|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
115-622 |
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 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 194
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtQLLDPMLAEAPTTPLAQaPGKGMDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05939 82 ----------------------------------NLLDPLLTQSSTEPPSQ-DDVNFRDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 354
Cdd:cd05939 127 SRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 355 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 434
Cdd:cd05939 207 LLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 435 VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 514
Cdd:cd05939 287 VDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 515 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPI 594
Cdd:cd05939 367 FKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQ 446
|
490 500
....*....|....*....|....*...
gi 1907189407 595 FLRLLPQVDTTGTFKIQKTRLQREGFDP 622
Cdd:cd05939 447 FIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
53-657 |
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 1907189407 53 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGDTIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 132
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSI--SYAELNARANRYAHWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 133 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 212
Cdd:PRK08279 81 ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 213 kFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHhSYSMR 291
Cdd:PRK08279 161 -LWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGG-LLRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 292 AADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL 371
Cdd:PRK08279 239 PDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 372 AVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHvyPIRLVKVNEDTMEPLRDSEGLCI 451
Cdd:PRK08279 319 MIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRCI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 452 PCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVS 531
Cdd:PRK08279 397 KVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 532 TTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 610
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKY 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1907189407 611 QKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDERVHARICAGDFSL 657
Cdd:PRK08279 554 RKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
115-622 |
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: 649.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 194
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05940 82 ----------------------------------------------------------DAALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 354
Cdd:cd05940 104 RRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 355 LLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 434
Cdd:cd05940 184 LLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 435 VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 514
Cdd:cd05940 264 YDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 515 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQ-LDPNSMYQELQKVLASYARP 593
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEeFDLSALAAHLEKNLPGYARP 420
|
490 500
....*....|....*....|....*....
gi 1907189407 594 IFLRLLPQVDTTGTFKIQKTRLQREGFDP 622
Cdd:cd05940 421 LFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
116-644 |
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 1907189407 116 TFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 194
Cdd:cd05938 7 TYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EMAAAVAEVSEQLGKSLLKFcsGDLGPESILPDTQLLDPMLAEAPTTPLAQ---APGKGMDDRLfYIYTSGTTGLPKAAI 271
Cdd:cd05938 87 ELQEAVEEVLPALRADGVSV--WYLSHTSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTGLPKAAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 272 VVHSRYYRIAAFgHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEI 351
Cdd:cd05938 164 ISHLRVLQCSGF-LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 352 CRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIR 431
Cdd:cd05938 243 LRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 432 LVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDPlrrFDGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDEL 510
Cdd:cd05938 323 LIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAGDKEqTEKKLLRDVFKKGDVYFNTGDLLVQDQQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 511 GYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI--ADPHsQLDPNSMYQELQKVLA 588
Cdd:cd05938 400 NFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPGH-EFDGKKLYQHVREYLP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 589 SYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYVPLDE 644
Cdd:cd05938 479 AYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTP 534
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
115-622 |
1.68e-139 |
|
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: 1.68e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFR-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYg 193
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 gemaaavaevseqlgksllkfcsgdlgpesilpdtqllDPmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVV 273
Cdd:cd05937 85 --------------------------------------DP------------------DDPAILIYTSGTTGLPKAAAIS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 274 HSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 353
Cdd:cd05937 109 WRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 354 YLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANM---DGKVGSCGFNSRILTHVY-- 428
Cdd:cd05937 189 YLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAGAIGHHGLIRRWKFen 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 429 PIRLVKVNEDTMEPLRD-SEGLCIPCQPGEPGLLVGQINqQDPLRRFDGYVSDS-ATNKKIAHSVFRKGDSAYLSGDVLV 506
Cdd:cd05937 269 QVVLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVP-FKNREAFQGYLHNEdATESKLVRDVFRKGDIYFRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 507 MDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-----ADPHSQLDPNSMYQ 581
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAItleesSAVPTEFTKSLLAS 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907189407 582 ELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 622
Cdd:cd05937 428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-618 |
3.39e-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: 3.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:COG0318 4 LLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIYggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgm 251
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 ddrLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAS 331
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 332 RFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIA- 408
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPVVTv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 409 ----NMDGKVGSCGfnsRILTHVyPIRLVkvnedtmeplrDSEGlcIPCQPGEPGLLVGQINQQdplrrFDGYVSD-SAT 483
Cdd:COG0318 259 npedPGERRPGSVG---RPLPGV-EVRIV-----------DEDG--RELPPGEVGEIVVRGPNV-----MKGYWNDpEAT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 484 NKKIAHSVFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAG 563
Cdd:COG0318 317 AEAFRDGWLR-------TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE-KWGERV 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 564 MAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 618
Cdd:COG0318 389 VAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
114-616 |
1.93e-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: 263.77 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 114 CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtsaakaliyg 193
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGD----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 gEMAAAVAEVseqlgksllkfcsgdlGPESILPDTQLLdpmlaeapttplaqapgkgmddrlfyIYTSGTTGLPKAAIVV 273
Cdd:cd05934 66 -ELAYIIDHS----------------GAQLVVVDPASI--------------------------LYTSGTTGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 274 HSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 353
Cdd:cd05934 103 HANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 354 YLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN---MDGKVGSCGfnsrilthvYPI 430
Cdd:cd05934 183 YLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGSIG---------RPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 431 RLVKVNedtmepLRDSEGLciPCQPGEPGLLVgqINQQDPLRRFDGYVSD-SATNKKIAHSVFRKGDSAYlsgdvlvMDE 509
Cdd:cd05934 253 PGYEVR------IVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNMpEATAEAMRNGWFHTGDLGY-------RDA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 510 LGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLAS 589
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*..
gi 1907189407 590 YARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
85-628 |
4.53e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 258.53 E-value: 4.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 85 AGDTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 164
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 165 VAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVseqlgksllkfcsgDLGPESiLPDTQLLD------------ 232
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--------------DPGDLP-LPAVWLLDapasvsvpagws 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 233 --PMLA-EAPTTPLAQAPGkgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNI 309
Cdd:PRK06155 162 taPLPPlDAPAPAAAVQPG----DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 310 MGVgQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRF 389
Cdd:PRK06155 238 AFF-QALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 390 GVPQIgEFYGATECNCSIANM--DGKVGSC-----GFNSRILthvypirlvkvnedtmeplrDSEGLCIPcqPGEPGLLV 462
Cdd:PRK06155 317 GVDLL-DGYGSTETNFVIAVThgSQRPGSMgrlapGFEARVV--------------------DEHDQELP--DGEPGELL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 463 GQINQqdPLRRFDGYVSDSATnkkiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 542
Cdd:PRK06155 374 LRADE--PFAFATGYFGMPEK------TVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 543 LGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 622
Cdd:PRK06155 446 PAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
....*.
gi 1907189407 623 rQTSDR 628
Cdd:PRK06155 526 -DTWDR 530
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
93-526 |
4.33e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 217.57 E-value: 4.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 93 FQAVARRQPERLALVDASsGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 172
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 173 LRREPLAFCLGTSAAKALIYGGE-MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQApgkgm 251
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKK 327
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 328 FSA---SRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVEQRHRVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATE 402
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGApkRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIANMD------GKVGSCGfnsRILTHVypiRLVKVNEDTMEPLRdseglcipcqPGEPG-LLVGQINQqdplrrFD 475
Cdd:pfam00501 314 TTGVVTTPLpldedlRSLGSVG---RPLPGT---EVKIVDDETGEPVP----------PGEPGeLCVRGPGV------MK 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 476 GYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 526
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 ... |
253-611 |
1.00e-59 |
|
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: 203.29 E-value: 1.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSASR 332
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 333 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATECNCSIA-- 408
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 409 ---NMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQPGEPGLLVGQINQqdplrRFDGYVSDSATNK 485
Cdd:cd04433 159 ppdDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 486 kiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA 565
Cdd:cd04433 217 ------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907189407 566 AI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQ 611
Cdd:cd04433 290 VVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
97-653 |
2.20e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 208.34 E-value: 2.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQLGFAPGDV-VAVFLEGRPEFVgLWLGLAK-AGVVAALLNvNLR 174
Cdd:PRK13388 11 DRAGDDTIAV--RYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAAlGGYVLVGLN-TTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 175 ReplafclgtsaakaliyGGEMAAAVAEVSEQL------GKSLLKfcsgDLGpesiLPDTQLLD---PMLAE--APTTPL 243
Cdd:PRK13388 87 R-----------------GAALAADIRRADCQLlvtdaeHRPLLD----GLD----LPGVRVLDvdtPAYAElvAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 244 AQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV 323
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 324 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATEC 403
Cdd:PRK13388 222 LPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGYGSSEG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 404 NCSIANMDGK-VGSCGfnsrilthvypiR----LVKVNEDTMEPlrdseglCIPCQPGEPGLL------VGQINQQDPLR 472
Cdd:PRK13388 301 AVIVVREPGTpPGSIG------------RgapgVAIYNPETLTE-------CAVARFDAHGALlnadeaIGELVNTAGAG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 473 RFDGYVSD-SATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 551
Cdd:PRK13388 362 FFEGYYNNpEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVY 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 552 GVAVPGVeGKAGMAAI--ADPHSqLDPNSMYQEL--QKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFdpRQTSD 627
Cdd:PRK13388 435 AVPDERV-GDQVMAALvlRDGAT-FDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW--ATGDP 510
|
570 580
....*....|....*....|....*.
gi 1907189407 628 RLFFLDLKQGRYVPLDERVHARICAG 653
Cdd:PRK13388 511 VTLWVRRGGPAYRLMSEPAKAALAAE 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
142-621 |
1.92e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 194.51 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 142 VAVFLEGRPEFvGLWLGLAK-AGVVAALLNVNLRREPLA---------FCLGTSAAKALIYGGEMAAAVAEVSEQlgksl 211
Cdd:PRK07867 57 VGVLLDNTPEF-SLLLGAAAlSGIVPVGLNPTRRGAALArdiahadcqLVLTESAHAELLDGLDPGVRVINVDSP----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 212 lkfcsgdlgpesilPDTQLLDPmLAEAPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGH---HSY 288
Cdd:PRK07867 131 --------------AWADELAA-HRDAEPPFRVADP----DDLFMLIFTSGTSGDPKAVRCTHRK---VASAGVmlaQRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 289 SMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHR 368
Cdd:PRK07867 189 GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 369 VRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANM-DGKVGSCGfnsrilthVYPIRLVKVNEDTMEPlrdse 447
Cdd:PRK07867 269 LRIVYGNEGAPGDIARFARRFGC-VVVDGFGSTEGGVAITRTpDTPPGALG--------PLPPGVAIVDPDTGTE----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 448 glCIPCQPGEPGLL-----VGQ-INQQDPlRRFDGYVSDS-ATNKKIAHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSG 520
Cdd:PRK07867 335 --CPPAEDADGRLLnadeaIGElVNTAGP-GGFEGYYNDPeADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 521 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMAAIA-DPHSQLDPNSMYQEL--QKVLASYARPIFLR 597
Cdd:PRK07867 405 DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV-GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVR 483
|
490 500
....*....|....*....|....
gi 1907189407 598 LLPQVDTTGTFKIQKTRLQREGFD 621
Cdd:PRK07867 484 VCAELPRTATFKVLKRQLSAEGVD 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
86-616 |
1.46e-50 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 183.73 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 86 GDTIPCIFQAVARRQPERLALV-DASSGIC--WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 162
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfESSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 163 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESIlPDTQLLDPMLAEAPTTp 242
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPAD-DGVSSFTQLKAQQPAT- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 243 LAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHHSY---SMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 319
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 320 LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVR-----LAVGNGLRpaiwEEFTQRFGVpQI 394
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEERFGV-RL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 GEFYGATEcncSIANMDG----------KVGSCGFNsrilthvYPIRLVKVNEDTMEPLRDSEgLCIpcqPGEPGLLVgq 464
Cdd:PRK08008 316 LTSYGMTE---TIVGIIGdrpgdkrrwpSIGRPGFC-------YEAEIRDDHNRPLPAGEIGE-ICI---KGVPGKTI-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 465 inqqdplrrFDGYVSD-SATNKKI-AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 542
Cdd:PRK08008 380 ---------FKEYYLDpKATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 543 LGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:PRK08008 444 PKIQDIVVVGIKDS-IRDEAIKAfVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
97-612 |
3.17e-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: 180.50 E-value: 3.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:cd17631 5 ARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLF 256
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDD 336
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 337 CVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFtQRFGVpQIGEFYGATECNCSIANMD--- 411
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGV-KFVQGYGMTETSPGVTFLSped 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 412 --GKVGSCGfnsRILTHVyPIRLVKVNEDtmeplrdseglciPCQPGEpgllVGQINQQDPLrRFDGYVSDSATNKKiah 489
Cdd:cd17631 261 hrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAGYWNRPEATAA--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 490 sVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA 568
Cdd:cd17631 316 -AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAVVV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907189407 569 -DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 612
Cdd:cd17631 391 pRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
105-611 |
8.36e-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: 8.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 105 ALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 184
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 185 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLgPESILPDTQLLDPmLAEAPTTPLAQAPGKGMDDRLFYIYTSGTT 264
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDK-PDGVLSIEDLLSP-TLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 265 GLPKAAIVVHSRYyrIA----AFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGqCVIYGLTVVLRKKFSASRFWDDCVKY 340
Cdd:cd05911 159 GLPKGVCLSHRNL--IAnlsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 341 NCTVVQYIGEICRYLLRQPVRDVEQRHRVR-LAVGNG-LRPAIWEEFTQRFGVPQIGEFYGATECNCSIA---NMDGKVG 415
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 416 SCGfnsrILTHVYPIRLvkVNEDTMEPLrdseglcipcQPGEPG-LLV--GQInqqdplrrFDGYVSD-SATNKKIAHSV 491
Cdd:cd05911 316 SVG----RLLPNVEAKI--VDDDGKDSL----------GPNEPGeICVrgPQV--------MKGYYNNpEATKETFDEDG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 492 FRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIA-DP 570
Cdd:cd05911 372 WLH------TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVrKP 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907189407 571 HSQLDPNSMYQELQKVLASY----ARPIFLRLLPQvdtTGTFKIQ 611
Cdd:cd05911 445 GEKLTEKEVKDYVAKKVASYkqlrGGVVFVDEIPK---SASGKIL 486
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
88-618 |
4.37e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.83 E-value: 4.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA 167
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksLLKFC--SGDLGPESILPDTQLLDPMLAEAPTTPLaq 245
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLP--TVRTVivEGDGPAAPLAPEVGEYEELLAAASDTFD-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 246 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGniMGVGQCVIY-GLTVVL 324
Cdd:PRK06187 161 FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPYLALMaGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 325 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVpQIGEFYGATE 402
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CncsianmdGKVGSCGFNSRILTHVYPIRL----------VKVNEDTMEPLrdseglciPCQPGEPGLLV--GQINQQdp 470
Cdd:PRK06187 318 T--------SPVVSVLPPEDQLPGQWTKRRsagrplpgveARIVDDDGDEL--------PPDGGEVGEIIvrGPWLMQ-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 471 lrrfdGYVSD-SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 549
Cdd:PRK06187 380 -----GYWNRpEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 550 VYGV----------AVpgVEGKAGMaaiadphsQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqRE 618
Cdd:PRK06187 448 VIGVpdekwgerpvAV--VVLKPGA--------TLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
97-626 |
1.07e-46 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 173.76 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDAS---SGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 173
Cdd:COG0365 19 AEGRGDKVALIWEGedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 174 RREPLAFCLGTSAAKALI------YGG---EMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTT-PL 243
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglRGGkviDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEfEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 244 AQAPGkgmDDRLFYIYTSGTTGLPKAaiVVHS-RYYRIAA--FGHHSYSMRAADVLY---DClplyhsaGNIMGVGQCVI 317
Cdd:COG0365 179 EPTDA---DDPLFILYTSGTTGKPKG--VVHThGGYLVHAatTAKYVLDLKPGDVFWctaDI-------GWATGHSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 318 YGL----TVVL---RKKF-SASRFWDDCVKYNCTVvqyigeIC------RYLLRQPVRDVEQRHRVRL----AVGNGLRP 379
Cdd:COG0365 247 GPLlngaTVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDLSSLrllgSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 380 AIWEEFTQRFGVPqIGEFYGATECNCSIAN----MDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGlcIPCQP 455
Cdd:COG0365 321 EVWEWWYEAVGVP-IVDGWGQTETGGIFISnlpgLPVKPGSMGK---------PVPGYDVA------VVDEDG--NPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 456 GEPGLLVgqinqqdpLRR-----FDGYVSDSATNKKiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 530
Cdd:COG0365 383 GEEGELV--------IKGpwpgmFRGYWNDPERYRE---TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 531 STTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNsMYQELQ----KVLASYARP---IFLRLLPq 601
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAfvVLKPGVEPSDE-LAKELQahvrEELGPYAYPreiEFVDELP- 527
|
570 580
....*....|....*....|....*..
gi 1907189407 602 vdTTGTFKIQKTRLQR--EGFDPRQTS 626
Cdd:COG0365 528 --KTRSGKIMRRLLRKiaEGRPLGDTS 552
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
78-553 |
3.68e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 162.79 E-value: 3.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 78 ELRRHRRagDTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWL 157
Cdd:PRK08316 4 RSTRARR--QTIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 158 GLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKS---LLKFCSGDLGPESILPDTQLLDpm 234
Cdd:PRK08316 80 ACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtliLSLVLGGREAPGGWLDFADWAE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 235 lAEAPTTPLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYR-IAAFGhhsysMRAADVLYDCLPLYHSAGni 309
Cdd:PRK08316 158 -AGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHraliAEYVScIVAGD-----MSADDIPLHALPLYHCAQ-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 310 MGV--GQCVIYGLTVVLRKKFSASRFWDDCVKYNC-------TVvqYIGeicryLLRQPVRDveqrhRVRLAvgnGLRPA 380
Cdd:PRK08316 227 LDVflGPYLYVGATNVILDAPDPELILRTIEAERItsffappTV--WIS-----LLRHPDFD-----TRDLS---SLRKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 381 ----------IWEEFTQRFgvPQIG--EFYGATEcncsIA---------NMDGKVGSCG---FN--SRIlthvypirlvk 434
Cdd:PRK08316 292 yygasimpveVLKELRERL--PGLRfyNCYGQTE----IAplatvlgpeEHLRRPGSAGrpvLNveTRV----------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 435 VNEDtMEPLrdseglcipcQPGEPGLLVGQINQQdplrrFDGYVSDSAtnkKIAHSvFRKGdsAYLSGDVLVMDELGYMY 514
Cdd:PRK08316 355 VDDD-GNDV----------APGEVGEIVHRSPQL-----MLGYWDDPE---KTAEA-FRGG--WFHSGDLGVMDEEGYIT 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907189407 515 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:PRK08316 413 VVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
101-615 |
5.43e-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: 5.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALI--YGGEMAA---------AVAEVSEQLGKSLLKFCSGDLGPesilpdtqlLDPMLAEAPTTPLAQAPgk 249
Cdd:cd05926 81 YLADLGSKLVLtpKGELGPAsraasklglAILELALDVGVLIRAPSAESLSN---------LLADKKNAKSEGVPLPD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 250 gmDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRK 326
Cdd:cd05926 150 --DLALI-LHTSGTTGRPKGVPLTHR---NLAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 327 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFTQRFGVPQIgEFYGATE- 402
Cdd:cd05926 224 RFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPpklRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEa 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 -----CNCSIANMDgKVGSCGFNS----RILthvypirlvkvnedtmeplrDSEGLciPCQPGEpgllVGQINQQDPlRR 473
Cdd:cd05926 303 ahqmtSNPLPPGPR-KPGSVGKPVgvevRIL--------------------DEDGE--ILPPGV----VGEICLRGP-NV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 474 FDGYVSDSATNKKIAHSV--FRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 551
Cdd:cd05926 355 TRGYLNNPEANAEAAFKDgwFRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAF 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 552 GVAVPgVEGKAGMAAI-ADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRL 615
Cdd:cd05926 428 GVPDE-KYGEEVAAAVvLREGASVTEEELRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
88-616 |
4.37e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 159.68 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 167
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLaeAPTTPLAQ 245
Cdd:PRK07656 82 VVPLNTRYTAdeAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFL--AAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 246 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLR 325
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPQIGEFYGATEC 403
Cdd:PRK07656 240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 404 nCSIANM-----DGKV--GSCGfnsrilthvYPIRLVKvnedtmepLRDSEGLCIPCQPGEPGLLVgqinqqdpLRRFD- 475
Cdd:PRK07656 320 -SGVTTFnrlddDRKTvaGTIG---------TAIAGVE--------NKIVNELGEEVPVGEVGELL--------VRGPNv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 476 --GYVSDS-ATnkkiAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 552
Cdd:PRK07656 374 mkGYYDDPeAT----AAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 553 VAVPGVeGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPqVDTTGtfKIQKTRLQ 616
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 ... |
115-615 |
5.60e-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: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 194
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EmaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05972 81 E---------------------------------------------------------DPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 SryyriAAFGHHSYS-----MRAADVLY---DCLPLYHSAGNIMGVgqcVIYGLTVVL--RKKFSASRFWDDCVKYNCTV 344
Cdd:cd05972 104 S-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 345 VQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIAN---MDGKVGSC 417
Cdd:cd05972 176 FCGPPTAYRMLIKQ---DLSSYKFSHLrlvvSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNfpdMPVKPGSM 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 418 GFNsrilTHVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKiahsVFRKGds 497
Cdd:cd05972 252 GRP----TPGYDVAII-----------DDDGR--ELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEA----SIRGD-- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 498 AYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPN 577
Cdd:cd05972 306 YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAFVVLTSGYEPSE 384
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907189407 578 SMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
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 ... |
92-612 |
2.48e-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: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALV---DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 168
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 169 LNVNLRREPLAFCLGTSAAKALIYGGE--MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMlAEAPTTPLAQA 246
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNA-SPDFERPTANS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 247 PGKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYriaAFGHHSYSMRAADVLYDCLplyHSAGNIMGVGQCV---IYG---- 319
Cdd:cd05970 181 YPCGEDILLVY-FSSGTTGMPK--MVEHDFTY---PLGHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGqwia 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 320 ---LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRhRVRLAV--GNGLRPAIWEEFTQRFGVpQI 394
Cdd:cd05970 252 gaaVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS-SLRYCTtaGEALNPEVFNTFKEKTGI-KL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 GEFYGATECNCSIAN---MDGKVGSCGFNsrilTHVYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINQQDPL 471
Cdd:cd05970 330 MEGFGQTETTLTIATfpwMEPKPGSMGKP----APGYEIDLI-----------DREGR--SCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 472 RRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 551
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 552 GVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQK 612
Cdd:cd05970 467 GVPDP-IRGQVVKATIVLAKGYEPSEELKKELQdhvkKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
92-616 |
1.05e-39 |
|
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: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:cd05936 4 LLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLkfcsgdlgpesilpdtqlldPMLAEAPTTPlaqapgkgm 251
Cdd:cd05936 82 LYTPRELEHILNDSGAKALI--------VAVSFTDLLAAGA--------------------PLGERVALTP--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSY--SMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFS 329
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 330 ASRFWDDCVKYNCTVVQ-----YIGeicryLLRQPVRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATE 402
Cdd:cd05936 205 PIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIA-N-MDG--KVGSCGfnsrilthvYPIRLVKVNedtmepLRDSEGLCIPcqPGEPGLLVgqinqqdpLR---RFD 475
Cdd:cd05936 279 TSPVVAvNpLDGprKPGSIG---------IPLPGTEVK------IVDDDGEELP--PGEVGELW--------VRgpqVMK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 476 GYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAV 555
Cdd:cd05936 334 GYWNRPEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPD 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 556 P--GVEGKAgmAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLQ 616
Cdd:cd05936 408 PysGEAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPrqvEFRDELPK-SAVG--KILRRELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
116-616 |
1.08e-34 |
|
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: 136.82 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlFYIYTSGTTGLPKAAIVVHS 275
Cdd:cd05919 92 DIA---------------------------------------------------------YLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 276 RYYRIA-AFGHHSYSMRAADVLYDCLPLYHSAG---NIMGVGQCviyGLTVVLRKKF-SASRFWDDCVKYNCTVVQYIGE 350
Cdd:cd05919 115 DPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGlgnSLWFPLAV---GASAVLNPGWpTAERVLATLARFRPTVLYGVPT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 351 ICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEFYGATEC-NCSIANMDGKV--GSCGfnsRILT 425
Cdd:cd05919 192 FYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGGP-ILDGIGATEVgHIFLSNRPGAWrlGSTG---RPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 426 HvYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPlrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVL 505
Cdd:cd05919 268 G-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRA----TFNGG--WYRTGDKF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 506 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAAIADPHSQLDPN-----SMY 580
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPAAPQeslarDIH 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907189407 581 QELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
53-604 |
3.06e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 137.37 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 53 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGdTIPcifQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 132
Cdd:PRK07788 19 HYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFA-GLV---AHAARRAPDRAALIDERGTL--TYAELDEQSNALARGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 133 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 212
Cdd:PRK07788 93 ALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 213 KFCSGDLGPESIlPDTQLLDPMLAEAPTTPLAQAPGKGMddrlFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHsYSMR 291
Cdd:PRK07788 173 WGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEpSPLAPLAGLLSR-VPFR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 292 AADVLYDCLPLYHSagniMGVGQCVI---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRH- 367
Cdd:PRK07788 247 AGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLG-PEVLAKYd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 368 ----RVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECN-CSIANMD------GKVGScgfnsrilthvyPIRLVKVN 436
Cdd:PRK07788 322 tsslKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAfATIATPEdlaeapGTVGR------------PPKGVTVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 437 edtmepLRDSEGLCIPcqPGEPG-LLVGQINQqdplrrFDGYVSDSatNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYF 515
Cdd:PRK07788 389 ------ILDENGNEVP--RGVVGrIFVGNGFP------FEGYTDGR--DKQIIDGLLSSGDVGYF-------DEDGLLFV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 516 RDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARP 593
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDEDAIKDYVRDNLARYKVP 523
|
570
....*....|....
gi 1907189407 594 ---IFLRLLPQVDT 604
Cdd:PRK07788 524 rdvVFLDELPRNPT 537
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
97-618 |
3.34e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 133.55 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK03640 12 AFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKfcsgdlgpesilpdtqlldpmLAEAPTTPLAQAPgkgmDDRLF 256
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMN---------------------GPKEEAEIQEEFD----LDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YI-YTSGTTGLPKAAivvhsryyrIAAFGHHSYS---------MRAADVLYDCLPLYHSAG-NIMGVGqcVIYGLTVVLR 325
Cdd:PRK03640 145 TImYTSGTTGKPKGV---------IQTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGlSILMRS--VIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 KKFSASRFWDDCVKYNCT---VVQyigeicrYLLRQPVRDVEQRH-----RVRLaVGNGLRPAIWEEFTQRFGVPQIgEF 397
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTiisVVS-------TMLQRLLERLGEGTypssfRCML-LGGGPAPKPLLEQCKEKGIPVY-QS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 398 YGATECNCSIANMD-----GKVGSCG---FNSRIlthvypirlvKVNEDTMEplrdseglCIPCQPGE-----PGLLVGQ 464
Cdd:PRK03640 285 YGMTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvkgPNVTKGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 465 INQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 544
Cdd:PRK03640 347 LNRED------------ATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPG 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 545 QTDVAVYGVAvpgvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQRE 618
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 ... |
92-615 |
4.25e-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: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSL--TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKF-CSGDLGPESILPD-TQLLD---PMLAEAPTTPlaqa 246
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLiVSGGAGPEAGALLlAELVAaeaEQLKPAATHA---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 247 pgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIY----GLT 321
Cdd:cd05959 163 -----DDPAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLRKKF-SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVpQIGEFY 398
Cdd:cd05959 234 TVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 399 GATEC-NCSIANMDGKV--GSCGfnsrILTHVYPIRLVkvnEDTMEPLRDSEglcipcqPGE-----PGLLVGQINQQDP 470
Cdd:cd05959 313 GSTEMlHIFLSNRPGRVryGTTG----KPVPGYEVELR---DEDGGDVADGE-------PGElyvrgPSSATMYWNNRDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 471 LRR-FDGYvsdsatnkkiahsvfrkgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQTDVA 549
Cdd:cd05959 379 TRDtFQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-----VQHPA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 550 VYGVAVPGVEGKAGM----AAIADPHSQLDPNSMYQELQK----VLASYARP---IFLRLLPQvdtTGTFKIQKTRL 615
Cdd:cd05959 434 VLEAAVVGVEDEDGLtkpkAFVVLRPGYEDSEALEEELKEfvkdRLAPYKYPrwiVFVDELPK---TATGKIQRFKL 507
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
97-566 |
3.42e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 127.89 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFcsgDLGPESILPDTQLLDPMLAEAPTTPLAQAP-GKGMddrl 255
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIADESlGTDM---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 256 fyIYTSGTTGLPKAAivvhsryYR------------IAAFGHHSYSMRAADVLYDCLPLYHSA-GNIMGVGQCViyGLTV 322
Cdd:PRK13391 160 --LYSSGTTGRPKGI-------KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL--GGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 323 VLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVrlavgNGLRPAIW----------EEFTQRFGvP 392
Cdd:PRK13391 229 IVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP-EEVRDKYDL-----SSLEVAIHaaapcppqvkEQMIDWWG-P 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 393 QIGEFYGATECN----CSIANMDGKVGSCGfnsRILTHVYPIRlvkvnEDTMEplrdseglciPCQPGEPgllvGQINQQ 468
Cdd:PRK13391 302 IIHEYYAATEGLgftaCDSEEWLAHPGTVG---RAMFGDLHIL-----DDDGA----------ELPPGEP----GTIWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 469 DPlRRFDgYVSDSAtnkKIAHSvfRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 547
Cdd:PRK13391 360 GG-RPFE-YLNDPA---KTAEA--RHPDGTWsTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAD 432
|
490 500 510
....*....|....*....|....*....|...
gi 1907189407 548 VAVYGV--------------AVPGVEGKAGMAA 566
Cdd:PRK13391 433 AAVFGVpnedlgeevkavvqPVDGVDPGPALAA 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-617 |
7.52e-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: 125.62 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 194
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeaptTPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05971 84 ----------------------------------------------TDGS-------DDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 sryyRIaAFGHhsysmraADVLYDCLPLYHSAGNIM----------GVGQCVI----YGLTVVLRK--KFSASRFWDDCV 338
Cdd:cd05971 111 ----RV-LLGH-------LPGVQFPFNLFPRDGDLYwtpadwawigGLLDVLLpslyFGVPVLAHRmtKFDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 339 KYNCTVVqYIGEICRYLLRQpVRDVEQRHRVRL-AVGNGLRPAIWEEF---TQRFGVPqIGEFYGATECNCSIAN----M 410
Cdd:cd05971 179 RYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLrAIATGGESLGEELLgwaREQFGVE-VNEFYGQTECNLVIGNcsalF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 411 DGKVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEPGLLVgqINQQDPLrRFDGYVSD-SATNKKIAH 489
Cdd:cd05971 256 PIKPGSMG-------KPIPGHRVAIVDDNGTPL----------PPGEVGEIA--VELPDPV-AFLGYWNNpSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 490 SVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIAD 569
Cdd:cd05971 316 DWLLTGDLGRKDSD-------GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP-IRGEIVKAFVVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 570 PHSQLDPNSMYQELQKV----LASYARPIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:cd05971 388 NPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
105-553 |
1.03e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 126.56 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 105 ALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 184
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 185 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPdtqlLDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGT 263
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPDTPIAdETAGADM------LYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 264 TGLPK---------AAIVVHSRYYRIAAFGHHSYsmrAADVLYDCLPLYHSAGN--IMGVGQCviyGLTVVLRKKFSASR 332
Cdd:PRK08276 152 TGRPKgikrplpglDPDEAPGMMLALLGFGMYGG---PDSVYLSPAPLYHTAPLrfGMSALAL---GGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 333 FWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVRlavgnGLRPAI----------------WeeftqrFGvPQIGE 396
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLP-EEVRARYDVS-----SLRVAIhaaapcpvevkramidW------WG-PIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 397 FYGATECN----CSIANMDGKVGSCGfnsRILTHVypirlVKVNEDTMEPLrdseglciPcqPGEPGLLVGQINQQDplr 472
Cdd:PRK08276 293 YYASSEGGgvtvITSEDWLAHPGSVG---KAVLGE-----VRILDEDGNEL--------P--PGEIGTVYFEMDGYP--- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 473 rFDgYVSDSATNKKIAHsvfRKGDSAYlsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 552
Cdd:PRK08276 352 -FE-YHNDPEKTAAARN---PHGWVTV--GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG 424
|
.
gi 1907189407 553 V 553
Cdd:PRK08276 425 V 425
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
97-616 |
1.04e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.07 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRre 176
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 plafclgtsaakaliyGGEMAAAVAEVSEQLgksLLkfcsGDLGPESILPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLF 256
Cdd:PRK09088 83 ----------------ASELDALLQDAEPRL---LL----GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVHSRYYRIAA-FGHHSYSMRAADVLYDClPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD 335
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQTAHnFGVLGRVDAHSSFLCDA-PMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 336 DCVKYNCTVVQYIG--EICRYLLRQPVRDVEQ-RHRVRLAVGNGLRPAI----WEE----FTQRFGVPQIGEFYGATeCN 404
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDdgipMVDGFGMSEAGTVFGMS-VD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 405 CSIanMDGKVGSCGfnsrILTHVYPIRLVKVNEdtmeplRDseglcipCQPGEPG--LLVGQinqqdplRRFDGYVSDSA 482
Cdd:PRK09088 298 CDV--IRAKAGAAG----IPTPTVQTRVVDDQG------ND-------CPAGVPGelLLRGP-------NLSPGYWRRPQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 483 TNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGvEGKA 562
Cdd:PRK09088 352 ATARA-----FTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ-WGEV 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 563 GMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:PRK09088 426 GYLAIVpADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
116-650 |
9.02e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 125.99 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLnvnlrrEPlafclgtsaakaliyGGE 195
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM------PP---------------DTD 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAAV--AEVSE------------QLGKSLLKFCSGD-----LGPESILPDTQLLDPMLAEAPTTplaQAPGKGMDDRLF 256
Cdd:PRK07868 533 LAAAVrlGGVTEiitdptnleaarQLPGRVLVLGGGEsrdldLPDDADVIDMEKIDPDAVELPGW---YRPNPGLARDLA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVHSRYyRIAAFGHHSY-SMRAADVLYdCL-PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFW 334
Cdd:PRK07868 610 FIAFSTAGGELVAKQITNYRW-ALSAFGTASAaALDRRDTVY-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 335 DDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG-K 413
Cdd:PRK07868 688 QEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaK 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 414 VGSCGfnsRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGqinqqdplrRFDGYVSDSATNKKiahSVFR 493
Cdd:PRK07868 768 IGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLA---------RARGPIDPTASVKR---GVFA 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 494 KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRlLGQTDVAV-YGVAVPGVEgkAGMAAIA-DPH 571
Cdd:PRK07868 833 PADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGR-IGGVDLAVtYGVEVGGRQ--LAVAAVTlRPG 909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 572 SQLDPnsmyQELQKVLASYA---RPIFLRLLPQVDTTGTFKIQKTRLQREGFdPRqTSDRLFFLDLKQGRYVPLDERVHA 648
Cdd:PRK07868 910 AAITA----ADLTEALASLPvglGPDIVHVVPEIPLSATYRPTVSALRAAGI-PK-PGRQAWYFDPETNRYRRLTPAVRA 983
|
..
gi 1907189407 649 RI 650
Cdd:PRK07868 984 EL 985
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
90-554 |
3.45e-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: 121.85 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 90 PCIFQAVAR---RQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 166
Cdd:cd05923 1 QTVFEMLRRaasRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 167 ALLNVNLRREPLAFClgtsaakalIYGGEMAAAVAEVSEQlgksllkfcsgdLGPESILPDTQLL----DPMLAEAPT-T 241
Cdd:cd05923 81 ALINPRLKAAELAEL---------IERGEMTAAVIAVDAQ------------VMDAIFQSGVRVLalsdLVGLGEPESaG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 242 PLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHS-YSMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 319
Cdd:cd05923 140 PLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 320 LTVVLRKKFSASRfwddcvkynctVVQYIGE---ICRYL-----------LRQPVRDVEQRHRVRLAvGNGLRPAIWEEF 385
Cdd:cd05923 220 GTYVVVEEFDPAD-----------ALKLIEQervTSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVLERV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 386 TQRFGVPQIgEFYGATECNCSIANMDGKVGSC---GFNSRilthvypIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLV 462
Cdd:cd05923 288 NQHLPGEKV-NIYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEALANGEEGELIVAAAADAAFT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 463 GQINQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYL--SGDVLVMDELGYMYFrdrSGdtfrwrGENVSTTEVEAVLS 540
Cdd:cd05923 360 GYLNQPE------------ATAKKLQDGWYRTGDVGYVdpSGDVRILGRVDDMII---SG------GENIHPSEIERVLS 418
|
490
....*....|....
gi 1907189407 541 RLLGQTDVAVYGVA 554
Cdd:cd05923 419 RHPGVTEVVVIGVA 432
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-618 |
6.81e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.34 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 86 GDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvv 165
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 166 AALLNVN--LRREPLAFCLGTSAAKALIYGGEMAAA--VAEVSEqLGKSLLKFCSGDLGPESiLPDTQLLDPMLAEAPTT 241
Cdd:PRK12583 95 AILVNINpaYRASELEYALGQSGVRWVICADAFKTSdyHAMLQE-LLPGLAEGQPGALACER-LPELRGVVSLAPAPPPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 242 PLA----QAPGKGM--------------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLY 303
Cdd:PRK12583 173 FLAwhelQARGETVsrealaerqasldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 304 HSAGNIMGVGQCVIYGLTVVL-RKKFSASRFWDDCVKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GN 375
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGImaGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 376 GLRPAIWEEFTQRFGVPQIGEFYGATECN------CSIANMDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGL 449
Cdd:PRK12583 328 PCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqtTAADDLERRVETVG---RTQPHLE----VKV--------VDPDGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 450 CIPcqPGEPGLLVgqinqqdplrrFDGYV-------SDSATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDT 522
Cdd:PRK12583 393 TVP--RGEIGELC-----------TRGYSvmkgywnNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 523 FRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLP 600
Cdd:PRK12583 454 IIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*...
gi 1907189407 601 QVDTTGTFKIQKTRLqRE 618
Cdd:PRK12583 532 EFPMTVTGKVQKFRM-RE 548
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
97-617 |
1.54e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALV------DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAlLN 170
Cdd:PRK07529 35 AARHPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP-IN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 171 VNLRREPLAFCLGTSAAKALIYGGEMAAA-----VAEVSEQL--GKSLLK-FCSGDLGPESILPDTQL----------LD 232
Cdd:PRK07529 114 PLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVLAALpeLRTVVEvDLARYLPGPKRLAVPLIrrkaharildFD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 233 PMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGV 312
Cdd:PRK07529 194 AELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 313 GQCVIYGLTVVL------RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVEQrhrVRLAVGNG--LRPAIW 382
Cdd:PRK07529 274 LAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVdgHDISS---LRYALCGAapLPVEVF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 383 EEFTQRFGVPqIGEFYGATECNC--SIANMDG--KVGSCGFnsRI-LTHVypiRLVKVNEDTmEPLRDseglcipCQPGE 457
Cdd:PRK07529 351 RRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGL--RLpYQRV---RVVILDDAG-RYLRD-------CAVDE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 458 PGLLVgqinQQDPlRRFDGYVsDSATNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 537
Cdd:PRK07529 417 VGVLC----IAGP-NVFSGYL-EAAHNKGL-----WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 538 VLSRLlgqtdvavygvavPGVegkAGMAAIA--DPHS--------QLDPNSMYQELQkvLASYAR---------PIFLRL 598
Cdd:PRK07529 486 ALLRH-------------PAV---ALAAAVGrpDAHAgelpvayvQLKPGASATEAE--LLAFARdhiaeraavPKHVRI 547
|
570
....*....|....*....
gi 1907189407 599 LPQVDTTGTFKIQKTRLQR 617
Cdd:PRK07529 548 LDALPKTAVGKIFKPALRR 566
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
93-620 |
2.50e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.13 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 93 FQAVARRQPERLAL-VDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:PRK07514 6 FDALRAAFADRDAPfIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPESilpdtqLLDpmLAEAPTTPLAQAPgKGM 251
Cdd:PRK07514 86 AYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV-ETLDADGTGS------LLE--AAAAAPDDFETVP-RGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSAs 331
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 332 rfwDDCVKY--NCTVVqyIGEICRY--LLRQPVRDVEQRHRVRLAVgNGLRPAIWE---EFTQRFGVPqIGEFYGATECN 404
Cdd:PRK07514 235 ---DAVLALmpRATVM--MGVPTFYtrLLQEPRLTREAAAHMRLFI-SGSAPLLAEthrEFQERTGHA-ILERYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 405 CSIAN-MDGK--VGSCGFnsrilthvyPIRLVKV---NEDTMEPLrdseglcipcQPGEpgllVGQINQQDPlRRFDGY- 477
Cdd:PRK07514 308 MNTSNpYDGErrAGTVGF---------PLPGVSLrvtDPETGAEL----------PPGE----IGMIEVKGP-NVFKGYw 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 -VSDsatnkKIAHSvFRkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 556
Cdd:PRK07514 364 rMPE-----KTAEE-FR-ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 557 GVeGKAGMAA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 620
Cdd:PRK07514 437 DF-GEGVTAVvVPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL-REQY 499
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
97-616 |
2.96e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 116.68 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK06178 43 ARERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGPESI---LPD---------TQLLDPMLAEAPTTPL 243
Cdd:PRK06178 121 ELSYELNDAGAEVLLALDQLAPVVEQVRAETSlRHVIVTSLADVLPAEPtlpLPDslraprlaaAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 244 AQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGL 320
Cdd:PRK06178 201 VPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 321 TVVLRKKFSASRFWDDCVKYNCT----VVQYIGEIC------RYLLR--QPVR--------DVEQRHRVRLAVGNGLRPA 380
Cdd:PRK06178 279 TLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVELMdhprfaEYDLSslRQVRvvsfvkklNPDYRQRWRALTGSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 381 IWeeftqrfgvpqigefyGATE---CNCSIANMdgKVGSCGFNSRILTHVYPI---RLVKVNEDTMEPLrdseglciPC- 453
Cdd:PRK06178 359 AW----------------GMTEthtCDTFTAGF--QDDDFDLLSQPVFVGLPVpgtEFKICDFETGELL--------PLg 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 454 QPGE-----PGLLVGQINQQDplrrfdgyvsdsATnkkiAHSvFRkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 528
Cdd:PRK06178 413 AEGEivvrtPSLLKGYWNKPE------------AT----AEA-LR--DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 529 NVSTTEVEAvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAIA----DPHSQLDPNSMYQELQKVLASYARPIfLRLLPQV 602
Cdd:PRK06178 474 SVFPSEVEA----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDAL 546
|
570
....*....|....
gi 1907189407 603 DTTGTFKIQKTRLQ 616
Cdd:PRK06178 547 PMTATGKVRKQDLQ 560
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
115-617 |
6.15e-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: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFclgtsaakaliygg 194
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtQLLDpmlAEApttplaqapgkGMDDRLFYIYTSGTTGLPKAAIVvh 274
Cdd:cd05912 68 ----------------------------------QLKD---SDV-----------KLDDIATIMYTSGTTGKPKGVQQ-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 sryyriaAFGHHSYSMRAADV---LYD------CLPLYHSAG-NIMGVGqcVIYGLTVVLRKKFSASRFWDDCVKYNCTV 344
Cdd:cd05912 98 -------TFGNHWWSAIGSALnlgLTEddnwlcALPLFHISGlSILMRS--VIYGMTVYLVDKFDAEQVLHLINSGKVTI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 345 VQYIGEICRYLLRQPVRDVEQRHRVRLaVGNGLRPAIWEEFTQRFGVPqIGEFYGATE-----CNCSIANMDGKVGSCG- 418
Cdd:cd05912 169 ISVVPTMLQRLLEILGEGYPNNLRCIL-LGGGPAPKPLLEQCKEKGIP-VYQSYGMTEtcsqiVTLSPEDALNKIGSAGk 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 419 --FNSRilthvypIRLVKVNEDtmeplrdseglciPCQPGE-----PGLLVGQINQQDplrrfdgyvsdsATNKKIAHSV 491
Cdd:cd05912 247 plFPVE-------LKIEDDGQP-------------PYEVGEillkgPNVTKGYLNRPD------------ATEESFENGW 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 492 FRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA--D 569
Cdd:cd05912 295 FKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VGIP--DDKWGQVPVAfvV 363
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 570 PHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLQR 617
Cdd:cd05912 364 SERPISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
94-617 |
1.05e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.19 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 94 QAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFR-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 172
Cdd:PRK06839 9 EKRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 173 LRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESILPDTQLLDPmlAEAPTTPLAQAPGKGMD 252
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQ---------------KVSYVQRVISITSL--KEIEDRKIDNFVEKNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASR 332
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 333 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVgNGLRPA---IWEEFTQRfGVPqIGEFYGATECNCS--- 406
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCpeeLMREFIDR-GFL-FGQGFGMTETSPTvfm 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 IANMDG--KVGSCG----FNSrilthvypIRLVKVNEDTMEplrdseglcipcqPGEpgllVGQINQQDPLRRFDGYVSD 480
Cdd:PRK06839 307 LSEEDArrKVGSIGkpvlFCD--------YELIDENKNKVE-------------VGE----VGELLIRGPNVMKEYWNRP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 481 SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE- 559
Cdd:PRK06839 362 DATEETIQ-------DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHVKw 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 560 GKAGMAAIA-DPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvDTTGtfKIQKTRLQR 617
Cdd:PRK06839 433 GEIPIAFIVkKSSSVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
97-618 |
2.67e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK06145 12 ARRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksllkfcsgdLGPESILPDTQLLDPMLAEAPTTPLAQapgkgmDDRLF 256
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEFDAIVALETPKIV----------IDAAAQADSRRLAQGGLEIPPQAAVAP------TDLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVHSRYY-----RIAAFGhhsysMRAADVLYDCLPLYHsagnimgVGQCVIYGLTVV-------L 324
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHwksidHVIALG-----LTASERLLVVGPLYH-------VGAFDLPGIAVLwvggtlrI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 325 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLR-PAI-WEEFTQRFGVPQIGEFYGATE 402
Cdd:PRK06145 222 HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIRDFTRVFTRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIANMDG-----KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGLCIPcqPGEPGllvgQINQQDPlRRFDGY 477
Cdd:PRK06145 302 TCSGDTLMEAgreieKIGSTG---RALAHV-EIRI-----------ADGAGRWLP--PNMKG----EICMRGP-KVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 VSDSatnKKIAHSVFrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 557
Cdd:PRK06145 360 WKDP---EKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 558 VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 618
Cdd:PRK06145 434 WGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
87-615 |
1.49e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 110.99 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 87 DTIPCIFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 166
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 167 ALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGKSLLKFCSGDLGPESIlPDTQLLDPMLA---EA 238
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLRAIAVVDDAADAT-PAPAPGARVQLfalPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 239 PTTPLAQAPGKGMDDRLFYIY-TSGTTGLPKaaIVVHS-----RYYRIAAfghHSYSMRAADVLYDCLPLYHSAGNIMGV 312
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFtTSGTTSGPK--LVLHRqatllRHARAIA---RAYGYDPGAVLLAALPFCGVFGFSTLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 313 GqCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNgLRPAiWEEFTQRF--- 389
Cdd:PRK06164 242 G-ALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPA-LGELAALArar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 390 GVPQIGeFYGATECncsIANMDGKVGSCGFNSRIL---THVYPIRLVKVnedtmeplRDSEGLCIpCQPGEPgllvGQIN 466
Cdd:PRK06164 319 GVPLTG-LYGSSEV---QALVALQPATDPVSVRIEgggRPASPEARVRA--------RDPQDGAL-LPDGES----GEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 467 QQDPlRRFDGYVSD-SATNKKI-AHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 544
Cdd:PRK06164 382 IRAP-SLMRGYLDNpDATARALtDDGYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 545 QTDVAVYGVAvpgVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASY---ARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:PRK06164 454 VAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPVTESANGAKIQKHRL 526
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
80-618 |
1.65e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.99 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 80 RRHRRAG----DTIPCIFQAVARRQPERLALVDaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 155
Cdd:PRK06087 12 AAYRQQGywgdASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 156 WLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG--------EMAAAVAEVSEQLGKSLLkfcSGDLGPE-SILP 226
Cdd:PRK06087 91 YLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVG---VDKLAPAtSSLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 227 DTQLLdpmlaeAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYriaaFGHHSYSMR----AADVLYDCLPL 302
Cdd:PRK06087 168 LSQII------ADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYCARlnltWQDVFMMPAPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 303 YHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVrDVEQRhRVRLAVGNGLR 378
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPA-DLSAL-RFFLCGGTTIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 379 PAIWEEfTQRFGVpQIGEFYGATE-CNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTmeplrdseglcIPCqpGE 457
Cdd:PRK06087 316 KKVARE-CQQRGI-KLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-----------LPP--GC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 458 PGLLVGQINQQdplrrFDGYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 536
Cdd:PRK06087 381 EGEEASRGPNV-----FMGYLDEpELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 537 AVLSRLLGQTDVAVygVAVP----GvEGKAGMAAIADPHSQLdpnsmyqELQKVLASYAR--------PIFLRLLPQVDT 604
Cdd:PRK06087 450 DILLQHPKIHDACV--VAMPderlG-ERSCAYVVLKAPHHSL-------TLEEVVAFFSRkrvakykyPEHIVVIDKLPR 519
|
570
....*....|....
gi 1907189407 605 TGTFKIQKTRLQRE 618
Cdd:PRK06087 520 TASGKIQKFLLRKD 533
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
70-618 |
1.91e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 110.91 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 70 SVLIRVRLElrRHRRAG----DTIPCIFQAVARRQPERLALVDASSGIC----WTFAQLDTYSNAVANLFRQLGFAPGDV 141
Cdd:PRK13295 5 AVLLPPRRA--ASIAAGhwhdRTINDDLDACVASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLARLGVGRGDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 142 VAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGK-SLLKFC 215
Cdd:PRK13295 83 VSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPELPAlRHVVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 216 SGDlGPESIlpDTQLLDPMLAEAP-TTPLAQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRIAAFghHSYSMR--- 291
Cdd:PRK13295 163 GGD-GADSF--EALLITPAWEQEPdAPAILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANI--VPYAERlgl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 292 -AADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWD----DCVKYNCTVVQYIGEICRyLLRQPVRDVEQR 366
Cdd:PRK13295 236 gADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTR-AVKESGRPVSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 367 hRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNC----SIANMDGKVGScgfnsrilTHVYPIRLVKVNedtmep 442
Cdd:PRK13295 315 -RTFLCAGAPIPGALVERARAALGA-KIVSAWGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 443 LRDSEGLCIPcqPGEPGLLV--GQINqqdplrrFDGYVSDSATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSG 520
Cdd:PRK13295 379 VVDADGAPLP--AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGRSK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 521 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA----DPHSQLDPNSM--YQELQKVLASYArPI 594
Cdd:PRK13295 443 DVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvpRPGQSLDFEEMveFLKAQKVAKQYI-PE 517
|
570 580
....*....|....*....|....
gi 1907189407 595 FLRLLPQVDTTGTFKIQKTRLQRE 618
Cdd:PRK13295 518 RLVVRDALPRTPSGKIQKFRLREM 541
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
116-615 |
3.08e-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: 109.01 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygge 195
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 maaavaeVSEQLGKsllkfcsgdlgpesilpdtqlldpmlaeapTTPLAQApgkgmDDRLFYIYTSGTTGLPKAAIVVHS 275
Cdd:cd05903 79 -------VPERFRQ------------------------------FDPAAMP-----DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 276 R-YYRIAAFGHHsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGE 350
Cdd:cd05903 117 TlSASIRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 351 ICRYLLRQPvrDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsianmdGKVGSC--GFNSRIL-THV 427
Cdd:cd05903 196 LLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECP-------GAVTSItpAPEDRRLyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 428 YPIRLVKVNedtmepLRDSEGLCIPcqPGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAHSVFrkgdsaYLSGDVLVM 507
Cdd:cd05903 266 RPLPGVEIK------VVDDTGATLA--PGV----EGELLSRGP-SVFLGYLDRPDLTADAAPEGW------FRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 508 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA-----DPHSqLDPNSMYQE 582
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DERLGERACAvvvtkSGAL-LTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....
gi 1907189407 583 LQKV-LASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05903 402 LDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
101-615 |
6.09e-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: 108.38 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSgiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 178
Cdd:cd05930 1 PDAVAVVDGDQ--SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG--AAYVPLDPSypAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIYGGEMAAAVaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlfyI 258
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDLAYV---------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 259 YTSGTTGLPKAAIVVHsryyriAAFGHHSYSMRAAdvlY-----DCLPLYHSAGNIMGVGQ---CVIYGLTVVLRKK--- 327
Cdd:cd05930 100 YTSGSTGKPKGVMVEH------RGLVNLLLWMQEA---YpltpgDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevr 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 328 FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATECNc 405
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEAT- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 406 sianmdgkvgscgfnsrILTHVYPIRLVKVNEDTM---EPLRDSEGL-----CIPCQPGEPG-LLVG--QINQqdplrrf 474
Cdd:cd05930 248 -----------------VDATYYRVPPDDEEDGRVpigRPIPNTRVYvldenLRPVPPGVPGeLYIGgaGLAR------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 475 dGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygV 553
Cdd:cd05930 304 -GYLNRPElTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV--V 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 554 AVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05930 381 AREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
93-610 |
9.15e-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: 9.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 93 FQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 172
Cdd:cd17651 1 FERQAARTPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 173 LRREPLAFCLGTSAAKALIyggemAAAVAevseqlgksllkfcSGDLGPESIlPDTQLLDPMLAEAPTTPLaqAPGKGMD 252
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL-----THPAL--------------AGELAVELV-AVTLLDQPGAAAGADAEP--DPALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHS----------RYYRIAAFGHHS-YSMRAADVlydclplyhSAGNIMGVgqcVIYGLT 321
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRslanlvawqaRASSLGPGARTLqFAGLGFDV---------SVQEIFST---LCAGAT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLRK---KFSASRFWDDCVKYNCTVV----QYIGEICRYLLRQPVRDVEQRHRV----RLAVGNGLRpaiweEFTQRFG 390
Cdd:cd17651 205 LVLPPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLR-----EFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 391 VPQIGEFYGATECNCSIA-NMDGKVGSCGFNSRILTHVYPIRLVKVNEDtmepLRdseglciPCQPGEPG-LLVGqinqQ 468
Cdd:cd17651 280 GLRLHNHYGPTETHVVTAlSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA----LR-------PVPPGVPGeLYIG----G 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 469 DPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 547
Cdd:cd17651 345 AGLAR--GYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 548 VAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 610
Cdd:cd17651 423 AVV--LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
97-550 |
1.10e-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: 108.09 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN-VNLRR 175
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 176 EpLAFCLGTSAAKALIyggeMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPmlAEAPTTPLAQapgkgmDDRL 255
Cdd:cd05904 95 E-IAKQVKDSGAKLAF----TTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADE--AEPPVVVIKQ------DDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 256 FYIYTSGTTGLPKAAIVVHSRYyrIAAF-GHHSY--SMRAADVLYDC-LPLYHSAGnIMGVGQCVI-YGLTVVLRKKFSA 330
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNL--IAMVaQFVAGegSNSDSEDVFLCvLPMFHIYG-LSSFALGLLrLGATVVVMPRFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 331 SRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRlAVGNG---LRPAIWEEFTQRFGVPQIGEFYGATECNCSI 407
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 408 ANMD------GKVGSCGFnsrilthVYPIRLVK-VNEDTMEPLRdseglciPCQPGEpgLLV-G-QINQqdplrrfdGYV 478
Cdd:cd05904 318 AMCFapekdrAKYGSVGR-------LVPNVEAKiVDPETGESLP-------PNQTGE--LWIrGpSIMK--------GYL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189407 479 SD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 550
Cdd:cd05904 374 NNpEATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
117-615 |
1.13e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 108.25 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 117 FAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEM 196
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 197 AAAVAEVSEQlGKSLLKFCSgdlgPESIL-------------PDTQLLDPMLA--EAPTTPLAQAPGKgmddrlfYIYTS 261
Cdd:PRK12406 94 LHGLASALPA-GVTVLSVPT----PPEIAaayrispalltppAGAIDWEGWLAqqEPYDGPPVPQPQS-------MIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 262 GTTGLPK-----AAIVVHSRYY---RIAAFGHHSySMRAadVLYDclPLYHSAGNIMGVgQCVIYGLTVVLRKKFSASRF 333
Cdd:PRK12406 162 GTTGHPKgvrraAPTPEQAAAAeqmRALIYGLKP-GIRA--LLTG--PLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 334 WDDCVKYNCTVVQYIGEICRYLLRQP--VR---DVEQ-RHRVRLAvgnGLRPA-IWEEFTQRFGvPQIGEFYGATECncs 406
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKLPeeVRakyDVSSlRHVIHAA---APCPAdVKRAMIEWWG-PVIYEYYGSTES--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 ianmdGKVGSCGfNSRILTHvyPIRLVKVNEDTMEPLRDSEGLCIPcqPGEPGllvgqinqqDPLRRFDGYVSDSATNKK 486
Cdd:PRK12406 309 -----GAVTFAT-SEDALSH--PGTVGKAAPGAELRFVDEDGRPLP--QGEIG---------EIYSRIAGNPDFTYHNKP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 487 IAHSVFRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMA 565
Cdd:PRK12406 370 EKRAEIDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEALMA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 566 AI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:PRK12406 447 VVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
96-623 |
1.22e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.20 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 96 VARRQPERLALVDASSgiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVaaLLNVNLR 174
Cdd:PRK07470 16 AARRFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMFAAF-RLGAV--WVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 175 REP--LAFCLGTSAAKALIYGG---EMAAAVAEVSEQLgKSLLKFCSGDLGPEsilpdtqlLDPMLAEAPTTPLAQAPGK 249
Cdd:PRK07470 91 QTPdeVAYLAEASGARAMICHAdfpEHAAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGARVANAAVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 250 gMDDRLFYIYTSGTTGLPKAAIVVHSRYyriaAF-------------GHHSYSMRAAdvlydclPLYHSAGnIMGVGQcV 316
Cdd:PRK07470 162 -HDDPCWFFFTSGTTGRPKAAVLTHGQM----AFvitnhladlmpgtTEQDASLVVA-------PLSHGAG-IHQLCQ-V 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 317 IYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGlRPAIWEEftQRFGVPQI 394
Cdd:PRK07470 228 ARGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG-APMYRAD--QKRALAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 G----EFYGATECNCSIANM--------DG---KVGSCGFnsrilthvypirlvkvnEDT-ME-PLRDSEGLciPCQPGE 457
Cdd:PRK07470 305 GkvlvQYFGLGEVTGNITVLppalhdaeDGpdaRIGTCGF-----------------ERTgMEvQIQDDEGR--ELPPGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 458 pgllVGQINQQDPlRRFDGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 537
Cdd:PRK07470 366 ----TGEICVIGP-AVFAGYYNNPEANAK----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 538 VLSRLLGQTDVAVYGVAVPgVEGKAGMAA-IADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKt 613
Cdd:PRK07470 435 KLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFFWDALPK---SGYGKITK- 509
|
570
....*....|
gi 1907189407 614 RLQREGFDPR 623
Cdd:PRK07470 510 KMVREELEER 519
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
85-553 |
6.16e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 106.12 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 85 AGDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 164
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 165 VAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTqlLDpmlAEAPTTPLA 244
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVH--LD---AATEPTPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 245 QAP-GKGMDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGL 320
Cdd:PRK05852 169 STPeGLRPDDAMI-MFTGGTTGLPKMVPWTHA---NIASSVRAiitGYRLSPRDATVAVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 321 TVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGVPQI 394
Cdd:PRK05852 245 AVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrfirSCSAPLTAETAQALQTEFAAPVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 gEFYGATECNCSIANMDGKVGSCGFNSRILTHVypirlvkVNEDTMEPLR--DSEGLciPCQPGEpgllVGQINQQDP-- 470
Cdd:PRK05852 325 -CAFGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDGL--PLPAGA----VGEVWLRGTtv 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 471 LRrfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 549
Cdd:PRK05852 391 VR---GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAA 460
|
....
gi 1907189407 550 VYGV 553
Cdd:PRK05852 461 VFGV 464
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
102-615 |
1.82e-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: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 102 ERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGF-APGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALIYGGEMaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmddrlfyIYT 260
Cdd:cd05941 79 VITDSEPSLVLDPALI-------------------------------------------------------------LYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 261 SGTTGLPKAaiVVHSRyYRIAAFGH---HSYSMRAADVLYDCLPLYHSAGNIMGVgQCVIY-GLTVVLRKKFSASRFWDD 336
Cdd:cd05941 98 SGTTGRPKG--VVLTH-ANLAANVRalvDAWRWTEDDVLLHVLPLHHVHGLVNAL-LCPLFaGASVEFLPKFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 337 CVKYNCTVVQYIGEICRYLLRQPVRDVEQR--------HRVRLAV-GNG-LRPAIWEEFTQRFGVPqIGEFYGATECNCS 406
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFTDPqfaraaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGMA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 IAN-MDG--KVGSCGFnsrilthvyPIRLVK---VNEDTMEPL-RDSEG-LCIPcqpgEPGLlvgqinqqdplrrFDGYV 478
Cdd:cd05941 253 LSNpLDGerRPGTVGM---------PLPGVQariVDEETGEPLpRGEVGeIQVR----GPSV-------------FKEYW 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 479 SDSATNKKiahsVFRkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPg 557
Cdd:cd05941 307 NKPEATKE----EFT-DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP- 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 558 VEGKAGMAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05941 381 DWGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
115-556 |
2.50e-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: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 194
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtqlLDPMLAEAPTtplaqapgkgMDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05969 78 ------------------------------------TTEELYERTD----------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRK-KFSASRFWDDCVKYNCTVVQYIGEICR 353
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 354 YLLR---QPVRDVEQRH-RVRLAVGNGLRPAI--WEEftQRFGVPqIGEFYGATECNC-SIAN---MDGKVGSCGfnsri 423
Cdd:cd05969 192 MLMKegdELARKYDLSSlRFIHSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTETGSiMIANypcMPIKPGSMG----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 424 lthvYPIRLVK--VNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYLS 501
Cdd:cd05969 264 ----KPLPGVKaaVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEE---RYKNS--------------FIDG--WYLT 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 502 GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 556
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
88-349 |
2.96e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.20 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 167
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRL--TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 LLNVNLR--REPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLaq 245
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERD-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 246 aPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRiAAFG------------HHSYSMRAAD----VLYDCLPLYHSAGnI 309
Cdd:PRK07798 158 -FGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFR-VLLGgrdfatgepiedEEELAKRAAAgpgmRRFPAPPLMHGAG-Q 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907189407 310 MGVGQCVIYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIG 349
Cdd:PRK07798 235 WAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
92-617 |
3.44e-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: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNV 171
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSL--TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG--AAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NlrreplafclgtsaakaliyGGEMAAAVAEVSEQLGKSLLkfcsgdlgpesILPDTQlldpmlaeapttplaqapgkgm 251
Cdd:cd17653 78 D--------------------AKLPSARIQAILRTSGATLL-----------LTTDSP---------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD-------VLYDClplyhSAGNIMGvgqCVIYGLTVVL 324
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 325 RkkfSASRFWDDcVKYNCTVVQYIGEICRYLlrqPVRDVEQRHRVRLAvGNGLRPAIWEEFTqrfGVPQIGEFYGATECN 404
Cdd:cd17653 177 A---DPSDPFAH-VARTVDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRWS---PGRRLYNAYGPTECT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 405 CSIAN---MDGKVGSCGfnsrilthvYPIRLVKV---NEDTMEPLRDSEG-LCIpcqpGEPGLLVGQINQQdplrrfdgy 477
Cdd:cd17653 246 ISSTMtelLPGQPVTIG---------KPIPNSTCyilDADLQPVPEGVVGeICI----SGVQVARGYLGNP--------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 vsdSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtdvaVYGVAVPG 557
Cdd:cd17653 304 ---ALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE----VTQAAAIV 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 558 VEGKagMAAIADPHSqLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:cd17653 377 VNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
83-617 |
3.66e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.68 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 83 RRAGDTIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 162
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDELGTL--TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 163 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllKFCSGDLGPESILPDTQLLDPMLAEA-PTT 241
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD-----------RALADCPQATRIVAWTDEDHDLTVEVlIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 242 PLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIYGL- 320
Cdd:PRK13382 186 HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHA----WGFSQLVLAASl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 321 --TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGvPQI 394
Cdd:PRK13382 262 acTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGsrMRPDVVIAFMDQFG-DVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 GEFYGATECN-CSIANMDGkvgscgfnsrilTHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEpgllVGQINQQDPLrR 473
Cdd:PRK13382 341 YNNYNATEAGmIATATPAD------------LRAAPDTAGRPAEGTEIRILDQDFREVP--TGE----VGTIFVRNDT-Q 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 474 FDGYVSDSATNkkiahsvFRKGDSAylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:PRK13382 402 FDGYTSGSTKD-------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 554 AVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:PRK13382 473 DDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
97-620 |
3.67e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 103.70 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICWtfAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPdtqlLDPMLAEA-PTTPLAQAPGkgmDDRL 255
Cdd:PRK07786 105 EIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG----YEDLLAEAgPAHAPVDIPN---DSPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 256 FYIYTSGTTGLPKAAIVVHSRYYRIAAfgHHSYSMRA---ADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLR--KKFSA 330
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVLTHANLTGQAM--TCLRTNGAdinSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 331 SRFWDDCVKYNCTVV-----QYIGeICRYLLRQPvRDVEQRhrvrlAVGNGLRPA---IWEEFTQRFGVPQIGEFYGATE 402
Cdd:PRK07786 255 GQLLDVLEAEKVTGIflvpaQWQA-VCAEQQARP-RDLALR-----VLSWGAAPAsdtLLRQMAATFPEAQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIANMDG-----KVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdseglcipcQPGEpgllVGQINQQDPlrrfdGY 477
Cdd:PRK07786 328 MSPVTCMLLGedairKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-----TL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 VSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 557
Cdd:PRK07786 382 MSGYWNNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 558 -VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqREGF 620
Cdd:PRK07786 460 wGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
98-588 |
3.78e-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: 104.20 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 98 RRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 173
Cdd:cd17634 64 RENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 174 RREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksLLKFCSGDLGPESILPDTQLL------------------DPML 235
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITADGGVRAGRSVP------LKKNVDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDLI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 236 AEAPT--TPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGNIMGv 312
Cdd:cd17634 218 AKASPehQPEAMNA----EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYW----CTADVGWVTG- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 313 GQCVIY-----GLTVVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRP 379
Cdd:cd17634 289 HSYLLYgplacGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLrilgSVGEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 380 AIWEEFTQRFG---VPQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSE-GLCIPCQP 455
Cdd:cd17634 369 EAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlVITDPWPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 456 GEPGLLvgqinqQDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 535
Cdd:cd17634 449 QTRTLF------GDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEI 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907189407 536 EAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHSQLDPNSMYQELQKVLA 588
Cdd:cd17634 509 ESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
97-616 |
4.84e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVAALLNVNLRR 175
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 176 EPLAFCLGTSAAKALIYGGEMAAAVAEVSEQL------GKSLLKFcsGDLgpESILPDTqllDPMLAEAPTtplaqapGK 249
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGADLplrlsfGGEIDGF--GSF--EAALAGA---GPRLTEQPC-------GA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 250 GMddrlfyIYTSGTTGLPKA------AIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAgNIMGVGQCVIYGLTVV 323
Cdd:PRK13390 152 VM------LYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 324 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQpvrDVEQRHRVRL----AVGNGLRPA---IWEEFTQRFGvPQIGE 396
Cdd:PRK13390 225 LAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKL---DADVRTRYDVsslrAVIHAAAPCpvdVKHAMIDWLG-PIVYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 397 FYGATECNcSIANMD-----GKVGSCGFNSRILTHVYpirlvkvnedtmeplrDSEGLCIPCqpGEPGLLVGQINQQdPL 471
Cdd:PRK13390 301 YYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHIC----------------DDDGNELPA--GRIGTVYFERDRL-PF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 472 RrfdgYVSD---SATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 548
Cdd:PRK13390 361 R----YLNDpekTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 549 AVYGVAVP--GVEGKAGMAAIA--DPHSQLdPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:PRK13390 431 AVIGVPDPemGEQVKAVIQLVEgiRGSDEL-ARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
115-618 |
6.63e-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: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQL-GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG 193
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 GEMAAAVAEVSEQLG-------------------KSLLKFCSgdlgPESILPDTQLLDPMLaeapttplaqapgkgmddr 254
Cdd:cd05928 122 DELAPEVDSVASECPslktkllvseksrdgwlnfKELLNEAS----TEHHCVETGSQEPMA------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 255 lfyIY-TSGTTGLPKAAIVVHSRY-YRIAAFGHHSYSMRAADVLY---DCLPLYHSAGNIMG---VGQCVIygltVVLRK 326
Cdd:cd05928 179 ---IYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWntsDTGWIKSAWSSLFEpwiQGACVF----VHHLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 327 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNC 405
Cdd:cd05928 252 RFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKfPSLQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 406 SIANMDG---KVGSCGFNSRilthVYPIRLVkvnedtmeplrDSEGLCIPcqPGEPGLLVGQINQQDPLRRFDGYVSDSa 482
Cdd:cd05928 331 ICANFKGmkiKPGSMGKASP----PYDVQII-----------DDNGNVLP--PGTEGDIGIRVKPIRPFGLFSGYVDNP- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 483 tnKKIAHSvfRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKA 562
Cdd:cd05928 393 --EKTAAT--IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 563 GMAAI--ADPHSQLDPNSMYQELQ----KVLASYARPIFLRLLPQVDTTGTFKIQKTRLQRE 618
Cdd:cd05928 467 VKAFVvlAPQFLSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-610 |
1.37e-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: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 124 SNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIygGEMAAAVAEV 203
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV-----PLNPTLKESVLRYLV--ADAGGRIVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 204 SEQLGkSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAF 283
Cdd:cd05922 76 DAGAA-DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSH------EDLALLLYTSGSTGSPKLVRLSH-QNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 284 GHHSY-SMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSASR-FWDDCVKYNCT---VVQYIGEICRYLLRQ 358
Cdd:cd05922 148 SIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 359 P-----VRDVEQrhrvrlaVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDG-----KVGSCGfnsrilthvy 428
Cdd:cd05922 227 PaklpsLRYLTQ-------AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPerileKPGSIG---------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 429 pirlVKVNEDTMEPLRDSEGlciPCQPGEPGLLVgqinqqdpLRR---FDGYVSDSATNKKIAhsvfRKGDSAYlSGDVL 505
Cdd:cd05922 290 ----LAIPGGEFEILDDDGT---PTPPGEPGEIV--------HRGpnvMKGYWNDPPYRRKEG----RGGGVLH-TGDLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 506 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAgMAAIADPHSQLDPNSMYqeLQK 585
Cdd:cd05922 350 RRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPKDVLRS--LAE 426
|
490 500
....*....|....*....|....*
gi 1907189407 586 VLASYARPIFLRLLPQVDTTGTFKI 610
Cdd:cd05922 427 RLPPYKVPATVRVVDELPLTASGKV 451
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
115-562 |
6.02e-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: 97.18 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 194
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EMAAAVAEVSeqLGKSLLKFCSGDLGPESIL---------PDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTG 265
Cdd:cd05968 172 GFTRRGREVN--LKEEADKACAQCPTVEKVVvvrhlgndfTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 266 LPKAAIVVHSRYYRIAAFG-HHSYSMRAADVLYdclpLYHSAGNIMG---VGQCVIYGLTVVLRKKF----SASRFWDDC 337
Cdd:cd05968 250 KPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLT----WFTDLGWMMGpwlIFGGLILGATMVLYDGApdhpKADRLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 338 VKYNCTVVQYIGEICRYLL---RQPVRdVEQRHRVRLAVGNG--LRPAIWEEFTQRFG---VPqIGEFYGATECNCSI-- 407
Cdd:cd05968 326 EDHEITHLGLSPTLIRALKprgDAPVN-AHDLSSLRVLGSTGepWNPEPWNWLFETVGkgrNP-IINYSGGTEISGGIlg 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 408 ANMDGKVGSCGFNSrilthVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGePGLLVGqiNQQDPLRRFDGYvsdsatnkki 487
Cdd:cd05968 404 NVLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAPW-PGMTRG--FWRDEDRYLETY---------- 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 488 ahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKA 562
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, ... |
254-610 |
9.17e-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: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 254 RLFYI-YTSGTTGLPKAaivvhsrYYR-----IAAF--GHHSYSMRAADVLYDCLPLYHSaGNIMGVGQCVIYGLTVVLR 325
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 KKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVEQRHRVR--LAVGNGLRPAIWEEFTQRFGVPQIGEFYGATEC 403
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 404 NCSIANMDG---KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSEGlcipcqpGEPGLLVGQINQqdplrRFDGYVSD 480
Cdd:cd17633 149 SFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM-----VFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 481 SATNKkiaHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV------- 553
Cdd:cd17633 202 GFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarfge 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 554 -AVPGVEGKagmaaiadphsQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKI 610
Cdd:cd17633 272 iAVALYSGD-----------KLTYKQLKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
88-403 |
9.98e-21 |
|
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: 97.62 E-value: 9.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 167
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG--AA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 L--LNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgDLGPESILPDTQLLDPMLAEAPTTPLAq 245
Cdd:COG1020 553 YvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLP----------------ELGVPVLALDALALAAEPATNPPVPVT- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 246 apgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVlydcLPLYH------SAGNIMGvgqCVIY 318
Cdd:COG1020 616 ------PDDLAYvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR----VLQFAslsfdaSVWEIFG---ALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 319 GLTVVLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrdVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQ 393
Cdd:COG1020 683 GATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLvgGEALPPELVRRWRARLPGAR 759
|
330
....*....|
gi 1907189407 394 IGEFYGATEC 403
Cdd:COG1020 760 LVNLYGPTET 769
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
115-615 |
1.33e-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: 94.85 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLG-TSAAKALIY 192
Cdd:cd05958 11 WTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 193 GGEMAAavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIV 272
Cdd:cd05958 91 HALTAS-----------------------------------------------------DDICILAFTSGTTGAPKATMH 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 273 VHSRYYRIA-AFGHHSYSMRAADVLYDCLPLYHSagniMGVGQCVIY----GLTVVLRKKFSASRFWDDCVKYNCTVVQY 347
Cdd:cd05958 118 FHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 348 IGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIgEFYGATEC-NCSIANMDGkvgscgfnsril 424
Cdd:cd05958 194 APTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMfHIFISARPG------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 425 tHVYPIRLVKVNEDTMEPLRDSEGLCIPcqPGEPGLLVgqinqqdpLRRFDGYVSDSatnKKIAHSVFRKGDSAylSGDV 504
Cdd:cd05958 261 -DARPGATGKPVPGYEAKVVDDEGNPVP--DGTIGRLA--------VRGPTGCRYLA---DKRQRTYVQGGWNI--TGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 505 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG--------VEGKAGMAAIADPHSQLdp 576
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvvkafVVLRPGVIPGPVLAREL-- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907189407 577 nsmyQELQK-VLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05958 403 ----QDHAKaHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
116-550 |
1.53e-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: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFA-PGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 194
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EMAAAVAEVseqlgksllkfcsgdlgPESILPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:TIGR01733 81 ALASRLAGL-----------------VLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 ----------SRYY------RIAAFghHSYSMRAAdVLYDCLPLYHsagnimGVGQCVIYGltVVLRKKFSASRFWDDcv 338
Cdd:TIGR01733 143 rslvnllawlARRYgldpddRVLQF--ASLSFDAS-VEEIFGALLA------GATLVVPPE--DEERDDAALLAALIA-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 339 KYNCTVVQYIGEICRYLLRQPVRDVEQRHRVrLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECN--CSIANMDGKVGS 416
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPALASLRLV-ILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 417 CGFNSRI---LTHVypiRLVKVNEDTMeplrdseglciPCQPGEPG-LLVGQINqqdpLRRfdGYVSDSA-TNKKIAHSV 491
Cdd:TIGR01733 289 RESPVPIgrpLANT---RLYVLDDDLR-----------PVPVGVVGeLYIGGPG----VAR--GYLNRPElTAERFVPDP 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 492 FRKGDSA--YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 550
Cdd:TIGR01733 349 FAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
85-322 |
2.26e-20 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 95.55 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 85 AGDTIPCIFQAVARRQPERLALVDASSGI--CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 162
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 163 GVVAALLNVNLRREPLAFCLGTSAAKALIYGG-EMAAAVAEVSEQLGkSLLKFCSGDLGPESILPDTQLLDPMLA----- 236
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELP-SLRHIVVLDPRGLRDDPRLLSLDELLAlgrev 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 237 EAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGqCV 316
Cdd:COG1022 168 ADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-AL 246
|
....*.
gi 1907189407 317 IYGLTV 322
Cdd:COG1022 247 AAGATV 252
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
93-615 |
3.09e-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: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 93 FQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 172
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 173 LRREPLAFCLGTSAAKALIYGGEMAAAVAEVseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKgmD 252
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAG---------------------GDVALLGDEALAAPPATPPLVPPRP--D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVL-------YDC------LPLYHSAGNIMGV--GQCVI 317
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVlqktplsFDVsvwelfWPLVAGARLVVARpgGHRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 318 YGLTVVLRkkfsasrfwDDCVkyncTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIG 395
Cdd:cd17646 219 AYLAALIR---------EHGV----TTCHFVPSMLRVFLAEP--AAGSCASLRRVFcsGEALPPELAARFLALPGAE-LH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 396 EFYGATE-------CNCSIANMDGKV--GSCGFNSRILthvypirlvkVNEDTMEplrdseglciPCQPGEPG-LLVGQI 465
Cdd:cd17646 283 NLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTRLY----------VLDDALR----------PVPVGVPGeLYLGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 466 nqqdPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 544
Cdd:cd17646 343 ----QLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 545 QTDVAVygVAVPGVEGKAGMAA---IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd17646 417 VTHAVV--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
116-610 |
3.33e-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: 93.70 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 275
Cdd:cd05935 83 L-------------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 276 RYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYL 355
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 356 LRQPvrDVEQRHRVRLAV----GNGLRPAIWEEFTQRFGVPQIgEFYGATEcNCSianmdgkvgscgfnsriLTHVYPIR 431
Cdd:cd05935 188 LATP--EFKTRDLSSLKVltggGAPMPPAVAEKLLKLTGLRFV-EGYGLTE-TMS-----------------QTHTNPPL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 432 LVKVNEDTMePLRDSEGLCIPCQPGE--PGLLVGQINQQDPlRRFDGYVSDSATNKKIAhsVFRKGDSAYLSGDVLVMDE 509
Cdd:cd05935 247 RPKLQCLGI-P*FGVDARVIDIETGRelPPNEVGEIVVRGP-QIFKGYWNRPEETEESF--IEIKGRRFFRTGDLGYMDE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 510 LGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP--GVEGKAGMAAIADPHSQLDPNSMYQELQKVL 587
Cdd:cd05935 323 EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDErvGEEVKAFIVLRPEYRGKVTEEDIIEWAREQM 402
|
490 500
....*....|....*....|....*.
gi 1907189407 588 ASYARP---IFLRLLPQvdtTGTFKI 610
Cdd:cd05935 403 AAYKYPrevEFVDELPR---SASGKI 425
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-617 |
6.96e-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: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvnlrREPL--AFclgtsaakaliyg 193
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAV---------YQPLftAF------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 gemaaavaevseqlgksllkfcsgdlGPESIlpdTQLLDPMLAEAPTTPLAQApGKGMDDRLFYIYTSGTTGLPKaAIVV 273
Cdd:cd05973 60 --------------------------GPKAI---EHRLRTSGARLVVTDAANR-HKLDSDPFVMMFTSGTTGLPK-GVPV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 274 HSRYyrIAAFghHSYSMRAADVLYDclplyHSAGNIMGVGQCviYGL-------------TVVLRKKFSASRFWDDCVKY 340
Cdd:cd05973 109 PLRA--LAAF--GAYLRDAVDLRPE-----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 341 NCTVVQYIGEICRYLLRQPVrDVEQRHRVRLAV----GNGLRPAIWEEFTQRFGVPqIGEFYGATECNCSIANMDG---- 412
Cdd:cd05973 178 GVTNLAGSPTAYRLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALGVP-IHDHYGQTELGMVLANHHAlehp 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 413 -KVGSCGFnsrilthVYP-IRLVKVNEDTMEPLrdseglcipcqPGEPGLLVGQINQQdPLRRFDGYvsdsatnkkiahs 490
Cdd:cd05973 256 vHAGSAGR-------AMPgWRVAVLDDDGDELG-----------PGEPGRLAIDIANS-PLMWFRGY------------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 491 vFRKGDSA-----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG----VEGK 561
Cdd:cd05973 304 -QLPDTPAidggyYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPErtevVKAF 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 562 AGMAAIADPHSQLDpNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:cd05973 383 VVLRGGHEGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
92-615 |
1.09e-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: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:cd12117 2 LFEEQAARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKgm 251
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGG----------------------LEVAVVIDEALDAGPAGNPAVPVSP-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIV--------VHSRYYriAAFGHHSYSMRAADVLYD--CLPLYhsaGNIMGVGQCVIYGLT 321
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVAVthrgvvrlVKNTNY--VTLGPDDRVLQTSPLAFDasTFEIW---GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLrkkfSASRFWDDCVKYNCTVVQyigeICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFTQRFGVPQIGEFY 398
Cdd:cd12117 211 TLL----DPDALGALIAEEGVTVLW----LTAALFNQLADEDPECFaglRELLTGGEVVSPPHVRRVLAACPGLRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 399 GATE-----CNCSIANMDGKVGScgfnsrilthvYPI-------RLVKVNEDtmepLRdseglciPCQPGEPG-LLVGqi 465
Cdd:cd12117 283 GPTEnttftTSHVVTELDEVAGS-----------IPIgrpiantRVYVLDED----GR-------PVPPGVPGeLYVG-- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 466 nqQDPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLG 544
Cdd:cd12117 339 --GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 545 QTDVAVygVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd12117 415 VREAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
80-268 |
4.28e-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: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 80 RRHRRAG----DTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 155
Cdd:COG1021 14 ARYREAGywrgETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 156 WLGLAKAGV--VAALlnVNLRR-EPLAFClGTSAAKALI----YGG----EMAAAVAEVSEQLGKSLLkfcSGDLGPESI 224
Cdd:COG1021 92 FFALFRAGAipVFAL--PAHRRaEISHFA-EQSEAVAYIipdrHRGfdyrALARELQAEVPSLRHVLV---VGDAGEFTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907189407 225 LPDtqlldpmLAEAPTTPLAQAPgkGMDDRLFYIYTSGTTGLPK 268
Cdd:COG1021 166 LDA-------LLAAPADLSEPRP--DPDDVAFFQLSGGTTGLPK 200
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
82-553 |
5.07e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 90.82 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 82 HRRAGDTIPCIFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEfvgLWLGLAk 161
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 162 AGVVAALLNVNLrrEPL------AFCLGTSAAKALIY--------GGEMAAAVAEVseqlgKSLLKFCSGDLGPEsilpd 227
Cdd:PRK06188 81 AAQLAGLRRTAL--HPLgslddhAYVLEDAGISTLIVdpapfverALALLARVPSL-----KHVLTLGPVPDGVD----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 228 tqlldpMLAEAPTTPLAQA-PGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSA 306
Cdd:PRK06188 149 ------LLAAAAKFGPAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 307 GNImgVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV----GNGLRPAIW 382
Cdd:PRK06188 223 GAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHP--DLRTRDLSSLETvyygASPMSPVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 383 EEFTQRFGvPQIGEFYGATECNCSIANMD---------GKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPc 453
Cdd:PRK06188 299 AEAIERFG-PIFAQYYGQTEAPMVITYLRkrdhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 454 qPGEPgllvGQINQQDPLrRFDGYVSDSATNKKiahsVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVST 532
Cdd:PRK06188 362 -QGEV----GEICVRGPL-VMDGYWNRPEETAE----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFP 428
|
490 500
....*....|....*....|.
gi 1907189407 533 TEVEAVLSRLLGQTDVAVYGV 553
Cdd:PRK06188 429 REVEDVLAEHPAVAQVAVIGV 449
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-616 |
5.49e-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: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 259 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL-RKKFSASRFWDDC 337
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 338 VKYNCTVVQ-----YIGEicrylLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIAN- 409
Cdd:cd05917 89 EKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 410 -----MDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSEGLCIPcQPGEPGLLVgqinqqdpLRRFD---GYVSD- 480
Cdd:cd05917 164 rtddsIEKRVNTVG---RIMPHTE----AKI--------VDPEGGIVP-PVGVPGELC--------IRGYSvmkGYWNDp 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 481 SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeG 560
Cdd:cd05917 220 EKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-G 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 561 KAGMAAIA-DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:cd05917 293 EEVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
102-553 |
9.92e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 89.95 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 102 ERLAL--VDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLeGR-PEFVGLWLGLAKAGVVAALLNVNLRREPL 178
Cdd:PRK04319 59 DKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFM-PRiPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIYGGEMAAAVaeVSEQLGKslLK--FCSGDLGPESilPDTQLLDPMLAEAPTTplAQAPGKGMDDRLF 256
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALLERK--PADDLPS--LKhvLLVGEDVEEG--PGTLDFNALMEQASDE--FDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVHSryyriAAFGHH---SYSM--RAADVlYDCL---------------PLYHSAGNimgvgqcv 316
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHN-----AMLQHYqtgKYVLdlHEDDV-YWCTadpgwvtgtsygifaPWLNGATN-------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 317 iygltVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVrDVEQRH-----RVRLAVGNGLRP-AIWeeFTQR-F 389
Cdd:PRK04319 276 -----VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGD-DLVKKYdlsslRHILSVGEPLNPeVVR--WGMKvF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 390 GVPqIGEFYGATECNCS-IAN---MDGKVGSCGfnsRILTHVYpIRLVKVNEDTMEPLRDSEgLCIpcQPGEPGLLVGQI 465
Cdd:PRK04319 348 GLP-IHDNWWMTETGGImIANypaMDIKPGSMG---KPLPGIE-AAIVDDQGNELPPNRMGN-LAI--KKGWPSMMRGIW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 466 NQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEavlSRLLGQ 545
Cdd:PRK04319 420 NNPE---KYESY--------------FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE---SKLMEH 477
|
....*...
gi 1907189407 546 TDVAVYGV 553
Cdd:PRK04319 478 PAVAEAGV 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
86-323 |
1.48e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.48 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 86 GDTIPCIFQAVARRQPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 165
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 166 aaLLNVN--LRREPLAFCLGTSAAKALIYGG--------EMAAAVA-EVSEQLGKSL-------LKF-CSgdLGPESIlP 226
Cdd:PRK08315 95 --LVTINpaYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYELApELATCEPGQLqsarlpeLRRvIF--LGDEKH-P 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 227 DTQLLDPMLAEAPTTPLAQ--APGKGM--DDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHH-SYSMR--AADVLYDC 299
Cdd:PRK08315 170 GMLNFDELLALGRAVDDAElaARQATLdpDDPINIQYTSGTTGFPKGATLTH---RNILNNGYFiGEAMKltEEDRLCIP 246
|
250 260
....*....|....*....|....
gi 1907189407 300 LPLYHSAGNIMGVGQCVIYGLTVV 323
Cdd:PRK08315 247 VPLYHCFGMVLGNLACVTHGATMV 270
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
97-541 |
2.06e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.86 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGIcwTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRR 175
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAI--SYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 176 EPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDL---GPESILPD---TQLLDPMLAEAPTTPLAQA-- 246
Cdd:PRK08314 98 EELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYlpaEPEIAVPAwlrAEPPLQALAPGGVVAWKEAla 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 247 ----PGK---GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYG 319
Cdd:PRK08314 178 aglaPPPhtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 320 LTVVLrkkfsASRfWD-----DCV-KYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLA-VGNG---LRPAIWEEFTQRF 389
Cdd:PRK08314 258 ATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASP--GLAERDLSSLRyIGGGgaaMPEAVAERLKELT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 390 GVPQIgEFYGATECNC-SIAN-MDGKVGSC------GFNSRIlthvypirlvkVNEDTMEPLrdseglcipcQPGEpgll 461
Cdd:PRK08314 330 GLDYV-EGYGLTETMAqTHSNpPDRPKLQClgiptfGVDARV-----------IDPETLEEL----------PPGE---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 462 VGQINQQDPlRRFDGYVSDSATNKKI-----AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVE 536
Cdd:PRK08314 384 VGEIVVHGP-QVFKGYWNRPEATAEAfieidGKRFFRTGDLGR-------MDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
....*
gi 1907189407 537 AVLSR 541
Cdd:PRK08314 456 NLLYK 460
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
86-593 |
2.34e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 85.82 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 86 GDTIPCIFQAVARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 165
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 166 AALLNVNLRREPLAFCLGTSAAKALIYGGEmaaaVAEVSEQLgksllkfcSGDLGPESI--------LPDTQLL------ 231
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIVWDK----VAPTVERL--------RRTTPLETIvsvnmiaaMPLLQRLalrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 232 -------DPMLAEAP-TTPLAQ-----APGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHH--S 287
Cdd:PRK05605 177 palrkarAALTGPAPgTVPWETlvdaaIGGDGSdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 288 YSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEIcrYllrQPVRDVEQRH 367
Cdd:PRK05605 257 GLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL--Y---EKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 368 RVRLavgNGLRPAI-------------WEEFTQRFGVpqigEFYGATECN----CSIANMDGKVGSCG--FNSRIlthvy 428
Cdd:PRK05605 332 GVDL---SGVRNAFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMSDDRRPGYVGvpFPDTE----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 429 pIRLVkvneDTMEPLRDseglcIPcqPGEPG-LLVgqinqQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVM 507
Cdd:PRK05605 400 -VRIV----DPEDPDET-----MP--DGEEGeLLV-----RGP-QVFKGYWNRPEETAKSFL------DGWFRTGDVVVM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 508 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQK 585
Cdd:PRK05605 456 EEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVAavVLEPGAALDPEGLRAYCRE 533
|
....*...
gi 1907189407 586 VLASYARP 593
Cdd:PRK05605 534 HLTRYKVP 541
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
92-568 |
2.97e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 85.42 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRqPERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:PLN02246 29 CFERLSEF-SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIyggEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQapgkgm 251
Cdd:PLN02246 108 FYTPAEIAKQAKASGAKLII---TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISP------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAF--GHH-SYSMRAADVLYDCLPLYH--SAGNIMGVGQCViyGLTVVLR 325
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHkGLVTSVAQQvdGENpNLYFHSDDVILCVLPMFHiySLNSVLLCGLRV--GAAILIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLaVGNGLRPAIWE-EFTQRFGVPQ--IGEFYGATE 402
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPLGKElEDAFRAKLPNavLGQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIAnM---------DGKVGSCGfnsrilTHVYPIRLVKVNEDTMEPLRDSeglcipcQPGEPGLLVGQInqqdplrr 473
Cdd:PLN02246 336 AGPVLA-MclafakepfPVKSGSCG------TVVRNAELKIVDPETGASLPRN-------QPGEICIRGPQI-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 474 FDGYVSD-SATNKKI-----AHSvfrkGDSAYLSGDvlvmDElgyMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 547
Cdd:PLN02246 394 MKGYLNDpEATANTIdkdgwLHT----GDIGYIDDD----DE---LFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD 462
|
490 500
....*....|....*....|.
gi 1907189407 548 VAVygvaVPGVEGKAGMAAIA 568
Cdd:PLN02246 463 AAV----VPMKDEVAGEVPVA 479
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
87-553 |
4.55e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 84.89 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 87 DTIPCIFQAVARrqPERLALVDASSGICWTFAQLDTYSNAVAN-LFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 165
Cdd:PLN02574 41 DAVSFIFSHHNH--NGDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 166 AALLNvnlrrePLAfCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdLG-PESILPDTQLLDPMLAEAPT---- 240
Cdd:PLN02574 119 VTTMN------PSS-SLGEIKKRVVDCSVGLAFTSPENVEKLSP---------LGvPVIGVPENYDFDSKRIEFPKfyel 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 241 ----TPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYyrIAA------FGHHSYSMRAADVLY-DCLPLYHSAGNI 309
Cdd:PLN02574 183 ikedFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNL--IAMvelfvrFEASQYEYPGSDNVYlAALPMFHIYGLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 310 MGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPA---IWEEFT 386
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLsgkFIQDFV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 387 QRFGVPQIGEFYGATEcncSIAnmdgkVGSCGFNSRILTHVYPIRLVKVNedtMEP--LRDSEGLCIPcqPGE------- 457
Cdd:PLN02574 341 QTLPHVDFIQGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPN---MQAkvVDWSTGCLLP--PGNcgelwiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 458 -PGLLVGQINqqdplrrfDGYVSDSATNKkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 536
Cdd:PLN02574 408 gPGVMKGYLN--------NPKATQSTIDK----------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
|
490
....*....|....*..
gi 1907189407 537 AVLSRLLGQTDVAVYGV 553
Cdd:PLN02574 470 AVLISHPEIIDAAVTAV 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
118-615 |
4.99e-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: 84.35 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 118 AQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLakaGVVAALLNVNLRREPLAF---CLGTSAAKALIYGG 194
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIAD---GVYIYLINSILTVFAAAAawkCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EMAAAVAEVseqlgKSLLKFCSGDLGPESILPDTQLlDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGTTGLPKA---- 269
Cdd:cd05929 79 AEACAIIEI-----KAAALVCGLFTGGGALDGLEDY-EAAEGGSPETPIEdEAAGWKM------LYSGGTTGRPKGikrg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 270 --AIVVHSRYYRIAAFGhhsYSMRAADVLYDCLPLYHSAGNI--MGVgqcVIYGLTVVLRKKFSASRFWDDCVKYNCTVV 345
Cdd:cd05929 147 lpGGPPDNDTLMAAALG---FGPGADSVYLSPAPLYHAAPFRwsMTA---LFMGGTLVLMEKFDPEEFLRLIERYRVTFA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 346 QYIGEICRYLLRQP--VRDVEQRHRVRLAVGNGLRPAIW-EEFTQRFGVPQIGEFYGATECNcsianmdgkvGSCGFNS- 421
Cdd:cd05929 221 QFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAAPCPPWvKEQWIDWGGPIIWEYYGGTEGQ----------GLTIINGe 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 422 RILTHvyPIRLVKVNEDTMEpLRDSEGLciPCQPGEPGLLVgqinqqdplrrFDGYVSDSATNK--KIAHSVFRKGDSAY 499
Cdd:cd05929 291 EWLTH--PGSVGRAVLGKVH-ILDEDGN--EVPPGEIGEVY-----------FANGPGFEYTNDpeKTAAARNEGGWSTL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 500 lsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIaDPHSQLDPNS 578
Cdd:cd05929 355 --GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QPAPGADAGT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907189407 579 MYQE-----LQKVLASYARP---IFLRLLPQVDTTgtfKIQKTRL 615
Cdd:cd05929 430 ALAEeliafLRDRLSRYKCPrsiEFVAELPRDDTG---KLYRRLL 471
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
101-556 |
6.29e-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: 83.89 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASsgICWTFAQldTYSNAV--ANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 178
Cdd:cd12118 18 PDRTSIVYGD--RRYTWRQ--TYDRCRrlASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIyggemaaavaeVSEQL-GKSLLKfcSGDLGPESILPDTQlldpmlaeapttplaqapgkgmDDRLFY 257
Cdd:cd12118 94 AFILRHSEAKVLF-----------VDREFeYEDLLA--EGDPDFEWIPPADE----------------------WDPIAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 258 IYTSGTTGLPKAaIVVHSRYYRIAAFGH-HSYSMRAADVLYDCLPLYHSAG--NIMGVGqcVIYGLTVVLRKkFSASRFW 334
Cdd:cd12118 139 NYTSGTTGRPKG-VVYHHRGAYLNALANiLEWEMKQHPVYLWTLPMFHCNGwcFPWTVA--AVGGTNVCLRK-VDAKAIY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 335 DDCVKYNCT-------VVQYIGEiCRYLLRQPVRdveqrHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNcsi 407
Cdd:cd12118 215 DLIEKHKVThfcgaptVLNMLAN-APPSDARPLP-----HRVHVMTAGAPPPAAVLAKMEELGF-DVTHVYGLTETY--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 408 anmdGKVGSC---------------GFNSRI-LTHVYPIRLVKVNEDTMEPL-RDSEGLcipcqpGEPgLLVGQINQQdp 470
Cdd:cd12118 285 ----GPATVCawkpewdelpteeraRLKARQgVRYVGLEEVDVLDPETMKPVpRDGKTI------GEI-VFRGNIVMK-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 471 lrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 550
Cdd:cd12118 352 -----GYLKNPEATAE----AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
....*.
gi 1907189407 551 ygVAVP 556
Cdd:cd12118 421 --VARP 424
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
82-618 |
2.24e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.77 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 82 HRRAGDTIPC--IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGL 159
Cdd:PRK06710 17 STISYDIQPLhkYVEQMASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 160 AKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG---------KSLLKFCSGDLGPESILPDTQL 230
Cdd:PRK06710 95 LLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKiehvivtriADFLPFPKNLLYPFVQKKQSNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 231 LdPMLAEAPTTPLAQAPGKGMD-----------DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYS-MRAADVLY 297
Cdd:PRK06710 175 V-VKVSESETIHLWNSVEKEVNtgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 298 DCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNG 376
Cdd:PRK06710 254 GVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 377 LRPAIWEEFTQRFGVPQIGEFYGATEcncsianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPG 456
Cdd:PRK06710 334 PLPVEVQEKFETVTGGKLVEGYGLTE------------------SSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 457 E---PGLlVGQINQQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 533
Cdd:PRK06710 396 EalpPGE-IGEIVVKGP-QIMKGYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 534 EVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 613
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
....*
gi 1907189407 614 RLQRE 618
Cdd:PRK06710 548 VLIEE 552
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
101-615 |
2.59e-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: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALIyggemaaavaevseqlgksllkFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPgkGMDDRLFYIYT 260
Cdd:cd12114 79 ILADAGARLVL----------------------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 261 SGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRAADVLYDCLPLYH--SAGNIMGVgqcVIYGLTVVL----RKKFSASrf 333
Cdd:cd12114 135 SGSTGTPKGVMISHRAALNtILDINRR-FAVGPDDRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 334 WDDCV-KYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLA------VGNGLRPAIWeeftQRFGVPQIGEFYGATEcncs 406
Cdd:cd12114 209 WAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVllsgdwIPLDLPARLR----ALAPDARLISLGGATE---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 ianmdgkvGScgfnsrILTHVYPIRlvKVNEDTME-----PLR-------DSEGLciPCQPGEPG-LLVGQIN-----QQ 468
Cdd:cd12114 281 --------AS------IWSIYHPID--EVPPDWRSipygrPLAnqryrvlDPRGR--DCPDWVPGeLWIGGRGvalgyLG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 469 DPLRRFDGYVSDSAtnkkiAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 548
Cdd:cd12114 343 DPELTAARFVTHPD-----GERLYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 549 AVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd12114 411 VVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
252-556 |
1.07e-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: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFghhsYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLR-- 325
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHknllANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpn 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 ----KKFSasRFWDDcvkYNCTVVQYIGEICRYLLR--QPvrdvEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPqIGEF 397
Cdd:cd05909 223 pldyKKIP--ELIYD---KKATILLGTPTFLRGYARaaHP----EDFSSLRLVVagAEKLKDTLRQEFQEKFGIR-ILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 398 YGATEC----NCSIANMDGKVGSCGfnsRILTHVyPIRLVKVnedtmeplrdsEGLCiPCQPGEPGLLVGQINQqdplrR 473
Cdd:cd05909 293 YGTTECspviSVNTPQSPNKEGTVG---RPLPGM-EVKIVSV-----------ETHE-EVPIGEGGLLLVRGPN-----V 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 474 FDGYVSDSatnkkiAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtDVAVYGV 553
Cdd:cd05909 352 MLGYLNEP------ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVV 424
|
...
gi 1907189407 554 AVP 556
Cdd:cd05909 425 SVP 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-624 |
1.34e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.16 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 53 RFLRIVCKTARRDLFGLSVLIRV--RLELRRHRRAGDTIPC------IFQAVARRQPERLALVdaSSGICWTFAQLDTYS 124
Cdd:PRK12316 1961 HLLEQMAEDAQAALGELALLDAGerQRILADWDRTPEAYPRgpgvhqRIAEQAARAPEAIAVV--FGDQHLSYAELDSRA 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 125 NAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAavaevs 204
Cdd:PRK12316 2039 NRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE------ 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 205 eqlgksllkfcsgDLGPESILPDTQLLDPM-LAEAPTT-PLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVHSRYY-RIA 281
Cdd:PRK12316 2113 -------------RLPLPAGVARLPLDRDAeWADYPDTaPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVaHCQ 2176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 282 AFGhHSYSMRAADVLYDCLPLYHSaGNIMGVGQCVIYGLTVVLR--KKFSASRFWDDCVKYNCTVVQYIGEicrYLlrQP 359
Cdd:PRK12316 2177 AAG-ERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPV---YL--QQ 2249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 360 VRDVEQRHRVRLAV------GNGLRPAIWEEFTQRFGVPQIGEFYGATEcncsiANMDGKVGSCGFNSRILTHVYPI--- 430
Cdd:PRK12316 2250 LAEHAERDGRPPAVrvycfgGEAVPAASLRLAWEALRPVYLFNGYGPTE-----AVVTPLLWKCRPQDPCGAAYVPIgra 2324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 431 ---RLVKVNEDTMEPLrdSEGLCIPCQPGEPGLLVGQINQqdPLRRFDGYVSDSATNkkiahsvfrKGDSAYLSGDVLVM 507
Cdd:PRK12316 2325 lgnRRAYILDADLNLL--APGMAGELYLGGEGLARGYLNR--PGLTAERFVPDPFSA---------SGERLYRTGDLARY 2391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 508 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMA-AIADPHSQLDPNSMYQELQKV 586
Cdd:PRK12316 2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAyVVPDDAAEDLLAELRAWLAAR 2469
|
570 580 590
....*....|....*....|....*....|....*...
gi 1907189407 587 LASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQ 624
Cdd:PRK12316 2470 LPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-615 |
1.83e-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: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 80 RRHRRAG----DTIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGL 155
Cdd:cd05920 4 RRYRAAGywqdEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 156 WLGLAKAGVVAAL-LNVNLRREPLAFClGTSAAKALIyggemaaavaeVSEQLGksllKFCSGDLGPEsilpdtqlldpM 234
Cdd:cd05920 82 FFALLRLGAVPVLaLPSHRRSELSAFC-AHAEAVAYI-----------VPDRHA----GFDHRALARE-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 235 LAEAPTTPLAQAPGkgmddrlfyiytsGTTGLPKAAIVVHSRYyriaafghhSYSMRAA--------DVLYDC-LPLYH- 304
Cdd:cd05920 135 AESIPEVALFLLSG-------------GTTGTPKLIPRTHNDY---------AYNVRASaevcgldqDTVYLAvLPAAHn 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 305 ---SAGNIMGVGQCviyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLL--RQPVRDVEQRHRVRLAVGNGLRP 379
Cdd:cd05920 193 fplACPGVLGTLLA---GGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLdaAASRRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 380 AIWEEFTQRFGvPQIGEFYGATE---CNCSIANMDGKVgsCGFNSRILTHVYPIRLVkvnedtmeplrDSEGLCIPcqPG 456
Cdd:cd05920 270 ALARRVPPVLG-CTLQQVFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV-----------DEEGNPVP--PG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 457 EPGLLvgqinqqdpLRR----FDGYVSDSATNKKiahsVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 532
Cdd:cd05920 334 EEGEL---------LTRgpytIRGYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 533 TEVEAVLSRLLGQTDVAVygVAVPG-VEGKAGMAAIADPHSQLDPNSMYQEL-QKVLASYARPIFLRLLPQVDTTGTFKI 610
Cdd:cd05920 400 EEVENLLLRHPAVHDAAV--VAMPDeLLGERSCAFVVLRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
....*
gi 1907189407 611 QKTRL 615
Cdd:cd05920 478 DKKAL 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
258-612 |
4.51e-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: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 258 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDC 337
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 338 VKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV-GNGLRPAIW-EEFTQRFGVPQIGEFYGATECNCSianmdgkvg 415
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 416 scgfnsrilthvypirlvkvnedTM-EPLRDSEGLCIPCQPGEPGLLVGQINQQDPLRR----FDGYVSD-SATNKKIah 489
Cdd:cd17638 157 -----------------------TMcRPGDDAETVATTCGRACPGFEVRIADDGEVLVRgynvMQGYLDDpEATAEAI-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 490 svfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMA-AIA 568
Cdd:cd17638 212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGKAfVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907189407 569 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQK 612
Cdd:cd17638 287 RPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
92-615 |
4.64e-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: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:cd17645 3 LFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttplaqapgKGM 251
Cdd:cd17645 81 DYPGERIAYMLADSSAKILL---------------------------------------------------------TNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD--VLYDCLPLYHSAGNIMgvgQCVIYGLTVVL---RK 326
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALHVvpsER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 327 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrdvEQRHRVRLAVGNGLRPAIWEEFtqrfgvpQIGEFYGATECN-- 404
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFMQLD----NQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTENTvv 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 405 CSIANMDGKVGSCGFNSRILThvypIRLVKVNED-TMEPLRDSEGLCIPcqpGEpGLLVGQINQQDplrrfdgyvsdsAT 483
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDN----TRVYILDEAlQLQPIGVAGELCIA---GE-GLARGYLNRPE------------LT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 484 NKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAG 563
Cdd:cd17645 310 AEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDADGRKY 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 564 MAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
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 ... |
115-552 |
5.33e-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: 77.64 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 194
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 emaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlAEAPttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:cd05907 83 -----------------------------------------VEDP------------DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 275 SRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVV-----------LRKK-----FSASRFWDdcv 338
Cdd:cd05907 110 RNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddLSEVrptvfLAVPRVWE--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 339 K-YNCTVVQYIGEICRYLLRQPVRDveqrhRVRLAVGNG--LRPAIwEEFTQRFGVPqIGEFYGATECnCSIANM----D 411
Cdd:cd05907 187 KvYAAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGIP-VYEGYGLTET-SAVVTLnppgD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 412 GKVGSCGfnsriltHVYPIRLVKVNEDtmeplrdseglcipcqpGEpgLLV-GQINqqdplrrFDGYVSDSATNKKIAhs 490
Cdd:cd05907 259 NRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV-------MLGYYKNPEATAEAL-- 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 491 vfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEAVL--SRLLGQtdVAVYG 552
Cdd:cd05907 304 ---DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLISQ--AVVIG 363
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
101-615 |
8.32e-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: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd17650 1 PDAIAVSDATRQL--TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALiyggemaaavaevseqlgksllkfcsgdlgpesilpdtqLLDPmlaeapttplaqapgkgmDDRLFYIYT 260
Cdd:cd17650 79 MLEDSGAKLL---------------------------------------LTQP------------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 261 SGTTGLPKAAIVVHS----------RYYRIAAFGHHSYSMR--AADVLYDCLPLYHSAGnimgvGQCVIygltVVLRKKF 328
Cdd:cd17650 102 SGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRLLQMAsfSFDVFAGDFARSLLNG-----GTLVI----CPDEVKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 329 SASRFWDDCVKYNCTVVQYIGEICRyllrqPVRDVEQRHRVR------LAVGNGLRPAIW-EEFTQRFGVP-QIGEFYGA 400
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIR-----PVMAYVYRNGLDlsamrlLIVGSDGCKAQDfKTLAARFGQGmRIINSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 401 TEcncsiANMDGKVGSCGFNSRILTHVYPI-------RLVKVNE-DTMEPLRDSEGLCIpcqpGEPGLLVGQINQQDplr 472
Cdd:cd17650 248 TE-----ATIDSTYYEEGRDPLGDSANVPIgrplpntAMYVLDErLQPQPVGVAGELYI----GGAGVARGYLNRPE--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 473 rfdgyvsdsATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVyg 552
Cdd:cd17650 316 ---------LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV-- 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189407 553 VAVPGVEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd17650 385 AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
97-324 |
2.98e-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: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGfAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL--- 169
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 170 --NVNLRRepLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAP 247
Cdd:cd05931 82 tpGRHAER--LAAILADAGPRVVLTTAAALAAVRAFAASRPA---------------AGTPRLLVVDLLPDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 248 GKGMDDRLFYIYTSGTTGLPKAAIVVHsryyriAAFGH------HSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLT 321
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
...
gi 1907189407 322 VVL 324
Cdd:cd05931 219 SVL 221
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
101-553 |
5.60e-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: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALIYGGEMAAAVAEVseqlgKSLLKFCSG--------DLGPESILPD--TQLLDPMLAEAPTTPlaqaPGKG 250
Cdd:cd17642 111 SLNISKPTIVFCSKKGLQKVLNV-----QKKLKIIKTiiildskeDYKGYQCLYTfiTQNLPPGFNEYDFKP----PSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 251 MDDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRAADVLYD-----CLPLYHSAGNIMGVGQcVIYGLTVVL 324
Cdd:cd17642 182 RDEQVALImNSSGSTGLPKGVQLTHKNI--VARFSHARDPIFGNQIIPDtailtVIPFHHGFGMFTTLGY-LICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 325 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD-VEQRHRVRLAVGNG-LRPAIWEEFTQRFGVPQIGEFYGATE 402
Cdd:cd17642 259 MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSI---ANMDGKVGSCGfnsriltHVYPIRLVKVnedtMEPlrDSEGLCIPCQPGE-----PGLLVGQINQQDplrrf 474
Cdd:cd17642 339 TTSAIlitPEGDDKPGAVG-------KVVPFFYAKV----VDL--DTGKTLGPNERGElcvkgPMIMKGYVNNPE----- 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 475 dgyvsdsATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:cd17642 401 -------ATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
101-615 |
5.96e-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: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 178
Cdd:cd17643 1 PEAVAVVDEDRRL--TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAypVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapTTPlaqapgkgmDDRLFYI 258
Cdd:cd17643 77 AFILADSGPSLLL------------------------------------------------TDP---------DDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 259 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYdclpLYHSAG------NIMGVgqcVIYGLTVVLRKKF---S 329
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 330 ASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGV--PQIGEFYGATEcnc 405
Cdd:cd17643 173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLdrPQLVNMYGITE--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 406 sianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEP-----------LRDSEGLCIPcqPGEPGLLV--------GQIN 466
Cdd:cd17643 250 ---------------TTVHVTFRPLDAADLPAAAASPigrplpglrvyVLDADGRPVP--PGVVGELYvsgagvarGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 467 QQD-PLRRFdgyVSDSATNkkiahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 545
Cdd:cd17643 313 RPElTAERF---VANPFGG---------PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSV 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 546 TDVAVygVAVPGVEGKAGMAA--IADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd17643 381 RDAAV--IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
85-623 |
6.58e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 85 AGDTIPCIFQAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEF-VGLwLGLAKAG 163
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 164 VVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESILPDTQLLDPMLAEAPTTPL 243
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE---------------GVSAIALDSLHLDSWPSQAPGLHL 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 244 AqapgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSagniMGVGQC---VIYG 319
Cdd:PRK05691 1271 H-------GDNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD----VSVWECfwpLITG 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 320 LTVVLR---KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQI 394
Cdd:PRK05691 1340 CRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP--LAAACTSLRRLFsgGEALPAELRNRVLQRLPQVQL 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 GEFYGATEC-------NCSIAnmDGKVGSCGfnsRILTHVypirLVKVNEDTMEPLrdseglcipcQPGEPG-LLVGQIN 466
Cdd:PRK05691 1418 HNRYGPTETainvthwQCQAE--DGERSPIG---RPLGNV----LCRVLDAELNLL----------PPGVAGeLCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 467 qqdpLRRfdGYVSDSATNKK--IAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAvlsRLLG 544
Cdd:PRK05691 1479 ----LAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQA---RLLA 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 545 QTDVAVYGVAVPgvEGKAGMAAI----ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL----- 615
Cdd:PRK05691 1550 QPGVAQAAVLVR--EGAAGAQLVgyytGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepvw 1627
|
....*....
gi 1907189407 616 -QREGFDPR 623
Cdd:PRK05691 1628 qQREHVEPR 1636
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
80-556 |
1.98e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 80 RRHRRAGDTIPCIFQAVARRQPERLALVDaSSGICWTFAQLDTYSNAVANLFRQLgFAPGDVVAVFLegrPEFVG---LW 156
Cdd:PRK08633 608 KSRKEALPPLAEAWIDTAKRNWSRLAVAD-STGGELSYGKALTGALALARLLKRE-LKDEENVGILL---PPSVAgalAN 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 157 LGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIyggemaaavaeVSEQ-LGKSLLKFCSGDLGP-------ESILPDT 228
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVI-----------TSRKfLEKLKNKGFDLELPEnvkviylEDLKAKI 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 229 QLLDPMLAE-----APTTPLAQA--PGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAA--------FGhhsysMRAA 293
Cdd:PRK08633 752 SKVDKLTALlaarlLPARLLKRLygPTFKPDDTATIIFSSGSEGEPKGVMLSH---HNILSnieqisdvFN-----LRND 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 294 DVLYDCLPLYHSagnimgvgqcviYGLTV----VLRKKFSASRFWDD---------CVKYNCTVVQYIGEICRYLLRQPV 360
Cdd:PRK08633 824 DVILSSLPFFHS------------FGLTVtlwlPLLEGIKVVYHPDPtdalgiaklVAKHRATILLGTPTFLRLYLRNKK 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 361 RDVEQRHRVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsrilt 425
Cdd:PRK08633 892 LHPLMFASLRLVVAGAekLKPEVADAFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG------- 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 426 HVYPIRLVK-VNEDTMEPLrdseglcipcQPGEPGL-LVGQINqqdplrRFDGYVSDSA-TNKKIAHSvfrKGDSAYLSG 502
Cdd:PRK08633 964 MPLPGVAVRiVDPETFEEL----------PPGEDGLiLIGGPQ------VMKGYLGDPEkTAEVIKDI---DGIGWYVTG 1024
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 503 DVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 556
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-539 |
2.50e-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: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvnlrreplafclgtsaakaliygge 195
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 maaavaevseqlgksllkfcsgdlgpesILPDTQLLDP-----MLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKaa 270
Cdd:cd05974 52 ----------------------------VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 271 IVVHSryYRIAAFGHHS----YSMRAADVLYD-CLPLY--HSAGNIMG---VGQCVIygltVVLRKKFSASRFWDDCVKY 340
Cdd:cd05974 102 LVEHT--HRSYPVGHLStmywIGLKPGDVHWNiSSPGWakHAWSCFFApwnAGATVF----LFNYARFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 341 NCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECNCSIANMDGKVGSCGFN 420
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVKAGSM 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 421 SRILTHvYPIRLVkvnedtmeplrDSEGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSAtnkKIAHSVfrkGDSAYL 500
Cdd:cd05974 255 GRPLPG-YRVALL-----------DPDGA--PATEGEVALDLGDTR---PVGLMKGYAGDPD---KTAHAM---RGGYYR 311
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907189407 501 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 539
Cdd:cd05974 312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
97-616 |
2.69e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 72.50 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPgDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK07638 11 ASLQPNKIAIKENDRVL--TYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFCLGTSAAKALIyggemaaavaevseqlgksLLKFCSGDLGPEsilpDTQLLD-----PMLAEAPTTPlaqAPGKGM 251
Cdd:PRK07638 88 ELKERLAISNADMIV-------------------TERYKLNDLPDE----EGRVIEidewkRMIEKYLPTY---APIENV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAF--GHHSYSMRAADVLYDCLPLYHSAgNIMGVGQCVIYGLTVVLRKKF 328
Cdd:PRK07638 142 QNAPFYMgFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 329 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPvRDVEQRHRVrlaVGNGlrpAIW-----EEFTQRFGVPQIGEFYGATEC 403
Cdd:PRK07638 219 IPNQVLDKLETENISVMYTVPTMLESLYKEN-RVIENKMKI---ISSG---AKWeaeakEKIKNIFPYAKLYEFYGASEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 404 NCSIANMDG----KVGSCGfnsrilTHVYPIRLVKVNEDTMEplrdseglcipCQPGEpgllVGQINQQDPLRrFDGYVS 479
Cdd:PRK07638 292 SFVTALVDEeserRPNSVG------RPFHNVQVRICNEAGEE-----------VQKGE----IGTVYVKSPQF-FMGYII 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 480 DSATNKKIAhsvfrkgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgv 558
Cdd:PRK07638 350 GGVLARELN-------ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS-- 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 559 egKAGMAAIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQ 616
Cdd:PRK07638 421 --YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
93-303 |
2.71e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.01 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 93 FQAVARRQPERLALV-----DASSGICW---TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 164
Cdd:PRK09274 12 LPRAAQERPDQLAVAvpggrGADGKLAYdelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 165 VAALLNVNLRREPLAFCLGTSAAKALIygGEMAAAVAEVSEQLGKSLLKF---CSGDLGPESILPDTQLLDPMLAEAPTT 241
Cdd:PRK09274 92 VPVLVDPGMGIKNLKQCLAEAQPDAFI--GIPKAHLARRLFGWGKPSVRRlvtVGGRLLWGGTTLATLLRDGAAAPFPMA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189407 242 PLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRAADVLYDCLPLY 303
Cdd:PRK09274 170 DLAP------DDMAAILFTSGSTGTPKGVVYTHGMFEAqIEALRED-YGIEPGEIDLPTFPLF 225
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
133-553 |
2.90e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.91 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 133 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtSAAKALiyggEMAAAVAEVSEQLGKS-- 210
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFE--------EAKSAM----LLVRPVMLVTDETCSSwy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 211 ---------------LLKFCSGDLGPE--SILPDTQLLDPMLAEaPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVV 273
Cdd:PLN02860 119 eelqndrlpslmwqvFLESPSSSVFIFlnSFLTTEMLKQRALGT-TELDYAWAP----DDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 274 HSRYY-----RIAAFGHHSysmraADVLYDCLPLYH-----SAGNIMGVGQCviygltVVLRKKFSASRFWD----DCVK 339
Cdd:PLN02860 194 HSALIvqslaKIAIVGYGE-----DDVYLHTAPLCHigglsSALAMLMVGAC------HVLLPKFDAKAALQaikqHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 340 YNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCSIANMDGKVGSCGF 419
Cdd:PLN02860 263 SMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 420 NSRILTHVYPIRLVKVNEdtmeplrdSEGLCI----P------CQPGEPGllVGQINQQDP---LRRFDGYVSDSATnkk 486
Cdd:PLN02860 343 PKQTLQTVNQTKSSSVHQ--------PQGVCVgkpaPhvelkiGLDESSR--VGRILTRGPhvmLGYWGQNSETASV--- 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 487 iahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:PLN02860 410 ------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-617 |
3.09e-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: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVL------R 325
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 326 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV-RDVEQrhrVRLAVGNG--LRPAIWEEFTQRFGVPqIGEFYGATE 402
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVnADISS---LRFAMSGAapLPVELRARFEDATGLP-VVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CNCSIA----NMDGKVGSCGFNsrilthvYPIRLVKVNEDtmeplrDSEGLCI-PCQPGEpgllVGQINQQDPlRRFDGY 477
Cdd:cd05944 158 ATCLVAvnppDGPKRPGSVGLR-------LPYARVRIKVL------DGVGRLLrDCAPDE----VGEICVAGP-GVFGGY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 V-SDSATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRllgQTDVAVYGvAVP 556
Cdd:cd05944 220 LyTEGNKNAFVADGWLNTGDLGRL-------DADGYLFITGRAKDLIIRGGHNIDPALIEEALLR---HPAVAFAG-AVG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 557 GVEGKAGMAAIAdpHSQLDPNSMYQELQkvLASYAR---------PIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:cd05944 289 QPDAHAGELPVA--YVQLKPGAVVEEEE--LLAWARdhvperaavPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
101-618 |
3.69e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGICWtfaqLDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 178
Cdd:PRK08162 32 PDRPAVIHGDRRRTW----AETYARCrrLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPEsiLPDTQLL-----DPMLAEAPTTPLAQAPgkgmDD 253
Cdd:PRK08162 108 AFMLRHGEAKVLIVDTEFAEVAREALALLPGPKP-LVIDVDDPE--YPGGRFIgaldyEAFLASGDPDFAWTLP----AD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 254 RLFYI---YTSGTTGLPKaAIVVHSRYYRIAAFGHH-SYSMRAADVLYDCLPLYHSagNimgvGQC------VIYGLTVV 323
Cdd:PRK08162 181 EWDAIalnYTSGTTGNPK-GVVYHHRGAYLNALSNIlAWGMPKHPVYLWTLPMFHC--N----GWCfpwtvaARAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 324 LRkKFSASRFWDDCVKYNctVVQYIGE-ICRYLL-------RQPVrdveqRHRVRLAVGNGLRPAIWEEFTQRFGVpQIG 395
Cdd:PRK08162 254 LR-KVDPKLIFDLIREHG--VTHYCGApIVLSALinapaewRAGI-----DHPVHAMVAGAAPPAAVIAKMEEIGF-DLT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 396 EFYGATECNcsianmdGKVGSC---------------GFNSRilTHV-YPIR--LVKVNEDTMEPL-RDSEGLcipcqpG 456
Cdd:PRK08162 325 HVYGLTETY-------GPATVCawqpewdalplderaQLKAR--QGVrYPLQegVTVLDPDTMQPVpADGETI------G 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 457 E---PGLLVgqinqqdplrrFDGYVSdsatNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 533
Cdd:PRK08162 390 EimfRGNIV-----------MKGYLK----NPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 534 EVEAVLSRLLGQTDVAVygVAVPG----------VEGKAGMAAIADphsqldpnsmyqEL----QKVLASYARP--IFLR 597
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAV--VAKPDpkwgevpcafVELKDGASATEE------------EIiahcREHLAGFKVPkaVVFG 518
|
570 580
....*....|....*....|.
gi 1907189407 598 LLPQvdtTGTFKIQKTRLQRE 618
Cdd:PRK08162 519 ELPK---TSTGKIQKFVLREQ 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
253-617 |
1.04e-12 |
|
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: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAaiVVHSRYYRIAAF--GHHSYSMRAADVLYDCLPLYHSAGnIMGVGQCVIYGLTVVLRKKFSA 330
Cdd:cd17630 1 RLATVILTSGSTGTPKA--VVHTAANLLASAagLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 331 SRfwDDCVKYNCTVVQYIGEICRYLLRQPVrDVEQRHRVR-LAVGNGlrpAIWEEFTQRF---GVPqIGEFYGATEcncs 406
Cdd:cd17630 78 LA--EDLAPPGVTHVSLVPTQLQRLLDSGQ-GPAALKSLRaVLLGGA---PIPPELLERAadrGIP-LYTTYGMTE---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 ianMDGKVGSCGFNSRILTHVYPI---RLVKVNEDTMeplrdseglcipCQPGEPGLLVGQINQQDPLRRFDGyvsdsat 483
Cdd:cd17630 147 ---TASQVATKRPDGFGRGGVGVLlpgRELRIVEDGE------------IWVGGASLAMGYLRGQLVPEFNED------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 484 nkkiahSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKAG 563
Cdd:cd17630 205 ------GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELG 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 564 MAAIA--DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQR 617
Cdd:cd17630 268 QRPVAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
72-625 |
1.18e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 71.73 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 72 LIRVRLELRRHRRAGDTIPCIFQAVARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE 151
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 152 FVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAavaevseqlgksLLKFCSGdlgpESILPDTQLL 231
Cdd:PRK12467 575 MVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA------------QLPVPAG----LRSLCLDEPA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 232 DPMLAEAP-TTPLAQAPgkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNI 309
Cdd:PRK12467 639 DLLCGYSGhNPEVALDP-----DNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 310 MGVGQcVIYGLTVVLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGLRPAI---WE 383
Cdd:PRK12467 714 ELFGA-LASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLlarVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 384 EFTqrfgvPQIGEF--YGATEcncsiANMDGKVGSCGFNSRILTHVyPIRlvkvnedtmEPLRDSeGLCI------PCQP 455
Cdd:PRK12467 793 ALG-----PGARLInhYGPTE-----TTVGVSTYELSDEERDFGNV-PIG---------QPLANL-GLYIldhylnPVPV 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 456 GEPG-LLVGqinqQDPLRRfdGYVSDSA-TNKKIAHSVF-RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 532
Cdd:PRK12467 852 GVVGeLYIG----GAGLAR--GYHRRPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIEL 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 533 TEVEAvlsRLLGQTDV--AVYgVAVPGVEGK--------AGMAAIADPHSQLDpnSMYQELQKVLASYARPIFLRLLPQV 602
Cdd:PRK12467 926 GEIEA---RLLAQPGVreAVV-LAQPGDAGLqlvaylvpAAVADGAEHQATRD--ELKAQLRQVLPDYMVPAHLLLLDSL 999
|
570 580
....*....|....*....|....
gi 1907189407 603 DTTGTFKIQKTRL-QREGFDPRQT 625
Cdd:PRK12467 1000 PLTPNGKLDRKALpKPDASAVQAT 1023
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
58-615 |
2.88e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 69.64 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 58 VCKTARRDLFGLSVLI----RVRLELRRHRRAGDTIPCIFQAV-ARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFR 132
Cdd:PRK13383 1 VAPTAARALVRSGLLNppspRAVLRLLREASRGGTNPYTLLAVtAARWPGRTAIIDDDGAL--SYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 133 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksll 212
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 213 kfcsgdlgpesilpdtqLLDPMLA---EAPTTPLAQAPGKgmddrlFYIYTSGTTGLPKAaivVHSRYYRIAAFG----- 284
Cdd:PRK13383 155 -----------------VIDPATAgaeESGGRPAVAAPGR------IVLLTSGTTGKPKG---VPRAPQLRSAVGvwvti 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 285 HHSYSMRAADVLYDCLPLYHSagniMGVGQCVI---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVR 361
Cdd:PRK13383 209 LDRTRLRTGSRISVAMPMFHG----LGLGMLMLtiaLGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 362 dVEQRH-----RVRLAVGNGLRPAIWEEFTQRFGvPQIGEFYGATECN----CSIANMD------GK-VGSCgfnsrilt 425
Cdd:PRK13383 285 -VRARNplpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGigalATPADLRdapetvGKpVAGC-------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 426 hvyPIRLVKVNEDtmeplrdseglciPCQPGEPGLLV--GQINQqdplrrfDGYVSDSAtnKKIAHSVFRKGDSAYLsgd 503
Cdd:PRK13383 355 ---PVRILDRNNR-------------PVGPRVTGRIFvgGELAG-------TRYTDGGG--KAVVDGMTSTGDMGYL--- 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 504 vlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMYQEL 583
Cdd:PRK13383 407 ----DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYL 482
|
570 580 590
....*....|....*....|....*....|..
gi 1907189407 584 QKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:PRK13383 483 KDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
88-624 |
6.53e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 68.51 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 167
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVseqLGKSLLKF----CSGD-LG-----------------PES 223
Cdd:PRK07059 100 VVNVNPLYTPreLEHQLKDSGAEAIVVLENFATTVQQV---LAKTAVKHvvvaSMGDlLGfkghivnfvvrrvkkmvPAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 224 ILPDTQLLDPMLAEAPTTPLaQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAAD--VLY 297
Cdd:PRK07059 177 SLPGHVRFNDALAEGARQTF-KPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 298 DC-LPLYH----SAGNIMGVGQCviyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLA 372
Cdd:PRK07059 256 VCaLPLYHifalTVCGLLGMRTG---GRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 373 VGNGL--RPAIWEEFTQRFGVPqIGEFYGATECN----CSIANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDS 446
Cdd:PRK07059 333 NGGGMavQRPVAERWLEMTGCP-ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS------IRDD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 447 EGLCIPC-QPGE-----PGLLVGQINQQDPLRRF---DGYvsdsatnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRD 517
Cdd:PRK07059 397 DGNDLPLgEPGEicirgPQVMAGYWNRPDETAKVmtaDGF--------------FR-------TGDVGVMDERGYTKIVD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 518 RSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVavpgvegkagmaaiADPHS---------QLDPNSMYQELQKV-- 586
Cdd:PRK07059 456 RKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV--------------PDEHSgeavklfvvKKDPALTEEDVKAFck 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1907189407 587 --LASYARPIFLRLLPQVDTTGTFKIqktrLQREGFDPRQ 624
Cdd:PRK07059 522 erLTNYKRPKFVEFRTELPKTNVGKI----LRRELRDGKA 557
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
88-295 |
7.53e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.92 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 88 TIPCIFQAVARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEgRPEFVGLWL-GLAKAGvvA 166
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAIVEAG--A 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 167 ALLNVNLRR--EPLAFCLGTSAAKALIyggemaaavaEVSEQLGKsllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLA 244
Cdd:PRK10252 534 AWLPLDTGYpdDRLKMMLEDARPSLLI----------TTADQLPR---------------FADVPDLTSLCYNAPLAPQG 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189407 245 QAPGKGM--DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADV 295
Cdd:PRK10252 589 AAPLQLSqpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDV 641
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
116-618 |
1.47e-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: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAAVAEVSEQL--GKSLLKFCSGDLGPESILPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVV 273
Cdd:cd12119 107 FLPLLEAIAPRLptVEHVVVMTDDAAMPEPAGVGVLAYEELLAAES--PEYDWPDFDENTAAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 274 HSRYYriaafgHHSYSMRAADVLY----D----CLPLYHsaGNIMGVG-QCVIYGLTVVLRKKF----SASRFWDdcvKY 340
Cdd:cd12119 185 HRSLV------LHAMAALLTDGLGlsesDvvlpVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYldpaSLAELIE---RE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 341 NCTVVQYIGEICRYLLRQPVR-DVEQRHRVRLAVGNG-LRPAIWEEFTQRfGVPQIgEFYGATE-CNCSIAN-----MDG 412
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEAnGRDLSSLRRVVIGGSaVPRSLIEAFEER-GVRVI-HAWGMTEtSPLGTVArppseHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 413 KVGSCGFNSRILTHvYPIRLVK---VNEDTMEPLRDSEGLcipcqpGE-----PGLLVGQINQQDPLRRF--DGYvsdsa 482
Cdd:cd12119 332 LSEDEQLALRAKQG-RPVPGVElriVDDDGRELPWDGKAV------GElqvrgPWVTKSYYKNDEESEALteDGW----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 483 tnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKA 562
Cdd:cd12119 400 ---------LR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP----KW 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 563 G---MAAI-ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLqRE 618
Cdd:cd12119 460 GerpLAVVvLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL-RE 518
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
101-275 |
1.62e-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: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDasSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALIYGGEMAAAvaevseqlgksllkfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFY-IY 259
Cdd:cd12116 79 ILEDAEPALVLTDDALPDR-------------------------LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYvIY 133
|
170
....*....|....*.
gi 1907189407 260 TSGTTGLPKAAIVVHS 275
Cdd:cd12116 134 TSGSTGRPKGVVVSHR 149
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
92-553 |
2.07e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 67.00 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDAssGICWTFAQLDTYSNA-VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAalLN 170
Cdd:PRK08974 28 MFEQAVARYADQPAFINM--GEVMTFRKLEERSRAfAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV--VN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 171 VNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQ----------LGKSL-----------LKFCSGdLGPESILPD 227
Cdd:PRK08974 104 VNPLYTPreLEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrMGDQLstakgtlvnfvVKYIKR-LVPKYHLPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 228 tqlldpmlaeAPTTPLAQAPGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYyrIA----AFGHHSYSMR-AA 293
Cdd:PRK08974 183 ----------AISFRSALHKGRRMqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNM--LAnleqAKAAYGPLLHpGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 294 DVLYDCLPLYHsagnimgvgqcvIYGLTVvlrkkfsasrfwddcvkyNCTVVQYIGeICRYLLRQPvRDVE------QRH 367
Cdd:PRK08974 251 ELVVTALPLYH------------IFALTV------------------NCLLFIELG-GQNLLITNP-RDIPgfvkelKKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 368 RV---------------------------RLAVGNGL--RPAI---WEEFTQRFgvpqIGEFYGATECN----CSIANMD 411
Cdd:PRK08974 299 PFtaitgvntlfnallnneefqeldfsslKLSVGGGMavQQAVaerWVKLTGQY----LLEGYGLTECSplvsVNPYDLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 412 GKVGSCGFnsrilthvyPIrlvkvnEDTMEPLRDSEGLCIPcqPGEPGLLVG---QINQ---QDPlrrfdgyvsdSATNK 485
Cdd:PRK08974 375 YYSGSIGL---------PV------PSTEIKLVDDDGNEVP--PGEPGELWVkgpQVMLgywQRP----------EATDE 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 486 kiahsVFRKGdsaYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:PRK08974 428 -----VIKDG---WLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
97-615 |
2.64e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.57 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLAL--VDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLR 174
Cdd:PRK05857 24 ARQQPEAIALrrCDGTSAL--RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 175 REPLA-FCLGTSAAKALIYGGEmaaavaevseQLGKSLLKfcSGDLGPESILPDTQLLDPMLAEAPTTP-LAQAPGKGMD 252
Cdd:PRK05857 102 IAAIErFCQITDPAAALVAPGS----------KMASSAVP--EALHSIPVIAVDIAAVTRESEHSLDAAsLAGNADQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYRIA----AFGHHSYSMRAADVLYDCLPLYHSAG------NIMGVGQCVIYG-LT 321
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLANRTFFAVPdilqKEGLNWVTWVVGETTYSPLPATHIGGlwwiltCLMHGGLCVTGGeNT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLRKKFSASRfwddcVKYNCTVVQYIGEICrYLLRQPVRDVEQrhrVRLAVGNGLRpAIWEE--FTQRFGVpQIGEFYG 399
Cdd:PRK05857 250 TSLLEILTTNA-----VATTCLVPTLLSKLV-SELKSANATVPS---LRLVGYGGSR-AIAADvrFIEATGV-RTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 400 ATECNCSIANMDGKVGSCgfnSRI----LTHVYPirLVKVNedtmepLRDSEGLCIPCQPGEPGLLVGQINQQDPLRRFd 475
Cdd:PRK05857 319 LSETGCTALCLPTDDGSI---VKIeagaVGRPYP--GVDVY------LAATDGIGPTAPGAGPSASFGTLWIKSPANML- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 476 GYVSDSATNKKIAhsvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAV 555
Cdd:PRK05857 387 GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 556 PGVEGKAGMAAIadPHSQLDPNSMYQELQKVLASY-------ARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:PRK05857 461 EEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
115-616 |
3.32e-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: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG- 193
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 ----GEMAAAVAEvseqlgksllKFCSGDLGPESILPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKA 269
Cdd:cd05932 87 lddwKAMAPGVPE----------GLISISLPPPSAANCQYQWDDLIAQHP--PLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 270 AIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTV------------VLRKK----FSASRF 333
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 334 WddcVKYNCTVVQYIG-EICRYLLRQPVRDVEQRHRV---------RLAVGNG--LRPAIWEEFtQRFGVPqIGEFYGAT 401
Cdd:cd05932 235 W---TKFQQGVQDKIPqQKLNLLLKIPVVNSLVKRKVlkglgldqcRLAGCGSapVPPALLEWY-RSLGLN-ILEAYGMT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 402 EcNCSIANM----DGKVGSCGFNsrilthvYPIRLVKVNEDTmEPLRDSeglcipcqpgePGLLVGQinqqdplrrfdgY 477
Cdd:cd05932 310 E-NFAYSHLnypgRDKIGTVGNA-------GPGVEVRISEDG-EILVRS-----------PALMMGY------------Y 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 VSDSATNkkiahSVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEAVLSR--------LLGQTDV 548
Cdd:cd05932 358 KDPEATA-----EAFTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEhdrvemvcVIGSGLP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 549 AVYGVAVPGVEGKAGMAAIA-------------------DPHSQLDPNSMYQELQKVLASYARPiflrllpqvdttgTFK 609
Cdd:cd05932 432 APLALVVLSEEARLRADAFAraeleaslrahlarvnstlDSHEQLAGIVVVKDPWSIDNGILTP-------------TLK 498
|
....*..
gi 1907189407 610 IQKTRLQ 616
Cdd:cd05932 499 IKRNVLE 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
94-324 |
5.13e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 94 QAVARR---QPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGfAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 166
Cdd:PRK05691 13 QALQRRaaqTPDRLALRfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 167 A---------------LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgdlgPESILPDTqlL 231
Cdd:PRK05691 92 VpayppesarrhhqerLLSIIADAEPRLLLTVADLRDSLLQMEELAAANA-------------------PELLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 232 DPMLAEApttplAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAA--DVLYDCLPLYHSAGNI 309
Cdd:PRK05691 151 DPALAEA-----WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLI 225
|
250
....*....|....*
gi 1907189407 310 MGVGQCVIYGLTVVL 324
Cdd:PRK05691 226 GGLLQPIFSGVPCVL 240
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
99-275 |
7.01e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.20 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 99 RQPERLALVDAS-SGI--CWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPE-FVGLwlgLAKA------------ 162
Cdd:PRK03584 96 RRDDRPAIIFRGeDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPEtVVAM---LATAslgaiwsscspd 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 163 -GVVAALlnvnlRReplafcLGTSAAKALI------YGG---EMAAAVAEVSEQLgKSLLKFCS----GDLGPESILPDT 228
Cdd:PRK03584 173 fGVQGVL-----DR------FGQIEPKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAAALPGA 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907189407 229 QLLDPMLAEAPTTPLAQAPGkGMDDRLFYIYTSGTTGLPKAaiVVHS 275
Cdd:PRK03584 241 LLWEDFLAPAEAAELEFEPV-PFDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
101-556 |
8.25e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 65.04 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGICWTfaqlDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 178
Cdd:PLN03102 28 PNRTSIIYGKTRFTWP----QTYDRCcrLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIYGGEMAAAVAEVSeqlgkSLLKFCSGDLGPESIL---------PDTQLLD--PMLAEAPTTPLAQAp 247
Cdd:PLN03102 104 AAILRHAKPKILFVDRSFEPLAREVL-----HLLSSEDSNLNLPVIFiheidfpkrPSSEELDyeCLIQRGEPTPSLVA- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 248 gkgmddRLFYI----------YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVI 317
Cdd:PLN03102 178 ------RMFRIqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 318 YGLTVVLRkKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDveQRHR---VRLAVGNGLRPAIWEEFTQRFGVpQI 394
Cdd:PLN03102 252 GGTSVCMR-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLD--LSPRsgpVHVLTGGSPPPAALVKKVQRLGF-QV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 395 GEFYGATECNcsianmdGKVGSCGFN---SRILTH----------VYPIRLVKV---NEDTMEPL-RDSEGLcipcqpGE 457
Cdd:PLN03102 328 MHAYGLTEAT-------GPVLFCEWQdewNRLPENqqmelkarqgVSILGLADVdvkNKETQESVpRDGKTM------GE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 458 PgLLVGQINQQdplrrfdGYVSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 536
Cdd:PLN03102 395 I-VIKGSSIMK-------GYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
|
490 500
....*....|....*....|
gi 1907189407 537 AVLSRLLGQTDVAVygVAVP 556
Cdd:PLN03102 460 NVLYKYPKVLETAV--VAMP 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
92-291 |
8.89e-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: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLAlVDASSGiCWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLrrePLAFclgtsaakaliyggemaaaVAEVSEQLGKSLlkfcsgdlgpesilpdtqlldpMLAEAPttplaqapgkgm 251
Cdd:cd05918 82 SH---PLQR-------------------LQEILQDTGAKV----------------------VLTSSP------------ 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMR 291
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGRALG 143
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
102-552 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 102 ERLALVDAS---SGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 178
Cdd:cd05915 9 GRKEVVSRLhtgEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 179 AFCLGTSAAKALIYGGEMAAaVAEVSEQLGKSLLKfcsgdlGPESILPDTQLLDPMLAEAPTTplaqAPGKGMD--DRLF 256
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLP-LVEAIRGELKTVQH------FVVMDEKAPEGYLAYEEALGEE----ADPVRVPerAACG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHSYSMRAADVLYDC-LPLYHSAGnimgvgQCVIY------GLTVVLRKKF 328
Cdd:cd05915 158 MAYTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPvVPMFHVNA------WCLPYaatlvgAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 329 SASRFWDDCVKYNCTvvQYIGEICRYLLRQPVRDVEQRH---RVRLAVGNGLRPAIWEEFtQRFGVPQIGEFYGATEcnc 405
Cdd:cd05915 232 DPASLVELFDGEGVT--FTAGVPTVWLALADYLESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 406 sianMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGllVGQINQQDPLRR---FDGYVSDSA 482
Cdd:cd05915 306 ----TSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEE 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 483 TNKKIAhsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 552
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 ... |
258-556 |
2.61e-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: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 258 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGniMGVGQCVIY--GLTVVLRKkFSASRFWD 335
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 336 DCVKYNCTVVQYIGEICRYLLrqpvrDVEQRHRVRLAvgnGLR-------PaiweEFTQRFGVPQIGEF---YGATECNC 405
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLL-----DAAEKSGVDLS---SLRhvlgldaP----ETIQRFEETTGATFwslYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 406 --SIANMDGKVGSCGfnsRILthvyPIRLVKVNEDTMEPLRdseglcipcqPGEPGllvgQINQQDPLRrFDGYVSDSAT 483
Cdd:cd17637 151 lvTLSPYRERPGSAG---RPG----PLVRVRIVDDNDRPVP----------AGETG----EIVVRGPLV-FQGYWNLPEL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189407 484 NkkiAHSvFRKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 556
Cdd:cd17637 209 T---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP 277
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
116-630 |
2.77e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 63.51 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAAVAEvseqlgksllkfcSGDLGPESILPDTQLLDPmlaeAPTTPLaqapgkGMDDRLFYIYTSGTTGLPKAAIVVHS 275
Cdd:PRK06060 112 LRDRFQP-------------SRVAEAAELMSEAARVAP----GGYEPM------GGDALAYATYTSGTTGPPKAAIHRHA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 276 RYYR-IAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGV-------GQCVIYGLTVVLRKKFSASRFWDDCVKYNctVVQY 347
Cdd:PRK06060 169 DPLTfVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVwfplatgGSAVINSAPVTPEAAAILSARFGPSVLYG--VPNF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 348 IGEICRYLLRQPVRDVeqrhRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECNCS-IANM--DGKVGSCGfnsRIL 424
Cdd:PRK06060 247 FARVIDSCSPDSFRSL----RCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTfVSNRvdEWRLGTLG---RVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 425 THvYPIRLVKVNEDTMEPlrdseglcipcqPGEPGLLVgqinqQDPlrrfdgyvsdsatnkKIAHSVFRKGDSAYLSGDV 504
Cdd:PRK06060 320 PP-YEIRVVAPDGTTAGP------------GVEGDLWV-----RGP---------------AIAKGYWNRPDSPVANEGW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 505 L------VMDELGYMYFRDRSGDTFRWRGENVSTTEVEavlsRLLGQTDvAVYGVAVPGVEGKAGMAAIadpHSQLDPNS 578
Cdd:PRK06060 367 LdtrdrvCIDSDGWVTYRCRADDTEVIGGVNVDPREVE----RLIIEDE-AVAEAAVVAVRESTGASTL---QAFLVATS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 579 MyqelQKVLASYARPIFLRLLPQVDttgTFKIQKTRLQREGFdPRQTSDRLF 630
Cdd:PRK06060 439 G----ATIDGSVMRDLHRGLLNRLS---AFKVPHRFAVVDRL-PRTPNGKLV 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-625 |
5.56e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRL--SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDP 3139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALiyggemaaavaevseqLGKSLLKfcsgdlgpesiLPDTQLLDPMLAEAPTTPLAQA--PGK 249
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQLL----------------LSQSHLR-----------LPLAQGVQVLDLDRGDENYAEAnpAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 250 GMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLydclpLYHSAGNIMGVGQCVIYGLTVVLRKKF 328
Cdd:PRK12316 3193 TMPENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPLMSGARVVL 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 329 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE----QRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYGATECN 404
Cdd:PRK12316 3268 AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEeedaHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEAT 3347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 405 CSIANMDgkVGSCGFNSRILTHVYPIRLVKVNEDTMEPlrDSEGLCIPCQPGEPGLLVGQINQQDplrrfdgyvsdsATN 484
Cdd:PRK12316 3348 ITVTHWQ--CVEEGKDAVPIGRPIANRACYILDGSLEP--VPVGALGELYLGGEGLARGYHNRPG------------LTA 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 485 KKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQTDVAVYGVAVPGVEGKAGM 564
Cdd:PRK12316 3412 ERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL-----LEHPWVREAVVLAVDGRQLV 3486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 565 AAIADPHSQLD-PNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQT 625
Cdd:PRK12316 3487 AYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-615 |
5.85e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKL--TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIyggemaaAVAEVSEQL----GKSLLkfcsgDLGPESILPDTQLLDPMLAEAPttplaqap 247
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLL-------TQSHLLQRLpipdGLASL-----ALDRDEDWEGFPAHDPAVRLHP-------- 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 248 gkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPlYHSAGNIMGVGQCVIYGLTVVLRK 326
Cdd:PRK12316 4694 -----DNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 327 kfsaSRFWD------DCVKYNCTVVQYIGEICRYLLRQPVRDVE-QRHRVRLAVGNGLRPAIWEEFTQRFGVPQIGEFYG 399
Cdd:PRK12316 4768 ----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYG 4843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 400 ATECNCSIANMDGKVGS-CGFNSRILTHVYPIRLVKVNEDTMEPLrdseglciPC-QPGEpgLLVGqinqQDPLRRfdGY 477
Cdd:PRK12316 4844 PTETTVTVLLWKARDGDaCGAAYMPIGTPLGNRSGYVLDGQLNPL--------PVgVAGE--LYLG----GEGVAR--GY 4907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 VSDSA-TNKKIAHSVFRK-GDSAYLSGDVL------VMDELGymyfrdRSGDTFRWRGENVSTTEVEAvlsRLLGQTDV- 548
Cdd:PRK12316 4908 LERPAlTAERFVPDPFGApGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIEA---RLREHPAVr 4978
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 549 -AVYgVAVPGVEGK--AGMAAIADPHSQLDP-------NSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:PRK12316 4979 eAVV-IAQEGAVGKqlVGYVVPQDPALADADeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
97-615 |
8.84e-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: 61.49 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDAssGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNvnlrre 176
Cdd:cd05945 1 AAANPDRPAVVEG--GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 plafclGTSAAkaliyggEMAAAVAEVSeqlgksllkfcsgdlGPESILPDtqlldpmlaeapttplaqapgkgmDDRLF 256
Cdd:cd05945 73 ------ASSPA-------ERIREILDAA---------------KPALLIAD------------------------GDDNA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 257 YI-YTSGTTGLPKAaiVVHSrYYRIAAFGHHS---YSMRAADVLYdCLPLYHSAGNIMGVGQCVIYGLTVV-LRKKFSAS 331
Cdd:cd05945 101 YIiFTSGSTGRPKG--VQIS-HDNLVSFTNWMlsdFPLGPGDVFL-NQAPFSFDLSVMDLYPALASGATLVpVPRDATAD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 332 --RFWDDCVKYNCTV---VQYIGEICrylLRQPVRDVEQRHRVRLAVGNGlrpaiwEEFT--------QRFGVPQIGEFY 398
Cdd:cd05945 177 pkQLFRFLAEHGITVwvsTPSFAAMC---LLSPTFTPESLPSLRHFLFCG------EVLPhktaralqQRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 399 GATECN--CSIANMDGKVgsCGFNSRIlthvyPIRLVKVNEDTMepLRDSEGLCIPcqPGEPG--LLVGQinqqdplRRF 474
Cdd:cd05945 248 GPTEATvaVTYIEVTPEV--LDGYDRL-----PIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP-------SVS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 475 DGYVSDSATNKKIAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVA 554
Cdd:cd05945 310 KGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VP 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 555 VPGVEGKAGMAAIADPH---SQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05945 386 KYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
112-570 |
1.12e-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: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 112 GICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALi 191
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 192 yggemaaavaevseqlgksllkFCSgdlgpesilpdtqllDPmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAI 271
Cdd:cd05914 84 ----------------------FVS---------------DE------------------DDVALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 272 VVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFwDDCVKYNCTVV------ 345
Cdd:cd05914 109 LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-IALAFAQVTPTlgvpvp 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 346 -------------QYIGEICRYLLRQPVRDVEQRHRVRLAV--------------GNGLRPAIwEEFTQRFGVPQIgEFY 398
Cdd:cd05914 188 lviekifkmdiipKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggnikefvigGAKINPDV-EEFLRTIGFPYT-IGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 399 GATECN---CSIANMDGKVGSCGFnsrilthvyPIRLVKVNEDTMEPlrdseglcipcQPGEPGLLVGQINQqdplrrFD 475
Cdd:cd05914 266 GMTETApiiSYSPPNRIRLGSAGK---------VIDGVEVRIDSPDP-----------ATGEGEIIVRGPNV------MK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 476 GYVSdsatNKKIAHSVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEAVLSRLlgqTDVAVYGVA 554
Cdd:cd05914 320 GYYK----NPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNM---PFVLESLVV 391
|
490
....*....|....*.
gi 1907189407 555 VpgVEGKAGMAAIADP 570
Cdd:cd05914 392 V--QEKKLVALAYIDP 405
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
134-307 |
2.89e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.02 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 134 LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAF------------CLGTSAAKALIYGGEMAAAVA 201
Cdd:PRK09192 69 LGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL-----PMGFggresyiaqlrgMLASAQPAAIITPDELLPWVN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 202 EVSEqlGKSLLKfcsgdlgpesILPDTQLldpMLAEAPTTPLAQA-PgkgmDDRLFYIYTSGTTGLPKAAIVVH-SRYYR 279
Cdd:PRK09192 144 EATH--GNPLLH----------VLSHAWF---KALPEADVALPRPtP----DDIAYLQYSSGSTRFPRGVIITHrALMAN 204
|
170 180
....*....|....*....|....*...
gi 1907189407 280 IAAFGHHSYSMRAADVLYDCLPLYHSAG 307
Cdd:PRK09192 205 LRAISHDGLKVRPGDRCVSWLPFYHDMG 232
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
94-618 |
6.59e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 59.01 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 94 QAVARRQPERLALVDASS--GICWTFAQLDTYSNAVANLFRQL-GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaaLLN 170
Cdd:PRK05677 27 QAVLKQSCQRFADKPAFSnlGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI--VVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 171 VN---LRREpLAFCLGTSAAKALIYGGEMA--------------AAVAEVSEQLG-------KSLLKFCSgDLGPESILP 226
Cdd:PRK05677 105 TNplyTARE-MEHQFNDSGAKALVCLANMAhlaekvlpktgvkhVIVTEVADMLPplkrlliNAVVKHVK-KMVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 227 DTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGHHSYSMRAADVLYDC------L 300
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRN---LVANMLQCRALMGSNLNEGCeiliapL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 301 PLYH------SAGNIMGVGQCVIY--------GLTVVLRK-KFSAsrFwddcVKYNCTVVQyigeICRyllRQPVRDVE- 364
Cdd:PRK05677 259 PLYHiyaftfHCMAMMLIGNHNILisnprdlpAMVKELGKwKFSG--F----VGLNTLFVA----LCN---NEAFRKLDf 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 365 QRHRVRLAVGNGLRPAIWEEFTQRFGVPqIGEFYGATECN--CSIANMDG-KVGSCGFNsrilthvYPIRLVKVNEDTME 441
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETSpvVSVNPSQAiQVGTIGIP-------VPSTLCKVIDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 442 --PLRDSEGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRS 519
Cdd:PRK05677 398 elPLGEVGELCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIALIQEDGYMRIVDRK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 520 GDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AIADPHSQLDPNSMYQELQKVLASYARPIF 595
Cdd:PRK05677 456 KDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEHMRANLTGYKVPKA 531
|
570 580
....*....|....*....|...
gi 1907189407 596 LRLLPQVDTTGTFKIQKTRLQRE 618
Cdd:PRK05677 532 VEFRDELPTTNVGKILRRELRDE 554
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
101-282 |
7.86e-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: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 101 PERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 180
Cdd:cd17652 1 PDAPAVVFGDETL--TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 181 CLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapTTPlaqapgkgmdDRLFY-IY 259
Cdd:cd17652 79 MLADARPALLL------------------------------------------------TTP----------DNLAYvIY 100
|
170 180
....*....|....*....|...
gi 1907189407 260 TSGTTGLPKAAIVVHSRYYRIAA 282
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAA 123
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
116-600 |
8.12e-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: 58.48 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvaallnvnlrreplafclgtsAAKALIYGGE 195
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIG----------------------AIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPL-------------AQAPGKGMD---------- 252
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHhvlvlnrpqvpadLTKPGRDLDwsellakaep 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 ---------DRLFYIYTSGTTGLPKAaIVVHSRYYRIAAfghhSYSMRAadvLYDCLP--LYHSAGNImG--VGQCVI-Y 318
Cdd:cd05967 222 vdcvpvaatDPLYILYTSGTTGKPKG-VVRDNGGHAVAL----NWSMRN---IYGIKPgdVWWAASDV-GwvVGHSYIvY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 319 G------LTVVLRKKFS----ASRFWDDCVKYNCTVVQYIGEICRYLLRQP-----VRDVE-QRHRVRLAVGNGLRPAIW 382
Cdd:cd05967 293 GpllhgaTTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDlSSLRTLFLAGERLDPPTL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 383 EEFTQRFGVPQIgEFYGATE------CNCS-IANMDGKVGSC-----GFNsrilthvypirlVKVNEDTMEPLRDSE--G 448
Cdd:cd05967 373 EWAENTLGVPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGYQ------------VQVLDEDGEPVGPNElgN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 449 LCIPCqPGEPGLLVGQINQQDplrRF-DGYVSDSatnkkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 527
Cdd:cd05967 440 IVIKL-PLPPGCLLTLWKNDE---RFkKLYLSKF--------------PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 528 ENVSTTEVEAVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AIADPHSQLDPNSMYQELQKV-------LASYARPIFLRLL 599
Cdd:cd05967 502 HRLSTGEMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKELVALvreqigpVAAFRLVIFVKRL 580
|
.
gi 1907189407 600 P 600
Cdd:cd05967 581 P 581
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
252-553 |
2.38e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 57.19 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYS-----MRAADVLYDCLPLYH----SAGNI--MGVGqcviyGL 320
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHifalTANGLvfMKIG-----GC 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 321 TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRLAVGNGL--RPAIWEEFTQRFGVPQIgEFY 398
Cdd:PRK08751 283 NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 399 GATECNcsianmdgkVGSCgfnsrilthVYPIRLVKVNEDTMEPLrDSEGLCIPCQPGEpGLLVGQINQ---QDPlRRFD 475
Cdd:PRK08751 362 GLTETS---------PAAC---------INPLTLKEYNGSIGLPI-PSTDACIKDDAGT-VLAIGEIGElciKGP-QVMK 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 476 GYVSDSATNKKIAHSvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 553
Cdd:PRK08751 421 GYWKRPEETAKVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
97-307 |
3.06e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.42 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVdaSSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 176
Cdd:PRK09029 13 AQVRPQAIALR--LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLafclgtsaakaliyggemaaavAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPTTPLAQAPgkgMddrlf 256
Cdd:PRK09029 91 LL----------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLAT---M----- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189407 257 yIYTSGTTGLPKAaiVVHSryyriaaFGHHSYSmrAADVL----YDC-------LPLYHSAG 307
Cdd:PRK09029 141 -TLTSGSTGLPKA--AVHT-------AQAHLAS--AEGVLslmpFTAqdswllsLPLFHVSG 190
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-294 |
3.35e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.10 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 83 RRAGDTIPCIFQAVARRQPERLALVDASSGICwtFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 162
Cdd:PRK05691 2184 ARLDQTLHGLFAAQAARTPQAPALTFAGQTLS--YAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 163 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqLGKSLLKFCsgdlgpesiLPDTQlldPMLAEAPTTP 242
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE----LPAGVARWC---------LEDDA---AALAAYSDAP 2325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 243 LAQAPGKgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGhhsysMRAAD 294
Cdd:PRK05691 2326 LPFLSLP--QHQAYLIYTSGSTGKPKGVVVSHGEIAMhcqavIERFG-----MRADD 2375
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
253-612 |
6.84e-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: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYriAAFGH---HSYSMRAADVLYDCLPLYHSAGN------IMGVGQCVIYGLTVV 323
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHIGGLwwiltcLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 324 LRKKFSASRFWDdcVKYNCTVVQYIGEICRyLLRQPVRDVEQrhrVRLAVGNGLRP-AIWEEFTQRFGVPQIGEFYGATE 402
Cdd:cd17635 80 YKSLFKILTTNA--VTTTCLVPTLLSKLVS-ELKSANATVPS---LRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 403 CN--CSIANMDG--KVGSCGfnsriltHVYPIRLVKV-NEDTMEPLRDSEGLCIPCQPgepgllvgqinqqdplRRFDGY 477
Cdd:cd17635 154 TGtaLCLPTDDDsiEINAVG-------RPYPGVDVYLaATDGIAGPSASFGTIWIKSP----------------ANMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 478 VSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvAVP 556
Cdd:cd17635 211 WN----NPERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EIS 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 557 GVEGKAGMAAIADPHSQLDPNSMYQELQKV---LASYARPIFLRLLPQVDTTGTFKIQK 612
Cdd:cd17635 282 DEEFGELVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
534-609 |
7.01e-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: 7.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 534 EVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-275 |
7.07e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALVDASSGIcwTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 171
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETL--DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 172 NLRREPLAFCLGTSAAKALIyggemaaavaevSEQlgkSLLKFCSGDLGPESILPD--TQLLDPMLAEAPTTPLAQapgk 249
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLL------------SQS---HLGRKLPLAAGVQVLDLDrpAAWLEGYSEENPGTELNP---- 654
|
170 180
....*....|....*....|....*..
gi 1907189407 250 gmdDRLFY-IYTSGTTGLPKAAIVVHS 275
Cdd:PRK12316 655 ---ENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
253-602 |
1.18e-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: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 253 DRLFYIYTSGTTGLPKAAIVVHSRYYRI----AAFGHHSYSM---------RAAD-VLYDCLPLYHSAGNIMGVGQcVIY 318
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMlmggADFGTGEFTPsedahkaaaAAAGtVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 319 GLTVVL-RKKFSASRFWDDCVKYNCTVVQYIGEIcryLLRQPVRDVEQRHRVRL----AVGNGlrPAIW-EEFTQRF--G 390
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVTSMTIVGDA---MARPLIDALRDAGPYDLsslfAISSG--GALLsPEVKQGLleL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 391 VPQIG--EFYGATEcncSIANMDGKVGSCGFNSRILTHVYPiRLVKVNEDTMEPLRDSEGlcipcqpgepgllVGQINQQ 468
Cdd:cd05924 158 VPNITlvDAFGSSE---TGFTGSGHSAGSGPETGPFTRANP-DTVVLDDDGRVVPPGSGG-------------VGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 469 D--PLrrfdGYVSDSatnKKIAHSVFRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 545
Cdd:cd05924 221 GhiPL----GYYGDE---AKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189407 546 TDVAVYGVAVP--GVEgkagMAAI--ADPHSQLDPNSMYQELQKVLASYARPIFLRLLPQV 602
Cdd:cd05924 294 YDVLVVGRPDErwGQE----VVAVvqLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEI 350
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
116-615 |
2.24e-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: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygGE 195
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI--GI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 maaavaevseqlgksllkfcsgdlgpesilpdtqlldpmlaeapttPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 275
Cdd:cd05910 82 ----------------------------------------------PKA-------DEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 276 RYY-RIAAFgHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCV-----IYGLTVVLRKKFSASRfwddcvKYNCTVV---- 345
Cdd:cd05910 109 TFAaQIDAL-RQLYGIRPGEVDLATFPLFALFGPALGLTSVIpdmdpTRPARADPQKLVGAIR------QYGVSIVfgsp 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 346 QYIGEICRYLLRQPvRDVEQRHRVrLAVGNGLRPAIWEEFtqRFGVPQIGEF---YGATEC--NCSIANMD--------- 411
Cdd:cd05910 182 ALLERVARYCAQHG-ITLPSLRRV-LSAGAPVPIALAARL--RKMLSDEAEIltpYGATEAlpVSSIGSREllatttaat 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 412 -GKVGSCgfnsriLTHVYPIRLVKVNEDTMEPLRDSEG-LCIPcqPGEpgllVGQINQQDPLrrfdgyVSDSATNKKIAH 489
Cdd:cd05910 258 sGGAGTC------VGRPIPGVRVRIIEIDDEPIAEWDDtLELP--RGE----IGEITVTGPT------VTPTYVNRPVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 490 SVFRKGDSA----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAG-- 563
Cdd:cd05910 320 ALAKIDDNSegfwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLcv 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 564 --MAAIADPHSQLdpnsmYQELQKVLASYA-----RPIFLRLLPQVDTTGTFKIQKTRL 615
Cdd:cd05910 400 epLPGTITPRARL-----EQELRALAKDYPhtqriGRFLIHPSFPVDIRHNAKIFREKL 453
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
89-283 |
3.16e-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: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 89 IPCIFQAVARRQPERLALVDASSGIC-------WTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAK 161
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 162 AGVVAALLNVNLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAE---- 237
Cdd:TIGR03443 318 AGATFSVIDPAYPPARQTIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVggsl 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 238 --------APTTPLAQAPGK---GMDDRLFYIYTSGTTGLPKAaivVHSRYYRIAAF 283
Cdd:TIGR03443 390 eggetdvlAPYQALKDTPTGvvvGPDSNPTLSFTSGSEGIPKG---VLGRHFSLAYY 443
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
100-539 |
1.38e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 51.38 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 100 QPERLALVDASSGICWtfaqLDTYSNA--VANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREP 177
Cdd:PLN02479 33 HPTRKSVVHGSVRYTW----AQTYQRCrrLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 178 LAFCLGTSAAKALIYGGEMAAAVAE----VSEQLGKSL---LKFCSGD-----------LGPESILPDTQLL--DPMLAE 237
Cdd:PLN02479 109 IAFLLEHSKSEVVMVDQEFFTLAEEalkiLAEKKKSSFkppLLIVIGDptcdpkslqyaLGKGAIEYEKFLEtgDPEFAW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 238 APTTPLAQAPGKGmddrlfyiYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVI 317
Cdd:PLN02479 189 KPPADEWQSIALG--------YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 318 YGLTVVLRKkFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD--VEQRHRVRLAV-GNGLRPAIWEEFTQR-FGVPQ 393
Cdd:PLN02479 261 CGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTaGAAPPPSVLFAMSEKgFRVTH 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 394 ---IGEFYG-ATECN----------CSIANMDGKVGscgfnsriLTHVYPIRLVKVNEDTMEPLrdseglcipcqPGEpG 459
Cdd:PLN02479 340 tygLSETYGpSTVCAwkpewdslppEEQARLNARQG--------VRYIGLEGLDVVDTKTMKPV-----------PAD-G 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 460 LLVGQInqqdpLRRFDGYVSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 539
Cdd:PLN02479 400 KTMGEI-----VMRGNMVMKGYLKNPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
116-275 |
1.48e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 51.52 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 maaAVAEVSEQLGKSLLKFCS----GDLgPES-------ILPDTQLLDPMLAEAPTTPLaqaPGKGMDDRLFYI-YTSGT 263
Cdd:PTZ00216 203 ---NVPNLLRLMKSGGMPNTTiiylDSL-PASvdtegcrLVAWTDVVAKGHSAGSHHPL---NIPENNDDLALImYTSGT 275
|
170
....*....|..
gi 1907189407 264 TGLPKAaiVVHS 275
Cdd:PTZ00216 276 TGDPKG--VMHT 285
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
252-617 |
1.61e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.44 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 252 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRIAAFgHHSYSMRAADVLY---DClplyhsaGNIMGvGQCVIYG-----LT 321
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITG-HSYVTYGpmlngAT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVEQRHRVRL----AVGNGLRPAIWEEFTQRFGvpq 393
Cdd:PLN02654 346 VLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLrvlgSVGEPINPSAWRWFFNVVG--- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 394 igefygatECNCSIANMDGKVGSCGFNSRILTHVYP------------IRLVKVNEDTMEPLRDSEG-LCIPCQ-PGEPG 459
Cdd:PLN02654 423 --------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCVKKSwPGAFR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 460 LLVGQINQQDP--LRRFDGYvsdsatnkkiahsvfrkgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 537
Cdd:PLN02654 495 TLYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVES 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 538 VLSRLLGQTDVAVYGV--AVPGvEGKAGMAAIAD--PHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKT 613
Cdd:PLN02654 554 ALVSHPQCAEAAVVGIehEVKG-QGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRR 632
|
....
gi 1907189407 614 RLQR 617
Cdd:PLN02654 633 ILRK 636
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
92-307 |
2.79e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 50.73 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAV--ARRQ--PERLALVDASSGICwTFAQLDTYSNAVANLFRQlGFAPGDVVAVFLegrPEFVGL---WLGLAKAGV 164
Cdd:PRK06814 633 LFEALieAAKIhgFKKLAVEDPVNGPL-TYRKLLTGAFVLGRKLKK-NTPPGENVGVML---PNANGAavtFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 165 VAALLN-----VNLrrepLAFCLGTS-----AAKALIYGGEMAAAVAEVSEQLGKSLLkfcsgdlgpESILPDTQLLDPM 234
Cdd:PRK06814 708 VPAMINfsagiANI----LSACKAAQvktvlTSRAFIEKARLGPLIEALEFGIRIIYL---------EDVRAQIGLADKI 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 235 LAE-APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAA---FGhhsysmrAADVLYDCLPLYHSA 306
Cdd:PRK06814 775 KGLlAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFHSF 847
|
.
gi 1907189407 307 G 307
Cdd:PRK06814 848 G 848
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
248-547 |
3.14e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.20 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 248 GKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYHSAG-NIMGV-----GQCVIYGLT 321
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLfpllsGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 322 VVLRKKFsaSRFWDDcvkyncTVVQYIGE---ICRYLLRQPVRDVEQRHRVRLAV--GNGLRPAIWEEFTQRFGVPQIGE 396
Cdd:PRK06334 259 PLYPKKI--VEMIDE------AKVTFLGStpvFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 397 FYGATECN--CSIANMDG-KVGSCgfnsrilthvypirlVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVGQINQQdplrr 473
Cdd:PRK06334 331 GYGTTECSpvITINTVNSpKHESC---------------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL----- 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189407 474 FDGYVSDSATNKKIAHSvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 547
Cdd:PRK06334 391 FSGYLGEDFGQGFVELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNA 460
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
115-304 |
5.63e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 49.71 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 W-TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 193
Cdd:PLN02736 78 WmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE----WLIVDHACSAYSYVSV-----PLYDTLGPDAVKFIVNH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 GEMAAAVaeVSEQLGKSLLKFCSgDL----------GPESILPDTQL--------LDPMLAEAPTTPLAQAPGKGmDDRL 255
Cdd:PLN02736 149 AEVAAIF--CVPQTLNTLLSCLS-EIpsvrlivvvgGADEPLPSLPSgtgveivtYSKLLAQGRSSPQPFRPPKP-EDVA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189407 256 FYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDCLPLYH 304
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
97-571 |
6.36e-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: 49.48 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALV----DASSGICWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvn 172
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 173 lrreplafclgtsaaKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPT---------TPL 243
Cdd:cd05966 136 ---------------HSVVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKCPSvekvlvvkrTGG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 244 AQAPGKGMD----------------------DRLFYIYTSGTTGLPKAaiVVHS----------------------RYYR 279
Cdd:cd05966 201 EVPMTEGRDlwwhdlmakqspecepewmdseDPLFILYTSGSTGKPKG--VVHTtggyllyaattfkyvfdyhpddIYWC 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 280 IAAFG---HHSYsmraadVLYDclPLyhsagnimgvgqcvIYGLTVVLrkkF-------SASRFWDDCVKYNCTVVQYIG 349
Cdd:cd05966 279 TADIGwitGHSY------IVYG--PL--------------ANGATTVM---FegtptypDPGRYWDIVEKHKVTIFYTAP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 350 EICRYLLRQPvRDVEQRH-----RVRLAVGNGLRPAIWEEFTQRFG---VPqIGEFYGATEC-NCSIANMDG----KVGS 416
Cdd:cd05966 334 TAIRALMKFG-DEWVKKHdlsslRVLGSVGEPINPEAWMWYYEVIGkerCP-IVDTWWQTETgGIMITPLPGatplKPGS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 417 CGFnsrilthvyP---IRLVKVNEDTMEPLRDSEG-LCIPcQPGePGLLVGQINqqDPLRRFDGYvsdsatnkkiahsvF 492
Cdd:cd05966 412 ATR---------PffgIEPAILDEEGNEVEGEVEGyLVIK-RPW-PGMARTIYG--DHERYEDTY--------------F 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 493 RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgqtdvavygVAVPGVegkAGMAAIADPH 571
Cdd:cd05966 465 SKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVGRPH 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
92-539 |
7.99e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.05 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLALvdASSGICWTFAQLDTYSNAVANLFRQ-LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaaLLN 170
Cdd:PRK12492 29 VFERSCKKFADRPAF--SNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLI--VVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 171 VN---LRREpLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGP--ESILPDTqLLDPMLAEAPTTPLA 244
Cdd:PRK12492 105 TNplyTARE-MRHQFKDSGARALVYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLPaaKGWLVNT-VVDKVKKMVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 245 QAPG-----------------KGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGH-----HSYSMRAADVLY 297
Cdd:PRK12492 183 QAVPfkqalrqgrglslkpvpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvRACLSQlgpdgQPLMKEGQEVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 298 DCLPLYHsagnimgvgqcvIYGLT-------------VVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP-VRDV 363
Cdd:PRK12492 263 APLPLYH------------IYAFTancmcmmvsgnhnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPgFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 364 EQRH-RVRLAVGNGLRPAIWEEFTQRFGVpQIGEFYGATECN-CSIANMDGKVgscgfnSRILTHVYPI--RLVKV-NED 438
Cdd:PRK12492 331 DFSAlKLTNSGGTALVKATAERWEQLTGC-TIVEGYGLTETSpVASTNPYGEL------ARLGTVGIPVpgTALKViDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 439 TME-PLRDSEGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKI-AHSVFRkgdsaylSGDVLVMDELGYMYFR 516
Cdd:PRK12492 404 GNElPLGERGELCIK----GPQVMKGYWQQPE------------ATAEALdAEGWFK-------TGDIAVIDPDGFVRIV 460
|
490 500
....*....|....*....|...
gi 1907189407 517 DRSGDTFRWRGENVSTTEVEAVL 539
Cdd:PRK12492 461 DRKKDLIIVSGFNVYPNEIEDVV 483
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
116-620 |
9.78e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 48.59 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 195
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 196 MAAAVAEVSEQLgKSLLKFCSgdLGPESILPDTQLLDpmlAEAPTTPLAQAPG----KGMDDRLF--YIYTSGTTGLPKA 269
Cdd:PRK06018 121 FVPILEKIADKL-PSVERYVV--LTDAAHMPQTTLKN---AVAYEEWIAEADGdfawKTFDENTAagMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 270 AI------VVHSryyrIAAFGHHSYSMRAADVLYDCLPLYHSagNIMGVGqcviygltvvlrkkFSASRFWDDCVKYNCt 343
Cdd:PRK06018 195 VLyshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA--NSWGIA--------------FSAPSMGTKLVMPGA- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 344 vvQYIGEICRYLLrqpvrDVEQrhrVRLAVGnglRPAIWEEFTQ-----RFGVPQIGEFY-GATECNCSIANMDGKVGSC 417
Cdd:PRK06018 254 --KLDGASVYELL-----DTEK---VTFTAG---VPTVWLMLLQymekeGLKLPHLKMVVcGGSAMPRSMIKAFEDMGVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 418 GFNSRILTHVYPIRLVKVNEDTMEPLRDSEGLCIPCQPGEPGLLVgQINQQDPLRR---FDG------YVSDSAtnkkIA 488
Cdd:PRK06018 321 VRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDAGKelpWDGktfgrlKVRGPA----VA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 489 HSVFRKGDSA------YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE--AVlsrllGQTDV---AVYGVAVPG 557
Cdd:PRK06018 396 AAYYRVDGEIldddgfFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnlAV-----GHPKVaeaAVIGVYHPK 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189407 558 VEGKAGMAAIADPHSQLDPNSMYQELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 620
Cdd:PRK06018 471 WDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPddvAFVDAIPH---TATGKILKTAL-REQF 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
92-272 |
2.70e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 92 IFQAVARRQPERLAL--VDASsgicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL 169
Cdd:PRK05691 3725 LFEAQVAAHPQRIAAscLDQQ----WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 170 NVNLRREPLAFCLGTSAAKALIyggeMAAAVAEvseqLGKSLLKFCSGDLGPesilpdtQLLdpMLAEAPTTPLAQA-PG 248
Cdd:PRK05691 3801 DPGLPAQRLQRIIELSRTPVLV----CSAACRE----QARALLDELGCANRP-------RLL--VWEEVQAGEVASHnPG 3863
|
170 180
....*....|....*....|....*.
gi 1907189407 249 --KGMDDRLFYIYTSGTTGLPKAAIV 272
Cdd:PRK05691 3864 iySGPDNLAYVIYTSGSTGLPKGVMV 3889
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
99-317 |
4.36e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.52 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 99 RQPERLALVDASSGicWTFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV--VAALLNVNlRRE 176
Cdd:PRK10946 35 AASDAIAVICGERQ--FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVapVNALFSHQ-RSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 177 PLAFC-------LGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGpesilpdtqLLDPMLAEAPTTPLAQAPGk 249
Cdd:PRK10946 112 LNAYAsqiepalLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHS---------LDDAINHPAEDFTATPSPA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 250 gmDDRLFYIYTSGTTGLPKAAIVVHSRYYriaafghhsYSMRA--------ADVLYDC-LPLYH----SAGNIMGV---G 313
Cdd:PRK10946 182 --DEVAFFQLSGGSTGTPKLIPRTHNDYY---------YSVRRsveicgftPQTRYLCaLPAAHnypmSSPGALGVflaG 250
|
....
gi 1907189407 314 QCVI 317
Cdd:PRK10946 251 GTVV 254
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
70-309 |
4.88e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.58 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 70 SVLIRVRLELRRHRRagdTIPCIFQAVARRQPER--LALVDASSGiCW---TFAQLDTYSNAVANLFRQLGFAPGDVVAV 144
Cdd:PRK12582 35 SIVIKSRHPLGPYPR---SIPHLLAKWAAEAPDRpwLAQREPGHG-QWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 145 fLEGRP-EFVGLWLGLAKAGVVAA-------LLNVNLRRepLAFCLgTSAAKALIY---GGEMAAAVAEVSEQlGKSLLk 213
Cdd:PRK12582 111 -LSGNSiEHALMTLAAMQAGVPAApvspaysLMSHDHAK--LKHLF-DLVKPRVVFaqsGAPFARALAALDLL-DVTVV- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 214 FCSGDLGPESILPdtqlLDPMLAEAPTTPLAQAPGK-GMDDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAFGHHSYSMRA 292
Cdd:PRK12582 185 HVTGPGEGIASIA----FADLAATPPTAAVAAAIAAiTPDTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPRE 259
|
250 260
....*....|....*....|..
gi 1907189407 293 AD----VLYDCLPLYH-SAGNI 309
Cdd:PRK12582 260 PDppppVSLDWMPWNHtMGGNA 281
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
97-319 |
8.01e-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: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 97 ARRQPERLALVDASSGICW---TFAQLDTYSNAVANLFRQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA------ 167
Cdd:cd05921 5 ARQAPDRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApvspay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 168 -LLNVNLRRepLAFCLGTsAAKALIY---GGEMAAAVAEVsEQLGKSLLKFCSGDLGPESILPDTQLLDPMLAEAPttpl 243
Cdd:cd05921 85 sLMSQDLAK--LKHLFEL-LKPGLVFaqdAAPFARALAAI-FPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVD---- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189407 244 AQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAAD--VLYDCLPLYHSAGNIMGVGqCVIYG 319
Cdd:cd05921 157 AAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFN-LVLYN 233
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
115-319 |
8.37e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.88 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 115 W-TFAQ-LDTYSNAVANLFrQLGFAPGDVVAVFLEGRPEfvglWL----GLAKAGVVAALLNVNLRREPLAFCLGTSAAK 188
Cdd:PLN02387 106 WiTYGQvFERVCNFASGLV-ALGHNKEERVAIFADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 189 ALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESILPDTQLLDPMLA----------EAPTTPLAQAPgkgmDDRLFYI 258
Cdd:PLN02387 181 TVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSsfseveklgkENPVDPDLPSP----NDIAVIM 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 259 YTSGTTGLPKAAIVVHSRYY-RIAAFGHHSYSMRAADVLYDCLPLYH----SAGNIM-GVGQCVIYG 319
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVaTVAGVMTVVPKLGKNDVYLAYLPLAHilelAAESVMaAVGAAIGYG 323
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
491-610 |
1.22e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.03 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 491 VFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvavPGVEGKAG--MAAIA 568
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGerVKAKV 360
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907189407 569 DPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKI 610
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
501-620 |
2.42e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 44.31 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 501 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHSQLDPNSMY 580
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELL 492
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907189407 581 QELQKVLASYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 620
Cdd:PRK07008 493 AFYEGKVAKWWIPddvVFVDAIPH---TATGKLQKLKL-REQF 531
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
258-619 |
2.92e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 43.83 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 258 IYTSGTTGLPKAaiVVHSRyyRIAAFG----HHSYSMRAADVLYDCLPLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRF 333
Cdd:PRK07787 134 VYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 334 WDDCvKYNCTVvqYIGEICRYllRQPVRDVEQRH---RVRLAV-GNGLRPA-IWEEFTQRFGVPQIgEFYGATEC--NCS 406
Cdd:PRK07787 210 AQAL-SEGGTL--YFGVPTVW--SRIAADPEAARalrGARLLVsGSAALPVpVFDRLAALTGHRPV-ERYGMTETliTLS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 407 I-ANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSEGLCIPCQpGEPgllVGQINQQDPLrRFDGYVsdsatNK 485
Cdd:PRK07787 284 TrADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD-GET---VGELQVRGPT-LFDGYL-----NR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 486 KIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVlsrLLGQTDVAvyGVAVPGVE----G 560
Cdd:PRK07787 339 PDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETA---LLGHPGVR--EAAVVGVPdddlG 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 561 KAGMAAIAdPHSQLDPNSMYQELQKVLASYARPIFLRLLPQVDTTGTFKIQKTRLQREG 619
Cdd:PRK07787 414 QRIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
258-322 |
4.47e-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: 4.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189407 258 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAADVLYDC----LPLYHSAGNIMGVGQCVIYGLTV 322
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-304 |
9.56e-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: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 116 TFAQLDTYSNAVANLFRQLGF--APGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 193
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPE----WIISELACYAYSLVTV-----PLYDTLGPEAIEYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 194 GEMaaavaevseqlgkSLLkFCSGDLGPESIlpdTQLLDpMLAEAPTTPLAQAPgkgmdDRLFYI-YTSGTTGLPKAAIV 272
Cdd:cd05927 78 AEI-------------SIV-FCDAGVKVYSL---EEFEK-LGKKNKVPPPPPKP-----EDLATIcYTSGTTGNPKGVML 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907189407 273 VH----SRYYRIAAFGHHSYSMRAADVLYDCLPLYH 304
Cdd:cd05927 135 THgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
230-424 |
1.24e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.00 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 230 LLDPMLAEAPTTPlaqapgkgmDDRLFYIYTSGTTGLPKAaiVVHS---------RYYRIAAFGHHSYSMRAadvlydcL 300
Cdd:PRK08043 352 LLMPRLAQVKQQP---------EDAALILFTSGSEGHPKG--VVHShksllanveQIKTIADFTPNDRFMSA-------L 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 301 PLYHSAGNIMGVGQCVIYGLTVVLRKKFSASRFWDDCV-KYNCTVV----QYIGEICRYllRQPVrdveQRHRVRLAVGN 375
Cdd:PRK08043 414 PLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNYARF--ANPY----DFARLRYVVAG 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189407 376 GLRPA-----IWEEftqRFGVpQIGEFYGATECNCSIA---NMDGKVGSCGfnsRIL 424
Cdd:PRK08043 488 AEKLQestkqLWQD---KFGL-RILEGYGVTECAPVVSinvPMAAKPGTVG---RIL 537
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
127-309 |
1.35e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.91 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 127 VANLFRQLGFAPGDVVAVfLEGRPEFV-----GLWLglakAGVVAALLNVNLRREPLAF-------CLGTSAAKALIYGG 194
Cdd:PRK07768 42 IAGGLAAAGVGPGDAVAV-LAGAPVEIaptaqGLWM----RGASLTMLHQPTPRTDLAVwaedtlrVIGMIGAKAVVVGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189407 195 EMAAAvAEVSEQLGKSLLkfcsgdlgpesilpdtqLLDPMLAEAPTTPlaqaPGKGMDDRLFYIYTSGTTGLPKAAIVVH 274
Cdd:PRK07768 117 PFLAA-APVLEEKGIRVL-----------------TVADLLAADPIDP----VETGEDDLALMQLTSGSTGSPKAVQITH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907189407 275 SR-YYRIAAfghhsysMRAA-------DVLYDCLPLYHSAGNI 309
Cdd:PRK07768 175 GNlYANAEA-------MFVAaefdvetDVMVSWLPLFHDMGMV 210
|
|
| |
