|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
104-611 |
0e+00 |
|
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: 860.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 183
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtQLLDPMLAEAPTTPLAQaPGKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05939 82 ----------------------------------NLLDPLLTQSSTEPPSQ-DDVNFRDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 343
Cdd:cd05939 127 SRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 344 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 423
Cdd:cd05939 207 LLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 424 VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 503
Cdd:cd05939 287 VDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 504 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPI 583
Cdd:cd05939 367 FKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQ 446
|
490 500
....*....|....*....|....*...
gi 1268743554 584 FLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05939 447 FIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
42-646 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 691.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGDTIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 121
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSI--SYAELNARANRYAHWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 122 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 201
Cdd:PRK08279 81 ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 202 kFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHhSYSMR 280
Cdd:PRK08279 161 -LWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGG-LLRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 281 AADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL 360
Cdd:PRK08279 239 PDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 361 AVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHvyPIRLVKVNEDTMEPLRDSEGLCI 440
Cdd:PRK08279 319 MIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRCI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 441 PCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVS 520
Cdd:PRK08279 397 KVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 521 TTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 599
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKY 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1268743554 600 QKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDERVHARICAGDFSL 646
Cdd:PRK08279 554 RKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
104-611 |
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: 650.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 183
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05940 82 ----------------------------------------------------------DAALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 343
Cdd:cd05940 104 RRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 344 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 423
Cdd:cd05940 184 LLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 424 VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 503
Cdd:cd05940 264 YDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 504 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQ-LDPNSMYQELQKVLASYARP 582
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEeFDLSALAAHLEKNLPGYARP 420
|
490 500
....*....|....*....|....*....
gi 1268743554 583 IFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05940 421 LFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
105-633 |
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: 597.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 183
Cdd:cd05938 7 TYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EMAAAVAEVSEQLGKSLLKFcsGDLGPESILPDTQLLDPMLAEAPTTPLAQ---APGKGMDDRLfYIYTSGTTGLPKAAI 260
Cdd:cd05938 87 ELQEAVEEVLPALRADGVSV--WYLSHTSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTGLPKAAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 261 VVHSRYYRIAAFgHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEI 340
Cdd:cd05938 164 ISHLRVLQCSGF-LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 341 CRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIR 420
Cdd:cd05938 243 LRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 421 LVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDPlrrFDGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDEL 499
Cdd:cd05938 323 LIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAGDKEqTEKKLLRDVFKKGDVYFNTGDLLVQDQQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 500 GYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI--ADPHsQLDPNSMYQELQKVLA 577
Cdd:cd05938 400 NFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPGH-EFDGKKLYQHVREYLP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 578 SYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDE 633
Cdd:cd05938 479 AYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTP 534
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
104-611 |
9.95e-140 |
|
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: 415.68 E-value: 9.95e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFR-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYg 182
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 gemaaavaevseqlgksllkfcsgdlgpesilpdtqllDPmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVV 262
Cdd:cd05937 85 --------------------------------------DP------------------DDPAILIYTSGTTGLPKAAAIS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 263 HSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 342
Cdd:cd05937 109 WRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 343 YLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANM---DGKVGSCGFNSRILTHVY-- 417
Cdd:cd05937 189 YLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAGAIGHHGLIRRWKFen 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 418 PIRLVKVNEDTMEPLRD-SEGLCIPCQPGEPGLLVGQINqQDPLRRFDGYVSDS-ATNKKIAHSVFRKGDSAYLSGDVLV 495
Cdd:cd05937 269 QVVLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVP-FKNREAFQGYLHNEdATESKLVRDVFRKGDIYFRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 496 MDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-----ADPHSQLDPNSMYQ 570
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAItleesSAVPTEFTKSLLAS 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1268743554 571 ELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05937 428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
81-607 |
2.46e-87 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 279.77 E-value: 2.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:COG0318 4 LLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIYggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgm 240
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 ddrLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAS 320
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 321 RFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIA- 397
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 398 ----NMDGKVGSCGfnsRILTHVyPIRLVkvnedtmeplrDSEGlcIPCQPGEPGLLVGQINQQdplrrFDGYVSD-SAT 472
Cdd:COG0318 259 npedPGERRPGSVG---RPLPGV-EVRIV-----------DEDG--RELPPGEVGEIVVRGPNV-----MKGYWNDpEAT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 473 NKKIAHSVFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAG 552
Cdd:COG0318 317 AEAFRDGWLR-------TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE-KWGERV 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 553 MAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:COG0318 389 VAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-605 |
1.16e-81 |
|
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: 264.15 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 103 CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtsaakaliyg 182
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGD----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 gEMAAAVAEVseqlgksllkfcsgdlGPESILPDTQLLdpmlaeapttplaqapgkgmddrlfyIYTSGTTGLPKAAIVV 262
Cdd:cd05934 66 -ELAYIIDHS----------------GAQLVVVDPASI--------------------------LYTSGTTGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 263 HSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 342
Cdd:cd05934 103 HANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 343 YLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN---MDGKVGSCGfnsrilthvYPI 419
Cdd:cd05934 183 YLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGSIG---------RPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 420 RLVKVNedtmepLRDSEGLciPCQPGEPGLLVgqINQQDPLRRFDGYVSD-SATNKKIAHSVFRKGDSAYlsgdvlvMDE 498
Cdd:cd05934 253 PGYEVR------IVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNMpEATAEAMRNGWFHTGDLGY-------RDA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 499 LGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLAS 578
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*..
gi 1268743554 579 YARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-617 |
2.86e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 258.92 E-value: 2.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 74 AGDTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 153
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 154 VAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVseqlgksllkfcsgDLGPESiLPDTQLLD------------ 221
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--------------DPGDLP-LPAVWLLDapasvsvpagws 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 222 --PMLA-EAPTTPLAQAPGkgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNI 298
Cdd:PRK06155 162 taPLPPlDAPAPAAAVQPG----DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 299 MGVgQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRF 378
Cdd:PRK06155 238 AFF-QALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 379 GVPQIgEFYGATECNCSIANM--DGKVGSC-----GFNSRILthvypirlvkvnedtmeplrDSEGLCIPcqPGEPGLLV 451
Cdd:PRK06155 317 GVDLL-DGYGSTETNFVIAVThgSQRPGSMgrlapGFEARVV--------------------DEHDQELP--DGEPGELL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 452 GQINQqdPLRRFDGYVSDSATnkkiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 531
Cdd:PRK06155 374 LRADE--PFAFATGYFGMPEK------TVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 532 LGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:PRK06155 446 PAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
....*.
gi 1268743554 612 rQTSDR 617
Cdd:PRK06155 526 -DTWDR 530
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-515 |
3.01e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 217.95 E-value: 3.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 82 FQAVARRQPERLALVDASsGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 161
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 162 LRREPLAFCLGTSAAKALIYGGE-MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQApgkgm 240
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKK 316
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 317 FSA---SRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVEQRHRVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATE 391
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGApkRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIANMD------GKVGSCGfnsRILTHVypiRLVKVNEDTMEPLRdseglcipcqPGEPG-LLVGQINQqdplrrFD 464
Cdd:pfam00501 314 TTGVVTTPLpldedlRSLGSVG---RPLPGT---EVKIVDDETGEPVP----------PGEPGeLCVRGPGV------MK 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 465 GYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 515
Cdd:pfam00501 372 GYLNDpELTAEAF------DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
242-600 |
7.03e-60 |
|
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: 203.67 E-value: 7.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSASR 321
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 322 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATECNCSIA-- 397
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 398 ---NMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQPGEPGLLVGQINQqdplrRFDGYVSDSATNK 474
Cdd:cd04433 159 ppdDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 475 kiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA 554
Cdd:cd04433 217 ------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1268743554 555 AI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQ 600
Cdd:cd04433 290 VVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
86-642 |
1.49e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 208.73 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQLGFAPGDV-VAVFLEGRPEFVgLWLGLAK-AGVVAALLNvNLR 163
Cdd:PRK13388 11 DRAGDDTIAV--RYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAAlGGYVLVGLN-TTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 164 ReplafclgtsaakaliyGGEMAAAVAEVSEQL------GKSLLKfcsgDLGpesiLPDTQLLD---PMLAE--APTTPL 232
Cdd:PRK13388 87 R-----------------GAALAADIRRADCQLlvtdaeHRPLLD----GLD----LPGVRVLDvdtPAYAElvAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 233 AQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV 312
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 313 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATEC 392
Cdd:PRK13388 222 LPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGYGSSEG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 393 NCSIANMDGK-VGSCGfnsrilthvypiR----LVKVNEDTMEPlrdseglCIPCQPGEPGLL------VGQINQQDPLR 461
Cdd:PRK13388 301 AVIVVREPGTpPGSIG------------RgapgVAIYNPETLTE-------CAVARFDAHGALlnadeaIGELVNTAGAG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 462 RFDGYVSD-SATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 540
Cdd:PRK13388 362 FFEGYYNNpEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVY 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 541 GVAVPGVeGKAGMAAI--ADPHSqLDPNSMYQEL--QKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFdpRQTSD 616
Cdd:PRK13388 435 AVPDERV-GDQVMAALvlRDGAT-FDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW--ATGDP 510
|
570 580
....*....|....*....|....*.
gi 1268743554 617 RLFFLDLKQGRYVPLDERVHARICAG 642
Cdd:PRK13388 511 VTLWVRRGGPAYRLMSEPAKAALAAE 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
131-610 |
1.49e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 194.51 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 131 VAVFLEGRPEFvGLWLGLAK-AGVVAALLNVNLRREPLA---------FCLGTSAAKALIYGGEMAAAVAEVSEQlgksl 200
Cdd:PRK07867 57 VGVLLDNTPEF-SLLLGAAAlSGIVPVGLNPTRRGAALArdiahadcqLVLTESAHAELLDGLDPGVRVINVDSP----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 201 lkfcsgdlgpesilPDTQLLDPmLAEAPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGH---HSY 277
Cdd:PRK07867 131 --------------AWADELAA-HRDAEPPFRVADP----DDLFMLIFTSGTSGDPKAVRCTHRK---VASAGVmlaQRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 278 SMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHR 357
Cdd:PRK07867 189 GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 358 VRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANM-DGKVGSCGfnsrilthVYPIRLVKVNEDTMEPlrdse 436
Cdd:PRK07867 269 LRIVYGNEGAPGDIARFARRFGC-VVVDGFGSTEGGVAITRTpDTPPGALG--------PLPPGVAIVDPDTGTE----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 437 glCIPCQPGEPGLL-----VGQ-INQQDPlRRFDGYVSDS-ATNKKIAHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSG 509
Cdd:PRK07867 335 --CPPAEDADGRLLnadeaIGElVNTAGP-GGFEGYYNDPeADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 510 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMAAIA-DPHSQLDPNSMYQEL--QKVLASYARPIFLR 586
Cdd:PRK07867 405 DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV-GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVR 483
|
490 500
....*....|....*....|....
gi 1268743554 587 LLPQVDTTGTFKIQKTRLQREGFD 610
Cdd:PRK07867 484 VCAELPRTATFKVLKRQLSAEGVD 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
75-605 |
1.25e-50 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 183.73 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 75 GDTIPCIFQAVARRQPERLALV-DASSGIC--WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 151
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfESSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 152 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESIlPDTQLLDPMLAEAPTTp 231
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPAD-DGVSSFTQLKAQQPAT- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 232 LAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHHSY---SMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 308
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 309 LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVR-----LAVGNGLRpaiwEEFTQRFGVpQI 383
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEERFGV-RL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 GEFYGATEcncSIANMDG----------KVGSCGFNsrilthvYPIRLVKVNEDTMEPLRDSEgLCIpcqPGEPGLLVgq 453
Cdd:PRK08008 316 LTSYGMTE---TIVGIIGdrpgdkrrwpSIGRPGFC-------YEAEIRDDHNRPLPAGEIGE-ICI---KGVPGKTI-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 454 inqqdplrrFDGYVSD-SATNKKI-AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 531
Cdd:PRK08008 380 ---------FKEYYLDpKATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 532 LGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK08008 444 PKIQDIVVVGIKDS-IRDEAIKAfVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-601 |
2.48e-50 |
|
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: 180.88 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:cd17631 5 ARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLF 245
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDD 325
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 326 CVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFtQRFGVpQIGEFYGATECNCSIANMD--- 400
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGV-KFVQGYGMTETSPGVTFLSped 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 401 --GKVGSCGfnsRILTHVyPIRLVKVNEDtmeplrdseglciPCQPGEpgllVGQINQQDPLrRFDGYVSDSATNKKiah 478
Cdd:cd17631 261 hrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAGYWNRPEATAA--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 479 sVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA 557
Cdd:cd17631 316 -AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAVVV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1268743554 558 -DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17631 391 pRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
94-600 |
7.19e-49 |
|
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: 178.18 E-value: 7.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 94 ALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 173
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 174 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLgPESILPDTQLLDPmLAEAPTTPLAQAPGKGMDDRLFYIYTSGTT 253
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDK-PDGVLSIEDLLSP-TLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 254 GLPKAAIVVHSRYyrIA----AFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGqCVIYGLTVVLRKKFSASRFWDDCVKY 329
Cdd:cd05911 159 GLPKGVCLSHRNL--IAnlsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 330 NCTVVQYIGEICRYLLRQPVRDVEQRHRVR-LAVGNG-LRPAIWEEFTQRFGVPQIGEFYGATECNCSIA---NMDGKVG 404
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 405 SCGfnsrILTHVYPIRLvkVNEDTMEPLrdseglcipcQPGEPG-LLV--GQInqqdplrrFDGYVSD-SATNKKIAHSV 480
Cdd:cd05911 316 SVG----RLLPNVEAKI--VDDDGKDSL----------GPNEPGeICVrgPQV--------MKGYYNNpEATKETFDEDG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 481 FRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIA-DP 559
Cdd:cd05911 372 WLH------TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVrKP 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1268743554 560 HSQLDPNSMYQELQKVLASY----ARPIFLRLLPQvdtTGTFKIQ 600
Cdd:cd05911 445 GEKLTEKEVKDYVAKKVASYkqlrGGVVFVDEIPK---SASGKIL 486
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
77-607 |
3.49e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 174.22 E-value: 3.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA 156
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksLLKFC--SGDLGPESILPDTQLLDPMLAEAPTTPLaq 234
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLP--TVRTVivEGDGPAAPLAPEVGEYEELLAAASDTFD-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 235 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGniMGVGQCVIY-GLTVVL 313
Cdd:PRK06187 161 FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPYLALMaGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 314 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVpQIGEFYGATE 391
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CncsianmdGKVGSCGFNSRILTHVYPIRL----------VKVNEDTMEPLrdseglciPCQPGEPGLLV--GQINQQdp 459
Cdd:PRK06187 318 T--------SPVVSVLPPEDQLPGQWTKRRsagrplpgveARIVDDDGDEL--------PPDGGEVGEIIvrGPWLMQ-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 460 lrrfdGYVSD-SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 538
Cdd:PRK06187 380 -----GYWNRpEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 539 VYGV----------AVpgVEGKAGMaaiadphsQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqRE 607
Cdd:PRK06187 448 VIGVpdekwgerpvAV--VVLKPGA--------TLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
86-615 |
5.97e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 174.14 E-value: 5.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDAS---SGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 162
Cdd:COG0365 19 AEGRGDKVALIWEGedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 163 RREPLAFCLGTSAAKALI------YGG---EMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTT-PL 232
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglRGGkviDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEfEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 233 AQAPGkgmDDRLFYIYTSGTTGLPKAaiVVHS-RYYRIAA--FGHHSYSMRAADVLY---DClplyhsaGNIMGVGQCVI 306
Cdd:COG0365 179 EPTDA---DDPLFILYTSGTTGKPKG--VVHThGGYLVHAatTAKYVLDLKPGDVFWctaDI-------GWATGHSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 307 YGL----TVVL---RKKF-SASRFWDDCVKYNCTVvqyigeIC------RYLLRQPVRDVEQRHRVRL----AVGNGLRP 368
Cdd:COG0365 247 GPLlngaTVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDLSSLrllgSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 369 AIWEEFTQRFGVPqIGEFYGATECNCSIAN----MDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQP 444
Cdd:COG0365 321 EVWEWWYEAVGVP-IVDGWGQTETGGIFISnlpgLPVKPGSMGK---------PVPGYDVA------VVDEDG--NPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 445 GEPGLLVgqinqqdpLRR-----FDGYVSDSATNKKiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 519
Cdd:COG0365 383 GEEGELV--------IKGpwpgmFRGYWNDPERYRE---TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 520 STTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNsMYQELQ----KVLASYARP---IFLRLLPq 590
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAfvVLKPGVEPSDE-LAKELQahvrEELGPYAYPreiEFVDELP- 527
|
570 580
....*....|....*....|....*..
gi 1268743554 591 vdTTGTFKIQKTRLQR--EGFDPRQTS 615
Cdd:COG0365 528 --KTRSGKIMRRLLRKiaEGRPLGDTS 552
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
67-542 |
3.88e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 162.79 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 67 ELRRHRRagDTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWL 146
Cdd:PRK08316 4 RSTRARR--QTIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 147 GLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKS---LLKFCSGDLGPESILPDTQLLDpm 223
Cdd:PRK08316 80 ACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtliLSLVLGGREAPGGWLDFADWAE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 224 lAEAPTTPLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYR-IAAFGhhsysMRAADVLYDCLPLYHSAGni 298
Cdd:PRK08316 158 -AGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHraliAEYVScIVAGD-----MSADDIPLHALPLYHCAQ-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 299 MGV--GQCVIYGLTVVLRKKFSASRFWDDCVKYNC-------TVvqYIGeicryLLRQPVRDveqrhRVRLAvgnGLRPA 369
Cdd:PRK08316 227 LDVflGPYLYVGATNVILDAPDPELILRTIEAERItsffappTV--WIS-----LLRHPDFD-----TRDLS---SLRKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 370 ----------IWEEFTQRFgvPQIG--EFYGATEcncsIA---------NMDGKVGSCG---FN--SRIlthvypirlvk 423
Cdd:PRK08316 292 yygasimpveVLKELRERL--PGLRfyNCYGQTE----IAplatvlgpeEHLRRPGSAGrpvLNveTRV----------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 424 VNEDtMEPLrdseglcipcQPGEPGLLVGQINQQdplrrFDGYVSDSAtnkKIAHSvFRKGdsAYLSGDVLVMDELGYMY 503
Cdd:PRK08316 355 VDDD-GNDV----------APGEVGEIVHRSPQL-----MLGYWDDPE---KTAEA-FRGG--WFHSGDLGVMDEEGYIT 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 1268743554 504 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:PRK08316 413 VVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-604 |
4.81e-43 |
|
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: 161.71 E-value: 4.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALI--YGGEMAA---------AVAEVSEQLGKSLLKFCSGDLGPesilpdtqlLDPMLAEAPTTPLAQAPgk 238
Cdd:cd05926 81 YLADLGSKLVLtpKGELGPAsraasklglAILELALDVGVLIRAPSAESLSN---------LLADKKNAKSEGVPLPD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 239 gmDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRK 315
Cdd:cd05926 150 --DLALI-LHTSGTTGRPKGVPLTHR---NLAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 316 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFTQRFGVPQIgEFYGATE- 391
Cdd:cd05926 224 RFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPpklRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEa 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 -----CNCSIANMDgKVGSCGFNS----RILthvypirlvkvnedtmeplrDSEGLciPCQPGEpgllVGQINQQDPlRR 462
Cdd:cd05926 303 ahqmtSNPLPPGPR-KPGSVGKPVgvevRIL--------------------DEDGE--ILPPGV----VGEICLRGP-NV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 463 FDGYVSDSATNKKIAHSV--FRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 540
Cdd:cd05926 355 TRGYLNNPEANAEAAFKDgwFRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAF 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 541 GVAVPgVEGKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRL 604
Cdd:cd05926 428 GVPDE-KYGEEVAAAVvLREGASVTEEELRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
77-605 |
3.92e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 159.68 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 156
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLaeAPTTPLAQ 234
Cdd:PRK07656 82 VVPLNTRYTAdeAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFL--AAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 235 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLR 314
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPQIGEFYGATEC 392
Cdd:PRK07656 240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 393 nCSIANM-----DGKV--GSCGfnsrilthvYPIRLVKvnedtmepLRDSEGLCIPCQPGEPGLLVgqinqqdpLRRFD- 464
Cdd:PRK07656 320 -SGVTTFnrlddDRKTvaGTIG---------TAIAGVE--------NKIVNELGEEVPVGEVGELL--------VRGPNv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 465 --GYVSDS-ATnkkiAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 541
Cdd:PRK07656 374 mkGYYDDPeAT----AAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 542 VAVPGVeGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPqVDTTGtfKIQKTRLQ 605
Cdd:PRK07656 448 VPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPrsiEFLDELP-KNATG--KVLKRALR 511
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
104-604 |
4.13e-41 |
|
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: 154.80 E-value: 4.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 183
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EmaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05972 81 E---------------------------------------------------------DPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 SryyriAAFGHHSYS-----MRAADVLY---DCLPLYHSAGNIMGVgqcVIYGLTVVL--RKKFSASRFWDDCVKYNCTV 333
Cdd:cd05972 104 S-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 334 VQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN---MDGKVGSC 406
Cdd:cd05972 176 FCGPPTAYRMLIKQ---DLSSYKFSHLrlvvSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNfpdMPVKPGSM 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 407 GFNsrilTHVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKiahsVFRKGds 486
Cdd:cd05972 252 GRP----TPGYDVAII-----------DDDGR--ELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEA----SIRGD-- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 487 AYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPN 566
Cdd:cd05972 306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAFVVLTSGYEPSE 384
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1268743554 567 SMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05972 385 ELAEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
81-601 |
2.22e-40 |
|
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: 154.96 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALV---DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 157
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 158 LNVNLRREPLAFCLGTSAAKALIYGGE--MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMlAEAPTTPLAQA 235
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNA-SPDFERPTANS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 236 PGKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYriaAFGHHSYSMRAADVLYDCLplyHSAGNIMGVGQCV---IYG---- 308
Cdd:cd05970 181 YPCGEDILLVY-FSSGTTGMPK--MVEHDFTY---PLGHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGqwia 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 309 ---LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRhRVRLAV--GNGLRPAIWEEFTQRFGVpQI 383
Cdd:cd05970 252 gaaVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS-SLRYCTtaGEALNPEVFNTFKEKTGI-KL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 GEFYGATECNCSIAN---MDGKVGSCGFNsrilTHVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINQQDPL 460
Cdd:cd05970 330 MEGFGQTETTLTIATfpwMEPKPGSMGKP----APGYEIDLI-----------DREGR--SCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 461 RRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 540
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 541 GVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd05970 467 GVPDP-IRGQVVKATIVLAKGYEPSEELKKELQdhvkKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
81-605 |
9.62e-40 |
|
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: 151.95 E-value: 9.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:cd05936 4 LLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLkfcsgdlgpesilpdtqlldPMLAEAPTTPlaqapgkgm 240
Cdd:cd05936 82 LYTPRELEHILNDSGAKALI--------VAVSFTDLLAAGA--------------------PLGERVALTP--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSY--SMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFS 318
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 319 ASRFWDDCVKYNCTVVQ-----YIGeicryLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATE 391
Cdd:cd05936 205 PIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIA-N-MDG--KVGSCGfnsrilthvYPIRLVKVNedtmepLRDSEGLCIPcqPGEPGLLVgqinqqdpLR---RFD 464
Cdd:cd05936 279 TSPVVAvNpLDGprKPGSIG---------IPLPGTEVK------IVDDDGEELP--PGEVGELW--------VRgpqVMK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 465 GYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAV 544
Cdd:cd05936 334 GYWNRPEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPD 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 545 P--GVEGKAgmAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLQ 605
Cdd:cd05936 408 PysGEAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPrqvEFRDELPK-SAVG--KILRRELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
105-605 |
8.65e-35 |
|
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: 137.21 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05919 92 DIA---------------------------------------------------------YLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 265 RYYRIA-AFGHHSYSMRAADVLYDCLPLYHSAG---NIMGVGQCviyGLTVVLRKKF-SASRFWDDCVKYNCTVVQYIGE 339
Cdd:cd05919 115 DPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGlgnSLWFPLAV---GASAVLNPGWpTAERVLATLARFRPTVLYGVPT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 340 ICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATEC-NCSIANMDGKV--GSCGfnsRILT 414
Cdd:cd05919 192 FYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVgHIFLSNRPGAWrlGSTG---RPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 415 HvYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPlrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVL 494
Cdd:cd05919 268 G-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRA----TFNGG--WYRTGDKF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 495 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAAIADPHSQLDPN-----SMY 569
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPAAPQeslarDIH 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 1268743554 570 QELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-593 |
3.08e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 137.37 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGdTIPcifQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 121
Cdd:PRK07788 19 HYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFA-GLV---AHAARRAPDRAALIDERGTL--TYAELDEQSNALARGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 122 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 201
Cdd:PRK07788 93 ALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 202 KFCSGDLGPESIlPDTQLLDPMLAEAPTTPLAQAPGKGMddrlFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHsYSMR 280
Cdd:PRK07788 173 WGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEpSPLAPLAGLLSR-VPFR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 281 AADVLYDCLPLYHSagniMGVGQCVI---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRH- 356
Cdd:PRK07788 247 AGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLG-PEVLAKYd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 357 ----RVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECN-CSIANMD------GKVGScgfnsrilthvyPIRLVKVN 425
Cdd:PRK07788 322 tsslKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfATIATPEdlaeapGTVGR------------PPKGVTVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 426 edtmepLRDSEGLCIPcqPGEPG-LLVGQINQqdplrrFDGYVSDSatNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYF 504
Cdd:PRK07788 389 ------ILDENGNEVP--RGVVGrIFVGNGFP------FEGYTDGR--DKQIIDGLLSSGDVGYF-------DEDGLLFV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 505 RDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARP 582
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
570
....*....|....
gi 1268743554 583 ---IFLRLLPQVDT 593
Cdd:PRK07788 524 rdvVFLDELPRNPT 537
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
86-607 |
3.11e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 133.55 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK03640 12 AFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKfcsgdlgpesilpdtqlldpmLAEAPTTPLAQAPgkgmDDRLF 245
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMN---------------------GPKEEAEIQEEFD----LDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YI-YTSGTTGLPKAAivvhsryyrIAAFGHHSYS---------MRAADVLYDCLPLYHSAG-NIMGVGqcVIYGLTVVLR 314
Cdd:PRK03640 145 TImYTSGTTGKPKGV---------IQTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGlSILMRS--VIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 KKFSASRFWDDCVKYNCT---VVQyigeicrYLLRQPVRDVEQRH-----RVRLaVGNGLRPAIWEEFTQRFGVPQIgEF 386
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTiisVVS-------TMLQRLLERLGEGTypssfRCML-LGGGPAPKPLLEQCKEKGIPVY-QS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 387 YGATECNCSIANMD-----GKVGSCG---FNSRIlthvypirlvKVNEDTMEplrdseglCIPCQPGE-----PGLLVGQ 453
Cdd:PRK03640 285 YGMTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvkgPNVTKGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 454 INQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 533
Cdd:PRK03640 347 LNRED------------ATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPG 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 534 QTDVAVYGVAvpgvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQRE 607
Cdd:PRK03640 408 VAEAGVVGVP----DDKWGQVPVAFvvKSGEVTEEELRHFCEEKLAKYKVPkrfYFVEELPR---NASGKLLRHELKQL 479
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
81-604 |
4.18e-33 |
|
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: 133.65 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSL--TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKF-CSGDLGPESILPD-TQLLD---PMLAEAPTTPlaqa 235
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLiVSGGAGPEAGALLlAELVAaeaEQLKPAATHA---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 236 pgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIY----GLT 310
Cdd:cd05959 163 -----DDPAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLRKKF-SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVpQIGEFY 387
Cdd:cd05959 234 TVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 388 GATEC-NCSIANMDGKV--GSCGfnsrILTHVYPIRLVkvnEDTMEPLRDSEglcipcqPGE-----PGLLVGQINQQDP 459
Cdd:cd05959 313 GSTEMlHIFLSNRPGRVryGTTG----KPVPGYEVELR---DEDGGDVADGE-------PGElyvrgPSSATMYWNNRDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 460 LRR-FDGYvsdsatnkkiahsvfrkgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQTDVA 538
Cdd:cd05959 379 TRDtFQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-----VQHPA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 539 VYGVAVPGVEGKAGM----AAIADPHSQLDPNSMYQELQK----VLASYARP---IFLRLLPQvdtTGTFKIQKTRL 604
Cdd:cd05959 434 VLEAAVVGVEDEDGLtkpkAFVVLRPGYEDSEALEEELKEfvkdRLAPYKYPrwiVFVDELPK---TATGKIQRFKL 507
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
86-555 |
2.79e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 128.27 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFcsgDLGPESILPDTQLLDPMLAEAPTTPLAQAP-GKGMddrl 244
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIADESlGTDM---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 245 fyIYTSGTTGLPKAAivvhsryYR------------IAAFGHHSYSMRAADVLYDCLPLYHSA-GNIMGVGQCViyGLTV 311
Cdd:PRK13391 160 --LYSSGTTGRPKGI-------KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL--GGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 312 VLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVrlavgNGLRPAIW----------EEFTQRFGvP 381
Cdd:PRK13391 229 IVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP-EEVRDKYDL-----SSLEVAIHaaapcppqvkEQMIDWWG-P 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 382 QIGEFYGATECN----CSIANMDGKVGSCGfnsRILTHVYPIRlvkvnEDTMEplrdseglciPCQPGEPgllvGQINQQ 457
Cdd:PRK13391 302 IIHEYYAATEGLgftaCDSEEWLAHPGTVG---RAMFGDLHIL-----DDDGA----------ELPPGEP----GTIWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 458 DPlRRFDgYVSDSAtnkKIAHSvfRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 536
Cdd:PRK13391 360 GG-RPFE-YLNDPA---KTAEA--RHPDGTWsTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAD 432
|
490 500 510
....*....|....*....|....*....|...
gi 1268743554 537 VAVYGV--------------AVPGVEGKAGMAA 555
Cdd:PRK13391 433 AAVFGVpnedlgeevkavvqPVDGVDPGPALAA 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
104-606 |
5.56e-31 |
|
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: 126.01 E-value: 5.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 183
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeaptTPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05971 84 ----------------------------------------------TDGS-------DDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 sryyRIaAFGHhsysmraADVLYDCLPLYHSAGNIM----------GVGQCVI----YGLTVVLRK--KFSASRFWDDCV 327
Cdd:cd05971 111 ----RV-LLGH-------LPGVQFPFNLFPRDGDLYwtpadwawigGLLDVLLpslyFGVPVLAHRmtKFDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 328 KYNCTVVqYIGEICRYLLRQpVRDVEQRHRVRL-AVGNGLRPAIWEEF---TQRFGVPqIGEFYGATECNCSIAN----M 399
Cdd:cd05971 179 RYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLrAIATGGESLGEELLgwaREQFGVE-VNEFYGQTECNLVIGNcsalF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 400 DGKVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEPGLLVgqINQQDPLrRFDGYVSD-SATNKKIAH 478
Cdd:cd05971 256 PIKPGSMG-------KPIPGHRVAIVDDNGTPL----------PPGEVGEIA--VELPDPV-AFLGYWNNpSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 479 SVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIAD 558
Cdd:cd05971 316 DWLLTGDLGRKDSD-------GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP-IRGEIVKAFVVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 559 PHSQLDPNSMYQELQKV----LASYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05971 388 NPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
86-605 |
8.73e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.46 E-value: 8.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRre 165
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 plafclgtsaakaliyGGEMAAAVAEVSEQLgksLLkfcsGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLF 245
Cdd:PRK09088 83 ----------------ASELDALLQDAEPRL---LL----GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVHSRYYRIAA-FGHHSYSMRAADVLYDClPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD 324
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQTAHnFGVLGRVDAHSSFLCDA-PMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 325 DCVKYNCTVVQYIG--EICRYLLRQPVRDVEQ-RHRVRLAVGNGLRPAI----WEE----FTQRFGVPQIGEFYGATeCN 393
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDdgipMVDGFGMSEAGTVFGMS-VD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 394 CSIanMDGKVGSCGfnsrILTHVYPIRLVKVNEdtmeplRDseglcipCQPGEPG--LLVGQinqqdplRRFDGYVSDSA 471
Cdd:PRK09088 298 CDV--IRAKAGAAG----IPTPTVQTRVVDDQG------ND-------CPAGVPGelLLRGP-------NLSPGYWRRPQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 472 TNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGvEGKA 551
Cdd:PRK09088 352 ATARA-----FTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ-WGEV 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 552 GMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK09088 426 GYLAIVpADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
94-542 |
9.15e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 126.56 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 94 ALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 173
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 174 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPdtqlLDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGT 252
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPDTPIAdETAGADM------LYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 253 TGLPK---------AAIVVHSRYYRIAAFGHHSYsmrAADVLYDCLPLYHSAGN--IMGVGQCviyGLTVVLRKKFSASR 321
Cdd:PRK08276 152 TGRPKgikrplpglDPDEAPGMMLALLGFGMYGG---PDSVYLSPAPLYHTAPLrfGMSALAL---GGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 322 FWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVRlavgnGLRPAI----------------WeeftqrFGvPQIGE 385
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLP-EEVRARYDVS-----SLRVAIhaaapcpvevkramidW------WG-PIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 386 FYGATECN----CSIANMDGKVGSCGfnsRILTHVypirlVKVNEDTMEPLrdseglciPcqPGEPGLLVGQINQQDplr 461
Cdd:PRK08276 293 YYASSEGGgvtvITSEDWLAHPGSVG---KAVLGE-----VRILDEDGNEL--------P--PGEIGTVYFEMDGYP--- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 462 rFDgYVSDSATNKKIAHsvfRKGDSAYlsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 541
Cdd:PRK08276 352 -FE-YHNDPEKTAAARN---PHGWVTV--GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG 424
|
.
gi 1268743554 542 V 542
Cdd:PRK08276 425 V 425
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
105-639 |
8.33e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 125.99 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLnvnlrrEPlafclgtsaakaliyGGE 184
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM------PP---------------DTD 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAAV--AEVSE------------QLGKSLLKFCSGD-----LGPESILPDTQLLDPMLAEAPTTplaQAPGKGMDDRLF 245
Cdd:PRK07868 533 LAAAVrlGGVTEiitdptnleaarQLPGRVLVLGGGEsrdldLPDDADVIDMEKIDPDAVELPGW---YRPNPGLARDLA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVHSRYyRIAAFGHHSY-SMRAADVLYdCL-PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFW 323
Cdd:PRK07868 610 FIAFSTAGGELVAKQITNYRW-ALSAFGTASAaALDRRDTVY-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 324 DDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG-K 402
Cdd:PRK07868 688 QEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaK 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 403 VGSCGfnsRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGqinqqdplrRFDGYVSDSATNKKiahSVFR 482
Cdd:PRK07868 768 IGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLA---------RARGPIDPTASVKR---GVFA 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 483 KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRlLGQTDVAV-YGVAVPGVEgkAGMAAIA-DPH 560
Cdd:PRK07868 833 PADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGR-IGGVDLAVtYGVEVGGRQ--LAVAAVTlRPG 909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 561 SQLDPnsmyQELQKVLASYA---RPIFLRLLPQVDTTGTFKIQKTRLQREGFdPRqTSDRLFFLDLKQGRYVPLDERVHA 637
Cdd:PRK07868 910 AAITA----ADLTEALASLPvglGPDIVHVVPEIPLSATYRPTVSALRAAGI-PK-PGRQAWYFDPETNRYRRLTPAVRA 983
|
..
gi 1268743554 638 RI 639
Cdd:PRK07868 984 EL 985
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
79-543 |
3.66e-29 |
|
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: 121.46 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 79 PCIFQAVAR---RQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 155
Cdd:cd05923 1 QTVFEMLRRaasRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 156 ALLNVNLRREPLAFClgtsaakalIYGGEMAAAVAEVSEQlgksllkfcsgdLGPESILPDTQLL----DPMLAEAPT-T 230
Cdd:cd05923 81 ALINPRLKAAELAEL---------IERGEMTAAVIAVDAQ------------VMDAIFQSGVRVLalsdLVGLGEPESaG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 231 PLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHS-YSMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 308
Cdd:cd05923 140 PLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 309 LTVVLRKKFSASRfwddcvkynctVVQYIGE---ICRYL-----------LRQPVRDVEQRHRVRLAvGNGLRPAIWEEF 374
Cdd:cd05923 220 GTYVVVEEFDPAD-----------ALKLIEQervTSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVLERV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 375 TQRFGVPQIgEFYGATECNCSIANMDGKVGSC---GFNSRilthvypIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLV 451
Cdd:cd05923 288 NQHLPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEALANGEEGELIVAAAADAAFT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 452 GQINQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYL--SGDVLVMDELGYMYFrdrSGdtfrwrGENVSTTEVEAVLS 529
Cdd:cd05923 360 GYLNQPE------------ATAKKLQDGWYRTGDVGYVdpSGDVRILGRVDDMII---SG------GENIHPSEIERVLS 418
|
490
....*....|....
gi 1268743554 530 RLLGQTDVAVYGVA 543
Cdd:cd05923 419 RHPGVTEVVVIGVA 432
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-607 |
5.38e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.72 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 75 GDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvv 154
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 155 AALLNVN--LRREPLAFCLGTSAAKALIYGGEMAAA--VAEVSEqLGKSLLKFCSGDLGPESiLPDTQLLDPMLAEAPTT 230
Cdd:PRK12583 95 AILVNINpaYRASELEYALGQSGVRWVICADAFKTSdyHAMLQE-LLPGLAEGQPGALACER-LPELRGVVSLAPAPPPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 231 PLA----QAPGKGM--------------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLY 292
Cdd:PRK12583 173 FLAwhelQARGETVsrealaerqasldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 293 HSAGNIMGVGQCVIYGLTVVL-RKKFSASRFWDDCVKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GN 364
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGImaGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 365 GLRPAIWEEFTQRFGVPQIGEFYGATECN------CSIANMDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGL 438
Cdd:PRK12583 328 PCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqtTAADDLERRVETVG---RTQPHLE----VKV--------VDPDGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 439 CIPcqPGEPGLLVgqinqqdplrrFDGYV-------SDSATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDT 511
Cdd:PRK12583 393 TVP--RGEIGELC-----------TRGYSvmkgywnNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 512 FRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLP 589
Cdd:PRK12583 454 IIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*...
gi 1268743554 590 QVDTTGTFKIQKTRLqRE 607
Cdd:PRK12583 532 EFPMTVTGKVQKFRM-RE 548
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
86-606 |
1.25e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALV------DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAlLN 159
Cdd:PRK07529 35 AARHPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP-IN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 160 VNLRREPLAFCLGTSAAKALIYGGEMAAA-----VAEVSEQL--GKSLLK-FCSGDLGPESILPDTQL----------LD 221
Cdd:PRK07529 114 PLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVLAALpeLRTVVEvDLARYLPGPKRLAVPLIrrkaharildFD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 222 PMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGV 301
Cdd:PRK07529 194 AELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 302 GQCVIYGLTVVL------RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVEQrhrVRLAVGNG--LRPAIW 371
Cdd:PRK07529 274 LAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVdgHDISS---LRYALCGAapLPVEVF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 372 EEFTQRFGVPqIGEFYGATECNC--SIANMDG--KVGSCGFnsRI-LTHVypiRLVKVNEDTmEPLRDseglcipCQPGE 446
Cdd:PRK07529 351 RRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGL--RLpYQRV---RVVILDDAG-RYLRD-------CAVDE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 447 PGLLVgqinQQDPlRRFDGYVsDSATNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 526
Cdd:PRK07529 417 VGVLC----IAGP-NVFSGYL-EAAHNKGL-----WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 527 VLSRLlgqtdvavygvavPGVegkAGMAAIA--DPHS--------QLDPNSMYQELQkvLASYAR---------PIFLRL 587
Cdd:PRK07529 486 ALLRH-------------PAV---ALAAAVGrpDAHAgelpvayvQLKPGASATEAE--LLAFARdhiaeraavPKHVRI 547
|
570
....*....|....*....
gi 1268743554 588 LPQVDTTGTFKIQKTRLQR 606
Cdd:PRK07529 548 LDALPKTAVGKIFKPALRR 566
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
86-605 |
2.47e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 116.68 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK06178 43 ARERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGPESI---LPD---------TQLLDPMLAEAPTTPL 232
Cdd:PRK06178 121 ELSYELNDAGAEVLLALDQLAPVVEQVRAETSlRHVIVTSLADVLPAEPtlpLPDslraprlaaAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 233 AQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGL 309
Cdd:PRK06178 201 VPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 310 TVVLRKKFSASRFWDDCVKYNCT----VVQYIGEIC------RYLLR--QPVR--------DVEQRHRVRLAVGNGLRPA 369
Cdd:PRK06178 279 TLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVELMdhprfaEYDLSslRQVRvvsfvkklNPDYRQRWRALTGSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 370 IWeeftqrfgvpqigefyGATE---CNCSIANMdgKVGSCGFNSRILTHVYPI---RLVKVNEDTMEPLrdseglciPC- 442
Cdd:PRK06178 359 AW----------------GMTEthtCDTFTAGF--QDDDFDLLSQPVFVGLPVpgtEFKICDFETGELL--------PLg 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 443 QPGE-----PGLLVGQINQQDplrrfdgyvsdsATnkkiAHSvFRkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 517
Cdd:PRK06178 413 AEGEivvrtPSLLKGYWNKPE------------AT----AEA-LR--DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 518 NVSTTEVEAvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAIA----DPHSQLDPNSMYQELQKVLASYARPIfLRLLPQV 591
Cdd:PRK06178 474 SVFPSEVEA----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDAL 546
|
570
....*....|....
gi 1268743554 592 DTTGTFKIQKTRLQ 605
Cdd:PRK06178 547 PMTATGKVRKQDLQ 560
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
82-609 |
2.64e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.13 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 82 FQAVARRQPERLAL-VDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:PRK07514 6 FDALRAAFADRDAPfIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPESilpdtqLLDpmLAEAPTTPLAQAPgKGM 240
Cdd:PRK07514 86 AYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV-ETLDADGTGS------LLE--AAAAAPDDFETVP-RGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAs 320
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 321 rfwDDCVKY--NCTVVqyIGEICRY--LLRQPVRDVEQRHRVRLAVgNGLRPAIWE---EFTQRFGVPqIGEFYGATECN 393
Cdd:PRK07514 235 ---DAVLALmpRATVM--MGVPTFYtrLLQEPRLTREAAAHMRLFI-SGSAPLLAEthrEFQERTGHA-ILERYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 394 CSIAN-MDGK--VGSCGFnsrilthvyPIRLVKV---NEDTMEPLrdseglcipcQPGEpgllVGQINQQDPlRRFDGY- 466
Cdd:PRK07514 308 MNTSNpYDGErrAGTVGF---------PLPGVSLrvtDPETGAEL----------PPGE----IGMIEVKGP-NVFKGYw 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 -VSDsatnkKIAHSvFRkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 545
Cdd:PRK07514 364 rMPE-----KTAEE-FR-ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 546 GVeGKAGMAA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 609
Cdd:PRK07514 437 DF-GEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL-REQY 499
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
104-606 |
5.89e-27 |
|
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: 113.60 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFclgtsaakaliygg 183
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtQLLDpmlAEApttplaqapgkGMDDRLFYIYTSGTTGLPKAAIVvh 263
Cdd:cd05912 68 ----------------------------------QLKD---SDV-----------KLDDIATIMYTSGTTGKPKGVQQ-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 sryyriaAFGHHSYSMRAADV---LYD------CLPLYHSAG-NIMGVGqcVIYGLTVVLRKKFSASRFWDDCVKYNCTV 333
Cdd:cd05912 98 -------TFGNHWWSAIGSALnlgLTEddnwlcALPLFHISGlSILMRS--VIYGMTVYLVDKFDAEQVLHLINSGKVTI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 334 VQYIGEICRYLLRQPVRDVEQRHRVRLaVGNGLRPAIWEEFTQRFGVPqIGEFYGATE-----CNCSIANMDGKVGSCG- 407
Cdd:cd05912 169 ISVVPTMLQRLLEILGEGYPNNLRCIL-LGGGPAPKPLLEQCKEKGIP-VYQSYGMTEtcsqiVTLSPEDALNKIGSAGk 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 408 --FNSRilthvypIRLVKVNEDtmeplrdseglciPCQPGE-----PGLLVGQINQQDplrrfdgyvsdsATNKKIAHSV 480
Cdd:cd05912 247 plFPVE-------LKIEDDGQP-------------PYEVGEillkgPNVTKGYLNRPD------------ATEESFENGW 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 481 FRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA--D 558
Cdd:cd05912 295 FKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VGIP--DDKWGQVPVAfvV 363
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 559 PHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQR 606
Cdd:cd05912 364 SERPISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
83-606 |
9.27e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.19 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 83 QAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFR-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 161
Cdd:PRK06839 9 EKRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 162 LRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESILPDTQLLDPmlAEAPTTPLAQAPGKGMD 241
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQ---------------KVSYVQRVISITSL--KEIEDRKIDNFVEKNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASR 321
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 322 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVgNGLRPA---IWEEFTQRfGVPqIGEFYGATECNCS--- 395
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCpeeLMREFIDR-GFL-FGQGFGMTETSPTvfm 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 IANMDG--KVGSCG----FNSrilthvypIRLVKVNEDTMEplrdseglcipcqPGEpgllVGQINQQDPLRRFDGYVSD 469
Cdd:PRK06839 307 LSEEDArrKVGSIGkpvlFCD--------YELIDENKNKVE-------------VGE----VGELLIRGPNVMKEYWNRP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 470 SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE- 548
Cdd:PRK06839 362 DATEETIQ-------DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHVKw 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 549 GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLQR 606
Cdd:PRK06839 433 GEIPIAFIVkKSSSVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
86-607 |
2.27e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK06145 12 ARRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksllkfcsgdLGPESILPDTQLLDPMLAEAPTTPLAQapgkgmDDRLF 245
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEFDAIVALETPKIV----------IDAAAQADSRRLAQGGLEIPPQAAVAP------TDLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVHSRYY-----RIAAFGhhsysMRAADVLYDCLPLYHsagnimgVGQCVIYGLTVV-------L 313
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHwksidHVIALG-----LTASERLLVVGPLYH-------VGAFDLPGIAVLwvggtlrI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 314 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLR-PAI-WEEFTQRFGVPQIGEFYGATE 391
Cdd:PRK06145 222 HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIRDFTRVFTRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIANMDG-----KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGLCIPcqPGEPGllvgQINQQDPlRRFDGY 466
Cdd:PRK06145 302 TCSGDTLMEAgreieKIGSTG---RALAHV-EIRI-----------ADGAGRWLP--PNMKG----EICMRGP-KVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 VSDSatnKKIAHSVFrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 546
Cdd:PRK06145 360 WKDP---EKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 547 VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK06145 434 WGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
76-604 |
1.40e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 111.37 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 76 DTIPCIFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 155
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 156 ALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGKSLLKFCSGDLGPESIlPDTQLLDPMLA---EA 227
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLRAIAVVDDAADAT-PAPAPGARVQLfalPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 228 PTTPLAQAPGKGMDDRLFYIY-TSGTTGLPKaaIVVHS-----RYYRIAAfghHSYSMRAADVLYDCLPLYHSAGNIMGV 301
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFtTSGTTSGPK--LVLHRqatllRHARAIA---RAYGYDPGAVLLAALPFCGVFGFSTLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 302 GqCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNgLRPAiWEEFTQRF--- 378
Cdd:PRK06164 242 G-ALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPA-LGELAALArar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 379 GVPQIGeFYGATECncsIANMDGKVGSCGFNSRIL---THVYPIRLVKVnedtmeplRDSEGLCIpCQPGEPgllvGQIN 455
Cdd:PRK06164 319 GVPLTG-LYGSSEV---QALVALQPATDPVSVRIEgggRPASPEARVRA--------RDPQDGAL-LPDGES----GEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 456 QQDPlRRFDGYVSD-SATNKKI-AHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 533
Cdd:PRK06164 382 IRAP-SLMRGYLDNpDATARALtDDGYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 534 QTDVAVYGVAvpgVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASY---ARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK06164 454 VAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPVTESANGAKIQKHRL 526
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
69-607 |
1.58e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.99 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 69 RRHRRAG----DTIPCIFQAVARRQPERLALVDaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 144
Cdd:PRK06087 12 AAYRQQGywgdASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 145 WLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG--------EMAAAVAEVSEQLGKSLLkfcSGDLGPE-SILP 215
Cdd:PRK06087 91 YLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVG---VDKLAPAtSSLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 216 DTQLLdpmlaeAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYriaaFGHHSYSMR----AADVLYDCLPL 291
Cdd:PRK06087 168 LSQII------ADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYCARlnltWQDVFMMPAPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 292 YHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVrDVEQRhRVRLAVGNGLR 367
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPA-DLSAL-RFFLCGGTTIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 368 PAIWEEfTQRFGVpQIGEFYGATE-CNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTmeplrdseglcIPCqpGE 446
Cdd:PRK06087 316 KKVARE-CQQRGI-KLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-----------LPP--GC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 447 PGLLVGQINQQdplrrFDGYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PRK06087 381 EGEEASRGPNV-----FMGYLDEpELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 526 AVLSRLLGQTDVAVygVAVP----GvEGKAGMAAIADPHSQLdpnsmyqELQKVLASYAR--------PIFLRLLPQVDT 593
Cdd:PRK06087 450 DILLQHPKIHDACV--VAMPderlG-ERSCAYVVLKAPHHSL-------TLEEVVAFFSRkrvakykyPEHIVVIDKLPR 519
|
570
....*....|....
gi 1268743554 594 TGTFKIQKTRLQRE 607
Cdd:PRK06087 520 TASGKIQKFLLRKD 533
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
59-607 |
1.82e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 110.91 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 59 SVLIRVRLElrRHRRAG----DTIPCIFQAVARRQPERLALVDASSGIC----WTFAQLDTYSNAVANLFRQLGFAPGDV 130
Cdd:PRK13295 5 AVLLPPRRA--ASIAAGhwhdRTINDDLDACVASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLARLGVGRGDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 131 VAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGK-SLLKFC 204
Cdd:PRK13295 83 VSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPELPAlRHVVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 205 SGDlGPESIlpDTQLLDPMLAEAP-TTPLAQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRIAAFghHSYSMR--- 280
Cdd:PRK13295 163 GGD-GADSF--EALLITPAWEQEPdAPAILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANI--VPYAERlgl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 281 -AADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD----DCVKYNCTVVQYIGEICRyLLRQPVRDVEQR 355
Cdd:PRK13295 236 gADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTR-AVKESGRPVSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 356 hRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNC----SIANMDGKVGScgfnsrilTHVYPIRLVKVNedtmep 431
Cdd:PRK13295 315 -RTFLCAGAPIPGALVERARAALGA-KIVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 432 LRDSEGLCIPcqPGEPGLLV--GQINqqdplrrFDGYVSDSATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSG 509
Cdd:PRK13295 379 VVDADGAPLP--AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 510 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA----DPHSQLDPNSM--YQELQKVLASYArPI 583
Cdd:PRK13295 443 DVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvpRPGQSLDFEEMveFLKAQKVAKQYI-PE 517
|
570 580
....*....|....*....|....
gi 1268743554 584 FLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK13295 518 RLVVRDALPRTPSGKIQKFRLREM 541
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
105-604 |
2.58e-25 |
|
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: 109.39 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygge 184
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 maaavaeVSEQLGKsllkfcsgdlgpesilpdtqlldpmlaeapTTPLAQApgkgmDDRLFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05903 79 -------VPERFRQ------------------------------FDPAAMP-----DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 265 R-YYRIAAFGHHsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGE 339
Cdd:cd05903 117 TlSASIRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 340 ICRYLLRQPvrDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsianmdGKVGSC--GFNSRIL-THV 416
Cdd:cd05903 196 LLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECP-------GAVTSItpAPEDRRLyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 417 YPIRLVKVNedtmepLRDSEGLCIPcqPGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAHSVFrkgdsaYLSGDVLVM 496
Cdd:cd05903 266 RPLPGVEIK------VVDDTGATLA--PGV----EGELLSRGP-SVFLGYLDRPDLTADAAPEGW------FRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 497 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA-----DPHSqLDPNSMYQE 571
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DERLGERACAvvvtkSGAL-LTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....
gi 1268743554 572 LQKV-LASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05903 402 LDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
90-604 |
7.24e-25 |
|
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: 108.00 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSgiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 167
Cdd:cd05930 1 PDAVAVVDGDQ--SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG--AAYVPLDPSypAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIYGGEMAAAVaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlfyI 247
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDLAYV---------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 248 YTSGTTGLPKAAIVVHsryyriAAFGHHSYSMRAAdvlY-----DCLPLYHSAGNIMGVGQ---CVIYGLTVVLRKK--- 316
Cdd:cd05930 100 YTSGSTGKPKGVMVEH------RGLVNLLLWMQEA---YpltpgDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevr 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 317 FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATECNc 394
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEAT- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 395 sianmdgkvgscgfnsrILTHVYPIRLVKVNEDTM---EPLRDSeGLCI------PCQPGEPG-LLVG--QINQqdplrr 462
Cdd:cd05930 248 -----------------VDATYYRVPPDDEEDGRVpigRPIPNT-RVYVldenlrPVPPGVPGeLYIGgaGLAR------ 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 463 fdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVyg 541
Cdd:cd05930 304 --GYLNRPElTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV-- 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 542 VAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05930 380 VAREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
106-604 |
8.06e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 108.63 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 106 FAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEM 185
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 186 AAAVAEVSEQlGKSLLKFCSgdlgPESIL-------------PDTQLLDPMLA--EAPTTPLAQAPGKgmddrlfYIYTS 250
Cdd:PRK12406 94 LHGLASALPA-GVTVLSVPT----PPEIAaayrispalltppAGAIDWEGWLAqqEPYDGPPVPQPQS-------MIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 251 GTTGLPK-----AAIVVHSRYY---RIAAFGHHSySMRAadVLYDclPLYHSAGNIMGVgQCVIYGLTVVLRKKFSASRF 322
Cdd:PRK12406 162 GTTGHPKgvrraAPTPEQAAAAeqmRALIYGLKP-GIRA--LLTG--PLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 323 WDDCVKYNCTVVQYIGEICRYLLRQP--VR---DVEQ-RHRVRLAvgnGLRPA-IWEEFTQRFGvPQIGEFYGATECncs 395
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKLPeeVRakyDVSSlRHVIHAA---APCPAdVKRAMIEWWG-PVIYEYYGSTES--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 ianmdGKVGSCGfNSRILTHvyPIRLVKVNEDTMEPLRDSEGLCIPcqPGEPGllvgqinqqDPLRRFDGYVSDSATNKK 475
Cdd:PRK12406 309 -----GAVTFAT-SEDALSH--PGTVGKAAPGAELRFVDEDGRPLP--QGEIG---------EIYSRIAGNPDFTYHNKP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 476 IAHSVFRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMA 554
Cdd:PRK12406 370 EKRAEIDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEALMA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 555 AI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK12406 447 VVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-599 |
9.44e-25 |
|
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: 108.20 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 82 FQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 161
Cdd:cd17651 1 FERQAARTPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 162 LRREPLAFCLGTSAAKALIyggemAAAVAevseqlgksllkfcSGDLGPESIlPDTQLLDPMLAEAPTTPLaqAPGKGMD 241
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL-----THPAL--------------AGELAVELV-AVTLLDQPGAAAGADAEP--DPALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHS----------RYYRIAAFGHHS-YSMRAADVlydclplyhSAGNIMGVgqcVIYGLT 310
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRslanlvawqaRASSLGPGARTLqFAGLGFDV---------SVQEIFST---LCAGAT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLRK---KFSASRFWDDCVKYNCTVV----QYIGEICRYLLRQPVRDVEQRHRV----RLAVGNGLRpaiweEFTQRFG 379
Cdd:cd17651 205 LVLPPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLR-----EFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 380 VPQIGEFYGATECNCSIA-NMDGKVGSCGFNSRILTHVYPIRLVKVNEDtmepLRdseglciPCQPGEPG-LLVGqinqQ 457
Cdd:cd17651 280 GLRLHNHYGPTETHVVTAlSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA----LR-------PVPPGVPGeLYIG----G 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 458 DPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 536
Cdd:cd17651 345 AGLAR--GYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 537 VAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 599
Cdd:cd17651 423 AVV--LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
85-612 |
1.08e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.20 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 85 VARRQPERLALVDASSgiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVaaLLNVNLR 163
Cdd:PRK07470 16 AARRFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMFAAF-RLGAV--WVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 164 REP--LAFCLGTSAAKALIYGG---EMAAAVAEVSEQLgKSLLKFCSGDLGPEsilpdtqlLDPMLAEAPTTPLAQAPGK 238
Cdd:PRK07470 91 QTPdeVAYLAEASGARAMICHAdfpEHAAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGARVANAAVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 239 gMDDRLFYIYTSGTTGLPKAAIVVHSRYyriaAF-------------GHHSYSMRAAdvlydclPLYHSAGnIMGVGQcV 305
Cdd:PRK07470 162 -HDDPCWFFFTSGTTGRPKAAVLTHGQM----AFvitnhladlmpgtTEQDASLVVA-------PLSHGAG-IHQLCQ-V 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 306 IYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGlRPAIWEEftQRFGVPQI 383
Cdd:PRK07470 228 ARGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG-APMYRAD--QKRALAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 G----EFYGATECNCSIANM--------DG---KVGSCGFnsrilthvypirlvkvnEDT-ME-PLRDSEGLciPCQPGE 446
Cdd:PRK07470 305 GkvlvQYFGLGEVTGNITVLppalhdaeDGpdaRIGTCGF-----------------ERTgMEvQIQDDEGR--ELPPGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 447 pgllVGQINQQDPlRRFDGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 526
Cdd:PRK07470 366 ----TGEICVIGP-AVFAGYYNNPEANAK----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 527 VLSRLLGQTDVAVYGVAVPgVEGKAGMAA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKt 602
Cdd:PRK07470 435 KLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFFWDALPK---SGYGKITK- 509
|
570
....*....|
gi 1268743554 603 RLQREGFDPR 612
Cdd:PRK07470 510 KMVREELEER 519
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
86-539 |
1.37e-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: 107.71 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN-VNLRR 164
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 165 EpLAFCLGTSAAKALIyggeMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPmlAEAPTTPLAQapgkgmDDRL 244
Cdd:cd05904 95 E-IAKQVKDSGAKLAF----TTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADE--AEPPVVVIKQ------DDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 245 FYIYTSGTTGLPKAAIVVHSRYyrIAAF-GHHSY--SMRAADVLYDC-LPLYHSAGnIMGVGQCVI-YGLTVVLRKKFSA 319
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNL--IAMVaQFVAGegSNSDSEDVFLCvLPMFHIYG-LSSFALGLLrLGATVVVMPRFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 320 SRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRlAVGNG---LRPAIWEEFTQRFGVPQIGEFYGATECNCSI 396
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 397 ANMD------GKVGSCGFnsrilthVYPIRLVK-VNEDTMEPLRdseglciPCQPGEpgLLV-G-QINQqdplrrfdGYV 467
Cdd:cd05904 318 AMCFapekdrAKYGSVGR-------LVPNVEAKiVDPETGESLP-------PNQTGE--LWIrGpSIMK--------GYL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 468 SD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 539
Cdd:cd05904 374 NNpEATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
74-542 |
4.89e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 106.51 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 74 AGDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 153
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 154 VAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTqlLDpmlAEAPTTPLA 233
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVH--LD---AATEPTPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 234 QAP-GKGMDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGL 309
Cdd:PRK05852 169 STPeGLRPDDAMI-MFTGGTTGLPKMVPWTHA---NIASSVRAiitGYRLSPRDATVAVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 310 TVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPQI 383
Cdd:PRK05852 245 AVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrfirSCSAPLTAETAQALQTEFAAPVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 gEFYGATECNCSIANMDGKVGSCGFNSRILTHVypirlvkVNEDTMEPLR--DSEGLciPCQPGEpgllVGQINQQDP-- 459
Cdd:PRK05852 325 -CAFGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDGL--PLPAGA----VGEVWLRGTtv 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 460 LRrfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 538
Cdd:PRK05852 391 VR---GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAA 460
|
....
gi 1268743554 539 VYGV 542
Cdd:PRK05852 461 VFGV 464
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-604 |
1.69e-23 |
|
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: 103.91 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 91 ERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGF-APGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALIYGGEMaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlfyIYT 249
Cdd:cd05941 79 VITDSEPSLVLDPALI-------------------------------------------------------------LYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 250 SGTTGLPKAaiVVHSRyYRIAAFGH---HSYSMRAADVLYDCLPLYHSAGNIMGVgQCVIY-GLTVVLRKKFSASRFWDD 325
Cdd:cd05941 98 SGTTGRPKG--VVLTH-ANLAANVRalvDAWRWTEDDVLLHVLPLHHVHGLVNAL-LCPLFaGASVEFLPKFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 326 CVKYNCTVVQYIGEICRYLLRQPVRDVEQR--------HRVRLAV-GNG-LRPAIWEEFTQRFGVPqIGEFYGATECNCS 395
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFTDPqfaraaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGMA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 IAN-MDG--KVGSCGFnsrilthvyPIRLVK---VNEDTMEPL-RDSEG-LCIPcqpgEPGLlvgqinqqdplrrFDGYV 467
Cdd:cd05941 253 LSNpLDGerRPGTVGM---------PLPGVQariVDEETGEPLpRGEVGeIQVR----GPSV-------------FKEYW 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 468 SDSATNKKiahsVFRkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPg 546
Cdd:cd05941 307 NKPEATKE----EFT-DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP- 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 547 VEGKAGMAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05941 381 DWGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
104-545 |
2.41e-23 |
|
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: 103.35 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 183
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtqlLDPMLAEAPTtplaqapgkgMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05969 78 ------------------------------------TTEELYERTD----------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRK-KFSASRFWDDCVKYNCTVVQYIGEICR 342
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 343 YLLR---QPVRDVEQRH-RVRLAVGNGLRPAI--WEEftQRFGVPqIGEFYGATECNC-SIAN---MDGKVGSCGfnsri 412
Cdd:cd05969 192 MLMKegdELARKYDLSSlRFIHSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTETGSiMIANypcMPIKPGSMG----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 413 lthvYPIRLVK--VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYLS 490
Cdd:cd05969 264 ----KPLPGVKaaVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEE---RYKNS--------------FIDG--WYLT 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 491 GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 545
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
87-577 |
2.51e-23 |
|
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: 104.58 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 87 RRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 162
Cdd:cd17634 64 RENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 163 RREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksLLKFCSGDLGPESILPDTQLL------------------DPML 224
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITADGGVRAGRSVP------LKKNVDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDLI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 225 AEAPT--TPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGNIMGv 301
Cdd:cd17634 218 AKASPehQPEAMNA----EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYW----CTADVGWVTG- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 302 GQCVIY-----GLTVVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRP 368
Cdd:cd17634 289 HSYLLYgplacGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLrilgSVGEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 369 AIWEEFTQRFG---VPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSE-GLCIPCQP 444
Cdd:cd17634 369 EAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlVITDPWPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 445 GEPGLLvgqinqQDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 524
Cdd:cd17634 449 QTRTLF------GDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEI 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 525 EAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQKVLA 577
Cdd:cd17634 509 ESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
77-338 |
2.84e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.20 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 156
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRL--TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 LLNVNLR--REPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLaq 234
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERD-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 235 aPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRiAAFG------------HHSYSMRAAD----VLYDCLPLYHSAGnI 298
Cdd:PRK07798 158 -FGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFR-VLLGgrdfatgepiedEEELAKRAAAgpgmRRFPAPPLMHGAG-Q 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1268743554 299 MGVGQCVIYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIG 338
Cdd:PRK07798 235 WAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
72-606 |
3.27e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.68 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 72 RRAGDTIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 151
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDELGTL--TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 152 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllKFCSGDLGPESILPDTQLLDPMLAEA-PTT 230
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD-----------RALADCPQATRIVAWTDEDHDLTVEVlIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 231 PLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIYGL- 309
Cdd:PRK13382 186 HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHA----WGFSQLVLAASl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 310 --TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGvPQI 383
Cdd:PRK13382 262 acTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGsrMRPDVVIAFMDQFG-DVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 GEFYGATECN-CSIANMDGkvgscgfnsrilTHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEpgllVGQINQQDPLrR 462
Cdd:PRK13382 341 YNNYNATEAGmIATATPAD------------LRAAPDTAGRPAEGTEIRILDQDFREVP--TGE----VGTIFVRNDT-Q 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 463 FDGYVSDSATNkkiahsvFRKGDSAylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:PRK13382 402 FDGYTSGSTKD-------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 543 AVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:PRK13382 473 DDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
86-609 |
3.31e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 103.70 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICWtfAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPdtqlLDPMLAEA-PTTPLAQAPGkgmDDRL 244
Cdd:PRK07786 105 EIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG----YEDLLAEAgPAHAPVDIPN---DSPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 245 FYIYTSGTTGLPKAAIVVHSRYYRIAAfgHHSYSMRA---ADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLR--KKFSA 319
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVLTHANLTGQAM--TCLRTNGAdinSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 320 SRFWDDCVKYNCTVV-----QYIGeICRYLLRQPvRDVEQRhrvrlAVGNGLRPA---IWEEFTQRFGVPQIGEFYGATE 391
Cdd:PRK07786 255 GQLLDVLEAEKVTGIflvpaQWQA-VCAEQQARP-RDLALR-----VLSWGAAPAsdtLLRQMAATFPEAQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIANMDG-----KVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEpgllVGQINQQDPlrrfdGY 466
Cdd:PRK07786 328 MSPVTCMLLGedairKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-----TL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 VSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 546
Cdd:PRK07786 382 MSGYWNNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 547 -VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqREGF 609
Cdd:PRK07786 460 wGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
81-606 |
3.38e-23 |
|
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: 102.77 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNV 160
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSL--TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG--AAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NlrreplafclgtsaakaliyGGEMAAAVAEVSEQLGKSLLkfcsgdlgpesILPDTQlldpmlaeapttplaqapgkgm 240
Cdd:cd17653 78 D--------------------AKLPSARIQAILRTSGATLL-----------LTTDSP---------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD-------VLYDClplyhSAGNIMGvgqCVIYGLTVVL 313
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 314 RkkfSASRFWDDcVKYNCTVVQYIGEICRYLlrqPVRDVEQRHRVRLAvGNGLRPAIWEEFTqrfGVPQIGEFYGATECN 393
Cdd:cd17653 177 A---DPSDPFAH-VARTVDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRWS---PGRRLYNAYGPTECT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 394 CSIAN---MDGKVGSCGfnsrilthvYPIRLVKV---NEDTMEPLRDSEG-LCIpcqpGEPGLLVGQINQQdplrrfdgy 466
Cdd:cd17653 246 ISSTMtelLPGQPVTIG---------KPIPNSTCyilDADLQPVPEGVVGeICI----SGVQVARGYLGNP--------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 vsdSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtdvaVYGVAVPG 546
Cdd:cd17653 304 ---ALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE----VTQAAAIV 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 547 VEGKagMAAIADPHSqLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd17653 377 VNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
86-605 |
4.65e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVAALLNVNLRR 164
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 165 EPLAFCLGTSAAKALIYGGEMAAAVAEVSEQL------GKSLLKFcsGDLgpESILPDTqllDPMLAEAPTtplaqapGK 238
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGADLplrlsfGGEIDGF--GSF--EAALAGA---GPRLTEQPC-------GA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 239 GMddrlfyIYTSGTTGLPKA------AIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAgNIMGVGQCVIYGLTVV 312
Cdd:PRK13390 152 VM------LYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 313 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPA---IWEEFTQRFGvPQIGE 385
Cdd:PRK13390 225 LAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKL---DADVRTRYDVsslrAVIHAAAPCpvdVKHAMIDWLG-PIVYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 386 FYGATECNcSIANMD-----GKVGSCGFNSRILTHVYpirlvkvnedtmeplrDSEGLCIPCqpGEPGLLVGQINQQdPL 460
Cdd:PRK13390 301 YYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHIC----------------DDDGNELPA--GRIGTVYFERDRL-PF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 461 RrfdgYVSD---SATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 537
Cdd:PRK13390 361 R----YLNDpekTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 538 AVYGVAVP--GVEGKAGMAAIA--DPHSQLdPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK13390 431 AVIGVPDPemGEQVKAVIQLVEgiRGSDEL-ARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
104-607 |
6.37e-23 |
|
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: 102.93 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQL-GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG 182
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 GEMAAAVAEVSEQLG-------------------KSLLKFCSgdlgPESILPDTQLLDPMLaeapttplaqapgkgmddr 243
Cdd:cd05928 122 DELAPEVDSVASECPslktkllvseksrdgwlnfKELLNEAS----TEHHCVETGSQEPMA------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 244 lfyIY-TSGTTGLPKAAIVVHSRY-YRIAAFGHHSYSMRAADVLY---DCLPLYHSAGNIMG---VGQCVIygltVVLRK 315
Cdd:cd05928 179 ---IYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWntsDTGWIKSAWSSLFEpwiQGACVF----VHHLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 316 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNC 394
Cdd:cd05928 252 RFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKfPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 395 SIANMDG---KVGSCGFNSRilthVYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPLRRFDGYVSDSa 471
Cdd:cd05928 331 ICANFKGmkiKPGSMGKASP----PYDVQII-----------DDNGNVLP--PGTEGDIGIRVKPIRPFGLFSGYVDNP- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 472 tnKKIAHSvfRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKA 551
Cdd:cd05928 393 --EKTAAT--IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 552 GMAAI--ADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:cd05928 467 VKAFVvlAPQFLSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
113-599 |
1.36e-22 |
|
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: 101.36 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 113 SNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIygGEMAAAVAEV 192
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV-----PLNPTLKESVLRYLV--ADAGGRIVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 193 SEQLGkSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAF 272
Cdd:cd05922 76 DAGAA-DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSH------EDLALLLYTSGSTGSPKLVRLSH-QNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 273 GHHSY-SMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSASR-FWDDCVKYNCT---VVQYIGEICRYLLRQ 347
Cdd:cd05922 148 SIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 348 P-----VRDVEQrhrvrlaVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG-----KVGSCGfnsrilthvy 417
Cdd:cd05922 227 PaklpsLRYLTQ-------AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPerileKPGSIG---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 418 pirlVKVNEDTMEPLRDSEGlciPCQPGEPGLLVgqinqqdpLRR---FDGYVSDSATNKKIAhsvfRKGDSAYlSGDVL 494
Cdd:cd05922 290 ----LAIPGGEFEILDDDGT---PTPPGEPGEIV--------HRGpnvMKGYWNDPPYRRKEG----RGGGVLH-TGDLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 495 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAgMAAIADPHSQLDPNSMYqeLQK 574
Cdd:cd05922 350 RRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPKDVLRS--LAE 426
|
490 500
....*....|....*....|....*
gi 1268743554 575 VLASYARPIFLRLLPQVDTTGTFKI 599
Cdd:cd05922 427 RLPPYKVPATVRVVDELPLTASGKV 451
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
104-551 |
3.89e-21 |
|
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: 97.95 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 183
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EMAAAVAEVSeqLGKSLLKFCSGDLGPESIL---------PDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTG 254
Cdd:cd05968 172 GFTRRGREVN--LKEEADKACAQCPTVEKVVvvrhlgndfTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 255 LPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGNIMG---VGQCVIYGLTVVLRKKF----SASRFWDDC 326
Cdd:cd05968 250 KPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLT----WFTDLGWMMGpwlIFGGLILGATMVLYDGApdhpKADRLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 327 VKYNCTVVQYIGEICRYLL---RQPVRdVEQRHRVRLAVGNG--LRPAIWEEFTQRFG---VPqIGEFYGATECNCSI-- 396
Cdd:cd05968 326 EDHEITHLGLSPTLIRALKprgDAPVN-AHDLSSLRVLGSTGepWNPEPWNWLFETVGkgrNP-IINYSGGTEISGGIlg 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 397 ANMDGKVGSCGFNSrilthVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGePGLLVGqiNQQDPLRRFDGYvsdsatnkki 476
Cdd:cd05968 404 NVLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAPW-PGMTRG--FWRDEDRYLETY---------- 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 477 ahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKA 551
Cdd:cd05968 466 ----WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEA 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
243-599 |
8.93e-21 |
|
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: 93.62 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 243 RLFYI-YTSGTTGLPKAaivvhsrYYR-----IAAF--GHHSYSMRAADVLYDCLPLYHSaGNIMGVGQCVIYGLTVVLR 314
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 KKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVEQRHRVR--LAVGNGLRPAIWEEFTQRFGVPQIGEFYGATEC 392
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 393 NCSIANMDG---KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGlcipcqpGEPGLLVGQINQqdplrRFDGYVSD 469
Cdd:cd17633 149 SFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM-----VFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 470 SATNKkiaHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV------- 542
Cdd:cd17633 202 GFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarfge 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 543 -AVPGVEGKagmaaiadphsQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKI 599
Cdd:cd17633 272 iAVALYSGD-----------KLTYKQLKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
104-604 |
1.13e-20 |
|
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: 95.24 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLG-TSAAKALIY 181
Cdd:cd05958 11 WTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 182 GGEMAAavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIV 261
Cdd:cd05958 91 HALTAS-----------------------------------------------------DDICILAFTSGTTGAPKATMH 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 262 VHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIY----GLTVVLRKKFSASRFWDDCVKYNCTVVQY 336
Cdd:cd05958 118 FHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 337 IGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIgEFYGATEC-NCSIANMDGkvgscgfnsril 413
Cdd:cd05958 194 APTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMfHIFISARPG------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 414 tHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEPGLLVgqinqqdpLRRFDGYVSDSatnKKIAHSVFRKGDSAylSGDV 493
Cdd:cd05958 261 -DARPGATGKPVPGYEAKVVDDEGNPVP--DGTIGRLA--------VRGPTGCRYLA---DKRQRTYVQGGWNI--TGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 494 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG--------VEGKAGMAAIADPHSQLdp 565
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvvkafVVLRPGVIPGPVLAREL-- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1268743554 566 nsmyQELQK-VLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05958 403 ----QDHAKaHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
77-392 |
1.28e-20 |
|
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: 97.23 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 156
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG--AA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 L--LNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgDLGPESILPDTQLLDPMLAEAPTTPLAq 234
Cdd:COG1020 553 YvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLP----------------ELGVPVLALDALALAAEPATNPPVPVT- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 235 apgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVlydcLPLYH------SAGNIMGvgqCVIY 307
Cdd:COG1020 616 ------PDDLAYvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR----VLQFAslsfdaSVWEIFG---ALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 308 GLTVVLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrdVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQ 382
Cdd:COG1020 683 GATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLvgGEALPPELVRRWRARLPGAR 759
|
330
....*....|
gi 1268743554 383 IGEFYGATEC 392
Cdd:COG1020 760 LVNLYGPTET 769
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
105-539 |
1.50e-20 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 94.25 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFA-PGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 183
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EMAAAVAEVseqlgksllkfcsgdlgPESILPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:TIGR01733 81 ALASRLAGL-----------------VLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 ----------SRYY------RIAAFghHSYSMRAAdVLYDCLPLYHsagnimGVGQCVIYGltVVLRKKFSASRFWDDcv 327
Cdd:TIGR01733 143 rslvnllawlARRYgldpddRVLQF--ASLSFDAS-VEEIFGALLA------GATLVVPPE--DEERDDAALLAALIA-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 328 KYNCTVVQYIGEICRYLLRQPVRDVEQRHRVrLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECN--CSIANMDGKVGS 405
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPALASLRLV-ILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 406 CGFNSRI---LTHVypiRLVKVNEDTMeplrdseglciPCQPGEPG-LLVGQINqqdpLRRfdGYVSDSA-TNKKIAHSV 480
Cdd:TIGR01733 289 RESPVPIgrpLANT---RLYVLDDDLR-----------PVPVGVVGeLYIGGPG----VAR--GYLNRPElTAERFVPDP 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 481 FRKGDSA--YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 539
Cdd:TIGR01733 349 FAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-311 |
2.29e-20 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 95.17 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 74 AGDTIPCIFQAVARRQPERLALVDASSGI--CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 151
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 152 GVVAALLNVNLRREPLAFCLGTSAAKALIYGG-EMAAAVAEVSEQLGkSLLKFCSGDLGPESILPDTQLLDPMLA----- 225
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELP-SLRHIVVLDPRGLRDDPRLLSLDELLAlgrev 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 226 EAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGqCV 305
Cdd:COG1022 168 ADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-AL 246
|
....*.
gi 1268743554 306 IYGLTV 311
Cdd:COG1022 247 AAGATV 252
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
105-599 |
2.72e-20 |
|
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: 94.08 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05935 83 L-------------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 265 RYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYL 344
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 345 LRQPvrDVEQRHRVRLAV----GNGLRPAIWEEFTQRFGVPQIgEFYGATEcNCSianmdgkvgscgfnsriLTHVYPIR 420
Cdd:cd05935 188 LATP--EFKTRDLSSLKVltggGAPMPPAVAEKLLKLTGLRFV-EGYGLTE-TMS-----------------QTHTNPPL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 421 LVKVNEDTMePLRDSEGLCIPCQPGE--PGLLVGQINQQDPlRRFDGYVSDSATNKKIAhsVFRKGDSAYLSGDVLVMDE 498
Cdd:cd05935 247 RPKLQCLGI-P*FGVDARVIDIETGRelPPNEVGEIVVRGP-QIFKGYWNRPEETEESF--IEIKGRRFFRTGDLGYMDE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 499 LGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP--GVEGKAGMAAIADPHSQLDPNSMYQELQKVL 576
Cdd:cd05935 323 EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDErvGEEVKAFIVLRPEYRGKVTEEDIIEWAREQM 402
|
490 500
....*....|....*....|....*.
gi 1268743554 577 ASYARP---IFLRLLPQvdtTGTFKI 599
Cdd:cd05935 403 AAYKYPrevEFVDELPR---SASGKI 425
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-604 |
2.99e-20 |
|
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: 94.26 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 82 FQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 162 LRREPLAFCLGTSAAKALIYGGEMAAAVAEVseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKgmD 241
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAG---------------------GDVALLGDEALAAPPATPPLVPPRP--D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVL-------YDC------LPLYHSAGNIMGV--GQCVI 306
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVlqktplsFDVsvwelfWPLVAGARLVVARpgGHRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 307 YGLTVVLRkkfsasrfwDDCVkyncTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIG 384
Cdd:cd17646 219 AYLAALIR---------EHGV----TTCHFVPSMLRVFLAEP--AAGSCASLRRVFcsGEALPPELAARFLALPGAE-LH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 385 EFYGATE-------CNCSIANMDGKV--GSCGFNSRILthvypirlvkVNEDTMEplrdseglciPCQPGEPG-LLVGQI 454
Cdd:cd17646 283 NLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTRLY----------VLDDALR----------PVPVGVPGeLYLGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 455 nqqdPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 533
Cdd:cd17646 343 ----QLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 534 QTDVAVygVAVPGVEGKAGMAA---IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17646 417 VTHAVV--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-606 |
6.44e-20 |
|
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: 92.97 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvnlrREPL--AFclgtsaakaliyg 182
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAV---------YQPLftAF------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 gemaaavaevseqlgksllkfcsgdlGPESIlpdTQLLDPMLAEAPTTPLAQApGKGMDDRLFYIYTSGTTGLPKaAIVV 262
Cdd:cd05973 60 --------------------------GPKAI---EHRLRTSGARLVVTDAANR-HKLDSDPFVMMFTSGTTGLPK-GVPV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 263 HSRYyrIAAFghHSYSMRAADVLYDclplyHSAGNIMGVGQCviYGL-------------TVVLRKKFSASRFWDDCVKY 329
Cdd:cd05973 109 PLRA--LAAF--GAYLRDAVDLRPE-----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 330 NCTVVQYIGEICRYLLRQPVrDVEQRHRVRLAV----GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIANMDG---- 401
Cdd:cd05973 178 GVTNLAGSPTAYRLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehp 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 402 -KVGSCGFnsrilthVYP-IRLVKVNEDTMEPLrdseglcipcqPGEPGLLVGQINQQdPLRRFDGYvsdsatnkkiahs 479
Cdd:cd05973 256 vHAGSAGR-------AMPgWRVAVLDDDGDELG-----------PGEPGRLAIDIANS-PLMWFRGY------------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 480 vFRKGDSA-----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG----VEGK 550
Cdd:cd05973 304 -QLPDTPAidggyYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPErtevVKAF 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 551 AGMAAIADPHSQLDpNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05973 383 VVLRGGHEGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
81-604 |
1.13e-19 |
|
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: 92.65 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:cd12117 2 LFEEQAARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKgm 240
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGG----------------------LEVAVVIDEALDAGPAGNPAVPVSP-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIV--------VHSRYYriAAFGHHSYSMRAADVLYD--CLPLYhsaGNIMGVGQCVIYGLT 310
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVAVthrgvvrlVKNTNY--VTLGPDDRVLQTSPLAFDasTFEIW---GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLrkkfSASRFWDDCVKYNCTVVQyigeICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFTQRFGVPQIGEFY 387
Cdd:cd12117 211 TLL----DPDALGALIAEEGVTVLW----LTAALFNQLADEDPECFaglRELLTGGEVVSPPHVRRVLAACPGLRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 388 GATE-----CNCSIANMDGKVGScgfnsrilthvYPI-------RLVKVNEDtmepLRdseglciPCQPGEPG-LLVGqi 454
Cdd:cd12117 283 GPTEnttftTSHVVTELDEVAGS-----------IPIgrpiantRVYVLDED----GR-------PVPPGVPGeLYVG-- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 455 nqQDPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 533
Cdd:cd12117 339 --GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 534 QTDVAVygVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd12117 415 VREAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
69-257 |
4.39e-19 |
|
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: 90.98 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 69 RRHRRAG----DTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 144
Cdd:COG1021 14 ARYREAGywrgETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 145 WLGLAKAGV--VAALlnVNLRR-EPLAFClGTSAAKALI----YGG----EMAAAVAEVSEQLGKSLLkfcSGDLGPESI 213
Cdd:COG1021 92 FFALFRAGAipVFAL--PAHRRaEISHFA-EQSEAVAYIipdrHRGfdyrALARELQAEVPSLRHVLV---VGDAGEFTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1268743554 214 LPDtqlldpmLAEAPTTPLAQAPgkGMDDRLFYIYTSGTTGLPK 257
Cdd:COG1021 166 LDA-------LLAAPADLSEPRP--DPDDVAFFQLSGGTTGLPK 200
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-542 |
4.72e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 90.82 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 71 HRRAGDTIPCIFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEfvgLWLGLAk 150
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 151 AGVVAALLNVNLrrEPL------AFCLGTSAAKALIY--------GGEMAAAVAEVseqlgKSLLKFCSGDLGPEsilpd 216
Cdd:PRK06188 81 AAQLAGLRRTAL--HPLgslddhAYVLEDAGISTLIVdpapfverALALLARVPSL-----KHVLTLGPVPDGVD----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 217 tqlldpMLAEAPTTPLAQA-PGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSA 295
Cdd:PRK06188 149 ------LLAAAAKFGPAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 296 GNImgVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV----GNGLRPAIW 371
Cdd:PRK06188 223 GAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHP--DLRTRDLSSLETvyygASPMSPVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 372 EEFTQRFGvPQIGEFYGATECNCSIANMD---------GKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPc 442
Cdd:PRK06188 299 AEAIERFG-PIFAQYYGQTEAPMVITYLRkrdhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 443 qPGEPgllvGQINQQDPLrRFDGYVSDSATNKKiahsVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVST 521
Cdd:PRK06188 362 -QGEV----GEICVRGPL-VMDGYWNRPEETAE----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFP 428
|
490 500
....*....|....*....|.
gi 1268743554 522 TEVEAVLSRLLGQTDVAVYGV 542
Cdd:PRK06188 429 REVEDVLAEHPAVAQVAVIGV 449
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-605 |
5.34e-19 |
|
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: 88.87 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 248 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL-RKKFSASRFWDDC 326
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 327 VKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIAN- 398
Cdd:cd05917 89 EKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 399 -----MDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGLCIPcQPGEPGLLVgqinqqdpLRRFD---GYVSD- 469
Cdd:cd05917 164 rtddsIEKRVNTVG---RIMPHTE----AKI--------VDPEGGIVP-PVGVPGELC--------IRGYSvmkGYWNDp 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 470 SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeG 549
Cdd:cd05917 220 EKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-G 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 550 KAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05917 293 EEVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
91-542 |
8.31e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 90.34 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 91 ERLAL--VDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLeGR-PEFVGLWLGLAKAGVVAALLNVNLRREPL 167
Cdd:PRK04319 59 DKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFM-PRiPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIYGGEMAAAVaeVSEQLGKslLK--FCSGDLGPESilPDTQLLDPMLAEAPTTplAQAPGKGMDDRLF 245
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALLERK--PADDLPS--LKhvLLVGEDVEEG--PGTLDFNALMEQASDE--FDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVHSryyriAAFGHH---SYSM--RAADVlYDCL---------------PLYHSAGNimgvgqcv 305
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHN-----AMLQHYqtgKYVLdlHEDDV-YWCTadpgwvtgtsygifaPWLNGATN-------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 306 iygltVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVrDVEQRH-----RVRLAVGNGLRP-AIWeeFTQR-F 378
Cdd:PRK04319 276 -----VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGD-DLVKKYdlsslRHILSVGEPLNPeVVR--WGMKvF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 379 GVPqIGEFYGATECNCS-IAN---MDGKVGSCGfnsRILTHVYpIRLVKVNEDTMEPLRDSEgLCIpcQPGEPGLLVGQI 454
Cdd:PRK04319 348 GLP-IHDNWWMTETGGImIANypaMDIKPGSMG---KPLPGIE-AAIVDDQGNELPPNRMGN-LAI--KKGWPSMMRGIW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 455 NQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEavlSRLLGQ 534
Cdd:PRK04319 420 NNPE---KYESY--------------FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE---SKLMEH 477
|
....*...
gi 1268743554 535 TDVAVYGV 542
Cdd:PRK04319 478 PAVAEAGV 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
75-312 |
1.24e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.87 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 75 GDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 154
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 155 aaLLNVN--LRREPLAFCLGTSAAKALIYGG--------EMAAAVA-EVSEQLGKSL-------LKF-CSgdLGPESIlP 215
Cdd:PRK08315 95 --LVTINpaYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYELApELATCEPGQLqsarlpeLRRvIF--LGDEKH-P 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 216 DTQLLDPMLAEAPTTPLAQ--APGKGM--DDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHH-SYSMR--AADVLYDC 288
Cdd:PRK08315 170 GMLNFDELLALGRAVDDAElaARQATLdpDDPINIQYTSGTTGFPKGATLTH---RNILNNGYFiGEAMKltEEDRLCIP 246
|
250 260
....*....|....*....|....
gi 1268743554 289 LPLYHSAGNIMGVGQCVIYGLTVV 312
Cdd:PRK08315 247 VPLYHCFGMVLGNLACVTHGATMV 270
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
86-530 |
1.82e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 89.25 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGIcwTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRR 164
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAI--SYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 165 EPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDL---GPESILPD---TQLLDPMLAEAPTTPLAQA-- 235
Cdd:PRK08314 98 EELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYlpaEPEIAVPAwlrAEPPLQALAPGGVVAWKEAla 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 236 ----PGK---GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 308
Cdd:PRK08314 178 aglaPPPhtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 309 LTVVLrkkfsASRfWD-----DCV-KYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLA-VGNG---LRPAIWEEFTQRF 378
Cdd:PRK08314 258 ATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASP--GLAERDLSSLRyIGGGgaaMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 379 GVPQIgEFYGATECNC-SIAN-MDGKVGSC------GFNSRIlthvypirlvkVNEDTMEPLrdseglcipcQPGEpgll 450
Cdd:PRK08314 330 GLDYV-EGYGLTETMAqTHSNpPDRPKLQClgiptfGVDARV-----------IDPETLEEL----------PPGE---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 451 VGQINQQDPlRRFDGYVSDSATNKKI-----AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PRK08314 384 VGEIVVHGP-QVFKGYWNRPEATAEAfieidGKRFFRTGDLGR-------MDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
....*
gi 1268743554 526 AVLSR 530
Cdd:PRK08314 456 NLLYK 460
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
75-582 |
2.00e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 85.82 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 75 GDTIPCIFQAVARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 154
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 155 AALLNVNLRREPLAFCLGTSAAKALIYGGEmaaaVAEVSEQLgksllkfcSGDLGPESI--------LPDTQLL------ 220
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIVWDK----VAPTVERL--------RRTTPLETIvsvnmiaaMPLLQRLalrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 221 -------DPMLAEAP-TTPLAQ-----APGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHH--S 276
Cdd:PRK05605 177 palrkarAALTGPAPgTVPWETlvdaaIGGDGSdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 277 YSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEIcrYllrQPVRDVEQRH 356
Cdd:PRK05605 257 GLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL--Y---EKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 357 RVRLavgNGLRPAI-------------WEEFTQRFGVpqigEFYGATECN----CSIANMDGKVGSCG--FNSRIlthvy 417
Cdd:PRK05605 332 GVDL---SGVRNAFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMSDDRRPGYVGvpFPDTE----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 418 pIRLVkvneDTMEPLRDseglcIPcqPGEPG-LLVgqinqQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVM 496
Cdd:PRK05605 400 -VRIV----DPEDPDET-----MP--DGEEGeLLV-----RGP-QVFKGYWNRPEETAKSFL------DGWFRTGDVVVM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 497 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQK 574
Cdd:PRK05605 456 EEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVAavVLEPGAALDPEGLRAYCRE 533
|
....*...
gi 1268743554 575 VLASYARP 582
Cdd:PRK05605 534 HLTRYKVP 541
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-557 |
2.87e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 85.42 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRqPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:PLN02246 29 CFERLSEF-SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIyggEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQapgkgm 240
Cdd:PLN02246 108 FYTPAEIAKQAKASGAKLII---TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISP------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAF--GHH-SYSMRAADVLYDCLPLYH--SAGNIMGVGQCViyGLTVVLR 314
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHkGLVTSVAQQvdGENpNLYFHSDDVILCVLPMFHiySLNSVLLCGLRV--GAAILIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLaVGNGLRPAIWE-EFTQRFGVPQ--IGEFYGATE 391
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPLGKElEDAFRAKLPNavLGQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIAnM---------DGKVGSCGfnsrilTHVYPIRLVKVNEDTMEPLRDSeglcipcQPGEPGLLVGQInqqdplrr 462
Cdd:PLN02246 336 AGPVLA-MclafakepfPVKSGSCG------TVVRNAELKIVDPETGASLPRN-------QPGEICIRGPQI-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 463 FDGYVSD-SATNKKI-----AHSvfrkGDSAYLSGDvlvmDElgyMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 536
Cdd:PLN02246 394 MKGYLNDpEATANTIdkdgwLHT----GDIGYIDDD----DE---LFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD 462
|
490 500
....*....|....*....|.
gi 1268743554 537 VAVygvaVPGVEGKAGMAAIA 557
Cdd:PLN02246 463 AAV----VPMKDEVAGEVPVA 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
107-604 |
3.77e-17 |
|
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: 84.74 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 107 AQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLakaGVVAALLNVNLRREPLAF---CLGTSAAKALIYGG 183
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIAD---GVYIYLINSILTVFAAAAawkCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EMAAAVAEVseqlgKSLLKFCSGDLGPESILPDTQLlDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGTTGLPKA---- 258
Cdd:cd05929 79 AEACAIIEI-----KAAALVCGLFTGGGALDGLEDY-EAAEGGSPETPIEdEAAGWKM------LYSGGTTGRPKGikrg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 259 --AIVVHSRYYRIAAFGhhsYSMRAADVLYDCLPLYHSAGNI--MGVgqcVIYGLTVVLRKKFSASRFWDDCVKYNCTVV 334
Cdd:cd05929 147 lpGGPPDNDTLMAAALG---FGPGADSVYLSPAPLYHAAPFRwsMTA---LFMGGTLVLMEKFDPEEFLRLIERYRVTFA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 335 QYIGEICRYLLRQP--VRDVEQRHRVRLAVGNGLRPAIW-EEFTQRFGVPQIGEFYGATECNcsianmdgkvGSCGFNS- 410
Cdd:cd05929 221 QFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAAPCPPWvKEQWIDWGGPIIWEYYGGTEGQ----------GLTIINGe 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 411 RILTHvyPIRLVKVNEDTMEpLRDSEGLciPCQPGEPGLLVgqinqqdplrrFDGYVSDSATNK--KIAHSVFRKGDSAY 488
Cdd:cd05929 291 EWLTH--PGSVGRAVLGKVH-ILDEDGN--EVPPGEIGEVY-----------FANGPGFEYTNDpeKTAAARNEGGWSTL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 489 lsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIaDPHSQLDPNS 567
Cdd:cd05929 355 --GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QPAPGADAGT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1268743554 568 MYQE-----LQKVLASYARP---IFLRLLPQVDTTgtfKIQKTRL 604
Cdd:cd05929 430 ALAEeliafLRDRLSRYKCPrsiEFVAELPRDDTG---KLYRRLL 471
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
76-542 |
4.76e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 84.89 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 76 DTIPCIFQAVARrqPERLALVDASSGICWTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 154
Cdd:PLN02574 41 DAVSFIFSHHNH--NGDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 155 AALLNvnlrrePLAfCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdLG-PESILPDTQLLDPMLAEAPT---- 229
Cdd:PLN02574 119 VTTMN------PSS-SLGEIKKRVVDCSVGLAFTSPENVEKLSP---------LGvPVIGVPENYDFDSKRIEFPKfyel 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 230 ----TPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYyrIAA------FGHHSYSMRAADVLY-DCLPLYHSAGNI 298
Cdd:PLN02574 183 ikedFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNL--IAMvelfvrFEASQYEYPGSDNVYlAALPMFHIYGLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 299 MGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPA---IWEEFT 375
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLsgkFIQDFV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 376 QRFGVPQIGEFYGATEcncSIAnmdgkVGSCGFNSRILTHVYPIRLVKVNedtMEP--LRDSEGLCIPcqPGE------- 446
Cdd:PLN02574 341 QTLPHVDFIQGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPN---MQAkvVDWSTGCLLP--PGNcgelwiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 447 -PGLLVGQINqqdplrrfDGYVSDSATNKkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PLN02574 408 gPGVMKGYLN--------NPKATQSTIDK----------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
|
490
....*....|....*..
gi 1268743554 526 AVLSRLLGQTDVAVYGV 542
Cdd:PLN02574 470 AVLISHPEIIDAAVTAV 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
90-545 |
5.05e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 84.27 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASsgICWTFAQldTYSNAV--ANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 167
Cdd:cd12118 18 PDRTSIVYGD--RRYTWRQ--TYDRCRrlASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIyggemaaavaeVSEQL-GKSLLKfcSGDLGPESILPDTQlldpmlaeapttplaqapgkgmDDRLFY 246
Cdd:cd12118 94 AFILRHSEAKVLF-----------VDREFeYEDLLA--EGDPDFEWIPPADE----------------------WDPIAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 247 IYTSGTTGLPKAaIVVHSRYYRIAAFGH-HSYSMRAADVLYDCLPLYHSAG--NIMGVGqcVIYGLTVVLRKkFSASRFW 323
Cdd:cd12118 139 NYTSGTTGRPKG-VVYHHRGAYLNALANiLEWEMKQHPVYLWTLPMFHCNGwcFPWTVA--AVGGTNVCLRK-VDAKAIY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 324 DDCVKYNCT-------VVQYIGEiCRYLLRQPVRdveqrHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsi 396
Cdd:cd12118 215 DLIEKHKVThfcgaptVLNMLAN-APPSDARPLP-----HRVHVMTAGAPPPAAVLAKMEELGF-DVTHVYGLTETY--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 397 anmdGKVGSC---------------GFNSRI-LTHVYPIRLVKVNEDTMEPL-RDSEGLcipcqpGEPgLLVGQINQQdp 459
Cdd:cd12118 285 ----GPATVCawkpewdelpteeraRLKARQgVRYVGLEEVDVLDPETMKPVpRDGKTI------GEI-VFRGNIVMK-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 460 lrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 539
Cdd:cd12118 352 -----GYLKNPEATAE----AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
....*.
gi 1268743554 540 ygVAVP 545
Cdd:cd12118 421 --VARP 424
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
71-607 |
2.17e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.77 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 71 HRRAGDTIPC--IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGL 148
Cdd:PRK06710 17 STISYDIQPLhkYVEQMASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 149 AKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG---------KSLLKFCSGDLGPESILPDTQL 219
Cdd:PRK06710 95 LLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKiehvivtriADFLPFPKNLLYPFVQKKQSNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 220 LdPMLAEAPTTPLAQAPGKGMD-----------DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYS-MRAADVLY 286
Cdd:PRK06710 175 V-VKVSESETIHLWNSVEKEVNtgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 287 DCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNG 365
Cdd:PRK06710 254 GVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 366 LRPAIWEEFTQRFGVPQIGEFYGATEcncsianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPG 445
Cdd:PRK06710 334 PLPVEVQEKFETVTGGKLVEGYGLTE------------------SSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 446 E---PGLlVGQINQQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 522
Cdd:PRK06710 396 EalpPGE-IGEIVVKGP-QIMKGYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 523 EVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 602
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
....*
gi 1268743554 603 RLQRE 607
Cdd:PRK06710 548 VLIEE 552
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
90-604 |
2.60e-16 |
|
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: 81.93 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALIyggemaaavaevseqlgksllkFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPgkGMDDRLFYIYT 249
Cdd:cd12114 79 ILADAGARLVL----------------------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 250 SGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRAADVLYDCLPLYH--SAGNIMGVgqcVIYGLTVVL----RKKFSASrf 322
Cdd:cd12114 135 SGSTGTPKGVMISHRAALNtILDINRR-FAVGPDDRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 323 WDDCV-KYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLA------VGNGLRPAIWeeftQRFGVPQIGEFYGATEcncs 395
Cdd:cd12114 209 WAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVllsgdwIPLDLPARLR----ALAPDARLISLGGATE---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 ianmdgkvGScgfnsrILTHVYPIRlvKVNEDTME-----PLR-------DSEGLciPCQPGEPG-LLVGQIN-----QQ 457
Cdd:cd12114 281 --------AS------IWSIYHPID--EVPPDWRSipygrPLAnqryrvlDPRGR--DCPDWVPGeLWIGGRGvalgyLG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 458 DPLRRFDGYVSDSAtnkkiAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 537
Cdd:cd12114 343 DPELTAARFVTHPD-----GERLYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 538 AVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd12114 411 VVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
241-545 |
1.04e-15 |
|
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: 80.07 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFghhsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLR-- 314
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHknllANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpn 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 ----KKFSasRFWDDcvkYNCTVVQYIGEICRYLLR--QPvrdvEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEF 386
Cdd:cd05909 223 pldyKKIP--ELIYD---KKATILLGTPTFLRGYARaaHP----EDFSSLRLVVagAEKLKDTLRQEFQEKFGIR-ILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 387 YGATEC----NCSIANMDGKVGSCGfnsRILTHVyPIRLVKVnedtmeplrdsEGLCiPCQPGEPGLLVGQINQqdplrR 462
Cdd:cd05909 293 YGTTECspviSVNTPQSPNKEGTVG---RPLPGM-EVKIVSV-----------ETHE-EVPIGEGGLLLVRGPN-----V 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 463 FDGYVSDSatnkkiAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtDVAVYGV 542
Cdd:cd05909 352 MLGYLNEP------ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVV 424
|
...
gi 1268743554 543 AVP 545
Cdd:cd05909 425 SVP 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-613 |
1.45e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 42 RFLRIVCKTARRDLFGLSVLIRV--RLELRRHRRAGDTIPC------IFQAVARRQPERLALVdaSSGICWTFAQLDTYS 113
Cdd:PRK12316 1961 HLLEQMAEDAQAALGELALLDAGerQRILADWDRTPEAYPRgpgvhqRIAEQAARAPEAIAVV--FGDQHLSYAELDSRA 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 114 NAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAavaevs 193
Cdd:PRK12316 2039 NRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE------ 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 194 eqlgksllkfcsgDLGPESILPDTQLLDPM-LAEAPTT-PLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVHSRYY-RIA 270
Cdd:PRK12316 2113 -------------RLPLPAGVARLPLDRDAeWADYPDTaPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVaHCQ 2176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 271 AFGhHSYSMRAADVLYDCLPLYHSaGNIMGVGQCVIYGLTVVLR--KKFSASRFWDDCVKYNCTVVQYIGEicrYLlrQP 348
Cdd:PRK12316 2177 AAG-ERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPV---YL--QQ 2249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 349 VRDVEQRHRVRLAV------GNGLRPAIWEEFTQRFGVPQIGEFYGATEcncsiANMDGKVGSCGFNSRILTHVYPI--- 419
Cdd:PRK12316 2250 LAEHAERDGRPPAVrvycfgGEAVPAASLRLAWEALRPVYLFNGYGPTE-----AVVTPLLWKCRPQDPCGAAYVPIgra 2324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 420 ---RLVKVNEDTMEPLrdSEGLCIPCQPGEPGLLVGQINQqdPLRRFDGYVSDSATNkkiahsvfrKGDSAYLSGDVLVM 496
Cdd:PRK12316 2325 lgnRRAYILDADLNLL--APGMAGELYLGGEGLARGYLNR--PGLTAERFVPDPFSA---------SGERLYRTGDLARY 2391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 497 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMA-AIADPHSQLDPNSMYQELQKV 575
Cdd:PRK12316 2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAyVVPDDAAEDLLAELRAWLAAR 2469
|
570 580 590
....*....|....*....|....*....|....*...
gi 1268743554 576 LASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQ 613
Cdd:PRK12316 2470 LPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
69-604 |
2.03e-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: 79.29 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 69 RRHRRAG----DTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 144
Cdd:cd05920 4 RRYRAAGywqdEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 145 WLGLAKAGVVAAL-LNVNLRREPLAFClGTSAAKALIyggemaaavaeVSEQLGksllKFCSGDLGPEsilpdtqlldpM 223
Cdd:cd05920 82 FFALLRLGAVPVLaLPSHRRSELSAFC-AHAEAVAYI-----------VPDRHA----GFDHRALARE-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 224 LAEAPTTPLAQAPGkgmddrlfyiytsGTTGLPKAAIVVHSRYyriaafghhSYSMRAA--------DVLYDC-LPLYH- 293
Cdd:cd05920 135 AESIPEVALFLLSG-------------GTTGTPKLIPRTHNDY---------AYNVRASaevcgldqDTVYLAvLPAAHn 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 294 ---SAGNIMGVGQCviyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLL--RQPVRDVEQRHRVRLAVGNGLRP 368
Cdd:cd05920 193 fplACPGVLGTLLA---GGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLdaAASRRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 369 AIWEEFTQRFGvPQIGEFYGATE---CNCSIANMDGKVgsCGFNSRILTHVYPIRLVkvnedtmeplrDSEGLCIPcqPG 445
Cdd:cd05920 270 ALARRVPPVLG-CTLQQVFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV-----------DEEGNPVP--PG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 446 EPGLLvgqinqqdpLRR----FDGYVSDSATNKKiahsVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 521
Cdd:cd05920 334 EEGEL---------LTRgpytIRGYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 522 TEVEAVLSRLLGQTDVAVygVAVPG-VEGKAGMAAIADPHSQLDPNSMYQEL-QKVLASYARPIFLRLLPQVDTTGTFKI 599
Cdd:cd05920 400 EEVENLLLRHPAVHDAAV--VAMPDeLLGERSCAFVVLRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
....*
gi 1268743554 600 QKTRL 604
Cdd:cd05920 478 DKKAL 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
247-601 |
4.44e-15 |
|
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: 76.77 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 247 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDC 326
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 327 VKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNGLRPAIW-EEFTQRFGVPQIGEFYGATECNCSianmdgkvg 404
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 405 scgfnsrilthvypirlvkvnedTM-EPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRR----FDGYVSD-SATNKKIah 478
Cdd:cd17638 157 -----------------------TMcRPGDDAETVATTCGRACPGFEVRIADDGEVLVRgynvMQGYLDDpEATAEAI-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 479 svfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMA-AIA 557
Cdd:cd17638 212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGKAfVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1268743554 558 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17638 287 RPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
81-604 |
4.51e-15 |
|
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: 77.98 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:cd17645 3 LFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgKGM 240
Cdd:cd17645 81 DYPGERIAYMLADSSAKILL---------------------------------------------------------TNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD--VLYDCLPLYHSAGNIMgvgQCVIYGLTVVL---RK 315
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALHVvpsER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 316 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrdvEQRHRVRLAVGNGLRPAIWEEFtqrfgvpQIGEFYGATECN-- 393
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFMQLD----NQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTENTvv 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 394 CSIANMDGKVGSCGFNSRILThvypIRLVKVNED-TMEPLRDSEGLCIPcqpGEpGLLVGQINQQDplrrfdgyvsdsAT 472
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDN----TRVYILDEAlQLQPIGVAGELCIA---GE-GLARGYLNRPE------------LT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 473 NKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAG 552
Cdd:cd17645 310 AEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDADGRKY 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 553 MAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17645 388 LVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
104-541 |
4.73e-15 |
|
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: 78.02 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 183
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlAEAPttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05907 83 -----------------------------------------VEDP------------DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 264 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV-----------LRKK-----FSASRFWDdcv 327
Cdd:cd05907 110 RNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddLSEVrptvfLAVPRVWE--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 328 K-YNCTVVQYIGEICRYLLRQPVRDveqrhRVRLAVGNG--LRPAIwEEFTQRFGVPqIGEFYGATECnCSIANM----D 400
Cdd:cd05907 187 KvYAAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGIP-VYEGYGLTET-SAVVTLnppgD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 401 GKVGSCGfnsriltHVYPIRLVKVNEDtmeplrdseglcipcqpGEpgLLV-GQINqqdplrrFDGYVSDSATNKKIAhs 479
Cdd:cd05907 259 NRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV-------MLGYYKNPEATAEAL-- 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 480 vfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEAVL--SRLLGQtdVAVYG 541
Cdd:cd05907 304 ---DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLISQ--AVVIG 363
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
90-604 |
9.07e-15 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 77.12 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd17650 1 PDAIAVSDATRQL--TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALiyggemaaavaevseqlgksllkfcsgdlgpesilpdtqLLDPmlaeapttplaqapgkgmDDRLFYIYT 249
Cdd:cd17650 79 MLEDSGAKLL---------------------------------------LTQP------------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 250 SGTTGLPKAAIVVHS----------RYYRIAAFGHHSYSMR--AADVLYDCLPLYHSAGnimgvGQCVIygltVVLRKKF 317
Cdd:cd17650 102 SGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRLLQMAsfSFDVFAGDFARSLLNG-----GTLVI----CPDEVKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 318 SASRFWDDCVKYNCTVVQYIGEICRyllrqPVRDVEQRHRVR------LAVGNGLRPAIW-EEFTQRFGVP-QIGEFYGA 389
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIR-----PVMAYVYRNGLDlsamrlLIVGSDGCKAQDfKTLAARFGQGmRIINSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 390 TEcncsiANMDGKVGSCGFNSRILTHVYPI-------RLVKVNE-DTMEPLRDSEGLCIpcqpGEPGLLVGQINQQDplr 461
Cdd:cd17650 248 TE-----ATIDSTYYEEGRDPLGDSANVPIgrplpntAMYVLDErLQPQPVGVAGELYI----GGAGVARGYLNRPE--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 462 rfdgyvsdsATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVyg 541
Cdd:cd17650 316 ---------LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV-- 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 542 VAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17650 385 AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
86-313 |
2.89e-14 |
|
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: 75.74 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGfAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL--- 158
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 159 --NVNLRRepLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAP 236
Cdd:cd05931 82 tpGRHAER--LAAILADAGPRVVLTTAAALAAVRAFAASRPA---------------AGTPRLLVVDLLPDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 237 GKGMDDRLFYIYTSGTTGLPKAAIVVHsryyriAAFGH------HSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLT 310
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
...
gi 1268743554 311 VVL 313
Cdd:cd05931 219 SVL 221
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-542 |
5.43e-14 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 74.87 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALIYGGEMAAAVAEVseqlgKSLLKFCSG--------DLGPESILPD--TQLLDPMLAEAPTTPlaqaPGKG 239
Cdd:cd17642 111 SLNISKPTIVFCSKKGLQKVLNV-----QKKLKIIKTiiildskeDYKGYQCLYTfiTQNLPPGFNEYDFKP----PSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 240 MDDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRAADVLYD-----CLPLYHSAGNIMGVGQcVIYGLTVVL 313
Cdd:cd17642 182 RDEQVALImNSSGSTGLPKGVQLTHKNI--VARFSHARDPIFGNQIIPDtailtVIPFHHGFGMFTTLGY-LICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 314 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD-VEQRHRVRLAVGNG-LRPAIWEEFTQRFGVPQIGEFYGATE 391
Cdd:cd17642 259 MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSI---ANMDGKVGSCGfnsriltHVYPIRLVKVnedtMEPlrDSEGLCIPCQPGE-----PGLLVGQINQQDplrrf 463
Cdd:cd17642 339 TTSAIlitPEGDDKPGAVG-------KVVPFFYAKV----VDL--DTGKTLGPNERGElcvkgPMIMKGYVNNPE----- 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 464 dgyvsdsATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:cd17642 401 -------ATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-604 |
5.89e-14 |
|
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: 74.65 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 167
Cdd:cd17643 1 PEAVAVVDEDRRL--TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAypVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapTTPlaqapgkgmDDRLFYI 247
Cdd:cd17643 77 AFILADSGPSLLL------------------------------------------------TDP---------DDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 248 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYdclpLYHSAG------NIMGVgqcVIYGLTVVLRKKF---S 318
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 319 ASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGV--PQIGEFYGATEcnc 394
Cdd:cd17643 173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLdrPQLVNMYGITE--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 395 sianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEP-----------LRDSEGLCIPcqPGEPGLLV--------GQIN 455
Cdd:cd17643 250 ---------------TTVHVTFRPLDAADLPAAAASPigrplpglrvyVLDADGRPVP--PGVVGELYvsgagvarGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 456 QQD-PLRRFdgyVSDSATNkkiahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 534
Cdd:cd17643 313 RPElTAERF---VANPFGG---------PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSV 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 535 TDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17643 381 RDAAV--IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
74-612 |
6.48e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 74 AGDTIPCIFQAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEF-VGLwLGLAKAG 152
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 153 VVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESILPDTQLLDPMLAEAPTTPL 232
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE---------------GVSAIALDSLHLDSWPSQAPGLHL 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 233 AqapgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSagniMGVGQC---VIYG 308
Cdd:PRK05691 1271 H-------GDNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD----VSVWECfwpLITG 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 309 LTVVLR---KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQI 383
Cdd:PRK05691 1340 CRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP--LAAACTSLRRLFsgGEALPAELRNRVLQRLPQVQL 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 GEFYGATEC-------NCSIAnmDGKVGSCGfnsRILTHVypirLVKVNEDTMEPLrdseglcipcQPGEPG-LLVGQIN 455
Cdd:PRK05691 1418 HNRYGPTETainvthwQCQAE--DGERSPIG---RPLGNV----LCRVLDAELNLL----------PPGVAGeLCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 456 qqdpLRRfdGYVSDSATNKK--IAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAvlsRLLG 533
Cdd:PRK05691 1479 ----LAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQA---RLLA 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 534 QTDVAVYGVAVPgvEGKAGMAAI----ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL----- 604
Cdd:PRK05691 1550 QPGVAQAAVLVR--EGAAGAQLVgyytGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepvw 1627
|
....*....
gi 1268743554 605 -QREGFDPR 612
Cdd:PRK05691 1628 qQREHVEPR 1636
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-528 |
2.34e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 72.60 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvnlrreplafclgtsaakaliygge 184
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 maaavaevseqlgksllkfcsgdlgpesILPDTQLLDP-----MLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKaa 259
Cdd:cd05974 52 ----------------------------VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 260 IVVHSryYRIAAFGHHS----YSMRAADVLYD-CLPLY--HSAGNIMG---VGQCVIygltVVLRKKFSASRFWDDCVKY 329
Cdd:cd05974 102 LVEHT--HRSYPVGHLStmywIGLKPGDVHWNiSSPGWakHAWSCFFApwnAGATVF----LFNYARFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 330 NCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANMDGKVGSCGFN 409
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVKAGSM 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 410 SRILTHvYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSAtnkKIAHSVfrkGDSAYL 489
Cdd:cd05974 255 GRPLPG-YRVALL-----------DPDGA--PATEGEVALDLGDTR---PVGLMKGYAGDPD---KTAHAM---RGGYYR 311
|
410 420 430
....*....|....*....|....*....|....*....
gi 1268743554 490 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 528
Cdd:cd05974 312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
69-545 |
2.37e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 69 RRHRRAGDTIPCIFQAVARRQPERLALVDaSSGICWTFAQLDTYSNAVANLFRQLgFAPGDVVAVFLegrPEFVG---LW 145
Cdd:PRK08633 608 KSRKEALPPLAEAWIDTAKRNWSRLAVAD-STGGELSYGKALTGALALARLLKRE-LKDEENVGILL---PPSVAgalAN 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 146 LGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIyggemaaavaeVSEQ-LGKSLLKFCSGDLGP-------ESILPDT 217
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVI-----------TSRKfLEKLKNKGFDLELPEnvkviylEDLKAKI 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 218 QLLDPMLAE-----APTTPLAQA--PGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAA--------FGhhsysMRAA 282
Cdd:PRK08633 752 SKVDKLTALlaarlLPARLLKRLygPTFKPDDTATIIFSSGSEGEPKGVMLSH---HNILSnieqisdvFN-----LRND 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 283 DVLYDCLPLYHSagnimgvgqcviYGLTV----VLRKKFSASRFWDD---------CVKYNCTVVQYIGEICRYLLRQPV 349
Cdd:PRK08633 824 DVILSSLPFFHS------------FGLTVtlwlPLLEGIKVVYHPDPtdalgiaklVAKHRATILLGTPTFLRLYLRNKK 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 350 RDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsrilt 414
Cdd:PRK08633 892 LHPLMFASLRLVVAGAekLKPEVADAFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG------- 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 415 HVYPIRLVK-VNEDTMEPLrdseglcipcQPGEPGL-LVGQINqqdplrRFDGYVSDSA-TNKKIAHSvfrKGDSAYLSG 491
Cdd:PRK08633 964 MPLPGVAVRiVDPETFEEL----------PPGEDGLiLIGGPQ------VMKGYLGDPEkTAEVIKDI---DGIGWYVTG 1024
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 492 DVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 545
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
241-606 |
2.61e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 71.74 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL------R 314
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 315 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV-RDVEQrhrVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATE 391
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVnADISS---LRFAMSGAapLPVELRARFEDATGLP-VVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CNCSIA----NMDGKVGSCGFNsrilthvYPIRLVKVNEDtmeplrDSEGLCI-PCQPGEpgllVGQINQQDPlRRFDGY 466
Cdd:cd05944 158 ATCLVAvnppDGPKRPGSVGLR-------LPYARVRIKVL------DGVGRLLrDCAPDE----VGEICVAGP-GVFGGY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 V-SDSATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRllgQTDVAVYGvAVP 545
Cdd:cd05944 220 LyTEGNKNAFVADGWLNTGDLGRL-------DADGYLFITGRAKDLIIRGGHNIDPALIEEALLR---HPAVAFAG-AVG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 546 GVEGKAGMAAIAdpHSQLDPNSMYQELQkvLASYAR---------PIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05944 289 QPDAHAGELPVA--YVQLKPGAVVEEEE--LLAWARdhvperaavPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
86-605 |
2.62e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 72.50 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPgDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK07638 11 ASLQPNKIAIKENDRVL--TYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFCLGTSAAKALIyggemaaavaevseqlgksLLKFCSGDLGPEsilpDTQLLD-----PMLAEAPTTPlaqAPGKGM 240
Cdd:PRK07638 88 ELKERLAISNADMIV-------------------TERYKLNDLPDE----EGRVIEidewkRMIEKYLPTY---APIENV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAF--GHHSYSMRAADVLYDCLPLYHSAgNIMGVGQCVIYGLTVVLRKKF 317
Cdd:PRK07638 142 QNAPFYMgFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 318 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVrlaVGNGlrpAIW-----EEFTQRFGVPQIGEFYGATEC 392
Cdd:PRK07638 219 IPNQVLDKLETENISVMYTVPTMLESLYKEN-RVIENKMKI---ISSG---AKWeaeakEKIKNIFPYAKLYEFYGASEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 393 NCSIANMDG----KVGSCGfnsrilTHVYPIRLVKVNEDTMEplrdseglcipCQPGEpgllVGQINQQDPLRrFDGYVS 468
Cdd:PRK07638 292 SFVTALVDEeserRPNSVG------RPFHNVQVRICNEAGEE-----------VQKGE----IGTVYVKSPQF-FMGYII 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 469 DSATNKKIAhsvfrkgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgv 547
Cdd:PRK07638 350 GGVLARELN-------ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS-- 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 548 egKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK07638 421 --YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
82-292 |
2.65e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.62 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 82 FQAVARRQPERLALV-----DASSGICW---TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 153
Cdd:PRK09274 12 LPRAAQERPDQLAVAvpggrGADGKLAYdelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 154 VAALLNVNLRREPLAFCLGTSAAKALIygGEMAAAVAEVSEQLGKSLLKF---CSGDLGPESILPDTQLLDPMLAEAPTT 230
Cdd:PRK09274 92 VPVLVDPGMGIKNLKQCLAEAQPDAFI--GIPKAHLARRLFGWGKPSVRRlvtVGGRLLWGGTTLATLLRDGAAAPFPMA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 231 PLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRAADVLYDCLPLY 292
Cdd:PRK09274 170 DLAP------DDMAAILFTSGSTGTPKGVVYTHGMFEAqIEALRED-YGIEPGEIDLPTFPLF 225
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
122-542 |
2.82e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.91 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 122 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtSAAKALiyggEMAAAVAEVSEQLGKS-- 199
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFE--------EAKSAM----LLVRPVMLVTDETCSSwy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 200 ---------------LLKFCSGDLGPE--SILPDTQLLDPMLAEaPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVV 262
Cdd:PLN02860 119 eelqndrlpslmwqvFLESPSSSVFIFlnSFLTTEMLKQRALGT-TELDYAWAP----DDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 263 HSRYY-----RIAAFGHHSysmraADVLYDCLPLYH-----SAGNIMGVGQCviygltVVLRKKFSASRFWD----DCVK 328
Cdd:PLN02860 194 HSALIvqslaKIAIVGYGE-----DDVYLHTAPLCHigglsSALAMLMVGAC------HVLLPKFDAKAALQaikqHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 329 YNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGF 408
Cdd:PLN02860 263 SMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 409 NSRILTHVYPIRLVKVNEdtmeplrdSEGLCI----P------CQPGEPGllVGQINQQDP---LRRFDGYVSDSATnkk 475
Cdd:PLN02860 343 PKQTLQTVNQTKSSSVHQ--------PQGVCVgkpaPhvelkiGLDESSR--VGRILTRGPhvmLGYWGQNSETASV--- 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 476 iahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:PLN02860 410 ------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
90-607 |
3.29e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.67 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGICWtfaqLDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 167
Cdd:PRK08162 32 PDRPAVIHGDRRRTW----AETYARCrrLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPEsiLPDTQLL-----DPMLAEAPTTPLAQAPgkgmDD 242
Cdd:PRK08162 108 AFMLRHGEAKVLIVDTEFAEVAREALALLPGPKP-LVIDVDDPE--YPGGRFIgaldyEAFLASGDPDFAWTLP----AD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 243 RLFYI---YTSGTTGLPKaAIVVHSRYYRIAAFGHH-SYSMRAADVLYDCLPLYHSagNimgvGQC------VIYGLTVV 312
Cdd:PRK08162 181 EWDAIalnYTSGTTGNPK-GVVYHHRGAYLNALSNIlAWGMPKHPVYLWTLPMFHC--N----GWCfpwtvaARAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 313 LRkKFSASRFWDDCVKYNctVVQYIGE-ICRYLL-------RQPVrdveqRHRVRLAVGNGLRPAIWEEFTQRFGVpQIG 384
Cdd:PRK08162 254 LR-KVDPKLIFDLIREHG--VTHYCGApIVLSALinapaewRAGI-----DHPVHAMVAGAAPPAAVIAKMEEIGF-DLT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 385 EFYGATECNcsianmdGKVGSC---------------GFNSRilTHV-YPIR--LVKVNEDTMEPL-RDSEGLcipcqpG 445
Cdd:PRK08162 325 HVYGLTETY-------GPATVCawqpewdalplderaQLKAR--QGVrYPLQegVTVLDPDTMQPVpADGETI------G 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 446 E---PGLLVgqinqqdplrrFDGYVSdsatNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 522
Cdd:PRK08162 390 EimfRGNIV-----------MKGYLK----NPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 523 EVEAVLSRLLGQTDVAVygVAVPG----------VEGKAGMAAIADphsqldpnsmyqEL----QKVLASYARP--IFLR 586
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAV--VAKPDpkwgevpcafVELKDGASATEE------------EIiahcREHLAGFKVPkaVVFG 518
|
570 580
....*....|....*....|.
gi 1268743554 587 LLPQvdtTGTFKIQKTRLQRE 607
Cdd:PRK08162 519 ELPK---TSTGKIQKFVLREQ 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
242-606 |
9.13e-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: 69.67 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAaiVVHSRYYRIAAF--GHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSA 319
Cdd:cd17630 1 RLATVILTSGSTGTPKA--VVHTAANLLASAagLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 320 SRfwDDCVKYNCTVVQYIGEICRYLLRQPVrDVEQRHRVR-LAVGNGlrpAIWEEFTQRF---GVPqIGEFYGATEcncs 395
Cdd:cd17630 78 LA--EDLAPPGVTHVSLVPTQLQRLLDSGQ-GPAALKSLRaVLLGGA---PIPPELLERAadrGIP-LYTTYGMTE---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 ianMDGKVGSCGFNSRILTHVYPI---RLVKVNEDTMeplrdseglcipCQPGEPGLLVGQINQQDPLRRFDGyvsdsat 472
Cdd:cd17630 147 ---TASQVATKRPDGFGRGGVGVLlpgRELRIVEDGE------------IWVGGASLAMGYLRGQLVPEFNED------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 473 nkkiahSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKAG 552
Cdd:cd17630 205 ------GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELG 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 553 MAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd17630 268 QRPVAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-614 |
1.24e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 61 LIRVRLELRRHRRAGDTIPCIFQAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE 140
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 141 FVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAavaevseqlgksLLKFCSGdlgpESILPDTQLL 220
Cdd:PRK12467 575 MVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA------------QLPVPAG----LRSLCLDEPA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 221 DPMLAEAP-TTPLAQAPgkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNI 298
Cdd:PRK12467 639 DLLCGYSGhNPEVALDP-----DNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 299 MGVGQcVIYGLTVVLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAI---WE 372
Cdd:PRK12467 714 ELFGA-LASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLlarVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 373 EFTqrfgvPQIGEF--YGATEcncsiANMDGKVGSCGFNSRILTHVyPIRlvkvnedtmEPLRDSeGLCI------PCQP 444
Cdd:PRK12467 793 ALG-----PGARLInhYGPTE-----TTVGVSTYELSDEERDFGNV-PIG---------QPLANL-GLYIldhylnPVPV 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 445 GEPG-LLVGqinqQDPLRRfdGYVSDSA-TNKKIAHSVF-RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 521
Cdd:PRK12467 852 GVVGeLYIG----GAGLAR--GYHRRPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIEL 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 522 TEVEAvlsRLLGQTDV--AVYgVAVPGVEGK--------AGMAAIADPHSQLDpnSMYQELQKVLASYARPIFLRLLPQV 591
Cdd:PRK12467 926 GEIEA---RLLAQPGVreAVV-LAQPGDAGLqlvaylvpAAVADGAEHQATRD--ELKAQLRQVLPDYMVPAHLLLLDSL 999
|
570 580
....*....|....*....|....
gi 1268743554 592 DTTGTFKIQKTRL-QREGFDPRQT 614
Cdd:PRK12467 1000 PLTPNGKLDRKALpKPDASAVQAT 1023
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
47-604 |
2.80e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 69.64 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 47 VCKTARRDLFGLSVLI----RVRLELRRHRRAGDTIPCIFQAV-ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 121
Cdd:PRK13383 1 VAPTAARALVRSGLLNppspRAVLRLLREASRGGTNPYTLLAVtAARWPGRTAIIDDDGAL--SYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 122 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksll 201
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 202 kfcsgdlgpesilpdtqLLDPMLA---EAPTTPLAQAPGKgmddrlFYIYTSGTTGLPKAaivVHSRYYRIAAFG----- 273
Cdd:PRK13383 155 -----------------VIDPATAgaeESGGRPAVAAPGR------IVLLTSGTTGKPKG---VPRAPQLRSAVGvwvti 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 274 HHSYSMRAADVLYDCLPLYHSagniMGVGQCVI---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVR 350
Cdd:PRK13383 209 LDRTRLRTGSRISVAMPMFHG----LGLGMLMLtiaLGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 351 dVEQRH-----RVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECN----CSIANMD------GK-VGSCgfnsrilt 414
Cdd:PRK13383 285 -VRARNplpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGigalATPADLRdapetvGKpVAGC-------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 415 hvyPIRLVKVNEDtmeplrdseglciPCQPGEPGLLV--GQINQqdplrrfDGYVSDSAtnKKIAHSVFRKGDSAYLsgd 492
Cdd:PRK13383 355 ---PVRILDRNNR-------------PVGPRVTGRIFvgGELAG-------TRYTDGGG--KAVVDGMTSTGDMGYL--- 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 493 vlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQEL 572
Cdd:PRK13383 407 ----DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYL 482
|
570 580 590
....*....|....*....|....*....|..
gi 1268743554 573 QKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK13383 483 KDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
77-613 |
6.45e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 68.51 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 156
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVseqLGKSLLKF----CSGD-LG-----------------PES 212
Cdd:PRK07059 100 VVNVNPLYTPreLEHQLKDSGAEAIVVLENFATTVQQV---LAKTAVKHvvvaSMGDlLGfkghivnfvvrrvkkmvPAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 213 ILPDTQLLDPMLAEAPTTPLaQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAAD--VLY 286
Cdd:PRK07059 177 SLPGHVRFNDALAEGARQTF-KPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 287 DC-LPLYH----SAGNIMGVGQCviyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLA 361
Cdd:PRK07059 256 VCaLPLYHifalTVCGLLGMRTG---GRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 362 VGNGL--RPAIWEEFTQRFGVPqIGEFYGATECN----CSIANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDS 435
Cdd:PRK07059 333 NGGGMavQRPVAERWLEMTGCP-ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS------IRDD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 436 EGLCIPC-QPGE-----PGLLVGQINQQDPLRRF---DGYvsdsatnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRD 506
Cdd:PRK07059 397 DGNDLPLgEPGEicirgPQVMAGYWNRPDETAKVmtaDGF--------------FR-------TGDVGVMDERGYTKIVD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 507 RSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVavpgvegkagmaaiADPHS---------QLDPNSMYQELQKV-- 575
Cdd:PRK07059 456 RKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV--------------PDEHSgeavklfvvKKDPALTEEDVKAFck 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1268743554 576 --LASYARPIFLRLLPQVDTTGTFKIqktrLQREGFDPRQ 613
Cdd:PRK07059 522 erLTNYKRPKFVEFRTELPKTNVGKI----LRRELRDGKA 557
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
77-284 |
7.69e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.92 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 77 TIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEgRPEFVGLWL-GLAKAGvvA 155
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAIVEAG--A 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 156 ALLNVNLRR--EPLAFCLGTSAAKALIyggemaaavaEVSEQLGKsllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLA 233
Cdd:PRK10252 534 AWLPLDTGYpdDRLKMMLEDARPSLLI----------TTADQLPR---------------FADVPDLTSLCYNAPLAPQG 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 234 QAPGKGM--DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADV 284
Cdd:PRK10252 589 AAPLQLSqpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDV 641
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
105-607 |
1.32e-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: 67.27 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAAVAEVSEQL--GKSLLKFCSGDLGPESILPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVV 262
Cdd:cd12119 107 FLPLLEAIAPRLptVEHVVVMTDDAAMPEPAGVGVLAYEELLAAES--PEYDWPDFDENTAAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 263 HSRYYriaafgHHSYSMRAADVLY----D----CLPLYHsaGNIMGVG-QCVIYGLTVVLRKKF----SASRFWDdcvKY 329
Cdd:cd12119 185 HRSLV------LHAMAALLTDGLGlsesDvvlpVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYldpaSLAELIE---RE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 330 NCTVVQYIGEICRYLLRQPVR-DVEQRHRVRLAVGNG-LRPAIWEEFTQRfGVPQIgEFYGATE-CNCSIAN-----MDG 401
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEAnGRDLSSLRRVVIGGSaVPRSLIEAFEER-GVRVI-HAWGMTEtSPLGTVArppseHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 402 KVGSCGFNSRILTHvYPIRLVK---VNEDTMEPLRDSEGLcipcqpGE-----PGLLVGQINQQDPLRRF--DGYvsdsa 471
Cdd:cd12119 332 LSEDEQLALRAKQG-RPVPGVElriVDDDGRELPWDGKAV------GElqvrgPWVTKSYYKNDEESEALteDGW----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 472 tnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKA 551
Cdd:cd12119 400 ---------LR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP----KW 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743554 552 G---MAAI-ADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqRE 607
Cdd:cd12119 460 GerpLAVVvLKEGATVTAEELLEFLADKVAKWWLPddvVFVDEIPK---TSTGKIDKKAL-RE 518
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-264 |
1.52e-11 |
|
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: 66.93 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALIYGGEMAAAvaevseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFY-IY 248
Cdd:cd12116 79 ILEDAEPALVLTDDALPDR-------------------------LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYvIY 133
|
170
....*....|....*.
gi 1268743554 249 TSGTTGLPKAAIVVHS 264
Cdd:cd12116 134 TSGSTGRPKGVVVSHR 149
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
81-542 |
2.01e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 67.00 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNA-VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAalLN 159
Cdd:PRK08974 28 MFEQAVARYADQPAFINM--GEVMTFRKLEERSRAfAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV--VN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 160 VNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQ----------LGKSL-----------LKFCSGdLGPESILPD 216
Cdd:PRK08974 104 VNPLYTPreLEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrMGDQLstakgtlvnfvVKYIKR-LVPKYHLPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 217 tqlldpmlaeAPTTPLAQAPGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYyrIA----AFGHHSYSMR-AA 282
Cdd:PRK08974 183 ----------AISFRSALHKGRRMqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNM--LAnleqAKAAYGPLLHpGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 283 DVLYDCLPLYHsagnimgvgqcvIYGLTVvlrkkfsasrfwddcvkyNCTVVQYIGeICRYLLRQPvRDVE------QRH 356
Cdd:PRK08974 251 ELVVTALPLYH------------IFALTV------------------NCLLFIELG-GQNLLITNP-RDIPgfvkelKKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 357 RV---------------------------RLAVGNGL--RPAI---WEEFTQRFgvpqIGEFYGATECN----CSIANMD 400
Cdd:PRK08974 299 PFtaitgvntlfnallnneefqeldfsslKLSVGGGMavQQAVaerWVKLTGQY----LLEGYGLTECSplvsVNPYDLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 401 GKVGSCGFnsrilthvyPIrlvkvnEDTMEPLRDSEGLCIPcqPGEPGLLVG---QINQ---QDPlrrfdgyvsdSATNK 474
Cdd:PRK08974 375 YYSGSIGL---------PV------PSTEIKLVDDDGNEVP--PGEPGELWVkgpQVMLgywQRP----------EATDE 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 475 kiahsVFRKGdsaYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:PRK08974 428 -----VIKDG---WLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
86-604 |
2.24e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.57 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLAL--VDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLR 163
Cdd:PRK05857 24 ARQQPEAIALrrCDGTSAL--RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 164 REPLA-FCLGTSAAKALIYGGEmaaavaevseQLGKSLLKfcSGDLGPESILPDTQLLDPMLAEAPTTP-LAQAPGKGMD 241
Cdd:PRK05857 102 IAAIErFCQITDPAAALVAPGS----------KMASSAVP--EALHSIPVIAVDIAAVTRESEHSLDAAsLAGNADQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRIA----AFGHHSYSMRAADVLYDCLPLYHSAG------NIMGVGQCVIYG-LT 310
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLANRTFFAVPdilqKEGLNWVTWVVGETTYSPLPATHIGGlwwiltCLMHGGLCVTGGeNT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLRKKFSASRfwddcVKYNCTVVQYIGEICrYLLRQPVRDVEQrhrVRLAVGNGLRpAIWEE--FTQRFGVpQIGEFYG 388
Cdd:PRK05857 250 TSLLEILTTNA-----VATTCLVPTLLSKLV-SELKSANATVPS---LRLVGYGGSR-AIAADvrFIEATGV-RTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 389 ATECNCSIANMDGKVGSCgfnSRI----LTHVYPirLVKVNedtmepLRDSEGLCIPCQPGEPGLLVGQINQQDPLRRFd 464
Cdd:PRK05857 319 LSETGCTALCLPTDDGSI---VKIeagaVGRPYP--GVDVY------LAATDGIGPTAPGAGPSASFGTLWIKSPANML- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 465 GYVSDSATNKKIAhsvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAV 544
Cdd:PRK05857 387 GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 545 PGVEGKAGMAAIadPHSQLDPNSMYQELQKVLASY-------ARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK05857 461 EEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-605 |
3.12e-11 |
|
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: 65.95 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG- 182
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 ----GEMAAAVAEvseqlgksllKFCSGDLGPESILPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKA 258
Cdd:cd05932 87 lddwKAMAPGVPE----------GLISISLPPPSAANCQYQWDDLIAQHP--PLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 259 AIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTV------------VLRKK----FSASRF 322
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 323 WddcVKYNCTVVQYIG-EICRYLLRQPVRDVEQRHRV---------RLAVGNG--LRPAIWEEFtQRFGVPqIGEFYGAT 390
Cdd:cd05932 235 W---TKFQQGVQDKIPqQKLNLLLKIPVVNSLVKRKVlkglgldqcRLAGCGSapVPPALLEWY-RSLGLN-ILEAYGMT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 391 EcNCSIANM----DGKVGSCGFNsrilthvYPIRLVKVNEDTmEPLRDSeglcipcqpgePGLLVGQinqqdplrrfdgY 466
Cdd:cd05932 310 E-NFAYSHLnypgRDKIGTVGNA-------GPGVEVRISEDG-EILVRS-----------PALMMGY------------Y 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 VSDSATNkkiahSVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEAVLSR--------LLGQTDV 537
Cdd:cd05932 358 KDPEATA-----EAFTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEhdrvemvcVIGSGLP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 538 AVYGVAVPGVEGKAGMAAIA-------------------DPHSQLDPNSMYQELQKVLASYARPiflrllpqvdttgTFK 598
Cdd:cd05932 432 APLALVVLSEEARLRADAFAraeleaslrahlarvnstlDSHEQLAGIVVVKDPWSIDNGILTP-------------TLK 498
|
....*..
gi 1268743554 599 IQKTRLQ 605
Cdd:cd05932 499 IKRNVLE 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-313 |
5.15e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 83 QAVARR---QPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGfAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 155
Cdd:PRK05691 13 QALQRRaaqTPDRLALRfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 156 A---------------LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgdlgPESILPDTqlL 220
Cdd:PRK05691 92 VpayppesarrhhqerLLSIIADAEPRLLLTVADLRDSLLQMEELAAANA-------------------PELLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 221 DPMLAEApttplAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAA--DVLYDCLPLYHSAGNI 298
Cdd:PRK05691 151 DPALAEA-----WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLI 225
|
250
....*....|....*
gi 1268743554 299 MGVGQCVIYGLTVVL 313
Cdd:PRK05691 226 GGLLQPIFSGVPCVL 240
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
88-264 |
6.20e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.59 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 88 RQPERLALVDAS-SGI--CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLwlgLAKA------------ 151
Cdd:PRK03584 96 RRDDRPAIIFRGeDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPEtVVAM---LATAslgaiwsscspd 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 152 -GVVAALlnvnlRReplafcLGTSAAKALI------YGG---EMAAAVAEVSEQLgKSLLKFCS----GDLGPESILPDT 217
Cdd:PRK03584 173 fGVQGVL-----DR------FGQIEPKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAAALPGA 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1268743554 218 QLLDPMLAEAPTTPLAQAPGkGMDDRLFYIYTSGTTGLPKAaiVVHS 264
Cdd:PRK03584 241 LLWEDFLAPAEAAELEFEPV-PFDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
90-545 |
8.02e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 65.04 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGICWTfaqlDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 167
Cdd:PLN03102 28 PNRTSIIYGKTRFTWP----QTYDRCcrLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIYGGEMAAAVAEVSeqlgkSLLKFCSGDLGPESIL---------PDTQLLD--PMLAEAPTTPLAQAp 236
Cdd:PLN03102 104 AAILRHAKPKILFVDRSFEPLAREVL-----HLLSSEDSNLNLPVIFiheidfpkrPSSEELDyeCLIQRGEPTPSLVA- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 237 gkgmddRLFYI----------YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVI 306
Cdd:PLN03102 178 ------RMFRIqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 307 YGLTVVLRkKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDveQRHR---VRLAVGNGLRPAIWEEFTQRFGVpQI 383
Cdd:PLN03102 252 GGTSVCMR-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLD--LSPRsgpVHVLTGGSPPPAALVKKVQRLGF-QV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 384 GEFYGATECNcsianmdGKVGSCGFN---SRILTH----------VYPIRLVKV---NEDTMEPL-RDSEGLcipcqpGE 446
Cdd:PLN03102 328 MHAYGLTEAT-------GPVLFCEWQdewNRLPENqqmelkarqgVSILGLADVdvkNKETQESVpRDGKTM------GE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 447 PgLLVGQINQQdplrrfdGYVSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PLN03102 395 I-VIKGSSIMK-------GYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
|
490 500
....*....|....*....|
gi 1268743554 526 AVLSRLLGQTDVAVygVAVP 545
Cdd:PLN03102 460 NVLYKYPKVLETAV--VAMP 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-280 |
8.73e-11 |
|
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: 64.49 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLAlVDASSGiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLrrePLAFclgtsaakaliyggemaaaVAEVSEQLGKSLlkfcsgdlgpesilpdtqlldpMLAEAPttplaqapgkgm 240
Cdd:cd05918 82 SH---PLQR-------------------LQEILQDTGAKV----------------------VLTSSP------------ 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMR 280
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGRALG 143
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
91-541 |
1.39e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 63.99 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 91 ERLALVDAS---SGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 167
Cdd:cd05915 9 GRKEVVSRLhtgEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 168 AFCLGTSAAKALIYGGEMAAaVAEVSEQLGKSLLKfcsgdlGPESILPDTQLLDPMLAEAPTTplaqAPGKGMD--DRLF 245
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLP-LVEAIRGELKTVQH------FVVMDEKAPEGYLAYEEALGEE----ADPVRVPerAACG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHSYSMRAADVLYDC-LPLYHSAGnimgvgQCVIY------GLTVVLRKKF 317
Cdd:cd05915 158 MAYTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPvVPMFHVNA------WCLPYaatlvgAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 318 SASRFWDDCVKYNCTvvQYIGEICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFtQRFGVPQIGEFYGATEcnc 394
Cdd:cd05915 232 DPASLVELFDGEGVT--FTAGVPTVWLALADYLESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 395 sianMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGllVGQINQQDPLRR---FDGYVSDSA 471
Cdd:cd05915 306 ----TSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEE 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 472 TNKKIAhsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 541
Cdd:cd05915 380 ATRSAL---TPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
247-545 |
2.40e-10 |
|
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: 62.29 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 247 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGniMGVGQCVIY--GLTVVLRKkFSASRFWD 324
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 325 DCVKYNCTVVQYIGEICRYLLrqpvrDVEQRHRVRLAvgnGLR-------PaiweEFTQRFGVPQIGEF---YGATECNC 394
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLL-----DAAEKSGVDLS---SLRhvlgldaP----ETIQRFEETTGATFwslYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 395 --SIANMDGKVGSCGfnsRILthvyPIRLVKVNEDTMEPLRdseglcipcqPGEPGllvgQINQQDPLRrFDGYVSDSAT 472
Cdd:cd17637 151 lvTLSPYRERPGSAG---RPG----PLVRVRIVDDNDRPVP----------AGETG----EIVVRGPLV-FQGYWNLPEL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743554 473 NkkiAHSvFRKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 545
Cdd:cd17637 209 T---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP 277
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
105-619 |
2.69e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 63.51 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAAVAEvseqlgksllkfcSGDLGPESILPDTQLLDPmlaeAPTTPLaqapgkGMDDRLFYIYTSGTTGLPKAAIVVHS 264
Cdd:PRK06060 112 LRDRFQP-------------SRVAEAAELMSEAARVAP----GGYEPM------GGDALAYATYTSGTTGPPKAAIHRHA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 265 RYYR-IAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGV-------GQCVIYGLTVVLRKKFSASRFWDDCVKYNctVVQY 336
Cdd:PRK06060 169 DPLTfVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVwfplatgGSAVINSAPVTPEAAAILSARFGPSVLYG--VPNF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 337 IGEICRYLLRQPVRDVeqrhRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCS-IANM--DGKVGSCGfnsRIL 413
Cdd:PRK06060 247 FARVIDSCSPDSFRSL----RCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTfVSNRvdEWRLGTLG---RVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 414 THvYPIRLVKVNEDTMEPlrdseglcipcqPGEPGLLVgqinqQDPlrrfdgyvsdsatnkKIAHSVFRKGDSAYLSGDV 493
Cdd:PRK06060 320 PP-YEIRVVAPDGTTAGP------------GVEGDLWV-----RGP---------------AIAKGYWNRPDSPVANEGW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 494 L------VMDELGYMYFRDRSGDTFRWRGENVSTTEVEavlsRLLGQTDvAVYGVAVPGVEGKAGMAAIadpHSQLDPNS 567
Cdd:PRK06060 367 LdtrdrvCIDSDGWVTYRCRADDTEVIGGVNVDPREVE----RLIIEDE-AVAEAAVVAVRESTGASTL---QAFLVATS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 568 MyqelQKVLASYARPIFLRLLPQVDttgTFKIQKTRLQREGFdPRQTSDRLF 619
Cdd:PRK06060 439 G----ATIDGSVMRDLHRGLLNRLS---AFKVPHRFAVVDRL-PRTPNGKLV 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-614 |
5.99e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRL--SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDP 3139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALiyggemaaavaevseqLGKSLLKfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQA--PGK 238
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQLL----------------LSQSHLR-----------LPLAQGVQVLDLDRGDENYAEAnpAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 239 GMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLydclpLYHSAGNIMGVGQCVIYGLTVVLRKKF 317
Cdd:PRK12316 3193 TMPENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPLMSGARVVL 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 318 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE----QRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECN 393
Cdd:PRK12316 3268 AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEeedaHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEAT 3347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 394 CSIANMDgkVGSCGFNSRILTHVYPIRLVKVNEDTMEPlrDSEGLCIPCQPGEPGLLVGQINQQDplrrfdgyvsdsATN 473
Cdd:PRK12316 3348 ITVTHWQ--CVEEGKDAVPIGRPIANRACYILDGSLEP--VPVGALGELYLGGEGLARGYHNRPG------------LTA 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 474 KKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQTDVAVYGVAVPGVEGKAGM 553
Cdd:PRK12316 3412 ERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL-----LEHPWVREAVVLAVDGRQLV 3486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 554 AAIADPHSQLD-PNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQT 614
Cdd:PRK12316 3487 AYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-604 |
6.46e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIyggemaaAVAEVSEQL----GKSLLkfcsgDLGPESILPDTQLLDPMLAEAPttplaqap 236
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLL-------TQSHLLQRLpipdGLASL-----ALDRDEDWEGFPAHDPAVRLHP-------- 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 237 gkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPlYHSAGNIMGVGQCVIYGLTVVLRK 315
Cdd:PRK12316 4694 -----DNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 316 kfsaSRFWD------DCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYG 388
Cdd:PRK12316 4768 ----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYG 4843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 389 ATECNCSIANMDGKVGS-CGFNSRILTHVYPIRLVKVNEDTMEPLrdseglciPC-QPGEpgLLVGqinqQDPLRRfdGY 466
Cdd:PRK12316 4844 PTETTVTVLLWKARDGDaCGAAYMPIGTPLGNRSGYVLDGQLNPL--------PVgVAGE--LYLG----GEGVAR--GY 4907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 VSDSA-TNKKIAHSVFRK-GDSAYLSGDVL------VMDELGymyfrdRSGDTFRWRGENVSTTEVEAvlsRLLGQTDV- 537
Cdd:PRK12316 4908 LERPAlTAERFVPDPFGApGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIEA---RLREHPAVr 4978
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 538 -AVYgVAVPGVEGK--AGMAAIADPHSQLDP-------NSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK12316 4979 eAVV-IAQEGAVGKqlVGYVVPQDPALADADeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-604 |
8.92e-10 |
|
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: 61.11 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNvnlrre 165
Cdd:cd05945 1 AAANPDRPAVVEG--GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 plafclGTSAAkaliyggEMAAAVAEVSeqlgksllkfcsgdlGPESILPDtqlldpmlaeapttplaqapgkgmDDRLF 245
Cdd:cd05945 73 ------ASSPA-------ERIREILDAA---------------KPALLIAD------------------------GDDNA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 246 YI-YTSGTTGLPKAaiVVHSrYYRIAAFGHHS---YSMRAADVLYdCLPLYHSAGNIMGVGQCVIYGLTVV-LRKKFSAS 320
Cdd:cd05945 101 YIiFTSGSTGRPKG--VQIS-HDNLVSFTNWMlsdFPLGPGDVFL-NQAPFSFDLSVMDLYPALASGATLVpVPRDATAD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 321 --RFWDDCVKYNCTV---VQYIGEICrylLRQPVRDVEQRHRVRLAVGNGlrpaiwEEFT--------QRFGVPQIGEFY 387
Cdd:cd05945 177 pkQLFRFLAEHGITVwvsTPSFAAMC---LLSPTFTPESLPSLRHFLFCG------EVLPhktaralqQRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 388 GATECN--CSIANMDGKVgsCGFNSRIlthvyPIRLVKVNEDTMepLRDSEGLCIPcqPGEPG--LLVGQinqqdplRRF 463
Cdd:cd05945 248 GPTEATvaVTYIEVTPEV--LDGYDRL-----PIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP-------SVS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 464 DGYVSDSATNKKIAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVA 543
Cdd:cd05945 310 KGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VP 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 544 VPGVEGKAGMAAIADPH---SQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05945 386 KYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-559 |
1.10e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 60.92 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 101 GICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALi 180
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 181 yggemaaavaevseqlgksllkFCSgdlgpesilpdtqllDPmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05914 84 ----------------------FVS---------------DE------------------DDVALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 261 VVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFwDDCVKYNCTVV------ 334
Cdd:cd05914 109 LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-IALAFAQVTPTlgvpvp 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 335 -------------QYIGEICRYLLRQPVRDVEQRHRVRLAV--------------GNGLRPAIwEEFTQRFGVPQIgEFY 387
Cdd:cd05914 188 lviekifkmdiipKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggnikefvigGAKINPDV-EEFLRTIGFPYT-IGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 388 GATECN---CSIANMDGKVGSCGFnsrilthvyPIRLVKVNEDTMEPlrdseglcipcQPGEPGLLVGQINQqdplrrFD 464
Cdd:cd05914 266 GMTETApiiSYSPPNRIRLGSAGK---------VIDGVEVRIDSPDP-----------ATGEGEIIVRGPNV------MK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 465 GYVSdsatNKKIAHSVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEAVLSRLlgqTDVAVYGVA 543
Cdd:cd05914 320 GYYK----NPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNM---PFVLESLVV 391
|
490
....*....|....*.
gi 1268743554 544 VpgVEGKAGMAAIADP 559
Cdd:cd05914 392 V--QEKKLVALAYIDP 405
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
123-296 |
2.75e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.02 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 123 LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAF------------CLGTSAAKALIYGGEMAAAVA 190
Cdd:PRK09192 69 LGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL-----PMGFggresyiaqlrgMLASAQPAAIITPDELLPWVN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 191 EVSEqlGKSLLKfcsgdlgpesILPDTQLldpMLAEAPTTPLAQA-PgkgmDDRLFYIYTSGTTGLPKAAIVVH-SRYYR 268
Cdd:PRK09192 144 EATH--GNPLLH----------VLSHAWF---KALPEADVALPRPtP----DDIAYLQYSSGSTRFPRGVIITHrALMAN 204
|
170 180
....*....|....*....|....*...
gi 1268743554 269 IAAFGHHSYSMRAADVLYDCLPLYHSAG 296
Cdd:PRK09192 205 LRAISHDGLKVRPGDRCVSWLPFYHDMG 232
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
105-589 |
5.95e-09 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 58.87 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvaallnvnlrreplafclgtsAAKALIYGGE 184
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIG----------------------AIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPL-------------AQAPGKGMD---------- 241
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHhvlvlnrpqvpadLTKPGRDLDwsellakaep 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 ---------DRLFYIYTSGTTGLPKAaIVVHSRYYRIAAfghhSYSMRAadvLYDCLP--LYHSAGNImG--VGQCVI-Y 307
Cdd:cd05967 222 vdcvpvaatDPLYILYTSGTTGKPKG-VVRDNGGHAVAL----NWSMRN---IYGIKPgdVWWAASDV-GwvVGHSYIvY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 308 G------LTVVLRKKFS----ASRFWDDCVKYNCTVVQYIGEICRYLLRQP-----VRDVE-QRHRVRLAVGNGLRPAIW 371
Cdd:cd05967 293 GpllhgaTTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDlSSLRTLFLAGERLDPPTL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 372 EEFTQRFGVPQIgEFYGATE------CNCS-IANMDGKVGSC-----GFNsrilthvypirlVKVNEDTMEPLRDSE--G 437
Cdd:cd05967 373 EWAENTLGVPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGYQ------------VQVLDEDGEPVGPNElgN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 438 LCIPCqPGEPGLLVGQINQQDplrRF-DGYVSDSatnkkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 516
Cdd:cd05967 440 IVIKL-PLPPGCLLTLWKNDE---RFkKLYLSKF--------------PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 517 ENVSTTEVEAVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AIADPHSQLDPNSMYQELQKV-------LASYARPIFLRLL 588
Cdd:cd05967 502 HRLSTGEMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKELVALvreqigpVAAFRLVIFVKRL 580
|
.
gi 1268743554 589 P 589
Cdd:cd05967 581 P 581
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
83-607 |
6.25e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 59.01 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 83 QAVARRQPERLALVDASS--GICWTFAQLDTYSNAVANLFRQL-GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaaLLN 159
Cdd:PRK05677 27 QAVLKQSCQRFADKPAFSnlGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI--VVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 160 VN---LRREpLAFCLGTSAAKALIYGGEMA--------------AAVAEVSEQLG-------KSLLKFCSgDLGPESILP 215
Cdd:PRK05677 105 TNplyTARE-MEHQFNDSGAKALVCLANMAhlaekvlpktgvkhVIVTEVADMLPplkrlliNAVVKHVK-KMVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 216 DTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGHHSYSMRAADVLYDC------L 289
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRN---LVANMLQCRALMGSNLNEGCeiliapL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 290 PLYH------SAGNIMGVGQCVIY--------GLTVVLRK-KFSAsrFwddcVKYNCTVVQyigeICRyllRQPVRDVE- 353
Cdd:PRK05677 259 PLYHiyaftfHCMAMMLIGNHNILisnprdlpAMVKELGKwKFSG--F----VGLNTLFVA----LCN---NEAFRKLDf 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 354 QRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECN--CSIANMDG-KVGSCGFNsrilthvYPIRLVKVNEDTME 430
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETSpvVSVNPSQAiQVGTIGIP-------VPSTLCKVIDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 431 --PLRDSEGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRS 508
Cdd:PRK05677 398 elPLGEVGELCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIALIQEDGYMRIVDRK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 509 GDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AIADPHSQLDPNSMYQELQKVLASYARPIF 584
Cdd:PRK05677 456 KDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEHMRANLTGYKVPKA 531
|
570 580
....*....|....*....|...
gi 1268743554 585 LRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK05677 532 VEFRDELPTTNVGKILRRELRDE 554
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
90-271 |
7.60e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 58.42 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 90 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 169
Cdd:cd17652 1 PDAPAVVFGDETL--TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 170 CLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapTTPlaqapgkgmdDRLFY-IY 248
Cdd:cd17652 79 MLADARPALLL------------------------------------------------TTP----------DNLAYvIY 100
|
170 180
....*....|....*....|...
gi 1268743554 249 TSGTTGLPKAAIVVHSRYYRIAA 271
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAA 123
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
241-542 |
2.36e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 57.19 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYS-----MRAADVLYDCLPLYH----SAGNI--MGVGqcviyGL 309
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHifalTANGLvfMKIG-----GC 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 310 TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGL--RPAIWEEFTQRFGVPQIgEFY 387
Cdd:PRK08751 283 NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 388 GATECNcsianmdgkVGSCgfnsrilthVYPIRLVKVNEDTMEPLrDSEGLCIPCQPGEpGLLVGQINQ---QDPlRRFD 464
Cdd:PRK08751 362 GLTETS---------PAAC---------INPLTLKEYNGSIGLPI-PSTDACIKDDAGT-VLAIGEIGElciKGP-QVMK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 465 GYVSDSATNKKIAHSvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 542
Cdd:PRK08751 421 GYWKRPEETAKVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
86-296 |
2.83e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.42 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 165
Cdd:PRK09029 13 AQVRPQAIALR--LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLafclgtsaakaliyggemaaavAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPgkgMddrlf 245
Cdd:PRK09029 91 LL----------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLAT---M----- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268743554 246 yIYTSGTTGLPKAaiVVHSryyriaaFGHHSYSmrAADVL----YDC-------LPLYHSAG 296
Cdd:PRK09029 141 -TLTSGSTGLPKA--AVHT-------AQAHLAS--AEGVLslmpFTAqdswllsLPLFHVSG 190
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-283 |
3.32e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.10 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 72 RRAGDTIPCIFQAVARRQPERLALVDASSGICwtFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 151
Cdd:PRK05691 2184 ARLDQTLHGLFAAQAARTPQAPALTFAGQTLS--YAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 152 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqLGKSLLKFCsgdlgpesiLPDTQlldPMLAEAPTTP 231
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE----LPAGVARWC---------LEDDA---AALAAYSDAP 2325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 232 LAQAPGKgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGhhsysMRAAD 283
Cdd:PRK05691 2326 LPFLSLP--QHQAYLIYTSGSTGKPKGVVVSHGEIAMhcqavIERFG-----MRADD 2375
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
242-601 |
6.69e-08 |
|
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: 54.96 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYriAAFGH---HSYSMRAADVLYDCLPLYHSAGN------IMGVGQCVIYGLTVV 312
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHIGGLwwiltcLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 313 LRKKFSASRFWDdcVKYNCTVVQYIGEICRyLLRQPVRDVEQrhrVRLAVGNGLRP-AIWEEFTQRFGVPQIGEFYGATE 391
Cdd:cd17635 80 YKSLFKILTTNA--VTTTCLVPTLLSKLVS-ELKSANATVPS---LRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 392 CN--CSIANMDG--KVGSCGfnsriltHVYPIRLVKV-NEDTMEPLRDSEGLCIPCQPgepgllvgqinqqdplRRFDGY 466
Cdd:cd17635 154 TGtaLCLPTDDDsiEINAVG-------RPYPGVDVYLaATDGIAGPSASFGTIWIKSP----------------ANMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 467 VSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvAVP 545
Cdd:cd17635 211 WN----NPERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EIS 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 546 GVEGKAGMAAIADPHSQLDPNSMYQELQKV---LASYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17635 282 DEEFGELVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-264 |
6.94e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 160
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETL--DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 161 NLRREPLAFCLGTSAAKALIyggemaaavaevSEQlgkSLLKFCSGDLGPESILPD--TQLLDPMLAEAPTTPLAQapgk 238
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLL------------SQS---HLGRKLPLAAGVQVLDLDrpAAWLEGYSEENPGTELNP---- 654
|
170 180
....*....|....*....|....*..
gi 1268743554 239 gmdDRLFY-IYTSGTTGLPKAAIVVHS 264
Cdd:PRK12316 655 ---ENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
523-598 |
7.37e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 49.85 E-value: 7.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 523 EVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFK 598
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-591 |
1.06e-07 |
|
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: 54.31 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRI----AAFGHHSYSM---------RAAD-VLYDCLPLYHSAGNIMGVGQcVIY 307
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMlmggADFGTGEFTPsedahkaaaAAAGtVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 308 GLTVVL-RKKFSASRFWDDCVKYNCTVVQYIGEIcryLLRQPVRDVEQRHRVRL----AVGNGlrPAIW-EEFTQRF--G 379
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVTSMTIVGDA---MARPLIDALRDAGPYDLsslfAISSG--GALLsPEVKQGLleL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 380 VPQIG--EFYGATEcncSIANMDGKVGSCGFNSRILTHVYPiRLVKVNEDTMEPLRDSEGlcipcqpgepgllVGQINQQ 457
Cdd:cd05924 158 VPNITlvDAFGSSE---TGFTGSGHSAGSGPETGPFTRANP-DTVVLDDDGRVVPPGSGG-------------VGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 458 D--PLrrfdGYVSDSatnKKIAHSVFRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 534
Cdd:cd05924 221 GhiPL----GYYGDE---AKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743554 535 TDVAVYGVAVP--GVEgkagMAAI--ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQV 591
Cdd:cd05924 294 YDVLVVGRPDErwGQE----VVAVvqLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEI 350
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-604 |
2.13e-07 |
|
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: 53.62 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygGE 184
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI--GI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 maaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05910 82 ----------------------------------------------PKA-------DEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 265 RYY-RIAAFgHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCV-----IYGLTVVLRKKFSASRfwddcvKYNCTVV---- 334
Cdd:cd05910 109 TFAaQIDAL-RQLYGIRPGEVDLATFPLFALFGPALGLTSVIpdmdpTRPARADPQKLVGAIR------QYGVSIVfgsp 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 335 QYIGEICRYLLRQPvRDVEQRHRVrLAVGNGLRPAIWEEFtqRFGVPQIGEF---YGATEC--NCSIANMD--------- 400
Cdd:cd05910 182 ALLERVARYCAQHG-ITLPSLRRV-LSAGAPVPIALAARL--RKMLSDEAEIltpYGATEAlpVSSIGSREllatttaat 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 401 -GKVGSCgfnsriLTHVYPIRLVKVNEDTMEPLRDSEG-LCIPcqPGEpgllVGQINQQDPLrrfdgyVSDSATNKKIAH 478
Cdd:cd05910 258 sGGAGTC------VGRPIPGVRVRIIEIDDEPIAEWDDtLELP--RGE----IGEITVTGPT------VTPTYVNRPVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 479 SVFRKGDSA----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAG-- 552
Cdd:cd05910 320 ALAKIDDNSegfwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLcv 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 553 --MAAIADPHSQLdpnsmYQELQKVLASYA-----RPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05910 400 epLPGTITPRARL-----EQELRALAKDYPhtqriGRFLIHPSFPVDIRHNAKIFREKL 453
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
78-272 |
3.08e-07 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 53.92 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 78 IPCIFQAVARRQPERLALVDASSGIC-------WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAK 150
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 151 AGVVAALLNVNLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAE---- 226
Cdd:TIGR03443 318 AGATFSVIDPAYPPARQTIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVggsl 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 227 --------APTTPLAQAPGK---GMDDRLFYIYTSGTTGLPKAaivVHSRYYRIAAF 272
Cdd:TIGR03443 390 eggetdvlAPYQALKDTPTGvvvGPDSNPTLSFTSGSEGIPKG---VLGRHFSLAYY 443
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
89-528 |
1.23e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 51.38 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 89 QPERLALVDASSGICWtfaqLDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREP 166
Cdd:PLN02479 33 HPTRKSVVHGSVRYTW----AQTYQRCrrLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 167 LAFCLGTSAAKALIYGGEMAAAVAE----VSEQLGKSL---LKFCSGD-----------LGPESILPDTQLL--DPMLAE 226
Cdd:PLN02479 109 IAFLLEHSKSEVVMVDQEFFTLAEEalkiLAEKKKSSFkppLLIVIGDptcdpkslqyaLGKGAIEYEKFLEtgDPEFAW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 227 APTTPLAQAPGKGmddrlfyiYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVI 306
Cdd:PLN02479 189 KPPADEWQSIALG--------YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 307 YGLTVVLRKkFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD--VEQRHRVRLAV-GNGLRPAIWEEFTQR-FGVPQ 382
Cdd:PLN02479 261 CGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTaGAAPPPSVLFAMSEKgFRVTH 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 383 ---IGEFYG-ATECN----------CSIANMDGKVGscgfnsriLTHVYPIRLVKVNEDTMEPLrdseglcipcqPGEpG 448
Cdd:PLN02479 340 tygLSETYGpSTVCAwkpewdslppEEQARLNARQG--------VRYIGLEGLDVVDTKTMKPV-----------PAD-G 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 449 LLVGQInqqdpLRRFDGYVSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 528
Cdd:PLN02479 400 KTMGEI-----VMRGNMVMKGYLKNPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
105-264 |
1.36e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 51.52 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 maaAVAEVSEQLGKSLLKFCS----GDLgPES-------ILPDTQLLDPMLAEAPTTPLaqaPGKGMDDRLFYI-YTSGT 252
Cdd:PTZ00216 203 ---NVPNLLRLMKSGGMPNTTiiylDSL-PASvdtegcrLVAWTDVVAKGHSAGSHHPL---NIPENNDDLALImYTSGT 275
|
170
....*....|..
gi 1268743554 253 TGLPKAaiVVHS 264
Cdd:PTZ00216 276 TGDPKG--VMHT 285
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
241-606 |
1.53e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.44 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 241 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRIAAFgHHSYSMRAADVLY---DClplyhsaGNIMGvGQCVIYG-----LT 310
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITG-HSYVTYGpmlngAT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGvpq 382
Cdd:PLN02654 346 VLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLrvlgSVGEPINPSAWRWFFNVVG--- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 383 igefygatECNCSIANMDGKVGSCGFNSRILTHVYP------------IRLVKVNEDTMEPLRDSEG-LCIPCQ-PGEPG 448
Cdd:PLN02654 423 --------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCVKKSwPGAFR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 449 LLVGQINQQDP--LRRFDGYvsdsatnkkiahsvfrkgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 526
Cdd:PLN02654 495 TLYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVES 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 527 VLSRLLGQTDVAVYGV--AVPGvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 602
Cdd:PLN02654 554 ALVSHPQCAEAAVVGIehEVKG-QGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRR 632
|
....
gi 1268743554 603 RLQR 606
Cdd:PLN02654 633 ILRK 636
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
81-296 |
2.87e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 50.73 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAV--ARRQ--PERLALVDASSGICwTFAQLDTYSNAVANLFRQlGFAPGDVVAVFLegrPEFVGL---WLGLAKAGV 153
Cdd:PRK06814 633 LFEALieAAKIhgFKKLAVEDPVNGPL-TYRKLLTGAFVLGRKLKK-NTPPGENVGVML---PNANGAavtFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 154 VAALLN-----VNLrrepLAFCLGTS-----AAKALIYGGEMAAAVAEVSEQLGKSLLkfcsgdlgpESILPDTQLLDPM 223
Cdd:PRK06814 708 VPAMINfsagiANI----LSACKAAQvktvlTSRAFIEKARLGPLIEALEFGIRIIYL---------EDVRAQIGLADKI 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 224 LAE-APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAA---FGhhsysmrAADVLYDCLPLYHSA 295
Cdd:PRK06814 775 KGLlAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFHSF 847
|
.
gi 1268743554 296 G 296
Cdd:PRK06814 848 G 848
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
237-536 |
3.07e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.20 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 237 GKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAG-NIMGV-----GQCVIYGLT 310
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLfpllsGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 311 VVLRKKFsaSRFWDDcvkyncTVVQYIGE---ICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGE 385
Cdd:PRK06334 259 PLYPKKI--VEMIDE------AKVTFLGStpvFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 386 FYGATECN--CSIANMDG-KVGSCgfnsrilthvypirlVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQdplrr 462
Cdd:PRK06334 331 GYGTTECSpvITINTVNSpKHESC---------------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL----- 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743554 463 FDGYVSDSATNKKIAHSvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 536
Cdd:PRK06334 391 FSGYLGEDFGQGFVELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNA 460
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
86-560 |
4.48e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 49.87 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvn 161
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 162 lrreplafclgtsaaKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPT---------TPL 232
Cdd:cd05966 136 ---------------HSVVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKCPSvekvlvvkrTGG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 233 AQAPGKGMD----------------------DRLFYIYTSGTTGLPKAaiVVHS----------------------RYYR 268
Cdd:cd05966 201 EVPMTEGRDlwwhdlmakqspecepewmdseDPLFILYTSGSTGKPKG--VVHTtggyllyaattfkyvfdyhpddIYWC 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 269 IAAFG---HHSYsmraadVLYDclPLyhsagnimgvgqcvIYGLTVVLrkkF-------SASRFWDDCVKYNCTVVQYIG 338
Cdd:cd05966 279 TADIGwitGHSY------IVYG--PL--------------ANGATTVM---FegtptypDPGRYWDIVEKHKVTIFYTAP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 339 EICRYLLRQPvRDVEQRH-----RVRLAVGNGLRPAIWEEFTQRFG---VPqIGEFYGATEC-NCSIANMDG----KVGS 405
Cdd:cd05966 334 TAIRALMKFG-DEWVKKHdlsslRVLGSVGEPINPEAWMWYYEVIGkerCP-IVDTWWQTETgGIMITPLPGatplKPGS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 406 CGFnsrilthvyP---IRLVKVNEDTMEPLRDSEG-LCIPcQPGePGLLVGQINqqDPLRRFDGYvsdsatnkkiahsvF 481
Cdd:cd05966 412 ATR---------PffgIEPAILDEEGNEVEGEVEGyLVIK-RPW-PGMARTIYG--DHERYEDTY--------------F 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 482 RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgqtdvavygVAVPGVegkAGMAAIADPH 560
Cdd:cd05966 465 SKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVGRPH 527
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-293 |
5.50e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 49.71 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 W-TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 182
Cdd:PLN02736 78 WmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE----WLIVDHACSAYSYVSV-----PLYDTLGPDAVKFIVNH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 GEMAAAVaeVSEQLGKSLLKFCSgDL----------GPESILPDTQL--------LDPMLAEAPTTPLAQAPGKGmDDRL 244
Cdd:PLN02736 149 AEVAAIF--CVPQTLNTLLSCLS-EIpsvrlivvvgGADEPLPSLPSgtgveivtYSKLLAQGRSSPQPFRPPKP-EDVA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1268743554 245 FYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYH 293
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
81-528 |
7.87e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.05 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQ-LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaaLLN 159
Cdd:PRK12492 29 VFERSCKKFADRPAF--SNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLI--VVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 160 VN---LRREpLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGP--ESILPDTqLLDPMLAEAPTTPLA 233
Cdd:PRK12492 105 TNplyTARE-MRHQFKDSGARALVYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLPaaKGWLVNT-VVDKVKKMVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 234 QAPG-----------------KGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGH-----HSYSMRAADVLY 286
Cdd:PRK12492 183 QAVPfkqalrqgrglslkpvpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvRACLSQlgpdgQPLMKEGQEVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 287 DCLPLYHsagnimgvgqcvIYGLT-------------VVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP-VRDV 352
Cdd:PRK12492 263 APLPLYH------------IYAFTancmcmmvsgnhnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPgFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 353 EQRH-RVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECN-CSIANMDGKVgscgfnSRILTHVYPI--RLVKV-NED 427
Cdd:PRK12492 331 DFSAlKLTNSGGTALVKATAERWEQLTGC-TIVEGYGLTETSpVASTNPYGEL------ARLGTVGIPVpgTALKViDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 428 TME-PLRDSEGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKI-AHSVFRkgdsaylSGDVLVMDELGYMYFR 505
Cdd:PRK12492 404 GNElPLGERGELCIK----GPQVMKGYWQQPE------------ATAEALdAEGWFK-------TGDIAVIDPDGFVRIV 460
|
490 500
....*....|....*....|...
gi 1268743554 506 DRSGDTFRWRGENVSTTEVEAVL 528
Cdd:PRK12492 461 DRKKDLIIVSGFNVYPNEIEDVV 483
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
105-609 |
8.69e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 48.59 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 184
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 185 MAAAVAEVSEQLgKSLLKFCSgdLGPESILPDTQLLDpmlAEAPTTPLAQAPG----KGMDDRLF--YIYTSGTTGLPKA 258
Cdd:PRK06018 121 FVPILEKIADKL-PSVERYVV--LTDAAHMPQTTLKN---AVAYEEWIAEADGdfawKTFDENTAagMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 259 AI------VVHSryyrIAAFGHHSYSMRAADVLYDCLPLYHSagNIMGVGqcviygltvvlrkkFSASRFWDDCVKYNCt 332
Cdd:PRK06018 195 VLyshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA--NSWGIA--------------FSAPSMGTKLVMPGA- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 333 vvQYIGEICRYLLrqpvrDVEQrhrVRLAVGnglRPAIWEEFTQ-----RFGVPQIGEFY-GATECNCSIANMDGKVGSC 406
Cdd:PRK06018 254 --KLDGASVYELL-----DTEK---VTFTAG---VPTVWLMLLQymekeGLKLPHLKMVVcGGSAMPRSMIKAFEDMGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 407 GFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVgQINQQDPLRR---FDG------YVSDSAtnkkIA 477
Cdd:PRK06018 321 VRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDAGKelpWDGktfgrlKVRGPA----VA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 478 HSVFRKGDSA------YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE--AVlsrllGQTDV---AVYGVAVPG 546
Cdd:PRK06018 396 AAYYRVDGEIldddgfFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnlAV-----GHPKVaeaAVIGVYHPK 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743554 547 VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 609
Cdd:PRK06018 471 WDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPddvAFVDAIPH---TATGKILKTAL-REQF 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
81-261 |
2.84e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 81 IFQAVARRQPERLAL--VDASsgicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL 158
Cdd:PRK05691 3725 LFEAQVAAHPQRIAAscLDQQ----WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 159 NVNLRREPLAFCLGTSAAKALIyggeMAAAVAEvseqLGKSLLKFCSGDLGPesilpdtQLLdpMLAEAPTTPLAQA-PG 237
Cdd:PRK05691 3801 DPGLPAQRLQRIIELSRTPVLV----CSAACRE----QARALLDELGCANRP-------RLL--VWEEVQAGEVASHnPG 3863
|
170 180
....*....|....*....|....*.
gi 1268743554 238 --KGMDDRLFYIYTSGTTGLPKAAIV 261
Cdd:PRK05691 3864 iySGPDNLAYVIYTSGSTGLPKGVMV 3889
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
88-306 |
4.33e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.52 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 88 RQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV--VAALLNVNlRRE 165
Cdd:PRK10946 35 AASDAIAVICGERQ--FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVapVNALFSHQ-RSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 166 PLAFC-------LGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGpesilpdtqLLDPMLAEAPTTPLAQAPGk 238
Cdd:PRK10946 112 LNAYAsqiepalLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHS---------LDDAINHPAEDFTATPSPA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 239 gmDDRLFYIYTSGTTGLPKAAIVVHSRYYriaafghhsYSMRA--------ADVLYDC-LPLYH----SAGNIMGV---G 302
Cdd:PRK10946 182 --DEVAFFQLSGGSTGTPKLIPRTHNDYY---------YSVRRsveicgftPQTRYLCaLPAAHnypmSSPGALGVflaG 250
|
....
gi 1268743554 303 QCVI 306
Cdd:PRK10946 251 GTVV 254
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
59-298 |
4.34e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.58 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 59 SVLIRVRLELRRHRRagdTIPCIFQAVARRQPER--LALVDASSGiCW---TFAQLDTYSNAVANLFRQLGFAPGDVVAV 133
Cdd:PRK12582 35 SIVIKSRHPLGPYPR---SIPHLLAKWAAEAPDRpwLAQREPGHG-QWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 134 fLEGRP-EFVGLWLGLAKAGVVAA-------LLNVNLRRepLAFCLgTSAAKALIY---GGEMAAAVAEVSEQlGKSLLk 202
Cdd:PRK12582 111 -LSGNSiEHALMTLAAMQAGVPAApvspaysLMSHDHAK--LKHLF-DLVKPRVVFaqsGAPFARALAALDLL-DVTVV- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 203 FCSGDLGPESILPdtqlLDPMLAEAPTTPLAQAPGK-GMDDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAFGHHSYSMRA 281
Cdd:PRK12582 185 HVTGPGEGIASIA----FADLAATPPTAAVAAAIAAiTPDTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPRE 259
|
250 260
....*....|....*....|..
gi 1268743554 282 AD----VLYDCLPLYH-SAGNI 298
Cdd:PRK12582 260 PDppppVSLDWMPWNHtMGGNA 281
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
86-308 |
7.50e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 45.89 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 86 ARRQPERLALVDASSGICW---TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA------ 156
Cdd:cd05921 5 ARQAPDRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApvspay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 157 -LLNVNLRRepLAFCLGTsAAKALIY---GGEMAAAVAEVsEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPttpl 232
Cdd:cd05921 85 sLMSQDLAK--LKHLFEL-LKPGLVFaqdAAPFARALAAI-FPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVD---- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743554 233 AQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD--VLYDCLPLYHSAGNIMGVGqCVIYG 308
Cdd:cd05921 157 AAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFN-LVLYN 233
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-308 |
8.18e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.88 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 104 W-TFAQ-LDTYSNAVANLFrQLGFAPGDVVAVFLEGRPEfvglWL----GLAKAGVVAALLNVNLRREPLAFCLGTSAAK 177
Cdd:PLN02387 106 WiTYGQvFERVCNFASGLV-ALGHNKEERVAIFADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 178 ALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLA----------EAPTTPLAQAPgkgmDDRLFYI 247
Cdd:PLN02387 181 TVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSsfseveklgkENPVDPDLPSP----NDIAVIM 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 248 YTSGTTGLPKAAIVVHSRYY-RIAAFGHHSYSMRAADVLYDCLPLYH----SAGNIM-GVGQCVIYG 308
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVaTVAGVMTVVPKLGKNDVYLAYLPLAHilelAAESVMaAVGAAIGYG 323
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
480-599 |
1.19e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.03 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 480 VFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvavPGVEGKAG--MAAIA 557
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGerVKAKV 360
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1268743554 558 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 599
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
490-609 |
2.50e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 43.93 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 490 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMY 569
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELL 492
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1268743554 570 QELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 609
Cdd:PRK07008 493 AFYEGKVAKWWIPddvVFVDAIPH---TATGKLQKLKL-REQF 531
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
247-608 |
2.88e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 43.83 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 247 IYTSGTTGLPKAaiVVHSRyyRIAAFG----HHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRF 322
Cdd:PRK07787 134 VYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 323 WDDCvKYNCTVvqYIGEICRYllRQPVRDVEQRH---RVRLAV-GNGLRPA-IWEEFTQRFGVPQIgEFYGATEC--NCS 395
Cdd:PRK07787 210 AQAL-SEGGTL--YFGVPTVW--SRIAADPEAARalrGARLLVsGSAALPVpVFDRLAALTGHRPV-ERYGMTETliTLS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 396 I-ANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPCQpGEPgllVGQINQQDPLrRFDGYVsdsatNK 474
Cdd:PRK07787 284 TrADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD-GET---VGELQVRGPT-LFDGYL-----NR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 475 KIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVlsrLLGQTDVAvyGVAVPGVE----G 549
Cdd:PRK07787 339 PDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETA---LLGHPGVR--EAAVVGVPdddlG 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 550 KAGMAAIAdPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREG 608
Cdd:PRK07787 414 QRIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
247-311 |
4.37e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.50 E-value: 4.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743554 247 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDC----LPLYHSAGNIMGVGQCVIYGLTV 311
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
105-293 |
9.35e-04 |
|
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: 42.20 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 105 TFAQLDTYSNAVANLFRQLGF--APGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 182
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPE----WIISELACYAYSLVTV-----PLYDTLGPEAIEYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 183 GEMaaavaevseqlgkSLLkFCSGDLGPESIlpdTQLLDpMLAEAPTTPLAQAPgkgmdDRLFYI-YTSGTTGLPKAAIV 261
Cdd:cd05927 78 AEI-------------SIV-FCDAGVKVYSL---EEFEK-LGKKNKVPPPPPKP-----EDLATIcYTSGTTGNPKGVML 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 1268743554 262 VH----SRYYRIAAFGHHSYSMRAADVLYDCLPLYH 293
Cdd:cd05927 135 THgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
116-298 |
1.27e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.91 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 116 VANLFRQLGFAPGDVVAVfLEGRPEFV-----GLWLglakAGVVAALLNVNLRREPLAF-------CLGTSAAKALIYGG 183
Cdd:PRK07768 42 IAGGLAAAGVGPGDAVAV-LAGAPVEIaptaqGLWM----RGASLTMLHQPTPRTDLAVwaedtlrVIGMIGAKAVVVGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 184 EMAAAvAEVSEQLGKSLLkfcsgdlgpesilpdtqLLDPMLAEAPTTPlaqaPGKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:PRK07768 117 PFLAA-APVLEEKGIRVL-----------------TVADLLAADPIDP----VETGEDDLALMQLTSGSTGSPKAVQITH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1268743554 264 SR-YYRIAAfghhsysMRAA-------DVLYDCLPLYHSAGNI 298
Cdd:PRK07768 175 GNlYANAEA-------MFVAaefdvetDVMVSWLPLFHDMGMV 210
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
219-413 |
1.41e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 41.62 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 219 LLDPMLAEAPTTPlaqapgkgmDDRLFYIYTSGTTGLPKAaiVVHS---------RYYRIAAFGHHSYSMRAadvlydcL 289
Cdd:PRK08043 352 LLMPRLAQVKQQP---------EDAALILFTSGSEGHPKG--VVHShksllanveQIKTIADFTPNDRFMSA-------L 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743554 290 PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCV-KYNCTVV----QYIGEICRYllRQPVrdveQRHRVRLAVGN 364
Cdd:PRK08043 414 PLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNYARF--ANPY----DFARLRYVVAG 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743554 365 GLRPA-----IWEEftqRFGVpQIGEFYGATECNCSIA---NMDGKVGSCGfnsRIL 413
Cdd:PRK08043 488 AEKLQestkqLWQD---KFGL-RILEGYGVTECAPVVSinvPMAAKPGTVG---RIL 537
|
|
| |
