|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-673 |
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: 985.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 87 GSRRFSYSEAERESNRAARAFLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggdgaargggaaapLSP 166
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAG---------------------------------------------------LRP 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAG 246
Cdd:cd05938 31 GDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQEAVEEVLPALRADGVSVWYLS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 247 PGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLA 326
Cdd:cd05938 111 HTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYIT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 327 LPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRP 406
Cdd:cd05938 191 LPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 407 DTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPG 486
Cdd:cd05938 271 DVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 487 LLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEA 566
Cdd:cd05938 351 LLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 567 LDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGF 646
Cdd:cd05938 431 LDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGF 510
|
570 580
....*....|....*....|....*..
gi 1393643644 647 DPSTLSDPLYVLDQAVGAYLPLTTARY 673
Cdd:cd05938 511 NPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
60-682 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 633.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 60 GPEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARaFLRALGwdwgpdggdsgegsagegeraapgagd 139
Cdd:PRK08279 32 TPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAH-WAAARG--------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 140 aaagsgaefaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALV 219
Cdd:PRK08279 84 ------------------------VGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 220 LAPEFLESLEpDLPALRAMGLHLWAAGPGT--HPAGISDLlAEVSAEVDGPVPgylSSPQSIT--DTCLYIFTSGTTGLP 295
Cdd:PRK08279 140 VGEELVEAFE-EARADLARPPRLWVAGGDTldDPEGYEDL-AAAAAGAPTTNP---ASRSGVTakDTAFYIYTSGTTGLP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 296 KAARISHLKILQC-QGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQY 374
Cdd:PRK08279 215 KAAVMSHMRWLKAmGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 375 IGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGR-ASWLYKh 453
Cdd:PRK08279 295 IGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRvPLWLAH- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 454 ifPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVSQQSPFLGYAGgPELAQGKLLKDVFRPGDVFFNTGDLLVCD 533
Cdd:PRK08279 374 --PYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 534 DQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENL 613
Cdd:PRK08279 451 GFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERL 530
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393643644 614 PPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARYSALLAGNLR 682
Cdd:PRK08279 531 PAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFR 599
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
164-648 |
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: 566.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLapefleslepdlpalramglhlw 243
Cdd:cd05940 25 LKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV----------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aagpgthpagisdllaevsaevdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQ-LCGVHQEDV 322
Cdd:cd05940 82 -------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAgSGGALPSDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGS 402
Cdd:cd05940 125 LYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 403 GLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSP 482
Cdd:cd05940 205 GLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 483 GEPGLLVAPVSQQSPFLGYAGGPElAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAE 562
Cdd:cd05940 285 GEPGLLISRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 563 VFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMA 642
Cdd:cd05940 364 VLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
....*.
gi 1393643644 643 NEGFDP 648
Cdd:cd05940 444 NEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
167-648 |
2.41e-165 |
|
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: 483.08 E-value: 2.41e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLapEFLESLEPDLPalramglhlwaag 246
Cdd:cd05939 28 GDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF--NLLDPLLTQSS------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 247 pgTHPAGISDLlaevsaevdgpvpgylsspqSITDTCLYIFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIYL 325
Cdd:cd05939 93 --TEPPSQDDV--------------------NFRDKLFYIYTSGTTGLPKAAVIVHSRYYRiAAGAYYAFGMRPEDVVYD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 326 ALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLR 405
Cdd:cd05939 151 CLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 406 PDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEP 485
Cdd:cd05939 231 PQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 486 GLLVAPVSQQSP---FLGYAGGPELAQgKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAE 562
Cdd:cd05939 311 GLLVGKIIQNDPlrrFDGYVNEGATNK-KIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 563 VFEALDFLQEVNVYGVTVPGHEGRAGMAALVlRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMA 642
Cdd:cd05939 390 ILSNVLGLEDVVVYGVEVPGVEGRAGMAAIV-DPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
....*.
gi 1393643644 643 NEGFDP 648
Cdd:cd05939 469 KEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
166-648 |
3.89e-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: 402.58 E-value: 3.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEfleslepdlpalramglhlwaa 245
Cdd:cd05937 30 AGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDPD---------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 246 gpgthpagisdllaevsaevdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIY 324
Cdd:cd05937 88 -----------------------------------DPAILIYTSGTTGLPKAAAISWRRTLVtSNLLSHDLNLKNGDRTY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 325 LALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGL 404
Cdd:cd05937 133 TCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 405 RPDTWERFVRRFGPLQVLETYGLTEGNVATINY-TGQ--RGAVGRASWLYKHIF--PFSLIRYDVTTGEPIRDPQ-GHCM 478
Cdd:cd05937 213 RPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGDfgAGAIGHHGLIRRWKFenQVVLVKMDPETDDPIRDPKtGFCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 479 ATSPGEPGLLVA--PVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVA 556
Cdd:cd05937 293 RAPVGEPGEMLGrvPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 557 TTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLR----PPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTE 632
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEessaVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTD 452
|
490
....*....|....*.
gi 1393643644 633 TFKQQKVRMANEGFDP 648
Cdd:cd05937 453 NHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
67-644 |
1.96e-81 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 265.52 E-value: 1.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 67 LAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsga 146
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAA-LRALG---------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 147 efaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVlapefle 226
Cdd:COG0318 46 -----------------VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 227 slepdlpalramglhlwaagpgthpagisdllaevsaevdgpvpgylsspqsitdTCLYIFTSGTTGLPKAARISHLKIL 306
Cdd:COG0318 102 -------------------------------------------------------TALILYTSGTTGRPKGVMLTHRNLL 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 307 -QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQ 385
Cdd:COG0318 127 aNAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRH 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 386 PPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPlQVLETYGLTEGN-VATINYTGQR----GAVGRAswlykhiFPFS 458
Cdd:COG0318 207 PEFARYDLSSLRLVVsgGAPLPPELLERFEERFGV-RIVEGYGLTETSpVVTVNPEDPGerrpGSVGRP-------LPGV 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 459 LIRydvttgepIRDPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPElaqgkLLKDVFRPGdvFFNTGDLLVCDDQGFL 538
Cdd:COG0318 279 EVR--------IVDEDGRELP--PGEVGEIV--VRGPNVMKGYWNDPE-----ATAEAFRDG--WLRTGDLGRLDEDGYL 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 539 RFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENLPPYAR 618
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
570 580
....*....|....*....|....*.
gi 1393643644 619 PRFLRLQESLATTETFKQQKVRMANE 644
Cdd:COG0318 419 PRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
89-638 |
1.13e-80 |
|
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: 262.23 E-value: 1.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 89 RRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggdgaargggaaapLSPGA 168
Cdd:cd05934 2 RRWTYAELLRESARIAAA-LAALG---------------------------------------------------IRPGD 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 169 TVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVlapefleslepdlpalramglhlwaagpg 248
Cdd:cd05934 30 RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV----------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 249 thpagisdllaevsaevdgpvpgylsspqsiTDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLAL 327
Cdd:cd05934 81 -------------------------------VDPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFGLGEDDVYLTVL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 328 PLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPD 407
Cdd:cd05934 130 PLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPE 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 408 TWERFVRRFGpLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKHifpfslirYDVTtgepIRDPQGHCMATspGEPG- 486
Cdd:cd05934 210 LHEEFEERFG-VRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPG--------YEVR----IVDDDGQELPA--GEPGe 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 487 LLVAPVSQQSPFLGYAGGPElaqgKLLKdVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEA 566
Cdd:cd05934 275 LVIRGLRGWGFFKGYYNMPE----ATAE-AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 567 LDFLQEVNVYGvtVPGHEG-RAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd05934 348 HPAVREAAVVA--VPDEVGeDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
281-635 |
8.49e-66 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 220.23 E-value: 8.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGsLLGIVGCMGIGATVVLKSKFSAGQ 359
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 FWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPlQVLETYGLTEGNVATINY 437
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsgGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 438 TG-----QRGAVGRAswlykhiFPFSLIRydvttgepIRDPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAQgkl 512
Cdd:cd04433 159 PPdddarKPGSVGRP-------VPGVEVR--------IVDPDGGELP--PGEIGELV--VRGPSVMKGYWNNPEATA--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 513 lkDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAAL 592
Cdd:cd04433 217 --AVDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1393643644 593 VLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd04433 292 VLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
71-650 |
7.75e-63 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 218.47 E-value: 7.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHT----FLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsga 146
Cdd:PRK06155 23 LPAMLARQAERYpdrpLLVFGGTRWTYAEAARAAAAAAHA-LAAAG---------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 147 efaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLE 226
Cdd:PRK06155 68 -----------------VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 227 SLEPDLPALRAMGlHLW---AAGPGTHPAGISdllAEVSAEVDGPVPGYLSSPqsiTDTCLYIFTSGTTGLPKAARISHL 303
Cdd:PRK06155 131 ALEAADPGDLPLP-AVWlldAPASVSVPAGWS---TAPLPPLDAPAPAAAVQP---GDTAAILYTSGTTGPSKGVCCPHA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 304 KilqcqgFY-------QLCGVHQEDVIYLALPLYHMSgSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIG 376
Cdd:PRK06155 204 Q------FYwwgrnsaEDLEIGADDVLYTTLPLFHTN-ALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 377 ELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGNVA-TINYTGQR-GAVGRaswlykhi 454
Cdd:PRK06155 277 AMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNFViAVTHGSQRpGSMGR-------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 455 fpfslirydVTTGEPIRDPQGHCMATSPGEPGLLVAPVSQQSPFL-GYAGGPElaqgkllKDVFRPGDVFFNTGDLLVCD 533
Cdd:PRK06155 348 ---------LAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFAtGYFGMPE-------KTVEAWRNLWFHTGDRVVRD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 534 DQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAgMAALVLRPPHALDLMQLYTHVSENL 613
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVRHCEPRL 490
|
570 580 590
....*....|....*....|....*....|....*..
gi 1393643644 614 PPYARPRFLRLQESLATTETFKQQKVRMANEGFDPST 650
Cdd:PRK06155 491 AYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADT 527
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
71-551 |
1.87e-54 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 192.14 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHTFLIHGS-RRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefa 149
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAG-LRALG------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 150 ggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF-LESL 228
Cdd:pfam00501 43 --------------VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALkLEEL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 229 EPDLPALRAMGLHLWaagpgTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKIL-Q 307
Cdd:pfam00501 109 LEALGKLEVVKLVLV-----LDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVaN 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 308 CQGFYQLC----GVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSA---GQFWEDCQQHRVTVFQYIGELCR 380
Cdd:pfam00501 184 VLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 381 YLVNQPPSKAER--GHKVRLAVGSGLRPDTWERFVRRFGPlQVLETYGLTEGNVATINY------TGQRGAVGRaswlyk 452
Cdd:pfam00501 264 MLLEAGAPKRALlsSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPlpldedLRSLGSVGR------ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 453 hifPFSLIRY---DVTTGEPIRdpqghcmatsPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDVFRPGDvFFNTGDL 529
Cdd:pfam00501 337 ---PLPGTEVkivDDETGEPVP----------PGEPGELC--VRGPGVMKGYLNDPELT-----AEAFDEDG-WYRTGDL 395
|
490 500
....*....|....*....|..
gi 1393643644 530 LVCDDQGFLRFHDRTGDTFRWK 551
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
67-635 |
8.02e-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: 183.53 E-value: 8.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 67 LAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsagegeraapgagdaaagsga 146
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFA-AGLQNLG---------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 147 efaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVPTALRRGP--LLHCLRSCGARALVLAPEF 224
Cdd:cd05936 46 -----------------VQPGDRVALMLPNCPQFPIAYFGALKAGA--VVVPLNPLYTPreLEHILNDSGAKALIVAVSF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 225 LESLEPDLPAlramglhlwaagpgthpagisDLLAEVSAEvdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLK 304
Cdd:cd05936 107 TDLLAAGAPL---------------------GERVALTPE----------------DVAVLQYTSGTTGVPKGAMLTHRN 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 305 IL----QCQGFYQLCGVHqEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCR 380
Cdd:cd05936 150 LVanalQIKAWLEDLLEG-DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYI 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 381 YLVNQPPSKAERGHKVRLAVGSG--LRPDTWERFVRRFGpLQVLETYGLTE-GNVATIN-YTGQR--GAVGraswlykHI 454
Cdd:cd05936 229 ALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG-VPIVEGYGLTEtSPVVAVNpLDGPRkpGSIG-------IP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 455 FPFSLIRydvttgepIRDPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDVFRPGdvFFNTGDLLVCDD 534
Cdd:cd05936 301 LPGTEVK--------IVDDDGEELP--PGEVGELW--VRGPQVMKGYWNRPEET-----AEAFVDG--WLRTGDIGYMDE 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLP 614
Cdd:cd05936 362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDP-YSGEAVKAFVVLKEGASLTEEEIIAFCREQLA 440
|
570 580
....*....|....*....|.
gi 1393643644 615 PYARPRFLRLQESLATTETFK 635
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGK 461
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
170-658 |
8.38e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 184.88 E-value: 8.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 170 VALLLPAGPEFLWLwfgLAKAGLrTAFVPTAL---RRGPLL-------HClrscgarALVLA-PEFLESLEPDLPALRAM 238
Cdd:PRK07867 57 VGVLLDNTPEFSLL---LGAAAL-SGIVPVGLnptRRGAALardiahaDC-------QLVLTeSAHAELLDGLDPGVRVI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 239 GLH--LWAAGPGTHPAgisdllAEVSAEVDGPvpgylsspqsiTDTCLYIFTSGTTGLPKAARISHLKI-LQCQGFYQLC 315
Cdd:PRK07867 126 NVDspAWADELAAHRD------AEPPFRVADP-----------DDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHK 395
Cdd:PRK07867 189 GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 396 VRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGNVAtINYT--GQRGAVGRAswlykhifPFSLIRYDVTTGEP---- 469
Cdd:PRK07867 269 LRIVYGNEGAPGDIARFARRFG-CVVVDGFGSTEGGVA-ITRTpdTPPGALGPL--------PPGVAIVDPDTGTEcppa 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 470 IRDPQGHCMATSP-GEpglLVApVSQQSPFLGYAGGPElaqgkllKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTF 548
Cdd:PRK07867 339 EDADGRLLNADEAiGE---LVN-TAGPGGFEGYYNDPE-------ADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 549 RWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQL--YTHVSENLPPYARPRFLRLQE 626
Cdd:PRK07867 408 RVDGENLGTAPIERILLRYPDATEVAVYAVPDP-VVGDQVMAALVLAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCA 486
|
490 500 510
....*....|....*....|....*....|..
gi 1393643644 627 SLATTETFKQQKVRMANEGFDpstLSDPLYVL 658
Cdd:PRK07867 487 ELPRTATFKVLKRQLSAEGVD---CADPVWWI 515
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
73-638 |
3.67e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 180.26 E-value: 3.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 73 ELAQQRAAHTFLIHGS-----RRFSYSEAERESNRAARAFLrALGwdwgpdggdsgegsagegeraapgagdaaagsgae 147
Cdd:PRK08008 15 DLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFY-SLG----------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 148 faggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLES 227
Cdd:PRK08008 59 ----------------IRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPM 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 228 LEPDLPALRAMGLHLWAAGPGThPA--GISD---LLAEVSAEVDGPVPgyLSSpqsiTDTCLYIFTSGTTGLPKAARISH 302
Cdd:PRK08008 123 YRQIQQEDATPLRHICLTRVAL-PAddGVSSftqLKAQQPATLCYAPP--LST----DDTAEILFTSGTTSRPKGVVITH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 303 LKiLQCQGFYQL--CGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCR 380
Cdd:PRK08008 196 YN-LRFAGYYSAwqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 381 YLVNQPPSKAERGHKVR-----LAVGSGLRPDtwerFVRRFGpLQVLETYGLTEGNVATINYT--GQR--GAVGRASWLY 451
Cdd:PRK08008 275 TLMVQPPSANDRQHCLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTETIVGIIGDRpgDKRrwPSIGRPGFCY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 452 KhifpfslirydvttgEPIRDPQGHCMAtsPGEPG-LLVAPVSQQSPFLGYAGGPElAQGKLLKdvfrpGDVFFNTGDLL 530
Cdd:PRK08008 350 E---------------AEIRDDHNRPLP--AGEIGeICIKGVPGKTIFKEYYLDPK-ATAKVLE-----ADGWLHTGDTG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 531 VCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEgRAGMAALVLRPPHALDLMQLYTHVS 610
Cdd:PRK08008 407 YVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD-EAIKAFVVLNEGETLSEEEFFAFCE 485
|
570 580
....*....|....*....|....*...
gi 1393643644 611 ENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:PRK08008 486 QNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
170-679 |
4.47e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 177.53 E-value: 4.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 170 VALLLPAGPEFLwlwFGLAKAGLRTAFV----PTalRRGP-LLHCLRSCGARALVLAPEFLESLEP-DLPALRAMGLHLW 243
Cdd:PRK13388 55 VGVLLGNTPEML---FWLAAAALGGYVLvglnTT--RRGAaLAADIRRADCQLLVTDAEHRPLLDGlDLPGVRVLDVDTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPAGISDLLAEVSAEvdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKILQCQgfYQLC---GVHQE 320
Cdd:PRK13388 130 AYAELVAAAGALTPHREVDAM----------------DPFMLIFTSGTTGAPKAVRCSHGRLAFAG--RALTerfGLTRD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV 400
Cdd:PRK13388 192 DVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 401 GSGLRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTGQ-RGAVGRAswlykhiFPfSLIRYDVTTGEP----IRDPQG 475
Cdd:PRK13388 272 GNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIVVREPGTpPGSIGRG-------AP-GVAIYNPETLTEcavaRFDAHG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 476 HcmATSPGEP-GLLVApVSQQSPFLGYAGGPElAQGkllkDVFRPGDVFfnTGDLLVCDDQGFLRFHDRTGDTFRWKGEN 554
Cdd:PRK13388 343 A--LLNADEAiGELVN-TAGAGFFEGYYNNPE-ATA----ERMRHGMYW--SGDLAYRDADGWIYFAGRTADWMRVDGEN 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 555 VATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQL--YTHVSENLPPYARPRFLRLQESLATTE 632
Cdd:PRK13388 413 LSAAPIERILLRHPAINRVAVYAVPDE-RVGDQVMAALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRIAADLPSTA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1393643644 633 TFKQQKVRMANEGFDPSTlSDPLYVLDQAvGAYLPLTTARYSALLAG 679
Cdd:PRK13388 492 TNKVLKRELIAQGWATGD-PVTLWVRRGG-PAYRLMSEPAKAALAAE 536
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
71-641 |
2.96e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 157.66 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefag 150
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANA-LRALG-------------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 151 gdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGARALVLAPEF---L 225
Cdd:PRK06187 53 -------------VKKGDRVAVFDWNSHEYLEAYFAVPKIG--AVLHPINIRLKPeeIAYILNDAEDRVVLVDSEFvplL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 226 ESLEPDLPALRamglHLWAAGPGTHPAGI------SDLLAEVSAEVDGPVPGylsspqsITDTCLYIFTSGTTGLPKAAR 299
Cdd:PRK06187 118 AAILPQLPTVR----TVIVEGDGPAAPLApevgeyEELLAAASDTFDFPDID-------ENDAAAMLYTSGTTGHPKGVV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 300 ISH----LKILQCQGFYqlcGVHQEDVIYLALPLYHMSGSLLGIVGCMgIGATVVLKSKFSAGQFWEDCQQHRVTVFQYI 375
Cdd:PRK06187 187 LSHrnlfLHSLAVCAWL---KLSRDDVYLVIVPMFHVHAWGLPYLALM-AGAKQVIPRRFDPENLLDLIETERVTFFFAV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 376 GELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGpLQVLETYGLTE-GNVATINY-----TGQ---RGAV 444
Cdd:PRK06187 263 PTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTEtSPVVSVLPpedqlPGQwtkRRSA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 445 GRAswlykhiFPFSLIRydvttgepIRDPQGHCMATSPGEPGLLVApvsqQSPFL--GYAGGPELAQGKLLKDVFRpgdv 522
Cdd:PRK06187 342 GRP-------LPGVEAR--------IVDDDGDELPPDGGEVGEIIV----RGPWLmqGYWNRPEATAETIDGGWLH---- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 523 ffnTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDL 602
Cdd:PRK06187 399 ---TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDE-KWGERPVAVVVLKPGATLDA 474
|
570 580 590
....*....|....*....|....*....|....*....
gi 1393643644 603 MQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:PRK06187 475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
274-638 |
2.44e-39 |
|
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: 150.52 E-value: 2.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 274 SSPQSITDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLK 352
Cdd:cd05941 83 SEPSLVLDPALILYTSGTTGRPKGVVLTHANLAaNVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 353 SKFSAGQFWEDCQQHRVTVFQ-----YIGELCRYLVNQPPSKAERG---HKVRLAV-GSG-LRPDTWERFVRRFGpLQVL 422
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMgvptiYTRLLQYYEAHFTDPQFARAaaaERLRLMVsGSAaLPVPTLEEWEAITG-HTLL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 423 ETYGLTEGNVATIN-YTGQR--GAVGRAswlykhiFPFSLIR-YDVTTGEPirdpqghcmaTSPGEPG-LLVApvsqqSP 497
Cdd:cd05941 242 ERYGMTEIGMALSNpLDGERrpGTVGMP-------LPGVQARiVDEETGEP----------LPRGEVGeIQVR-----GP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 498 --FLGYAGGPELAqgkllKDVFRPgDVFFNTGDLLVCDDQGFLRFHDRTG-DTFRWKGENVATTEVAEVFEALDFLQEVN 574
Cdd:cd05941 300 svFKEYWNKPEAT-----KEEFTD-DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECA 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 575 VYGVTVPGHeGRAGMAALVLRPP-HALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd05941 374 VIGVPDPDW-GERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
70-628 |
2.27e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 149.28 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 70 RLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefa 149
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAA-LAALG------------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 150 ggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAG-----LRTAFVPTA----LRRGpllhclrscGARALVL 220
Cdd:PRK07656 52 --------------IGKGDRVAIWAPNSPHWVIAALGALKAGavvvpLNTRYTADEaayiLARG---------DAKALFV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 221 APEFLESLEP---DLPALRAMGLHLWAAGPGTHPAGI--SDLLA-----EVSAEVDGpvpgylsspqsiTDTCLYIFTSG 290
Cdd:PRK07656 109 LGLFLGVDYSattRLPALEHVVICETEEDDPHTEKMKtfTDFLAagdpaERAPEVDP------------DDVADILFTSG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 291 TTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRV 369
Cdd:PRK07656 177 TTGRPKGAMLTHRQLLSnAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERI 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 370 TVFQYIGELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTEGN-VATINYTGqRGAVGR 446
Cdd:PRK07656 257 TVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtgAASMPVALLERFESELGVDIVLTGYGLSEASgVTTFNRLD-DDRKTV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 447 ASwlykhifpfslirydvTTGEPIR-------DPQGHCMAtsPGEPG-LLVapvsqQSP--FLGYAGGPElAQGKLLKdv 516
Cdd:PRK07656 336 AG----------------TIGTAIAgvenkivNELGEEVP--VGEVGeLLV-----RGPnvMKGYYDDPE-ATAAAID-- 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 517 frpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLR 595
Cdd:PRK07656 390 ---ADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG--VPDERlGEVGKAYVVLK 464
|
570 580 590
....*....|....*....|....*....|...
gi 1393643644 596 PPHALDLMQLYTHVSENLPPYARPRFLRLQESL 628
Cdd:PRK07656 465 PGAELTEEELIAYCREHLAKYKVPRSIEFLDEL 497
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
164-616 |
2.53e-38 |
|
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: 148.51 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLepdLPALRAMGLHLW 243
Cdd:cd05911 32 LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKV---KEAAKELGPKDK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPAG---ISDLLAEVSAEVDGPVPGYLssPQSITDTCLYIFTSGTTGLPKAARISHLKIL----QCQGFYQLCg 316
Cdd:cd05911 109 IIVLDDKPDGvlsIEDLLSPTLGEEDEDLPPPL--KDGKDDTAAILYSSGTTGLPKGVCLSHRNLIanlsQVQTFLYGN- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 317 VHQEDVIYLALPLYHMSGsLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKV 396
Cdd:cd05911 186 DGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 397 RLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTE-GNVATINYTG--QRGAVGRaswlykhIFPFSLIRydvttgepIR 471
Cdd:cd05911 265 RVILsgGAPLSKELQELLAKRFPNATIKQGYGMTEtGGILTVNPDGddKPGSVGR-------LLPNVEAK--------IV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 DPQGhCMATSPGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDvfrpGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWK 551
Cdd:cd05911 330 DDDG-KDSLGPNEPGEIC--VRGPQVMKGYYNNPEATKETFDED----G--WLHTGDIGYFDEDGYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 552 GENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPY 616
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
75-660 |
1.22e-35 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 142.17 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 75 AQQRAAHTFLIHGS-----RRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsAGEGERaapgagdaaagsgaefa 149
Cdd:COG0365 19 AEGRGDKVALIWEGedgeeRTLTYAELRREVNRFA-NALRALG--------------VKKGDR----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 150 ggdgaargggaaaplspgatVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLE--- 226
Cdd:COG0365 67 --------------------VAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRggk 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 227 --SLEPDLPALRAMGLHLWA------AGPGTHPAGI---SDLLAEVSAEVDgPVPgyLSSpqsiTDTCLYIFTSGTTGLP 295
Cdd:COG0365 127 viDLKEKVDEALEELPSLEHvivvgrTGADVPMEGDldwDELLAAASAEFE-PEP--TDA----DDPLFILYTSGTTGKP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 296 KAARISHLKIL-QCQGFYQL-CGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVL---KSKF-SAGQFWEDCQQHRV 369
Cdd:COG0365 200 KGVVHTHGGYLvHAATTAKYvLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFpDPGRLWELIEKYGV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 370 TVFqyigelC------RYLVNQPPSKAERGH--KVRLA--VGSGLRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTG 439
Cdd:COG0365 280 TVF------FtaptaiRALMKAGDEPLKKYDlsSLRLLgsAGEPLNPEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 440 Q----RGAVGRASWLykhifpfslirYDVTtgepIRDPQGHCMAtsPGEPGLLVAPVSQQSPFLGYAGGPElaqgKLLKD 515
Cdd:COG0365 353 GlpvkPGSMGKPVPG-----------YDVA----VVDEDGNPVP--PGEEGELVIKGPWPGMFRGYWNDPE----RYRET 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 516 VFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHEGRAGMAALV-L 594
Cdd:COG0365 412 YFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG--VPDEIRGQVVKAFVvL 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393643644 595 RPPHALD------LMQlytHVSENLPPYARPRFLRLQESLATTETFKQQ-----KVRMANEGFDPSTLSDPlYVLDQ 660
Cdd:COG0365 490 KPGVEPSdelakeLQA---HVREELGPYAYPREIEFVDELPKTRSGKIMrrllrKIAEGRPLGDTSTLEDP-EALDE 562
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
77-638 |
1.19e-34 |
|
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: 136.97 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 77 QRAAH----TFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggd 152
Cdd:cd17631 3 RRARRhpdrTALVFGGRSLTYAELDERVNRLAHA-LRALG---------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 153 gaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGARALvlapefleslep 230
Cdd:cd17631 42 -----------VAKGDRVAVLSKNSPEFLELLFAAARLG--AVFVPLNFRLTPpeVAYILADSGAKVL------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 231 dlpalramglhlwaagpgthpagisdllaevsaevdgpvpgylsspqsITDTCLYIFTSGTTGLPKAARISHLKILqcqG 310
Cdd:cd17631 97 ------------------------------------------------FDDLALLMYTSGTTGRPKGAMLTHRNLL---W 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 311 FYQLCGVHQ----EDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQP 386
Cdd:cd17631 126 NAVNALAALdlgpDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHP 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 387 PSKAERGHKVR-LAVGSGLRPDTWERFVRRFGPlQVLETYGLTE--GNVATINYTGQR---GAVGRASwlykhifPFSLI 460
Cdd:cd17631 206 RFATTDLSSLRaVIYGGAPMPERLLRALQARGV-KFVQGYGMTEtsPGVTFLSPEDHRrklGSAGRPV-------FFVEV 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 461 RydvttgepIRDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFLRF 540
Cdd:cd17631 278 R--------IVDPDGR--EVPPGEVGEIV--VRGPHVMAGYWNRPEAT-----AAAFRDG--WFHTGDLGRLDEDGYLYI 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 541 HDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPgHE--GRAGMAALVLRPPHALDLMQLYTHVSENLPPYAR 618
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VP-DEkwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKI 415
|
570 580
....*....|....*....|
gi 1393643644 619 PRFLRLQESLATTETFKQQK 638
Cdd:cd17631 416 PKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
164-643 |
1.78e-33 |
|
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: 134.75 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARaLVLAPEfleslEPDLPALRAMGLHLW 243
Cdd:cd05926 36 IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK-LVLTPK-----GELGPASRAASKLGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPAGISDLL---AEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKIlqCQGFYQLCGVHQ- 319
Cdd:cd05926 110 AILELALDVGVLIRApsaESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNL--AASATNITNTYKl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 --EDVIYLALPLYHMSG---SLLGIVGCmgiGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERG- 393
Cdd:cd05926 188 tpDDRTLVVMPLFHVHGlvaSLLSTLAA---GGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 394 HKVRLA--VGSGLRPDTWERFVRRFGpLQVLETYGLTEG-NVATIN--YTGQR--GAVGRASwlykhifpfslirydvtt 466
Cdd:cd05926 265 PKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTEAaHQMTSNplPPGPRkpGSVGKPV------------------ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 467 GEPIR--DPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDvfrpGdvFFNTGDLLVCDDQGFLRFHDRT 544
Cdd:cd05926 326 GVEVRilDEDGEILP--PGVVGEIC--LRGPNVTRGYLNNPEANAEAAFKD----G--WFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 545 GDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRL 624
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYF 474
|
490
....*....|....*....
gi 1393643644 625 QESLATTETFKQQKVRMAN 643
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
74-638 |
5.03e-32 |
|
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: 130.57 E-value: 5.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 74 LAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggdg 153
Cdd:cd05959 13 LNEGRGDKTAFIDDAGSLTYAELEAEARRVAGA-LRALG----------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 154 aargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLP 233
Cdd:cd05959 51 ----------VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 234 ALRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPGylssPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFY- 312
Cdd:cd05959 121 KSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPA----ATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYa 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 313 -QLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKF-SAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKA 390
Cdd:cd05959 197 rNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 391 ERGHKVRLAVGSG--LRPDTWERFVRRFGpLQVLETYGLTEgnvatinytgqrgavgraswlYKHIFPFSL---IRYDvT 465
Cdd:cd05959 277 RDLSSLRLCVSAGeaLPAEVGERWKARFG-LDILDGIGSTE---------------------MLHIFLSNRpgrVRYG-T 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 466 TGEP-------IRDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFL 538
Cdd:cd05959 334 TGKPvpgyeveLRDEDGG--DVADGEPGELY--VRGPSSATMYWNNRDKT-----RDTFQGE--WTRTGDKYVRDDDGFY 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 539 RFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAgMAALVLRP---PHALDLMQLYTHVSENLPP 615
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KAFVVLRPgyeDSEALEEELKEFVKDRLAP 481
|
570 580
....*....|....*....|...
gi 1393643644 616 YARPRFLRLQESLATTETFKQQK 638
Cdd:cd05959 482 YKYPRWIVFVDELPKTATGKIQR 504
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
321-682 |
1.23e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 132.15 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV 400
Cdd:PRK07868 647 DTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 401 GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQR-GAVGRAswlykhiFPFS----LIRYDVTTGEPIRDPQG 475
Cdd:PRK07868 727 GSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGAKiGSKGRP-------LPGAgrveLAAYDPEHDLILEDDRG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 476 HCMATSPGEPGLLvapvsqqspfLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENV 555
Cdd:PRK07868 800 FVRRAEVNEVGVL----------LARARGPIDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPV 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 556 ATTEVAEVFEALDFLQEVNVYGVTVPGHEgrAGMAALVLRPPHALDLMQLyTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PRK07868 870 YTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAAITAADL-TEALASLPVGLGPDIVHVVPEIPLSATYR 946
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1393643644 636 QQKVRMANEGFdPSTLSDPLYvLDQAVGAYLPLTTARYSALLAGNLR 682
Cdd:PRK07868 947 PTVSALRAAGI-PKPGRQAWY-FDPETNRYRRLTPAVRAELTGGHRR 991
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
84-628 |
3.06e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 122.35 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 84 LIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggdgaargggaaap 163
Cdd:PRK08316 30 LVFGDRSWTYAELDAAVNRVAAA-LLDLG--------------------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVPT--ALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLH 241
Cdd:PRK08316 58 LKKGDRVAALGHNSDAYALLWLACARAGA--VHVPVnfMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 LWAAGPGT-HPAGISDLLAEVSAEVDGPVPGYLSspqsITDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQ 319
Cdd:PRK08316 136 LSLVLGGReAPGGWLDFADWAEAGSVAEPDVELA----DDDLAQILYTSGTESLPKGAMLTHRALIaEYVSCIVAGDMSA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALPLYH---MSGSLLGIVgcmGIGATVVLKSKFSAGQFWEDCQQHRVTVF-----QYIGelcryLVNQPpskae 391
Cdd:PRK08316 212 DDIPLHALPLYHcaqLDVFLGPYL---YVGATNVILDAPDPELILRTIEAERITSFfapptVWIS-----LLRHP----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 392 RGHKVRLavgSGLR---------P-DTWERFVRRFGPLQVLETYGLTE-GNVATI----NYTGQRGAVGRASwlykhifp 456
Cdd:PRK08316 279 DFDTRDL---SSLRkgyygasimPvEVLKELRERLPGLRFYNCYGQTEiAPLATVlgpeEHLRRPGSAGRPV-------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 457 fslirYDVTTgePIRDPQGHCMAtsPGEPGLLVApvsqQSPFL--GYAGGPELAQgkllkDVFRPGdvFFNTGDLLVCDD 534
Cdd:PRK08316 348 -----LNVET--RVVDDDGNDVA--PGEVGEIVH----RSPQLmlGYWDDPEKTA-----EAFRGG--WFHSGDLGVMDE 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLP 614
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP-KWIEAVTAVVVPKAGATVTEDELIAHCRARLA 486
|
570
....*....|....
gi 1393643644 615 PYARPRFLRLQESL 628
Cdd:PRK08316 487 GFKVPKRVIFVDEL 500
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
164-620 |
5.32e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 115.79 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF---LESLEPDLPALRAMGL 240
Cdd:PRK07788 96 VRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFtdlLSALPPDLGRLRAWGG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HLWAAGP-GTHPAGISDLLAEVSAEVdGPVPgylSSPQSITdtclyIFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVH 318
Cdd:PRK07788 176 NPDDDEPsGSTDETLDDLIAGSSTAP-LPKP---PKPGGIV-----ILTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 319 QEDVIYLALPLYHMSGSLLGIVGcMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAER----GH 394
Cdd:PRK07788 247 AGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKydtsSL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 395 KVRLAVGSGLRPDTWERFVRRFGPLqVLETYGLTEGNVATI----NYTGQRGAVGRASwlykhifpfslirydVTTGEPI 470
Cdd:PRK07788 326 KIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFATIatpeDLAEAPGTVGRPP---------------KGVTVKI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 RDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGG--PELAQGKLlkdvfrpgdvffNTGDLLVCDDQGFLRFHDRTGDTF 548
Cdd:PRK07788 390 LDENGN--EVPRGVVGRIF--VGNGFPFEGYTDGrdKQIIDGLL------------SSGDVGYFDEDGLLFVDGRDDDMI 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393643644 549 RWKGENVATTEVAEVFEALDFLQEVNVYGVTVP--GHEGRagmAALVLRPPHALDLMQLYTHVSENLPPYARPR 620
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefGQRLR---AFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-628 |
9.62e-26 |
|
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: 110.99 E-value: 9.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAG--LRTAFVPT-ALRRGPLLHCLRSCGARALVLAPEfleslepdlpalrAMGL 240
Cdd:cd05922 15 GVRGERVVLILPNRFTYIELSFAVAYAGgrLGLVFVPLnPTLKESVLRYLVADAGGRIVLADA-------------GAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HLWAAGPGTHPAGISdLLAEVSAEVDGPVPGYLSSPQsitDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQ 319
Cdd:cd05922 82 RLRDALPASPDPGTV-LDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLaNARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALPLYHMSG-SLLGIvgCMGIGATVVLKSKFSAGQ-FWEDCQQHRVTVFQ---YIGELCRYLVNQPpskAERGH 394
Cdd:cd05922 158 DDRALTVLPLSYDYGlSVLNT--HLLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpSTYAMLTRLGFDP---AKLPS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 395 KVRLA-VGSGLRPDTWERFVRRFGPLQVLETYGLTEGNvATINY-----TGQR-GAVGRAswlykhifpfslirydVTTG 467
Cdd:cd05922 233 LRYLTqAGGRLPQETIARLRELLPGAQVYVMYGQTEAT-RRMTYlpperILEKpGSIGLA----------------IPGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 468 E-PIRDPQGhcMATSPGEPGLLVAPVSqqspfLGYAGGPELAQGKLLKDvfRPGDVFFnTGDLLVCDDQGFLRFHDRTGD 546
Cdd:cd05922 296 EfEILDDDG--TPTPPGEPGEIVHRGP-----NVMKGYWNDPPYRRKEG--RGGGVLH-TGDLARRDEDGFLFIVGRRDR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 547 TFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEgraGMAALVLRPPhALDLMQLYTHVSENLPPYARPRFLRLQE 626
Cdd:cd05922 366 MIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPD-KIDPKDVLRSLAERLPPYKVPATVRVVD 441
|
..
gi 1393643644 627 SL 628
Cdd:cd05922 442 EL 443
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
166-641 |
1.27e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 111.68 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF--------LESLEPDLPALRa 237
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhaamARRLRPELPALR- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 238 mglHLWAAGpGTHPAGISDLLAEVSAEVDGPVPGYLSSPQ-SITDTCLYIFTSGTTGLPKAARISHLKILQCQGFY-QLC 315
Cdd:PRK13295 158 ---HVVVVG-GDGADSFEALLITPAWEQEPDAPAILARLRpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYaERL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTvFQ-----YIGELCRylvnqppSKA 390
Cdd:PRK13295 234 GLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastpFLTDLTR-------AVK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 391 ERGH-----KVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTGQrgavgraswlykhifpfSLIRYDVT 465
Cdd:PRK13295 306 ESGRpvsslRTFLCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVTLTKLDD-----------------PDERASTT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 466 TGEP-------IRDPQGhcMATSPGEPGLLVapVSQQSPFLGYAGGPEL----AQGkllkdvfrpgdvFFNTGDLLVCDD 534
Cdd:PRK13295 368 DGCPlpgvevrVVDADG--APLPAGQIGRLQ--VRGCSNFGGYLKRPQLngtdADG------------WFDTGDLARIDA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVaevfEALDF----LQEVNVYGVTVPGHEGRAgMAALVLRPPHALDL--MQLYTH 608
Cdd:PRK13295 432 DGYIRISGRSKDVIIRGGENIPVVEI----EALLYrhpaIAQVAIVAYPDERLGERA-CAFVVPRPGQSLDFeeMVEFLK 506
|
490 500 510
....*....|....*....|....*....|...
gi 1393643644 609 VSENLPPYArPRFLRLQESLATTETFKQQKVRM 641
Cdd:PRK13295 507 AQKVAKQYI-PERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
232-620 |
2.64e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.86 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 232 LPALRAMGLHLWAAGPGTHPagISDLLAEVsaevdGPVPGYLSSPQSIT--DTCLYIFTSGTTGLPKAARISHLKI---- 305
Cdd:PRK05605 176 IPALRKARAALTGPAPGTVP--WETLVDAA-----IGGDGSDVSHPRPTpdDVALILYTSGTTGKPKGAQLTHRNLfana 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 306 LQCQGFYQLCGVHQEdVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNq 385
Cdd:PRK05605 249 AQGKAWVPGLGDGPE-RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 386 ppSKAERG---HKVRLAV--GSGLRPDTWERFVRRFGPLQVlETYGLTE------GNvaTINYTGQRGAVGRAswlykhi 454
Cdd:PRK05605 327 --AAEERGvdlSGVRNAFsgAMALPVSTVELWEKLTGGLLV-EGYGLTEtspiivGN--PMSDDRRPGYVGVP------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 455 FPFSLIRydvttgepIRDPQGHCMATSPGEPGLLVAPVSQQspFLGYAGGPELAQGKLLKDVFRpgdvffnTGDLLVCDD 534
Cdd:PRK05605 395 FPDTEVR--------IVDPEDPDETMPDGEEGELLVRGPQV--FKGYWNRPEETAKSFLDGWFR-------TGDVVVMEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHEGRAGM-AALVLRPPHALDLMQLYTHVSENL 613
Cdd:PRK05605 458 DGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVvAAVVLEPGAALDPEGLRAYCREHL 535
|
....*..
gi 1393643644 614 PPYARPR 620
Cdd:PRK05605 536 TRYKVPR 542
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
164-538 |
5.88e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.04 E-value: 5.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPtALRRGPLLHCLRSCGARALV-LAPEFLESLEPDLPALRAMGLHL 242
Cdd:PRK07529 80 VGPGDVVAFLLPNLPETHFALWGGEAAGIANPINP-LLEPEQIAELLRAAGAKVLVtLGPFPGTDIWQKVAEVLAALPEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 243 -----------------WAAGP--GTHPAGISDLLAEVSAE-VDGPVPGylsSPQSITDTCLYIFTSGTTGLPKAARISH 302
Cdd:PRK07529 159 rtvvevdlarylpgpkrLAVPLirRKAHARILDFDAELARQpGDRLFSG---RPIGPDDVAAYFHTGGTTGMPKLAQHTH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 303 L-KILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSkfSAG--------QFWEDCQQHRVTVFQ 373
Cdd:PRK07529 236 GnEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAT--PQGyrgpgviaNFWKIVERYRINFLS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 374 YIGELCRYLVNQPPSKAERGhKVRLAV--GSGLRPDTWERFVRRFGpLQVLETYGLTEGN-VATINY-TGQR--GAVGRA 447
Cdd:PRK07529 314 GVPTVYAALLQVPVDGHDIS-SLRYALcgAAPLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPpDGERriGSVGLR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 448 swlykhiFPFSLIRYdvttgePIRDPQGH----CmatSPGEPGLLVapVSQQSPFLGYAggpELAQGKLLkdvfRPGDVF 523
Cdd:PRK07529 392 -------LPYQRVRV------VILDDAGRylrdC---AVDEVGVLC--IAGPNVFSGYL---EAAHNKGL----WLEDGW 446
|
410
....*....|....*
gi 1393643644 524 FNTGDLLVCDDQGFL 538
Cdd:PRK07529 447 LNTGDLGRIDADGYF 461
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
281-638 |
1.10e-24 |
|
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: 105.66 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLAL-PLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQ 359
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 FWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINY 437
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtgAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 438 TGQrgavgraswlykhifPFSLIRydVTTGEPIRDPQGHCmatspGEPGLLVapVSQQSPFLGYAGGPElAQGKLLKdvf 517
Cdd:cd17638 161 PGD---------------DAETVA--TTCGRACPGFEVRI-----ADDGEVL--VRGYNVMQGYLDDPE-ATAEAID--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 518 rpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLRP 596
Cdd:cd17638 213 --ADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKAFVVARP 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1393643644 597 PHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd17638 289 GVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
281-639 |
1.76e-24 |
|
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: 106.65 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISH---LKILQCQGFYQlcGVHQEDVIY-LALP--LYHMSGSLLGIvgcMGIGATVVL--K 352
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLHTHsypLGHIPTAAYWL--GLRPDDIHWnIADPgwAKGAWSSFFGP---WLLGATVFVyeG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 353 SKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHkVRLAVGSG--LRPDTWERFVRRFGpLQVLETYGLTEG 430
Cdd:cd05972 157 PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 431 NVATINYTGQR---GAVGRASWLYKhifpFSLIRYDvttGEPIrdpqghcmatSPGEPGLLVAPVSQQSPFLGYAGGPEl 507
Cdd:cd05972 235 GLTVGNFPDMPvkpGSMGRPTPGYD----VAIIDDD---GREL----------PPGEEGDIAIKLPPPGLFLGYVGDPE- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 508 aqgkLLKDVFRpGDVFFnTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATtevAEVFEALDFLQEVNVYGVTVPGHEGRA 587
Cdd:cd05972 297 ----KTEASIR-GDYYL-TGDRAYRDEDGYFWFVGRADDIIKSSGYRIGP---FEVESALLEHPAVAEAAVVGSPDPVRG 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393643644 588 GMA-ALVLRPPHALDLMQ----LYTHVSENLPPYARPRFLRLQESLATTETFKQQKV 639
Cdd:cd05972 368 EVVkAFVVLTSGYEPSEElaeeLQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
166-642 |
2.28e-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: 106.41 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCgARALVLAPEFLESLEpdlpalramglhlwaa 245
Cdd:cd05958 35 PGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA-RITVALCAHALTASD---------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 246 gpgthpagisdllaevsaevdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKILQ-CQGF-YQLCGVHQEDVI 323
Cdd:cd05958 98 -----------------------------------DICILAFTSGTTGAPKATMHFHRDPLAsADRYaVNVLRLREDDRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 324 YLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSG 403
Cdd:cd05958 143 VGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 404 --LRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTGQRGAVGraswlykhifpfslirydvTTGEP-------IRDPQ 474
Cdd:cd05958 223 eaLPAALHRAWKEATG-IPIIDGIGSTEMFHIFISARPGDARPG-------------------ATGKPvpgyeakVVDDE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 475 GHcmATSPGEPGLLVApvsqQSPfLGYAGGPELAQgkllKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGEN 554
Cdd:cd05958 283 GN--PVPDGTIGRLAV----RGP-TGCRYLADKRQ----RTYVQGG--WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 555 VATTEVAEVfealdFLQEVNVYGVTVPGHEGRAGM----AALVLRPPHALD---LMQLYTHVSENLPPYARPRFLRLQES 627
Cdd:cd05958 350 IAPPEVEDV-----LLQHPAVAECAVVGHPDESRGvvvkAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTE 424
|
490
....*....|....*
gi 1393643644 628 LATTETFKQQKVRMA 642
Cdd:cd05958 425 LPRTATGKLQRFALR 439
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
164-567 |
5.02e-24 |
|
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: 106.17 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGlrtAFVPTA---LRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGL 240
Cdd:cd05904 54 GRKGDVVLLLSPNSIEFPVAFLAVLSLG---AVVTTAnplSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HLwaagpgTHPAGISDLLAEVSaEVDGPVPgylssPQSITDTCLYIFTSGTTGLPKAARISHLK-ILQCQGF--YQLCGV 317
Cdd:cd05904 131 AE------FDSLSFSDLLFEAD-EAEPPVV-----VIKQDDVAALLYSSGTTGRSKGVMLTHRNlIAMVAQFvaGEGSNS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 318 HQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFqyigelcrYLVnqPP-----SKAER 392
Cdd:cd05904 199 DSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL--------PVV--PPivlalVKSPI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 GHKVRLA----VGSG---LRPDTWERFVRRFGPLQVLETYGLTE-GNVATINYT-----GQRGAVGR--ASWLYKHIfpf 457
Cdd:cd05904 269 VDKYDLSslrqIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApekdrAKYGSVGRlvPNVEAKIV--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 458 sliryDVTTGEPIrdPqghcmatsPGEPG-LLVapvsqQSPFL--GYAGGPELAQGKLLKDvfrpGdvFFNTGDLLVCDD 534
Cdd:cd05904 346 -----DPETGESL--P--------PNQTGeLWI-----RGPSImkGYLNNPEATAATIDKE----G--WLHTGDLCYIDE 399
|
410 420 430
....*....|....*....|....*....|...
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVaevfEAL 567
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAEL----EAL 428
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
280-642 |
8.07e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 103.51 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 280 TDTCLYIFTSGTTGLPKAARISHLKILQcQGFY--QLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK-FS 356
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVN-NGYFigERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 357 AGQFWEDCQQHRVTVFQ-----YIGELcrylvNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTE 429
Cdd:cd05917 81 PLAVLEAIEKEKCTALHgvptmFIAEL-----EHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 430 GN-VATINYTG----QR-GAVGRaswlykhIFPFSLIRydvttgepIRDPQGHCMAtSPGEPGLLVapVSQQSPFLGYAG 503
Cdd:cd05917 156 TSpVSTQTRTDdsieKRvNTVGR-------IMPHTEAK--------IVDPEGGIVP-PVGVPGELC--IRGYSVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 504 GPElaQGKLLKDvfrpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGH 583
Cdd:cd05917 218 DPE--KTAEAID----GDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 584 E-GRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRMA 642
Cdd:cd05917 290 RyGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
84-631 |
1.61e-23 |
|
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: 104.15 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 84 LIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggdgaargggaaap 163
Cdd:cd05930 6 VVDGDQSLTYAELDARANRLARY-LRERG--------------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVPtalrrgpllhclrscgaralvlapeflesLEPDLPALRamglhlw 243
Cdd:cd05930 34 VGPGDLVAVLLERSLEMVVAILAVLKAGA--AYVP-----------------------------LDPSYPAER------- 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aagpgthpagISDLLAEVSAEVdgpvpgYLSSPqsiTDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDV 322
Cdd:cd05930 76 ----------LAYILEDSGAKL------VLTDP---DDLAYVIYTSGSTGKPKGVMVEHRGLVnLLLWMQEAYPLTPGDR 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IyLALPLYHMSGSLLGIVGCMGIGATVVL---KSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPpsKAERGHKVRLA 399
Cdd:cd05930 137 V-LQFTSFSFDVSVWEIFGALLAGATLVVlpeEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 400 VGSG--LRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASwlykhifpfslirydVTTGEPIR------ 471
Cdd:cd05930 214 LVGGeaLPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGR---------------VPIGRPIPntrvyv 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 -DPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDT--- 547
Cdd:cd05930 279 lDENLRPVP--PGVPGELY--IGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQvki 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 548 --FRwkgenVATTEVAEVFEALDFLQEVNVygVTVPGHEGRAGMAA-LVLRPPHALDLMQLYTHVSENLPPYARPRFLRL 624
Cdd:cd05930 355 rgYR-----IELGEIEAALLAHPGVREAAV--VAREDGDGEKRLVAyVVPDEGGELDEEELRAHLAERLPDYMVPSAFVV 427
|
....*..
gi 1393643644 625 QESLATT 631
Cdd:cd05930 428 LDALPLT 434
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
166-641 |
2.99e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 104.47 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF--------LESLEP------- 230
Cdd:PRK12583 69 PGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFktsdyhamLQELLPglaegqp 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 231 ------DLPALRamGLHLWAAGPGTHPAGISDLLAE---VSAEVDGPVPGYLSSPQSITdtclYIFTSGTTGLPKAARIS 301
Cdd:PRK12583 149 galaceRLPELR--GVVSLAPAPPPGFLAWHELQARgetVSREALAERQASLDRDDPIN----IQYTSGTTGFPKGATLS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 302 HLKILQCQGFY-QLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK-FSAGQFWEDCQQHRVTVFQ-----Y 374
Cdd:PRK12583 223 HHNILNNGYFVaESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEaFDPLATLQAVEEERCTALYgvptmF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 375 IGELcrylvNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTG------QRGAVGR 446
Cdd:PRK12583 303 IAEL-----DHPQRGNFDLSSLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAaddlerRVETVGR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 447 aswlykhifpfSLIRYDVTtgepIRDPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPElAQGKLLKdvfrpGDVFFNT 526
Cdd:PRK12583 378 -----------TQPHLEVK----VVDPDGATVP--RGEIGELC--TRGYSVMKGYWNNPE-ATAESID-----EDGWMHT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 527 GDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHeGRAGMAALVLRPPHALDLMQLY 606
Cdd:PRK12583 433 GDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY-GEEIVAWVRLHPGHAASEEELR 511
|
490 500 510
....*....|....*....|....*....|....*
gi 1393643644 607 THVSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:PRK12583 512 EFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
164-641 |
4.41e-23 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 102.54 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVlapefleslepdlpalramglhlw 243
Cdd:cd05919 32 VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV------------------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aagpgthpagisdllaeVSAEvdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLK-ILQCQGF-YQLCGVHQED 321
Cdd:cd05919 88 -----------------TSAD----------------DIAYLLYSSGTTGPPKGVMHAHRDpLLFADAMaREALGLTPGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 322 VIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKF-SAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV 400
Cdd:cd05919 135 RVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 401 --GSGLRPDTWERFVRRFGpLQVLETYGLTE-GNVATINYTGQrgavgraswlykhifpfslIRYDvTTGEPI------- 470
Cdd:cd05919 215 saGEALPRGLGERWMEHFG-GPILDGIGATEvGHIFLSNRPGA-------------------WRLG-STGRPVpgyeirl 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 RDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDVFRPGDVFFntgdllvCDDQGFLRFHDRTGDTFRW 550
Cdd:cd05919 274 VDEEGH--TIPPGEEGDLL--VRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFC-------RDADGWYTHAGRADDMLKV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 551 KGENVATTEVAEVFEALDFLQEVNVYGVTvPGHEGRAGMAALVLRPPHALD--LMQ-LYTHVSENLPPYARPRFLRLQES 627
Cdd:cd05919 343 GGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAFVVLKSPAAPQesLARdIHRHLLERLSAHKVPRRIAFVDE 421
|
490
....*....|....
gi 1393643644 628 LATTETFKQQKVRM 641
Cdd:cd05919 422 LPRTATGKLQRFKL 435
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
166-641 |
9.60e-23 |
|
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: 101.69 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFleslepdlpalramGLHLWAA 245
Cdd:cd05903 25 PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERF--------------RQFDPAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 246 GPGthpagisdllaevsaevdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKILQCQGFY-QLCGVHQEDVIY 324
Cdd:cd05903 91 MPD--------------------------------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYaERLGLGPGDVFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 325 LALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQ----YIGELCRYLVNQPPskAERGHKVRLAV 400
Cdd:cd05903 139 VASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTDLLNAVEEAGE--PLSRLRTFVCG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 401 GSGLRPDTWERFVRRFGPLqVLETYGLTEGNVATINYTGQRgaVGRASWLYKHIFPFSLIRydvttgepIRDPQGhcMAT 480
Cdd:cd05903 217 GATVPRSLARRAAELLGAK-VCSAYGSTECPGAVTSITPAP--EDRRLYTDGRPLPGVEIK--------VVDDTG--ATL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 481 SPGEPGLLVApvsqQSP--FLGYAGGPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATT 558
Cdd:cd05903 284 APGVEGELLS----RGPsvFLGYLDRPDLT-----ADAAPEG--WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 559 EVAEVfealdFLQEVNVYGVTVPGHE----GRAGMAALVLRPPHALDLMQLYTHVS-ENLPPYARPRFLRLQESLATTET 633
Cdd:cd05903 353 EVEDL-----LLGHPGVIEAAVVALPderlGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPS 427
|
....*...
gi 1393643644 634 FKQQKVRM 641
Cdd:cd05903 428 GKVQKFRL 435
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
71-631 |
2.46e-22 |
|
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: 101.38 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHTFLIHGSRRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefag 150
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLA-AGLLALG-------------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 151 gdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAP-------- 222
Cdd:COG1021 72 -------------LRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 223 EFLESLEPDLPALRamglHLWAAGPGTHPAGISDLLAEvsaevdgPVPGYLSSPQSiTDTCLYIFTSGTTGLPK------ 296
Cdd:COG1021 139 ALARELQAEVPSLR----HVLVVGDAGEFTSLDALLAA-------PADLSEPRPDP-DDVAFFQLSGGTTGLPKliprth 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 297 ---------AARIshlkilqcqgfyqlCGVHQEDViYL-ALPLYH-MSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQ 365
Cdd:COG1021 207 ddylysvraSAEI--------------CGLDADTV-YLaALPAAHnFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 366 QHRVTVfqyIGelcryLVnqPP-------SKAERGHKVR-LAV----GSGLRPDTWERFVRRFGP-LQvlETYGLTEGnv 432
Cdd:COG1021 272 RERVTV---TA-----LV--PPlallwldAAERSRYDLSsLRVlqvgGAKLSPELARRVRPALGCtLQ--QVFGMAEG-- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 433 aTINYTG-------QRGAVGRAswlykhIFPFSLIRydvttgepIRDPQGHCMAtsPGEPGLLVApvsqQSP--FLGYAG 503
Cdd:COG1021 338 -LVNYTRlddpeevILTTQGRP------ISPDDEVR--------IVDEDGNPVP--PGEVGELLT----RGPytIRGYYR 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 504 GPELAQgkllkDVFRPgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGH 583
Cdd:COG1021 397 APEHNA-----RAFTP-DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV--VAMPDE 468
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1393643644 584 E-GRAGMAALVLRPPhALDLMQLYTHVSE-NLPPYARPRFLRLQESLATT 631
Cdd:COG1021 469 YlGERSCAFVVPRGE-PLTLAELRRFLRErGLAAFKLPDRLEFVDALPLT 517
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
66-641 |
3.79e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 97.51 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 66 SLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsagegeraapgagdaaagsg 145
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLA-AWLAAQG--------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 146 aefaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF- 224
Cdd:PRK06164 57 ------------------VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFk 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 225 -------LESLEPD-LPALRAMGLHLWAAG--PGTHPAGISDLLAEVSAEvdgPVPGyLSSPQSITDTCLYIF-TSGTTG 293
Cdd:PRK06164 119 gidfaaiLAAVPPDaLPPLRAIAVVDDAADatPAPAPGARVQLFALPDPA---PPAA-AGERAADPDAGALLFtTSGTTS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 294 LPK------AARISHLKILQcqgfyQLCGVHQEDVIYLALPlyhMSGS--LLGIVGCMGIGATVVLKSKFSAGQFWEDCQ 365
Cdd:PRK06164 195 GPKlvlhrqATLLRHARAIA-----RAYGYDPGAVLLAALP---FCGVfgFSTLLGALAGGAPLVCEPVFDAARTARALR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 366 QHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGS--GLRPDTWERFVRRFGPLQVL----ETYGLTEGNVATINYTG 439
Cdd:PRK06164 267 RHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASfaPALGELAALARARGVPLTGLygssEVQALVALQPATDPVSV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 440 QRGAVGRAswlykhIFPFSLIRydvttgepIRDPQGHCMAtSPGEPGLLvaPVSQQSPFLGYAGGPELAQgkllkDVFRP 519
Cdd:PRK06164 347 RIEGGGRP------ASPEARVR--------ARDPQDGALL-PDGESGEI--EIRAPSLMRGYLDNPDATA-----RALTD 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 520 gDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTvpgHEGRAGMAALVLRPPHA 599
Cdd:PRK06164 405 -DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT---RDGKTVPVAFVIPTDGA 480
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1393643644 600 -LDLMQLYTHVSENLPPYARPRFLRLQESLATTET---FKQQKVRM 641
Cdd:PRK06164 481 sPDEAGLMAACREALAGFKVPARVQVVEAFPVTESangAKIQKHRL 526
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
167-644 |
4.14e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 96.96 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALramglhlwaag 246
Cdd:PRK03640 52 GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVK----------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 247 pgthpagISDLLAEVSAEVDgpvpgyLSSPQSITDTCLYIFTSGTTGLPKA-----------ARISHLKIlqcqgfyqlc 315
Cdd:PRK03640 121 -------FAELMNGPKEEAE------IQEEFDLDEVATIMYTSGTTGKPKGviqtygnhwwsAVGSALNL---------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHQEDVIYLALPLYHMSG-SLL--GIVgcmgIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAER 392
Cdd:PRK03640 178 GLTEDDCWLAAVPIFHISGlSILmrSVI----YGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 GHKVRLAVGSGLRP-DTWERFVRRFGPlqVLETYGLTE--GNVATINYTGQRGAVGRASwlyKHIFPFSLirydvttgeP 469
Cdd:PRK03640 254 SSFRCMLLGGGPAPkPLLEQCKEKGIP--VYQSYGMTEtaSQIVTLSPEDALTKLGSAG---KPLFPCEL---------K 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 470 IRDPQGHCMATSPGEpgLLVapvsqQSPFL--GYaggpeLAQGKLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDT 547
Cdd:PRK03640 320 IEKDGVVVPPFEEGE--IVV-----KGPNVtkGY-----LNREDATRETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 548 FRWKGENVATTEVAEVFEALDFLQEVNVYGVT------VPghegragMAALVLRppHALDLMQLYTHVSENLPPYARPRF 621
Cdd:PRK03640 386 IISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwgqVP-------VAFVVKS--GEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|...
gi 1393643644 622 LRLQESLATTETFKQQKVRMANE 644
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
58-641 |
4.56e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 97.42 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 58 PEGPEGGCSLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsAGEGERaapga 137
Cdd:PRK06178 26 PEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFA-ALLRQRG--------------VGAGDR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 138 gdaaagsgaefaggdgaargggaaaplspgatVALLLPAGPEFLWLWFGLAKAGlrTAFVPTA--LRRGPLLHCLRSCGA 215
Cdd:PRK06178 86 --------------------------------VAVFLPNCPQFHIVFFGILKLG--AVHVPVSplFREHELSYELNDAGA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 216 RALVLAPEFLESLEPDLPALR-------AMGLHLWAA----------GPGTHPAGISDLLAEVSAEVDGP--VPGYLSSP 276
Cdd:PRK06178 132 EVLLALDQLAPVVEQVRAETSlrhvivtSLADVLPAEptlplpdslrAPRLAAAGAIDLLPALRACTAPVplPPPALDAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 277 QSITdtclyiFTSGTTGLPKAARISHLK-ILQCQGFYQLCGVHQEDVIYLA-LPLYHMSGSLLGIVGCMGIGATVVLKSK 354
Cdd:PRK06178 212 AALN------YTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSGATLVLLAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 355 FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAE--RGHKVRLAVG--SGLRPDTWERFVRRFGPLQVLETYGLTEG 430
Cdd:PRK06178 286 WDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYdlSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAAWGMTET 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 431 NVATINYTGQRgaVGRASWLYKHIF-----PFSLIRY-DVTTGEPIrdpqghcmatsP-GEPGLLVapVSQQSPFLGYAG 503
Cdd:PRK06178 366 HTCDTFTAGFQ--DDDFDLLSQPVFvglpvPGTEFKIcDFETGELL-----------PlGAEGEIV--VRTPSLLKGYWN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 504 GPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVaevfEALdFLQEVNVYGVTVPG- 582
Cdd:PRK06178 431 KPEAT-----AEALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV----EAL-LGQHPAVLGSAVVGr 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 583 ---HEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRfLRLQESLATTETFKQQKVRM 641
Cdd:PRK06178 499 pdpDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
167-638 |
1.77e-20 |
|
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: 94.82 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGArALVLAPEFLEslEPDLPALRAMglHLWAAG 246
Cdd:TIGR01923 24 GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDV-QLLLTDSLLE--EKDFQADSLD--RIEAAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 247 PgthpagisdllAEVSAEVDGPvpgyLSSPQSItdtclyIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYL 325
Cdd:TIGR01923 99 R-----------YETSLSASFN----MDQIATL------MFTSGTTGKPKAVPHTFRNHYaSAVGSKENLGFTEDDNWLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 326 ALPLYHMSGslLGIV-GCMGIGATVVLKSKFSagQFWEDCQQHRVTVFQYI-GELCRYLvnQPPSKAERGHKVRLavGSG 403
Cdd:TIGR01923 158 SLPLYHISG--LSILfRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVpTQLNRLL--DEGGHNENLRKILL--GGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 404 LRPDTWERFVRRFGpLQVLETYGLTEGN----VATINYTGQRGAVGRASwlykhifPFSLIRYDVttgePIRDPQGHCMA 479
Cdd:TIGR01923 230 AIPAPLIEEAQQYG-LPIYLSYGMTETCsqvtTATPEMLHARPDVGRPL-------AGREIKIKV----DNKEGHGEIMV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 480 TSPGEpgllvapvsqqspFLGYaggpeLAQGKLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTE 559
Cdd:TIGR01923 298 KGANL-------------MKGY-----LYQGELTPAFEQQG--WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 560 VAEVFEALDFLQEVNVygVTVPGHE-GRAGMAALVLRPPhaLDLMQLYTHVSENLPPYARP-RFLRLQEsLATTETFKQQ 637
Cdd:TIGR01923 358 IETVLYQHPGIQEAVV--VPKPDAEwGQVPVAYIVSESD--ISQAKLIAYLTEKLAKYKVPiAFEKLDE-LPYNASGKIL 432
|
.
gi 1393643644 638 K 638
Cdd:TIGR01923 433 R 433
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
164-643 |
5.55e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 93.77 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVPTALRRGP--LLHCLRSCGARALVLAPEFleslepdlpalRAMGLH 241
Cdd:PRK06839 50 VKKGERIAILSQNSLEYIVLLFAIAKVEC--IAVPLNIRLTEneLIFQLKDSGTTVLFVEKTF-----------QNMALS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 LWAAGPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSItdtClyiFTSGTTGLPKAARIShlkilQCQGFYQlcGVHQ-- 319
Cdd:PRK06839 117 MQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFII---C---YTSGTTGKPKGAVLT-----QENMFWN--ALNNtf 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 ------EDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERG 393
Cdd:PRK06839 184 aidltmHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 394 HKVRLAVGSGLR-PDTWER-FVRR---FGplqvlETYGLTEGN-----VATINYTGQRGAVGRaswlykhifPFSLIRYD 463
Cdd:PRK06839 264 QSVRWFYNGGAPcPEELMReFIDRgflFG-----QGFGMTETSptvfmLSEEDARRKVGSIGK---------PVLFCDYE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 464 VTtgepirDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGGPELAQgkllkDVFRPGdvFFNTGDLLVCDDQGFLRFHDR 543
Cdd:PRK06839 330 LI------DENKN--KVEVGEVGELL--IRGPNVMKEYWNRPDATE-----ETIQDG--WLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 544 TGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLR 623
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHV-KWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIV 471
|
490 500
....*....|....*....|
gi 1393643644 624 LQESLATTETFKQQKVRMAN 643
Cdd:PRK06839 472 FLKELPKNATGKIQKAQLVN 491
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
164-635 |
8.84e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 93.04 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPdLPALRAMGLHLW 243
Cdd:PRK08276 33 LREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAE-LAAELPAGVPLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPaGISDLLAEVSAEVDGPVPgylssPQSITDTCLYifTSGTTGLPKAAR--ISHLKILQCQG------FYQLC 315
Cdd:PRK08276 112 LVVAGPVP-GFRSYEEALAAQPDTPIA-----DETAGADMLY--SSGTTGRPKGIKrpLPGLDPDEAPGmmlallGFGMY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVhqEDVIYLA-LPLYHmSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAER-- 392
Cdd:PRK08276 184 GG--PDSVYLSpAPLYH-TAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARyd 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 --GHKVRLAVGSGLRPDTWERFVRRFGPLqVLETYGLTEGNVATI----NYTGQRGAVGRAsWLykhifpfSLIRydvtt 466
Cdd:PRK08276 261 vsSLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGGVTVitseDWLAHPGSVGKA-VL-------GEVR----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 467 gepIRDPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDVFRPGDvFFNTGDLLVCDDQGFLRFHDRTGD 546
Cdd:PRK08276 327 ---ILDEDGNELP--PGEIGTVY--FEMDGYPFEYHNDPEKT-----AAARNPHG-WVTVGDVGYLDEDGYLYLTDRKSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 547 TFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLRPPHALD---LMQLYTHVSENLPPYARPRFL 622
Cdd:PRK08276 394 MIISGGVNIYPQEIENLLVTHPKVADVAVFG--VPDEEmGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSI 471
|
490
....*....|...
gi 1393643644 623 RLQESLATTETFK 635
Cdd:PRK08276 472 DFEDELPRTPTGK 484
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
164-628 |
1.61e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 92.26 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGARALVLAPEFleslepdlpalramglh 241
Cdd:PRK06145 49 IGQGDVVALLMKNSAAFLELAFAASYLG--AVFLPINYRLAAdeVAYILGDAGAKLLLVDEEF----------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 lwAAGPGT-HPAGISDLLAEVSAEVDGPvPGYLSSPQSI---TDTCLYIFTSGTTGLPKAARISHLKiLQCQGFYQLC-- 315
Cdd:PRK06145 110 --DAIVALeTPKIVIDAAAQADSRRLAQ-GGLEIPPQAAvapTDLVRLMYTSGTTDRPKGVMHSYGN-LHWKSIDHVIal 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIG-ELCRYLVNQPPSKAERGh 394
Cdd:PRK06145 186 GLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPvMLSRVLTVPDRDRFDLD- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 395 KVRLAVGSGLRpdTWERFVRRFGPL----QVLETYGLTEG-NVATINYTGQR----GAVGRAswlykhiFPFSLIRydvt 465
Cdd:PRK06145 265 SLAWCIGGGEK--TPESRIRDFTRVftraRYIDAYGLTETcSGDTLMEAGREiekiGSTGRA-------LAHVEIR---- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 466 tgepIRDPQGHCMATS-PGEPGLLVAPVSQqspflGYAGGPELAQGKLLKDVFRPGDVFFntgdllvCDDQGFLRFHDRT 544
Cdd:PRK06145 332 ----IADGAGRWLPPNmKGEICMRGPKVTK-----GYWKDPEKTAEAFYGDWFRSGDVGY-------LDEEGFLYLTDRK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 545 GDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVtvpgHEGRAG---MAALVLRPPHALDLMQLYTHVSENLPPYARPRF 621
Cdd:PRK06145 396 KDMIISGGENIASSEVERVIYELPEVAEAAVIGV----HDDRWGeriTAVVVLNPGATLTLEALDRHCRQRLASFKVPRQ 471
|
....*..
gi 1393643644 622 LRLQESL 628
Cdd:PRK06145 472 LKVRDEL 478
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
257-635 |
2.66e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 92.02 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 257 LLAEVSAEVDGPVPgYLSSPQSitDTCLYIFTSGTTGLPKAARISHLKILQcqgfYQLCGVH-------QEDVIYLALPL 329
Cdd:PRK06710 186 LWNSVEKEVNTGVE-VPCDPEN--DLALLQYTGGTTGFPKGVMLTHKNLVS----NTLMGVQwlynckeGEEVVLGVLPF 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 330 YHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV-GSGLRP-D 407
Cdd:PRK06710 259 FHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPvE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 408 TWERFVRRFGPlQVLETYGLTEGNVATinytgqrgavgRASWLYKHIFPFSLirydvttGEPIRDPQGHCM------ATS 481
Cdd:PRK06710 339 VQEKFETVTGG-KLVEGYGLTESSPVT-----------HSNFLWEKRVPGSI-------GVPWPDTEAMIMsletgeALP 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 482 PGEPGLLVapVSQQSPFLGYAGGPELAQGKLlkdvfrpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVA 561
Cdd:PRK06710 400 PGEIGEIV--VKGPQIMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVE 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393643644 562 EVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PRK06710 471 EVLYEHEKVQEVVTIGVPDP-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGK 543
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
66-646 |
4.36e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 91.32 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 66 SLAWRLAELAQQRAAHTFLIH----GSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaa 141
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAG-LLALG----------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 142 agsgaefaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLA 221
Cdd:COG1022 62 ----------------------VKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 222 PEF----LESLEPDLPALRamglHLW---AAGPGTHPAGIS--DLLAE-VSAEVDGPVPGYLSSPQSiTDTCLYIFTSGT 291
Cdd:COG1022 120 DQEqldkLLEVRDELPSLR----HIVvldPRGLRDDPRLLSldELLALgREVADPAELEARRAAVKP-DDLATIIYTSGT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 292 TGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGiVGCMGIGATVVLKSkfSAGQFWEDCQQHRVT 370
Cdd:COG1022 195 TGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLSFLPLAHVFERTVS-YYALAAGATVAFAE--SPDTLAEDLREVKPT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 371 VF-------------------------------------QYIgelCRYLVNQPPSKAER------------------GHK 395
Cdd:COG1022 272 FMlavprvwekvyagiqakaeeagglkrklfrwalavgrRYA---RARLAGKSPSLLLRlkhaladklvfsklrealGGR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 396 VRLAV--GSGLRPDTwERFVRRFGpLQVLETYGLTE-GNVATINYTGQ--RGAVGRAswlykhiFPFSLIRydvttgepI 470
Cdd:COG1022 349 LRFAVsgGAALGPEL-ARFFRALG-IPVLEGYGLTEtSPVITVNRPGDnrIGTVGPP-------LPGVEVK--------I 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 rdpqghcmatspGEPG-LLVapvsqQSP--FLGYAGGPELAqgkllKDVFRPgDVFFNTGDLLVCDDQGFLRFHDRTGDT 547
Cdd:COG1022 412 ------------AEDGeILV-----RGPnvMKGYYKNPEAT-----AEAFDA-DGWLHTGDIGELDEDGFLRITGRKKDL 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 548 FrwK---GENVATTEVAEVFEALDFLQEVNVYGvtvpghEGRAGMAALVlrpphALDLmqlythvsENLPPYARPRFLRL 624
Cdd:COG1022 469 I--VtsgGKNVAPQPIENALKASPLIEQAVVVG------DGRPFLAALI-----VPDF--------EALGEWAEENGLPY 527
|
650 660
....*....|....*....|....*..
gi 1393643644 625 Q--ESLATTETFK---QQKVRMANEGF 646
Cdd:COG1022 528 TsyAELAQDPEVRaliQEEVDRANAGL 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
164-631 |
6.80e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 90.50 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFV-PTALRRgPLLHCLRSCGARALVLAPEFLESLEP---DLPA----L 235
Cdd:PRK08974 71 LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVnPLYTPR-ELEHQLNDSGAKAIVIVSNFAHTLEKvvfKTPVkhviL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 236 RAMGLHLwAAGPGThpagisdLLAEVSAEVDGPVPGYlSSPQSIT---------------------DTCLYIFTSGTTGL 294
Cdd:PRK08974 150 TRMGDQL-STAKGT-------LVNFVVKYIKRLVPKY-HLPDAISfrsalhkgrrmqyvkpelvpeDLAFLQYTGGTTGV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 295 PKAARISHLKI----LQCQGFYQLCGVHQEDVIYLALPLYH----MSGSLLGIVgcMGIGATVVLKSKFSAGqFWEDCQQ 366
Cdd:PRK08974 221 AKGAMLTHRNMlanlEQAKAAYGPLLHPGKELVVTALPLYHifalTVNCLLFIE--LGGQNLLITNPRDIPG-FVKELKK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 367 HRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLR-----PDTWERFVRRFgplqVLETYGLTEGN----VATINY 437
Cdd:PRK08974 298 YPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAvqqavAERWVKLTGQY----LLEGYGLTECSplvsVNPYDL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 438 TGQRGAVGraswlykhiFPFSlirydvTTGEPIRDPQGHCMAtsPGEPGLLVAPVSQQspFLGYAGGPElAQGKLLKDvf 517
Cdd:PRK08974 374 DYYSGSIG---------LPVP------STEIKLVDDDGNEVP--PGEPGELWVKGPQV--MLGYWQRPE-ATDEVIKD-- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 518 rpGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHEGRAGMAALVLRPP 597
Cdd:PRK08974 432 --G--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVG--VPSEVSGEAVKIFVVKKD 505
|
490 500 510
....*....|....*....|....*....|....
gi 1393643644 598 HALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK08974 506 PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKS 539
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
166-644 |
1.97e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.04 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALvLAPEFLESLEP---------DLPALR 236
Cdd:PRK06087 73 PGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF-FAPTLFKQTRPvdlilplqnQLPQLQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 237 AMGLHLWAAgpgthPAGISDLLAEVSAevDGPVpgyLSSPQSIT--DTCLYIFTSGTTGLPKAARISHLKILQCQGFY-Q 313
Cdd:PRK06087 152 QIVGVDKLA-----PATSSLSLSQIIA--DYEP---LTTAITTHgdELAAVLFTSGTEGLPKGVMLTHNNILASERAYcA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 314 LCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVT----VFQYIGELCRYLVNQPPsk 389
Cdd:PRK06087 222 RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDLLNLLEKQPA-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 390 aeRGHKVRL------AVGSGLRPDTWERFVRrfgplqVLETYGLTEGNvatinytgqrgavgraswlyKHIF-PF--SLI 460
Cdd:PRK06087 300 --DLSALRFflcggtTIPKKVARECQQRGIK------LLSVYGSTESS--------------------PHAVvNLddPLS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 461 RYDVTTGEP-----IRDPQGHCMATSPGEPGLLVAPVSQQspFLGYAGGPELAqGKLLKDvfrpgDVFFNTGDLLVCDDQ 535
Cdd:PRK06087 352 RFMHTDGYAaagveIKVVDEARKTLPPGCEGEEASRGPNV--FMGYLDEPELT-ARALDE-----EGWYYSGDLCRMDEA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 536 GFLRFHDRTGDTFRWKGENVATTEVAEVFeaLDFLQEVNVYGVTVPGHE-GRAGMAALVLRPP-HALDLMQLYTHVSEN- 612
Cdd:PRK06087 424 GYIKITGRKKDIIVRGGENISSREVEDIL--LQHPKIHDACVVAMPDERlGERSCAYVVLKAPhHSLTLEEVVAFFSRKr 501
|
490 500 510
....*....|....*....|....*....|..
gi 1393643644 613 LPPYARPRFLRLQESLATTETFKQQKVRMANE 644
Cdd:PRK06087 502 VAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
167-639 |
2.03e-18 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 89.09 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPE--FLESLEPDLPALRAMGLHLWA 244
Cdd:cd05970 72 GDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 245 AGPgtHPAGISDLLAEV-SAEVDGPVPGYLSSPQSiTDTCLYIFTSGTTGLPKAARISHL----KILQCQGFYQLcgvhQ 319
Cdd:cd05970 152 GDP--VPEGWIDFRKLIkNASPDFERPTANSYPCG-EDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNV----R 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALP----LYHMSGSLLG--IVGCmgigATVVLK-SKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAER 392
Cdd:cd05970 225 EGGLHLTVAdtgwGKAVWGKIYGqwIAGA----AVFVYDyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 GhKVRLAVGSG--LRPDTWERFvRRFGPLQVLETYGLTEGNVATINYTGQR---GAVGRASWLYkhifPFSLIRYD---V 464
Cdd:cd05970 301 S-SLRYCTTAGeaLNPEVFNTF-KEKTGIKLMEGFGQTETTLTIATFPWMEpkpGSMGKPAPGY----EIDLIDREgrsC 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 465 TTGEpirdpQGH-CMATSPGEP-GLlvapvsqqspFLGYAGGPELAQgkllkDVFRPGdvFFNTGDLLVCDDQGFLRFHD 542
Cdd:cd05970 375 EAGE-----EGEiVIRTSKGKPvGL----------FGGYYKDAEKTA-----EVWHDG--YYHTGDAAWMDEDGYLWFVG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 543 RTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVL----RPPHALDlMQLYTHVSENLPPYAR 618
Cdd:cd05970 433 RTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDP-IRGQVVKATIVLakgyEPSEELK-KELQDHVKKVTAPYKY 510
|
490 500
....*....|....*....|.
gi 1393643644 619 PRFLRLQESLATTETFKQQKV 639
Cdd:cd05970 511 PRIVEFVDELPKTISGKIRRV 531
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
278-635 |
2.39e-18 |
|
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: 87.92 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 278 SITDTCLYIFTSGTTGLPKAARISHLKIlQCQGFYQLC--GVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKF 355
Cdd:cd05935 82 ELDDLALIPYTSGTTGLPKGCMHTHFSA-AANALQSAVwtGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 356 SAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSG--LRPDTWERFVRRFGpLQVLETYGLTEGNVA 433
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETMSQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TINYTGQRgavGRASWLYKHIFPFSLIRYDVTTGEPIrdpqghcmatSPGEPGLLVapVSQQSPFLGYAGGPELAQGKLL 513
Cdd:cd05935 240 THTNPPLR---PKLQCLGIP*FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQIFKGYWNRPEETEESFI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 514 KDvfrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHE-GRAGMAAL 592
Cdd:cd05935 305 EI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV--ISVPDERvGEEVKAFI 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1393643644 593 VLRPPH--ALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd05935 380 VLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
196-620 |
2.71e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 88.56 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 196 FVPTALRRGP--LLHCLRSCGARALVLAPEFLESLEpdlpALRAMGLHL-WAAGPGTHPAGIsDLLAEVSAEVDGPVPgy 272
Cdd:PRK07470 84 WVPTNFRQTPdeVAYLAEASGARAMICHADFPEHAA----AVRAASPDLtHVVAIGGARAGL-DYEALVARHLGARVA-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 273 lssPQSIT--DTCLYIFTSGTTGLPKAARISHLKIlqcqGFY---QLC----GVHQEDVIYLALPLYHMSGSLLGIVGCM 343
Cdd:PRK07470 157 ---NAAVDhdDPCWFFFTSGTTGRPKAAVLTHGQM----AFVitnHLAdlmpGTTEQDASLVVAPLSHGAGIHQLCQVAR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 344 GIgATVVLKS-KFSAGQFWEDCQQHRVTVFQYIGELCRYLVnQPPSKAERGH-KVRLAVGSG---LRPDTwERFVRRFGP 418
Cdd:PRK07470 230 GA-ATVLLPSeRFDPAEVWALVERHRVTNLFTVPTILKMLV-EHPAVDRYDHsSLRYVIYAGapmYRADQ-KRALAKLGK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 419 LQVlETYGLTE--GNVATINYTGQRGAVGRASwlykHIFPFSLIRydvtTGE--PIRDPQGHCMAtsPGEPGLLVapVSQ 494
Cdd:PRK07470 307 VLV-QYFGLGEvtGNITVLPPALHDAEDGPDA----RIGTCGFER----TGMevQIQDDEGRELP--PGETGEIC--VIG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 495 QSPFLGYAGGPElAQGKllkdVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVN 574
Cdd:PRK07470 374 PAVFAGYYNNPE-ANAK----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1393643644 575 VYGVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPR 620
Cdd:PRK07470 447 VLGVPDPVW-GEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
164-620 |
4.14e-18 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 87.95 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEfleslEPDLPALRAMGLHLW 243
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD-----AQVMDAIFQSGVRVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AagpgthpagISDLLAEVSAEVDGPVPGylSSPQSITDTCLYIFTSGTTGLPKAARISHLKI--------LQCQGFYqlc 315
Cdd:cd05923 125 A---------LSDLVGLGEPESAGPLIE--DPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAesrvlfmsTQAGLRH--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHqEDVIYLaLPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVN---QPPSKAER 392
Cdd:cd05923 191 GRH-NVVLGL-MPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAaaeFAGLKLSS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 GHKVRLAVGSglRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWlykhifpFSLIRYDVTTGEPIRd 472
Cdd:cd05923 269 LRHVTFAGAT--MPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGF-------FSEVRIVRIGGSPDE- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 473 pqghcmATSPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLkdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKG 552
Cdd:cd05923 339 ------ALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 553 ENVATTEVAEVFEALDFLQEVNVYGVTvpghEGRAG--MAALVLRPPHAL--DLMQLYTHVSEnLPPYARPR 620
Cdd:cd05923 406 ENIHPSEIERVLSRHPGVTEVVVIGVA----DERWGqsVTACVVPREGTLsaDELDQFCRASE-LADFKRPR 472
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
166-611 |
5.97e-18 |
|
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: 87.39 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrtaFVP-----TALRRGpLLHCLRSCGARALVLAPEFLESL-EPDLPALRAmg 239
Cdd:cd05909 30 EGENVGVMLPPSAGGALANFALALSG----KVPvmlnyTAGLRE-LRACIKLAGIKTVLTSKQFIEKLkLHHLFDVEY-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 240 lhlwaagpgthPAGI---SDLLAEVS--------AEVDGPVPGYL----SSPQSITDTCLYIFTSGTTGLPKAARISHLK 304
Cdd:cd05909 103 -----------DARIvylEDLRAKISkadkckafLAGKFPPKWLLrifgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 305 ILQCQgfYQLCGV---HQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLK-SKFSAGQFWEDCQQHRVTVFQYIGELCR 380
Cdd:cd05909 172 LLANV--EQITAIfdpNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpNPLDYKKIPELIYDKKATILLGTPTFLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 381 YLVNQppSKAERGHKVRLAV--GSGLRPDTWERFVRRFGpLQVLETYGLTEGN-VATIN---YTGQRGAVGRaswlykhi 454
Cdd:cd05909 250 GYARA--AHPEDFSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECSpVISVNtpqSPNKEGTVGR-------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 455 fPFSLIRYDvttgepIRDPQGHCMATSpGEPGLLVapVSQQSPFLGYAGGPElaqgkllKDVFRPGDVFFNTGDLLVCDD 534
Cdd:cd05909 319 -PLPGMEVK------IVSVETHEEVPI-GEGGLLL--VRGPNVMLGYLNEPE-------LTSFAFGDGWYDTGDIGKIDG 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393643644 535 QGFLRFHDRTGDTFRWKGENVATTEVAE-VFEALDflQEVNVYGVTVPghEGRAGMAALVLRPPHALDLMQLYTHVSE 611
Cdd:cd05909 382 EGFLTITGRLSRFAKIAGEMVSLEAIEDiLSEILP--EDNEVAVVSVP--DGRKGEKIVLLTTTTDTDPSSLNDILKN 455
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
192-620 |
8.28e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 87.12 E-value: 8.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 192 LRTAFVPTALRrgpllHCLRSCGARALVLAPEFLESLEPDLpalramglhlwAAGPG-THPAGISDLLAEVSAEVDGPVP 270
Cdd:PRK13382 123 LNTSFAGPALA-----EVVTREGVDTVIYDEEFSATVDRAL-----------ADCPQaTRIVAWTDEDHDLTVEVLIAAH 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 271 GYLSSPQSITDTCLYIFTSGTTGLPKAARISHLK-ILQCQGFYQLCGVHQEDVIYLALPLYHMSG-SLLGIVGCMGigAT 348
Cdd:PRK13382 187 AGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGgIGTLKAILDRTPWRAEEPTVIVAPMFHAWGfSQLVLAASLA--CT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 349 VVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPP----SKAERGHKVRLAVGSGLRPDTWERFVRRFGPLqVLET 424
Cdd:PRK13382 265 IVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevrnRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 425 YGLTE-GNVATINytgqrgavgraswlykhifPFSLIRYDVTTGEP-------IRDPQGHCMATspGEPGLLVapVSQQS 496
Cdd:PRK13382 344 YNATEaGMIATAT-------------------PADLRAAPDTAGRPaegteirILDQDFREVPT--GEVGTIF--VRNDT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 497 PFLGYAGGPElaqgkllKDvFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVY 576
Cdd:PRK13382 401 QFDGYTSGST-------KD-FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVI 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1393643644 577 GVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPR 620
Cdd:PRK13382 471 GVDDEQY-GQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPR 513
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
286-632 |
1.07e-17 |
|
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: 85.01 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKIL----QCQGFYQLCGvhqEDVIYLALPLYHMSGSLLGIVgCMGIGATVVLKSKFSAGQFW 361
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIaanlQLIHAMGLTE---ADVYLNMLPLFHIAGLNLALA-TFHAGGANVVMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 362 EDCQQHRVTVFqyiGELCRYLVNQPPSKAERGHKVR-LAVGSGLR-PDTWERFvRRFGPLQVLETYGLTE--GNVATINY 437
Cdd:cd17637 82 ELIEEEKVTLM---GSFPPILSNLLDAAEKSGVDLSsLRHVLGLDaPETIQRF-EETTGATFWSLYGQTEtsGLVTLSPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 438 TGQRGAVGRASwlykhifPFSLIRYDVTTGEPIRdpqghcmatsPGEPGLLVApvsqQSP--FLGYAGGPELAQgkllkD 515
Cdd:cd17637 158 RERPGSAGRPG-------PLVRVRIVDDNDRPVP----------AGETGEIVV----RGPlvFQGYWNLPELTA-----Y 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 516 VFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWK--GENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALV 593
Cdd:cd17637 212 TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDP-KWGEGIKAVCV 288
|
330 340 350
....*....|....*....|....*....|....*....
gi 1393643644 594 LRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTE 632
Cdd:cd17637 289 LKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTA 327
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
166-619 |
1.41e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 86.10 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGARALVLApeflESLEPDLPALRAMGLHLW 243
Cdd:cd12117 46 PGDVVGVLAERSPELVVALLAVLKAG--AAYVPLDPELPAerLAFMLADAGAKVLLTD----RSLAGRAGGLEVAVVIDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGthpagisdllaevsaevDGPVPGylsSPQSITDTCLYIFTSGTTGLPKAARISHLKILQC---QGFYQLCGvhqE 320
Cdd:cd12117 120 ALDAG-----------------PAGNPA---VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLvknTNYVTLGP---D 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPL------YHMSGSLLGivgcmgiGATVVLKSK---FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSkAE 391
Cdd:cd12117 177 DRVLQTSPLafdastFEIWGALLN-------GARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLADEDPE-CF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 392 RGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASwlykhifpfslirydVTTGEPIR 471
Cdd:cd12117 249 AGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGS---------------IPIGRPIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 -------DPQGHCMAtsPGEPGLLV---APVSqqspfLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFH 541
Cdd:cd12117 314 ntrvyvlDEDGRPVP--PGVPGELYvggDGLA-----LGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 542 DRTGDTFRWKGENVattEVAEVFEALDFLQEVNVYGVTVpgHEGRAGMAALV--LRPPHALDLMQLYTHVSENLPPYARP 619
Cdd:cd12117 387 GRIDDQVKIRGFRI---ELGEIEAALRAHPGVREAVVVV--REDAGGDKRLVayVVAEGALDAAELRAFLRERLPAYMVP 461
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
286-631 |
1.67e-17 |
|
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: 85.76 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKIL----QCQGFYQLcgvhQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK---FSAG 358
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVsftnWMLSDFPL----GPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 359 QFWEDCQQHRVTVF---QYIGELCRYLvnqPPSKAERGHKVRLAVGSG--LRPDTWERFVRRFGPLQVLETYGLTEGNVA 433
Cdd:cd05945 179 QLFRFLAEHGITVWvstPSFAAMCLLS---PTFTPESLPSLRHFLFCGevLPHKTARALQQRFPDARIYNTYGPTEATVA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TinytgqrgavgraswLYKHIFPFSLIRYD-VTTGEP-------IRDPQGHCMatSPGEPGLLVapVSQQSPFLGYAGGP 505
Cdd:cd05945 256 V---------------TYIEVTPEVLDGYDrLPIGYAkpgaklvILDEDGRPV--PPGEKGELV--ISGPSVSKGYLNNP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 506 ELAQGKLLKDVFRPGdvfFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEG 585
Cdd:cd05945 317 EKTAAAFFPDEGQRA---YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYKGEK 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1393643644 586 RAGMAALVLRPPH--ALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:cd05945 392 VTELIAFVVPKPGaeAGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
164-635 |
2.01e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.08 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLE---PDLPALRAMgl 240
Cdd:PRK08751 73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqviADTPVKQVI-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 hlwaagpgthPAGISDLLAEVSAE--------VDGPVPGY-------------LSSPQSIT-------DTCLYIFTSGTT 292
Cdd:PRK08751 151 ----------TTGLGDMLGFPKAAlvnfvvkyVKKLVPEYringairfrealaLGRKHSMPtlqiepdDIAFLQYTGGTT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 293 GLPKAARISH----LKILQCQGFYQLCGVHQE--DVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK-FSAGQFWEDCQ 365
Cdd:PRK08751 221 GVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEgcEVVITALPLYHIFALTANGLVFMKIGGCNHLISNpRDMPGFVKELK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 366 QHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGL--RPDTWERFVRRFGpLQVLETYGLTEGN-VATINytgqrg 442
Cdd:PRK08751 301 KTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTG-LTLVEAYGLTETSpAACIN------ 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 443 avgraswlykhifPFSLIRYDVTTGEPI-------RDPQGHCMATspGEPGLLVAPVSQQspFLGYAGGPElAQGKLLKd 515
Cdd:PRK08751 374 -------------PLTLKEYNGSIGLPIpstdaciKDDAGTVLAI--GEIGELCIKGPQV--MKGYWKRPE-ETAKVMD- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 516 vfrpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHEGRAGMAALVLR 595
Cdd:PRK08751 435 ----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEKSGEIVKVVIVK 508
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1393643644 596 PPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PRK08751 509 KDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGK 548
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
166-529 |
3.29e-17 |
|
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: 84.24 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVP----TALRRgpLLHCLRSCGARALVLAPEFLESLepdlpalramglh 241
Cdd:TIGR01733 24 PGDRVAVLLERSAELVVAILAVLKAG--AAYVPldpaYPAER--LAFILEDAGARLLLTDSALASRL------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 lwaagPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQE 320
Cdd:TIGR01733 87 -----AGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIyLALPLYHMSGSLLGIVGCMGIGATVVL------KSKFSAGQFWEDcqQHRVTVFQ---YIGELCrylvnqPPSKAE 391
Cdd:TIGR01733 162 DRV-LQFASLSFDASVEEIFGALLAGATLVVppedeeRDDAALLAALIA--EHPVTVLNltpSLLALL------AAALPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 392 RGHKVRLAVGSG--LRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWL-YKHifPFSLIRYDVTtgE 468
Cdd:TIGR01733 233 ALASLRLVILGGeaLTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpIGR--PLANTRLYVL--D 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 469 PIRDPQGhcmatsPGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDVFRPGD--VFFNTGDL 529
Cdd:TIGR01733 309 DDLRPVP------VGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDL 363
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
281-638 |
5.13e-17 |
|
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: 83.08 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISH------LKILQCQGFyqlcGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK 354
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANktffavPDILQKEGL----NWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 355 FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRP-DTWERFVRRFGPLQVLETYGLTEGNVA 433
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TINYTGQR----GAVGRaswlykhifPFSLIRYDVTTGEPIRDPQghcmatspGEPGLLVApvsqQSP--FLGYAGGPEL 507
Cdd:cd17635 158 LCLPTDDDsieiNAVGR---------PYPGVDVYLAATDGIAGPS--------ASFGTIWI----KSPanMLGYWNNPER 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 508 AQGKLLkdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTvpghegRA 587
Cdd:cd17635 217 TAEVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS------DE 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393643644 588 GMAALVlrpphaldlmQLYTHVSE----------------NLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd17635 284 EFGELV----------GLAVVASAeldenairalkhtirrELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
284-635 |
8.42e-17 |
|
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: 82.07 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 284 LYI-FTSGTTGLPKAARISH---LKILQCQ--GFYqlcgVHQEDVIYLALPLYHmSGSLLGIVGCMGIGATVVLKSKFSA 357
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSErswIESFVCNedLFN----ISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 358 GQFWEDCQQHRVTVFQYIGELCR--YLVNQPPSKAerghKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATI 435
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQalARTLEPESKI----KSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 436 NYTGQ---RGAVGRaswlykhIFPFSLIRydvttgepIRDPQGhcmatspGEPGLLVApvsqQSP--FLGYAGGPELAQG 510
Cdd:cd17633 154 NFNQEsrpPNSVGR-------PFPNVEIE--------IRNADG-------GEIGKIFV----KSEmvFSGYVRGGFSNPD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 511 KllkdvfrpgdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTvpgHEGRaGMA 590
Cdd:cd17633 208 G-----------WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP---DARF-GEI 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1393643644 591 ALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd17633 273 AVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
164-638 |
9.38e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 83.59 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVL---APEFLESLEPDLPALRamgL 240
Cdd:PRK13391 46 LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITsaaKLDVARALLKQCPGVR---H 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HLWAAGPGTHPaGISDLLAEVSAEVDGPVPGylsspQSITDTCLYifTSGTTGLPKAAR--ISHLKILQCQGFYQLCGV- 317
Cdd:PRK13391 123 RLVLDGDGELE-GFVGYAEAVAGLPATPIAD-----ESLGTDMLY--SSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQRl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 318 --HQEDVIYLA-LPLYHmSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGEL-CRYLvnQPPSKAERG 393
Cdd:PRK13391 195 wgFRSDMVYLSpAPLYH-SAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMfSRML--KLPEEVRDK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 394 HKVrlavgSGLR----------PDTWERFVRRFGPLqVLETYGLTEGNVATINYTGQ----RGAVGRAswlykhIFpfsl 459
Cdd:PRK13391 272 YDL-----SSLEvaihaaapcpPQVKEQMIDWWGPI-IHEYYAATEGLGFTACDSEEwlahPGTVGRA------MF---- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 460 irydvttGEP-IRDPQGHCMatSPGEPGLLVapVSQQSPFlGYAGGPELAQGKllkdvfRPGDVFFNT-GDLLVCDDQGF 537
Cdd:PRK13391 336 -------GDLhILDDDGAEL--PPGEPGTIW--FEGGRPF-EYLNDPAKTAEA------RHPDGTWSTvGDIGYVDEDGY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 538 LRFHDRTGDTFRWKG--------ENVATTEvAEVFEAL-------DFLQEVNVYGVTVPGHEGRAGMAAlvlrpphaldl 602
Cdd:PRK13391 398 LYLTDRAAFMIISGGvniypqeaENLLITH-PKVADAAvfgvpneDLGEEVKAVVQPVDGVDPGPALAA----------- 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 1393643644 603 mQLYTHVSENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:PRK13391 466 -ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYK 500
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
164-631 |
9.53e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 83.78 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLapefleslEPDLPALRAMGLHLW 243
Cdd:PRK05852 65 LLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI--------DADGPHDRAEPTTRW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AagPGTHPAGISDLLAEVSAEVDGPVPGYL----SSPQSI-TDTCLYIFTSGTTGLPKAARISHLKILQ-----CQGfYQ 313
Cdd:PRK05852 137 W--PLTVNVGGDSGPSGGTLSVHLDAATEPtpatSTPEGLrPDDAMIMFTGGTTGLPKMVPWTHANIASsvraiITG-YR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 314 LcgvHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVL--KSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAE 391
Cdd:PRK05852 214 L---SPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 392 RG--HKVRL--AVGSGLRPDTWERFVRRFGPlQVLETYGLTEG--NVATINYTG---------QRGAVGRaswlykhifp 456
Cdd:PRK05852 291 GRkpAALRFirSCSAPLTAETAQALQTEFAA-PVVCAFGMTEAthQVTTTQIEGigqtenpvvSTGLVGR---------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 457 fslirydvTTGEPIR--DPQGH-CMATSPGEPGLLVAPVSQqspflGYAGGPELAQGKLLkdvfrpgDVFFNTGDLLVCD 533
Cdd:PRK05852 360 --------STGAQIRivGSDGLpLPAGAVGEVWLRGTTVVR-----GYLGDPTITAANFT-------DGWLRTGDLGSLS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 534 DQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENL 613
Cdd:PRK05852 420 AAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLY-GEAVAAVIVPRESAPPTAEELVQFCRERL 498
|
490
....*....|....*...
gi 1393643644 614 PPYARPRFLRLQESLATT 631
Cdd:PRK05852 499 AAFEIPASFQEASGLPHT 516
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
164-628 |
1.13e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 83.39 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGARALVLAPEFLESLEPdlPALRAMGLH 241
Cdd:PRK07514 50 VKPGDRVAVQVEKSPEALALYLATLRAGA--VFLPlnTAYTLAELDYFIGDAEPALVVCDPANFAWLSK--IAAAAGAPH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 LW---AAGPGThpagISDLLAEVSAEVDgPVPGYLSSPQSItdtcLYifTSGTTGLPKAARISHLKIL-QCQGFYQLCGV 317
Cdd:PRK07514 126 VEtldADGTGS----LLEAAAAAPDDFE-TVPRGADDLAAI----LY--TSGTTGRSKGAMLSHGNLLsNALTLVDYWRF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 318 HQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEdcQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVR 397
Cdd:PRK07514 195 TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLA--LMPRATVMMGVPTFYTRLLQEPRLTREAAAHMR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 398 LAV-GSG-LRPDTWERFVRRFGpLQVLETYGLTEGNVATIN-YTGQR--GAVGraswlykhiFPF---SLIRYDVTTGEP 469
Cdd:PRK07514 273 LFIsGSApLLAETHREFQERTG-HAILERYGMTETNMNTSNpYDGERraGTVG---------FPLpgvSLRVTDPETGAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 470 IrdpqghcmatSPGEPGLLvaPVSQQSPFLGYAGGPELAQGKllkdvFRPgDVFFNTGDLLVCDDQGFLRFHDRTGDTFR 549
Cdd:PRK07514 343 L----------PPGEIGMI--EVKGPNVFKGYWRMPEKTAEE-----FRA-DGFFITGDLGKIDERGYVHIVGRGKDLII 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393643644 550 WKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESL 628
Cdd:PRK07514 405 SGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDEL 482
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
286-638 |
1.78e-16 |
|
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: 82.01 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKA-----------ARISHLKIlqcqgfyqlcGVHQEDVIYLALPLYHMSGslLGIVGCMGI-GATVVLKS 353
Cdd:cd05912 83 MYTSGTTGKPKGvqqtfgnhwwsAIGSALNL----------GLTEDDNWLCALPLFHISG--LSILMRSVIyGMTVYLVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 354 KFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPlqVLETYGLTE--GN 431
Cdd:cd05912 151 KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIP--VYQSYGMTEtcSQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 432 VATINytgqrgavgraswlykhiFPFSLIRYDvTTGEP-------IRDPQGhcmatSPGEPG--LLVAP-VSQqspflGY 501
Cdd:cd05912 229 IVTLS------------------PEDALNKIG-SAGKPlfpvelkIEDDGQ-----PPYEVGeiLLKGPnVTK-----GY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 502 AGGPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVT-- 579
Cdd:cd05912 280 LNRPDAT-----EESFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPdd 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 580 ----VPghegragMAALVLRPPhaLDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd05912 353 kwgqVP-------VAFVVSERP--ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
164-593 |
2.10e-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: 82.26 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTafVPTALRRGP--LLHCLRSCGARALVlapefleslepdlpalramglh 241
Cdd:cd05907 27 VEPGDRVAILSRNRPEWTIADLAILAIGAVP--VPIYPTSSAeqIAYILNDSEAKALF---------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 lwaagpgthpagisdllaevsaeVDGPvpgylsspqsiTDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQE 320
Cdd:cd05907 83 -----------------------VEDP-----------DDLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSkfSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHK---VR 397
Cdd:cd05907 129 DRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKrklFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 398 LAVGSGLR----------PDTwERFVRRFGpLQVLETYGLTE-GNVATINyTGQRGAVGraswlykhifpfslirydvTT 466
Cdd:cd05907 207 LAVGGRLRfaasggaplpAEL-LHFFRALG-IPVYEGYGLTEtSAVVTLN-PPGDNRIG-------------------TV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 467 GEPIRDPqgHCMATSPGEpgLLV--APVsqqspFLGYAGGPElaqgKLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRT 544
Cdd:cd05907 265 GKPLPGV--EVRIADDGE--ILVrgPNV-----MLGYYKNPE----ATAEALDADG--WLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1393643644 545 GDTFRW-KGENVATTEVAEVFEALDFLQEVNVYGvtvpghEGRAGMAALV 593
Cdd:cd05907 330 KDLIITsGGKNISPEPIENALKASPLISQAVVIG------DGRPFLVALI 373
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
166-626 |
2.13e-16 |
|
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: 82.32 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVP--TALRRGPLLHCLRSCGARaLVLAPEFLESLEPDLPALRAMGLHLW 243
Cdd:cd17646 47 PEDRVAVLLPRSADLVVALLAVLKAG--AAYLPldPGYPADRLAYMLADAGPA-VVLTTADLAARLPAGGDVALLGDEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPAgisdllaevsAEVDGPVPGYLsspqsitdtclyIFTSGTTGLPKAARISHL----KILQCQGFYqlcGVHQ 319
Cdd:cd17646 124 AAPPATPPL----------VPPRPDNLAYV------------IYTSGSTGRPKGVMVTHAgivnRLLWMQDEY---PLGP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALPLyHMSGSLLGIVGCMGIGATVVL---KSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPpsKAERGHKV 396
Cdd:cd17646 179 GDRVLQKTPL-SFDVSVWELFWPLVAGARLVVarpGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEP--AAGSCASL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 397 RLAVGSG--LRPDTWERFVRRFG-PLQVLetYGLTEgnvATINYTGQ--RGAVGRASwlykhifpfslirydVTTGEPIR 471
Cdd:cd17646 256 RRVFCSGeaLPPELAARFLALPGaELHNL--YGPTE---AAIDVTHWpvRGPAETPS---------------VPIGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 DPQGHCMATS-----PGEPGLLV---APVSQqspflGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDR 543
Cdd:cd17646 316 NTRLYVLDDAlrpvpVGVPGELYlggVQLAR-----GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 544 TGDTFRWKGENVattEVAEVFEALDFLQEVNvyGVTVPGHEGRAG----MAALVLRPPHA-LDLMQLYTHVSENLPPYAR 618
Cdd:cd17646 391 SDDQVKIRGFRV---EPGEIEAALAAHPAVT--HAVVVARAAPAGaarlVGYVVPAAGAAgPDTAALRAHLAERLPEYMV 465
|
....*....
gi 1393643644 619 P-RFLRLQE 626
Cdd:cd17646 466 PaAFVVLDA 474
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
244-641 |
2.26e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.55 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGpGTHPAGISDLLAEVSAEvdGPVPGYLSSPQSITdtcLYIFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDV 322
Cdd:PRK09088 105 AAG-RTDVEDLAAFIASADAL--EPADTPSIPPERVS---LILFTSGTSGQPKGVMLSERNLQQtAHNFGVLGRVDAHSS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIG--ELCRYLVNQPPSKAER-GHKVRLA 399
Cdd:PRK09088 179 FLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 400 VGSGLRPDTWERFVRRFGpLQVLETYGLTEG--------NVATINytGQRGAVGRASwlykhifPfslirydvTTGEPIR 471
Cdd:PRK09088 259 TGGAPHAAEDILGWLDDG-IPMVDGFGMSEAgtvfgmsvDCDVIR--AKAGAAGIPT-------P--------TVQTRVV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 DPQGHCMAtsPGEPGLLVapVSQQSPFLGYAGGPELAQgkllkDVFrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWK 551
Cdd:PRK09088 321 DDQGNDCP--AGVPGELL--LRGPNLSPGYWRRPQATA-----RAF-TGDGWFRTGDIARRDADGFFWVVDRKKDMFISG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 552 GENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK09088 391 GENVYPAEIEAVLADHPGIRECAVVGMADA-QWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRT 469
|
410
....*....|
gi 1393643644 632 ETFKQQKVRM 641
Cdd:PRK09088 470 ASGKLQKARL 479
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
166-641 |
4.57e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 81.78 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEF--------LESLEPDL----- 232
Cdd:PRK08315 67 KGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyvamLYELAPELatcep 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 233 --------PALRAMgLHLwaaGPGTHPA--GISDLLAEVSAEVDGPVPGyLSSPQSITDTCLYIFTSGTTGLPKAARISH 302
Cdd:PRK08315 147 gqlqsarlPELRRV-IFL---GDEKHPGmlNFDELLALGRAVDDAELAA-RQATLDPDDPINIQYTSGTTGFPKGATLTH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 303 LKILQcQGFY--QLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKS-KFSAGQFWEDCQQHRVTVFQ-----Y 374
Cdd:PRK08315 222 RNILN-NGYFigEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGeGFDPLATLAAVEEERCTALYgvptmF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 375 IGELcrylvNQPpskaeRGHKVRLavgSGLR---------P-DTWERFVRRFGPLQVLETYGLTEGN-VATINYTG---- 439
Cdd:PRK08315 301 IAEL-----DHP-----DFARFDL---SSLRtgimagspcPiEVMKRVIDKMHMSEVTIAYGMTETSpVSTQTRTDdple 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 440 QR-GAVGRAswlykhiFPFSLIR-YDVTTGEPIRdpqghcmatsPGEPGLLVApvSQQSPFLGYAGGPELAQGKLLKDvf 517
Cdd:PRK08315 368 KRvTTVGRA-------LPHLEVKiVDPETGETVP----------RGEQGELCT--RGYSVMKGYWNDPEKTAEAIDAD-- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 518 rpGdvFFNTGDLLVCDDQGFLRFhdrTGdtfRWK------GENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAA 591
Cdd:PRK08315 427 --G--WMHTGDLAVMDEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVGVPDE-KYGEEVCAW 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1393643644 592 LVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:PRK08315 496 IILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
71-631 |
5.54e-16 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 81.24 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefag 150
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHR-LRARG-------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 151 gdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVPT--ALRRGPLLHCLRSCGARALVLAPEFLESL 228
Cdd:cd17651 42 -------------VGPGDLVALCARRSAELVVALLAILKAGA--AYVPLdpAYPAERLAFMLADAGPVLVLTHPALAGEL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 229 EPDLPALRAMGLHLWAAGPGTHPAgisdllaevsAEVDGPVPGYLsspqsitdtclyIFTSGTTGLPKAARISHLKIL-Q 307
Cdd:cd17651 107 AVELVAVTLLDQPGAAAGADAEPD----------PALDADDLAYV------------IYTSGSTGRPKGVVMPHRSLAnL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 308 CQGFYQLCGVHQED-VIYLALPLYHMsgSLLGIVGCMGIGATVVLKS---KFSAGQFWEDCQQHRVTVFQYIGELCRYLV 383
Cdd:cd17651 165 VAWQARASSLGPGArTLQFAGLGFDV--SVQEIFSTLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 384 NQPPSKAERGHKVRLAVGSGLRPDTWE---RFVRRFGPLQVLETYGLTEGNVATinytgqrgavgraswlyKHIFPFSLI 460
Cdd:cd17651 243 EHGRPLGVRLAALRYLLTGGEQLVLTEdlrEFCAGLPGLRLHNHYGPTETHVVT-----------------ALSLPGDPA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 461 RYD--VTTGEPIRDPQGHCMATS-----PGEPG-LLVAPVSQQSpflGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVC 532
Cdd:cd17651 306 AWPapPPIGRPIDNTRVYVLDAAlrpvpPGVPGeLYIGGAGLAR---GYLNRPELTAERFVPDPFVPGARMYRTGDLARW 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 533 DDQGFLRFHDRTGDTFRWKGENVattEVAEVFEALdfLQEVNVYGVTVPGHEGRAGMAALV----LRPPHALDLMQLYTH 608
Cdd:cd17651 383 LPDGELEFLGRADDQVKIRGFRI---ELGEIEAAL--ARHPGVREAVVLAREDRPGEKRLVayvvGDPEAPVDAAELRAA 457
|
570 580
....*....|....*....|...
gi 1393643644 609 VSENLPPYARPRFLRLQESLATT 631
Cdd:cd17651 458 LATHLPEYMVPSAFVLLDALPLT 480
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
167-628 |
6.37e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 81.36 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALRRGP--LLHCLRSCGARALVLAPefleSLEPDLPALRA----MGL 240
Cdd:PRK07786 67 GDRVLILMLNRTEFVESVLAANMLG--AIAVPVNFRLTPpeIAFLVSDCGAHVVVTEA----ALAPVATAVRDivplLST 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HLWAAGPGTHPA-GISDLLAEvsaevDGPVPGYLSSPQsitDT-CLYIFTSGTTGLPKAARISHLKiLQCQGFYQLCGVH 318
Cdd:PRK07786 141 VVVAGGSSDDSVlGYEDLLAE-----AGPAHAPVDIPN---DSpALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 319 ---QEDVIYLALPLYHMSGslLGIVGCM-GIGATVVLK--SKFSAGQFWEDCQQHRVT-VFQYIGELCRYLVNQPPskae 391
Cdd:PRK07786 212 adiNSDVGFVGVPLFHIAG--IGSMLPGlLLGAPTVIYplGAFDPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQA---- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 392 RGHKVRLAV---GSGLRPDTWER-FVRRFGPLQVLETYGLTEGNVATINYTG-----QRGAVGRaswlykhifPFSLIRY 462
Cdd:PRK07786 286 RPRDLALRVlswGAAPASDTLLRqMAATFPEAQILAAFGQTEMSPVTCMLLGedairKLGSVGK---------VIPTVAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 463 DVTTgEPIRDpqghcmaTSPGEPGLLV--APVSQQspflGYAGGPELAqgkllKDVFRPGdvFFNTGDLLVCDDQGFLRF 540
Cdd:PRK07786 357 RVVD-ENMND-------VPVGEVGEIVyrAPTLMS----GYWNNPEAT-----AEAFAGG--WFHSGDLVRQDEEGYVWV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 541 HDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTvpgHE--GRAGMAALVLRPPHA-LDLMQLYTHVSENLPPYA 617
Cdd:PRK07786 418 VDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA---DEkwGEVPVAVAAVRNDDAaLTLEDLAEFLTDRLARYK 494
|
490
....*....|.
gi 1393643644 618 RPRFLRLQESL 628
Cdd:PRK07786 495 HPKALEIVDAL 505
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
166-626 |
8.11e-16 |
|
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: 80.41 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGARALVLAPEfleslEPDLPALRAMGLHLW 243
Cdd:cd12116 36 PGDRVAVYLPRSARLVAAMLAVLKAGA--AYVPldPDYPADRLRYILEDAEPALVLTDDA-----LPDRLPAGLPVLLLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AAGPGTHPAgisdllaEVSAEVDGPVPGYLsspqsitdtclyIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDV 322
Cdd:cd12116 109 LAAAAAAPA-------APRTPVSPDDLAYV------------IYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGLGPGDR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IyLALPLYHMSGSLLGIVGCMGIGATVVLKSK---FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERghkVRLA 399
Cdd:cd12116 170 L-LAVTTYAFDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAG---LTAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 400 VG-SGLRPDTWERFVRRFGPLQVLetYGLTEgnvATINYTGQRGAVGRASwlykhifpfslirydVTTGEPIR------- 471
Cdd:cd12116 246 CGgEALPPDLAARLLSRVGSLWNL--YGPTE---TTIWSTAARVTAAAGP---------------IPIGRPLAntqvyvl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 472 DPQGhcMATSPGEPGLLV---APVSQqspflGYAGGPELAQGKLLKDVFR-PGDVFFNTGDLLVCDDQGFLRFHDRTGDT 547
Cdd:cd12116 306 DAAL--RPVPPGVPGELYiggDGVAQ-----GYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 548 FRWKGENVATTEVAEVFEALDFLQEVnvyGVTVPGHEGRAGMAALVLRP-PHALDLMQLYTHVSENLPPYARP-RFLRLQ 625
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQA---AVVVREDGGDRRLVAYVVLKaGAAPDAAALRAHLRATLPAYMVPsAFVRLD 455
|
.
gi 1393643644 626 E 626
Cdd:cd12116 456 A 456
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
166-635 |
9.16e-16 |
|
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: 80.24 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAG-----LRTAFVPtalrrGPLLHCLRSCGARALVLAPEFLESLEPDLPALramgL 240
Cdd:cd05969 24 KGDRVFVLSPRSPELYFSMLGIGKIGavicpLFSAFGP-----EAIRDRLENSEAKVLITTEELYERTDPEDPTL----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 241 HlwaagpgthpagisdllaevsaevdgpvpgylsspqsitdtclyiFTSGTTGLPKAARISH-LKILQCQGFYQLCGVHQ 319
Cdd:cd05969 95 H---------------------------------------------YTSGTTGTPKGVLHVHdAMIFYYFTGKYVLDLHP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALPLYHMSGSLLGIVGCMGIGATVVL-KSKFSAGQFWEDCQQHRVTVF----QYIGELCRYLVNQPPSKAERGH 394
Cdd:cd05969 130 DDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVyEGRFDAESWYGIIERVKVTVWytapTAIRMLMKEGDELARKYDLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 395 KVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTE-GNVATINYTGQR---GAVGRaswlykhifPFSLIRYDVTT--GE 468
Cdd:cd05969 210 RFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSIMIANYPCMPikpGSMGK---------PLPGVKAAVVDenGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 469 PIRDPQGHCMATSPGEPgllvapvsqqSPFLGYAGGPElaqgkLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTF 548
Cdd:cd05969 280 ELPPGTKGILALKPGWP----------SMFRGIWNDEE-----RYKNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 549 RWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLR----PPHALDlMQLYTHVSENLPPYARPRFLRL 624
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGEIIKAFISLKegfePSDELK-EEIINFVRQKLGAHVAPREIEF 420
|
490
....*....|.
gi 1393643644 625 QESLATTETFK 635
Cdd:cd05969 421 VDNLPKTRSGK 431
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
164-641 |
1.77e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 79.74 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPA--------- 234
Cdd:PRK12406 33 VRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPAgvtvlsvpt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 235 ----LRAMGLhlwAAGPGTHPAGISDL---LAEVSAEVDGPVPGylssPQSItdtclyIFTSGTTGLPKAARISHLKILQ 307
Cdd:PRK12406 113 ppeiAAAYRI---SPALLTPPAGAIDWegwLAQQEPYDGPPVPQ----PQSM------IYTSGTTGHPKGVRRAAPTPEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 308 CQGFYQLC----GVHQEDVIYLALPLYHMSGSLLGIVGcMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLV 383
Cdd:PRK12406 180 AAAAEQMRaliyGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 384 NQPPsKAERGHKVrlavgSGLR----------PDTWERFVRRFGPLqVLETYGLTEGNVATI----NYTGQRGAVGRASw 449
Cdd:PRK12406 259 KLPE-EVRAKYDV-----SSLRhvihaaapcpADVKRAMIEWWGPV-IYEYYGSTESGAVTFatseDALSHPGTVGKAA- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 450 lykhifPFSLIRYDVTTGEPIrdpqghcmatSPGEPGLLVAPVSQQSPFLgYAGGPElaqgkLLKDVFRPGdvFFNTGDL 529
Cdd:PRK12406 331 ------PGAELRFVDEDGRPL----------PQGEIGEIYSRIAGNPDFT-YHNKPE-----KRAEIDRGG--FITSGDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 530 LVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLRPPHALDLMQLYTH 608
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEALMAVVEPQPGATLDEADIRAQ 464
|
490 500 510
....*....|....*....|....*....|...
gi 1393643644 609 VSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:PRK12406 465 LKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
164-644 |
2.01e-15 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 79.43 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEflwlWFGLAKAGLRTA--FVP--TALRRGPLLHCLRSCGARALV----LAPEfLESLEPDLPAL 235
Cdd:cd05928 64 LQRGDRVAVILPRVPE----WWLVNVACIRTGlvFIPgtIQLTAKDILYRLQASKAKCIVtsdeLAPE-VDSVASECPSL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 236 RAMGLHLWAAGPGThpAGISDLLAEVSAEvDGPVPGYLSSPQSItdtclyIFTSGTTGLPKAARISH----LKILQCQGF 311
Cdd:cd05928 139 KTKLLVSEKSRDGW--LNFKELLNEASTE-HHCVETGSQEPMAI------YFTSGTTGSPKMAEHSHsslgLGLKVNGRY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 312 YQlcGVHQEDVIYlalplyHMS--GSLLGIVGCM----GIGATVVLKS--KFSAGQFWEDCQQHRVTVFQYIGELCRYLV 383
Cdd:cd05928 210 WL--DLTASDIMW------NTSdtGWIKSAWSSLfepwIQGACVFVHHlpRFDPLVILKTLSSYPITTFCGAPTVYRMLV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 384 NQPPSKAERGH-KVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTGQR---GAVGRASwlykhifpfsl 459
Cdd:cd05928 282 QQDLSSYKFPSlQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTETGLICANFKGMKikpGSMGKAS----------- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 460 IRYDVTtgepIRDPQGHCMAT-SPGEPGLLVAPVSQQSPFLGYAGGPELAQGKLLKDvfrpgdvFFNTGDLLVCDDQGFL 538
Cdd:cd05928 350 PPYDVQ----IIDDNGNVLPPgTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 539 RFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPP---HALDLM--QLYTHVSENL 613
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVVKAFVVLAPQflsHDPEQLtkELQQHVKSVT 497
|
490 500 510
....*....|....*....|....*....|.
gi 1393643644 614 PPYARPRFLRLQESLATTETFKQQKVRMANE 644
Cdd:cd05928 498 APYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
71-641 |
2.89e-15 |
|
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: 78.91 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 71 LAELAQQRAAHTFLIHGSRRFSYSEAERESNRAArAFLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefag 150
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLA-AGLRGLG-------------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 151 gdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVlapefleslep 230
Cdd:cd05920 62 -------------IRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYI----------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 231 dlpalramglhlwaaGPGTHPAGISDLLAEVSAEvdgpvpgylsspqSITDTCLYIFTSGTTGLPKAARISHlkilqcQG 310
Cdd:cd05920 118 ---------------VPDRHAGFDHRALARELAE-------------SIPEVALFLLSGGTTGTPKLIPRTH------ND 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 311 FY-------QLCGVHQEDVIYLALPLYH---MSGSllGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVT--------VF 372
Cdd:cd05920 164 YAynvrasaEVCGLDQDTVYLAVLPAAHnfpLACP--GVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTvtalvpalVS 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 373 QYIGELCRYlVNQPPSkaergHKVRLAVGSGLRPDTWERFVRRFGPlQVLETYGLTEGnvaTINYTgqrgavgraswlyk 452
Cdd:cd05920 242 LWLDAAASR-RADLSS-----LRLLQVGGARLSPALARRVPPVLGC-TLQQVFGMAEG---LLNYT-------------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 453 hifpfsliRYD-------VTTGEP--------IRDPQGHCMAtsPGEPGLLVApvsqQSP--FLGYAGGPELAQgkllkD 515
Cdd:cd05920 298 --------RLDdpdeviiHTQGRPmspddeirVVDEEGNPVP--PGEEGELLT----RGPytIRGYYRAPEHNA-----R 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 516 VFRPgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHE-GRAGMAALVL 594
Cdd:cd05920 359 AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV--VAMPDELlGERSCAFVVL 435
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1393643644 595 RPPhALDLMQLYTHVSE-NLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:cd05920 436 RDP-PPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
164-631 |
3.92e-15 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 78.91 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAgpeflWLWFGLAKAG-LRTAFV-----PTALRRgPLLHCLRSCGARALVLAPEFLESLEPDLP--AL 235
Cdd:PRK07059 70 LAKGARVAIMMPN-----VLQYPVAIAAvLRAGYVvvnvnPLYTPR-ELEHQLKDSGAEAIVVLENFATTVQQVLAktAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 236 R-----AMGLHLWAAG-------------------PGTHPagISDLLAEVSAEVDGPVPgylsspQSITDTCLYIFTSGT 291
Cdd:PRK07059 144 KhvvvaSMGDLLGFKGhivnfvvrrvkkmvpawslPGHVR--FNDALAEGARQTFKPVK------LGPDDVAFLQYTGGT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 292 TGLPKAARISHLKI----LQCQGFYQ---LCGVHQEDVIYL-ALPLYHMSG----SLLGivgcMGIGATVVL--KSKFSA 357
Cdd:PRK07059 216 TGVSKGATLLHRNIvanvLQMEAWLQpafEKKPRPDQLNFVcALPLYHIFAltvcGLLG----MRTGGRNILipNPRDIP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 358 GqFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGL---RPdTWERFVRRFGpLQVLETYGLTEGN-VA 433
Cdd:PRK07059 292 G-FIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMavqRP-VAERWLEMTG-CPITEGYGLSETSpVA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TINytgqrgavgraswlykhifPFSLIRYDVTTGEP-------IRDPQGHCMAtsPGEPGLLVAPVSQQSPflGYAGGP- 505
Cdd:PRK07059 369 TCN-------------------PVDATEFSGTIGLPlpstevsIRDDDGNDLP--LGEPGEICIRGPQVMA--GYWNRPd 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 506 ELAQgkllkdVFRPgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEG 585
Cdd:PRK07059 426 ETAK------VMTA-DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDE-HSG 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1393643644 586 RAGMAALVLRPPhALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK07059 498 EAVKLFVVKKDP-ALTEEDVKAFCKERLTNYKRPKFVEFRTELPKT 542
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
164-631 |
1.00e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.55 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLrtafvpTALRRGPLL------HCLRSCGARALVLAPEFLESLEPDLPALRA 237
Cdd:PRK12492 72 LVPGDRIAVQMPNVLQYPIAVFGALRAGL------IVVNTNPLYtaremrHQFKDSGARALVYLNMFGKLVQEVLPDTGI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 238 MglHLWAAGPG-THPAGISDLLAEVSAEVDGPVPGYlSSPQSIT---------------------DTCLYIFTSGTTGLP 295
Cdd:PRK12492 146 E--YLIEAKMGdLLPAAKGWLVNTVVDKVKKMVPAY-HLPQAVPfkqalrqgrglslkpvpvgldDIAVLQYTGGTTGLA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 296 KAARISH-------LKILQCQGFYQLCGVHQ----EDVIYLALPLYHMSGSLLGIVgCMGIGA--TVVLKSKFSAGQFWE 362
Cdd:PRK12492 223 KGAMLTHgnlvanmLQVRACLSQLGPDGQPLmkegQEVMIAPLPLYHIYAFTANCM-CMMVSGnhNVLITNPRDIPGFIK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 363 DCQQHRVTVFQYIGELCRYLVNQPPSKAE--RGHKVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGN-VATINYTG 439
Cdd:PRK12492 302 ELGKWRFSALLGLNTLFVALMDHPGFKDLdfSALKLTNSGGTALVKATAERWEQLTG-CTIVEGYGLTETSpVASTNPYG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 440 QRGAVGraswlykhifpfslirydvTTGEPIR-------DPQGHCMATspGEPGLLVAPVSQQspFLGYAGGPElAQGKL 512
Cdd:PRK12492 381 ELARLG-------------------TVGIPVPgtalkviDDDGNELPL--GERGELCIKGPQV--MKGYWQQPE-ATAEA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 513 LKdvfrpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEAldFLQEVNVYGVTVPghEGRAGMAA- 591
Cdd:PRK12492 437 LD-----AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA--HPKVANCAAIGVP--DERSGEAVk 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1393643644 592 --LVLRPPhALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK12492 508 lfVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMT 548
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
88-654 |
1.26e-14 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 77.15 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 88 SRRFSYSEAERESNRAARAfLRALGWdwgpdggdsgegsaGEGERaapgagdaaagsgaefaggdgaargggaaaplspg 167
Cdd:cd05968 89 SRTLTYGELLYEVKRLANG-LRALGV--------------GKGDR----------------------------------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 168 atVALLLPAGPEFLWLWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGARALVLAPEFLE-----SLEPDL-------P 233
Cdd:cd05968 119 --VGIYLPMIPEIVPAFLAVARIGG--IVVPifSGFGKEAAATRLQDAEAKALITADGFTRrgrevNLKEEAdkacaqcP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 234 ALRAMGLHLWAAGP-GTHPAGISDLLAEVSAEVDGpvpgylSSPQSITDTCLYIFTSGTTGLPKAARISH--LKILQCQG 310
Cdd:cd05968 195 TVEKVVVVRHLGNDfTPAKGRDLSYDEEKETAGDG------AERTESEDPLMIIYTSGTTGKPKGTVHVHagFPLKAAQD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 311 FYQLCGVHQEDVIYLALPLYHMSGSLLgIVGCMGIGATVVLKSKF----SAGQFWEDCQQHRVTVFQYIGELCRYLV--N 384
Cdd:cd05968 269 MYFQFDLKPGDLLTWFTDLGWMMGPWL-IFGGLILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 385 QPPSKAERGHKVRLAVGSG--LRPDTWERFVRRFGplqvletygltEGNVATINYTG----QRGAVGraSWLYKHIFPFS 458
Cdd:cd05968 348 DAPVNAHDLSSLRVLGSTGepWNPEPWNWLFETVG-----------KGRNPIINYSGgteiSGGILG--NVLIKPIKPSS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 459 L------IRYDV--TTGEPIRDPQGHCMATSPGePGLLvapvsqqspfLGYAGGPElaqgKLLKDVFRPGDVFFNTGDLL 530
Cdd:cd05968 415 FngpvpgMKADVldESGKPARPEVGELVLLAPW-PGMT----------RGFWRDED----RYLETYWSRFDNVWVHGDFA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 531 VCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRP---PHALDLMQLYT 607
Cdd:cd05968 480 YYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEAIVCFVVLKPgvtPTEALAEELME 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 608 HVSENLPPYARPRFLRLQESLATTETFK--QQKVRMANEGFDP---STLSDP 654
Cdd:cd05968 559 RVADELGKPLSPERILFVKDLPKTRNAKvmRRVIRAAYLGKELgdlSSLENP 610
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
166-631 |
1.32e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALR--RGPLLHCLRSCGARALVLAPEFLESLepDLPA-LRAMGLHL 242
Cdd:PRK12467 561 PDVLVGIAVERSIEMVVGLLAVLKAG--GAYVPLDPEypQDRLAYMLDDSGVRLLLTQSHLLAQL--PVPAgLRSLCLDE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 243 WAAgpgthpagisdlLAEVSAEVDGPVPgylSSPQSItdtCLYIFTSGTTGLPKAARISHLKILQ----CQGFYQLcgvh 318
Cdd:PRK12467 637 PAD------------LLCGYSGHNPEVA---LDPDNL---AYVIYTSGSTGQPKGVAISHGALANyvcvIAERLQL---- 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 319 QEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSK---FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHK 395
Cdd:PRK12467 695 AADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQR 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 396 VRLAVGSGLRPDTWERfVRRFGP-LQVLETYGLTEGNVATINYT-GQRGAVGRASWLYKHIFPFSLIRYDvttgepirdp 473
Cdd:PRK12467 775 ALVCGGEALQVDLLAR-VRALGPgARLINHYGPTETTVGVSTYElSDEERDFGNVPIGQPLANLGLYILD---------- 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 474 qgHCMATSP-GEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDVFRP-GDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWK 551
Cdd:PRK12467 844 --HYLNPVPvGVVGELY--IGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 552 GENVATTEVAEVFEALDFLQEVNVygVTVPGHEGRAGMAALVLRPP-----HALDLMQLYTHVSENLPPYARPRFLRLQE 626
Cdd:PRK12467 920 GFRIELGEIEARLLAQPGVREAVV--LAQPGDAGLQLVAYLVPAAVadgaeHQATRDELKAQLRQVLPDYMVPAHLLLLD 997
|
....*
gi 1393643644 627 SLATT 631
Cdd:PRK12467 998 SLPLT 1002
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-642 |
2.29e-14 |
|
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: 75.21 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 279 ITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQE-DVIYLALPLYHMSGSLLGIVGCMGIGATVVL------ 351
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPdDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 352 KSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVnQPPSKAERGhKVRLAV--GSGLRPDTWERFVRRFGpLQVLETYGLTE 429
Cdd:cd05944 81 RNPGLFDNFWKLVERYRITSLSTVPTVYAALL-QVPVNADIS-SLRFAMsgAAPLPVELRARFEDATG-LPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 430 GN-VATINYTG---QRGAVGRAswlykhiFPFSLIRYDVTtgepirDPQGHCM-ATSPGEpgllVAPVSQQSP--FLGYa 502
Cdd:cd05944 158 ATcLVAVNPPDgpkRPGSVGLR-------LPYARVRIKVL------DGVGRLLrDCAPDE----VGEICVAGPgvFGGY- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 503 ggpelAQGKLLKDVFrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVattEVAEVFEALDFLQEVNVYG-VTVP 581
Cdd:cd05944 220 -----LYTEGNKNAF-VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNI---DPALIEEALLRHPAVAFAGaVGQP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 582 -GHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYAR-PRFLRLQESLATT---ETFKQQKVRMA 642
Cdd:cd05944 291 dAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTavgKVFKPALRADA 356
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
235-645 |
2.46e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.80 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 235 LRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPGylSSPQSitdTCLYIFTSGTTGLPKAARISHLKILQC-QGFYQ 313
Cdd:PRK07787 88 LADSGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPE--PDPDA---PALIVYTSGTTGPPKGVVLSRRAIAADlDALAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 314 LCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRV------TVFQYIGElcrylvnqPP 387
Cdd:PRK07787 163 AWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSEGGTlyfgvpTVWSRIAA--------DP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 388 SKAERGHKVRLAV-GSGLRPDT-WERFVRRFGpLQVLETYGLTEG--NVATiNYTGQR--GAVGRAswlykhiFPFSLIR 461
Cdd:PRK07787 235 EAARALRGARLLVsGSAALPVPvFDRLAALTG-HRPVERYGMTETliTLST-RADGERrpGWVGLP-------LAGVETR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 462 YDVTTGEPIrdpqghcmaTSPGEPgllVAPVSQQSP--FLGYAGGPELAqgkllKDVFRPgDVFFNTGDLLVCDDQGFLR 539
Cdd:PRK07787 306 LVDEDGGPV---------PHDGET---VGELQVRGPtlFDGYLNRPDAT-----AAAFTA-DGWFRTGDVAVVDPDGMHR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 540 FHDRTG-DTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDlmQLYTHVSENLPPYAR 618
Cdd:PRK07787 368 IVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDD-DLGQRIVAYVVGADDVAAD--ELIDFVAQQLSVHKR 444
|
410 420
....*....|....*....|....*..
gi 1393643644 619 PRFLRLQESLATTETFKQQKVRMANEG 645
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
167-635 |
2.93e-14 |
|
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: 76.08 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAG-----LRTAFVPTALRRGpllhcLRSCGARALVLAPEFL-------------ESL 228
Cdd:cd17634 109 GDRVAIYMPMIPEAAVAMLACARIGavhsvIFGGFAPEAVAGR-----IIDSSSRLLITADGGVragrsvplkknvdDAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 229 EPDLPALRAMgLHLWAAGPGTHPAGISDLlaEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISH--LKIL 306
Cdd:cd17634 184 NPNVTSVEHV-IVLKRTGSDIDWQEGRDL--WWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVY 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 307 QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKF----SAGQFWEDCQQHRVTVFQYIGELCRYL 382
Cdd:cd17634 261 AATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 383 VNQPPSKAER----GHKVRLAVGSGLRPDTWERFVRRFGPLQ--VLETYGLTEGNVATInyTGQRGAVGRASWLYKHIFP 456
Cdd:cd17634 341 MAAGDDAIEGtdrsSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGGFMI--TPLPGAIELKAGSATRPVF 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 457 fsliRYDVTtgepIRDPQGHcmATSPGEPGLLVAPVSQQSPFLGYAGGPElaqgKLLKDVFRPGDVFFNTGDLLVCDDQG 536
Cdd:cd17634 419 ----GVQPA----VVDNEGH--PQPGGTEGNLVITDPWPGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDG 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 537 FLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLR----PPHALdLMQLYTHVSEN 612
Cdd:cd17634 485 YYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNhgvePSPEL-YAELRNWVRKE 562
|
490 500
....*....|....*....|...
gi 1393643644 613 LPPYARPRFLRLQESLATTETFK 635
Cdd:cd17634 563 IGPLATPDVVHWVDSLPKTRSGK 585
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
70-635 |
7.06e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 70 RLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefa 149
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHR-LRARG------------------------------------- 2049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 150 ggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGlrTAFVP--TALRRGPLLHCLRSCGARALVLAPEFLES 227
Cdd:PRK12316 2050 --------------VGPEVRVAIAAERSFELVVALLAVLKAG--GAYVPldPNYPAERLAYMLEDSGAALLLTQRHLLER 2113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 228 LEP--DLPALRAMGLHLWAAGPGTHPAgisdllaevsaevdgpvpgylssPQSITDTCLY-IFTSGTTGLPKAARISHLK 304
Cdd:PRK12316 2114 LPLpaGVARLPLDRDAEWADYPDTAPA-----------------------VQLAGENLAYvIYTSGSTGLPKGVAVSHGA 2170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 305 ILQ-CQGFYQLCGVHQEDVIylalpLYHMSGSLLGIV-GCMG---IGATVVLK--SKFSAGQFWEDCQQHRVTV------ 371
Cdd:PRK12316 2171 LVAhCQAAGERYELSPADCE-----LQFMSFSFDGAHeQWFHpllNGARVLIRddELWDPEQLYDEMERHGVTIldfppv 2245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 372 -FQYIGELCRYLVNQPPskaerghkVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRAS 448
Cdd:PRK12316 2246 yLQQLAEHAERDGRPPA--------VRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAA 2317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 449 WlykhifpfslirydVTTGEPIRDPQGHCMATS-----PGEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDVF-RPGDV 522
Cdd:PRK12316 2318 Y--------------VPIGRALGNRRAYILDADlnllaPGMAGELY--LGGEGLARGYLNRPGLTAERFVPDPFsASGER 2381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 523 FFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEGRAGMAALVLRPPHALDL 602
Cdd:PRK12316 2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLL 2459
|
570 580 590
....*....|....*....|....*....|...
gi 1393643644 603 MQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PRK12316 2460 AELRAWLAARLPAYMVPAHWVVLERLPLNPNGK 2492
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
66-436 |
1.01e-13 |
|
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: 74.89 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 66 SLAWRLAELAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsg 145
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHH-LRALG--------------------------------- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 146 aefaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLrtAFVP--TALRRGPLLHCLRSCGARALVLApe 223
Cdd:COG1020 523 ------------------VGPGDLVGVCLERSLEMVVALLAVLKAGA--AYVPldPAYPAERLAYMLEDAGARLVLTQ-- 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 224 flESLEPDLPALRAMGLHLWAAGPGTHPAgiSDLLAEVSAEvdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHL 303
Cdd:COG1020 581 --SALAARLPELGVPVLALDALALAAEPA--TNPPVPVTPD----------------DLAYVIYTSGSTGRPKGVMVEHR 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 304 KILQ-CQGFYQLCGVHQEDVIYLALPLyhmS--GSLLGIVGCMGIGATVVL---KSKFSAGQFWEDCQQHRVTVFQYIGE 377
Cdd:COG1020 641 ALVNlLAWMQRRYGLGPGDRVLQFASL---SfdASVWEIFGALLSGATLVLappEARRDPAALAELLARHRVTVLNLTPS 717
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393643644 378 LCRYLVNQPPskaERGHKVRLAVGSG--LRPDTWERFVRRFGPLQVLETYGLTEgnvATIN 436
Cdd:COG1020 718 LLRALLDAAP---EALPSLRLVLVGGeaLPPELVRRWRARLPGARLVNLYGPTE---TTVD 772
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
281-635 |
1.35e-13 |
|
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: 72.36 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGsLLGIVGCMGIGATVVLKSKFSAGQ 359
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 fwEDCQQHRVTVFQYI-GELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLqvLETYGLTE--GNVATIN 436
Cdd:cd17630 80 --EDLAPPGVTHVSLVpTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPL--YTTYGMTEtaSQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 437 YTG-QRGAVGRaswlykhifPFSLIRYDVTTGEPIrDPQGHCMAtspgepgllvapvsqqspfLGYAGGPELAQGkllkd 515
Cdd:cd17630 156 PDGfGRGGVGV---------LLPGRELRIVEDGEI-WVGGASLA-------------------MGYLRGQLVPEF----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 516 vfrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLR 595
Cdd:cd17630 202 ---NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE-ELGQRPVAVIVGR 277
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1393643644 596 PPHALDlmQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd17630 278 GPADPA--ELRAWLKDKLARFKLPKRIYPVPELPRTGGGK 315
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
164-631 |
1.96e-13 |
|
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: 73.07 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPtalrrgpllhclrscgaralvlapeflesLEPDLPALRAMGLHLW 243
Cdd:cd12114 34 VRPGDLVAVTLPKGPEQVVAVLGILAAG--AAYVP-----------------------------VDIDQPAARREAILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 AA-------GPGTHPAGISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQ-CQGFYQLC 315
Cdd:cd12114 83 AGarlvltdGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNtILDINRRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 316 GVHQEDVIyLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAG---QFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAER 392
Cdd:cd12114 163 AVGPDDRV-LALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdpaHWAELIERHGVTLWNSVPALLEMLLDVLEAAQAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 393 GHKVRLAVGSG--LRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASWLYKhiFPFSLIRYDVttgepi 470
Cdd:cd12114 242 LPSLRLVLLSGdwIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYG--RPLANQRYRV------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 RDPQG-HCMATSPGE---PGLLVApvsqqspfLGYAGGPELAQGKLLKDvfRPGDVFFNTGDLLVCDDQGFLRFHDRTGD 546
Cdd:cd12114 314 LDPRGrDCPDWVPGElwiGGRGVA--------LGYLGDPELTAARFVTH--PDGERLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 547 TFRWKGENVattEVAEVFEALDFLQEVNVYGVTV-PGHEGRAGMAALVLRPPHALDLMQ-LYTHVSENLPPYARPRFLRL 624
Cdd:cd12114 384 QVKVRGYRI---ELGEIEAALQAHPGVARAVVVVlGDPGGKRLAAFVVPDNDGTPIAPDaLRAFLAQTLPAYMIPSRVIA 460
|
....*..
gi 1393643644 625 QESLATT 631
Cdd:cd12114 461 LEALPLT 467
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
77-638 |
1.98e-13 |
|
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: 73.10 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 77 QRAA-----HTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefagg 151
Cdd:cd12118 11 ERAAavypdRTSIVYGDRRYTWRQTYDRCRRLASA-LAALG--------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 152 dgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLeslepd 231
Cdd:cd12118 51 ------------ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 232 lpalramglhlwaagpgthpagISDLLAEVSaevdgpvPGYLssPQSITDTCLYI---FTSGTTGLPKAARISHLKI-LQ 307
Cdd:cd12118 113 ----------------------YEDLLAEGD-------PDFE--WIPPADEWDPIalnYTSGTTGRPKGVVYHHRGAyLN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 308 CQGFYQLCGVHQEDViYL-ALPLYHMSGsLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQP 386
Cdd:cd12118 162 ALANILEWEMKQHPV-YLwTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 387 PSKAERG-HKVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEG-NVATINYTgqrgavgRASWlykHIFPFSL----- 459
Cdd:cd12118 240 PSDARPLpHRVHVMTAGAPPPAAVLAKMEELG-FDVTHVYGLTETyGPATVCAW-------KPEW---DELPTEErarlk 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 460 ----IRYDVTTGEPIRDPQGhcMATSP------GE---PGLLVApvsqqspfLGYAGGPELAqgkllKDVFRPGdvFFNT 526
Cdd:cd12118 309 arqgVRYVGLEEVDVLDPET--MKPVPrdgktiGEivfRGNIVM--------KGYLKNPEAT-----AEAFRGG--WFHS 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 527 GDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLY 606
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDE-KWGEVPCAFVELKEGAKVTEEEII 450
|
570 580 590
....*....|....*....|....*....|..
gi 1393643644 607 THVSENLPPYARPRFLRLQEsLATTETFKQQK 638
Cdd:cd12118 451 AFCREHLAGFMVPKTVVFGE-LPKTSTGKIQK 481
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
166-609 |
2.40e-13 |
|
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: 73.04 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGL--RTAFVPTALRRGP-LLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHL 242
Cdd:cd05931 47 PGDRVLLLAPPGLDFVAAFLGCLYAGAiaVPLPPPTPGRHAErLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 243 WAAGpgthpagisDLLA-EVSAEVDGPVPGylsspqsITDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQE 320
Cdd:cd05931 127 LLVV---------DLLPdTSAADWPPPSPD-------PDDIAYLQYTSGSTGTPKGVVVTHRNLLaNVRQIRRAYGLDPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSagqF------W-EDCQQHRVTV-----FQYigELCrylvnqpps 388
Cdd:cd05931 191 DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA---FlrrplrWlRLISRYRATIsaapnFAY--DLC--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 389 kAERGH----------KVRLAVgSG---LRPDTWERFVRRFGPL-----QVLETYGLTEGNVA-TinyTGQRGAVGRASW 449
Cdd:cd05931 257 -VRRVRdedlegldlsSWRVAL-NGaepVRPATLRRFAEAFAPFgfrpeAFRPSYGLAEATLFvS---GGPPGTGPVVLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 450 LYKHIFPFSLIRYD---------VTTGEP-------IRDPQGhCMATSPGEPGLL------VAPvsqqspflGYAGGPEL 507
Cdd:cd05931 332 VDRDALAGRAVAVAaddpaarelVSCGRPlpdqevrIVDPET-GRELPDGEVGEIwvrgpsVAS--------GYWGRPEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 508 AQGKLLKDVFRPGDVFFNTGDLlvcddqGFLrfHDR----TGdtfRWK------GENVATTEV-AEVFEALDFLQEVNVY 576
Cdd:cd05931 403 TAETFGALAATDEGGWLRTGDL------GFL--HDGelyiTG---RLKdliivrGRNHYPQDIeATAEEAHPALRPGCVA 471
|
490 500 510
....*....|....*....|....*....|....
gi 1393643644 577 GVTVPG-HEGRAGMAALVLRPPHALDLMQLYTHV 609
Cdd:cd05931 472 AFSVPDdGEERLVVVAEVERGADPADLAAIAAAI 505
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
68-376 |
5.64e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.84 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 68 AWRLAELAQQRAA----HTFLIHGSRRFSYSEAERESNRAARaFLRALGwdwgpdggdsgegsagegeraapgagdaaag 143
Cdd:PRK07798 2 AWNIADLFEAVADavpdRVALVCGDRRLTYAELEERANRLAH-YLIAQG------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 144 sgaefaggdgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAglRTAFVPTALR--RGPLLHCLRSCGARALVLA 221
Cdd:PRK07798 50 --------------------LGPGDHVGIYARNRIEYVEAMLGAFKA--RAVPVNVNYRyvEDELRYLLDDSDAVALVYE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 222 PEFLESLEPDLPALRamGLHLW-----AAGPGTHPAGIS--DLLAEVSAEVDGPVPgylsSPqsitDTCLYIFTSGTTGL 294
Cdd:PRK07798 108 REFAPRVAEVLPRLP--KLRTLvvvedGSGNDLLPGAVDyeDALAAGSPERDFGER----SP----DDLYLLYTGGTTGM 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 295 PKAARISHLKILQCQG----FYQLCGVHQED------------VIYLALPLYHMSGsLLGIVGCMGIGATVVL--KSKFS 356
Cdd:PRK07798 178 PKGVMWRQEDIFRVLLggrdFATGEPIEDEEelakraaagpgmRRFPAPPLMHGAG-QWAAFAALFSGQTVVLlpDVRFD 256
|
330 340
....*....|....*....|
gi 1393643644 357 AGQFWEDCQQHRVTVFQYIG 376
Cdd:PRK07798 257 ADEVWRTIEREKVNVITIVG 276
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
164-611 |
5.93e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 71.94 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEflwLWFGLAKAGLRtafvptALRRGPL---------LHCLRSCGARALVLAP-EFLESLEpdlp 233
Cdd:PRK06188 59 LGTGDAVALLSLNRPE---VLMAIGAAQLA------GLRRTALhplgslddhAYVLEDAGISTLIVDPaPFVERAL---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 234 AL--RAMGL-HLWAAGPGthpAGISDLLAEvsAEVDGPVPgyLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILqcqG 310
Cdd:PRK06188 126 ALlaRVPSLkHVLTLGPV---PDGVDLLAA--AAKFGPAP--LVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIA---T 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 311 FYQLCGVHQE---DVIYLAL-PLYHMSGSLlgIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQP 386
Cdd:PRK06188 196 MAQIQLAEWEwpaDPRFLMCtPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 387 PSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPLqVLETYGLTEGnVATINYTGQR----------GAVGRASwlykhi 454
Cdd:PRK06188 274 DLRTRDLSSLETVYygASPMSPVRLAEAIERFGPI-FAQYYGQTEA-PMVITYLRKRdhdpddpkrlTSCGRPT------ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 455 fPFSLIRydvttgepIRDPQGHcmATSPGEPG-LLVApvsqqSPFL--GYAGGPELAQgkllkDVFRPGdvFFNTGDLLV 531
Cdd:PRK06188 346 -PGLRVA--------LLDEDGR--EVAQGEVGeICVR-----GPLVmdGYWNRPEETA-----EAFRDG--WLHTGDVAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 532 CDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSE 611
Cdd:PRK06188 403 EDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKE 481
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
222-635 |
7.95e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 71.53 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 222 PEFLESlEPDLPALRAMGLHLW----AAG--PGTHPAGISDLlaevsaevdgpvpgylsspqsitdtCLYIFTSGTTGLP 295
Cdd:PRK08314 152 PAWLRA-EPPLQALAPGGVVAWkealAAGlaPPPHTAGPDDL-------------------------AVLPYTSGTTGVP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 296 KAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHmsgsLLGIVGCMG----IGATVVLKSKF---SAGQFWEDcqqH 367
Cdd:PRK08314 206 KGCMHTHRTVMaNAVGSVLWSNSTPESVVLAVLPLFH----VTGMVHSMNapiyAGATVVLMPRWdreAAARLIER---Y 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 368 RVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLR-PD-TWERFVRRFGpLQVLETYGLTEgnvaTINYTgqrgavg 445
Cdd:PRK08314 279 RVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAmPEaVAERLKELTG-LDYVEGYGLTE----TMAQT------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 446 raswlykHIFPFSLIR--------YDV-------TTGEPIrdpqghcmatSPGEPGLLVapVSQQSPFLGYAGGPELAQg 510
Cdd:PRK08314 347 -------HSNPPDRPKlqclgiptFGVdarvidpETLEEL----------PPGEVGEIV--VHGPQVFKGYWNRPEATA- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 511 kllkDVF--RPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVaevfEALDF----LQEVNVYGVTVPgHE 584
Cdd:PRK08314 407 ----EAFieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEV----ENLLYkhpaIQEACVIATPDP-RR 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 585 GRAGMAALVLRPPH-----ALDLMQLythVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PRK08314 478 GETVKAVVVLRPEArgkttEEEIIAW---AREHMAAYKYPRIVEFVDSLPKSGSGK 530
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
281-635 |
9.18e-13 |
|
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: 70.92 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAA------RISHLKILQcqgFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVL--K 352
Cdd:cd05971 89 DPALIIYTSGTTGPPKGAlhahrvLLGHLPGVQ---FPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 353 SKFSAGQFWEDCQQHRVT-VFQYIGELcRYLVNQPPSKAERGHKVRlAVGSGLRPD-----TWERfvRRFGpLQVLETYG 426
Cdd:cd05971 166 TKFDPKAALDLMSRYGVTtAFLPPTAL-KMMRQQGEQLKHAQVKLR-AIATGGESLgeellGWAR--EQFG-VEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 427 LTEGNVATIN----YTGQRGAVGRAswlykhiFPFSLIRYDVTTGEPIrdpqghcmatSPGEPGLLVAPVSQQSPFLGYA 502
Cdd:cd05971 241 QTECNLVIGNcsalFPIKPGSMGKP-------IPGHRVAIVDDNGTPL----------PPGEVGEIAVELPDPVAFLGYW 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 503 GGPELAQGKLLKDVFRpgdvffnTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPg 582
Cdd:cd05971 304 NNPSATEKKMAGDWLL-------TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP- 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 583 HEGRAGMAALVLRPPHALD---LMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd05971 376 IRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
280-635 |
1.43e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.78 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 280 TDTCLYIFTSGTTGLPKAARISHLKILQ--CQGFYQLCGVHQEDVIYLAL-PLYHMSGsLLGIV-GCMGIGATVVLKSKF 355
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEMIGQVVTLGLiPFFHIYG-ITGICcATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 356 SAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRL----AVGSGLRPDTWERFVRRFGPLQVLETYGLTEGN 431
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 432 VATINY--------TGQRGAVGraswlykHIFPFSLIRY-DVTTGEPIrdPQghcmaTSPGEpgllvAPVSQQSPFLGYA 502
Cdd:PLN02330 343 CITLTHgdpekghgIAKKNSVG-------FILPNLEVKFiDPDTGRSL--PK-----NTPGE-----LCVRSQCVMQGYY 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 503 GGPELAQGKLLKdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPG 582
Cdd:PLN02330 404 NNKEETDRTIDE------DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPD 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1393643644 583 HEGRAGMAALVLRPPHALDLMQ-LYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PLN02330 476 EEAGEIPAACVVINPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
276-543 |
1.51e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 71.11 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 276 PQSITDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMsgslLGIVG------CMGIGAt 348
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILsNIEQISDVFNLRNDDVILSSLPFFHS----FGLTVtlwlplLEGIKV- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 349 VVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVgSG---LRPDTWERFVRRFGpLQVLETY 425
Cdd:PRK08633 853 VYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVV-AGaekLKPEVADAFEEKFG-IRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 426 GLTEGN-VATIN-----------YTGQR-GAVGRAswlykhiFPFSLIR-YDVTTGEPIrdpqghcmatSPGEPGLLVap 491
Cdd:PRK08633 931 GATETSpVASVNlpdvlaadfkrQTGSKeGSVGMP-------LPGVAVRiVDPETFEEL----------PPGEDGLIL-- 991
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 492 VSQQSPFLGYAGGPELAqGKLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDR 543
Cdd:PRK08633 992 IGGPQVMKGYLGDPEKT-AEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
164-638 |
1.85e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.04 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVlAPEFLESLEP----DLPALRAMG 239
Cdd:PRK13390 46 LRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV-ASAALDGLAAkvgaDLPLRLSFG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 240 lhlwaagpgthpaGISDLLAEVSAEVDGPVPGYLSSPQSitdtCLYIFTSGTTGLPKAAR--ISHLKILQ--------CQ 309
Cdd:PRK13390 125 -------------GEIDGFGSFEAALAGAGPRLTEQPCG----AVMLYSSGTTGFPKGIQpdLPGRDVDApgdpivaiAR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 310 GFYqlcGVHQEDVIYLALPLYHmSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSK 389
Cdd:PRK13390 188 AFY---DISESDIYYSSAPIYH-AAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 390 AERGHKVRL-AVGSGLRP---DTWERFVRRFGPLqVLETYGLTEGNVATINYTGQ----RGAVGRASWLYKHIFpfslir 461
Cdd:PRK13390 264 RTRYDVSSLrAVIHAAAPcpvDVKHAMIDWLGPI-VYEYYSSTEAHGMTFIDSPDwlahPGSVGRSVLGDLHIC------ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 462 ydvttgepirDPQGHCMATspGEPGlLVAPVSQQSPFlGYAGGPE-LAQGKllkdvfRPGDVFFNT-GDLLVCDDQGFLR 539
Cdd:PRK13390 337 ----------DDDGNELPA--GRIG-TVYFERDRLPF-RYLNDPEkTAAAQ------HPAHPFWTTvGDLGSVDEDGYLY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 540 FHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVP--GHEGRAgMAALV--LRPPHALdLMQLYTHVSENLPP 615
Cdd:PRK13390 397 LADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemGEQVKA-VIQLVegIRGSDEL-ARELIDYTRSRIAH 474
|
490 500
....*....|....*....|...
gi 1393643644 616 YARPRFLRLQESLATTETFKQQK 638
Cdd:PRK13390 475 YKAPRSVEFVDELPRTPTGKLVK 497
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
286-631 |
2.48e-12 |
|
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: 69.32 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIylaLPLYHMS--GSLLGIVGCMGIGATVVLKSK---FSAGQ 359
Cdd:cd17649 100 IYTSGSTGTPKGVAVSHGPLAAhCQATAERYGLTPGDRE---LQFASFNfdGAHEQLLPPLICGACVVLRPDelwASADE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 FWEDCQQHRVTVFQ----YIGELCRYLVNQPPSKAERghkVRLAV--GSGLRPDTWERFvrRFGPLQVLETYGLTEGNVA 433
Cdd:cd17649 177 LAEMVRELGVTVLDlppaYLQQLAEEADRTGDGRPPS---LRLYIfgGEALSPELLRRW--LKAPVRLFNAYGPTEATVT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TINYTGQRGAvgRASWLYKHIfpfslirydvttGEP-------IRDPQGHcmATSPGEPGLLVapVSQQSPFLGYAGGPE 506
Cdd:cd17649 252 PLVWKCEAGA--ARAGASMPI------------GRPlggrsayILDADLN--PVPVGVTGELY--IGGEGLARGYLGRPE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 507 LAQGKLLKDVF-RPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEG 585
Cdd:cd17649 314 LTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV--VALDGAGG 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1393643644 586 RAGMAALVLRPPHAL--DLMQLYTHVSENLPPYARP-RFLRLqESLATT 631
Cdd:cd17649 392 KQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPaHLVFL-ARLPLT 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
164-638 |
2.85e-12 |
|
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: 69.08 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAG-----LRTAFVPTALRrgpllHCLRSCGARALVLAPEFLESLEpdlpalram 238
Cdd:cd05973 22 VGPGDVVAGLLPRTPELVVTILGIWRLGavyqpLFTAFGPKAIE-----HRLRTSGARLVVTDAANRHKLD--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 239 glhlwaagpgthpagisdllaevsaevdgpvpgylsspqsiTDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLC-GV 317
Cdd:cd05973 88 -----------------------------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAvDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 318 HQEDVIY-LALP-----LYHmsgsllGIVGCMGIG-ATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKA 390
Cdd:cd05973 127 RPEDSFWnAADPgwaygLYY------AITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 391 ERgHKVRLAV----GSGLRPDTWERFVRRFGpLQVLETYGLTEGNVATINYTG-----QRGAVGRAswlykhiFP-FSLI 460
Cdd:cd05973 201 AR-PKGRLRRvssaGEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHHAlehpvHAGSAGRA-------MPgWRVA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 461 RYDVTTGEPirdpqghcmatSPGEPGLLVAPVSqQSP---FLGYAGGPELAqgkllkdvfrPGDVFFNTGDLLVCDDQGF 537
Cdd:cd05973 272 VLDDDGDEL-----------GPGEPGRLAIDIA-NSPlmwFRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGS 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 538 LRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLRPPH--ALDLM-QLYTHVSENL 613
Cdd:cd05973 330 FSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG--VPDPErTEVVKAFVVLRGGHegTPALAdELQLHVKKRL 407
|
490 500
....*....|....*....|....*
gi 1393643644 614 PPYARPRFLRLQESLATTETFKQQK 638
Cdd:cd05973 408 SAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
281-635 |
3.19e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.49 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLK-ILQCQGFYQLCGVHQE----DVIYLA-LPLYHMSGSLLGIVGCMGIGATVVLKSK 354
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNlIAMVELFVRFEASQYEypgsDNVYLAaLPMFHIYGLSLFVVGLLSLGSTIVVMRR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 355 FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRP---DTWERFVRRFGPLQVLETYGLTEGN 431
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPlsgKFIQDFVQTLPHVDFIQGYGMTEST 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 432 vatinytgqrgAVGRASWLYKHIFPFSLIRY----------DVTTGEPIrdPQGHCMATSPGEPGLLVapvsqqspflGY 501
Cdd:PLN02574 359 -----------AVGTRGFNTEKLSKYSSVGLlapnmqakvvDWSTGCLL--PPGNCGELWIQGPGVMK----------GY 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 502 AGGPELAQGKLLKdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVP 581
Cdd:PLN02574 416 LNNPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA--VP 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 582 GHE-GRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:PLN02574 488 DKEcGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGK 542
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
272-626 |
1.17e-11 |
|
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: 67.33 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 272 YLSSPQsitDTCLYIFTSGTTGLPKAARISH---LKILQCQGFYQLCGVHQEDVIYLALPLyhmSGSLLGIVGCMGIGAT 348
Cdd:cd17653 100 TTDSPD---DLAYIIFTSGSTGIPKGVMVPHrgvLNYVSQPPARLDVGPGSRVAQVLSIAF---DACIGEIFSTLCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 349 VVLKSkfsAGQFWEDCQQhRVTVFQYIGELcryLVNQPPSKAERGHKVRLAvGSGLRP---DTWeRFVRRFgplqvLETY 425
Cdd:cd17653 174 LVLAD---PSDPFAHVAR-TVDALMSTPSI---LSTLSPQDFPNLKTIFLG-GEAVPPsllDRW-SPGRRL-----YNAY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 426 GLTEGNVATinytgqrgavgraswLYKHIFPfsliRYDVTTGEPIR-------DPQGhcMATSPGEPGLLVapVSQQSPF 498
Cdd:cd17653 240 GPTECTISS---------------TMTELLP----GQPVTIGKPIPnstcyilDADL--QPVPEGVVGEIC--ISGVQVA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 499 LGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDflqeVNVYGV 578
Cdd:cd17653 297 RGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ----PEVTQA 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1393643644 579 TVPGHEGRagMAALVLrpPHALDLMQLYTHVSENLPPYARP-RFLRLQE 626
Cdd:cd17653 373 AAIVVNGR--LVAFVT--PETVDVDGLRSELAKHLPSYAVPdRIIALDS 417
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
166-622 |
1.25e-11 |
|
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: 67.11 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPtalrrgpllhclrscgaralvlapeflesLEPDLPALRamglhlwaa 245
Cdd:cd17650 36 PGSVVGVCADRSLDAIVGLLAVLKAG--GAYVP-----------------------------IDPDYPAER--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 246 gpgthpagISDLLAEVSAEVdgpvpgYLSSPqsiTDTCLYIFTSGTTGLPKAARISHLKILQCqgfyqlcgVHQEDVIY- 324
Cdd:cd17650 76 --------LQYMLEDSGAKL------LLTQP---EDLAYVIYTSGTTGKPKGVMVEHRNVAHA--------AHAWRREYe 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 325 -LALPLYHMSGSLLGIVGCMG-------IGATVVL---KSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERG 393
Cdd:cd17650 131 lDSFPVRLLQMASFSFDVFAGdfarsllNGGTLVIcpdEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 394 HKVR-LAVGSGLRPDTWER-FVRRFGP-LQVLETYGLTEGNVATINYTGQRGAVGRASwlykhifpfsliryDVTTGEPI 470
Cdd:cd17650 211 SAMRlLIVGSDGCKAQDFKtLAARFGQgMRIINSYGVTEATIDSTYYEEGRDPLGDSA--------------NVPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 -----------RDPQGHCMAtspGEPGLLVAPVSQqspflGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLR 539
Cdd:cd17650 277 pntamyvlderLQPQPVGVA---GELYIGGAGVAR-----GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 540 FHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEGRAGMAALVLrPPHALDLMQLYTHVSENLPPYARP 619
Cdd:cd17650 349 LLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV--AVREDKGGEARLCAYVV-AAATLNTAELRAFLAKELPSYMIP 425
|
...
gi 1393643644 620 RFL 622
Cdd:cd17650 426 SYY 428
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
280-620 |
1.32e-11 |
|
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: 67.55 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 280 TDTCLYIFTSGTTGLPKAARISHLKIL----QCQGFYQLCGVHQEDVIYLALPLYHMSG--SLLGIVGCmgiGATVVLKS 353
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVarfsHARDPIFGNQIIPDTAILTVIPFHHGFGmfTTLGYLIC---GFRVVLMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 354 KFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQP-PSKAERGHKVRLAVGSG-LRPDTWERFVRRFGPLQVLETYGLTEGN 431
Cdd:cd17642 261 KFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 432 VATI--NYTGQR-GAVGRaswlykhIFPFSLIRY-DVTTGEPIrdpqghcmatSPGEPGLLVApvsqQSPFL--GYAGGP 505
Cdd:cd17642 341 SAILitPEGDDKpGAVGK-------VVPFFYAKVvDLDTGKTL----------GPNERGELCV----KGPMImkGYVNNP 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 506 ELAQGKLLKdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEG 585
Cdd:cd17642 400 EATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE-DAG 472
|
330 340 350
....*....|....*....|....*....|....*
gi 1393643644 586 RAGMAALVLRPPHALDLMQLYTHVSENLPPYARPR 620
Cdd:cd17642 473 ELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
286-631 |
1.69e-11 |
|
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: 67.07 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIyLALPLYHMSGSLLGIVGCMGIGATVVLKSK---FSAGQFW 361
Cdd:cd17644 112 IYTSGSTGKPKGVMIEHQSLVNlSHGLIKEYGITSSDRV-LQFASIAFDVAAEEIYVTLLSGATLVLRPEemrSSLEDFV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 362 EDCQQHRVTVFQYIGELCRYLVNQ-PPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPL-QVLETYGLTEGNVATIny 437
Cdd:cd17644 191 QYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLRLVIvgGEAVQPELVRQWQKNVGNFiQLINVYGPTEATIAAT-- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 438 tgqrgavgraswLYKHIFPFSLIRYDVTTGEPIRDPQGHCM-----ATSPGEPG-LLVAPVSQQSpflGYAGGPELAQGK 511
Cdd:cd17644 269 ------------VCRLTQLTERNITSVPIGRPIANTQVYILdenlqPVPVGVPGeLHIGGVGLAR---GYLNRPELTAEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 512 LLKDVFR--PGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVfealdFLQEVNVYGVTVPGHEGRAG- 588
Cdd:cd17644 334 FISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV-----LSQHNDVKTAVVIVREDQPGn 408
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1393643644 589 ---MAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:cd17644 409 krlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLT 454
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
286-626 |
1.75e-11 |
|
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: 66.95 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKILQ----CQGFYqlcGVHQEDVIYlalpLYHMSG---SLLGIVGCMGIGATVVLKSKF--- 355
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVLAlfaaTQRWF---GFNEDDVWT----LFHSYAfdfSVWEIWGALLHGGRLVVVPYEvar 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 356 SAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVRRFGPL--QVLETYGLTEgn 431
Cdd:cd17643 172 SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDrpQLVNMYGITE-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 432 vATINYTgqrgavgraswlYKHIFPFSLIRYDVTT-GEPIRDPQGHCMATS-----PGEPGLLVAPVSQQSPflGYAGGP 505
Cdd:cd17643 250 -TTVHVT------------FRPLDAADLPAAAASPiGRPLPGLRVYVLDADgrpvpPGVVGELYVSGAGVAR--GYLGRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 506 ELAQGKLLKDVF-RPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVattEVAEVFEALDFLQEVNVYGVTVpgHE 584
Cdd:cd17643 315 ELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRI---ELGEIEAALATHPSVRDAAVIV--RE 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1393643644 585 GRAG----MAALVLRPPHALDLMQLYTHVSENLPPYARP-RFLRLQE 626
Cdd:cd17643 390 DEPGdtrlVAYVVADDGAAADIAELRALLKELLPDYMVPaRYVPLDA 436
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
281-577 |
2.08e-11 |
|
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: 66.61 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVgCMGIGATVVLKSKFSAGQ 359
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYTSIRTLKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 FWEDCQQH------RVTVFQYIGeLCRYLVNQPPSK------AERGHKVRLAV-GSGLRPDTWERFVRRFGpLQVLETYG 426
Cdd:cd17640 168 DLKRVKPHyivsvpRLWESLYSG-IQKQVSKSSPIKqflflfFLSGGIFKFGIsGGGALPPHVDTFFEAIG-IEVLNGYG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 427 LTE-GNVATINYTGQ--RGAVGraswlykHIFPFSLIRydvttgepIRDPQGHcMATSPGEPGLLVApvsqQSP--FLGY 501
Cdd:cd17640 246 LTEtSPVVSARRLKCnvRGSVG-------RPLPGTEIK--------IVDPEGN-VVLPPGEKGIVWV----RGPqvMKGY 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393643644 502 AGGPElAQGKLLKDvfrpgDVFFNTGDL--LVCDdqGFLRFHDRTGDTFRWK-GENVATTEVAEVFEALDFLQEVNVYG 577
Cdd:cd17640 306 YKNPE-ATSKVLDS-----DGWFNTGDLgwLTCG--GELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
272-651 |
2.63e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.75 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 272 YLSSPQSITDTClyiFTSGTTGLPKAARISHLK-ILQCQGFYQLCGVHQEDVIYLALPLYHMSgsllGIVGCMGI---GA 347
Cdd:PLN02860 167 YAWAPDDAVLIC---FTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHIG----GLSSALAMlmvGA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 348 TVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNqpPSKAERGHKVRLAV------GSGLRPDTWERFVRRFGPLQV 421
Cdd:PLN02860 240 CHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMTWKVFPSVrkilngGGSLSSRLLPDAKKLFPNAKL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 422 LETYGLTEgnvatinytgqrgAVGRASWLYKH-----IFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLV-APVSQQ 495
Cdd:PLN02860 318 FSAYGMTE-------------ACSSLTFMTLHdptleSPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIgLDESSR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 496 S-------P--FLGYAGGPELAQGKllkdvfRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVfea 566
Cdd:PLN02860 385 VgriltrgPhvMLGYWGQNSETASV------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV--- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 567 ldFLQEVNVYGVTVPG-HEGRAG-MAALVLR-----------PPHALDLMQ-----LYTHVSE-NLPPYARPR-FLRLQE 626
Cdd:PLN02860 456 --LSQHPGVASVVVVGvPDSRLTeMVVACVRlrdgwiwsdneKENAKKNLTlssetLRHHCREkNLSRFKIPKlFVQWRK 533
|
410 420 430
....*....|....*....|....*....|
gi 1393643644 627 SLATTETFKQQK--VR---MANEGFDPSTL 651
Cdd:PLN02860 534 PFPLTTTGKIRRdeVRrevLSHLQSLPSNL 563
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
167-371 |
6.73e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.39 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 167 GATVALLLPAGPEFLWLWFGLAKAG--LRTA---FVPTALRRGpllhcLRSCGARALVLAPEFLESLePDLPALRAMGLH 241
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGavTTTAnpfYTPAEIAKQ-----AKASGAKLIITQSCYVDKL-KGLAEDDGVTVV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 242 LwaagPGTHPAG---ISDLLAEVSAEVDGPVpgylSSPQsitDTCLYIFTSGTTGLPKAARISHlKIL------QCQG-- 310
Cdd:PLN02246 149 T----IDDPPEGclhFSELTQADENELPEVE----ISPD---DVVALPYSSGTTGLPKGVMLTH-KGLvtsvaqQVDGen 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393643644 311 --FYqlcgVHQEDVIYLALPLYHMSgSLLGIVGC-MGIGATVVLKSKFSAGQFWEDCQQHRVTV 371
Cdd:PLN02246 217 pnLY----FHSDDVILCVLPMFHIY-SLNSVLLCgLRVGAAILIMPKFEIGALLELIQRHKVTI 275
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
166-641 |
6.92e-11 |
|
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: 65.34 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAG--LRTAFVptalRRGP--LLHCLRSCGARALVLAPEFL---ESLEPDLPALRAM 238
Cdd:cd12119 49 PGDRVATLAWNTHRHLELYYAVPGMGavLHTINP----RLFPeqIAYIINHAEDRVVFVDRDFLpllEAIAPRLPTVEHV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 239 GLHLWAAG-PGTHPAGI---SDLLAEVSAEVDGPVpgylSSPQSITDTClyiFTSGTTGLPKAARISH-------LKILQ 307
Cdd:cd12119 125 VVMTDDAAmPEPAGVGVlayEELLAAESPEYDWPD----FDENTAAAIC---YTSGTTGNPKGVVYSHrslvlhaMAALL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 308 CQGFyqlcGVHQEDVIYLALPLYHMSGSLLGIVGCMgIGATVVLKSKFSAG----QFWEdcqQHRVTVFQ-----YIGEL 378
Cdd:cd12119 198 TDGL----GLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAKLVLPGPYLDPaslaELIE---REGVTFAAgvptvWQGLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 379 CRYLVNqppsKAERGHKVRLAV-GSGLRPDTWERFVRRFgpLQVLETYGLTE----GNVATINyTGQRGAVGRASWlykh 453
Cdd:cd12119 270 DHLEAN----GRDLSSLRRVVIgGSAVPRSLIEAFEERG--VRVIHAWGMTEtsplGTVARPP-SEHSNLSEDEQL---- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 454 ifpfsliRYDVTTGEP-------IRDPQGHCMATSPGEPGLLVApvsqQSPFL--GYAGGPELAQGKLlkdvfrpGDVFF 524
Cdd:cd12119 339 -------ALRAKQGRPvpgvelrIVDDDGRELPWDGKAVGELQV----RGPWVtkSYYKNDEESEALT-------EDGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 525 NTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTvpgHE--GRAGMAALVLRPPHALDL 602
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP---HPkwGERPLAVVVLKEGATVTA 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 1393643644 603 MQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
281-620 |
7.94e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 64.33 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKILQCQG---------FYQLCGVHQEDV------IYLALPLYHMSGSLLGIVGCMGI 345
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMggadfgtgeFTPSEDAHKAAAaaagtvMFPAPPLMHGTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 346 GATVVLKSKFSAGQFWEDCQQHRVTVFQYIGE-LCRYLVNQppskAERGHKVRL----AVGSG---LRPDTWERFVRRFG 417
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDA----LRDAGPYDLsslfAISSGgalLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 418 PLQVLETYGLTEGNVATINYTGQRGAVGRaswlykhifPFSLIRYDVTtgepIRDPQGHCMATSPGEPGLL----VAPvs 493
Cdd:cd05924 160 NITLVDAFGSSETGFTGSGHSAGSGPETG---------PFTRANPDTV----VLDDDGRVVPPGSGGVGWIarrgHIP-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 494 qqspfLGYAGGPElaqgKLLKDVFRPGDVFFN-TGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEAldflqE 572
Cdd:cd05924 225 -----LGYYGDEA----KTAETFPEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-----H 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 573 VNVYGVTVPGH-EGRAG--MAALV-LRPPHALDLMQLYTHVSENLPPYARPR 620
Cdd:cd05924 291 PAVYDVLVVGRpDERWGqeVVAVVqLREGAGVDLEELREHCRTRIARYKLPK 342
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
164-340 |
9.82e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 64.51 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWfgLAkaglrtafvptALRrgpllhclrsCGARALVLAPEFLESLEPDLpaLRAMGL-HL 242
Cdd:PRK09029 50 VVEGSGVALRGKNSPETLLAY--LA-----------LLQ----------CGARVLPLNPQLPQPLLEEL--LPSLTLdFA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 243 WAAGPGTHPAGISDLLAEVSAEVDgPVPGYLSSPQSITdtclyiFTSGTTGLPKAARIS---HLKilQCQGFYQLCGVHQ 319
Cdd:PRK09029 105 LVLEGENTFSALTSLHLQLVEGAH-AVAWQPQRLATMT------LTSGSTGLPKAAVHTaqaHLA--SAEGVLSLMPFTA 175
|
170 180
....*....|....*....|.
gi 1393643644 320 EDVIYLALPLYHMSGslLGIV 340
Cdd:PRK09029 176 QDSWLLSLPLFHVSG--QGIV 194
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
208-556 |
2.51e-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: 63.26 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 208 HCLRSCGARALVLAP----EFLESLEPDLPALRAMGLHlwaaGPGTHPAGISDLLAEVSAEVDGPVPGylssPQSITDTc 283
Cdd:cd05932 72 YVLEHSESKALFVGKlddwKAMAPGVPEGLISISLPPP----SAANCQYQWDDLIAQHPPLEERPTRF----PEQLATL- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 284 lyIFTSGTTGLPKAARISHLKI-LQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSkfSAGQFWE 362
Cdd:cd05932 143 --IYTSGTTGQPKGVMLTFGSFaWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 363 DCQQHRVTVFQYIGELC-----RYLVNQPPSKAER-----------GHKV---------RLAV-GSGLRPDTWERFVRRF 416
Cdd:cd05932 219 DVQRARPTLFFSVPRLWtkfqqGVQDKIPQQKLNLllkipvvnslvKRKVlkglgldqcRLAGcGSAPVPPALLEWYRSL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 417 GpLQVLETYGLTEG-NVATINYTGQR--GAVGRASwlykhifpfslirydvtTGEPIR-DPQGHCMATSPGEpgllvapv 492
Cdd:cd05932 299 G-LNILEAYGMTENfAYSHLNYPGRDkiGTVGNAG-----------------PGVEVRiSEDGEILVRSPAL-------- 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 493 sqqspFLGYAGGPElAQGKLLKDvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDTFRW-KGENVA 556
Cdd:cd05932 353 -----MMGYYKDPE-ATAEAFTA-----DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVA 406
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
206-621 |
2.68e-10 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 62.96 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 206 LLHCLRSCGA----RALVLAPEFLESLEPDLPALRAMGLHLwAAGPGTHPAGISDLLAEVSAEVdgpvpgYLSSPQsitD 281
Cdd:cd17645 36 LARHLRGKGVkpddQVGIMLDKSLDMIAAILGVLKAGGAYV-PIDPDYPGERIAYMLADSSAKI------LLTNPD---D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 282 TCLYIFTSGTTGLPKAARISHLKILQCQGFYQLC-GVHQED--VIYLAlplYHMSGSLLGIVGCMGIGATV-VLKS--KF 355
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfGVTPADksLVYAS---FSFDASAWEIFPHLTAGAALhVVPSerRL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 356 SAGQFWEDCQQHRVTVfqyigelcRYLvnqPPSKAER-----GHKVRLAVGSGlrpDTWERFVRRfgPLQVLETYGLTEG 430
Cdd:cd17645 183 DLDALNDYFNQEGITI--------SFL---PTGAAEQfmqldNQSLRVLLTGG---DKLKKIERK--GYKLVNNYGPTEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 431 NVATINytgqrgavgraswlykhiFPFSLIRYDVTTGEPIRDPQ----GHCMATSP-GEPGLLVapVSQQSPFLGYAGGP 505
Cdd:cd17645 247 TVVATS------------------FEIDKPYANIPIGKPIDNTRvyilDEALQLQPiGVAGELC--IAGEGLARGYLNRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 506 ELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEG 585
Cdd:cd17645 307 ELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDADG 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 1393643644 586 RAGMAALVLrPPHALDLMQLYTHVSENLPPYARPRF 621
Cdd:cd17645 385 RKYLVAYVT-APEEIPHEELREWLKNDLPDYMIPTY 419
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
273-626 |
1.21e-09 |
|
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: 61.19 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 273 LSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLK 352
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 353 SKFSAGQFWEDCQ---QHRVTVfqyIGELCRYLVNQPPSKAERGHKVR--LAVGSGLRPDTWERFVRRFGP-LQVLETYG 426
Cdd:cd17655 210 RKETVLDGQALTQyirQNRITI---IDLTPAHLKLLDAADDSEGLSLKhlIVGGEALSTELAKKIIELFGTnPTITNAYG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 427 LTEGnvatinytgqrgAVGRASWLYKhifPFSLIRYDVTTGEP-------IRDPQGHCMATspGEPGLLVapVSQQSPFL 499
Cdd:cd17655 287 PTET------------TVDASIYQYE---PETDQQVSVPIGKPlgntriyILDQYGRPQPV--GVAGELY--IGGEGVAR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 500 GYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVT 579
Cdd:cd17655 348 GYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV--IA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1393643644 580 VPGHEGRAGMAALVLRPPHaLDLMQLYTHVSENLPPYARPR-FLRLQE 626
Cdd:cd17655 426 RKDEQGQNYLCAYIVSEKE-LPVAQLREFLARELPDYMIPSyFIKLDE 472
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
559-635 |
2.40e-09 |
|
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: 54.09 E-value: 2.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393643644 559 EVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
165-600 |
4.29e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.18 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 165 SPGATVALLLPAGPEFLWLWFGLAKAGLRT--AFVPTALRRGPLLHcLRSCGARAlvlAPEFLESLEPDLPALRAMGLHL 242
Cdd:PRK05691 62 SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAvpAYPPESARRHHQER-LLSIIADA---EPRLLLTVADLRDSLLQMEELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 243 WAAGPGThpAGISDLLAEVSAEVDGP-VPGylsspqsiTDTCLYIFTSGTTGLPKAARISHLKI-----LQCQGFYqlCG 316
Cdd:PRK05691 138 AANAPEL--LCVDTLDPALAEAWQEPaLQP--------DDIAFLQYTSGSTALPKGVQVSHGNLvaneqLIRHGFG--ID 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 317 VHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLkskFSAGQF------W-EDCQQHRVTV-----FQYigELCRYLVN 384
Cdd:PRK05691 206 LNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPAYFlerplrWlEAISEYGGTIsggpdFAY--RLCSERVS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 385 QppSKAER----GHKVRLAVGSGLRPDTWERFVRRFG-----PLQVLETYGLTEgnvATINYTGQRGAVGRASwLYKHIF 455
Cdd:PRK05691 281 E--SALERldlsRWRVAYSGSEPIRQDSLERFAEKFAacgfdPDSFFASYGLAE---ATLFVSGGRRGQGIPA-LELDAE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 456 PFSLIRYDVTTGEPIRDpqghCMATSPGEPGLLVAPVSQQSpfLG-------YAGGPELAQGKLLKD-------VFRPGD 521
Cdd:PRK05691 355 ALARNRAEPGTGSVLMS----CGRSQPGHAVLIVDPQSLEV--LGdnrvgeiWASGPSIAHGYWRNPeasaktfVEHDGR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 522 VFFNTGDLlvcddqGFLRFHD-----RTGDTFRWKGENVATTEVAEVFEA-LDFLQE--VNVYGVTVPGHEGrAGMAALV 593
Cdd:PRK05691 429 TWLRTGDL------GFLRDGElfvtgRLKDMLIVRGHNLYPQDIEKTVEReVEVVRKgrVAAFAVNHQGEEG-IGIAAEI 501
|
490
....*....|...
gi 1393643644 594 LR------PPHAL 600
Cdd:PRK05691 502 SRsvqkilPPQAL 514
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
251-642 |
8.23e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 58.48 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 251 PAGISDLLAEVSAEVDGPVPGYLSS-PQSITDTCL-YIFTSGTTGLPKAARISHLK------ILQCQGFYQLCGVHQEdV 322
Cdd:PRK05857 138 PVIAVDIAAVTRESEHSLDAASLAGnADQGSEDPLaMIFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWVVGE-T 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IYLALPLYHMSGsLLGIVGCMGIGATVVLKSKFSAgQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGS 402
Cdd:PRK05857 217 TYSPLPATHIGG-LWWILTCLMHGGLCVTGGENTT-SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 403 GLRPDTWE-RFVRRFGpLQVLETYGLTE------------GNVATInytgQRGAVGRaswlykhifPFSLIRYDVTtgep 469
Cdd:PRK05857 295 GSRAIAADvRFIEATG-VRTAQVYGLSEtgctalclptddGSIVKI----EAGAVGR---------PYPGVDVYLA---- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 470 irDPQGHCMATSPGEPGLLVAPVSQQSP--FLGYAGGPELAQGKLLkdvfrpgDVFFNTGDLLVCDDQGFLRFHDRTGDT 547
Cdd:PRK05857 357 --ATDGIGPTAPGAGPSASFGTLWIKSPanMLGYWNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEM 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 548 FRWKGENVATTEVAEVFEALDFLQEVNVYgvTVPGHE-----GRAGMAALVLRPPHALDLMQL----YTHVSENLppyAR 618
Cdd:PRK05857 428 IICGGVNIAPDEVDRIAEGVSGVREAACY--EIPDEEfgalvGLAVVASAELDESAARALKHTiaarFRRESEPM---AR 502
|
410 420
....*....|....*....|....
gi 1393643644 619 PRFLRLQESLATTETFKQQKVRMA 642
Cdd:PRK05857 503 PSTIVIVTDIPRTQSGKVMRASLA 526
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
169-635 |
1.51e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 57.48 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 169 TVALLLPAGPEFLWLWFGLAKAGLrTAfVPTALR--RGPLLHCLRSCGARALVLAPEFLESL-EPDLPALRamglhlwaa 245
Cdd:PRK07638 52 TIAILLENRIEFLQLFAGAAMAGW-TC-VPLDIKwkQDELKERLAISNADMIVTERYKLNDLpDEEGRVIE--------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 246 gpgthpagISDLLAEVSAEVDGPVPGylsspQSITDTCLYI-FTSGTTGLPKA---ARISHLKILQC--QGFyqlcGVHQ 319
Cdd:PRK07638 121 --------IDEWKRMIEKYLPTYAPI-----ENVQNAPFYMgFTSGSTGKPKAflrAQQSWLHSFDCnvHDF----HMKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 320 EDVIYLALPLYHmSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQppsKAERGHKVRLa 399
Cdd:PRK07638 184 EDSVLIAGTLVH-SLFLYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKI- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 400 VGSGLRpdtW-----ERFVRRFGPLQVLETYGLTEGNVATI----NYTGQRGAVGRaswlykhifPFSLIRYDVTtgepi 470
Cdd:PRK07638 259 ISSGAK---WeaeakEKIKNIFPYAKLYEFYGASELSFVTAlvdeESERRPNSVGR---------PFHNVQVRIC----- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 471 RDPQGHCMatsPGEPGLLVApvsqQSP--FLGYAGGPELAQGKllkdvfrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTF 548
Cdd:PRK07638 322 NEAGEEVQ---KGEIGTVYV----KSPqfFMGYIIGGVLAREL-------NADGWMTVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 549 RWKGENVATTEVAEVFEALDFLQEVNVYGVTVP--GHEgragMAALVLRPPHAldlMQLYTHVSENLPPYARPRFLRLQE 626
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSywGEK----PVAIIKGSATK---QQLKSFCLQRLSSFKIPKEWHFVD 460
|
....*....
gi 1393643644 627 SLATTETFK 635
Cdd:PRK07638 461 EIPYTNSGK 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
77-638 |
1.68e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.65 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 77 QRAA-----HTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefagg 151
Cdd:PRK08162 25 ERAAevypdRPAVIHGDRRRTWAETYARCRRLASA-LARRG--------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 152 dgaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAG--LRTafVPTALRRGPLLHCLRSCGARALVLAPEFLESLE 229
Cdd:PRK08162 65 ------------IGRGDTVAVLLPNIPAMVEAHFGVPMAGavLNT--LNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 230 PdlpALRAM-GLHLW------AAGPGTHPAGISD---LLAEVSAEVDGPVPGylSSPQSITDTclyiFTSGTTGLPKAAR 299
Cdd:PRK08162 131 E---ALALLpGPKPLvidvddPEYPGGRFIGALDyeaFLASGDPDFAWTLPA--DEWDAIALN----YTSGTTGNPKGVV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 300 ISHL-KILQCQGFYQLCGVHQEDViYL-ALPLYHmsgsllgivgCMG---------IGATVVLKSKFSAGQFWEDCQQHR 368
Cdd:PRK08162 202 YHHRgAYLNALSNILAWGMPKHPV-YLwTLPMFH----------CNGwcfpwtvaaRAGTNVCLRKVDPKLIFDLIREHG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 369 VTvfqyigELC------RYLVNQPPS-KAERGHKVRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTE--GNvATINytg 439
Cdd:PRK08162 271 VT------HYCgapivlSALINAPAEwRAGIDHPVHAMVAGAAPPAAVIAKMEEIG-FDLTHVYGLTEtyGP-ATVC--- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 440 qrgaVGRASWlykHIFPFSL---------IRYDVTTGEPIRDPQghCMATSP------GE---PGLLVAPvsqqspflGY 501
Cdd:PRK08162 340 ----AWQPEW---DALPLDEraqlkarqgVRYPLQEGVTVLDPD--TMQPVPadgetiGEimfRGNIVMK--------GY 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 502 AGGPELAQgkllkDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVfeaLDFLQEVNVYGVTVP 581
Cdd:PRK08162 403 LKNPKATE-----EAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDV---LYRHPAVLVAAVVAK 472
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393643644 582 GHE--GRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQEsLATTETFKQQK 638
Cdd:PRK08162 473 PDPkwGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQK 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
286-631 |
2.51e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKILQ----CQGFYQLCGvhqEDVIYLALPlYHMSGSLLGIVGCMGIGATVVLK---SKFSAG 358
Cdd:PRK12467 1724 IYTSGSTGRPKGAGNRHGALVNrlcaTQEAYQLSA---ADVVLQFTS-FAFDVSVWELFWPLINGARLVIAppgAHRDPE 1799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 359 QFWEDCQQHRVTVFQYIGELCRYLVnQPPSKAERGHKVRLAVGSG--LRPDTWERFVRRFGPLQVLETYGLTEgnvATIN 436
Cdd:PRK12467 1800 QLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHPLSLRRVVCGGeaLEVEALRPWLERLPDTGLFNLYGPTE---TAVD 1875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 437 YTgqrgavgraSWLYKHIFPFSliRYDVTTGEPIRDPQGHCMatspgEPGLLVAPVSQQSPFlgYAGGPELAQGKLLkdv 516
Cdd:PRK12467 1876 VT---------HWTCRRKDLEG--RDSVPIGQPIANLSTYIL-----DASLNPVPIGVAGEL--YLGGVGLARGYLN--- 1934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 517 fRPGdvffNTGDLLVCD--DQGFLRFHdRTGDTFRWKGENVAT---------------TEVAEVfEAlDFLQEVNVYGVT 579
Cdd:PRK12467 1935 -RPA----LTAERFVADpfGTVGSRLY-RTGDLARYRADGVIEylgridhqvkirgfrIELGEI-EA-RLREQGGVREAV 2006
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 580 VPGHEGRAG---MAALVLRPPHALDLM--------QLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK12467 2007 VIAQDGANGkqlVAYVVPTDPGLVDDDeaqvalraILKNHLKASLPEYMVPAHLVFLARMPLT 2069
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
166-631 |
3.32e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.27 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrTAFVPTALR--RGPLLHCLRSCGArALVLAPEFLEslePDLPAlramglhlw 243
Cdd:PRK12316 4600 PEVLVGIAMERSAEMMVGLLAVLKAG--GAYVPLDPEypRERLAYMMEDSGA-ALLLTQSHLL---QRLPI--------- 4664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aagpgthPAGISDLlaevSAEVDGPVPGYLSS-PQSITDT---CLYIFTSGTTGLPKAARISHLKILQCQGFY-QLCGVH 318
Cdd:PRK12316 4665 -------PDGLASL----ALDRDEDWEGFPAHdPAVRLHPdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHATgERYELT 4733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 319 QEDVIyLALPLYHMSGSLLGIVGCMGIGATVVLK--SKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGH-K 395
Cdd:PRK12316 4734 PDDRV-LQFMSFSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSlR 4812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 396 VRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINYTGQRGAVGRASwlYKHIfpfslirydvttGEPIRDPQG 475
Cdd:PRK12316 4813 VYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAA--YMPI------------GTPLGNRSG 4878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 476 HCMATSpGEPgllvAPVSQQSPFL--------GYAGGPELAQGKLLKDVF-RPGDVFFNTGDLLVCDDQGFLRFHDRTGD 546
Cdd:PRK12316 4879 YVLDGQ-LNP----LPVGVAGELYlggegvarGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDH 4953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 547 TFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEGRAGMAALVLRPPHALDLM--------QLYTHVSENLPPYAR 618
Cdd:PRK12316 4954 QVKIRGFRIELGEIEARLREHPAVREAVV--IAQEGAVGKQLVGYVVPQDPALADADeaqaelrdELKAALRERLPEYMV 5031
|
490
....*....|...
gi 1393643644 619 PRFLRLQESLATT 631
Cdd:PRK12316 5032 PAHLVFLARMPLT 5044
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
164-635 |
4.95e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 56.16 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLepdlpalramglhlw 243
Cdd:PRK13383 82 VAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERI--------------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aAGPGTHPAGISDllAEVSAEVDGPVPGyLSSPQSITdtclyIFTSGTTGLPKAA-RISHLK--ILQCQGFYQLCGVHQE 320
Cdd:PRK13383 147 -AGADDAVAVIDP--ATAGAEESGGRPA-VAAPGRIV-----LLTSGTTGKPKGVpRAPQLRsaVGVWVTILDRTRLRTG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 321 DVIYLALPLYHMSGslLG-IVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGH--KVR 397
Cdd:PRK13383 218 SRISVAMPMFHGLG--LGmLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPlpQLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 398 LAVGSG--LRPDTWERFVRRFGPLqVLETYGLTE---GNVATinytgqrgavgraswlykhifPFSLIRYDVTTGEPIrd 472
Cdd:PRK13383 296 VVMSSGdrLDPTLGQRFMDTYGDI-LYNGYGSTEvgiGALAT---------------------PADLRDAPETVGKPV-- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 473 pqGHCMATSPGEPGLLVAPVSQQSPFLGyaggpelaqGKLLKDVFRPG------DVFFNTGDLLVCDDQGFLRFHDRTGD 546
Cdd:PRK13383 352 --AGCPVRILDRNNRPVGPRVTGRIFVG---------GELAGTRYTDGggkavvDGMTSTGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 547 TFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQ 625
Cdd:PRK13383 421 MIISGGENVYPRAVENALAAHPAVADNAVIG--VPDERfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIV 498
|
490
....*....|
gi 1393643644 626 ESLATTETFK 635
Cdd:PRK13383 499 SSIPRNPTGK 508
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
278-635 |
5.24e-08 |
|
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: 55.87 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 278 SITDTCLYIFTSGTTGLPKAARISHLKILQCQ----GFYQLCGVHQEDVIYLA-----LPLYHMSGSLLGivgcmgiGAT 348
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRtslsERYFGRDNGDEAVLFFSnyvfdFFVEQMTLALLN-------GQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 349 VVLKS---KFSAGQFWEDCQQHRVTvfqyigelcrYLvNQPPSK------AERGH-KVRLAVGSGLRPDTWERFVRRFgP 418
Cdd:cd17648 165 LVVPPdemRFDPDRFYAYINREKVT----------YL-SGTPSVlqqydlARLPHlKRVDAAGEEFTAPVFEKLRSRF-A 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 419 LQVLETYGLTEGNVATInytgqrgavgraswlyKHIFPFSLiRYDVTTGEPIRDPQ----GHCMATSP----GE---PGL 487
Cdd:cd17648 233 GLIINAYGPTETTVTNH----------------KRFFPGDQ-RFDKSLGRPVRNTKcyvlNDAMKRVPvgavGElylGGD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 488 LVAPvsqqspflGYAGGPELAQGKLLKDVFR-PGDV-------FFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTE 559
Cdd:cd17648 296 GVAR--------GYLNRPELTAERFLPNPFQtEQERargrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 560 VAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALV---LRPPHALDLMQLYTHVSENLPPYARP-RFLRLqESLATTETFK 635
Cdd:cd17648 368 VEAALASYPGVRECAVVAKEDASQAQSRIQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPaRLVRL-EGIPVTINGK 446
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
61-371 |
6.86e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 55.67 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 61 PEGGCSLAW----RLAE--LAQQRAAHTFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsAGEGERaa 134
Cdd:PRK04319 38 ETGKVNIAYeaidRHADggRKDKVALRYLDASRKEKYTYKELKELSNKFANV-LKELG--------------VEKGDR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 135 pgagdaaagsgaefaggdgaargggaaaplspgatVALLLPAGPEFLWLWFGLAKAG-----LRTAFVPTALR-Rgpllh 208
Cdd:PRK04319 101 -----------------------------------VFIFMPRIPELYFALLGALKNGaivgpLFEAFMEEAVRdR----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 209 cLRSCGARALVLAPEFLESL-EPDLPALRAMglhLWAAGPGTHPAGISD---LLAEVSAEVDGPvpgylssPQSITDTCL 284
Cdd:PRK04319 141 -LEDSEAKVLITTPALLERKpADDLPSLKHV---LLVGEDVEEGPGTLDfnaLMEQASDEFDIE-------WTDREDGAI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 285 YIFTSGTTGLPKAARISHLKILQ--CQGFYQLcGVHQEDVIY-LALPLYhMSGSLLGIVGCMGIGAT-VVLKSKFSAGQF 360
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLQhyQTGKYVL-DLHEDDVYWcTADPGW-VTGTSYGIFAPWLNGATnVIDGGRFSPERW 287
|
330
....*....|.
gi 1393643644 361 WEDCQQHRVTV 371
Cdd:PRK04319 288 YRILEDYKVTV 298
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
248-631 |
8.82e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 248 GTHPAGIS-----DLLAEVSAEVDGPVPgYLSSPQSitdTCLYIFTSGTTGLPKAARISHLKI-LQCQGFYQLCGVHQED 321
Cdd:PRK05691 2300 GELPAGVArwcleDDAAALAAYSDAPLP-FLSLPQH---QAYLIYTSGSTGKPKGVVVSHGEIaMHCQAVIERFGMRADD 2375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 322 ViylALPLYHM-----SGSLLGIVGCmgiGATVVLKSKfsaGQfW---EDCQ---QHRVTVF----QYIGELCRYLVNQp 386
Cdd:PRK05691 2376 C---ELHFYSInfdaaSERLLVPLLC---GARVVLRAQ---GQ-WgaeEICQlirEQQVSILgftpSYGSQLAQWLAGQ- 2444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 387 pskaERGHKVRLAV--GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATI-NYTGQRGAVGRASwlykhifpfsliryd 463
Cdd:PRK05691 2445 ----GEQLPVRMCItgGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLaCLAPEQLEEGAAS--------------- 2505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 464 VTTGEPIRDPQGHCMATSpgepgllVAPVSQQSPFLGYAGGPELAQG----------KLLKDVFRP-GDVFFNTGDLLVC 532
Cdd:PRK05691 2506 VPIGRVVGARVAYILDAD-------LALVPQGATGELYVGGAGLAQGyhdrpgltaeRFVADPFAAdGGRLYRTGDLVRL 2578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 533 DDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMaaLVLRPPHALDLMQ------LY 606
Cdd:PRK05691 2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGY--LVSAVAGQDDEAQaalreaLK 2656
|
410 420
....*....|....*....|....*
gi 1393643644 607 THVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK05691 2657 AHLKQQLPDYMVPAHLILLDSLPLT 2681
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
213-641 |
9.90e-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: 55.08 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 213 CGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAGISDLLAEVSAEVDGPVPgylssPQSITDTCLYifTSGTT 292
Cdd:cd05929 65 CGACPAYKSSRAPRAEACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIE-----DEAAGWKMLY--SGGTT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 293 GLPKAARISH----LKILQCQGFYQLCGvHQEDVIYLA-LPLYHMSGSllgiVGCMG---IGATVVLKSKFSAGQFWEDC 364
Cdd:cd05929 138 GRPKGIKRGLpggpPDNDTLMAAALGFG-PGADSVYLSpAPLYHAAPF----RWSMTalfMGGTLVLMEKFDPEEFLRLI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 365 QQHRVTVFQYIGELCRYLVNQPpsKAERGH------KVRLAVGSGLRPDTWERFVRRFGPLqVLETYGLTEGNVATI--- 435
Cdd:cd05929 213 ERYRVTFAQFVPTMFVRLLKLP--EAVRNAydlsslKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLTIing 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 436 -NYTGQRGAVGRAswlykhifpfslirydVTTGEPIRDPQGHCMAtsPGEPGLLVapVSQQSPFLgYAGGPELAQGKLLK 514
Cdd:cd05929 290 eEWLTHPGSVGRA----------------VLGKVHILDEDGNEVP--PGEIGEVY--FANGPGFE-YTNDPEKTAAARNE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 515 DVFRpgdvffNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGvtVPGHE-GRAGMAalV 593
Cdd:cd05929 349 GGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHA--V 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 594 LRP-----PHALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFKQQKVRM 641
Cdd:cd05929 419 VQPapgadAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
286-626 |
2.35e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 53.86 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLKILQCQGFY-------QLCGVHQEDVIYLALPLYHMSGSLlgivgcmGIGATVVLKSkfSAG 358
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNAAAFLQWAaaafsaeELAGVLASTSICFDLSVFELFGPL-------ATGGKVVLAD--NVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 359 QFWEDCQQHRVTVFQYIGELCRYLVNQ---PPSKaergHKVRLAvGSGLRPDTWERFVRRFGPLQVLETYGLTEgnvATI 435
Cdd:cd12115 182 ALPDLPAAAEVTLINTVPSAAAELLRHdalPASV----RVVNLA-GEPLPRDLVQRLYARLQVERVVNLYGPSE---DTT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 436 NYTG---QRGAVGraswlykhifpfsliryDVTTGEPIRDPQGHCMATS-----PGEPGLLV---APVSQqspflGYAGG 504
Cdd:cd12115 254 YSTVapvPPGASG-----------------EVSIGRPLANTQAYVLDRAlqpvpLGVPGELYiggAGVAR-----GYLGR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 505 PELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVnVYGVTVPGHE 584
Cdd:cd12115 312 PGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA-VVVAIGDAAG 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1393643644 585 GRAGMAALVLRPPHALDLMQLYTHVSENLPPYARP-RFLRLQE 626
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPsRFVRLDA 433
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
210-641 |
2.46e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 53.73 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 210 LRSCGA----RALVLAPEFLESLEPDLPALRAMGLHLwaagPGTHPAGISDLLAEVsaEVDGPVPGYLSSPQSITDTCLY 285
Cdd:cd05974 17 LRSIGVgrgdRILLMLGNVVELWEAMLAAMKLGAVVI----PATTLLTPDDLRDRV--DRGGAVYAAVDENTHADDPMLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 286 IFTSGTTGLPKAARISHLK--ILQCQGFYQLcGVHQEDViylalplyHMSGSLLG--------IVGCMGIGATVVL--KS 353
Cdd:cd05974 91 YFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDV--------HWNISSPGwakhawscFFAPWNAGATVFLfnYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 354 KFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERfVRRFGPLQVLETYGLTEGNVA 433
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQ-VRRAWGLTIRDGYGQTETTAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 434 TINYTGQR---GAVGRASWLYKHIfpfslirydvttgepIRDPQGhcmatSPGEPGLLVAPVSQQSP---FLGYAGGPEL 507
Cdd:cd05974 241 VGNSPGQPvkaGSMGRPLPGYRVA---------------LLDPDG-----APATEGEVALDLGDTRPvglMKGYAGDPDK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 508 AQGKLlkdvfrpGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVygVTVPGHEGRA 587
Cdd:cd05974 301 TAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPDPVRLS 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393643644 588 GMAALVL-------RPPHALDLMQlytHVSENLPPYARPRFLRLQEsLATTETFKQQKVRM 641
Cdd:cd05974 372 VPKAFIVlragyepSPETALEIFR---FSRERLAPYKRIRRLEFAE-LPKTISGKIRRVEL 428
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
214-433 |
2.67e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.85 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 214 GARALVLAPEFLESLepdlPALRAMGLHLWAagpgthpagISDLLAEVSAEvdgPVPgylsSPQSitDTCLYIFTSGTTG 293
Cdd:PRK07768 108 GAKAVVVGEPFLAAA----PVLEEKGIRVLT---------VADLLAADPID---PVE----TGED--DLALMQLTSGSTG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 294 LPKAARISHLKILQC-QGFYQLCGVHQE-DVIYLALPLYH-MsgsllGIVGC----MGIGATVVlksKFSAGQF------ 360
Cdd:PRK07768 166 SPKAVQITHGNLYANaEAMFVAAEFDVEtDVMVSWLPLFHdM-----GMVGFltvpMYFGAELV---KVTPMDFlrdpll 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 361 W-EDCQQHRVTV-----FQYiGELCRYLVNQPPSKAERGHKVRLAV--GSGLRPDTWERFVR---RFG--PLQVLETYGL 427
Cdd:PRK07768 238 WaELISKYRGTMtaapnFAY-ALLARRLRRQAKPGAFDLSSLRFALngAEPIDPADVEDLLDagaRFGlrPEAILPAYGM 316
|
....*.
gi 1393643644 428 TEGNVA 433
Cdd:PRK07768 317 AEATLA 322
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
250-631 |
5.79e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 250 HPAGISDLLAEVSAEVDGPV-PGYLSSPQSITdtcLYIFTSGTTGLPKAARISHLKILQCQGFYQLCGVHQEDVIYLALP 328
Cdd:PRK12316 3168 LAQGVQVLDLDRGDENYAEAnPAIRTMPENLA---YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 329 LYHMSGSLLGIVGCMGIGATVVLKSK---FSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPPSKAERGHKVRLAVGSGLR 405
Cdd:PRK12316 3245 TFSFDVFVEELFWPLMSGARVVLAGPedwRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALP 3324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 406 PDTWERFvrrFGPLQVLETYGLTEGNVATINYTGQRGAVGRASwLYKHIFPFSLIRYDVtTGEPIrdPQGHCMATSPGEP 485
Cdd:PRK12316 3325 ADLQQQV---FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVP-IGRPIANRACYILDG-SLEPV--PVGALGELYLGGE 3397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 486 GLLvapvsqqspfLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFE 565
Cdd:PRK12316 3398 GLA----------RGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 566 ALDFLQEVNVYGVtvpghEGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESLATT 631
Cdd:PRK12316 3468 EHPWVREAVVLAV-----DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLT 3528
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
287-620 |
6.52e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 52.71 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 287 FTSGTTGLPKAARISHlkilqcQGFYqLCGVH-----QEDV--IYL-ALPLYHMSGSLLgIVGCMGIGATVVLKSKFSAG 358
Cdd:PLN03102 193 YTSGTTADPKGVVISH------RGAY-LSTLSaiigwEMGTcpVYLwTLPMFHCNGWTF-TWGTAARGGTSVCMRHVTAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 359 QFWEDCQQHRVTVFQYIGELCRYLVNQppSKAERGHK---VRLAVGSGLRPDTWERFVRRFGpLQVLETYGLTEGNvati 435
Cdd:PLN03102 265 EIYKNIEMHNVTHMCCVPTVFNILLKG--NSLDLSPRsgpVHVLTGGSPPPAALVKKVQRLG-FQVMHAYGLTEAT---- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 436 nytgqrGAVGRASW------LYKH----------IFPFSLIRYDVTTGEPI----RDpqGHCMatspgepGLLVapVSQQ 495
Cdd:PLN03102 338 ------GPVLFCEWqdewnrLPENqqmelkarqgVSILGLADVDVKNKETQesvpRD--GKTM-------GEIV--IKGS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 496 SPFLGYAGGPelaqgKLLKDVFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNV 575
Cdd:PLN03102 401 SIMKGYLKNP-----KATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 576 YGVTVPGHeGRAGMAALVLR-----PPHALDLMQ-----LYTHVSENLPPYARPR 620
Cdd:PLN03102 474 VAMPHPTW-GETPCAFVVLEkgettKEDRVDKLVtrerdLIEYCRENLPHFMCPR 527
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
74-560 |
6.99e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.30 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 74 LAQQRAAH-TFLIHGSRRFSYSEAERESNRAARAfLRALGwdwgpdggdsgegsagegeraapgagdaaagsgaefaggd 152
Cdd:PRK10946 31 LTRHAASDaIAVICGERQFSYRELNQASDNLACS-LRRQG---------------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 153 gaargggaaapLSPGATVALLLPAGPEFLWLWFGLAKAGLrtafVP-TAL---RRGPLLHCLRSCGARALVLAPE----- 223
Cdd:PRK10946 70 -----------IKPGDTALVQLGNVAEFYITFFALLKLGV----APvNALfshQRSELNAYASQIEPALLIADRQhalfs 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 224 ---FLESLEPDLPALRAMGLHlwaAGPGTHpaGISDLLAEvsaevdgPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARI 300
Cdd:PRK10946 135 dddFLNTLVAEHSSLRVVLLL---NDDGEH--SLDDAINH-------PAEDFTATPSPADEVAFFQLSGGSTGTPKLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 301 SHlkilqcQGFY-------QLCGVHQEDVIYLALPLYH---MS--GSLlgivGCMGIGATVVLKSKFSAGQFWEDCQQHR 368
Cdd:PRK10946 203 TH------NDYYysvrrsvEICGFTPQTRYLCALPAAHnypMSspGAL----GVFLAGGTVVLAPDPSATLCFPLIEKHQ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 369 VTVFQyigelcryLVnqPPS-------KAERGHKVRLA------VGsGLRPDtwERFVRRFGPL---QVLETYGLTEGNV 432
Cdd:PRK10946 273 VNVTA--------LV--PPAvslwlqaIAEGGSRAQLAslkllqVG-GARLS--ETLARRIPAElgcQLQQVFGMAEGLV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 433 atiNYTgqrgavgRASWLYKHIFpfslirydVTTGEPIR--------DPQGHCMAtsPGEPGLLVApvsqQSP--FLGYA 502
Cdd:PRK10946 340 ---NYT-------RLDDSDERIF--------TTQGRPMSpddevwvaDADGNPLP--QGEVGRLMT----RGPytFRGYY 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393643644 503 GGPEL-AQgkllkdVFrPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEV 560
Cdd:PRK10946 396 KSPQHnAS------AF-DANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
281-628 |
7.75e-07 |
|
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: 51.53 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKILqCQGFyQLCGVHQ--EDVIYL-ALPLYHMsGSLLGIVGCMGIGATVVLKSKFSA 357
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALL-AQAL-VLAVLQAidEGTVFLnSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 358 GQFWEDCQQHRVT----VFQYIGELCRylVNqppskAERGHKVrlavgSGLRP----DTWE--------RFVRRFGplqv 421
Cdd:cd17636 78 EEVLELIEAERCThaflLPPTIDQIVE--LN-----ADGLYDL-----SSLRSspaaPEWNdmatvdtsPWGRKPG---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 422 leTYGLTE-GNVATINYTG--QRGAVGRASwlykhifPFSLIRydvttgepIRDPQGHCMAtsPGEPGLLVApvsqQSP- 497
Cdd:cd17636 142 --GYGQTEvMGLATFAALGggAIGGAGRPS-------PLVQVR--------ILDEDGREVP--DGEVGEIVA----RGPt 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 498 -FLGYAGGPELAQGKllkdvFRPGdvFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVY 576
Cdd:cd17636 199 vMAGYWNRPEVNARR-----TRGG--WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1393643644 577 GVTVPGHeGRAGMAALVLRPPHALDLMQLYTHVSENLPPYARPRFLRLQESL 628
Cdd:cd17636 272 GVPDPRW-AQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADAL 322
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
280-373 |
1.40e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 51.32 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 280 TDTCL-Y-IFTSGTTGLPKAARISHLKILQ-CQGFYQLCGVHQEDVIYLALPLyHMSGSLLGIVGCMGIGATV------- 349
Cdd:cd17654 116 TDECLaYvIHTSGTTGTPKIVAVPHKCILPnIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATLlivptsv 194
|
90 100
....*....|....*....|....*
gi 1393643644 350 -VLKSKFSAGQFwedcQQHRVTVFQ 373
Cdd:cd17654 195 kVLPSKLADILF----KRHRITVLQ 215
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
281-538 |
3.92e-06 |
|
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: 49.75 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQ 359
Cdd:cd05914 90 DVALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 360 FwEDCQQHRVTVFqyIGeLCRYLV-------NQPPSKAERGHKVRLAV-----------------------------GSG 403
Cdd:cd05914 170 I-IALAFAQVTPT--LG-VPVPLViekifkmDIIPKLTLKKFKFKLAKkinnrkirklafkkvheafggnikefvigGAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 404 LRPDTwERFVRRFGpLQVLETYGLTEgNVATINYTgqrgavgraswlykhifPFSLIRYDvTTGEPIRDPQGHCMATSP- 482
Cdd:cd05914 246 INPDV-EEFLRTIG-FPYTIGYGMTE-TAPIISYS-----------------PPNRIRLG-SAGKVIDGVEVRIDSPDPa 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 483 GEPGLLVapVSQQSPFLGYAGGPELAQGKLLKDvfrpGdvFFNTGDLLVCDDQGFL 538
Cdd:cd05914 305 TGEGEII--VRGPNVMKGYYKNPEATAEAFDKD----G--WFHTGDLGKIDAEGYL 352
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
163-336 |
4.70e-06 |
|
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: 49.59 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 163 PLSPGATVALLLPAGPEFL-WLWfglakAGLRTAFVPTALRRGP-----------LLHCLRSCGaRALVLAPEfleSLEP 230
Cdd:cd05906 60 GLRPGDSVILQFDDNEDFIpAFW-----ACVLAGFVPAPLTVPPtydepnarlrkLRHIWQLLG-SPVVLTDA---ELVA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 231 DLPALRAMGLHLwaagpgthpaGISDLLAEVSAEVDGPVPGYLSSPQsitDTCLYIFTSGTTGLPKAARISHLKIL-QCQ 309
Cdd:cd05906 131 EFAGLETLSGLP----------GIRVLSIEELLDTAADHDLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILaRSA 197
|
170 180
....*....|....*....|....*..
gi 1393643644 310 GFYQLCGVHQEDVIYLALPLYHMSGSL 336
Cdd:cd05906 198 GKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
257-654 |
7.51e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 49.01 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 257 LLAEVSAEVDGPVpgylsspQSITDTCLYIFTSGTTGLPKAARISH----LKILQCQGFYQLCGVHQEDVIyLALPLYHM 332
Cdd:PRK05620 165 LLDGRSTVYDWPE-------LDETTAAAICYSTGTTGAPKGVVYSHrslyLQSLSLRTTDSLAVTHGESFL-CCVPIYHV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 333 SGSLLGIVGCMGiGATVVLK----SKFSAGQFWEDC---QQHRVTVFqYIGELCRYLVNQPpskaERGHKVRLAVGSGLR 405
Cdd:PRK05620 237 LSWGVPLAAFMS-GTPLVFPgpdlSAPTLAKIIATAmprVAHGVPTL-WIQLMVHYLKNPP----ERMSLQEIYVGGSAV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 406 P----DTWErfvRRFGpLQVLETYGLTE-GNVATINYTgQRGAVGRASWLYKHI---FPFSLiRYDVTTgepirdpQGHC 477
Cdd:PRK05620 311 PpiliKAWE---ERYG-VDVVHVWGMTEtSPVGTVARP-PSGVSGEARWAYRVSqgrFPASL-EYRIVN-------DGQV 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 478 MATS---PGE---PGLLVAPVSQQSPFLGYAGGPELAQGKLLKDVFRP--GDVFFNTGDLLVCDDQGFLRFHDRTGDTFR 549
Cdd:PRK05620 378 MESTdrnEGEiqvRGNWVTASYYHSPTEEGGGAASTFRGEDVEDANDRftADGWLRTGDVGSVTRDGFLTIHDRARDVIR 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 550 WKGENVATTEVAEVFEALDFLQEVNVYGVTVPgHEGRAGMAALVLRP---PHALDLMQLYTHVSENLPPYARPRFLRLQE 626
Cdd:PRK05620 458 SGGEWIYSAQLENYIMAAPEVVECAVIGYPDD-KWGERPLAVTVLAPgiePTRETAERLRDQLRDRLPNWMLPEYWTFVD 536
|
410 420 430
....*....|....*....|....*....|..
gi 1393643644 627 SLATT--ETFKQQKVR--MANEGFDPSTLSDP 654
Cdd:PRK05620 537 EIDKTsvGKFDKKDLRqhLADGDFEIIKLKGP 568
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
163-637 |
7.82e-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: 48.99 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 163 PLSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGARALVLAPEFLE---SLEPDLPALRAMG 239
Cdd:cd17632 89 PVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDlavEAVLEGGTPPRLV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 240 LHLWAAGPGTHPAGIS-------------DLLAEVSAEVDGPVPGYLSSPQSITDT-CLYIFTSGTTGLPKAARISHLKI 305
Cdd:cd17632 169 VFDHRPEVDAHRAALEsarerlaavgipvTTLTLIAVRGRDLPPAPLFRPEPDDDPlALLIYTSGSTGTPKGAMYTERLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 306 LQC-QGFYQLCGVHQEDVIYLA-LPLYHMSGSLLgIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVT-----------VF 372
Cdd:cd17632 249 ATFwLKVSSIQDIRPPASITLNfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLFDDLALVRPTelflvprvcdmLF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 373 Q-YIGELCRYLVN-------QPPSKAE-----RGHKVRLAV-GSGLRPDTWERFVRRFGPLQVLETYGLTEGNVATINyt 438
Cdd:cd17632 328 QrYQAELDRRSVAgadaetlAERVKAElrervLGGRLLAAVcGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILD-- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 439 gqrGAVGRASWL-YKHIfpfsliryDVttgepirdPQ-GHCMATSPGEPGLLVapVSQQSPFLGYAGGPELAqgkllKDV 516
Cdd:cd17632 406 ---GVIVRPPVLdYKLV--------DV--------PElGYFRTDRPHPRGELL--VKTDTLFPGYYKRPEVT-----AEV 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 517 FRPgDVFFNTGDLL--VCDDQgfLRFHDRTGDTFRW-KGENVATTEVAEVFEALDFLQEVNVYG---------VTVPGHE 584
Cdd:cd17632 460 FDE-DGFYRTGDVMaeLGPDR--LVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGnserayllaVVVPTQD 536
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 585 GRAGMAALVLRPPHALDLMQLYThvSENLPPYARPRflrlqESLATTETFKQQ 637
Cdd:cd17632 537 ALAGEDTARLRAALAESLQRIAR--EAGLQSYEIPR-----DFLIETEPFTIA 582
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
281-577 |
1.33e-05 |
|
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: 48.37 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 281 DTCLYIFTSGTTGLPKAARISHLKIL-QCQGFY----QLCGVHQEDVIYLALPLYHMSGSLLgIVGCMGIGATVvlkskf 355
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHGNIVsNVAGVFkileILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKI------ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 356 saGqFW--------EDCQQHRVTVF------------------QYIGELCRYLVNQPPSKAERG---------------- 393
Cdd:cd05927 188 --G-FYsgdirlllDDIKALKPTVFpgvprvlnriydkifnkvQAKGPLKRKLFNFALNYKLAElrsgvvraspfwdklv 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 394 -HKVRLAVGSGLR----------PDTwERFVRR-FGpLQVLETYGLTEGN-VATINYTGQR--GAVGRaswlykhIFPFS 458
Cdd:cd05927 265 fNKIKQALGGNVRlmltgsaplsPEV-LEFLRVaLG-CPVLEGYGQTECTaGATLTLPGDTsvGHVGG-------PLPCA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 459 LIR--------YDVTTGEP-----IRdpqGHCMatspgepgllvapvsqqspFLGYAGGPELAQGKLLKDvfrpGdvFFN 525
Cdd:cd05927 336 EVKlvdvpemnYDAKDPNPrgevcIR---GPNV-------------------FSGYYKDPEKTAEALDED----G--WLH 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 526 TGDLLVCDDQGFLRFHDRTGDTFRW-KGENVATTEVAEVFEALDFLQEVNVYG 577
Cdd:cd05927 388 TGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
275-349 |
2.21e-05 |
|
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: 47.74 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 275 SPQSITDTCLYIFTSGTTGLPKAARISHLKIL-----QCQGFYQLCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATV 349
Cdd:cd05933 145 SSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITwtakaASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
495-620 |
3.56e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 46.91 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 495 QSPFLGYAggPElaqgkllkdvFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVN 574
Cdd:PRK07445 309 QSLALGYY--PQ----------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVC 376
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1393643644 575 VYGVTVPgHEGRAGMAALVLRPPhALDLMQLYTHVSENLPPYARPR 620
Cdd:PRK07445 377 VLGLPDP-HWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPK 420
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-582 |
7.56e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 45.91 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTAFVPTALRRGPLLHCLrscgaralvlapeflESLEPDlpalramglhlw 243
Cdd:cd05910 24 IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCL---------------QEAEPD------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 244 aagpgthpAGISDLLAEvsaevdgpvpgylsspqsitDTCLYIFTSGTTGLPKAARISHLKIL-QCQGFYQLCGVHQEDV 322
Cdd:cd05910 77 --------AFIGIPKAD--------------------EPAAILFTSGSTGTPKGVVYRHGTFAaQIDALRQLYGIRPGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 323 IYLALPLYHMSGSLLGIvgcmgigATVVLKSKFSA------GQFWEDCQQHRVT-------VFQYIGELCRYLVNQPPSk 389
Cdd:cd05910 129 DLATFPLFALFGPALGL-------TSVIPDMDPTRparadpQKLVGAIRQYGVSivfgspaLLERVARYCAQHGITLPS- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 390 aerghkVR--LAVGSGLRPDTWERFVRRFGP-LQVLETYGLTE-------GNVATINYTGQRGAVGRASWLyKHIFPFSL 459
Cdd:cd05910 201 ------LRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvssiGSRELLATTTAATSGGAGTCV-GRPIPGVR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 460 IRYDVTTGEPIRDPQGHcMATSPGEPGLLVapVSQQSPFLGYAGGPElaQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLR 539
Cdd:cd05910 274 VRIIEIDDEPIAEWDDT-LELPRGEIGEIT--VTGPTVTPTYVNRPV--ATALAKIDDNSEGFWHRMGDLGYLDDEGRLW 348
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1393643644 540 FHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPG 582
Cdd:cd05910 349 FCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
164-433 |
1.21e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 45.38 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 164 LSPGATVALLLPAGPEFLWLWFGLAKAGLRTA--FVPTAL--RRG---PLLHCLRSCGARALVLAPEFLESLEPDLPALR 236
Cdd:PRK09192 71 LKPGDRVALIAETDGDFVEAFFACQYAGLVPVplPLPMGFggRESyiaQLRGMLASAQPAAIITPDELLPWVNEATHGNP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 237 AmglhLWAAGPgthpagiSDLLAEVSAEVDGPVPgylsSPqsiTDTCLYIFTSGTTGLPKAARISH------LKILQCQG 310
Cdd:PRK09192 151 L----LHVLSH-------AWFKALPEADVALPRP----TP---DDIAYLQYSSGSTRFPRGVIITHralmanLRAISHDG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 311 FyqlcGVHQEDVIYLALPLYH-MsgsllGIVGC-MGIGATVVLKSKFSAGQF------WED-CQQHRVTV-----FQYig 376
Cdd:PRK09192 213 L----KVRPGDRCVSWLPFYHdM-----GLVGFlLTPVATQLSVDYLPTRDFarrplqWLDlISRNRGTIsysppFGY-- 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393643644 377 ELCRYLVNQPPSKAERGHKVRLAvGSG---LRPDTWERFVRRFGPL-----QVLETYGLTEGNVA 433
Cdd:PRK09192 282 ELCARRVNSKDLAELDLSCWRVA-GIGadmIRPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLA 345
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
166-619 |
2.08e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.65 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPagpeflwlwfglakaglRTAFVPTALrrgpllHCLRSCGARALVLAPEF--------LESLEPDLPALRA 237
Cdd:PRK10252 507 PGDSVAVALP-----------------RSVFLTLAL------HAIVEAGAAWLPLDTGYpddrlkmmLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 238 MGLHLWAAGPGTHPAGISDLLAevsaeVDGPVPGYLSSPQsitDTCLYIFTSGTTGLPKAARISHLKI----LQCQGFYq 313
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLA-----PQGAAPLQLSQPH---HTAYIIFTSGSTGRPKGVMVGQTAIvnrlLWMQNHY- 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 314 lcGVHQEDVIYLALPLyHMSGSLLGIVGCMGIGATVVL------KSKFSAGQFWEDcqqHRVTVFQYIGELCRYLVNQPP 387
Cdd:PRK10252 635 --PLTADDVVLQKTPC-SFDVSVWEFFWPFIAGAKLVMaepeahRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVASLT 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 388 SKAERGHKVRLA----VGSGLRPDTWERFVRRFG-PLQVLetYGLTEGNV----------ATINYTGQRGAVGRASWlyk 452
Cdd:PRK10252 709 PEGARQSCASLRqvfcSGEALPADLCREWQQLTGaPLHNL--YGPTEAAVdvswypafgeELAAVRGSSVPIGYPVW--- 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 453 hifpfslirydvTTGEPIRDPQGHcmATSPGEPGLLVAPVSQQSPflGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVC 532
Cdd:PRK10252 784 ------------NTGLRILDARMR--PVPPGVAGDLYLTGIQLAQ--GYLGRPDLTASRFIADPFAPGERMYRTGDVARW 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 533 DDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAG-----MAALVLRPPHALDLMQLYT 607
Cdd:PRK10252 848 LDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGdarqlVGYLVSQSGLPLDTSALQA 927
|
490
....*....|..
gi 1393643644 608 HVSENLPPYARP 619
Cdd:PRK10252 928 QLRERLPPHMVP 939
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
500-635 |
6.02e-04 |
|
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: 42.85 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 500 GYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGENVATTEVAEVFEALDFLQE--VNVYG 577
Cdd:cd17656 340 GYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEavVLDKA 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393643644 578 VTVPGHEGRAGMAALVlrpphALDLMQLYTHVSENLPPYARPRFLRLQESLATTETFK 635
Cdd:cd17656 420 DDKGEKYLCAYFVMEQ-----ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
205-429 |
7.64e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 205 PLLHCLRSCGARALVLAPEFLESLEPDLPAlramglhlwaaGPGTHPAGISDLLAEVSAEVDGPVPgylSSPQSITDTCl 284
Cdd:PLN02736 163 TLLSCLSEIPSVRLIVVVGGADEPLPSLPS-----------GTGVEIVTYSKLLAQGRSSPQPFRP---PKPEDVATIC- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 285 yiFTSGTTGLPKAARISHLK-ILQCQGFYQLCGVHQEDVIYLALPLYHMSgSLLGIVGCMGIGATV------VLKskfsa 357
Cdd:PLN02736 228 --YTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDVHISYLPLAHIY-ERVNQIVMLHYGVAVgfyqgdNLK----- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 358 gqFWEDCQQHRVTVF------------------QYIGELCRYLVN-------------QPPS-----------KAERGHK 395
Cdd:PLN02736 300 --LMDDLAALRPTIFcsvprlynriydgitnavKESGGLKERLFNaaynakkqalengKNPSpmwdrlvfnkiKAKLGGR 377
|
250 260 270
....*....|....*....|....*....|....*...
gi 1393643644 396 VRLaVGSG---LRPDTWErFVRR-FGPlQVLETYGLTE 429
Cdd:PLN02736 378 VRF-MSSGaspLSPDVME-FLRIcFGG-RVLEGYGMTE 412
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
249-631 |
8.12e-04 |
|
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: 42.53 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 249 THPAG-ISDLLAEVSAEVdgpvpgYLSSpqSITDTCLYIFTSGTTGLPKAARISHLKILQC-QGFYQLCGVHQEDVIyLA 326
Cdd:cd05918 82 SHPLQrLQEILQDTGAKV------VLTS--SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSaLAHGRALGLTSESRV-LQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 327 LPLYHMSGSLLGIVGCMGIGATVVLKSKfsagqfwEDCQQHRVTVFQyigelcRYLVNQ---PPSkaerghkvrlaVGSG 403
Cdd:cd05918 153 FASYTFDVSILEIFTTLAAGGCLCIPSE-------EDRLNDLAGFIN------RLRVTWaflTPS-----------VARL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 404 LRP---------------------DTWERFVRrfgplqVLETYGLTEgnvATINYTGQRgaVGRASwlykhifPFSLIRY 462
Cdd:cd05918 209 LDPedvpslrtlvlggealtqsdvDTWADRVR------LINAYGPAE---CTIAATVSP--VVPST-------DPRNIGR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 463 DVTTGEPIRDPQGHCMATSPGEPG-LLVapvsqQSPFL--GYAGGPELAQGK-------LLKDVFRPGDVFFNTGDLLVC 532
Cdd:cd05918 271 PLGATCWVVDPDNHDRLVPIGAVGeLLI-----EGPILarGYLNDPEKTAAAfiedpawLKQEGSGRGRRLYRTGDLVRY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 533 DDQGFLRFHDRTGDTFRWKGENVattEVAEVfEA-----LDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDlMQLYT 607
Cdd:cd05918 346 NPDGSLEYVGRKDTQVKIRGQRV---ELGEI-EHhlrqsLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSG-SGDGD 420
|
410 420
....*....|....*....|....
gi 1393643644 608 HVSENLPPYARPRFLRLQESLATT 631
Cdd:cd05918 421 SLFLEPSDEFRALVAELRSKLRQR 444
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
284-387 |
1.09e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.04 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 284 LYI-FTSGTTGLPKAARISHLKILQCQG-FYQLCGVHQEDVIYLAlplYHMSGSL---LGIVGCMGIGATVVL------K 352
Cdd:PTZ00237 257 LYIlYTSGTTGNSKAVVRSNGPHLVGLKyYWRSIIEKDIPTVVFS---HSSIGWVsfhGFLYGSLSLGNTFVMfeggiiK 333
|
90 100 110
....*....|....*....|....*....|....*
gi 1393643644 353 SKFSAGQFWEDCQQHRVTVFQYIGELCRYLVNQPP 387
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP 368
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
258-302 |
2.69e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 40.65 E-value: 2.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1393643644 258 LAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISH 302
Cdd:PRK04813 121 LDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISH 165
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
166-340 |
3.79e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 40.72 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 166 PGATVALLLPAGPEFLWLWFGLAKAGlrtaFVPTALR--RGP--LLHCLRSCGARALVLAPEFLES--LEPDLPALRAMG 239
Cdd:PRK06814 681 PGENVGVMLPNANGAAVTFFALQSAG----RVPAMINfsAGIanILSACKAAQVKTVLTSRAFIEKarLGPLIEALEFGI 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 240 LHLWaagpgthpagISDLLAEVS------AEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILqcQGFYQ 313
Cdd:PRK06814 757 RIIY----------LEDVRAQIGladkikGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLL--ANRAQ 824
|
170 180 190
....*....|....*....|....*....|....
gi 1393643644 314 LCGV---HQEDVIYLALPLYH----MSGSLLGIV 340
Cdd:PRK06814 825 VAARidfSPEDKVFNALPVFHsfglTGGLVLPLL 858
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
170-309 |
4.22e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 170 VALLLPAGPEFLWLWFGLAKAGlrTAFVP-------------TALRRGPLLHCLRSCGARALVLAPEFLESLEPDLpalr 236
Cdd:PRK05691 3773 VALLAERGLDLLGMIVGSFKAG--AGYLPldpglpaqrlqriIELSRTPVLVCSAACREQARALLDELGCANRPRL---- 3846
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393643644 237 amglHLWaagpgthpagiSDLLAEVSAEVDgpvPGYLSSPQSITdtcLYIFTSGTTGLPKAARISHLKILQCQ 309
Cdd:PRK05691 3847 ----LVW-----------EEVQAGEVASHN---PGIYSGPDNLA---YVIYTSGSTGLPKGVMVEQRGMLNNQ 3898
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
232-372 |
4.85e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 40.16 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393643644 232 LPALRAMGL--HLWAAGPGTHPAGISDLlAEVSAEVDGPVPGYLSSPqsiTDTCLYI-FTSGTTGLPKA-------ARIS 301
Cdd:PRK03584 216 LPSLEHVVVvpYLGPAAAAAALPGALLW-EDFLAPAEAAELEFEPVP---FDHPLWIlYSSGTTGLPKCivhghggILLE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393643644 302 HLKILQCQgfyqlCGVHQEDVI-YLALPLYHMSGSLlgiVGCMGIGATVVL--KSKF--SAGQFWEDCQQHRVTVF 372
Cdd:PRK03584 292 HLKELGLH-----CDLGPGDRFfWYTTCGWMMWNWL---VSGLLVGATLVLydGSPFypDPNVLWDLAAEEGVTVF 359
|
|
| |
