGLHLwatgPE 232
Cdd:PRK12467 566 GIAVERSIEMVVGLLAVLKAG--GAYVPLDPEypQDRLAYMLDDSGV-RLLLTQSHLLAQLPVPAGLRSLCLDE----PA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 233 TNVAGISNLLSEAAdqvdepvpgylSAPQNImdtCLYIFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQE-----DVI 307
Cdd:PRK12467 639 DLLCGYSGHNPEVA-----------LDPDNL---AYVIYTSGSTGQPKGVAISHGALAN-----YVCVIAERlqlaaDDS 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 308 YLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVnQPPSKAECDHKVRLAV 384
Cdd:PRK12467 700 MLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVC 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 GSGLRPDTWERFLRRFGP-LQILETYGMTEGNVATFNYT-GRQGAVGRASWLYKHIFPFSLIRYDvmtgepirnaqgHCM 462
Cdd:PRK12467 779 GGEALQVDLLARVRALGPgARLINHYGPTETTVGVSTYElSDEERDFGNVPIGQPLANLGLYILD------------HYL 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 463 TTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVA 540
Cdd:PRK12467 847 NPVPvGVVGELY--IGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIE 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 541 TTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAALALRPP------QALNLvQLYSHVSENLPPYARPRFLRLQESLAT 614
Cdd:PRK12467 925 LGEIEARLLAQPGVREAVV--LAQPGDAGLQLVAYLVPAAVadgaehQATRD-ELKAQLRQVLPDYMVPAHLLLLDSLPL 1001
|
.
gi 82581629 615 T 615
Cdd:PRK12467 1002 T 1002
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
79-610 |
5.94e-16 |
|
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: 80.81 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgstEEGARvappagdaaargttapplaPGATVALLL 158
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLR-----------------AEGVG-------------------PGDRVALAL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRAMGLHlwatgpetNVAGI 238
Cdd:cd17643 45 PRSAELIVALLAILKAG--GAYVP-----------------------------IDPAYPVERIAFIL--------ADSGP 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 239 SNLLSEAADqvdepvPGYLsapqnimdtclyIFTSGTTGLPKAARISHLKVLQ----CQgfyHLCGVHQEDVIYlalpLY 314
Cdd:cd17643 86 SLLLTDPDD------LAYV------------IYTSGSTGRPKGVVVSHANVLAlfaaTQ---RWFGFNEDDVWT----LF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 315 HMSG---SLLGIVGCLGIGATVVLKPKF---SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GS 386
Cdd:cd17643 141 HSYAfdfSVWEIWGALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 387 GLRPDTWERFLRRFGPL--QILETYGMTEGNV-ATFNYTGRQGAVGRASwlykhifpfSLIrydvmtGEPIRNAQGHCMT 463
Cdd:cd17643 221 ALEAAMLRPWAGRFGLDrpQLVNMYGITETTVhVTFRPLDAADLPAAAA---------SPI------GRPLPGLRVYVLD 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 464 TS-----PGEPGLLVAPVSQQSPflGYAGAPELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGE 537
Cdd:cd17643 286 ADgrpvpPGVVGELYVSGAGVAR--GYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 538 NVATTEVAEVLETLDFLQEVniyGVTVpgHEGRAG----MAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLQE 610
Cdd:cd17643 364 RIELGEIEAALATHPSVRDA---AVIV--REDEPGdtrlVAYVVADDGAAADIAELRALLKELLPDYMVPaRYVPLDA 436
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
71-622 |
7.85e-16 |
|
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: 80.81 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQ---PTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttapp 147
Cdd:cd12118 7 LSFLERAAavyPDRTSIVYGDRRYTWRQTYDRCRRLASAL-------------------------------AALG----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEF-----LESLEPDLPALRAm 222
Cdd:cd12118 51 ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFeyedlLAEGDPDFEWIPP- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 223 glhlwatgpetnvagisnllseaadqVDEPVPGYLSapqnimdtclyiFTSGTTGLPKAARISHlkvlqcQGFY------ 296
Cdd:cd12118 130 --------------------------ADEWDPIALN------------YTSGTTGRPKGVVYHH------RGAYlnalan 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 297 -HLCGVHQEDViYL-ALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA 374
Cdd:cd12118 166 iLEWEMKQHPV-YLwTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 375 E-CDHKVRLAVGSGLRPdtwERFLRRFGPL--QILETYGMTEG-NVATFNY----------------TGRQGavgraswl 434
Cdd:cd12118 244 RpLPHRVHVMTAGAPPP---AAVLAKMEELgfDVTHVYGLTETyGPATVCAwkpewdelpteerarlKARQG-------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 435 ykhifpfslIRYDVMTGEPIRNAQGhcMTTSP------GE---PGLLVApvsqqspfLGYAGAPElAKDKLLKDvFWsgd 505
Cdd:cd12118 313 ---------VRYVGLEEVDVLDPET--MKPVPrdgktiGEivfRGNIVM--------KGYLKNPE-ATAEAFRG-GW--- 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 506 vfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALN 585
Cdd:cd12118 369 --FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDE-KWGEVPCAFVELKEGAKVT 445
|
570 580 590
....*....|....*....|....*....|....*..
gi 82581629 586 LVQLYSHVSENLPPYARPRFLRLQEsLATTETFKQQK 622
Cdd:cd12118 446 EEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQK 481
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
265-619 |
1.06e-15 |
|
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: 79.78 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAA------RISHLKVLQcqgFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL--K 336
Cdd:cd05971 89 DPALIIYTSGTTGPPKGAlhahrvLLGHLPGVQ---FPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 337 PKFSASQFWDDCQKHRVT-VFQYIGELcRYLVNQPPSKAECDHKVRlAVGSGLRPD-----TWERflRRFGpLQILETYG 410
Cdd:cd05971 166 TKFDPKAALDLMSRYGVTtAFLPPTAL-KMMRQQGEQLKHAQVKLR-AIATGGESLgeellGWAR--EQFG-VEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 411 MTEGNVATFN----YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGhcMTTSPGEPGLLVAPVSQQSPFLGYA 486
Cdd:cd05971 241 QTECNLVIGNcsalFPIKPGSMGKP-------IPGHRVA--------IVDDNG--TPLPPGEVGEIAVELPDPVAFLGYW 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 487 GAPELAKDKLLKDvfwsgdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 566
Cdd:cd05971 304 NNPSATEKKMAGD-------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP- 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 567 HEGRAGMAALALRP----PQALNlVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd05971 376 IRGEIVKAFVVLNPgetpSDALA-REIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
79-615 |
1.07e-15 |
|
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: 80.10 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLL 158
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRL-------------------------------RALG-----VGPEVRVGIAL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRamgLHLWATGpetnvAGI 238
Cdd:cd17649 45 ERSLEMVVALLAILKAG--GAYVP-----------------------------LDPEYPAER---LRYMLED-----SGA 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 239 SNLLSEAADQvdepvPGYLsapqnimdtclyIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIylaLPLYHMS 317
Cdd:cd17649 86 GLLLTHHPRQ-----LAYV------------IYTSGSTGTPKGVAVSHGPLAAhCQATAERYGLTPGDRE---LQFASFN 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 318 --GSLLGIVGCLGIGATVVLKPKfsasQFWDDCQ-------KHRVTVFQ----YIGELCRYLVNQPPSKAEcdhKVRLAV 384
Cdd:cd17649 146 fdGAHEQLLPPLICGACVVLRPD----ELWASADelaemvrELGVTVLDlppaYLQQLAEEADRTGDGRPP---SLRLYI 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 385 --GSGLRPDTWERFLRrfGPLQILETYGMTEGNVATFNYTGRQGAvgRASWLYKHIfpfslirYDVMTGEPIRNAQGHCM 462
Cdd:cd17649 219 fgGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGA--ARAGASMPI-------GRPLGGRSAYILDADLN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 463 TTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFW-SGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVAT 541
Cdd:cd17649 288 PVPVGVTGELY--IGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 542 TEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLqESLATT 615
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPaHLVFL-ARLPLT 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
66-580 |
1.10e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.39 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 66 SLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIArAFLrargwtggrrgsgrgSTEEGARvappagdaaargtta 145
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLA-GYL---------------QQECGVR--------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 146 pplaPGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTA--LRRGPLLHCLRSCGASALVLATEFLESLEPdlpALRAMG 223
Cdd:PRK08314 60 ----KGDRVLLYMQNSPQFVIAYYAILRAN--AVVVPVNpmNREEELAHYVTDSGARVAIVGSELAPKVAP---AVGNLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 224 L-HLWATG------PETNVAGISNLLSEAADQVDEP--------------VPGYLSAPQNimDTCLYIFTSGTTGLPKAA 282
Cdd:PRK08314 131 LrHVIVAQysdylpAEPEIAVPAWLRAEPPLQALAPggvvawkealaaglAPPPHTAGPD--DLAVLPYTSGTTGVPKGC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 283 RISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqfWD-----DC-QKHRVTV 355
Cdd:PRK08314 209 MHTHRTVMaNAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------WDreaaaRLiERYRVTH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 356 FQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLR-PD-TWERFLRRFGpLQILETYGMTE------GN-----------V 416
Cdd:PRK08314 283 WTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAmPEaVAERLKELTG-LDYVEGYGLTEtmaqthSNppdrpklqclgI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ATFNYTGRqgavgraswlykhifpfsLIryDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKL 496
Cdd:PRK08314 362 PTFGVDAR------------------VI--DPETLEEL----------PPGEVGEIV--VHGPQVFKGYWNRPEATAEAF 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 497 LKdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 576
Cdd:PRK08314 410 IE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDP-RRGETVKAVV 485
|
....
gi 82581629 577 ALRP 580
Cdd:PRK08314 486 VLRP 489
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
79-606 |
1.59e-15 |
|
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: 79.43 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATVALLL 158
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTL-------------------------------RGLG-----VAPGSVVGVCA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRamglhlwatgpetnvagI 238
Cdd:cd17650 45 DRSLDAIVGLLAVLKAG--GAYVP-----------------------------IDPDYPAER-----------------L 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 239 SNLLSEAAdqvdepVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQEDVIY--LALPLYHM 316
Cdd:cd17650 77 QYMLEDSG------AKLLLTQPE---DLAYVIYTSGTTGKPKGVMVEH------RNVAHA--AHAWRREYelDSFPVRLL 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 317 SGSLLGI-------VGCLGIGATVVLKP---KFSASQFWDDCQKHRVTVFQYIGELCRYLVnqppskAECD-HKVR---- 381
Cdd:cd17650 140 QMASFSFdvfagdfARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVM------AYVYrNGLDlsam 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 --LAVGSGLRPDTWERFL-RRFGP-LQILETYGMTEGNVATFNYTGRQGAVGRASwlykhifpfsliryDVMTGEPIRNA 457
Cdd:cd17650 214 rlLIVGSDGCKAQDFKTLaARFGQgMRIINSYGVTEATIDSTYYEEGRDPLGDSA--------------NVPIGRPLPNT 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 458 QGHCMTTS--------PGEPGLLVAPVSQqspflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTG 529
Cdd:cd17650 280 AMYVLDERlqpqpvgvAGELYIGGAGVAR-----GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVD 354
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82581629 530 DTIRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHEGRAGMAALA--LRPPQALNLVQLYSHVSENLPPYARPRFL 606
Cdd:cd17650 355 HQVKIRGFRIELGEIESQL-----ARHPAIDEAVVAVREDKGGEARLCayVVAAATLNTAELRAFLAKELPSYMIPSYY 428
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
176-604 |
1.80e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 79.80 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 176 LRTAFVPTALRrgpllHCLRSCGASALVLATEFLESLEPDLPAL-RAMGLHLWATGP-ETNVAGisnLLSEAADQvdEPV 253
Cdd:PRK13382 123 LNTSFAGPALA-----EVVTREGVDTVIYDEEFSATVDRALADCpQATRIVAWTDEDhDLTVEV---LIAAHAGQ--RPE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 254 PgylsAPQNimdTCLYIFTSGTTGLPKAARISHLKvlqcqGFYHLCGV------HQEDVIYLALPLYHMSGsLLGIVGCL 327
Cdd:PRK13382 193 P----TGRK---GRVILLTSGTTGTPKGARRSGPG-----GIGTLKAIldrtpwRAEEPTVIVAPMFHAWG-FSQLVLAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 328 GIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP---SKAECDH-KVRLAVGSGLRPDTWERFLRRFGPL 403
Cdd:PRK13382 260 SLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevrNRYSGRSlRFAAASGSRMRPDVVIAFMDQFGDV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 404 qILETYGMTE-GNVATFNYTGRQGA---VGRASwlykhifpfslirydvmTGEPIRNAQGHCMTTSPGEPGLLVapVSQQ 479
Cdd:PRK13382 340 -IYNNYNATEaGMIATATPADLRAApdtAGRPA-----------------EGTEIRILDQDFREVPTGEVGTIF--VRND 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 480 SPFLGYagAPELAKDkllkdvFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNI 559
Cdd:PRK13382 400 TQFDGY--TSGSTKD------FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAV 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 82581629 560 YGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 604
Cdd:PRK13382 470 IGVDDEQY-GQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPR 513
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
153-619 |
1.97e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 79.44 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 153 TVALLLPAGPDFLWIWFGLAKAGLrTAfVPTALR--RGPLLHCLRSCGASALVLATEFLESLepdlpalramglhlwaTG 230
Cdd:PRK07638 52 TIAILLENRIEFLQLFAGAAMAGW-TC-VPLDIKwkQDELKERLAISNADMIVTERYKLNDL----------------PD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 231 PETNVAGISNLLSEAADQVDEPVPGylsapQNIMDTCLYI-FTSGTTGLPKA---ARISHLKVLQCQGfyHLCGVHQEDV 306
Cdd:PRK07638 114 EEGRVIEIDEWKRMIEKYLPTYAPI-----ENVQNAPFYMgFTSGSTGKPKAflrAQQSWLHSFDCNV--HDFHMKREDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 307 IYLALPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQppsKAECDHKVRLaVGS 386
Cdd:PRK07638 187 VLIAGTLVH-SLFLYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKI-ISS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 387 GLRpdtW-----ERFLRRFGPLQILETYGMTEGNVATF----NYTGRQGAVGRaswlykhifPFSLIRYDvmtgepIRNA 457
Cdd:PRK07638 262 GAK---WeaeakEKIKNIFPYAKLYEFYGASELSFVTAlvdeESERRPNSVGR---------PFHNVQVR------ICNE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 458 QGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDklLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWK 535
Cdd:PRK07638 324 AGE--EVQKGEIGTVYV----KSPqfFMGYIIGGVLARE--LNADGW-----MTVRDVGYEDEEGFIYIVGREKNMILFG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 536 GENVATTEVAEVLETLDFLQEVNIYGVTVPghegRAGMAALALRPPQAlNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:PRK07638 391 GINIFPEEIESVLHEHPAVDEIVVIGVPDS----YWGEKPVAIIKGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYT 465
|
....
gi 82581629 616 ETFK 619
Cdd:PRK07638 466 NSGK 469
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
270-615 |
2.09e-15 |
|
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: 79.21 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAARISHLKVLQcqgFY-HLCG---VHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSAS 342
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVS---FTnWMLSdfpLGPGDVF-LNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 343 QFWDDCQKHRVTVF---QYIGELCR----YLVNQPPSkaecdhkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 413
Cdd:cd05945 179 QLFRFLAEHGITVWvstPSFAAMCLlsptFTPESLPS-------LRHFLFCGevLPHKTARALQQRFPDARIYNTYGPTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 GNVATfnytgrqgavgraswLYKHIFPFSLIRYDVMT-GEP-------IRNAQGHCMttSPGEPGLLVapVSQQSPFLGY 485
Cdd:cd05945 252 ATVAV---------------TYIEVTPEVLDGYDRLPiGYAkpgaklvILDEDGRPV--PPGEKGELV--ISGPSVSKGY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 486 AGAPELAKDKLLKDvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVP 565
Cdd:cd05945 313 LNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKY 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 82581629 566 GHEGRAGMAA-LALRPP-QALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:cd05945 388 KGEKVTELIAfVVPKPGaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
138-622 |
2.65e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 78.90 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVlATEFLESLEP--- 214
Cdd:PRK13390 36 ALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV-ASAALDGLAAkvg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 215 -DLPALRAMGLHLWATGP-ETNVAGISNLLSEaadqvdEPVPGYLsapqnimdtclyIFTSGTTGLPKAAR--ISHLKVL 290
Cdd:PRK13390 115 aDLPLRLSFGGEIDGFGSfEAALAGAGPRLTE------QPCGAVM------------LYSSGTTGFPKGIQpdLPGRDVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 291 Q--------CQGFYhlcGVHQEDVIYLALPLYHMSG-SLLGIVGCLGigATVVLKPKFSASQFWDDCQKHRVTVFQYIGE 361
Cdd:PRK13390 177 ApgdpivaiARAFY---DISESDIYYSSAPIYHAAPlRWCSMVHALG--GTVVLAKRFDAQATLGHVERYRITVTQMVPT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 362 L-CRYLVNQPPSKAECDHKVRLAVGSGLRP---DTWERFLRRFGPLqILETYGMTEGNVATFNYTGR----QGAVGRAsw 433
Cdd:PRK13390 252 MfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvDVKHAMIDWLGPI-VYEYYSSTEAHGMTFIDSPDwlahPGSVGRS-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 434 lykhifpfslirydVMTGEPIRNAQGHCMTTspGEPGlLVAPVSQQSPFlGYAGAPE-LAKDKLLKDVFWSgdvffNTGD 512
Cdd:PRK13390 329 --------------VLGDLHICDDDGNELPA--GRIG-TVYFERDRLPF-RYLNDPEkTAAAQHPAHPFWT-----TVGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 513 LLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP--GHEGRAGMAALA-LRPPQALNLvQL 589
Cdd:PRK13390 386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemGEQVKAVIQLVEgIRGSDELAR-EL 464
|
490 500 510
....*....|....*....|....*....|...
gi 82581629 590 YSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:PRK13390 465 IDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVK 497
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
140-622 |
3.22e-15 |
|
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: 78.33 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 140 ARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAG-----LRTAFVPTALRrgpllHCLRSCGASALVlatefleslep 214
Cdd:cd05973 14 ANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGavyqpLFTAFGPKAIE-----HRLRTSGARLVV----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 215 dlpalramglhlwatgpeTNVAGISNLLSeaadqvdepvpgylsapqnimDTCLYIFTSGTTGLPKAARIShLKVLQCQG 294
Cdd:cd05973 78 ------------------TDAANRHKLDS---------------------DPFVMMFTSGTTGLPKGVPVP-LRALAAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 295 FY--HLCGVHQEDVIY-LALP-----LYHmsgsllGIVGCLGIG-ATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRY 365
Cdd:cd05973 118 AYlrDAVDLRPEDSFWnAADPgwaygLYY------AITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 366 LVNQPPSkAECDHKVRLAV----GSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFNYTG-----RQGAVGRAswlyk 436
Cdd:cd05973 192 LMAAGAE-VPARPKGRLRRvssaGEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHHAlehpvHAGSAGRA----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 437 hiFP-FSLIRYDVMTGEPirnaqghcmttSPGEPGLLVAPVSQqSP---FLGYAGAPELAKDkllkdvfwsGDvFFNTGD 512
Cdd:cd05973 265 --MPgWRVAVLDDDGDEL-----------GPGEPGRLAIDIAN-SPlmwFRGYQLPDTPAID---------GG-YYLTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 513 LLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYG--------------VTVPGHEGRAGMAAlal 578
Cdd:cd05973 321 TVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGvpdpertevvkafvVLRGGHEGTPALAD--- 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 82581629 579 rppqalnlvQLYSHVSENLPPYARPRFLRLQESLATTETFKQQK 622
Cdd:cd05973 398 ---------ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
149-413 |
3.60e-15 |
|
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: 78.82 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 149 APGATVALLLPAGPDFLWIWFGLAKAGL--RTAFVPTALRRGP-LLHCLRSCGASALVLATEFLESLEPDLPALRAMGLH 225
Cdd:cd05931 46 KPGDRVLLLAPPGLDFVAAFLGCLYAGAiaVPLPPPTPGRHAErLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATgpetnvagISNLLSEAADQVDEPVPGYLsapqnimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQE 304
Cdd:cd05931 126 RLLV--------VDLLPDTSAADWPPPSPDPD-------DIAYLQYTSGSTGTPKGVVVTHRNLLaNVRQIRRAYGLDPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 305 DVIYLALPLYH-MsgsllGIVGCLGI----GATVVLKPKFSASQ---FW-DDCQKHRVTV-----FQYigELC-RYLvnQ 369
Cdd:cd05931 191 DVVVSWLPLYHdM-----GLIGGLLTplysGGPSVLMSPAAFLRrplRWlRLISRYRATIsaapnFAY--DLCvRRV--R 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 82581629 370 PPSKAECD-HKVRLAVgSG---LRPDTWERFLRRFGPL-----QILETYGMTE 413
Cdd:cd05931 262 DEDLEGLDlSSWRVAL-NGaepVRPATLRRFAEAFAPFgfrpeAFRPSYGLAE 313
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
79-610 |
5.08e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 78.10 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGTTapplaPGATVALLL 158
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARL-------------------------------RARGVG-----PGDRVAVYL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGAsALVLATEFLeslePDLPALRAMGLHLWATGPEtnva 236
Cdd:cd12116 45 PRSARLVAAMLAVLKAGA--AYVPldPDYPADRLRYILEDAEP-ALVLTDDAL----PDRLPAGLPVLLLALAAAA---- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 237 gisnllsEAADQVDEPVPGYLSApqnimdtclY-IFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIyLALPLY 314
Cdd:cd12116 114 -------AAPAAPRTPVSPDDLA---------YvIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGLGPGDRL-LAVTTY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 315 HMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAEcdhKVRLAVG-SGLRP 390
Cdd:cd12116 177 AFDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRA---GLTALCGgEALPP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 391 DTWERFLRRFGPLQILetYGMTEGNVATfnytgrqgAVGRASWLYKHIfpfslirydvMTGEPIRNAQGHC-----MTTS 465
Cdd:cd12116 254 DLAARLLSRVGSLWNL--YGPTETTIWS--------TAARVTAAAGPI----------PIGRPLANTQVYVldaalRPVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 466 PGEPGLLV---APVSQqspflGYAGAPELAKDKLLKDVFW-SGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVAT 541
Cdd:cd12116 314 PGVPGELYiggDGVAQ-----GYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82581629 542 TEVAEVLETLDFLQEVniyGVTVPGHEGRAGMAALALRP-PQALNLVQLYSHVSENLPPYARP-RFLRLQE 610
Cdd:cd12116 389 GEIEAALAAHPGVAQA---AVVVREDGGDRRLVAYVVLKaGAAPDAAALRAHLRATLPAYMVPsAFVRLDA 456
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
268-625 |
5.83e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 77.92 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWD 346
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQtAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 347 DCQKHRVTVFQYIG--ELCRYLVNQPP-SKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY- 421
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGfDAAALRHLTALFTGGAPHAAEDILGWLDDG-IPMVDGFGMSEaGTVFGMSVd 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 422 ----TGRQGAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPG--LLVAPvsqqSPFLGYAGAPELAKDK 495
Cdd:PRK09088 298 cdviRAKAGAAGIPT-------PTVQTR--------VVDDQGN--DCPAGVPGelLLRGP----NLSPGYWRRPQATARA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 496 LlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAA 575
Cdd:PRK09088 357 F------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA-QWGEVGYLA 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 82581629 576 LALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 625
Cdd:PRK09088 430 IVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
138-629 |
1.28e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 76.57 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGASALvlatefLESLEPD 215
Cdd:PRK07787 32 AGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAG--VPVVPVPPDSGVaeRRHILADSGAQAW------LGPAPDD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 216 LPALRAMGLHLWATGPETnvagisnllseaadqVDEPVPGylsapqnimDTCLYIFTSGTTGLPKAARISHLKVLQC-QG 294
Cdd:PRK07787 104 PAGLPHVPVRLHARSWHR---------------YPEPDPD---------APALIVYTSGTTGPPKGVVLSRRAIAADlDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 295 FYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRV------TVFQYIGElcrylvn 368
Cdd:PRK07787 160 LAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSEGGTlyfgvpTVWSRIAA------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 369 qPPSKAECDHKVRLAV-GSGLRPDT-WERFLRRFGpLQILETYGMTEG--NVAT-FNYTGRQGAVGRAswlykhiFPFSL 443
Cdd:PRK07787 233 -DPEAARALRGARLLVsGSAALPVPvFDRLAALTG-HRPVERYGMTETliTLSTrADGERRPGWVGLP-------LAGVE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 444 IRYDVMTGEPIrnaqghcmtTSPGEPgllVAPVSQQSP--FLGYAGAPELAKDKllkdvfWSGDVFFNTGDLLVCDEQGF 521
Cdd:PRK07787 304 TRLVDEDGGPV---------PHDGET---VGELQVRGPtlFDGYLNRPDATAAA------FTADGWFRTGDVAVVDPDGM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 522 LHFHDRTG-DTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQlysHVSENLPPY 600
Cdd:PRK07787 366 HRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELID---FVAQQLSVH 442
|
490 500
....*....|....*....|....*....
gi 82581629 601 ARPRFLRLQESLATTETFKQQKVRMANEG 629
Cdd:PRK07787 443 KRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
265-527 |
2.44e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 76.89 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMsgslLGIVG------CLGIGATVVLKP 337
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILsNIEQISDVFNLRNDDVILSSLPFFHS----FGLTVtlwlplLEGIKVVYHPDP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 338 kFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFGpLQILETYGMTEG 414
Cdd:PRK08633 859 -TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVV-AGaekLKPEVADAFEEKFG-IRILEGYGATET 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 415 N-VATFN-----------YTG-RQGAVGRAswlykhiFPFSLIR-YDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQS 480
Cdd:PRK08633 936 SpVASVNlpdvlaadfkrQTGsKEGSVGMP-------LPGVAVRiVDPETFEEL----------PPGEDGLIL--IGGPQ 996
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 82581629 481 PFLGYAGAPELAKdKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDR 527
Cdd:PRK08633 997 VMKGYLGDPEKTA-EVIKDIDGIG--WYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
79-425 |
3.25e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.69 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdaaARGttappLAPGATVALLL 158
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLI-------------------------------AQG-----LGPGDHVGIYA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAglRTAFVPTALR--RGPLLHCLRSCGASALVLATEFLESLEPDLPALRamGLHLW-----ATGP 231
Cdd:PRK07798 61 RNRIEYVEAMLGAFKA--RAVPVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLP--KLRTLvvvedGSGN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 232 ETNVAGISnLLSEAADQVDEPVPGYLSApqnimDTCLYIFTSGTTGLPKAA--RISHLKVLQCQGFYHLCG--VHQED-- 305
Cdd:PRK07798 137 DLLPGAVD-YEDALAAGSPERDFGERSP-----DDLYLLYTGGTTGMPKGVmwRQEDIFRVLLGGRDFATGepIEDEEel 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 306 ----------VIYLALPLYHMSGsLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTVFQYIGE-LCRYLVN--QP 370
Cdd:PRK07798 211 akraaagpgmRRFPAPPLMHGAG-QWAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLLDalEA 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 371 PSKAECDHKVrlAVGSG---LRPDTWERFLRRFGPLQILETYGMTEgnvATFNYTGRQ 425
Cdd:PRK07798 290 RGPYDLSSLF--AIASGgalFSPSVKEALLELLPNVVLTDSIGSSE---TGFGGSGTV 342
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
79-615 |
3.82e-14 |
|
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: 75.39 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAflrargwtggrrgsgrgsteegarvappagdAAARGttappLAPGATVALLL 158
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGA-------------------------------LKAAG-----VRPGDLVAVTL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGlrTAFVPT-----ALRRGPLLHclrSCGASaLVLATEFLESLEPDLPALramglhlwatgpet 233
Cdd:cd12114 45 PKGPEQVVAVLGILAAG--AAYVPVdidqpAARREAILA---DAGAR-LVLTDGPDAQLDVAVFDV-------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 234 nvagiSNLLSEAADQVDEPVPGyLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALP 312
Cdd:cd12114 105 -----LILDLDALAAPAPPPPV-DVAPD---DLAYVIFTSGSTGTPKGVMISHRAALNtILDINRRFAVGPDDRV-LALS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 313 LYHMSGSLLGIVGCLGIGATVVLKP---KFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG-- 387
Cdd:cd12114 175 SLSFDLSVYDIFGALSAGATLVLPDearRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdw 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 388 LRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKhiFPFSLIRYDVMtgepirNAQG-HCMTTSP 466
Cdd:cd12114 255 IPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYG--RPLANQRYRVL------DPRGrDCPDWVP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 467 GE---PGLLVApvsqqspfLGYAGAPELAKDKLLKDVfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTE 543
Cdd:cd12114 327 GElwiGGRGVA--------LGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82581629 544 VAEVLETldfLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQ--LYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:cd12114 397 IEAALQA---HPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPdaLRAFLAQTLPAYMIPSRVIALEALPLT 467
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
251-566 |
3.88e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 75.61 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 251 EPVPGYLSAPQNIMDTClyiFTSGTTGLPKAARISHLkVLQCQGFYHLCGV-HQEDVIYL-ALPLYHMsGSLLGIVGCLG 328
Cdd:PLN02860 162 TTELDYAWAPDDAVLIC---FTSGTTGRPKGVTISHS-ALIVQSLAKIAIVgYGEDDVYLhTAPLCHI-GGLSSALAMLM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 329 IGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA--ECDHKVR--LAVGSGLRPDTWERFLRRFGPLQ 404
Cdd:PLN02860 237 VGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMtwKVFPSVRkiLNGGGSLSSRLLPDAKKLFPNAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 405 ILETYGMTEG-NVATFN--YTGRQGAVGRASWLYKHIFPFSLIRYD-VMTGEPIRNAQ-GHCMTTSPGEPGLLVapvsqQ 479
Cdd:PLN02860 317 LFSAYGMTEAcSSLTFMtlHDPTLESPKQTLQTVNQTKSSSVHQPQgVCVGKPAPHVElKIGLDESSRVGRILT-----R 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 480 SP--FLGYAG-APELAKDKllkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLetldfLQE 556
Cdd:PLN02860 392 GPhvMLGYWGqNSETASVL-------SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL-----SQH 459
|
330
....*....|
gi 82581629 557 VNIYGVTVPG 566
Cdd:PLN02860 460 PGVASVVVVG 469
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
256-610 |
4.11e-14 |
|
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: 75.04 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 256 YLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHL---CGVHQEDVIYLALPLyhmSGSLLGIVGCLGIGAT 332
Cdd:cd17653 100 TTDSPD---DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPArldVGPGSRVAQVLSIAF---DACIGEIFSTLCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 333 VVLK-PKFSASQFWDDC----------QKHRVTVFQYIGELcrYLVNQPPSKAecdhkvrLAvgsglrpDTWeRFLRRFg 401
Cdd:cd17653 174 LVLAdPSDPFAHVARTVdalmstpsilSTLSPQDFPNLKTI--FLGGEAVPPS-------LL-------DRW-SPGRRL- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 402 plqiLETYGMTEGNVATfnytgrqgavgraswLYKHIFPfsliRYDVMTGEPIRNA-----QGHCMTTSPGEPGLLVapV 476
Cdd:cd17653 236 ----YNAYGPTECTISS---------------TMTELLP----GQPVTIGKPIPNStcyilDADLQPVPEGVVGEIC--I 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 477 SQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDflQE 556
Cdd:cd17653 291 SGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ--PE 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 82581629 557 VNIYGVTVpgHEGRagmaALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLQE 610
Cdd:cd17653 369 VTQAAAIV--VNGR----LVAFVTPETVDVDGLRSELAKHLPSYAVPdRIIALDS 417
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
265-604 |
4.43e-14 |
|
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: 75.26 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVlqCQGFYH------LCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPK 338
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNI--VARFSHardpifGNQIIPDTAILTVIPFHHGFG-MFTTLGYLICGFRVVLMYK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 339 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLAVGSG-LRPDTWERFLRRFGPLQILETYGMTEGNV 416
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTS 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 A---TFNYTGRQGAVGRaswlykhIFPFSLIRY-DVMTGEpirnaqghcmTTSPGEPGLLVApvsqQSPFL--GYAGAPE 490
Cdd:cd17642 342 AiliTPEGDDKPGAVGK-------VVPFFYAKVvDLDTGK----------TLGPNERGELCV----KGPMImkGYVNNPE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 491 LAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGR 570
Cdd:cd17642 401 ATKALIDKD-GW-----LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE-DAGE 473
|
330 340 350
....*....|....*....|....*....|....
gi 82581629 571 AGMAALALRPPQALNLVQLYSHVSENLPPYARPR 604
Cdd:cd17642 474 LPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
151-619 |
3.03e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 72.57 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFG-LAKAGLRTAFVPTAlRRGPLLHCLRSCGASALVLATEFLESLEP-DLPALRAM-GLHLW 227
Cdd:PLN02574 92 GDVVLLLLPNSVYFPVIFLAvLSLGGIVTTMNPSS-SLGEIKKRVVDCSVGLAFTSPENVEKLSPlGVPVIGVPeNYDFD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 228 ATGPETnvAGISNLLSEAADQVDEPVPGylsapQNimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQE-- 304
Cdd:PLN02574 171 SKRIEF--PKFYELIKEDFDFVPKPVIK-----QD--DVAAIMYSSGTTGASKGVVLTHRNLIaMVELFVRFEASQYEyp 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 305 --DVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKV 380
Cdd:PLN02574 242 gsDNVYLAaLPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 381 RLaVGSGLRP---DTWERFLRRFGPLQILETYGMTEGNvatfnytgrqgAVGRASWLYKHIFPFSLIRYDV--MTGEPIR 455
Cdd:PLN02574 322 KQ-VSCGAAPlsgKFIQDFVQTLPHVDFIQGYGMTEST-----------AVGTRGFNTEKLSKYSSVGLLApnMQAKVVD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 456 NAQGHCMttSPGEPGLLVApvsqQSPFL--GYAGAPELAKDKLLKDVfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIR 533
Cdd:PLN02574 390 WSTGCLL--PPGNCGELWI----QGPGVmkGYLNNPKATQSTIDKDG-W-----LRTGDIAYFDEDGYLYIVDRLKEIIK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 534 WKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:PLN02574 458 YKGFQIAPADLEAVLISHPEIIDAAVTA--VPDKEcGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSI 535
|
....*..
gi 82581629 613 ATTETFK 619
Cdd:PLN02574 536 PKSPAGK 542
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
140-619 |
1.49e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 140 ARGTTAPPLAPGATVALLLPAGPDFLWIWFG-LAKAGLRTAFVPTALRrGPLLHCLRSCGASALVlatefleSLEPDLPA 218
Cdd:PLN02330 69 AKALRSLGLRKGQVVVVVLPNVAEYGIVALGiMAAGGVFSGANPTALE-SEIKKQAEAAGAKLIV-------TNDTNYGK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 219 LRAMGLHLWATGPETNVAGIS-NLLSEAADQVdepvpGYLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLKVLQ--CQ 293
Cdd:PLN02330 141 VKGLGLPVIVLGEEKIEGAVNwKELLEAADRA-----GDTSDNEEILqtDLCALPFSSGTTGISKGVMLTHRNLVAnlCS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 294 GFYhlcGVHQE---DVIYLAL-PLYHMSGsLLGIV-GCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 368
Cdd:PLN02330 216 SLF---SVGPEmigQVVTLGLiPFFHIYG-ITGICcATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 369 QPPSKAECDHKVRL----AVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASwlyKHIFPFSLI 444
Cdd:PLN02330 292 NPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAK---KNSVGFILP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 445 RYDVMTGEPiRNAQGHCMTTsPGEpgllvAPVSQQSPFLGYAGAPElAKDKLLKDVFWsgdvfFNTGDLLVCDEQGFLHF 524
Cdd:PLN02330 369 NLEVKFIDP-DTGRSLPKNT-PGE-----LCVRSQCVMQGYYNNKE-ETDRTIDEDGW-----LHTGDIGYIDDDGDIFI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 525 HDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 603
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKESEEDILNFVAANVAHYKKV 513
|
490
....*....|....*.
gi 82581629 604 RFLRLQESLATTETFK 619
Cdd:PLN02330 514 RVVQFVDSIPKSLSGK 529
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-595 |
9.28e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 68.09 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAReQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAP 150
Cdd:PRK06188 19 VSALKR-YPDRPALVLGDTRLTYGQLADRISRYIQAF-------------------------------EALG-----LGT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDfLWIWFGLAK-AGLRTafvpTALRrgPL------LHCLRSCGASALVL-ATEFLESLEpdlpAL--R 220
Cdd:PRK06188 62 GDAVALLSLNRPE-VLMAIGAAQlAGLRR----TALH--PLgslddhAYVLEDAGISTLIVdPAPFVERAL----ALlaR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 221 AMGL-HLWATGPetnvAGISNLLSEAADQVdEPVPgyLSAPQNIMDTCLYIFTSGTTGLPKAARISH-----LKVLQCQG 294
Cdd:PRK06188 131 VPSLkHVLTLGP----VPDGVDLLAAAAKF-GPAP--LVAAALPPDIAGLAYTGGTTGKPKGVMGTHrsiatMAQIQLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 295 FYHlcgvhQEDVIYLAL-PLYHMSGSLlgIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSK 373
Cdd:PRK06188 204 WEW-----PADPRFLMCtPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 374 AECDHKVRLAV--GSGLRPDTWERFLRRFGPLqILETYGMTE-GNVATF--------NYTGRQGAVGRASwlykhifPFS 442
Cdd:PRK06188 277 TRDLSSLETVYygASPMSPVRLAEAIERFGPI-FAQYYGQTEaPMVITYlrkrdhdpDDPKRLTSCGRPT-------PGL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 443 LIRYDVMTGEPIrnaqghcmttSPGEPG-LLVApvsqqSPFL--GYAGAPElAKDKLLKDVfWsgdvfFNTGDLLVCDEQ 519
Cdd:PRK06188 349 RVALLDEDGREV----------AQGEVGeICVR-----GPLVmdGYWNRPE-ETAEAFRDG-W-----LHTGDVAREDED 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82581629 520 GFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSE 595
Cdd:PRK06188 407 GFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKE 481
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-604 |
9.70e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 67.02 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLCGVHQED-------------VIYLALPLYHMSGSLLGIVGCLGI 329
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedIFRMLMGGADFGTGEFTPSedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 330 GATVVLKPKFSASQFWDDCQKHRVTVFQYIGE-LCRYLVNQPPSKAECDHKVRLAVGSG---LRPDTWERFLRRFGPLQI 405
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 406 LETYGMTEGNVATFNYTGRQGAVGRaswlykhifPFSLIRYDVMTGEPirnaQGHCMTTSPGEPGLL----VAPvsqqsp 481
Cdd:cd05924 164 VDAFGSSETGFTGSGHSAGSGPETG---------PFTRANPDTVVLDD----DGRVVPPGSGGVGWIarrgHIP------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 482 fLGYAGAPELAKD--KLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETldflqEVNI 559
Cdd:cd05924 225 -LGYYGDEAKTAEtfPEVDGVRYA-----VPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-----HPAV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 82581629 560 YGVTVPGHE----GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 604
Cdd:cd05924 294 YDVLVVGRPderwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPK 342
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
262-619 |
1.27e-11 |
|
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: 67.04 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 262 NIMDTCLYIFTSGTTGLPKAARISHLKVLQCQ----GFYHLCGVHQEDVIYLA-----LPLYHMSGSLLGivgclgiGAT 332
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRtslsERYFGRDNGDEAVLFFSnyvfdFFVEQMTLALLN-------GQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 333 VVLKP---KFSASQFWDDCQKHRVTvfqyigelcrYLvNQPPSK------AECDH-KVRLAVGSGLRPDTWERFLRRFgP 402
Cdd:cd17648 165 LVVPPdemRFDPDRFYAYINREKVT----------YL-SGTPSVlqqydlARLPHlKRVDAAGEEFTAPVFEKLRSRF-A 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 403 LQILETYGMTEGNVATfnytgrqgavgraswlYKHIFPFSLiRYDVMTGEPIRNAQ----GHCMTTSP----GE---PGL 471
Cdd:cd17648 233 GLIINAYGPTETTVTN----------------HKRFFPGDQ-RFDKSLGRPVRNTKcyvlNDAMKRVPvgavGElylGGD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 472 LVAPvsqqspflGYAGAPELAKDKLLKDVFWSGD--------VFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTE 543
Cdd:cd17648 296 GVAR--------GYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 544 VAEVLETLDFLQE---VNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLqESLATTETFK 619
Cdd:cd17648 368 VEAALASYPGVREcavVAKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPaRLVRL-EGIPVTINGK 446
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
265-619 |
2.39e-11 |
|
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: 65.43 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 fwddcQKHRVTVFQYIG----ELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLqiLETYGMTE--GNVA 417
Cdd:cd17630 80 -----EDLAPPGVTHVSlvptQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPL--YTTYGMTEtaSQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 418 TFNYTG-RQGAVGRaswlykhifPFSLIRYDVmtgepirnaqghcmtTSPGEpgLLVAPVSQQSPFLGYAGAPELAKDKl 496
Cdd:cd17630 153 TKRPDGfGRGGVGV---------LLPGRELRI---------------VEDGE--IWVGGASLAMGYLRGQLVPEFNEDG- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 497 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 576
Cdd:cd17630 206 -----W-----FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE-ELGQRPVAVI 274
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 82581629 577 ALRPPqaLNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd17630 275 VGRGP--ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGK 315
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
75-610 |
2.57e-11 |
|
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: 66.58 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsTEEGarvappagdaaargttappLAPGATV 154
Cdd:cd17655 7 AEKTPDHTAVVFEDQTLTYRELNERANQLARTL-----------------REKG-------------------VGPDTIV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPT----ALRRgpLLHCLRSCGASaLVLATEFLESLEPDLPALRAMGLHLWATG 230
Cdd:cd17655 51 GIMAERSLEMIVGILGILKAG--GAYLPIdpdyPEER--IQYILEDSGAD-ILLTQSHLQPPIAFIGLIDLLDEDTIYHE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 231 PETNvagisnllseaadqvdepvpgyLSAPQNIMDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQ-EDVIYL 309
Cdd:cd17655 126 ESEN----------------------LEPVSKSDDLAYVIYTSGSTGKPKGVMIEH------RGVVNL--VEWaNKVIYQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 310 A----LPLY---HMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQ---KHRVTVfqyigelcrylVNQPPS------- 372
Cdd:cd17655 176 GehlrVALFasiSFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQyirQNRITI-----------IDLTPAhlkllda 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 373 ---KAECDHKVRLAVGSGLRPDTWERFLRRFGP-LQILETYGMTEGNV--ATFNYTGrqgavgraSWLYKHIFPFsliry 446
Cdd:cd17655 245 addSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVdaSIYQYEP--------ETDQQVSVPI----- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 447 dvmtGEPIRNAQGHCMTTS----P-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGF 521
Cdd:cd17655 312 ----GKPLGNTRIYILDQYgrpqPvGVAGELY--IGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGN 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 522 LHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAA-LALRPPqaLNLVQLYSHVSENLPPY 600
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV--IARKDEQGQNYLCAyIVSEKE--LPVAQLREFLARELPDY 461
|
570
....*....|.
gi 82581629 601 ARPR-FLRLQE 610
Cdd:cd17655 462 MIPSyFIKLDE 472
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
151-413 |
3.29e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.16 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 151 GATVALLLPAGPDFLWIWFGLAKAG--LRTA---FVPTALRRGpllhcLRSCGASALVLATEFLESLePDLPALRAMGLH 225
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGavTTTAnpfYTPAEIAKQ-----AKASGAKLIITQSCYVDKL-KGLAEDDGVTVV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATGPEtNVAGISNLLseAADqvDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHlKVL------QCQG----F 295
Cdd:PLN02246 149 TIDDPPE-GCLHFSELT--QAD--ENELPEVEISPD---DVVALPYSSGTTGLPKGVMLTH-KGLvtsvaqQVDGenpnL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 YhlcgVHQEDVIYLALPLYHMSgSLLGIVGC-LGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA 374
Cdd:PLN02246 220 Y----FHSDDVILCVLPMFHIY-SLNSVLLCgLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEK 294
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 82581629 375 ECDHKVRLaVGSGLRP--DTWERFLRRFGPLQIL-ETYGMTE 413
Cdd:PLN02246 295 YDLSSIRM-VLSGAAPlgKELEDAFRAKLPNAVLgQGYGMTE 335
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
148-615 |
1.26e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 64.46 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAGLrtafvpTALRRGPLL------HCLRSCGASALVLATEF---LESLEPD--- 215
Cdd:PRK12492 72 LVPGDRIAVQMPNVLQYPIAVFGALRAGL------IVVNTNPLYtaremrHQFKDSGARALVYLNMFgklVQEVLPDtgi 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 216 -----------LPALRAMGL-----HLWATGPETNV---AGISNLLSEAADQVDEPVPgylsapQNIMDTCLYIFTSGTT 276
Cdd:PRK12492 146 eylieakmgdlLPAAKGWLVntvvdKVKKMVPAYHLpqaVPFKQALRQGRGLSLKPVP------VGLDDIAVLQYTGGTT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 277 GLPKAARISH-------LKVLQCQGFYHLCGVHQ----EDVIYLALPLYHMSGSLLGIVGCLGIGATVVL--KPKfSASQ 343
Cdd:PRK12492 220 GLAKGAMLTHgnlvanmLQVRACLSQLGPDGQPLmkegQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLitNPR-DIPG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKaECDH---KVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN-VATF 419
Cdd:PRK12492 299 FIKELGKWRFSALLGLNTLFVALMDHPGFK-DLDFsalKLTNSGGTALVKATAERWEQLTG-CTIVEGYGLTETSpVAST 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 420 NYTG---RQGAVGraswlykhiFPFSLIRYDVMtgepirNAQGHCMTTspGEPGLLVAPVSQQspFLGYAGAPElAKDKL 496
Cdd:PRK12492 377 NPYGelaRLGTVG---------IPVPGTALKVI------DDDGNELPL--GERGELCIKGPQV--MKGYWQQPE-ATAEA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 497 LKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLetLDFLQEVNIYGVTVPghEGRAGMAAL 576
Cdd:PRK12492 437 LDAEGW-----FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV--MAHPKVANCAAIGVP--DERSGEAVK 507
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 82581629 577 ALRPP--QALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:PRK12492 508 LFVVArdPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMT 548
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
75-610 |
1.37e-10 |
|
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: 63.88 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLAPGATV 154
Cdd:cd12115 9 AARTPDAIALVCGDESLTYAELNRRANRLAARL-------------------------------RAAG-----VGPESRV 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLLPAGPDFLWIWFGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRAMGLhlwatgpeTN 234
Cdd:cd12115 53 GVCLERTPDLVVALLAVLKAG--AAYVP-----------------------------LDPAYPPERLRFI--------LE 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 235 VAGISNLLSEAADqvdepvPGYLsapqnimdtclyIFTSGTTGLPKAARISHLKVLQCQGFY-HLCGVHQedviyLALPL 313
Cdd:cd12115 94 DAQARLVLTDPDD------LAYV------------IYTSGSTGRPKGVAIEHRNAAAFLQWAaAAFSAEE-----LAGVL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 314 YHMSG----SLLGIVGCLGIGATVVLKPkfSASQFWDDCQKHRVTVFQYIGELCRYLVNQP--PSKAECdhkVRLAvGSG 387
Cdd:cd12115 151 ASTSIcfdlSVFELFGPLATGGKVVLAD--NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASVRV---VNLA-GEP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 388 LRPDTWERFLRRFGPLQILETYGMTEgnvATFNYTGrqGAVGRASwlykhifpfsliRYDVMTGEPIRNAQGHCMTTS-- 465
Cdd:cd12115 225 LPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTV--APVPPGA------------SGEVSIGRPLANTQAYVLDRAlq 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 466 ---PGEPGLLV---APVSQqspflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENV 539
Cdd:cd12115 288 pvpLGVPGELYiggAGVAR-----GYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRI 362
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82581629 540 ATTEVAEVLETLDFLQEVnIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLQE 610
Cdd:cd12115 363 ELGEIEAALRSIPGVREA-VVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPsRFVRLDA 433
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
265-561 |
1.43e-10 |
|
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: 63.92 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKpkfSASQ 343
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYT---SIRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQ---------YIGeLCRYLVNQPPSKAECDH------KVRLAV-GSGLRPDTWERFLRRFGpLQILE 407
Cdd:cd17640 165 LKDDLKRVKPHYIVsvprlweslYSG-IQKQVSKSSPIKQFLFLfflsggIFKFGIsGGGALPPHVDTFFEAIG-IEVLN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 408 TYGMTE-GNVATFNYTGR--QGAVGraswlykHIFPFSLIRY-DVMTGEPirnaqghcmtTSPGEPGLLVApvsqQSP-- 481
Cdd:cd17640 243 GYGLTEtSPVVSARRLKCnvRGSVG-------RPLPGTEIKIvDPEGNVV----------LPPGEKGIVWV----RGPqv 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 482 FLGYAGAPElAKDKLLkdvfwSGDVFFNTGDL--LVCDeqGFLHFHDRTGDTIRWK-GENVATTEVAEVLETLDFLQEVN 558
Cdd:cd17640 302 MKGYYKNPE-ATSKVL-----DSDGWFNTGDLgwLTCG--GELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIM 373
|
...
gi 82581629 559 IYG 561
Cdd:cd17640 374 VVG 376
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
140-583 |
1.79e-10 |
|
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: 63.84 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 140 ARGTTAPPLAPGATVALLLPAGPDFL-WIWfglakAGLRTAFVPTALRRGP-----------LLHCLRSCGaSALVLATE 207
Cdd:cd05906 53 AAGLRQLGLRPGDSVILQFDDNEDFIpAFW-----ACVLAGFVPAPLTVPPtydepnarlrkLRHIWQLLG-SPVVLTDA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 208 fleSLEPDLPALRAMGLHLwatgpetnvaGISNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHL 287
Cdd:cd05906 127 ---ELVAEFAGLETLSGLP----------GIRVLSIEELLDTAADHDLPQSRPD---DLALLMLTSGSTGFPKAVPLTHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 288 KVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSL-LGI----VGCLGIGA---TVVLKPkfsaSQFWDDCQKHRVTV--- 355
Cdd:cd05906 191 NILaRSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLravyLGCQQVHVpteEILADP----LRWLDLIDRYRVTItwa 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 356 --FQYiGELCRYLVNQPPSKAECDhKVRLAVGSG--LRPDTWERFLRRFGPLQ-----ILETYGMTE-GNVATFNYTGRQ 425
Cdd:cd05906 267 pnFAF-ALLNDLLEEIEDGTWDLS-SLRYLVNAGeaVVAKTIRRLLRLLEPYGlppdaIRPAFGMTEtCSGVIYSRSFPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 426 GAVGRASwlykhifPF-SLIRydVMTGEPIRNAQGHCMTTSPGEPGLLvaPVSQQSPFLGYAGAPELAKDKLLKDvFWsg 504
Cdd:cd05906 345 YDHSQAL-------EFvSLGR--PIPGVSMRIVDDEGQLLPEGEVGRL--QVRGPVVTKGYYNNPEANAEAFTED-GW-- 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82581629 505 dvfFNTGDLLVCDEqGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDflqevniyGVTVpghegrAGMAALALRPPQA 583
Cdd:cd05906 411 ---FRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVP--------GVEP------SFTAAFAVRDPGA 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
75-615 |
2.42e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 75 AREQPTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgstEEGARVAPPAGDAAARgttapplAPGATV 154
Cdd:PRK12316 521 VERTPEAPALAFGEETLDYAELNRRANRLAHALI-----------------ERGVGPDVLVGVAMER-------SIEMVV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 155 ALLlpagpdflwiwfGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALR----------AMGL 224
Cdd:PRK12316 577 ALL------------AILKAG--GAYVP-----------------------------LDPEYPAERlaymledsgvQLLL 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HLWATGPETNV-AGISNLlseAADQVDEPVPGYLSAPqniMDTCLY-------IFTSGTTGLPKAARISH--LKVLQC-- 292
Cdd:PRK12316 614 SQSHLGRKLPLaAGVQVL---DLDRPAAWLEGYSEEN---PGTELNpenlayvIYTSGSTGKPKGAGNRHraLSNRLCwm 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 293 QGFYHLcGVHQEdviYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVnQ 369
Cdd:PRK12316 688 QQAYGL-GVGDT---VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFL-Q 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 370 PPSKAECDHKVRLAV-GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQgAVGRAswlykhifpfslirydV 448
Cdd:PRK12316 763 DEDVASCTSLRRIVCsGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVE-EGGDS----------------V 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 449 MTGEPIRNAQGHCMttspgEPGLLVAPVSQQSPFL--------GYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQG 520
Cdd:PRK12316 826 PIGRPIANLACYIL-----DANLEPVPVGVLGELYlagrglarGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADG 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 521 FLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVtvpghEGRAGMAALALRPPQALNLVQLYSHVSENLPPY 600
Cdd:PRK12316 901 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGKQLVGYVVLESEGGDWREALKAHLAASLPEY 975
|
570
....*....|....*
gi 82581629 601 ARPRFLRLQESLATT 615
Cdd:PRK12316 976 MVPAQWLALERLPLT 990
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
71-622 |
3.21e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.04 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 71 LAYLAREQ---PTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttapp 147
Cdd:PRK08162 21 LSFLERAAevyPDRPAVIHGDRRRTWAETYARCRRLASAL-------------------------------ARRG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 148 LAPGATVALLLPAGPDFLWIWFGLAKAG--LRTafVPTALRRGPLLHCLRSCGASALVLATEFLESLEPdlpALRAM-GL 224
Cdd:PRK08162 65 IGRGDTVAVLLPNIPAMVEAHFGVPMAGavLNT--LNTRLDAASIAFMLRHGEAKVLIVDTEFAEVARE---ALALLpGP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 225 HLW----ATGPETNVAGISNLLSEAAdqVDEPVPGY-LSAPQNIMDTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHL 298
Cdd:PRK08162 140 KPLvidvDDPEYPGGRFIGALDYEAF--LASGDPDFaWTLPADEWDAIALNYTSGTTGNPKGVVYHHRgAYLNALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 299 CGVHQEDViYL-ALPLYHMSGSLLGIVGCLGIGATVVLKpKFSASQFWDDCQKHRVTvfqyigELC------RYLVNQPP 371
Cdd:PRK08162 218 WGMPKHPV-YLwTLPMFHCNGWCFPWTVAARAGTNVCLR-KVDPKLIFDLIREHGVT------HYCgapivlSALINAPA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 372 S-KAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE--GNV-----------------ATFNytGRQGavgra 431
Cdd:PRK08162 290 EwRAGIDHPVHAMVAGAAPPAAVIAKMEEIG-FDLTHVYGLTEtyGPAtvcawqpewdalplderAQLK--ARQG----- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 432 swlykhifpfslIRY---------DVMTGEPIrNAQGHCMttspGE---PGLLVAPvsqqspflGYagapeLAKDKLLKD 499
Cdd:PRK08162 362 ------------VRYplqegvtvlDPDTMQPV-PADGETI----GEimfRGNIVMK--------GY-----LKNPKATEE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 500 VFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETldfLQEVNIYGVTVPGHE--GRAGMAALA 577
Cdd:PRK08162 412 AFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYR---HPAVLVAAVVAKPDPkwGEVPCAFVE 486
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 82581629 578 LRPPQALNLVQLYSHVSENLPPYARPRFLRLQEsLATTETFKQQK 622
Cdd:PRK08162 487 LKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQK 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
192-540 |
3.22e-10 |
|
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: 62.87 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 192 HCLRSCGASALVL----ATEFLESLEPDLPALRAMGLHlwatGPETNVAGISNLLSEAADQVDEPVPGylsaPQNIMDTc 267
Cdd:cd05932 72 YVLEHSESKALFVgkldDWKAMAPGVPEGLISISLPPP----SAANCQYQWDDLIAQHPPLEERPTRF----PEQLATL- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 lyIFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLgIGATVVLKPKfSASQFWD 346
Cdd:cd05932 143 --IYTSGTTGQPKGVMLTFGSfAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSL-YGGVLVAFAE-SLDTFVE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 347 DCQKHRVTVFQYIGELC-----RYLVNQPPSKAE---------------------CDHKVRLAVGSGLRPDTWERFLRRF 400
Cdd:cd05932 219 DVQRARPTLFFSVPRLWtkfqqGVQDKIPQQKLNlllkipvvnslvkrkvlkglgLDQCRLAGCGSAPVPPALLEWYRSL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 401 GpLQILETYGMTEG-NVATFNYTGRQ--GAVGRASwlykhifPFSLIRYDvmtgepirnAQGHCMTTSPGEpgllvapvs 477
Cdd:cd05932 299 G-LNILEAYGMTENfAYSHLNYPGRDkiGTVGNAG-------PGVEVRIS---------EDGEILVRSPAL--------- 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82581629 478 qqspFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRW-KGENVA 540
Cdd:cd05932 353 ----MMGYYKDPEATAEAF------TADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVA 406
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
270-605 |
1.18e-09 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 61.03 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAARISHLKVLQCQGFYHLC-GVHQED--VIYLAlplYHMSGSLLGIVGCLGIGATVVLKP---KFSASQ 343
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfGVTPADksLVYAS---FSFDASAWEIFPHLTAGAALHVVPserRLDLDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FWDDCQKHRVTVFQYIGELCRYLVNQPpskaecDHKVRLAVGSGlrpDTWERFLRRfgPLQILETYGMTEGNV-ATfnyt 422
Cdd:cd17645 187 LNDYFNQEGITISFLPTGAAEQFMQLD------NQSLRVLLTGG---DKLKKIERK--GYKLVNNYGPTENTVvAT---- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 423 grqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLL 497
Cdd:cd17645 252 ---------------SFEIDKPYANIPIGKPIDNTRvyilDEALQLQPiGVAGELC--IAGEGLARGYLNRPELTAEKFI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 498 KDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEvniygVTVPGHEGRAGMAALA 577
Cdd:cd17645 315 VHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL-----AAVLAKEDADGRKYLV 389
|
330 340 350
....*....|....*....|....*....|
gi 82581629 578 --LRPPQALNLVQLYSHVSENLPPYARPRF 605
Cdd:cd17645 390 ayVTAPEEIPHEELREWLKNDLPDYMIPTY 419
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
270-626 |
1.48e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 60.79 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAARISHLK------VLQCQGFYHLCGVHQEdVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSAS- 342
Cdd:PRK05857 175 IFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWVVGE-TTYSPLPATHIGG-LWWILTCLMHGGLCVTGGENTTSl 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 343 -QFWDDcqkHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWE-RFLRRFGpLQILETYGMTE------- 413
Cdd:PRK05857 253 lEILTT---NAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADvRFIEATG-VRTAQVYGLSEtgctalc 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 -----GNVATFnytgRQGAVGRaswlykhifPFSLIR-YdvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQSP--FLGY 485
Cdd:PRK05857 329 lptddGSIVKI----EAGAVGR---------PYPGVDvY-------LAATDGIGPTAPGAGPSASFGTLWIKSPanMLGY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 486 AGAPELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP 565
Cdd:PRK05857 389 WNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 566 GHEGRAGMAALALRPPQALNLVQL-------YSHVSENLppyARPRFLRLQESLATTETFKQQKVRMA 626
Cdd:PRK05857 462 EFGALVGLAVVASAELDESAARALkhtiaarFRRESEPM---ARPSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
265-619 |
3.35e-09 |
|
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: 59.80 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLY-IFTSGTTGLPKAARISHLKVLQCQGFY--HLCGVHQEDVIYLALPLYHMSGSllGIVGCLGIGATVVLKP---K 338
Cdd:cd17656 128 DDLLYiIYTSGTTGKPKGVQLEHKNMVNLLHFEreKTNINFSDKVLQFATCSFDVCYQ--EIFSTLLSGGTLYIIReetK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 339 FSASQFWDDCQKHR-------VTVFQYIGELCRYLvnqpPSKAEC-DHKVrlAVGSGLR-PDTWERFLRRFGpLQILETY 409
Cdd:cd17656 206 RDVEQLFDLVKRHNievvflpVAFLKFIFSEREFI----NRFPTCvKHII--TAGEQLViTNEFKEMLHEHN-VHLHNHY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 410 GMTEGNVATfNYTGRQGAvgraswlykHIFPFSLIrydvmtGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLG 484
Cdd:cd17656 279 GPSETHVVT-TYTINPEA---------EIPELPPI------GKPISNTWiyilDQEQQLQPqGIVGELY--ISGASVARG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 485 YAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQE--VNIYGV 562
Cdd:cd17656 341 YLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEavVLDKAD 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 563 TVPGHEGRAGMAALalrppQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:cd17656 421 DKGEKYLCAYFVME-----QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
265-556 |
3.58e-09 |
|
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: 59.38 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 343
Cdd:cd05914 90 DVALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 344 FwDDCQKHRVTVFqyIGeLCRYLV-------NQPPSKAECDHKVRLAV-----------------------------GSG 387
Cdd:cd05914 170 I-IALAFAQVTPT--LG-VPVPLViekifkmDIIPKLTLKKFKFKLAKkinnrkirklafkkvheafggnikefvigGAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 388 LRPDTwERFLRRFGpLQILETYGMTE-GNVATFNYTGRqgavgraswlykhifpfslIRYDvMTGEPIRNAQghCMTTSP 466
Cdd:cd05914 246 INPDV-EEFLRTIG-FPYTIGYGMTEtAPIISYSPPNR-------------------IRLG-SAGKVIDGVE--VRIDSP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 467 ---GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTIRW-KGENVATT 542
Cdd:cd05914 302 dpaTGEGEII--VRGPNVMKGYYKNPEATAEAFDKD-GW-----FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPE 373
|
330 340
....*....|....*....|.
gi 82581629 543 EV-------AEVLETLDFLQE 556
Cdd:cd05914 374 EIeakinnmPFVLESLVVVQE 394
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
79-619 |
6.19e-09 |
|
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: 58.80 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 79 PTHTFLIHGAQRFSYAEAERESNRIARAFLrargwtggrrgsgrgstEEGARvappagdaaargttapplaPGATVALLL 158
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLA-----------------ARGVG-------------------PERLVALAL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 159 PAGPDFLWIWFGLAKAGlrTAFVPtalrrgpllhclrscgasalvlateflesLEPDLPALRamglhlwatgpetnvagI 238
Cdd:cd17652 45 PRSAELVVAILAVLKAG--AAYLP-----------------------------LDPAYPAER-----------------I 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 239 SNLLSEAADQVdepvpgYLSAPQNIMdtclY-IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHM 316
Cdd:cd17652 77 AYMLADARPAL------LLTTPDNLA----YvIYTSGSTGRPKGVVVTHRGLANlAAAQIAAFDVGPGSRV-LQFASPSF 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 317 SGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVfqyigelcrylVNQPPS-----KAECDHKVRLAVGSGL 388
Cdd:cd17652 146 DASVWELLMALLAGATLVLAPAeelLPGEPLADLLREHRITH-----------VTLPPAalaalPPDDLPDLRTLVVAGE 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 389 RP-----DTWERFlRRFgplqiLETYGMTEgnvATFNYTGRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMT 463
Cdd:cd17652 215 ACpaelvDRWAPG-RRM-----INAYGPTE---TTVCATMAGPLPGGGV---------------PPIGRPVPGTRVYVLD 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 464 TS-----PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGE 537
Cdd:cd17652 271 ARlrpvpPGVPGELY--IAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGF 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 538 NVATTEVAEVLETLDFLQEvniygVTVPGHEGRAGMAALAL----RPPQALNLVQLYSHVSENLPPYARPRFLRLQESLA 613
Cdd:cd17652 349 RIELGEVEAALTEHPGVAE-----AVVVVRDDRPGDKRLVAyvvpAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALP 423
|
....*.
gi 82581629 614 TTETFK 619
Cdd:cd17652 424 LTPNGK 429
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
244-550 |
1.15e-08 |
|
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: 57.77 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 244 EAADQVDEPVPGyLSAPQNIMdtclyiFTSGTTGLPKAARISH----LKVLQCQGFYHLCGvHQEDVIYLA-LPLYHMSG 318
Cdd:cd05929 112 AEGGSPETPIED-EAAGWKML------YSGGTTGRPKGIKRGLpggpPDNDTLMAAALGFG-PGADSVYLSpAPLYHAAP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 319 SLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpskAECDHKVRLA-------VGSGLRPD 391
Cdd:cd05929 184 FRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLP---EAVRNAYDLSslkrvihAAAPCPPW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 392 TWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAVGRAswlykhifpfslirydVMTGEPIRNAQGH-CMTTSP 466
Cdd:cd05929 260 VKEQWIDWGGPI-IWEYYGGTEGQGLTIingeEWLTHPGSVGRA----------------VLGKVHILDEDGNeVPPGEI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 467 GEPGLLVAPvsqqsPFLgYAGAPELAKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAE 546
Cdd:cd05929 323 GEVYFANGP-----GFE-YTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIEN 390
|
....
gi 82581629 547 VLET 550
Cdd:cd05929 391 ALIA 394
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
543-619 |
1.25e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 52.16 E-value: 1.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 543 EVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFK 619
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
271-537 |
1.59e-08 |
|
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: 57.64 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 271 FTSGTTGLPKAARISH-------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKPKF---- 339
Cdd:cd12119 170 YTSGTTGNPKGVVYSHrslvlhaMAALLTDGL----GLSESDVVLPVVPMFHVNAWGLPYA-AAMVGAKLVLPGPYldpa 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 340 SASQFWDdcqKHRVTVFQ-----YIGELCRYLVNqppsKAECDHKVRLAV-GSGLRPDTWERFLRRFgpLQILETYGMTE 413
Cdd:cd12119 245 SLAELIE---REGVTFAAgvptvWQGLLDHLEAN----GRDLSSLRRVVIgGSAVPRSLIEAFEERG--VRVIHAWGMTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 gnvatfnyTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEP-------IRNAQGHCMTTSPGEPGLLVApvsqQSPFL--G 484
Cdd:cd12119 316 --------TSPLGTVARPPSEHSNLSEDEQLALRAKQGRPvpgvelrIVDDDGRELPWDGKAVGELQV----RGPWVtkS 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 82581629 485 YAGAPElakdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGE 537
Cdd:cd12119 384 YYKNDE-------ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGE 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
235-615 |
3.70e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.27 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 235 VAGISNLLSEA-ADQVDEPVPGYLSAPQNImdtCLYIFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQ-----EDVIY 308
Cdd:PRK12316 3169 AQGVQVLDLDRgDENYAEANPAIRTMPENL---AYVIYTSGSTGKPKGVGIRHSALSN-----HLCWMQQayglgVGDRV 3240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 309 LALPLYHMSGSLLGIVGCLGIGATVVLkpkfSASQFWDD-------CQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR 381
Cdd:PRK12316 3241 LQFTTFSFDVFVEELFWPLMSGARVVL----AGPEDWRDpallvelINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRI 3316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 382 LAVGSGLRPDTWERFlrrFGPLQILETYGMTEgnvatfnytgrqGAVGRASWLYKHIFPFSlirydVMTGEPIRNAQGHC 461
Cdd:PRK12316 3317 VCGGEALPADLQQQV---FAGLPLYNLYGPTE------------ATITVTHWQCVEEGKDA-----VPIGRPIANRACYI 3376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 462 MTTS-PGEPGLLVAPVSQQSPFL--GYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGEN 538
Cdd:PRK12316 3377 LDGSlEPVPVGALGELYLGGEGLarGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFR 3456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 539 VATTEVAEVLetldfLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:PRK12316 3457 IELGEIEARL-----LEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLT 3528
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
265-612 |
4.93e-08 |
|
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: 55.39 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVLqCQGFyHLCGVHQ--EDVIYL-ALPLYHMsGSLLGIVGCLGIGATVVLKPKFSA 341
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALL-AQAL-VLAVLQAidEGTVFLnSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDCQKHRVT----VFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGplqileTYGMTE-GNV 416
Cdd:cd17636 78 EEVLELIEAERCThaflLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG------GYGQTEvMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ATFNYTGRQ--GAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELA 492
Cdd:cd17636 152 ATFAALGGGaiGGAGRPS-------PLVQVR--------ILDEDGR--EVPDGEVGEIVA----RGPtvMAGYWNRPEVN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 493 KDKlLKDVFWsgdvffNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAG 572
Cdd:cd17636 211 ARR-TRGGWH------HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRW-AQSV 282
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 82581629 573 MAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESL 612
Cdd:cd17636 283 KAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADAL 322
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
138-584 |
5.07e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTApplAPGATVALLLPAGPDFLWIWFGLAKAGLRT--AFVPTALRRGPLLHcLRSCGASA---LVLATEFLesl 212
Cdd:PRK05691 54 AAALQARA---SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAvpAYPPESARRHHQER-LLSIIADAeprLLLTVADL--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 213 epdLPALRAMGLHLWATGPEtnVAGISNLLSEAADQVDEP-VPGylsapqniMDTCLYIFTSGTTGLPKAARISHL---- 287
Cdd:PRK05691 127 ---RDSLLQMEELAAANAPE--LLCVDTLDPALAEAWQEPaLQP--------DDIAFLQYTSGSTALPKGVQVSHGnlva 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 288 -KVLQCQGFYhlCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLkpkFSASQFWDDCQKHRVTVFQYIG------ 360
Cdd:PRK05691 194 nEQLIRHGFG--IDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPAYFLERPLRWLEAISEYGGtisggp 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 361 ----ELCRYLVNQPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFG-----PLQILETYGMTEgnvATFNYTGRQGAV 428
Cdd:PRK05691 269 dfayRLCSERVSESALERLDLSRWRVAY-SGsepIRQDSLERFAEKFAacgfdPDSFFASYGLAE---ATLFVSGGRRGQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 429 GRASwLYKHIFPFSLIRYDVMTGEPIRNaqghCMTTSPGEPGLLVAPVSQQ---------------SPFLGYAGAPElAK 493
Cdd:PRK05691 345 GIPA-LELDAEALARNRAEPGTGSVLMS----CGRSQPGHAVLIVDPQSLEvlgdnrvgeiwasgpSIAHGYWRNPE-AS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 494 DKLLkdVFWSGDVFFNTGDLLVCDEqGFLHFHDRTGDTIRWKGENVATTEVAEVLET-LDFLQE--VNIYGVTVPGHEGr 570
Cdd:PRK05691 419 AKTF--VEHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVRKgrVAAFAVNHQGEEG- 494
|
490 500
....*....|....*....|
gi 82581629 571 AGMAALALR------PPQAL 584
Cdd:PRK05691 495 IGIAAEISRsvqkilPPQAL 514
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
137-566 |
8.62e-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: 55.16 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 137 DAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLrscgasalvlateflESLEPDl 216
Cdd:cd05910 13 DRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCL---------------QEAEPD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 217 palramglhlwatgpetnvagisnllseaadqvdepvpGYLSAPQnIMDTCLYIFTSGTTGLPKAARISH-LKVLQCQGF 295
Cdd:cd05910 77 --------------------------------------AFIGIPK-ADEPAAILFTSGSTGTPKGVVYRHgTFAAQIDAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 296 YHLCGVHQEDVIYLALPLYHMSGSLLGIvgclgigATVV-----LKPKFSASQF-WDDCQKHRVT-------VFQYIGEL 362
Cdd:cd05910 118 RQLYGIRPGEVDLATFPLFALFGPALGL-------TSVIpdmdpTRPARADPQKlVGAIRQYGVSivfgspaLLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 363 CRYLVNQPPSkaecdhkVR--LAVGSGLRPDTWERFLRRFGP-LQILETYGMTE-------GNVATFNYTGRQGAVGRAS 432
Cdd:cd05910 191 CAQHGITLPS-------LRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvssiGSRELLATTTAATSGGAGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 433 WLyKHIFPFSLIRYDVMTGEPIRNAQG-HCMttSPGEPGLLVAPVSQQSP-FLGYAGAPELAKDKLLKDVFWSgdvffNT 510
Cdd:cd05910 264 CV-GRPIPGVRVRIIEIDDEPIAEWDDtLEL--PRGEIGEITVTGPTVTPtYVNRPVATALAKIDDNSEGFWH-----RM 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 82581629 511 GDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPG 566
Cdd:cd05910 336 GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
150-548 |
1.18e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 54.90 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAG-----LRTAFVPTALR-RgpllhcLRSCGASALVLATEFLESL-EPDLPALRAM 222
Cdd:PRK04319 97 KGDRVFIFMPRIPELYFALLGALKNGaivgpLFEAFMEEAVRdR------LEDSEAKVLITTPALLERKpADDLPSLKHV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 223 GLHLWATGPETNVAGISNLLSEAADQVD-EPVpgylsAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ--CQGFYHLc 299
Cdd:PRK04319 171 LLVGEDVEEGPGTLDFNALMEQASDEFDiEWT-----DRE---DGAILHYTSGSTGKPKGVLHVHNAMLQhyQTGKYVL- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 300 GVHQEDVIY-LALPLYhMSGSLLGIVGCLGIGAT-VVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAEC- 376
Cdd:PRK04319 242 DLHEDDVYWcTADPGW-VTGTSYGIFAPWLNGATnVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKy 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 377 DHK-VR--LAVGSGLRPD--TWERflRRFGpLQILETYGMTE-GNVATFNYTG---RQGAVGRaswlykhifPFSLIRYD 447
Cdd:PRK04319 321 DLSsLRhiLSVGEPLNPEvvRWGM--KVFG-LPIHDNWWMTEtGGIMIANYPAmdiKPGSMGK---------PLPGIEAA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 448 VMTgepiRNAQGhcmtTSPGEPGLLVAPVSQQSPFLGYAGAPElakdkLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDR 527
Cdd:PRK04319 389 IVD----DQGNE----LPPNRMGNLAIKKGWPSMMRGIWNNPE-----KYESYFAGD--WYVSGDSAYMDEDGYFWFQGR 453
|
410 420
....*....|....*....|.
gi 82581629 528 TGDTIRWKGENVATTEVAEVL 548
Cdd:PRK04319 454 VDDVIKTSGERVGPFEVESKL 474
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
135-417 |
2.79e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.46 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 135 AGDAAARGTTapplaPGATVALLlpAGPDFLW------IWfgLAKAGLRTAFVPTalRRGPL-------LHCLRSCGASA 201
Cdd:PRK07768 43 AGGLAAAGVG-----PGDAVAVL--AGAPVEIaptaqgLW--MRGASLTMLHQPT--PRTDLavwaedtLRVIGMIGAKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 202 LVLATEFLESLepdlPALRAMGLhlwatgpetNVAGISNLLseAADQVDEPVPGylsapQNimDTCLYIFTSGTTGLPKA 281
Cdd:PRK07768 112 VVVGEPFLAAA----PVLEEKGI---------RVLTVADLL--AADPIDPVETG-----ED--DLALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 282 ARISHLKVLQC-QGFYHLCGVHQE-DVIYLALPLYH-MsgsllGIVGCLGI----GATVVlkpKFSASQFWDD------- 347
Cdd:PRK07768 170 VQITHGNLYANaEAMFVAAEFDVEtDVMVSWLPLFHdM-----GMVGFLTVpmyfGAELV---KVTPMDFLRDpllwael 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 348 CQKHRVTV-----FQYiGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLR---RFG--PLQILETYGMTEGN 415
Cdd:PRK07768 242 ISKYRGTMtaapnFAY-ALLARRLRRQAKPGAFDLSSLRFALngAEPIDPADVEDLLDagaRFGlrPEAILPAYGMAEAT 320
|
..
gi 82581629 416 VA 417
Cdd:PRK07768 321 LA 322
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
138-417 |
3.30e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.47 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 138 AAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTA--FVPTAL--RRG---PLLHCLRSCGASALVLATEFLE 210
Cdd:PRK09192 61 AGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplPLPMGFggRESyiaQLRGMLASAQPAAIITPDELLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 211 SLEPDLPALRAmglhLWATGPETnvagiSNLLSEAADQVDEPVPGylsapqnimDTCLYIFTSGTTGLPKAARISHLKVL 290
Cdd:PRK09192 141 WVNEATHGNPL----LHVLSHAW-----FKALPEADVALPRPTPD---------DIAYLQYSSGSTRFPRGVIITHRALM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 291 qcqgfyHLCGVHQEDVIYLA--------LPLYH-MsgsllGIVGCLgigatvvLKPkfSASQF----------------W 345
Cdd:PRK09192 203 ------ANLRAISHDGLKVRpgdrcvswLPFYHdM-----GLVGFL-------LTP--VATQLsvdylptrdfarrplqW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 346 -DDCQKHRVTV-----FQYigELCRYLVNQpPSKAECDHKVRLAVGSG---LRPDTWERFLRRFGPL-----QILETYGM 411
Cdd:PRK09192 263 lDLISRNRGTIsysppFGY--ELCARRVNS-KDLAELDLSCWRVAGIGadmIRPDVLHQFAEAFAPAgfddkAFMPSYGL 339
|
....*.
gi 82581629 412 TEGNVA 417
Cdd:PRK09192 340 AEATLA 345
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
191-413 |
6.23e-07 |
|
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: 52.47 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 191 LHCLRSCGASALVLATEFLES----LEPDLPALRAmgLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNImdt 266
Cdd:cd17654 46 LRCDRGTESPVAILAILFLGAayapIDPASPEQRS--LTVMKKCHVSYLLQNKELDNAPLSFTPEHRHFNIRTDECL--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 267 CLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVLKP---KFSAS 342
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPnIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPtsvKVLPS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 343 QFWD-DCQKHRVTVFQyigeLCRYLVNQPPSKAECDHKVR-------LAVGSGLRP-DTWERFLRRFGP-LQILETYGMT 412
Cdd:cd17654 200 KLADiLFKRHRITVLQ----ATPTLFRRFGSQSIKSTVLSatsslrvLALGGEPFPsLVILSSWRGKGNrTRIFNIYGIT 275
|
.
gi 82581629 413 E 413
Cdd:cd17654 276 E 276
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
197-338 |
6.69e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 52.18 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 197 CGASALVLATEFLESLEPDLpaLRAMGL-HLWATGPETNVAGISNLLSEaadqvdePVPGYLSAPQNIMDTCLYIFTSGT 275
Cdd:PRK09029 76 CGARVLPLNPQLPQPLLEEL--LPSLTLdFALVLEGENTFSALTSLHLQ-------LVEGAHAVAWQPQRLATMTLTSGS 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82581629 276 TGLPKAArishlkVLQCQGfyHLC---GV------HQEDVIYLALPLYHMSGslLGIV-GCLGIGATVVLKPK 338
Cdd:PRK09029 147 TGLPKAA------VHTAQA--HLAsaeGVlslmpfTAQDSWLLSLPLFHVSG--QGIVwRWLYAGATLVVRDK 209
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
265-625 |
1.18e-06 |
|
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: 51.41 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLK--VLQCQGFYHLcGVHQEDViylalplyHMSGSLLG--------IVGCLGIGATVV 334
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDV--------HWNISSPGwakhawscFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 335 L--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYG 410
Cdd:cd05974 157 LfnYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF--DVKLREVVGAGepLNPEVIEQVRRAWG-LTIRDGYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 411 MTEGNVATFNYTG---RQGAVGRAswlykhifpfsLIRYDVMTGEPIrnaqghcmtTSPGEPGLLVAPVSQQSP---FLG 484
Cdd:cd05974 234 QTETTALVGNSPGqpvKAGSMGRP-----------LPGYRVALLDPD---------GAPATEGEVALDLGDTRPvglMKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 485 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIygVTV 564
Cdd:cd05974 294 YAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPS 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82581629 565 PGHEGRAGMAALAL-----RPPQALNLVqLYSHVSENLPPYARPRFLRLQEsLATTETFKQQKVRM 625
Cdd:cd05974 365 PDPVRLSVPKAFIVlragyEPSPETALE-IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVEL 428
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
268-615 |
3.56e-06 |
|
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: 50.25 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYI-FTSGTTGLPKAarishlkVLQCQGFYhLCGV----------HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL- 335
Cdd:cd05966 234 LFIlYTSGSTGKPKG-------VVHTTGGY-LLYAattfkyvfdyHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMf 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 336 --KPKF-SASQFWDDCQKHRVTVFqY-----IGELCRYlVNQPPSKaeCDHK-VRL--AVGSGLRPDTWERFLRRFGP-- 402
Cdd:cd05966 306 egTPTYpDPGRYWDIVEKHKVTIF-YtaptaIRALMKF-GDEWVKK--HDLSsLRVlgSVGEPINPEAWMWYYEVIGKer 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 403 LQILETYGMTEgnvatfnyTG------RQGAV----GRASwlykhiFPFSLIRYDVM--TGEPIRNAQGhcmttspgepG 470
Cdd:cd05966 382 CPIVDTWWQTE--------TGgimitpLPGATplkpGSAT------RPFFGIEPAILdeEGNEVEGEVE----------G 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 471 LLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVL 548
Cdd:cd05966 438 YLVIKRPWPGMARTIYGDHE-----RYEDTYFSkfPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82581629 549 ETLDFLQEVNIYGVTvpgHE--GRAGMAALALRP--PQALNLVQ-LYSHVSENLPPYARPRFLRLQESLATT 615
Cdd:cd05966 512 VAHPAVAEAAVVGRP---HDikGEAIYAFVTLKDgeEPSDELRKeLRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
135-621 |
5.65e-06 |
|
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: 49.38 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 135 AGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESL-- 212
Cdd:cd17632 77 VGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAve 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 213 ----------------EPDLPALRAmGLHLwATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDT-CLYIFTSGT 275
Cdd:cd17632 157 avleggtpprlvvfdhRPEVDAHRA-ALES-ARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPlALLIYTSGS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 276 TGLPKAARISHLKVLQC-QGFYHLCGVHQEDVIYLA-LPLYHMSGSLLgIVGCLGIGATVVLKPKFSASQFWDDCQKHRV 353
Cdd:cd17632 235 TGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLFDDLALVRP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 354 T-----------VFQ-YIGELCRYLVN-------QPPSKAECDHKV---RLA---VGSGLRPDTWERFLRRFGPLQILET 408
Cdd:cd17632 314 TelflvprvcdmLFQrYQAELDRRSVAgadaetlAERVKAELRERVlggRLLaavCGSAPLSAEMKAFMESLLDLDLHDG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 409 YGMTEGNVATFNytgrqGAVGRASWL-YKHIfpfsliryDVmtgePirnAQGHCMTTSPGEPGLLVapVSQQSPFLGYAG 487
Cdd:cd17632 394 YGSTEAGAVILD-----GVIVRPPVLdYKLV--------DV----P---ELGYFRTDRPHPRGELL--VKTDTLFPGYYK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 488 APELAkdkllKDVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRW-KGENVATTEVAEVLETLDFLQEVNIYG----- 561
Cdd:cd17632 452 RPEVT-----AEVF-DEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGnsera 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82581629 562 ----VTVPGHEGRAGMAALALRPPQALNLVQLYShvSENLPPYARPRflrlqESLATTETFKQQ 621
Cdd:cd17632 526 yllaVVVPTQDALAGEDTARLRAALAESLQRIAR--EAGLQSYEIPR-----DFLIETEPFTIA 582
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
154-561 |
5.86e-06 |
|
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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 49.35 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 154 VALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALramglhlwatgpet 233
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGEL-------------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 234 nvagiSNLLSEAADQVD-EPVPGYLSA------PQNIMDTCLYI---FTSGTTGLPKAARISHlkvlqcQGFY---HLCG 300
Cdd:cd05915 118 -----KTVQHFVVMDEKaPEGYLAYEEalgeeaDPVRVPERAACgmaYTTGTTGLPKGVVYSH------RALVlhsLAAS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 301 VHQEDV-----IYL-ALPLYHMSG-SLLGIVGCLGiGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS- 372
Cdd:cd05915 187 LVDGTAlsekdVVLpVVPMFHVNAwCLPYAATLVG-AKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESt 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 373 KAECDHKVRLAVGSGLRPDTWERfLRRFGPLQILETYGMTEgnvatfnytgrQGAVGRAS-WL--YKHIFPFSLIRYDVM 449
Cdd:cd05915 266 GHRLKTLRRLVVGGSAAPRSLIA-RFERMGVEVRQGYGLTE-----------TSPVVVQNfVKshLESLSEEEKLTLKAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 450 TG-----EPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYagapelAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHF 524
Cdd:cd05915 334 TGlpiplVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGY------YGNEEATRSALTPDGFFRTGDIAVWDEEGYVEI 407
|
410 420 430
....*....|....*....|....*....|....*..
gi 82581629 525 HDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYG 561
Cdd:cd05915 408 KDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
265-561 |
6.15e-06 |
|
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: 49.14 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYH----LCGVHQEDVIYLALPLYHMSGSLLgIVGCLGIGATV------ 333
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHGNIVsNVAGVFKileiLNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIgfysgd 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 334 ---------VLKPKFSAS------QFWDDCQKHRV-------TVFQYIGELCRYLVNQPPSKAE------CDHKVRLAVG 385
Cdd:cd05927 194 irlllddikALKPTVFPGvprvlnRIYDKIFNKVQakgplkrKLFNFALNYKLAELRSGVVRASpfwdklVFNKIKQALG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 386 SGLR----------PDTwERFLRR-FGpLQILETYGMTEGNVATFnyTGRQGavgraSWLYKHI---FPFSLIR------ 445
Cdd:cd05927 274 GNVRlmltgsaplsPEV-LEFLRVaLG-CPVLEGYGQTECTAGAT--LTLPG-----DTSVGHVggpLPCAEVKlvdvpe 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 446 --YDVMTGEP-----IRnaqGHCMttspgepgllvapvsqqspFLGYAGAPELAKDKLlkdvfwsgdvffntgdllvcDE 518
Cdd:cd05927 345 mnYDAKDPNPrgevcIR---GPNV-------------------FSGYYKDPEKTAEAL--------------------DE 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82581629 519 QGFLHfhdrTGDTIRW-------------------KGENVAttevAEVLETL----DFLQEVNIYG 561
Cdd:cd05927 383 DGWLH----TGDIGEWlpngtlkiidrkknifklsQGEYVA----PEKIENIyarsPFVAQIFVYG 440
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
392-604 |
6.69e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.22 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 392 TWERFLR--RFGPLQILETYGMTE--GNVATfnytgrqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQghcMTTSPG 467
Cdd:PRK07445 242 AWPSLLEqaRQLQLRLAPTYGMTEtaSQIAT-------------------LKPDDFLAGNNSSGQVLPHAQ---ITIPAN 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 468 EPGLLVapVSQQSPFLGYAgaPElakdkllkdvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEV 547
Cdd:PRK07445 300 QTGNIT--IQAQSLALGYY--PQ----------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 82581629 548 LETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQaLNLVQLYSHVSENLPPYARPR 604
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDP-HWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPK 420
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
268-539 |
9.51e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.97 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYI-FTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLalpLYHMS-GSL---LGIVGCLGIGATVVL------K 336
Cdd:PTZ00237 257 LYIlYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVV---FSHSSiGWVsfhGFLYGSLSLGNTFVMfeggiiK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 337 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP------SKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYG 410
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPeatiirSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 411 MTEGNVATFnytgrqgavgrasWLYKHI--------FPFSLIRYDVMTGEPIR---NAQGHCMTTSPGEPGLlvapvsqq 479
Cdd:PTZ00237 414 QTEIGITYL-------------YCYGHInipynatgVPSIFIKPSILSEDGKElnvNEIGEVAFKLPMPPSF-------- 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82581629 480 spflgyagAPELAK-DKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENV 539
Cdd:PTZ00237 473 --------ATTFYKnDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKV 525
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
271-546 |
1.81e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.86 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 271 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIyLALPLYH-----------MSGSLLGIVG-------CLG 328
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHrslyLQSLSLRTTDSLAVTHGESFL-CCVPIYHvlswgvplaafMSGTPLVFPGpdlsaptLAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 329 IGATVVLKPKFSASQFWddcqkhrvtvfqyIGELCRYLVNqPPSKAECdhKVRLAVGSGLRP---DTWERflrRFGpLQI 405
Cdd:PRK05620 267 IIATAMPRVAHGVPTLW-------------IQLMVHYLKN-PPERMSL--QEIYVGGSAVPPiliKAWEE---RYG-VDV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 406 LETYGMTE----GNVATfnytGRQGAVGRASWLYKHI---FPFSLiRYDVMTgepirnaQGHCMTTS---PGE---PGLL 472
Cdd:PRK05620 327 VHVWGMTEtspvGTVAR----PPSGVSGEARWAYRVSqgrFPASL-EYRIVN-------DGQVMESTdrnEGEiqvRGNW 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 473 VAPVSQQSPFLGYAGAPELAKDKLLKDVF--WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKG--------EN--VA 540
Cdd:PRK05620 395 VTASYYHSPTEEGGGAASTFRGEDVEDANdrFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGewiysaqlENyiMA 474
|
....*.
gi 82581629 541 TTEVAE 546
Cdd:PRK05620 475 APEVVE 480
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
189-413 |
2.87e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.40 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 189 PLLHCLRSCGASALVLATEFLESLEPDLPAlramglhlwATGPEtnVAGISNLLSEAADQVDEPVPgylSAPQNIMDTCl 268
Cdd:PLN02736 163 TLLSCLSEIPSVRLIVVVGGADEPLPSLPS---------GTGVE--IVTYSKLLAQGRSSPQPFRP---PKPEDVATIC- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 269 yiFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATV------VLKpkfsa 341
Cdd:PLN02736 228 --YTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDVHISYLPLAHIY-ERVNQIVMLHYGVAVgfyqgdNLK----- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 sqFWDDCQKHRVTVF------------------QYIGELCRYLVN-------------QPPS-----------KAECDHK 379
Cdd:PLN02736 300 --LMDDLAALRPTIFcsvprlynriydgitnavKESGGLKERLFNaaynakkqalengKNPSpmwdrlvfnkiKAKLGGR 377
|
250 260 270
....*....|....*....|....*....|....*...
gi 82581629 380 VRLaVGSG---LRPDTWErFLRR-FGPlQILETYGMTE 413
Cdd:PLN02736 378 VRF-MSSGaspLSPDVME-FLRIcFGG-RVLEGYGMTE 412
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
500-603 |
4.31e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 46.57 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 500 VFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYgvtvPGHEGRAG-MAALAL 578
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGeRVKAKV 360
|
90 100
....*....|....*....|....*
gi 82581629 579 RPPQALNLVQLYSHVSENLPPYARP 603
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVP 385
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
268-604 |
4.63e-05 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 46.54 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYI-FTSGTTGLPKAarishlkVLQCQGFY---------HLCGVHQEDVIYlalplyhmSGSLLGIV--------GCLGI 329
Cdd:cd05967 233 LYIlYTSGTTGKPKG-------VVRDNGGHavalnwsmrNIYGIKPGDVWW--------AASDVGWVvghsyivyGPLLH 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 330 GATVVL---KPKFS--ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE---CD---HKVRLAVGSGLRPDTWErFLR 398
Cdd:cd05967 298 GATTVLyegKPVGTpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkYDlssLRTLFLAGERLDPPTLE-WAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 399 RFGPLQILETYGMTE-GNVATFNYTG------RQGAVGRaswlykhifpfSLIRYDVM----TGEPIR-NAQGHCMTTSP 466
Cdd:cd05967 377 NTLGVPVIDHWWQTEtGWPITANPVGleplpiKAGSPGK-----------PVPGYQVQvldeDGEPVGpNELGNIVIKLP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 467 GEPGLLvapvsqqspflgyagaPELAK-DKLLKDVFWSGDV-FFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEV 544
Cdd:cd05967 446 LPPGCL----------------LTLWKnDERFKKLYLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 545 AEVLETLDFLQEVNIYGVtvpgHEGRAGMAALAL--------RPPQALnLVQLYSHVSENLPPYARPR 604
Cdd:cd05967 510 EESVLSHPAVAECAVVGV----RDELKGQVPLGLvvlkegvkITAEEL-EKELVALVREQIGPVAAFR 572
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
70-413 |
6.38e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 70 RLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFlrargwtggrrgsgrgsteegarvappagdaAARGttappLA 149
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQTLSYAELDARANRLARAL-------------------------------RERG-----VG 2236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 150 PGATVALLLPAGPDFLWIWFGLAKAGlrTAFVPT----ALRRgplLHCLRSCGASALVLATEFLESLEPDLPAlramGLH 225
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAG--GAYVPLdpeyPLER---LHYMIEDSGIGLLLSDRALFEALGELPA----GVA 2307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 226 LWATgpETNVAGIsnllseaADQVDEPVPgYLSAPQNimdTCLYIFTSGTTGLPKAARISHLKV-LQCQGFYHLCGVHQE 304
Cdd:PRK05691 2308 RWCL--EDDAAAL-------AAYSDAPLP-FLSLPQH---QAYLIYTSGSTGKPKGVVVSHGEIaMHCQAVIERFGMRAD 2374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 305 DViylALPLYHM-----SGSLLGIVGClgiGATVVLKpkfsASQFWDD---CQ---KHRVTVF----QYIGELCRYLVNQ 369
Cdd:PRK05691 2375 DC---ELHFYSInfdaaSERLLVPLLC---GARVVLR----AQGQWGAeeiCQlirEQQVSILgftpSYGSQLAQWLAGQ 2444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 82581629 370 PPSKAecdhkVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTE 413
Cdd:PRK05691 2445 GEQLP-----VRMCItgGEALTGEHLQRIRQAFAPQLFFNAYGPTE 2485
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
89-293 |
7.24e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 89 QRFSYAEAERESNRIARAFLrargwtggrrgsgrgsteegarvappagdAAARGTTAPplapgatVALLLPAGPDFLWIW 168
Cdd:PRK05691 3744 QQWSYAELNRAANRLGHALR-----------------------------AAGVGVDQP-------VALLAERGLDLLGMI 3787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 169 FGLAKAGlrTAFVP-------------TALRRGPLLHCLRSCGASALVLATEFLESLEPDlpalramgLHLWATGPETNV 235
Cdd:PRK05691 3788 VGSFKAG--AGYLPldpglpaqrlqriIELSRTPVLVCSAACREQARALLDELGCANRPR--------LLVWEEVQAGEV 3857
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 236 AgisnllseaadqvdEPVPGYLSAPQNImdtCLYIFTSGTTGLPKAARISHLKVLQCQ 293
Cdd:PRK05691 3858 A--------------SHNPGIYSGPDNL---AYVIYTSGSTGLPKGVMVEQRGMLNNQ 3898
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
265-413 |
2.42e-04 |
|
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: 44.13 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 265 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYH-LCGVHQEDVIYLA-LPLYH-----------MSGSLLG-------- 322
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDrVPELLGPDDRYLAyLPLAHifelaaenvclYRGGTIGygsprtlt 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 323 ---IVGCLgiGATVVLKPKFSAS--QFWDDCQK-----------HRVTVFQYIGELCRYLVNQPPSKAECD----HKVRL 382
Cdd:cd17639 169 dksKRGCK--GDLTEFKPTLMVGvpAIWDTIRKgvlaklnpmggLKRTLFWTAYQSKLKALKEGPGTPLLDelvfKKVRA 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 82581629 383 AVGSGLR----------PDTwERFLRRF-GPlqILETYGMTE 413
Cdd:cd17639 247 ALGGRLRymlsggaplsADT-QEFLNIVlCP--VIQGYGLTE 285
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
268-356 |
2.62e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.02 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 268 LYI-FTSGTTGLPKA-------ARISHLKVLQCQgfyhlCGVHQEDVI-YLALPLYHMSGSLlgiVGCLGIGATVVL--- 335
Cdd:PRK03584 266 LWIlYSSGTTGLPKCivhghggILLEHLKELGLH-----CDLGPGDRFfWYTTCGWMMWNWL---VSGLLVGATLVLydg 337
|
90 100
....*....|....*....|....
gi 82581629 336 ---KPKFSAsqFWDDCQKHRVTVF 356
Cdd:PRK03584 338 spfYPDPNV--LWDLAAEEGVTVF 359
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
234-356 |
4.60e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); 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. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 43.41 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 234 NVAGISNLLSEAADQVDEPVPGYLSAPqnimdtcLYI-FTSGTTGLPKA-------ARISHLKVLQCQgfyhlCGVHQED 305
Cdd:cd05943 225 KALTLEDFLATGAAGELEFEPLPFDHP-------LYIlYSSGTTGLPKCivhgaggTLLQHLKEHILH-----CDLRPGD 292
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 306 VI-YLALPLYHMSGSLlgiVGCLGIGATVVL------KPKFSAsqFWDDCQKHRVTVF 356
Cdd:cd05943 293 RLfYYTTCGWMMWNWL---VSGLAVGATIVLydgspfYPDTNA--LWDLADEEGITVF 345
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
262-333 |
6.65e-04 |
|
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: 42.73 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 262 NIMDT------CLYIFTSGTTGLPKAARISHLKVL-----QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIG 330
Cdd:cd05933 142 AIISSqkpnqcCTLIYTSGTTGMPKGVMLSHDNITwtakaASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVG 221
|
...
gi 82581629 331 ATV 333
Cdd:cd05933 222 GQV 224
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
129-603 |
7.79e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 129 ARVAPPAGDAAARGTTapplaPGATVALLLPAGPDFLWIWFGLAKAG-----LRTAFVPTALRRgpllhCLRScGASALV 203
Cdd:PRK10252 491 EQVVALANLLRERGVK-----PGDSVAVALPRSVFLTLALHAIVEAGaawlpLDTGYPDDRLKM-----MLED-ARPSLL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 204 LATEFLESLEPDLPalramglhlwatgpetnvaGISNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAAR 283
Cdd:PRK10252 560 ITTADQLPRFADVP-------------------DLTSLCYNAPLAPQGAAPLQLSQPH---HTAYIIFTSGSTGRPKGVM 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 284 ISHL----KVLQCQGFYhlcGVHQEDVIY-------------LALPLyhMSGSLLgivgclgigatVVLKPK-----FSA 341
Cdd:PRK10252 618 VGQTaivnRLLWMQNHY---PLTADDVVLqktpcsfdvsvweFFWPF--IAGAKL-----------VMAEPEahrdpLAM 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 342 SQFWDDcqkHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLA----VGSGLRPDTWERFLRRFG-PLQILetYGMTEGNV 416
Cdd:PRK10252 682 QQFFAE---YGVTTTHFVPSMLAAFVASLTPEGARQSCASLRqvfcSGEALPADLCREWQQLTGaPLHNL--YGPTEAAV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 417 ----------ATFNYTGRQGAVGRASWlykhifpfslirydvMTGEPIRNAQGHcmTTSPGEPGLLVAPVSQQSPflGYA 486
Cdd:PRK10252 757 dvswypafgeELAAVRGSSVPIGYPVW---------------NTGLRILDARMR--PVPPGVAGDLYLTGIQLAQ--GYL 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 487 GAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPG 566
Cdd:PRK10252 818 GRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQ 897
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 82581629 567 HEGRAG-----MAALALRPPQALNLVQLYSHVSENLPPYARP 603
Cdd:PRK10252 898 AAATGGdarqlVGYLVSQSGLPLDTSALQAQLRERLPPHMVP 939
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
270-417 |
2.29e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 270 IFTSGTTGLPKAARISHLKVLQ-----CQGFyhlcGVhQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqf 344
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSftnwmLEDF----AL-PEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK------ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 345 wddcqkhrvTVFQYIGELCRYLVNQP-------PSKAE-C--------DHKVRLAV----GSGLRPDTWERFLRRFGPLQ 404
Cdd:PRK04813 218 ---------DMTANFKQLFETLPQLPinvwvstPSFADmClldpsfneEHLPNLTHflfcGEELPHKTAKKLLERFPSAT 288
|
170
....*....|...
gi 82581629 405 ILETYGMTEGNVA 417
Cdd:PRK04813 289 IYNTYGPTEATVA 301
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
271-544 |
6.66e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 39.73 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 271 FTSGTTGLPKAARISH----LKVLQCQGFYHLcGVHQEDVIYLALPLYHMSGslLGIV-GCLGIGATVVLK-PKFSASQF 344
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHrsnvLHALMANNGDAL-GTSAADTMLPVVPLFHANS--WGIAfSAPSMGTKLVMPgAKLDGASV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 345 WDDCQKHRV-------TVFQYigeLCRYLvnqPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE---- 413
Cdd:PRK06018 261 YELLDTEKVtftagvpTVWLM---LLQYM---EKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMG-VEVRHAWGMTEmspl 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82581629 414 GNVATFNyTGRQGAVG--RASWLYKHIFPFSLIRYDVMTGEPIR-----NAQGHCMTTSPGepgllvapvsqqspflgYA 486
Cdd:PRK06018 334 GTLAALK-PPFSKLPGdaRLDVLQKQGYPPFGVEMKITDDAGKElpwdgKTFGRLKVRGPA-----------------VA 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 82581629 487 GAPELAKDKLLKDvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEV 544
Cdd:PRK06018 396 AAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDL 448
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
258-299 |
9.95e-03 |
|
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: 39.06 E-value: 9.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 82581629 258 SAPQNIMdtclY-IFTSGTTGLPKAARISHLKVlqCQGFYHLC 299
Cdd:cd05918 103 SSPSDAA----YvIFTSGSTGKPKGVVIEHRAL--STSALAHG 139
|
|
| |
