|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
107-614 |
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: 855.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 186
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtQLLDPMLAEAPTTPLAQaPGKGMDDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05939 82 ----------------------------------NLLDPLLTQSSTEPPSQ-DDVNFRDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 346
Cdd:cd05939 127 SRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 347 LLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 426
Cdd:cd05939 207 LLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 427 VNEDTMEPLRDSQGLCIPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 506
Cdd:cd05939 287 VDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 507 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPI 586
Cdd:cd05939 367 FKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQ 446
|
490 500
....*....|....*....|....*...
gi 564388681 587 FLRLLPQVDTTGTFKIQKTRLQREGFDP 614
Cdd:cd05939 447 FIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
45-649 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 695.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 45 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGDTIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFL 124
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSI--SYAELNARANRYAHWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 125 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 204
Cdd:PRK08279 81 ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 205 KFCSGDLGPESVLPDTQLLDpMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHhSYSMR 283
Cdd:PRK08279 161 LWVAGGDTLDDPEGYEDLAA-AAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGG-LLRLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 284 ANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRL 363
Cdd:PRK08279 239 PDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 364 AVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHvyPIRLVKVNEDTMEPLRDSQGLCI 443
Cdd:PRK08279 319 MIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRCI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 444 PCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVS 523
Cdd:PRK08279 397 KVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 524 TTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI-ADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKI 602
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKY 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 564388681 603 QKTRLQREGFDPRQTSDRLFFLDLKQGRYLPLDERVHARICAGDFSL 649
Cdd:PRK08279 554 RKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
107-614 |
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: 647.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYgg 186
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05940 82 ----------------------------------------------------------DAALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRY 346
Cdd:cd05940 104 RRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 347 LLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVK 426
Cdd:cd05940 184 LLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 427 VNEDTMEPLRDSQGLCIPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMY 506
Cdd:cd05940 264 YDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 507 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQ-LDPNSMYQELQKVLASYAQP 585
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEeFDLSALAAHLEKNLPGYARP 420
|
490 500
....*....|....*....|....*....
gi 564388681 586 IFLRLLPQVDTTGTFKIQKTRLQREGFDP 614
Cdd:cd05940 421 LFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
108-636 |
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: 595.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFL-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 186
Cdd:cd05938 7 TYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 EMAAAVAEVSEQLGKSLLKFcsGDLGPESVLPDTQLLDPMLAEAPTTPLAQ---APGKGMDDRLfYIYTSGTTGLPKAAI 263
Cdd:cd05938 87 ELQEAVEEVLPALRADGVSV--WYLSHTSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTGLPKAAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 264 VVHSRYYRIAAFgHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEI 343
Cdd:cd05938 164 ISHLRVLQCSGF-LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 344 CRYLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIR 423
Cdd:cd05938 243 LRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 424 LVKVNEDTMEPLRDSQGLCIPCQPGEPGLLVGQINQQDPlrrFDGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDEL 502
Cdd:cd05938 323 LIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAGDKEqTEKKLLRDVFKKGDVYFNTGDLLVQDQQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 503 GYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAI--ADPHnQLDPNSMYQELQKVLA 580
Cdd:cd05938 400 NFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPGH-EFDGKKLYQHVREYLP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 581 SYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYLPLDE 636
Cdd:cd05938 479 AYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTP 534
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
107-614 |
1.83e-138 |
|
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: 412.60 E-value: 1.83e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFL-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYg 185
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 186 gemaaavaevseqlgksllkfcsgdlgpesvlpdtqllDPmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVV 265
Cdd:cd05937 85 --------------------------------------DP------------------DDPAILIYTSGTTGLPKAAAIS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 266 HSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 345
Cdd:cd05937 109 WRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 346 YLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANM---DGKVGSCGFNSRILTHVY-- 420
Cdd:cd05937 189 YLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAGAIGHHGLIRRWKFen 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 421 PIRLVKVNEDTMEPLRD-SQGLCIPCQPGEPGLLVGQINqQDPLRRFDGYVSDS-ATNKKIAHSVFRKGDSAYLSGDVLV 498
Cdd:cd05937 269 QVVLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVP-FKNREAFQGYLHNEdATESKLVRDVFRKGDIYFRTGDLLR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 499 MDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDP-----NSMYQ 573
Cdd:cd05937 348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPteftkSLLAS 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564388681 574 ELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 614
Cdd:cd05937 428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
81-610 |
2.67e-87 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 279.77 E-value: 2.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 160
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 161 LNVNLRREPLAFCLGTSAAKALIYggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapg 240
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 241 kgmddrLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKF 320
Cdd:COG0318 103 ------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 321 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRqIGEFYGATECNCS 398
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 399 IA-----NMDGKVGSCGfnsRILTHVyPIRLvkVNEDTMEplrdsqglcipCQPGEPGLLVGQINQQdplrrFDGYVSD- 472
Cdd:COG0318 256 VTvnpedPGERRPGSVG---RPLPGV-EVRI--VDEDGRE-----------LPPGEVGEIVVRGPNV-----MKGYWNDp 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 473 SATNKKIAHSVFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEG 552
Cdd:COG0318 314 EATAEAFRDGWLR-------TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE-KWG 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 553 KAGMAAI-ADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:COG0318 386 ERVVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
106-608 |
1.52e-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: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 106 CWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtsaakaliyg 185
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGD----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 186 gEMAAAVAEVseqlgksllkfcsgdlGPESVLPDTQLLdpmlaeapttplaqapgkgmddrlfyIYTSGTTGLPKAAIVV 265
Cdd:cd05934 66 -ELAYIIDHS----------------GAQLVVVDPASI--------------------------LYTSGTTGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 266 HSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICR 345
Cdd:cd05934 103 HANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 346 YLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRqIGEFYGATECNCSIAN---MDGKVGSCGfnsrilthvYPI 422
Cdd:cd05934 183 YLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGSIG---------RPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 423 RLVKVNedtmepLRDSQGLciPCQPGEPGLLVgqINQQDPLRRFDGYVSD-SATNKKIAHSVFRKGDSAYlsgdvlvMDE 501
Cdd:cd05934 253 PGYEVR------IVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNMpEATAEAMRNGWFHTGDLGY-------RDA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 502 LGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLAS 581
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*..
gi 564388681 582 YAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
77-620 |
6.86e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 257.76 E-value: 6.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 77 AGDTIPRIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV 156
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 157 VAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVseqlgksllkfcsgDLGPESvLPDTQLLD------------ 224
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--------------DPGDLP-LPAVWLLDapasvsvpagws 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 225 --PMLA-EAPTTPLAQAPGkgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNI 301
Cdd:PRK06155 162 taPLPPlDAPAPAAAVQPG----DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 302 MGVgQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRF 381
Cdd:PRK06155 238 AFF-QALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 382 GVRQIgEFYGATECNCSIANM--DGKVGSC-----GFNSRIlthvypirlvkVNEDTMEplrdsqglcIPcqPGEPGLLV 454
Cdd:PRK06155 317 GVDLL-DGYGSTETNFVIAVThgSQRPGSMgrlapGFEARV-----------VDEHDQE---------LP--DGEPGELL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 455 GQINQqdPLRRFDGYVSDSATnkkiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 534
Cdd:PRK06155 374 LRADE--PFAFATGYFGMPEK------TVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 535 LGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 614
Cdd:PRK06155 446 PAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
....*.
gi 564388681 615 rQTSDR 620
Cdd:PRK06155 526 -DTWDR 530
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
85-518 |
1.84e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 218.34 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 85 FQAVAQRQPERLALVDASsGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 164
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 165 LRREPLAFCLGTSAAKALIYGGE-MAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQApgkgm 243
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKK 319
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 FSA---SRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVR--LAVGNGLRPAIWEEFTQRFGvRQIGEFYGATE 394
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFG-GALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIANMD------GKVGSCGfnsRILTHVypiRLVKVNEDTMEPLRdsqglcipcqPGEPG-LLVGQINQqdplrrFD 467
Cdd:pfam00501 314 TTGVVTTPLpldedlRSLGSVG---RPLPGT---EVKIVDDETGEPVP----------PGEPGeLCVRGPGV------MK 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564388681 468 GYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 518
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 ... |
245-603 |
4.45e-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: 201.74 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGnIMGVGQCIIYGLTVVLRKKFSASR 324
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 325 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGVRqIGEFYGATECNCSIA-- 400
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 401 ---NMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSQGlcIPCQPGEPGLLVGQINQqdplrRFDGYVSDSATNK 477
Cdd:cd04433 159 ppdDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVRGPS-----VMKGYWNNPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 478 kiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA 557
Cdd:cd04433 217 ------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564388681 558 AI-ADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQ 603
Cdd:cd04433 290 VVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
107-645 |
2.20e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 202.56 E-value: 2.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDV-VAVFLEGRPEFVgLWLGLAK-AGVVAALLNvNLRReplafclgtsaakaliy 184
Cdd:PRK13388 27 WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAAlGGYVLVGLN-TTRR----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 185 GGEMAAAVAEVSEQL------GKSLLKfcsgDLGpesvLPDTQLLD---PMLAE--APTTPLAQAPGKGMDDRLFYIYTS 253
Cdd:PRK13388 88 GAALAADIRRADCQLlvtdaeHRPLLD----GLD----LPGVRVLDvdtPAYAElvAAAGALTPHREVDAMDPFMLIFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 254 GTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYN 333
Cdd:PRK13388 160 GTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 334 CTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVrQIGEFYGATECNCSIANMDGK-VGSCGfn 412
Cdd:PRK13388 240 ATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGYGSSEGAVIVVREPGTpPGSIG-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 413 srilthvypiR----LVKVNEDTMEPlrdsqglCIPCQPGEPGLL------VGQINQQDPLRRFDGYVSD-SATNKKIAH 481
Cdd:PRK13388 317 ----------RgapgVAIYNPETLTE-------CAVARFDAHGALlnadeaIGELVNTAGAGFFEGYYNNpEATAERMRH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 482 SVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMAAI-- 559
Cdd:PRK13388 380 GMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV-GDQVMAALvl 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 560 ADPHnQLDPNSMYQEL--QKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFdpRQTSDRLFFLDLKQGRYLPLDER 637
Cdd:PRK13388 452 RDGA-TFDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW--ATGDPVTLWVRRGGPAYRLMSEP 528
|
....*...
gi 564388681 638 VHARICAG 645
Cdd:PRK13388 529 AKAALAAE 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
134-613 |
2.95e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 196.83 E-value: 2.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 134 VAVFLEGRPEFvGLWLGLAK-AGVVAALLNVNLRREPLA---------FCLGTSAAKALIYGGEMAAAVAEVSEQlgksl 203
Cdd:PRK07867 57 VGVLLDNTPEF-SLLLGAAAlSGIVPVGLNPTRRGAALArdiahadcqLVLTESAHAELLDGLDPGVRVINVDSP----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 204 lkfcsgdlgpesvlPDTQLLDPmLAEAPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRyyrIAAFGH---HSY 280
Cdd:PRK07867 131 --------------AWADELAA-HRDAEPPFRVADP----DDLFMLIFTSGTSGDPKAVRCTHRK---VASAGVmlaQRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 281 SMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHH 360
Cdd:PRK07867 189 GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 361 VRLAVGNGLRPAIWEEFTQRFGVRQIgEFYGATECNCSIANM-DGKVGSCGfnsrilthVYPIRLVKVNEDTMEPlrdsq 439
Cdd:PRK07867 269 LRIVYGNEGAPGDIARFARRFGCVVV-DGFGSTEGGVAITRTpDTPPGALG--------PLPPGVAIVDPDTGTE----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 440 glCIPCQPGEPGLL-----VGQ-INQQDPlRRFDGYVSDS-ATNKKIAHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSG 512
Cdd:PRK07867 335 --CPPAEDADGRLLnadeaIGElVNTAGP-GGFEGYYNDPeADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 513 DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMAAIA-DPHNQLDPNSMYQEL--QKVLASYAQPIFLR 589
Cdd:PRK07867 405 DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV-GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVR 483
|
490 500
....*....|....*....|....
gi 564388681 590 LLPQVDTTGTFKIQKTRLQREGFD 613
Cdd:PRK07867 484 VCAELPRTATFKVLKRQLSAEGVD 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
78-608 |
3.35e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 187.97 E-value: 3.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 78 GDTIPRIFQAVAQRQPERLALV-DASSGIC--WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfESSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGpESVLPDTQLLDPMLAEAPTTp 234
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVA-LPADDGVSSFTQLKAQQPAT- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 235 LAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHHSY---SMRANDVLYDCLPLYHSAGNIMGVGQCIIYG 311
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVR-----LAVGNGLRpaiwEEFTQRFGVRQI 386
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEERFGVRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEfYGATEcncSIANMDG----------KVGSCGFNsrilthvYPIRlvkvnedtmepLRDSQGLCIPcqPGEpgllVGQ 456
Cdd:PRK08008 317 TS-YGMTE---TIVGIIGdrpgdkrrwpSIGRPGFC-------YEAE-----------IRDDHNRPLP--AGE----IGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 457 INQQD-PLRR-FDGYVSD-SATNKKI-AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLS 532
Cdd:PRK08008 369 ICIKGvPGKTiFKEYYLDpKATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 533 RLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:PRK08008 442 THPKIQDIVVVGIKDS-IRDEAIKAfVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
89-604 |
6.51e-49 |
|
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: 177.03 E-value: 6.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:cd17631 5 ARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmDDRLF 248
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDD 328
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 329 CVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNG--LRPAIWEEFtQRFGVRqIGEFYGATECNCSIANMD--- 403
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGVK-FVQGYGMTETSPGVTFLSped 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 404 --GKVGSCGfnsRILTHVyPIRLVKVNEDtmeplrdsqglciPCQPGEpgllVGQINQQDPLrRFDGYVSDSATNKKiah 481
Cdd:cd17631 261 hrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAGYWNRPEATAA--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 482 sVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA 560
Cdd:cd17631 316 -AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAVVV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564388681 561 -DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQK 604
Cdd:cd17631 391 pRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
97-559 |
1.11e-48 |
|
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: 177.40 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 97 ALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 176
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 177 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLgPESVLPDTQLLDPmLAEAPTTPLAQAPGKGMDDRLFYIYTSGTT 256
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDK-PDGVLSIEDLLSP-TLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 257 GLPKAAIVVHSRYyrIA----AFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGqCIIYGLTVVLRKKFSASRFWDDCVKY 332
Cdd:cd05911 159 GLPKGVCLSHRNL--IAnlsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 333 NCTVVQYIGEICRYLLRQPVRDVERRHHVR-LAVGNG-LRPAIWEEFTQRFGVRQIGEFYGATECNCSIA---NMDGKVG 407
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 408 SCGfnsrILTHVYPIRLvkVNEDTmeplRDSQGlcipcqPGEPG-LLV--GQInqqdplrrFDGYVSD-SATNKKIAHSV 483
Cdd:cd05911 316 SVG----RLLPNVEAKI--VDDDG----KDSLG------PNEPGeICVrgPQV--------MKGYYNNpEATKETFDEDG 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 484 FRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAI 559
Cdd:cd05911 372 WLH------TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYV 440
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
80-610 |
6.15e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.45 E-value: 6.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDASSGicWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA 159
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksLLKFC--SGDLGPESVLPDTQLLDPMLAEAPTTPLaq 237
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLP--TVRTVivEGDGPAAPLAPEVGEYEELLAAASDTFD-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 238 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGniMGVGQCIIY-GLTVVL 316
Cdd:PRK06187 161 FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPYLALMaGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 317 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQIgEFYGATE 394
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGIDLV-QGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CncsianmdGKVGSCGFNSRILTHVYPIRL----------VKVNEDTMEPLrdsqglciPCQPGEPGLLV--GQINQQdp 462
Cdd:PRK06187 318 T--------SPVVSVLPPEDQLPGQWTKRRsagrplpgveARIVDDDGDEL--------PPDGGEVGEIIvrGPWLMQ-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 463 lrrfdGYVSD-SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 541
Cdd:PRK06187 380 -----GYWNRpEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 542 VYGV----------AVpgVEGKAGMaaiadphnQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLqRE 610
Cdd:PRK06187 448 VIGVpdekwgerpvAV--VVLKPGA--------TLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
89-548 |
9.21e-45 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 167.98 E-value: 9.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDAS---SGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 165
Cdd:COG0365 19 AEGRGDKVALIWEGedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 166 RREPLAFCLGTSAAKALI------YGG---EMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTT-PL 235
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglRGGkviDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEfEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 236 AQAPGkgmDDRLFYIYTSGTTGLPKAaiVVHS-RYYRIAA--FGHHSYSMRANDVLY---DClplyhsaGNIMGVGQCII 309
Cdd:COG0365 179 EPTDA---DDPLFILYTSGTTGKPKG--VVHThGGYLVHAatTAKYVLDLKPGDVFWctaDI-------GWATGHSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 310 YGL----TVVL---RKKF-SASRFWDDCVKYNCTVvqyigeIC------RYLLRQPVRDVERRH--HVRLAVGNG--LRP 371
Cdd:COG0365 247 GPLlngaTVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDlsSLRLLGSAGepLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 372 AIWEEFTQRFGVrQIGEFYGATECNCSIAN----MDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSQGlcIPCQP 447
Cdd:COG0365 321 EVWEWWYEAVGV-PIVDGWGQTETGGIFISnlpgLPVKPGSMGK---------PVPGYDVA------VVDEDG--NPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 448 GEPGLLVgqinqqdpLRR-----FDGYVSDSATNKKiahSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 522
Cdd:COG0365 383 GEEGELV--------IKGpwpgmFRGYWNDPERYRE---TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRI 451
|
490 500
....*....|....*....|....*.
gi 564388681 523 STTEVEAVLSRLLGQTDVAVygVAVP 548
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAV--VGVP 475
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
80-608 |
5.59e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 165.08 E-value: 5.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 159
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLaeAPTTPLAQ 237
Cdd:PRK07656 82 VVPLNTRYTAdeAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFL--AAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 238 APGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLR 317
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGVRQIGEFYGATEC 395
Cdd:PRK07656 240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 nCSIANM-----DGKV--GSCGfnsRILTHVyPIRLVkvnedtmeplrDSQGLCIPcqPGEPGLLVgqinqqdpLRRFD- 467
Cdd:PRK07656 320 -SGVTTFnrlddDRKTvaGTIG---TAIAGV-ENKIV-----------NELGEEVP--VGEVGELL--------VRGPNv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 468 --GYVSDS-ATnkkiAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 544
Cdd:PRK07656 374 mkGYYDDPeAT----AAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388681 545 VAVPGVeGKAGMA-AIADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPqVDTTGtfKIQKTRLQ 608
Cdd:PRK07656 448 VPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPrsiEFLDELP-KNATG--KVLKRALR 511
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
70-545 |
7.35e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 162.02 E-value: 7.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 70 ELRRHRRagDTIPRIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWL 149
Cdd:PRK08316 4 RSTRARR--QTIGDILRRSARRYPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 150 GLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAE 229
Cdd:PRK08316 80 ACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 230 APTTPLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYR-IAAFGhhsysMRANDVLYDCLPLYHSAGniMGV 304
Cdd:PRK08316 160 SVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHraliAEYVScIVAGD-----MSADDIPLHALPLYHCAQ--LDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 305 --GQCIIYGLTVVLRKKFSASRFWDDCVKYNC-------TVvqYIGeicryLLRQPvrDVERRhhvRLAvgnGLRPA--- 372
Cdd:PRK08316 230 flGPYLYVGATNVILDAPDPELILRTIEAERItsffappTV--WIS-----LLRHP--DFDTR---DLS---SLRKGyyg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 373 -------IWEEFTQRFGVRQIGEFYGATEcncsIA---------NMDGKVGSCG---FN--SRIlthvypirlvkVNEDt 431
Cdd:PRK08316 295 asimpveVLKELRERLPGLRFYNCYGQTE----IAplatvlgpeEHLRRPGSAGrpvLNveTRV-----------VDDD- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 432 MEPLrdsqglcipcQPGEPGLLVGQINQQdplrrFDGYVSDSAtnkKIAHSvFRKGdsAYLSGDVLVMDELGYMYFRDRS 511
Cdd:PRK08316 359 GNDV----------APGEVGEIVHRSPQL-----MLGYWDDPE---KTAEA-FRGG--WFHSGDLGVMDEEGYITVVDRK 417
|
490 500 510
....*....|....*....|....*....|....
gi 564388681 512 GDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK08316 418 KDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
93-607 |
1.37e-41 |
|
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: 157.86 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALI--YGGEMAAAVAEVSEQLGKSLLKFCSGDL---GPESVLPdtqLLDPMLAEAPTTPLAQAPgkgmDDRL 247
Cdd:cd05926 81 YLADLGSKLVLtpKGELGPASRAASKLGLAILELALDVGVLiraPSAESLS---NLLADKKNAKSEGVPLPD----DLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 248 FyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASR 324
Cdd:cd05926 154 I-LHTSGTTGRPKGVPLTHR---NLAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 325 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHH----VRLAvGNGLRPAIWEEFTQRFGVRQIgEFYGATE------ 394
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPklrfIRSC-SASLPPAVLEALEATFGAPVL-EAYGMTEaahqmt 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIANMDgKVGSCGFNSrilthvyPIRLVKVNEDtmeplrdsqGLciPCQPGEpgllVGQINQQDPlRRFDGYVSDSA 474
Cdd:cd05926 308 SNPLPPGPR-KPGSVGKPV-------GVEVRILDED---------GE--ILPPGV----VGEICLRGP-NVTRGYLNNPE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 475 TNKKIAHSV--FRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEG 552
Cdd:cd05926 364 ANAEAAFKDgwFRTGDLGYL-------DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KYG 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 553 KAGMAAI---ADPHnqLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKIQKTRL 607
Cdd:cd05926 436 EEVAAAVvlrEGAS--VTEEELRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
84-604 |
2.82e-39 |
|
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: 151.88 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRQPERLALV---DASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 160
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 161 LNVNLRREPLAFCLGTSAAKALIYGGE--MAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMlAEAPTTPLAQA 238
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNA-SPDFERPTANS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 239 PGKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYriaAFGHHSYSMRANDVLYDCLplyHSAGNIMGVGQCI---IYG---- 311
Cdd:cd05970 181 YPCGEDILLVY-FSSGTTGMPK--MVEHDFTY---PLGHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGqwia 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 ---LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVR--DVERRHHVRLAvGNGLRPAIWEEFTQRFGVrQI 386
Cdd:cd05970 252 gaaVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSryDLSSLRYCTTA-GEALNPEVFNTFKEKTGI-KL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEFYGATECNCSIAN---MDGKVGSCGFNsrilTHVYPIRLVkvnedtmeplrDSQGLciPCQPGEPGLLVGQINQQDPL 463
Cdd:cd05970 330 MEGFGQTETTLTIATfpwMEPKPGSMGKP----APGYEIDLI-----------DREGR--SCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 464 RRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVY 543
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388681 544 GVAVPgVEGKAGMAAIADPHNQLDPNSMYQELQ----KVLASYAQPIFLRLLPQVDTTGTFKIQK 604
Cdd:cd05970 467 GVPDP-IRGQVVKATIVLAKGYEPSEELKKELQdhvkKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
81-545 |
3.86e-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: 150.41 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAVAQRQPERLALVDasSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 160
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 161 LNVNLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLKfcsGDLGPESVLPDTQLLdpmlaeapttplaqapg 240
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALI--------VAVSFTDLLAAGAP---LGERVALTPEDVAVL----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 241 kgmddrlfyIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSY--SMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRK 318
Cdd:cd05936 131 ---------QYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 319 KFSASRFWDDCVKYNCTVV-----QYIGeicryLLRQPVRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGVRqIGEFYG 391
Cdd:cd05936 202 RFRPIGVLKEIRKHRVTIFpgvptMYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 392 ATECNCSIA-N-MDG--KVGSCGfnsrilthvYPIRLVKVNedtmepLRDSQGLCIPcqPGEPGLLVgqinqqdpLR--- 464
Cdd:cd05936 276 LTETSPVVAvNpLDGprKPGSIG---------IPLPGTEVK------IVDDDGEELP--PGEVGELW--------VRgpq 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 465 RFDGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 544
Cdd:cd05936 331 VMKGYWNRPEETAE----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVG 404
|
.
gi 564388681 545 V 545
Cdd:cd05936 405 V 405
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
107-607 |
5.63e-38 |
|
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: 146.33 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 186
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 EmaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmdDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05972 81 E---------------------------------------------------------DPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 SryyriAAFGHHSYS-----MRANDVLY---DCLPLYHSAGNIMGVgqcIIYGLTVVL--RKKFSASRFWDDCVKYNCTV 336
Cdd:cd05972 104 S-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 337 VQYIGEICRyLLRQPVRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGVrQIGEFYGATECNCSIAN---MDGKVGSCGF 411
Cdd:cd05972 176 FCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGepLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNfpdMPVKPGSMGR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 412 NsrilTHVYPIRLVkvnedtmeplrDSQGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSATNKKiahsVFRKGdsAY 491
Cdd:cd05972 254 P----TPGYDVAII-----------DDDGR--ELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEA----SIRGD--YY 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 492 LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHNQLDPNSM 571
Cdd:cd05972 308 LTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAFVVLTSGYEPSEEL 386
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564388681 572 YQELQ----KVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05972 387 AEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
45-596 |
3.81e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 134.28 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 45 RFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGdtipRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFL 124
Cdd:PRK07788 19 HYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFA----GLVAHAARRAPDRAALIDERGTL--TYAELDEQSNALARGLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 125 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLL 204
Cdd:PRK07788 93 ALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 205 KFCSGDLGPESVlPDTQLLDPMLAEAPTTPLAQAPGKGMddrlFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHsYSMR 283
Cdd:PRK07788 173 WGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGAPRPEpSPLAPLAGLLSR-VPFR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 284 ANDVLYDCLPLYHSagniMGVGQCII---YGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHH 360
Cdd:PRK07788 247 AGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 361 VRLAV----GNGLRPAIWEEFTQRFGVRqIGEFYGATECN-CSIANMD------GKVGScgfnsrilthvyPIRLVKVNe 429
Cdd:PRK07788 323 SSLKIifvsGSALSPELATRALEAFGPV-LYNLYGSTEVAfATIATPEdlaeapGTVGR------------PPKGVTVK- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 430 dtmepLRDSQGLCIPcqPGEPG-LLVGQINQqdplrrFDGYVSDSatNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFR 508
Cdd:PRK07788 389 -----ILDENGNEVP--RGVVGrIFVGNGFP------FEGYTDGR--DKQIIDGLLSSGDVGYF-------DEDGLLFVD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 509 DRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--IADPHNQLDPNSMYQELQKVLASYAQP- 585
Cdd:PRK07788 447 GRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDEDAIKDYVRDNLARYKVPr 524
|
570
....*....|...
gi 564388681 586 --IFLRLLPQVDT 596
Cdd:PRK07788 525 dvVFLDELPRNPT 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
108-608 |
5.09e-32 |
|
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: 129.12 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 187
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MAAavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmddrlFYIYTSGTTGLPKAAIVVHS 267
Cdd:cd05919 92 DIA---------------------------------------------------------YLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 268 RYYRIA-AFGHHSYSMRANDVLYDCLPLYHSAG---NIMGVGQCiiyGLTVVLRKKF-SASRFWDDCVKYNCTVVQYIGE 342
Cdd:cd05919 115 DPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGlgnSLWFPLAV---GASAVLNPGWpTAERVLATLARFRPTVLYGVPT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 343 ICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVrQIGEFYGATEC-NCSIANMDGKV--GSCGfnsRILT 417
Cdd:cd05919 192 FYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGG-PILDGIGATEVgHIFLSNRPGAWrlGSTG---RPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 418 HvYPIRLVkvnedtmeplrDSQGLCIPcqPGEPGLLVGQINQQDPlrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVL 497
Cdd:cd05919 268 G-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRA----TFNGG--WYRTGDKF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 498 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAAIADPHNQLDPN-----SMY 572
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPAAPQeslarDIH 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 564388681 573 QELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
89-610 |
9.22e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 129.31 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGicWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK03640 12 AFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKfcsgdlgpesvlpdtqlldpmLAEAPTTPLAQAPgkgmDDRLF 248
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMN---------------------GPKEEAEIQEEFD----LDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YI-YTSGTTGLPKAAivvhsryyrIAAFGHHSYS---------MRANDVLYDCLPLYHSAG-NIMGVGqcIIYGLTVVLR 317
Cdd:PRK03640 145 TImYTSGTTGKPKGV---------IQTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGlSILMRS--VIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCT---VVQyigeicrYLLRQPVRDVERRH---HVR-LAVGNGLRP-AIWEEFTQR-FGVRQIge 388
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTiisVVS-------TMLQRLLERLGEGTypsSFRcMLLGGGPAPkPLLEQCKEKgIPVYQS-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 389 fYGATECNCSIANMD-----GKVGSCG---FNSRIlthvypirlvKVNEDTMEplrdsqglCIPCQPGE-----PGLLVG 455
Cdd:PRK03640 285 -YGMTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvkgPNVTKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 456 QINQQDplrrfdgyvsdsATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLL 535
Cdd:PRK03640 346 YLNRED------------ATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 536 GQTDVAVYGVAvpgvEGKAGMAAIAD--PHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKIQKTRLQRE 610
Cdd:PRK03640 407 GVAEAGVVGVP----DDKWGQVPVAFvvKSGEVTEEELRHFCEEKLAKYKVPkrfYFVEELPR---NASGKLLRHELKQL 479
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
84-607 |
7.88e-31 |
|
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: 126.71 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 163
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSL--TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 164 NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKF-CSGDLGPESVLPD-TQLLD---PMLAEAPTTPlaqa 238
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLiVSGGAGPEAGALLlAELVAaeaEQLKPAATHA---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 239 pgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA-AFGHHSYSMRANDVLYDCLPLYHS--AGNI----MGVGqciiyG 311
Cdd:cd05959 163 -----DDPAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAygLGNSltfpLSVG-----A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVrQIGEF 389
Cdd:cd05959 233 TTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 390 YGATEC-NCSIANMDGKV--GSCGfnsrILTHVYPIRLVkvnEDTMEPLRDsqglcipcqpGEPGLL--------VGQIN 458
Cdd:cd05959 312 IGSTEMlHIFLSNRPGRVryGTTG----KPVPGYEVELR---DEDGGDVAD----------GEPGELyvrgpssaTMYWN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 459 QQDPLRR-FDGYvsdsatnkkiahsvfrkgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQ 537
Cdd:cd05959 375 NRDKTRDtFQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-----V 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 538 TDVAVYGVAVPGVEGKAGM----AAIADPHNQLDPNSMYQELQK----VLASYAQP---IFLRLLPQvdtTGTFKIQKTR 606
Cdd:cd05959 430 QHPAVLEAAVVGVEDEDGLtkpkAFVVLRPGYEDSEALEEELKEfvkdRLAPYKYPrwiVFVDELPK---TATGKIQRFK 506
|
.
gi 564388681 607 L 607
Cdd:cd05959 507 L 507
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
89-546 |
3.66e-30 |
|
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: 124.54 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:cd05923 11 ASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFClgtsaakalIYGGEMAAAV----AEVSEQLGKSLLKFCSgdlgpESVLPDTQLLDpmlaeaPTTPLAQAPGKGMD 244
Cdd:cd05923 91 ELAEL---------IERGEMTAAViavdAQVMDAIFQSGVRVLA-----LSDLVGLGEPE------SAGPLIEDPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHS-YSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSA 322
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 323 SRfwddcvkynctVVQYIGE---ICRYL-----------LRQPVRDVERRHHVRLAvGNGLRPAIWEEFTQRFGVRQIgE 388
Cdd:cd05923 231 AD-----------ALKLIEQervTSLFAtpthldalaaaAEFAGLKLSSLRHVTFA-GATMPDAVLERVNQHLPGEKV-N 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 389 FYGATECNCSIANMDGKVGSC---GFNSRilthvypIRLVKVNEDTMEPLrdsqglcipcQPGEPGLLVGQINQQDplrR 465
Cdd:cd05923 298 IYGTTEAMNSLYMRDARTGTEmrpGFFSE-------VRIVRIGGSPDEAL----------ANGEEGELIVAAAADA---A 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 466 FDGYVSD-SATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 544
Cdd:cd05923 358 FTGYLNQpEATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
..
gi 564388681 545 VA 546
Cdd:cd05923 431 VA 432
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
108-642 |
6.65e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 126.37 E-value: 6.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLnvnlrrEPlafclgtsaakaliyGGE 187
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM------PP---------------DTD 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MAAAV--AEVSE------------QLGKSLLKFCSGD-----LGPESVLPDTQLLDPMLAEAPTTplaQAPGKGMDDRLF 248
Cdd:PRK07868 533 LAAAVrlGGVTEiitdptnleaarQLPGRVLVLGGGEsrdldLPDDADVIDMEKIDPDAVELPGW---YRPNPGLARDLA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVHSRYyRIAAFGHHSY-SMRANDVLYdCL-PLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFW 326
Cdd:PRK07868 610 FIAFSTAGGELVAKQITNYRW-ALSAFGTASAaALDRRDTVY-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFV 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 327 DDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDG-K 405
Cdd:PRK07868 688 QEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaK 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 406 VGSCGfnsRILTHVYPIRLVKVNEDTMEPLRDSQGLCIPCQPGEPGLLVGqinqqdplrRFDGYVSDSATNKKiahSVFR 485
Cdd:PRK07868 768 IGSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLA---------RARGPIDPTASVKR---GVFA 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 486 KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRlLGQTDVAV-YGVAVPGVEgkAGMAAIA-DPH 563
Cdd:PRK07868 833 PADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGR-IGGVDLAVtYGVEVGGRQ--LAVAAVTlRPG 909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 564 NQLDPnsmyQELQKVLASYA---QPIFLRLLPQVDTTGTFKIQKTRLQREGFdPRqTSDRLFFLDLKQGRYLPLDERVHA 640
Cdd:PRK07868 910 AAITA----ADLTEALASLPvglGPDIVHVVPEIPLSATYRPTVSALRAAGI-PK-PGRQAWYFDPETNRYRRLTPAVRA 983
|
..
gi 564388681 641 RI 642
Cdd:PRK07868 984 EL 985
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
89-608 |
3.17e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.84 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRre 168
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 plafclgtsaakaliyGGEMAAAVAEVSEQLgksLLkfcsGDLGPESVLPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLF 248
Cdd:PRK09088 83 ----------------ASELDALLQDAEPRL---LL----GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVHSRYYRIAA-FGHHSYSMRANDVLYDClPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWD 327
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQTAHnFGVLGRVDAHSSFLCDA-PMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 328 DCVKYNCTVVQYIG--EICRYLLRQPVRDVER-RHHVRLAVGNGLRPAI----WEE----FTQRFGVRQIGEFYGATeCN 396
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDdgipMVDGFGMSEAGTVFGMS-VD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 397 CSIanMDGKVGSCGfnsrILTHVYPIRLVKVNEdtmeplRDsqglcipCQPGEPG--LLVGQinqqdplRRFDGYVSDSA 474
Cdd:PRK09088 298 CDV--IRAKAGAAG----IPTPTVQTRVVDDQG------ND-------CPAGVPGelLLRGP-------NLSPGYWRRPQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 475 TNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGvEGKA 554
Cdd:PRK09088 352 ATARA-----FTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ-WGEV 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 564388681 555 GMAAIA-DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:PRK09088 426 GYLAIVpADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
89-558 |
4.09e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 121.72 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFcsgDLGPESVLPDTQLLDPMLAEAPTTPLAQAP-GKGMddrl 247
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIADESlGTDM---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 248 fyIYTSGTTGLPKAAivvhsryYR------------IAAFGHHSYSMRANDVLYDCLPLYHSAgNIMGVGQCIIYGLTVV 315
Cdd:PRK13391 160 --LYSSGTTGRPKGI-------KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSA-PQRAVMLVIRLGGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 316 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRD------VERRHH--------VRLAVGNGLRPAIWeeftq 379
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPeeVRDkydlssLEVAIHaaapcppqVKEQMIDWWGPIIH----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 380 rfgvrqigEFYGATECN----CSIANMDGKVGSCGfnsRILTHVYPIRlvkvnEDTMEplrdsqglciPCQPGEPgllvG 455
Cdd:PRK13391 305 --------EYYAATEGLgftaCDSEEWLAHPGTVG---RAMFGDLHIL-----DDDGA----------ELPPGEP----G 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 456 QINQQDPlRRFDgYVSDSAtnkKIAHSvfRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 534
Cdd:PRK13391 355 TIWFEGG-RPFE-YLNDPA---KTAEA--RHPDGTWsTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITH 427
|
490 500 510
....*....|....*....|....*....|....*...
gi 564388681 535 LGQTDVAVYGV--------------AVPGVEGKAGMAA 558
Cdd:PRK13391 428 PKVADAAVFGVpnedlgeevkavvqPVDGVDPGPALAA 465
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
93-612 |
1.67e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 119.60 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALvDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:PRK07514 16 RDAPFI-ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPESvlpdtqLLDpmLAEAPTTPLAQAPgKGMDDRLFYIYT 252
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKIAAAAGAPHV-ETLDADGTGS------LLE--AAAAAPDDFETVP-RGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 253 SGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSAsrfwDDCVKY 332
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDP----DAVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 333 --NCTVVqyIGEICRY--LLRQPVRDVERRHHVRLAVgNGLRPAIWE---EFTQRFGVRqIGEFYGATECNCSIAN-MDG 404
Cdd:PRK07514 241 mpRATVM--MGVPTFYtrLLQEPRLTREAAAHMRLFI-SGSAPLLAEthrEFQERTGHA-ILERYGMTETNMNTSNpYDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 405 K--VGSCGFnsrilthvyPIRLVKV---NEDTMEPLrdsqglcipcQPGEpgllVGQINQQDPlRRFDGY--VSDsatnk 477
Cdd:PRK07514 317 ErrAGTVGF---------PLPGVSLrvtDPETGAEL----------PPGE----IGMIEVKGP-NVFKGYwrMPE----- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 478 KIAHSvFRkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMA 557
Cdd:PRK07514 368 KTAEE-FR-ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 558 A-IADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvDTTGtfKIQKTRLqREGF 612
Cdd:PRK07514 445 VvVPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL-REQY 499
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
107-609 |
2.15e-28 |
|
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: 118.30 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 186
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeaptTPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05971 84 ----------------------------------------------TDGS-------DDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 sryyRIaAFGHhsysmraNDVLYDCLPLYHSAGNIM----------GVGQCII----YGLTVVLRK--KFSASRFWDDCV 330
Cdd:cd05971 111 ----RV-LLGH-------LPGVQFPFNLFPRDGDLYwtpadwawigGLLDVLLpslyFGVPVLAHRmtKFDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 331 KYNCTVVqYIGEICRYLLRQpVRDVERRHHVRL-AVGNGLRPAIWEEF---TQRFGVrQIGEFYGATECNCSIAN----M 402
Cdd:cd05971 179 RYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLrAIATGGESLGEELLgwaREQFGV-EVNEFYGQTECNLVIGNcsalF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 403 DGKVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdsqglcipcQPGEPGLLVgqINQQDPLrRFDGYVSD-SATNKKIAH 481
Cdd:cd05971 256 PIKPGSMG-------KPIPGHRVAIVDDNGTPL----------PPGEVGEIA--VELPDPV-AFLGYWNNpSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 482 SVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIAD 561
Cdd:cd05971 316 DWLLTGDLGRKDSD-------GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP-IRGEIVKAFVVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 564388681 562 PHNQLDPNSMYQELQKV----LASYAQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:cd05971 388 NPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
97-545 |
6.28e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 118.08 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 97 ALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGT 176
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 177 SAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPdtqlLDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGT 255
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPDTPIAdETAGADM------LYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 256 TGLPK---------AAIVVHSRYYRIAAFGHHSYsmrANDVLYDCLPLYHSAGN--IMGVGQCiiyGLTVVLRKKFSASR 324
Cdd:PRK08276 152 TGRPKgikrplpglDPDEAPGMMLALLGFGMYGG---PDSVYLSPAPLYHTAPLrfGMSALAL---GGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 325 FWDDCVKYNCTVVQYIGEICRYLLRQPvRDVERRHHV---RLAVgNGLRPAIWEeftqrfgVRQ---------IGEFYGA 392
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLP-EEVRARYDVsslRVAI-HAAAPCPVE-------VKRamidwwgpiIHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 393 TECN----CSIANMDGKVGSCGfnsRILTHVypirlVKVNEDTMEPLrdsqglciPcqPGEPGLLVGQINQQDplrrFDg 468
Cdd:PRK08276 297 SEGGgvtvITSEDWLAHPGSVG---KAVLGE-----VRILDEDGNEL--------P--PGEIGTVYFEMDGYP----FE- 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 469 YVSDSATNKKIAHsvfRKGDSAYlsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK08276 354 YHNDPEKTAAARN---PHGWVTV--GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
72-610 |
3.28e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.39 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 72 RRHRRAG----DTIPRIFQAVAQRQPERLALVDaSSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGL 147
Cdd:PRK06087 12 AAYRQQGywgdASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 148 WLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG--------EMAAAVAEVSEQLGKSLLkfcSGDLGPE-SVLP 218
Cdd:PRK06087 91 YLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVG---VDKLAPAtSSLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 219 DTQLLdpmlaeAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYriaaFGHHSYSMRAN----DVLYDCLPL 294
Cdd:PRK06087 168 LSQII------ADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYCARLNltwqDVFMMPAPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 295 YHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVRDVERRHHVrlaVGNGLR 370
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPADLSALRFFL---CGGTTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 371 PAIWEEFTQRFGVRqIGEFYGATE-CNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTmeplrdsqglcIPCqpGE 449
Cdd:PRK06087 315 PKKVARECQQRGIK-LLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-----------LPP--GC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 450 PGLLVGQINQQdplrrFDGYVSD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 528
Cdd:PRK06087 381 EGEEASRGPNV-----FMGYLDEpELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 529 AVLSRLLGQTDVAVygVAVP----GvEGKAGMAAIADPHNQLDPNSMYQEL-QKVLASYAQPIFLRLLPQVDTTGTFKIQ 603
Cdd:PRK06087 450 DILLQHPKIHDACV--VAMPderlG-ERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQ 526
|
....*..
gi 564388681 604 KTRLQRE 610
Cdd:PRK06087 527 KFLLRKD 533
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
74-609 |
3.52e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.59 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 74 HRRAGDTIPRIFQAVAQRQPERLALV------DASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGL 147
Cdd:PRK07529 20 ARDLPASTYELLSRAAARHPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 148 WLGLAKAGVVAAlLNVNLRREPLAFCLGTSAAKALI-YGGE----MAAAVAEVSEQL--GKSLLK-FCSGDLGPESVLPD 219
Cdd:PRK07529 100 LWGGEAAGIANP-INPLLEPEQIAELLRAAGAKVLVtLGPFpgtdIWQKVAEVLAALpeLRTVVEvDLARYLPGPKRLAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 220 TQL----------LDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLY 289
Cdd:PRK07529 179 PLIrrkaharildFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 290 DCLPLYHSAGNIMGVGQCIIYGLTVVL------RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV--RDVERrhhV 361
Cdd:PRK07529 259 CGLPLFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVdgHDISS---L 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 362 RLAVGNG--LRPAIWEEFTQRFGVRqIGEFYGATECNC--SIANMDG--KVGSCGFnsRI-LTHVypiRLVKVNEDTmEP 434
Cdd:PRK07529 336 RYALCGAapLPVEVFRRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGL--RLpYQRV---RVVILDDAG-RY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 435 LRDsqglcipCQPGEPGLLVgqinQQDPlRRFDGYVsDSATNKKIahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDT 514
Cdd:PRK07529 409 LRD-------CAVDEVGVLC----IAGP-NVFSGYL-EAAHNKGL-----WLEDGWLNTGDLGRIDADGYFWLTGRAKDL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 515 FRWRGENVSTTEVEAVLSRLLGQTDVAVYG--------VAVPGVEGKAGMAAIAdphnqldpnsmyQELQKVLASY---- 582
Cdd:PRK07529 471 IIRGGHNIDPAAIEEALLRHPAVALAAAVGrpdahageLPVAYVQLKPGASATE------------AELLAFARDHiaer 538
|
570 580
....*....|....*....|....*...
gi 564388681 583 -AQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:PRK07529 539 aAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
78-610 |
1.27e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.48 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 78 GDTIPRIFQAVAQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvv 157
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 158 AALLNVN--LRREPLAFCLGTSAAKALIYGGEMAAA--VAEVSEqLGKSLLKFCSGDLGPESvLPDTQLLDPMLAEAPTT 233
Cdd:PRK12583 95 AILVNINpaYRASELEYALGQSGVRWVICADAFKTSdyHAMLQE-LLPGLAEGQPGALACER-LPELRGVVSLAPAPPPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 234 PLA----QAPGKGM--------------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLY 295
Cdd:PRK12583 173 FLAwhelQARGETVsrealaerqasldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 296 HSAGNIMGVGQCIIYGLTVVL-RKKFSASRFWDDCVKYNCTVVQ-----YIGEicrylLRQPVRDVERRHHVRLAV--GN 367
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGImaGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 368 GLRPAIWEEFTQRFGVRQIGEFYGATECN------CSIANMDGKVGSCGfnsRILTHVYpirlVKVnedtmeplRDSQGL 441
Cdd:PRK12583 328 PCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqtTAADDLERRVETVG---RTQPHLE----VKV--------VDPDGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 442 CIPcqPGEPGLLVgqinqqdplrrFDGYV-------SDSATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDT 514
Cdd:PRK12583 393 TVP--RGEIGELC-----------TRGYSvmkgywnNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 515 FRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIA-DPHNQLDPNSMYQELQKVLASYAQPIFLRLLP 592
Cdd:PRK12583 454 IIRGGENIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*...
gi 564388681 593 QVDTTGTFKIQKTRLqRE 610
Cdd:PRK12583 532 EFPMTVTGKVQKFRM-RE 548
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
86-609 |
2.26e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.03 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 86 QAVAQRQPERLALVdaSSGICWTFAQLDTYSNAVANLFL-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 164
Cdd:PRK06839 9 EKRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 165 LRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESVLPDTQLLDPmlAEAPTTPLAQAPGKGMD 244
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQ---------------KVSYVQRVISITSL--KEIEDRKIDNFVEKNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASR 324
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 325 FWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVgNGLRPAIwEEFTQRFGVR--QIGEFYGATECNCS---I 399
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCP-EELMREFIDRgfLFGQGFGMTETSPTvfmL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 400 ANMDG--KVGSCG----FNSrilthvypIRLVKVNEDTMEplrdsqglcipcqPGEpgllVGQINQQDPLRRFDGYVSDS 473
Cdd:PRK06839 308 SEEDArrKVGSIGkpvlFCD--------YELIDENKNKVE-------------VGE----VGELLIRGPNVMKEYWNRPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 474 ATNKKIAhsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-G 552
Cdd:PRK06839 363 ATEETIQ-------DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHVKwG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 553 KAGMAAIA-DPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvDTTGtfKIQKTRLQR 609
Cdd:PRK06839 434 EIPIAFIVkKSSSVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
89-608 |
4.42e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 112.83 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK06178 43 ARERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGPES---VLPD---------TQLLDPMLAEAPTTPL 235
Cdd:PRK06178 121 ELSYELNDAGAEVLLALDQLAPVVEQVRAETSlRHVIVTSLADVLPAEptlPLPDslraprlaaAGAIDLLPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 236 AQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGL 312
Cdd:PRK06178 201 VPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 313 TVVLRKKFSASRFWDDCVKYNCT----VVQYIGEicryLLRQP---VRDVERRHHVRlAVG--NGLRPAI---WEEFTqr 380
Cdd:PRK06178 279 TLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVE----LMDHPrfaEYDLSSLRQVR-VVSfvKKLNPDYrqrWRALT-- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 381 fGVRQIGEFYGATE---CNCSIANMdgKVGSCGFNSRILTHVYPI---RLVKVNEDTMEPLrdsqglciPC-QPGE---- 449
Cdd:PRK06178 352 -GSVLAEAAWGMTEthtCDTFTAGF--QDDDFDLLSQPVFVGLPVpgtEFKICDFETGELL--------PLgAEGEivvr 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 450 -PGLLVGQINQQDplrrfdgyvsdsATnkkiAHSvFRkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 528
Cdd:PRK06178 421 tPSLLKGYWNKPE------------AT----AEA-LR--DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 529 AvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAIA----DPHNQLDPNSMYQELQKVLASYAQPIfLRLLPQVDTTGTFKI 602
Cdd:PRK06178 482 A----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKV 554
|
....*.
gi 564388681 603 QKTRLQ 608
Cdd:PRK06178 555 RKQDLQ 560
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-607 |
9.77e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 111.76 E-value: 9.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 79 DTIPRIFQAVAQRQPERLALVDasSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 158
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 159 ALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGKSLLKFCSGDLGpESVLPDTQLLDPMLA---EA 230
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPDALPPLRAIAVVDDA-ADATPAPAPGARVQLfalPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 231 PTTPLAQAPGKGMDDRLFYIY-TSGTTGLPKaaIVVHS-----RYYRIAAfghHSYSMRANDVLYDCLPLYHSAGNIMGV 304
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFtTSGTTSGPK--LVLHRqatllRHARAIA---RAYGYDPGAVLLAALPFCGVFGFSTLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 305 GqCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNgLRPAiWEEFTQRfgVR 384
Cdd:PRK06164 242 G-ALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPA-LGELAAL--AR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 385 QIGE----FYGATECncsIANMDGKVGSCGFNSRIL---THVYPIRLVKVnedtmeplRDSQGLCIpCQPGEPgllvGQI 457
Cdd:PRK06164 317 ARGVpltgLYGSSEV---QALVALQPATDPVSVRIEgggRPASPEARVRA--------RDPQDGAL-LPDGES----GEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 458 NQQDPlRRFDGYVSD-SATNKKI-AHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLL 535
Cdd:PRK06164 381 EIRAP-SLMRGYLDNpDATARALtDDGYFRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALP 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 536 GQTDVAVYGVAvpgVEGKAGMAA--IADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQVDTTGTFKIQKTRL 607
Cdd:PRK06164 453 GVAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFKVParvQVVEAFPVTESANGAKIQKHRL 526
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
89-610 |
6.14e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 108.82 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK06145 12 ARRTPDRAALVYRDQEI--SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGksllkfcsgdLGPESVLPDTQLLDPMLAEAPTTPLAQapgkgmDDRLF 248
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEFDAIVALETPKIV----------IDAAAQADSRRLAQGGLEIPPQAAVAP------TDLVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVHSRYY-----RIAAFGhhsysMRANDVLYDCLPLYHsagnimgVGQCIIYGLTVV-------L 316
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHwksidHVIALG-----LTASERLLVVGPLYH-------VGAFDLPGIAVLwvggtlrI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 317 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLR-PAI-WEEFTQRFGVRQIGEFYGATE 394
Cdd:PRK06145 222 HREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIRDFTRVFTRARYIDAYGLTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIANMDG-----KVGSCGfnsRILTHVypirlvkvnedTMEPLRDSQGLCIPCQPGEPGLLVGQINQqdplrrfdGY 469
Cdd:PRK06145 302 TCSGDTLMEAgreieKIGSTG---RALAHV-----------EIRIADGAGRWLPPNMKGEICMRGPKVTK--------GY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 470 VSDSatnKKIAHSVFrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 549
Cdd:PRK06145 360 WKDP---EKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 550 VEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:PRK06145 434 WGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
93-607 |
7.95e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 108.00 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSgiCWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 170
Cdd:cd05930 1 PDAVAVVDGDQ--SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG--AAYVPLDPSypAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 171 AFCLGTSAAKALIYGGEMAAAVaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmddrlfyI 250
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDLAYV---------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 251 YTSGTTGLPKAAIVVHsryyriAAFGHHSYSMRAndvLY-----DCLPLYHSAGNIMGVGQ---CIIYGLTVVLRKK--- 319
Cdd:cd05930 100 YTSGSTGKPKGVMVEH------RGLVNLLLWMQE---AYpltpgDRVLQFTSFSFDVSVWEifgALLAGATLVVLPEevr 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQIGEFYGATECNc 397
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEAT- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 398 sianmdgkvgscgfnsrILTHVYPIRLVKVNEDTM---EPLRDSQGL-----CIPCQPGEPG-LLVG--QINQqdplrrf 466
Cdd:cd05930 248 -----------------VDATYYRVPPDDEEDGRVpigRPIPNTRVYvldenLRPVPPGVPGeLYIGgaGLAR------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 467 dGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygV 545
Cdd:cd05930 304 -GYLNRPElTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV--V 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 546 AVPGVEGKAGMAA--IADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05930 381 AREDGDGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
108-607 |
1.17e-24 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 107.08 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygge 187
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 maaavaeVSEQLGKsllkfcsgdlgpesvlpdtqlldpmlaeapTTPLAQApgkgmDDRLFYIYTSGTTGLPKAAIVVHS 267
Cdd:cd05903 79 -------VPERFRQ------------------------------FDPAAMP-----DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 268 R-YYRIAAFGHHsYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQ----YIGE 342
Cdd:cd05903 117 TlSASIRQYAER-LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 343 ICRYLLRQPvrDVERRHHVRLAVGNGLRPAIWEEFTQRFGVRqIGEFYGATECNcsianmdGKVGSC--GFNSRIL-THV 419
Cdd:cd05903 196 LLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP-------GAVTSItpAPEDRRLyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 420 YPIRLVKVNedtmepLRDSQGLCIPcqPGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAHSVFrkgdsaYLSGDVLVM 499
Cdd:cd05903 266 RPLPGVEIK------VVDDTGATLA--PGV----EGELLSRGP-SVFLGYLDRPDLTADAAPEGW------FRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 500 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA-----DPHnQLDPNSMYQE 574
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DERLGERACAvvvtkSGA-LLTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....
gi 564388681 575 LQKV-LASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05903 402 LDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
62-610 |
1.22e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.22 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 62 SVLIRVRLElrRHRRAG----DTIPRIFQAVAQRQPERLALVDASSGIC----WTFAQLDTYSNAVANLFLQLGFAPGDV 133
Cdd:PRK13295 5 AVLLPPRRA--ASIAAGhwhdRTINDDLDACVASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLARLGVGRGDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 134 VAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIY-----GGEMAAAVAEVSEQLGK-SLLKFC 207
Cdd:PRK13295 83 VSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPELPAlRHVVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 208 SGDlGPESVlpDTQLLDPMLAEAP-TTPLAQAPGKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRIAAFghHSYSMR--- 283
Cdd:PRK13295 163 GGD-GADSF--EALLITPAWEQEPdAPAILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANI--VPYAERlgl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 284 -ANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWD----DCVKYNCTVVQYIGEICRY--LLRQPVRDVE 356
Cdd:PRK13295 236 gADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTRAvkESGRPVSSLR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 357 RrhhvRLAVGNGLRPAIWEEFTQRFGVRQIGEfYGATECNC----SIANMDGKVGScgfnsrilTHVYPIRLVKVNedtm 432
Cdd:PRK13295 316 T----FLCAGAPIPGALVERARAALGAKIVSA-WGMTENGAvtltKLDDPDERAST--------TDGCPLPGVEVR---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 433 epLRDSQGLCIPcqPGEPGLLV--GQINqqdplrrFDGYVSDSATNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDR 510
Cdd:PRK13295 379 --VVDADGAPLP--AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARIDAD-------GYIRISGR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 511 SGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA----DPHNQLDPNSM--YQELQKVLASYAq 584
Cdd:PRK13295 441 SKDVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvpRPGQSLDFEEMveFLKAQKVAKQYI- 515
|
570 580
....*....|....*....|....*.
gi 564388681 585 PIFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:PRK13295 516 PERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
89-612 |
4.46e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.79 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWtfAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPdtqlLDPMLAEA-PTTPLAQAPGkgmDDRL 247
Cdd:PRK07786 105 EIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG----YEDLLAEAgPAHAPVDIPN---DSPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 248 FYIYTSGTTGLPKAAIVVHSRYYRIAAfgHHSYSMRA---NDVLYDCLPLYHSAGnIMGVGQCIIYGLTVVLR--KKFSA 322
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVLTHANLTGQAM--TCLRTNGAdinSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 323 SRFWDDCVKYNCTVV-----QYIGeICRYLLRQPvRDVERRhhvrlAVGNGLRPA---IWEEFTQRFGVRQIGEFYGATE 394
Cdd:PRK07786 255 GQLLDVLEAEKVTGIflvpaQWQA-VCAEQQARP-RDLALR-----VLSWGAAPAsdtLLRQMAATFPEAQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIANMDG-----KVGSCGfnsriltHVYPIRLVKVNEDTMEPLrdsqglcipcQPGEpgllVGQINQQDPlrrfdGY 469
Cdd:PRK07786 328 MSPVTCMLLGedairKLGSVG-------KVIPTVAARVVDENMNDV----------PVGE----VGEIVYRAP-----TL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 470 VSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG 549
Cdd:PRK07786 382 MSGYWNNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 550 -VEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLqREGF 612
Cdd:PRK07786 460 wGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
85-602 |
7.90e-24 |
|
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: 105.50 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 85 FQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 164
Cdd:cd17651 1 FERQAARTPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 165 LRREPLAFCLGTSAAKALIyggemAAAVAevseqlgksllkfcSGDLGPESVlPDTQLLDPMLAEAPTTPLaqAPGKGMD 244
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL-----THPAL--------------AGELAVELV-AVTLLDQPGAAAGADAEP--DPALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVHsryyriaafghhsySMRANDVLYDCLPLYHSAG----NIMGVG-----QCII----YG 311
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPH--------------RSLANLVAWQARASSLGPGartlQFAGLGfdvsvQEIFstlcAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLRK---KFSASRFWDDCVKYNCTVV----QYIGEICRYLLRQPVRDVERRHHV----RLAVGNGLRpaiweEFTQR 380
Cdd:cd17651 203 ATLVLPPeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLR-----EFCAG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 381 FGVRQIGEFYGATECNCSIA-NMDGKVGSCGFNSRILTHVYPIRLVKVNEDtmepLRdsqglciPCQPGEPG-LLVGqin 458
Cdd:cd17651 278 LPGLRLHNHYGPTETHVVTAlSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA----LR-------PVPPGVPGeLYIG--- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 459 qQDPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 537
Cdd:cd17651 344 -GAGLAR--GYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 538 TDVAVygVAVPGVEGKAGMAA--IADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKI 602
Cdd:cd17651 421 REAVV--LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
88-615 |
8.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 105.51 E-value: 8.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 88 VAQRQPERLALVDASSgiCWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVaaLLNVNLR 166
Cdd:PRK07470 16 AARRFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMFAAF-RLGAV--WVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 167 REP--LAFCLGTSAAKALIYGG---EMAAAVAEVSEQLgKSLLKFCSGDLGPEsvlpdtqlLDPMLAEAPTTPLAQAPGK 241
Cdd:PRK07470 91 QTPdeVAYLAEASGARAMICHAdfpEHAAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGARVANAAVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 242 gMDDRLFYIYTSGTTGLPKAAIVVHSRyyriAAF-------------GHHSYSMRAndvlydcLPLYHSAGnIMGVGQcI 308
Cdd:PRK07470 162 -HDDPCWFFFTSGTTGRPKAAVLTHGQ----MAFvitnhladlmpgtTEQDASLVV-------APLSHGAG-IHQLCQ-V 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 309 IYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVERRHHvrlavgNGLRPAIWE-----EFTQRF 381
Cdd:PRK07470 228 ARGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHP--AVDRYDH------SSLRYVIYAgapmyRADQKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 382 GVRQIG----EFYGATECNCSIANM--------DG---KVGSCGFnsrilthvypirlvkvnEDT-ME-PLRDSQGLciP 444
Cdd:PRK07470 300 ALAKLGkvlvQYFGLGEVTGNITVLppalhdaeDGpdaRIGTCGF-----------------ERTgMEvQIQDDEGR--E 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 445 CQPGEpgllVGQINQQDPlRRFDGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 524
Cdd:PRK07470 361 LPPGE----TGEICVIGP-AVFAGYYNNPEANAK----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYP 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 525 TEVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMAA-IADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTF 600
Cdd:PRK07470 430 REIEEKLLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFFWDALPK---SGYG 505
|
570
....*....|....*
gi 564388681 601 KIQKtRLQREGFDPR 615
Cdd:PRK07470 506 KITK-KMVREELEER 519
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
80-341 |
1.25e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.97 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 159
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRL--TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 LLNVNLR--REPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLaq 237
Cdd:PRK07798 80 PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERD-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 238 aPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRiAAFG--------------HHSYSMRAND--VLYDCLPLYHSAGnI 301
Cdd:PRK07798 158 -FGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFR-VLLGgrdfatgepiedeeELAKRAAAGPgmRRFPAPPLMHGAG-Q 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564388681 302 MGVGQCIIYGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIG 341
Cdd:PRK07798 235 WAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
89-542 |
1.74e-23 |
|
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: 104.62 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN-VNLRR 167
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 168 EpLAFCLGTSAAKALIyggeMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPmlAEAPTTPLAQapgkgmDDRL 247
Cdd:cd05904 95 E-IAKQVKDSGAKLAF----TTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADE--AEPPVVVIKQ------DDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 248 FYIYTSGTTGLPKAAIVVHSRYyrIAAF-GHHSY--SMRANDVLYDC-LPLYHSAGnIMGVGQCII-YGLTVVLRKKFSA 322
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNL--IAMVaQFVAGegSNSDSEDVFLCvLPMFHIYG-LSSFALGLLrLGATVVVMPRFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 323 SRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRlAVGNG---LRPAIWEEFTQRFGVRQIGEFYGATECNCSI 399
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 400 ANMD------GKVGSCGFnsrilthVYPIRLVK-VNEDTMEPLRdsqglciPCQPGEpgLLV-G-QINQqdplrrfdGYV 470
Cdd:cd05904 318 AMCFapekdrAKYGSVGR-------LVPNVEAKiVDPETGESLP-------PNQTGE--LWIrGpSIMK--------GYL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388681 471 SD-SATNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 542
Cdd:cd05904 374 NNpEATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
107-609 |
2.00e-23 |
|
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: 103.20 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFclgtsaakaliygg 186
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtQLLDpmlAEApttplaqapgkGMDDRLFYIYTSGTTGLPKAAIVvh 266
Cdd:cd05912 68 ----------------------------------QLKD---SDV-----------KLDDIATIMYTSGTTGKPKGVQQ-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 sryyriaAFGHHSYSMRA---------NDVLYDCLPLYHSAG-NIMGVGqcIIYGLTVVLRKKFSASRFWDDCVKYNCTV 336
Cdd:cd05912 98 -------TFGNHWWSAIGsalnlglteDDNWLCALPLFHISGlSILMRS--VIYGMTVYLVDKFDAEQVLHLINSGKVTI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 337 VQYIGEICRYLLRqpvRDVERRH-HVRLAV-GNGLRPAIWEEFTQRFGVrQIGEFYGATE-----CNCSIANMDGKVGSC 409
Cdd:cd05912 169 ISVVPTMLQRLLE---ILGEGYPnNLRCILlGGGPAPKPLLEQCKEKGI-PVYQSYGMTEtcsqiVTLSPEDALNKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 410 G---FNSRIlthvypiRLVKVNEDtmeplrdsqglciPCQPGE-----PGLLVGQINQQDplrrfdgyvsdsATNKKIAH 481
Cdd:cd05912 245 GkplFPVEL-------KIEDDGQP-------------PYEVGEillkgPNVTKGYLNRPD------------ATEESFEN 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 482 SVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPgvEGKAGMAAIA- 560
Cdd:cd05912 293 GWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VGIP--DDKWGQVPVAf 361
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 564388681 561 -DPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKIQKTRLQR 609
Cdd:cd05912 362 vVSERPISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-607 |
2.82e-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: 103.14 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 94 ERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGF-APGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd05941 1 DRIAIVDDGDSI--TYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIYGGEMaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmddrlfyIYT 252
Cdd:cd05941 79 VITDSEPSLVLDPALI-------------------------------------------------------------LYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 253 SGTTGLPKAaiVVHSRyYRIAAFGH---HSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDC 329
Cdd:cd05941 98 SGTTGRPKG--VVLTH-ANLAANVRalvDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 330 VKYNCTVVQ-----YIGEICRYLLRQPVRDVERR---HHVRLAV-GNG-LRPAIWEEFTQRFGVRqIGEFYGATECNCSI 399
Cdd:cd05941 175 LMPSITVFMgvptiYTRLLQYYEAHFTDPQFARAaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 400 AN-MDG--KVGSCGFnsrilthvyPIRLVK---VNEDTMEPL-RDSQG-LCIPcqpgEPGLlvgqinqqdplrrFDGYVS 471
Cdd:cd05941 254 SNpLDGerRPGTVGM---------PLPGVQariVDEETGEPLpRGEVGeIQVR----GPSV-------------FKEYWN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 472 DSATNKKiahsVFRkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgV 550
Cdd:cd05941 308 KPEATKE----EFT-DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP-D 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 551 EGKAGMAAIA--DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05941 382 WGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-609 |
2.98e-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: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 83 RIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLN 162
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSL--TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG--AAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 163 VNlrreplafclgtsaakaliyGGEMAAAVAEVSEQLGKSLLKFCSGDlgpesvlpdtqlldpmlaeapttplaqapgkg 242
Cdd:cd17653 77 LD--------------------AKLPSARIQAILRTSGATLLLTTDSP-------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 243 mDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAND-------VLYDClplyhSAGNIMGvgqCIIYGLTVV 315
Cdd:cd17653 105 -DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrvaqvlsIAFDA-----CIGEIFS---TLCNGGTLV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 316 LRkkfSASRFWDDcVKYNCTVVQYIGEICRYLlrqPVRDVERRHHVRLAvGNGLRPAIWEEFTqrfGVRQIGEFYGATEC 395
Cdd:cd17653 176 LA---DPSDPFAH-VARTVDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRWS---PGRRLYNAYGPTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 NCSIAN---MDGKVGSCGfnsrilthvYPIRLVKV---NEDTMEPLRDSQG-LCIpcqpGEPGLLVGQINQQdplrrfdg 468
Cdd:cd17653 245 TISSTMtelLPGQPVTIG---------KPIPNSTCyilDADLQPVPEGVVGeICI----SGVQVARGYLGNP-------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 469 yvsdSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtdvaVYGVAVP 548
Cdd:cd17653 304 ----ALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE----VTQAAAI 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 549 GVEGKagMAAIADPHNqLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:cd17653 376 VVNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
109-607 |
3.68e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 103.62 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 109 FAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEM 188
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 189 AAAVAEVSEQLGKSLL-----------KFCSGDLGPEsvlPDTQLLDPMLA--EAPTTPLAQAPGKgmddrlfYIYTSGT 255
Cdd:PRK12406 94 LHGLASALPAGVTVLSvptppeiaaayRISPALLTPP---AGAIDWEGWLAqqEPYDGPPVPQPQS-------MIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 256 TGLPK-----AAIVVHSRYY-RIAAfghHSYSMRANDVLYDCLPLYHSAGNIMGVgQCIIYGLTVVLRKKFSASRFWDDC 329
Cdd:PRK12406 164 TGHPKgvrraAPTPEQAAAAeQMRA---LIYGLKPGIRALLTGPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELLQLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 330 VKYNCTVVQYIGEICRYLLRQP--VR---DVERRHHVRLAVGNGLRPaiweeftqrfgVRQ---------IGEFYGATEC 395
Cdd:PRK12406 240 ERHRITHMHMVPTMFIRLLKLPeeVRakyDVSSLRHVIHAAAPCPAD-----------VKRamiewwgpvIYEYYGSTES 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 ncsianmdGKVGSCGfNSRILTHvyPIRLVKVNEDTMEPLRDSQGLCIPcqPGEPGllvgqinqqDPLRRFDGYVSDSAT 475
Cdd:PRK12406 309 --------GAVTFAT-SEDALSH--PGTVGKAAPGAELRFVDEDGRPLP--QGEIG---------EIYSRIAGNPDFTYH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 476 NKKIAHSVFRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKA 554
Cdd:PRK12406 367 NKPEKRAEIDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 564388681 555 GMAAI-ADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:PRK12406 444 LMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
116-602 |
4.01e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 102.90 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 116 SNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIygGEMAAAVAEV 195
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFV-----PLNPTLKESVLRYLV--ADAGGRIVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 196 SEQLGkSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHsRYYRIAAF 275
Cdd:cd05922 76 DAGAA-DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSH------EDLALLLYTSGSTGSPKLVRLSH-QNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 276 GHHSY-SMRANDVLYDCLPLYHSAGnIMGVGQCIIYGLTVVLRKKFSASR-FWDDCVKYNCT---VVQYIGEIcrylLRQ 350
Cdd:cd05922 148 SIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAM----LTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 351 PVRDVERRHHVRL--AVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDG-----KVGSCGfnsrilthvypir 423
Cdd:cd05922 223 LGFDPAKLPSLRYltQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPerileKPGSIG------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 424 lVKVNEDTMEPLRDSQGlciPCQPGEPGLLVgqinqqdpLRR---FDGYVSDSATNKKIAhsvfRKGDSAYlSGDVLVMD 500
Cdd:cd05922 290 -LAIPGGEFEILDDDGT---PTPPGEPGEIV--------HRGpnvMKGYWNDPPYRRKEG----RGGGVLH-TGDLARRD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 501 ELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAgMAAIADPHNQLDPNSMYqeLQKVLA 580
Cdd:cd05922 353 EDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPKDVLRS--LAERLP 429
|
490 500
....*....|....*....|..
gi 564388681 581 SYAQPIFLRLLPQVDTTGTFKI 602
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGKV 451
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
77-545 |
7.28e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 102.66 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 77 AGDTIPRIF---QAVAQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAK 153
Cdd:PRK05852 11 ASDFGPRIAdlvEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 154 AGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKfcsgdLGPESVLPDTQLLDPMLAEAPTT 233
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVN-----VGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 234 PLAQAP-GKGMDDRLFyIYTSGTTGLPKAAIVVHSryyRIAAFGHH---SYSMRANDVLYDCLPLYHSAGNIMGVGQCII 309
Cdd:PRK05852 166 PATSTPeGLRPDDAMI-MFTGGTTGLPKMVPWTHA---NIASSVRAiitGYRLSPRDATVAVMPLYHGHGLIAALLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 310 YGLTVVL--RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRL----AVGNGLRPAIWEEFTQRFGV 383
Cdd:PRK05852 242 SGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrfirSCSAPLTAETAQALQTEFAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 384 RQIgEFYGATECNCSIANMDGKVGSCGFNSRILTHVypirlvkVNEDTMEPLR--DSQGLciPCQPGEpgllVGQINQQD 461
Cdd:PRK05852 322 PVV-CAFGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRivGSDGL--PLPAGA----VGEVWLRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 462 P--LRrfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQT 538
Cdd:PRK05852 388 TtvVR---GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVM 457
|
....*..
gi 564388681 539 DVAVYGV 545
Cdd:PRK05852 458 EAAVFGV 464
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
90-580 |
7.65e-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: 103.04 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 90 QRQPERLALV----DASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNL 165
Cdd:cd17634 64 RENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 166 RREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksLLKFCSGDLGPESVLPDTQLL------------------DPML 227
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITADGGVRAGRSVP------LKKNVDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDLI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 228 AEAPT--TPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYSMRANDVLYdclpLYHSAGNIMGv 304
Cdd:cd17634 218 AKASPehQPEAMNA----EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYW----CTADVGWVTG- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 305 GQCIIY-----GLTVVLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVER--RHHVRL--AVGNGLRP 371
Cdd:cd17634 289 HSYLLYgplacGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdRSSLRIlgSVGEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 372 AIWEEFTQRFGV--RQIGEFYGATECNCS-IANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSQ-GLCIPCQP 447
Cdd:cd17634 369 EAYEWYWKKIGKekCPVVDTWWQTETGGFmITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlVITDPWPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 448 GEPGLLvgqinqQDPLRRFDGYvsdsatnkkiahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 527
Cdd:cd17634 449 QTRTLF------GDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEI 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 564388681 528 EAVLSRLLGQTDVAVYGVAVPgVEGKAGMAAIADPHNQLDPNSMYQELQKVLA 580
Cdd:cd17634 509 ESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
89-608 |
1.41e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 101.62 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPE-FVGLWLGLaKAGVVAALLNVNLRR 167
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 168 EPLAFCLGTSAAKALIYGGEMAAAVAEVSEQL------GKSLLKFcsGDLgpESVLPDTqllDPMLAEAPTtplaqapGK 241
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGADLplrlsfGGEIDGF--GSF--EAALAGA---GPRLTEQPC-------GA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 242 GMddrlfyIYTSGTTGLPKA------AIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAgNIMGVGQCIIYGLTVV 315
Cdd:PRK13390 152 VM------LYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 316 LRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVrDVERRHHVrlavgNGLRPAIWEEFTQRFGVRQ---------I 386
Cdd:PRK13390 225 LAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDA-DVRTRYDV-----SSLRAVIHAAAPCPVDVKHamidwlgpiV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEFYGATECNcSIANMD-----GKVGSCGFNSRILTHVYpirlvkvnedtmeplrDSQGLCIPCqpGEPGLLVGQINQQd 461
Cdd:PRK13390 299 YEYYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHIC----------------DDDGNELPA--GRIGTVYFERDRL- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 462 PLRrfdgYVSD---SATNKKIAHSVFRKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQT 538
Cdd:PRK13390 359 PFR----YLNDpekTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVH 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 539 DVAVYGVAVP--GVEGKAGMAAIA--DPHNQLdPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:PRK13390 429 DVAVIGVPDPemGEQVKAVIQLVEgiRGSDEL-ARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
77-314 |
3.44e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 100.95 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 77 AGDTIPRIFQAVAQRQPERLALVDASSGI--CWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVAALLNVNLRREPLAFCLGTSAAKALIYGG-EMAAAVAEVSEQLGKslLKFC-----SGDLGPESVLPDTQLLDPMLA 228
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPS--LRHIvvldpRGLRDDPRLLSLDELLALGRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 229 EAPTTPLAQAPGK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGqC 307
Cdd:COG1022 167 VADPAELEARRAAvKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-A 245
|
....*..
gi 564388681 308 IIYGLTV 314
Cdd:COG1022 246 LAAGATV 252
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
107-610 |
1.11e-21 |
|
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: 99.08 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQL-GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG 185
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 186 GEMAAAVAEVSEQLG-------------------KSLLKFCSgdlgPESVLPDTQLLDPMLaeapttplaqapgkgmddr 246
Cdd:cd05928 122 DELAPEVDSVASECPslktkllvseksrdgwlnfKELLNEAS----TEHHCVETGSQEPMA------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 247 lfyIY-TSGTTGLPKAAIVVHSRY-YRIAAFGHHSYSMRANDVLY---DCLPLYHSAGNIMG---VGQCIIygltVVLRK 318
Cdd:cd05928 179 ---IYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWntsDTGWIKSAWSSLFEpwiQGACVF----VHHLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 319 KFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRH--HVrLAVGNGLRPAIWEEFTQRFGVrQIGEFYGATECN 396
Cdd:cd05928 252 RFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSlqHC-VTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 397 CSIANMDG---KVGSCGFNSRilthVYPIRLVkvnedtmeplrDSQGLCIPcqPGEPGLLVGQINQQDPLRRFDGYVSDS 473
Cdd:cd05928 330 LICANFKGmkiKPGSMGKASP----PYDVQII-----------DDNGNVLP--PGTEGDIGIRVKPIRPFGLFSGYVDNP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 474 atnKKIAHSvfRKGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGK 553
Cdd:cd05928 393 ---EKTAAT--IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGE 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388681 554 AGMAAI--ADPHNQLDPNSMYQELQ----KVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:cd05928 466 VVKAFVvlAPQFLSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
75-609 |
2.97e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.91 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 75 RRAGDTIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDELGTL--TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllKFCSGDLGPESVLPDTQLLDPMLAEA-PTT 233
Cdd:PRK13382 117 GADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD-----------RALADCPQATRIVAWTDEDHDLTVEVlIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 234 PLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSagniMGVGQCIIYGL- 312
Cdd:PRK13382 186 HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHA----WGFSQLVLAASl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 313 --TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP--VRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGvRQI 386
Cdd:PRK13382 262 acTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGsrMRPDVVIAFMDQFG-DVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEFYGATECN-CSIANMDGkvgscgfnsrilTHVYPIRLVKVNEDTMEPLRDSQGLCIPcqPGEpgllVGQINQQDPLrR 465
Cdd:PRK13382 341 YNNYNATEAGmIATATPAD------------LRAAPDTAGRPAEGTEIRILDQDFREVP--TGE----VGTIFVRNDT-Q 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 466 FDGYVSDSATNkkiahsvFRKGDSAylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK13382 402 FDGYTSGSTKD-------FHDGFMA--SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 546 AVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:PRK13382 473 DDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
107-548 |
5.04e-21 |
|
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: 96.42 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 186
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtqlLDPMLAEAPTtplaqapgkgMDDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05969 78 ------------------------------------TTEELYERTD----------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRK-KFSASRFWDDCVKYNCTVVQYIGEICR 345
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 346 YLLR---QPVR--DVERRHHVrLAVGNGLRPAI--WEEftQRFGVRqIGEFYGATECNC-SIAN---MDGKVGSCGfnsr 414
Cdd:cd05969 192 MLMKegdELARkyDLSSLRFI-HSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTETGSiMIANypcMPIKPGSMG---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 415 ilthvYPIRLVK--VNEDTMEPLRDSQGLCIPCQPGEPGLLVGQINQQDplrRFDGYvsdsatnkkiahsvFRKGdsAYL 492
Cdd:cd05969 264 -----KPLPGVKaaVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEE---RYKNS--------------FIDG--WYL 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 493 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 548
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
80-395 |
5.73e-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: 98.39 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAA 159
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG--AA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 L--LNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgDLGPESVLPDTQLLDPMLAEAPTTPLAq 237
Cdd:COG1020 553 YvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLP----------------ELGVPVLALDALALAAEPATNPPVPVT- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 238 apgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVlydcLPLYH------SAGNIMGvgqCIIY 310
Cdd:COG1020 616 ------PDDLAYvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR----VLQFAslsfdaSVWEIFG---ALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 311 GLTVVLRKK---FSASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPvrdverrHHVRLAV--GNGLRPAIWEEFTQRF 381
Cdd:COG1020 683 GATLVLAPPearRDPAALAELLARHRVTVLNltpsLLRALLDAAPEAL-------PSLRLVLvgGEALPPELVRRWRARL 755
|
330
....*....|....
gi 564388681 382 GVRQIGEFYGATEC 395
Cdd:COG1020 756 PGARLVNLYGPTET 769
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
108-542 |
1.88e-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: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVAN-LFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 186
Cdd:TIGR01733 1 TYRELDERANRLARhLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 EMAAAVAEVseqlgksllkfcsgdlgPESVLPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:TIGR01733 81 ALASRLAGL-----------------VLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 ----------SRYY------RIAAFGHHSYSMRANDVLydcLPLYHsagnimGVGQCIIYGltVVLRKKFSASRFWDDcv 330
Cdd:TIGR01733 143 rslvnllawlARRYgldpddRVLQFASLSFDASVEEIF---GALLA------GATLVVPPE--DEERDDAALLAALIA-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 331 KYNCTVVQYIGEICRYLLRQPVRDVERRHHVrLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECN--CSIANMDGKVGS 408
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPALASLRLV-ILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 409 CGFNSRI---LTHVypiRLVKVNEDTMeplrdsqglciPCQPGEPG-LLVGQINqqdpLRRfdGYVSDSA-TNKKIAHSV 483
Cdd:TIGR01733 289 RESPVPIgrpLANT---RLYVLDDDLR-----------PVPVGVVGeLYIGGPG----VAR--GYLNRPElTAERFVPDP 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 484 FRKGDSA--YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAV 542
Cdd:TIGR01733 349 FAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
107-554 |
3.11e-20 |
|
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: 94.86 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGG 186
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 EMAAAVAEVSeqLGKSLLKFCSGDLGPESVL---------PDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTG 257
Cdd:cd05968 172 GFTRRGREVN--LKEEADKACAQCPTVEKVVvvrhlgndfTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 258 LPKAAIVVHSRYYRIAAFG-HHSYSMRANDVLYdclpLYHSAGNIMG---VGQCIIYGLTVVLRKKF----SASRFWDDC 329
Cdd:cd05968 250 KPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLT----WFTDLGWMMGpwlIFGGLILGATMVLYDGApdhpKADRLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 330 VKYNCTVVQYIGEICRYLLRQPVRDVER--RHHVRLAVGNG--LRPAIWEEFtqrFGVRQIGE-----FYGATECNCSI- 399
Cdd:cd05968 326 EDHEITHLGLSPTLIRALKPRGDAPVNAhdLSSLRVLGSTGepWNPEPWNWL---FETVGKGRnpiinYSGGTEISGGIl 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 400 -ANMDGKVGSCGFNSrilthVYPIRLVKVNEDTMEPLRDSQGLCIPCQPGePGLLVGqiNQQDPLRRFDGYvsdsatnkk 478
Cdd:cd05968 403 gNVLIKPIKPSSFNG-----PVPGMKADVLDESGKPARPEVGELVLLAPW-PGMTRG--FWRDEDRYLETY--------- 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 479 iahsvFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgVEGKA 554
Cdd:cd05968 466 -----WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEA 535
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
78-315 |
3.33e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 94.49 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 78 GDTIPRIFQAVAQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 157
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 158 aaLLNVN--LRREPLAFCLGTSAAKALIYGG--------EMAAAVA-EVSEQLGKSL-------LKF-CSgdLGPESVlP 218
Cdd:PRK08315 95 --LVTINpaYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYELApELATCEPGQLqsarlpeLRRvIF--LGDEKH-P 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 219 DTQLLDPMLAEAPTTPLAQ--APGKGM--DDRLFYIYTSGTTGLPKAAIVVHsryYRIAAFGHH-SYSMR--ANDVLYDC 291
Cdd:PRK08315 170 GMLNFDELLALGRAVDDAElaARQATLdpDDPINIQYTSGTTGFPKGATLTH---RNILNNGYFiGEAMKltEEDRLCIP 246
|
250 260
....*....|....*....|....
gi 564388681 292 LPLYHSAGNIMGVGQCIIYGLTVV 315
Cdd:PRK08315 247 VPLYHCFGMVLGNLACVTHGATMV 270
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
72-260 |
3.94e-20 |
|
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: 94.44 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 72 RRHRRAG----DTIPRIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGL 147
Cdd:COG1021 14 ARYREAGywrgETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 148 WLGLAKAGV--VAALlnVNLRR-EPLAFClGTSAAKALI----YGG----EMAAAVAEVSEQLGKSLLkfcSGDLGPESV 216
Cdd:COG1021 92 FFALFRAGAipVFAL--PAHRRaEISHFA-EQSEAVAYIipdrHRGfdyrALARELQAEVPSLRHVLV---VGDAGEFTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388681 217 LPDtqlldpmLAEAPTTPLAQAPgkGMDDRLFYIYTSGTTGLPK 260
Cdd:COG1021 166 LDA-------LLAAPADLSEPRP--DPDDVAFFQLSGGTTGLPK 200
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
246-602 |
5.11e-20 |
|
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: 91.31 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 246 RLFYI-YTSGTTGLPKAaivvhsrYYR-----IAAF--GHHSYSMRANDVLYDCLPLYHSaGNIMGVGQCIIYGLTVVLR 317
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVERRHHVR--LAVGNGLRPAIWEEFTQRFGVRQIGEFYGATEC 395
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 NCSIANMDG---KVGSCGfnsRILTHVyPIRLvkvnedtmeplRDSQGlcipcqpGEPGLLVGQINQqdplrRFDGYVSD 472
Cdd:cd17633 149 SFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM-----VFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 473 SATNKkiaHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV------- 545
Cdd:cd17633 202 GFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdarfge 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 546 -AVPGVEGkagmaaiadphNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKI 602
Cdd:cd17633 272 iAVALYSG-----------DKLTYKQLKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-602 |
7.85e-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: 92.54 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 187
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 267
Cdd:cd05935 83 L-------------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 268 RYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYL 347
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 348 LRQPvrDVERRHHVRLAV----GNGLRPAIWEEFTQRFGVRQIgEFYGATEcNCSianmdgkvgscgfnsriLTHVYPir 423
Cdd:cd05935 188 LATP--EFKTRDLSSLKVltggGAPMPPAVAEKLLKLTGLRFV-EGYGLTE-TMS-----------------QTHTNP-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 424 lvkvnedtmePLR-DSQGLCIPCQ----------------PGEpgllVGQINQQDPlRRFDGYVSDSATNKKIAhsVFRK 486
Cdd:cd05935 245 ----------PLRpKLQCLGIP*FgvdarvidietgrelpPNE----VGEIVVRGP-QIFKGYWNRPEETEESF--IEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 487 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP--GVEGKAGMAAIADPHN 564
Cdd:cd05935 308 GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDErvGEEVKAFIVLRPEYRG 387
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564388681 565 QLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKI 602
Cdd:cd05935 388 KVTEEDIIEWAREQMAAYKYPrevEFVDELPR---SASGKI 425
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-607 |
3.02e-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: 91.11 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 83 RIFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN 162
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 163 VNLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqlgksllkfcsgdlgpesvLPDTQLLDPMLAEAPTTPLAQAPGKg 242
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLLTDRSLAGRAGG----------------------LEVAVVIDEALDAGPAGNPAVPVSP- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 243 mDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAfgHHSY-SMRANDVLYDCLPLYHSAG--NIMGvgqCIIYGLTVVLRKK 319
Cdd:cd12117 136 -DDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYvTLGPDDRVLQTSPLAFDAStfEIWG---ALLNGARLVLAPK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 ---FSASRFWDDCVKYNCTV---------------VQYIGEIcRYLL----RQPVRDVER--RHHVRLAVGNGLRPAIWE 375
Cdd:cd12117 210 gtlLDPDALGALIAEEGVTVlwltaalfnqladedPECFAGL-RELLtggeVVSPPHVRRvlAACPGLRLVNGYGPTENT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 376 EFTQRFGVRQIGEFYGATECNCSIANmdgkvgscgfnsrilTHVYPIrlvkvnedtmeplrDSQGlcIPCQPGEPG-LLV 454
Cdd:cd12117 289 TFTTSHVVTELDEVAGSIPIGRPIAN---------------TRVYVL--------------DEDG--RPVPPGVPGeLYV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 455 GqinqQDPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSR 533
Cdd:cd12117 338 G----GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 534 LLGQTDVAVygVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd12117 412 HPGVREAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
89-533 |
4.51e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 91.17 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGIcwTFAQLDTYSNAVANlFLQ--LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLR 166
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAI--SYRELLEEAERLAG-YLQqeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 167 REPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDL---GPESVLPD---TQLLDPMLAEAPTTPLAQA- 238
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYlpaEPEIAVPAwlrAEPPLQALAPGGVVAWKEAl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 239 -----PGK---GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIY 310
Cdd:PRK08314 177 aaglaPPPhtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 311 GLTVVLrkkfsASRfWD-----DCV-KYNCTVVQYIGEICRYLLRQPvrDVERRHHVRLA-VGNG---LRPAIWEEFTQR 380
Cdd:PRK08314 257 GATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASP--GLAERDLSSLRyIGGGgaaMPEAVAERLKEL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 381 FGVRQIgEFYGATECNC-SIAN-MDGKVGSC------GFNSRIlthvypirlvkVNEDTMEPLrdsqglcipcQPGEpgl 452
Cdd:PRK08314 329 TGLDYV-EGYGLTETMAqTHSNpPDRPKLQClgiptfGVDARV-----------IDPETLEEL----------PPGE--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 453 lVGQINQQDPlRRFDGYVSDSATNKKI-----AHSVFRKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEV 527
Cdd:PRK08314 384 -VGEIVVHGP-QVFKGYWNRPEATAEAfieidGKRFFRTGDLGR-------MDEEGYFFITDRLKRMINASGFKVWPAEV 454
|
....*.
gi 564388681 528 EAVLSR 533
Cdd:PRK08314 455 ENLLYK 460
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-607 |
4.77e-19 |
|
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: 90.23 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFL-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLG-TSAAKALIY 184
Cdd:cd05958 11 WTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 185 GGEMAAavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgkgmDDRLFYIYTSGTTGLPKAAIV 264
Cdd:cd05958 91 HALTAS-----------------------------------------------------DDICILAFTSGTTGAPKATMH 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 265 VHSRYYRIA-AFGHHSYSMRANDVLYDCLPLYHSagniMGVGQCIIY----GLTVVLRKKFSASRFWDDCVKYNCTVVQY 339
Cdd:cd05958 118 FHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 340 IGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQIgEFYGATEC-NCSIANMDGkvgscgfnsril 416
Cdd:cd05958 194 APTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMfHIFISARPG------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 417 tHVYPIRLVKVNEDTMEPLRDSQGLCIPcqPGEPGLLVgqinqqdpLRRFDGYVSDSatnKKIAHSVFRKGDSAylSGDV 496
Cdd:cd05958 261 -DARPGATGKPVPGYEAKVVDDEGNPVP--DGTIGRLA--------VRGPTGCRYLA---DKRQRTYVQGGWNI--TGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 497 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG--------VEGKAGMAAIADPHNQLdp 568
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvvkafVVLRPGVIPGPVLAREL-- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564388681 569 nsmyQELQK-VLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05958 403 ----QDHAKaHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
251-608 |
5.64e-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: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 251 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVL-RKKFSASRFWDDC 329
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 330 VKYNCTVVQ-----YIGEicrylLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIAN- 401
Cdd:cd05917 89 EKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 402 -----MDGKVGSCGfnsRILTHVYpirlVK-VNEDT-MEPLRDSQG-LCIpcqpgePGLLVGQINQQDPLRrfdgyvsds 473
Cdd:cd05917 164 rtddsIEKRVNTVG---RIMPHTE----AKiVDPEGgIVPPVGVPGeLCI------RGYSVMKGYWNDPEK--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 474 aTNKKIahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGK 553
Cdd:cd05917 222 -TAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-GE 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 554 AGMAAIA-DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:cd05917 294 EVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-607 |
8.52e-19 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 89.64 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 82 PRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL 161
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 162 NVNLRREPLAFCLGTSAAKALIYGGEMAAAvaevseqlgksllkfcsgdlgPESVLPDTQLLDPMLAEAPTTPLAQAPGK 241
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTADLAAR---------------------LPAGGDVALLGDEALAAPPATPPLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 242 gmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVL-------YDC------LPLYHSAGNIM---GVG 305
Cdd:cd17646 138 --DNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVlqktplsFDVsvwelfWPLVAGARLVVarpGGH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 306 QCIIYgLTVVLRkkfsasrfwDDCVkyncTVVQYIGEICRYLLRQPvrDVERRHHVRLAV--GNGLRPAIWEEFTQRFGV 383
Cdd:cd17646 216 RDPAY-LAALIR---------EHGV----TTCHFVPSMLRVFLAEP--AAGSCASLRRVFcsGEALPPELAARFLALPGA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 384 RqIGEFYGATE-------CNCSIANMDGKV--GSCGFNSRILthvypirlvkVNEDTMEplrdsqglciPCQPGEPG-LL 453
Cdd:cd17646 280 E-LHNLYGPTEaaidvthWPVRGPAETPSVpiGRPVPNTRLY----------VLDDALR----------PVPVGVPGeLY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 454 VGQInqqdPLRRfdGYVSDSA-TNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLS 532
Cdd:cd17646 339 LGGV----QLAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALA 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388681 533 RLLGQTDVAVygVAVPGVEGKAGMAA---IADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd17646 413 AHPAVTHAVV--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-609 |
4.76e-18 |
|
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: 87.19 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygge 187
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 maaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeaptTPLAQApGKGMDDRLFYIYTSGTTGLPKaAIVVHS 267
Cdd:cd05973 78 ---------------------------------------------TDAANR-HKLDSDPFVMMFTSGTTGLPK-GVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 268 RYyrIAAFghHSYSMRANDVLYDclplyHSAGNIMGVGQCiiYGL-------------TVVLRKKFSASRFWDDCVKYNC 334
Cdd:cd05973 111 RA--LAAF--GAYLRDAVDLRPE-----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 335 TVVQYIGEICRYLLRQPVrDVERRHHVRLAV----GNGLRPAIWEEFTQRFGVrQIGEFYGATECNCSIANMDG-----K 405
Cdd:cd05973 180 TNLAGSPTAYRLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALGV-PIHDHYGQTELGMVLANHHAlehpvH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 406 VGSCGFnsrilthVYP-IRLVKVNEDTMEPLrdsqglcipcqPGEPGLLVGQINQQdPLRRFDGYvsdsatnkkiahsvF 484
Cdd:cd05973 258 AGSAGR-------AMPgWRVAVLDDDGDELG-----------PGEPGRLAIDIANS-PLMWFRGY--------------Q 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 485 RKGDSA-----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPG----VEGKAG 555
Cdd:cd05973 305 LPDTPAidggyYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPErtevVKAFVV 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 564388681 556 MAAIADPHNQLDpNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:cd05973 385 LRGGHEGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
74-545 |
1.32e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 86.19 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 74 HRRAGDTIPRIFQAVAQRQPERLALVDasSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEfvgLWLGLAk 153
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE---VLMAIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 154 AGVVAALLNVNLrrEPL------AFCLGTSAAKALIY--------GGEMAAAVAEVseqlgKSLLKFCSGDLGPEsvlpd 219
Cdd:PRK06188 81 AAQLAGLRRTAL--HPLgslddhAYVLEDAGISTLIVdpapfverALALLARVPSL-----KHVLTLGPVPDGVD----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 220 tqlldpMLAEAPTTPLAQA-PGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSA 298
Cdd:PRK06188 149 ------LLAAAAKFGPAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 299 GNImgVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVERRHHVRLAV----GNGLRPAIW 374
Cdd:PRK06188 223 GAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHP--DLRTRDLSSLETvyygASPMSPVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 375 EEFTQRFGvrQI-GEFYGATECNCSIANMD---------GKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSQGLCIP 444
Cdd:PRK06188 299 AEAIERFG--PIfAQYYGQTEAPMVITYLRkrdhdpddpKRLTSCGR---------PTPGLRVA------LLDEDGREVA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 445 cqPGEPgllvGQINQQDPLrRFDGYVSDSATNKKiahsVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVS 523
Cdd:PRK06188 362 --QGEV----GEICVRGPL-VMDGYWNRPEETAE----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVF 427
|
490 500
....*....|....*....|..
gi 564388681 524 TTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVIGV 449
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
94-545 |
1.46e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.49 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 94 ERLAL--VDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLeGR-PEFVGLWLGLAKAGVVAALLNVNLRREPL 170
Cdd:PRK04319 59 DKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFM-PRiPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 171 AFCLGTSAAKALIYGGEMAAAVaeVSEQLGKslLK--FCSGDLGPESvlPDTQLLDPMLAEAPTTplAQAPGKGMDDRLF 248
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALLERK--PADDLPS--LKhvLLVGEDVEEG--PGTLDFNALMEQASDE--FDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVHSryyriAAFGHHS---YSM--RANDVlYDClplyhSA--GNIMGVGQCII----YGLT-VVL 316
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHN-----AMLQHYQtgkYVLdlHEDDV-YWC-----TAdpGWVTGTSYGIFapwlNGATnVID 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 317 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVrDVERRH---HVR--LAVGNGLRP-AIW---EEFTQRfgvrqIG 387
Cdd:PRK04319 279 GGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGD-DLVKKYdlsSLRhiLSVGEPLNPeVVRwgmKVFGLP-----IH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 388 EFYGATECNCS-IAN---MDGKVGSCGfnsRILTHVYpIRLVKVNEDTMEPLRDSQgLCIpcQPGEPGLLVGQINQQDpl 463
Cdd:PRK04319 353 DNWWMTETGGImIANypaMDIKPGSMG---KPLPGIE-AAIVDDQGNELPPNRMGN-LAI--KKGWPSMMRGIWNNPE-- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 464 rRFDGYvsdsatnkkiahsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEavlSRLLGQTDVAVY 543
Cdd:PRK04319 424 -KYESY--------------FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE---SKLMEHPAVAEA 483
|
..
gi 564388681 544 GV 545
Cdd:PRK04319 484 GV 485
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
93-607 |
3.69e-17 |
|
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: 84.63 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIyggemaaavaevseqlgksllkFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQAPgkGMDDRLFYIYT 252
Cdd:cd12114 79 ILADAGARLVL----------------------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 253 SGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRANDVLYDCLPLYH--SAGNIMGVgqcIIYGLTVVL----RKKFSASrf 325
Cdd:cd12114 135 SGSTGTPKGVMISHRAALNtILDINRR-FAVGPDDRVLALSSLSFdlSVYDIFGA---LSAGATLVLpdeaRRRDPAH-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 326 WDDCV-KYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLA------VGNGLRPAIWEeftQRFGVRQIGeFYGATEcncs 398
Cdd:cd12114 209 WAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVllsgdwIPLDLPARLRA---LAPDARLIS-LGGATE---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 399 ianmdgkvGScgfnsrILTHVYPIRlvKVNEDTME-----PLR-------DSQGLciPCQPGEPG-LLVGQIN-----QQ 460
Cdd:cd12114 281 --------AS------IWSIYHPID--EVPPDWRSipygrPLAnqryrvlDPRGR--DCPDWVPGeLWIGGRGvalgyLG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 461 DPLRRFDGYVSDSAtnkkiAHSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDV 540
Cdd:cd12114 343 DPELTAARFVTHPD-----GERLYRTGDLGRYRPD-------GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 541 AVygVAVPGVEGKAgMAAIADPHNQ---LDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd12114 411 VV--VVLGDPGGKR-LAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
84-560 |
2.53e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 82.34 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRqPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 163
Cdd:PLN02246 29 CFERLSEF-SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 164 NLRREPLAFCLGTSAAKALIyggEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQapgkgm 243
Cdd:PLN02246 108 FYTPAEIAKQAKASGAKLII---TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISP------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAF--GHH-SYSMRANDVLYDCLPLYH--SAGNIMGVGqcIIYGLTVVLR 317
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHkGLVTSVAQQvdGENpNLYFHSDDVILCVLPMFHiySLNSVLLCG--LRVGAAILIM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLaVGNGLRP---AIWEEFTQRFGVRQIGEFYGATE 394
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPlgkELEDAFRAKLPNAVLGQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIAnM---------DGKVGSCGfnsrilTHVYPIRLVKVNEDTMEPLRDSqglcipcQPGEPGLLVGQInqqdplrr 465
Cdd:PLN02246 336 AGPVLA-MclafakepfPVKSGSCG------TVVRNAELKIVDPETGASLPRN-------QPGEICIRGPQI-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 466 FDGYVSD-SATNKKI-----AHSvfrkGDSAYLSGDvlvmDElgyMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 539
Cdd:PLN02246 394 MKGYLNDpEATANTIdkdgwLHT----GDIGYIDDD----DE---LFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD 462
|
490 500
....*....|....*....|.
gi 564388681 540 VAVygvaVPGVEGKAGMAAIA 560
Cdd:PLN02246 463 AAV----VPMKDEVAGEVPVA 479
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
244-548 |
3.50e-16 |
|
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: 81.61 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFghhsYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRkk 319
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHknllANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 fsasrfwddcvkYNCTVVQYIGEI-----CRYLLRQPV--RDVERRHH------VRLAV--GNGLRPAIWEEFTQRFGVR 384
Cdd:cd05909 221 ------------PNPLDYKKIPELiydkkATILLGTPTflRGYARAAHpedfssLRLVVagAEKLKDTLRQEFQEKFGIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 385 qIGEFYGATEC----NCSIANMDGKVGSCGfnsRILTHVyPIRLVKVneDTMEPLRDsqglcipcqpGEPGLLVGQINQq 460
Cdd:cd05909 289 -ILEGYGTTECspviSVNTPQSPNKEGTVG---RPLPGM-EVKIVSV--ETHEEVPI----------GEGGLLLVRGPN- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 461 dplrRFDGYVSDSatnkkiAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQtDV 540
Cdd:cd05909 351 ----VMLGYLNEP------ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DN 419
|
....*...
gi 564388681 541 AVYGVAVP 548
Cdd:cd05909 420 EVAVVSVP 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-616 |
4.68e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 41 SGGWR-FLRIVCKTARRDLFGLSVLIRV--RLELRRHRRAGDTIPR---IFQAVAQ---RQPERLALVdaSSGICWTFAQ 111
Cdd:PRK12316 1956 DRHLLhLLEQMAEDAQAALGELALLDAGerQRILADWDRTPEAYPRgpgVHQRIAEqaaRAPEAIAVV--FGDQHLSYAE 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 112 LDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAa 191
Cdd:PRK12316 2034 LDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE- 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 192 vaevseqlgksllkfcsgDLGPESVLPDTQLLDPM-LAEAPTT-PLAQAPGkgmDDRLFYIYTSGTTGLPKAAIVVHSRY 269
Cdd:PRK12316 2113 ------------------RLPLPAGVARLPLDRDAeWADYPDTaPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGAL 2171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 270 Y-RIAAFGhHSYSMRANDVLYDCLPLYHSaGNIMGVGQCIIYGLTVVLR--KKFSASRFWDDCVKYNCTVVQYIGEICRY 346
Cdd:PRK12316 2172 VaHCQAAG-ERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPVYLQQ 2249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 347 LLRQPVRDvERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQIGEFYGATEcncsiANMDGKVGSCGFNSRILTHVYPI-- 422
Cdd:PRK12316 2250 LAEHAERD-GRPPAVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTE-----AVVTPLLWKCRPQDPCGAAYVPIgr 2323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 423 ----RLVKVNEDTMEPLrdSQGLCIPCQPGEPGLLVGQINQqdPLRRFDGYVSDSATNkkiahsvfrKGDSAYLSGDVLV 498
Cdd:PRK12316 2324 algnRRAYILDADLNLL--APGMAGELYLGGEGLARGYLNR--PGLTAERFVPDPFSA---------SGERLYRTGDLAR 2390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 499 MDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMA-AIADPHNQLDPNSMYQELQK 577
Cdd:PRK12316 2391 YRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAyVVPDDAAEDLLAELRAWLAA 2468
|
570 580 590
....*....|....*....|....*....|....*....
gi 564388681 578 VLASYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQ 616
Cdd:PRK12316 2469 RLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
89-548 |
4.71e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 81.19 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASsgICWTFAQldTYSNAV--ANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLR 166
Cdd:cd12118 14 AAVYPDRTSIVYGD--RRYTWRQ--TYDRCRrlASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 167 REPLAFCLGTSAAKALIYggemaaavaevseqlgksllkfcsgdlgpesvlpDTQLL-DPMLAEAPTTPLAQAPgKGMDD 245
Cdd:cd12118 90 AEEIAFILRHSEAKVLFV----------------------------------DREFEyEDLLAEGDPDFEWIPP-ADEWD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 246 RLFYIYTSGTTGLPKAaIVVHSRYYRIAAFGH-HSYSMRANDVLYDCLPLYHSAG-----NIMGVGqciiyGLTVVLRKk 319
Cdd:cd12118 135 PIALNYTSGTTGRPKG-VVYHHRGAYLNALANiLEWEMKQHPVYLWTLPMFHCNGwcfpwTVAAVG-----GTNVCLRK- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 FSASRFWDDCVKYNctVVQYIGE--ICRYLLRQPVRDVERR-HHVRLAVGNGLRPAIWEEFTQRFGVRqIGEFYGATECN 396
Cdd:cd12118 208 VDAKAIYDLIEKHK--VTHFCGAptVLNMLANAPPSDARPLpHRVHVMTAGAPPPAAVLAKMEELGFD-VTHVYGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 397 csianmdGKVGSC---------------GFNSRI-LTHVYPIRLVKVNEDTMEPL-RDSQGLcipcqpGEPgLLVGQINQ 459
Cdd:cd12118 285 -------GPATVCawkpewdelpteeraRLKARQgVRYVGLEEVDVLDPETMKPVpRDGKTI------GEI-VFRGNIVM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 460 QdplrrfdGYVSDSATNKKiahsVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 539
Cdd:cd12118 351 K-------GYLKNPEATAE----AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLE 417
|
....*....
gi 564388681 540 VAVygVAVP 548
Cdd:cd12118 418 AAV--VARP 424
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
74-610 |
4.77e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 81.62 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 74 HRRAGDTIP--RIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGL 151
Cdd:PRK06710 17 STISYDIQPlhKYVEQMASRYPEKKALHFLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 152 AKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG---------KSLLKFCSGDLGPESVLPDTQL 222
Cdd:PRK06710 95 LLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKiehvivtriADFLPFPKNLLYPFVQKKQSNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 223 LdPMLAEAPTTPLAQAPGKGMD-----------DRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFG-HHSYS-MRANDVLY 289
Cdd:PRK06710 175 V-VKVSESETIHLWNSVEKEVNtgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 290 DCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV-GNG 368
Cdd:PRK06710 254 GVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 369 LRPAIWEEFTQRFGVRQIGEFYGATEcncsianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEPLRDSQGLCIPCQPG 448
Cdd:PRK06710 334 PLPVEVQEKFETVTGGKLVEGYGLTE------------------SSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 449 E---PGLlVGQINQQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 525
Cdd:PRK06710 396 EalpPGE-IGEIVVKGP-QIMKGYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 526 EVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKT 605
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
....*
gi 564388681 606 RLQRE 610
Cdd:PRK06710 548 VLIEE 552
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
79-545 |
9.06e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 80.66 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 79 DTIPRIFQAvaQRQPERLALVDASSGICWTFAQLDTYSNAVAN-LFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 157
Cdd:PLN02574 41 DAVSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 158 AALLNvnlrrePLAfCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdLG-PESVLPDTQLLDPMLAEAPT---- 232
Cdd:PLN02574 119 VTTMN------PSS-SLGEIKKRVVDCSVGLAFTSPENVEKLSP---------LGvPVIGVPENYDFDSKRIEFPKfyel 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 233 ----TPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYyrIAA------FGHHSYSMRANDVLY-DCLPLYHSAGNI 301
Cdd:PLN02574 183 ikedFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNL--IAMvelfvrFEASQYEYPGSDNVYlAALPMFHIYGLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 302 MGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLR--QPVRDVERRHHVRLAVGNG-LRPAIWEEFT 378
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAApLSGKFIQDFV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 379 QRFGVRQIGEFYGATEcncSIAnmdgkVGSCGFNSRILTHVYPIRLVKVNedtMEP--LRDSQGLCIPcqPGE------- 449
Cdd:PLN02574 341 QTLPHVDFIQGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPN---MQAkvVDWSTGCLLP--PGNcgelwiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 450 -PGLLVGQINqqdplrrfDGYVSDSATNKkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 528
Cdd:PLN02574 408 gPGVMKGYLN--------NPKATQSTIDK----------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
|
490
....*....|....*..
gi 564388681 529 AVLSRLLGQTDVAVYGV 545
Cdd:PLN02574 470 AVLISHPEIIDAAVTAV 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
110-607 |
2.01e-15 |
|
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: 79.34 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 110 AQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLakaGVVAALLNVNLRREPLAF---CLGTSAAKALIYGG 186
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIAD---GVYIYLINSILTVFAAAAawkCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 EMAAAVAEVseqlgKSLLKFCSGDLGPE--SVLPDtqlLDPMLAEAPTTPLA-QAPGKGMddrlfyIYTSGTTGLPKA-- 261
Cdd:cd05929 79 AEACAIIEI-----KAAALVCGLFTGGGalDGLED---YEAAEGGSPETPIEdEAAGWKM------LYSGGTTGRPKGik 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 262 ----AIVVHSRYYRIAAFGhhsYSMRANDVLYDCLPLYHSAGNI--MGVgqcIIYGLTVVLRKKFSASRFWDDCVKYNCT 335
Cdd:cd05929 145 rglpGGPPDNDTLMAAALG---FGPGADSVYLSPAPLYHAAPFRwsMTA---LFMGGTLVLMEKFDPEEFLRLIERYRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 336 VVQYIGEICRYLLRQP--VRDVERRHHVRLAVGNGLRPAIW-EEFTQRFGVRQIGEFYGATECNcsianmdgkvGSCGFN 412
Cdd:cd05929 219 FAQFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAAPCPPWvKEQWIDWGGPIIWEYYGGTEGQ----------GLTIIN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 413 S-RILTHvyPIRLVKVNEDTMEpLRDSQGLciPCQPGEPGLLVgqinqqdplrrFDGYVSDSATNK--KIAHSVFRKGDS 489
Cdd:cd05929 289 GeEWLTH--PGSVGRAVLGKVH-ILDEDGN--EVPPGEIGEVY-----------FANGPGFEYTNDpeKTAAARNEGGWS 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 490 AYlsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAIaDPHNQLDP 568
Cdd:cd05929 353 TL--GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QPAPGADA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 564388681 569 NSMYQE-----LQKVLASYAQP---IFLRLLPQVDTTgtfKIQKTRL 607
Cdd:cd05929 428 GTALAEeliafLRDRLSRYKCPrsiEFVAELPRDDTG---KLYRRLL 471
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
78-585 |
2.11e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 79.66 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 78 GDTIPRIFQAVAQRQPERLALvdASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVV 157
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 158 AALLNVNLRREPLAFCLGTSAAKALIYGGEmaaaVAEVSEQLgksllkfcSGDLGPESV--------LPDTQLL------ 223
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIVWDK----VAPTVERL--------RRTTPLETIvsvnmiaaMPLLQRLalrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 224 -------DPMLAEAP-TTPLAQ-----APGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHH--S 279
Cdd:PRK05605 177 palrkarAALTGPAPgTVPWETlvdaaIGGDGSdvshprptpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 280 YSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEIcrYllrQPVRDVERRH 359
Cdd:PRK05605 257 GLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL--Y---EKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 360 HVRLavgNGLRPAI-------------WEEFTQRFGVrqigEFYGATECN----CSIANMDGKVGSCG--FNSRIlthvy 420
Cdd:PRK05605 332 GVDL---SGVRNAFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMSDDRRPGYVGvpFPDTE----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 421 pIRLVkvneDTMEPLRDsqglcIPcqPGEPG-LLVgqinqQDPlRRFDGYVSDSATNKKIAHsvfrkgDSAYLSGDVLVM 499
Cdd:PRK05605 400 -VRIV----DPEDPDET-----MP--DGEEGeLLV-----RGP-QVFKGYWNRPEETAKSFL------DGWFRTGDVVVM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 500 DELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVEGKAGMAA--IADPHNQLDPNSMYQELQK 577
Cdd:PRK05605 456 EEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVAavVLEPGAALDPEGLRAYCRE 533
|
....*...
gi 564388681 578 VLASYAQP 585
Cdd:PRK05605 534 HLTRYKVP 541
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
250-604 |
6.33e-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: 76.39 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 250 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDC 329
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 330 VKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV-GNGLRPAIW-EEFTQRFGVRQIGEFYGATECNCSianmdgkvg 407
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 408 scgfnsrilthvypirlvkvnedTM-EPLRDSQGLCIPCQPGEPGLLVGQINQQDPLRR----FDGYVSD-SATNKKIah 481
Cdd:cd17638 157 -----------------------TMcRPGDDAETVATTCGRACPGFEVRIADDGEVLVRgynvMQGYLDDpEATAEAI-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 482 svfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVeGKAGMA-AIA 560
Cdd:cd17638 212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGKAfVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 564388681 561 DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQK 604
Cdd:cd17638 287 RPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
81-295 |
1.05e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAVAQRQPERLALV-----DASSGICW---TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLA 152
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAvpggrGADGKLAYdelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 153 KAGVVAALLNVNLRREPLAFCLGTSAAKALIygGEMAAAVAEVSEQLGKSLLKF---CSGDLGPESVLPDTQLLDPMLAE 229
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI--GIPKAHLARRLFGWGKPSVRRlvtVGGRLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 230 APTTPLAQapgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHsYSMRANDVLYDCLPLY 295
Cdd:PRK09274 166 FPMADLAP------DDMAAILFTSGSTGTPKGVVYTHGMFEAqIEALRED-YGIEPGEIDLPTFPLF 225
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-617 |
1.46e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 64 LIRVRLELRRHRRAGDTIPRIFQAVAQRQPERLALVdaSSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPE 143
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 144 FVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAavaevseqlgksLLKFCSGdlgpESVLPDTQLL 223
Cdd:PRK12467 575 MVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA------------QLPVPAG----LRSLCLDEPA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 224 DPMLAEAP-TTPLAQAPgkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNI 301
Cdd:PRK12467 639 DLLCGYSGhNPEVALDP-----DNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 302 MGVGQcIIYGLTVVLRKK---FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRPAI---WE 375
Cdd:PRK12467 714 ELFGA-LASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLlarVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 376 EFtqRFGVRQIgEFYGATEcncsiANMDGKVGSCGFNSRILTHVyPIRlvkvnedtmEPLRDSqGLCI------PCQPGE 449
Cdd:PRK12467 793 AL--GPGARLI-NHYGPTE-----TTVGVSTYELSDEERDFGNV-PIG---------QPLANL-GLYIldhylnPVPVGV 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 450 PG-LLVGqinqQDPLRRfdGYVSDSA-TNKKIAHSVF-RKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTE 526
Cdd:PRK12467 854 VGeLYIG----GAGLAR--GYHRRPAlTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGE 927
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 527 VEAvlsRLLGQTDV--AVYgVAVPGVEGK--------AGMAAIADPHNQLDpnSMYQELQKVLASYAQPIFLRLLPQVDT 596
Cdd:PRK12467 928 IEA---RLLAQPGVreAVV-LAQPGDAGLqlvaylvpAAVADGAEHQATRD--ELKAQLRQVLPDYMVPAHLLLLDSLPL 1001
|
570 580
....*....|....*....|..
gi 564388681 597 TGTFKIQKTRL-QREGFDPRQT 617
Cdd:PRK12467 1002 TPNGKLDRKALpKPDASAVQAT 1023
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
89-316 |
3.63e-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: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALV----DASSGICWTFAQLDTYSNAVANLFLQLGfAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALL--- 161
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 162 --NVNLRRepLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKsllkfcsgdlgpesvLPDTQLLDPMLAEAPTTPLAQAP 239
Cdd:cd05931 82 tpGRHAER--LAAILADAGPRVVLTTAAALAAVRAFAASRPA---------------AGTPRLLVVDLLPDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 240 GKGMDDRLFYIYTSGTTGLPKAAIVVHsryyriAAFGH------HSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLT 313
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
...
gi 564388681 314 VVL 316
Cdd:cd05931 219 SVL 221
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
72-607 |
4.04e-14 |
|
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: 75.06 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 72 RRHRRAGDTIPRIFQAV----AQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGL 147
Cdd:cd05920 4 RRYRAAGYWQDEPLGDLlarsAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 148 WLGLAKAGVVAAL-LNVNLRREPLAFClGTSAAKALIyggemaaavaeVSEQLGksllKFCSGDLGPEsvlpdtqlldpM 226
Cdd:cd05920 82 FFALLRLGAVPVLaLPSHRRSELSAFC-AHAEAVAYI-----------VPDRHA----GFDHRALARE-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 227 LAEAPTTPLAQAPGkgmddrlfyiytsGTTGLPKAAIVVHSRYyriaafghhSYSMRAN--------DVLYDC-LPLYH- 296
Cdd:cd05920 135 AESIPEVALFLLSG-------------GTTGTPKLIPRTHNDY---------AYNVRASaevcgldqDTVYLAvLPAAHn 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 297 ---SAGNIMGVgqcIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVERR------HHVRLAVGN 367
Cdd:cd05920 193 fplACPGVLGT---LLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPA----LVSLWLDAAASRradlssLRLLQVGGA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 368 GLRPAIWEEFTQRFGVrQIGEFYGATE---CNCSIANMDGKVgsCGFNSRILTHVYPIRLVkvnedtmeplrDSQGLCIP 444
Cdd:cd05920 266 RLSPALARRVPPVLGC-TLQQVFGMAEgllNYTRLDDPDEVI--IHTQGRPMSPDDEIRVV-----------DEEGNPVP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 445 cqPGEPGLLvgqinqqdpLRR----FDGYVSDSATNKKiahsVFRKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 520
Cdd:cd05920 332 --PGEEGEL---------LTRgpytIRGYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGE 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 521 NVSTTEVEAVLSRLLGQTDVAVygVAVPG-VEGKAGMAAIADPHNQLDPNSMYQEL-QKVLASYAQPIFLRLLPQVDTTG 598
Cdd:cd05920 396 KIAAEEVENLLLRHPAVHDAAV--VAMPDeLLGERSCAFVVLRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTA 473
|
....*....
gi 564388681 599 TFKIQKTRL 607
Cdd:cd05920 474 VGKIDKKAL 482
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
83-607 |
5.28e-14 |
|
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: 74.51 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 83 RIFQAVAQRQPERLALVDasSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN 162
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 163 VNLRREPLAFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttplaqapgKG 242
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILL---------------------------------------------------------TN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 243 MDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAND--VLYDCLPLYHSAGNIMgvgQCIIYGLTVVL---R 317
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALHVvpsE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLR---QPVRdverrhhVRLAVGNGLRPAIWEEFtqrfgvrQIGEFYGATE 394
Cdd:cd17645 180 RRLDLDALNDYFNQEGITISFLPTGAAEQFMQldnQSLR-------VLLTGGDKLKKIERKGY-------KLVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CN--CSIANMDGKVGSCGFNSRILThvypIRLVKVNED-TMEPLRDSQGLCIPcqpGEpGLLVGQINQQDplrrfdgyvs 471
Cdd:cd17645 246 NTvvATSFEIDKPYANIPIGKPIDN----TRVYILDEAlQLQPIGVAGELCIA---GE-GLARGYLNRPE---------- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 472 dsATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVE 551
Cdd:cd17645 308 --LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDAD 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 552 GKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd17645 384 GRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
93-607 |
5.84e-14 |
|
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: 74.43 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd17650 1 PDAIAVSDATRQL--TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALiyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqLLDPmlaeapttplaqapgkgmDDRLFYIYT 252
Cdd:cd17650 79 MLEDSGAKLL---------------------------------------LTQP------------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 253 SGTTGLPKAAIVVHS----------RYYRIAAFGHHSYSMR--ANDVLYDCLPLYHSAGnimgvGQCIIygltVVLRKKF 320
Cdd:cd17650 102 SGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRLLQMAsfSFDVFAGDFARSLLNG-----GTLVI----CPDEVKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 321 SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVR-LAVGNGLRPAIW-EEFTQRFGVR-QIGEFYGATEcnc 397
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFGQGmRIINSYGVTE--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 398 siANMDGKVGSCGFNSRILTHVYPI-------RLVKVNE-DTMEPLRDSQGLCIpcqpGEPGLLVGQINQQDplrrfdgy 469
Cdd:cd17650 250 --ATIDSTYYEEGRDPLGDSANVPIgrplpntAMYVLDErLQPQPVGVAGELYI----GGAGVARGYLNRPE-------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 470 vsdsATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPG 549
Cdd:cd17650 316 ----LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV--AVRED 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 564388681 550 VEGKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd17650 390 KGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
107-544 |
1.10e-13 |
|
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: 73.78 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygg 186
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 187 emaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlAEAPttplaqapgkgmDDRLFYIYTSGTTGLPKAAIVVH 266
Cdd:cd05907 83 -----------------------------------------VEDP------------DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 267 SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVV-----------LRKK-----FSASRFWDdcv 330
Cdd:cd05907 110 RNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddLSEVrptvfLAVPRVWE--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 331 K-YNCTVVQYIGEICRYLLRQPVRDverrhHVRLAVGNG--LRPAIwEEFTQRFGVrQIGEFYGATECnCSIANM----D 403
Cdd:cd05907 187 KvYAAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGI-PVYEGYGLTET-SAVVTLnppgD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 404 GKVGSCGfnsriltHVYPIRLVKVNEDtmeplrdsqglcipcqpGEpgLLV-GQINqqdplrrFDGYVSDSATNKKIAhs 482
Cdd:cd05907 259 NRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV-------MLGYYKNPEATAEAL-- 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388681 483 vfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEAVL--SRLLGQtdVAVYG 544
Cdd:cd05907 304 ---DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLISQ--AVVIG 363
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
124-610 |
1.12e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 74.06 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 124 LQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREplafclgtSAAKALiyggEMAAAVAEVSEQLGKS- 202
Cdd:PLN02860 50 LRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFE--------EAKSAM----LLVRPVMLVTDETCSSw 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 203 ----------------LLKFCSGDLGPE--SVLPDTQLLDPMLAEaPTTPLAQAPgkgmDDRLFYIYTSGTTGLPKAAIV 264
Cdd:PLN02860 118 yeelqndrlpslmwqvFLESPSSSVFIFlnSFLTTEMLKQRALGT-TELDYAWAP----DDAVLICFTSGTTGRPKGVTI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 265 VHSRYY-----RIAAFGHHSysmraNDVLYDCLPLYH-----SAGNIMGVGQCiiygltVVLRKKFSASRFWD----DCV 330
Cdd:PLN02860 193 SHSALIvqslaKIAIVGYGE-----DDVYLHTAPLCHigglsSALAMLMVGAC------HVLLPKFDAKAALQaikqHNV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 331 KYNCTVVQYIGEICRYLLRQPVRDVerRHHVR--LAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCSIANMDGKVGS 408
Cdd:PLN02860 262 TSMITVPAMMADLISLTRKSMTWKV--FPSVRkiLNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 409 CGFNSRILTHVYPIRLVKVNEdtmeplrdSQGLCI----P------CQPGEPGllVGQINQQDP---LRRFDGYVSDSAT 475
Cdd:PLN02860 340 LESPKQTLQTVNQTKSSSVHQ--------PQGVCVgkpaPhvelkiGLDESSR--VGRILTRGPhvmLGYWGQNSETASV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 476 nkkiahsvfRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV--------AV 547
Cdd:PLN02860 410 ---------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVpdsrltemVV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 548 PGVEGKAGMA-AIADPHNQLDPNSMYQEL------QKVLASYAQP-IFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:PLN02860 481 ACVRLRDGWIwSDNEKENAKKNLTLSSETlrhhcrEKNLSRFKIPkLFVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
93-585 |
1.86e-13 |
|
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: 73.33 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIYGGEMAAAVAEVseqlgKSLLKFCSG--------DLGPESVLPD--TQLLDPMLAEAPTTPlaqaPGKG 242
Cdd:cd17642 111 SLNISKPTIVFCSKKGLQKVLNV-----QKKLKIIKTiiildskeDYKGYQCLYTfiTQNLPPGFNEYDFKP----PSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 243 MDDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRANDVLYD-----CLPLYHSAGNIMGVGQCIIyGLTVVL 316
Cdd:cd17642 182 RDEQVALImNSSGSTGLPKGVQLTHKNI--VARFSHARDPIFGNQIIPDtailtVIPFHHGFGMFTTLGYLIC-GFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 317 RKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD-VERRHHVRLAVGNG-LRPAIWEEFTQRFGVRQIGEFYGATE 394
Cdd:cd17642 259 MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSI---ANMDGKVGSCGfnsriltHVYPIRLVKVnedtMEPlrDSQGLCIPCQPGE-----PGLLVGQINQQDplrrf 466
Cdd:cd17642 339 TTSAIlitPEGDDKPGAVG-------KVVPFFYAKV----VDL--DTGKTLGPNERGElcvkgPMIMKGYVNNPE----- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 467 dgyvsdsATNKKIAHsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVA 546
Cdd:cd17642 401 -------ATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIP 467
|
490 500 510
....*....|....*....|....*....|....*....
gi 564388681 547 VPgVEGKAGMAAIADPHNQldpNSMYQELQKVLASYAQP 585
Cdd:cd17642 468 DE-DAGELPAAVVVLEAGK---TMTEKEVMDYVASQVST 502
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
72-548 |
2.03e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 72 RRHRRAGDTIPRIFQAVAQRQPERLALVDaSSGICWTFAQLDTYSNAVANLFLQLgFAPGDVVAVFLegrPEFVG---LW 148
Cdd:PRK08633 608 KSRKEALPPLAEAWIDTAKRNWSRLAVAD-STGGELSYGKALTGALALARLLKRE-LKDEENVGILL---PPSVAgalAN 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 149 LGLAKAGVVAALLNVNLRREPLAFCLG--------TS-------AAKALIYGGEMAAAV---AEVSEQLGKsLLKFCSgd 210
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEqaqiktviTSrkfleklKNKGFDLELPENVKViylEDLKAKISK-VDKLTA-- 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 211 LGPESVLPdTQLLDPMLAeapttplaqaPGKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRIAA--------FGhhsysM 282
Cdd:PRK08633 760 LLAARLLP-ARLLKRLYG----------PTFKPDDTATIIFSSGSEGEPKGVMLSH---HNILSnieqisdvFN-----L 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 283 RANDVLYDCLPLYHSagnimgvgqciiYGLTV----VLRKKFSASRFWDD---------CVKYNCTVVQYIGEICRYLLR 349
Cdd:PRK08633 821 RNDDVILSSLPFFHS------------FGLTVtlwlPLLEGIKVVYHPDPtdalgiaklVAKHRATILLGTPTFLRLYLR 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 350 QPVRDVERRHHVRLAVGNG--LRPAIWEEFTQRFGVRqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsr 414
Cdd:PRK08633 889 NKKLHPLMFASLRLVVAGAekLKPEVADAFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG---- 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 415 iltHVYPIRLVK-VNEDTMEPLrdsqglcipcQPGEPGL-LVGQINqqdplrRFDGYVSDSA-TNKKIAHSvfrKGDSAY 491
Cdd:PRK08633 964 ---MPLPGVAVRiVDPETFEEL----------PPGEDGLiLIGGPQ------VMKGYLGDPEkTAEVIKDI---DGIGWY 1021
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 492 LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 548
Cdd:PRK08633 1022 VTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
244-533 |
2.65e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 71.74 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVL------R 317
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 318 KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPV-RDVERrhhVRLAVGNG--LRPAIWEEFTQRFGVrQIGEFYGATE 394
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVnADISS---LRFAMSGAapLPVELRARFEDATGL-PVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 395 CNCSIA----NMDGKVGSCGfnsriLTHVYPIRLVKVNEDTMEPLRDsqglcipCQPGEpgllVGQINQQDPlRRFDGYV 470
Cdd:cd05944 158 ATCLVAvnppDGPKRPGSVG-----LRLPYARVRIKVLDGVGRLLRD-------CAPDE----VGEICVAGP-GVFGGYL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 471 -SDSATNKKIAHSVFRKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSR 533
Cdd:cd05944 221 yTEGNKNAFVADGWLNTGDLGRL-------DADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
245-609 |
3.50e-13 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 70.82 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAaiVVHSRYYRIAAF--GHHSYSMRANDVLYDCLPLYHSAGnIMGVGQCIIYGLTVVLRKKFSA 322
Cdd:cd17630 1 RLATVILTSGSTGTPKA--VVHTAANLLASAagLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 323 SRfwDDCVKYNCTVVQYIGEICRYLL--RQPVRDVERRHHVRLAVGnglrpAIWEEFTQRFGVRQIGEF--YGATEcncs 398
Cdd:cd17630 78 LA--EDLAPPGVTHVSLVPTQLQRLLdsGQGPAALKSLRAVLLGGA-----PIPPELLERAADRGIPLYttYGMTE---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 399 ianMDGKVGSCGFNSRILTHVYPI---RLVKVNEDTMeplrdsqglcipCQPGEPGLLVGQINQQDPLRRFDGyvsdsat 475
Cdd:cd17630 147 ---TASQVATKRPDGFGRGGVGVLlpgRELRIVEDGE------------IWVGGASLAMGYLRGQLVPEFNED------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 476 nkkiahSVFRKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKAG 555
Cdd:cd17630 205 ------GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELG 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 564388681 556 MAAIA--DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQR 609
Cdd:cd17630 268 QRPVAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
80-608 |
4.51e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 71.73 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPgDVVAVFLEGRPEFVGLWLGLAKAGVVAA 159
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVL--TYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 LLNVNLRREPLAFCLGTSAAKALIyggemaaavaevseqlgksLLKFCSGDLGPEsvlpDTQLLD-----PMLAEAPTTP 234
Cdd:PRK07638 79 PLDIKWKQDELKERLAISNADMIV-------------------TERYKLNDLPDE----EGRVIEidewkRMIEKYLPTY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 235 laqAPGKGMDDRLFYI-YTSGTTGLPKAAIVVHSRYyrIAAF--GHHSYSMRANDVLYDCLPLYHSAgNIMGVGQCIIYG 311
Cdd:PRK07638 136 ---APIENVQNAPFYMgFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLRKKFSASRFWDDCVKYNCTVVQYIGEicryLLRQPVRDVERRHHVRLAVGNGlrpAIW-----EEFTQRFGVRQI 386
Cdd:PRK07638 210 QTVHLMRKFIPNQVLDKLETENISVMYTVPT----MLESLYKENRVIENKMKIISSG---AKWeaeakEKIKNIFPYAKL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEFYGATECNCSIANMDG----KVGSCGfnsrilTHVYPIRLVKVNEDTMEplrdsqglcipCQPGEpgllVGQINQQDP 462
Cdd:PRK07638 283 YEFYGASELSFVTALVDEeserRPNSVG------RPFHNVQVRICNEAGEE-----------VQKGE----IGTVYVKSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 463 LRrFDGYVSDSATNKKIAhsvfrkgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVA 541
Cdd:PRK07638 342 QF-FMGYIIGGVLARELN-------ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 542 VYGVAVPgvegKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQ 608
Cdd:PRK07638 414 VIGVPDS----YWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
89-610 |
5.26e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.90 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICWtfaqLDTYSNA--VANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLR 166
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTW----AETYARCrrLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 167 REPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLkFCSGDLGPEsvLPDTQLL-----DPMLAEAPTTPLAQAPgk 241
Cdd:PRK08162 104 AASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKP-LVIDVDDPE--YPGGRFIgaldyEAFLASGDPDFAWTLP-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 242 gmDDRLFYI---YTSGTTGLPKaAIVVHSRYYRIAAFGHH-SYSMRANDVLYDCLPLYHSagNimgvGQC------IIYG 311
Cdd:PRK08162 179 --ADEWDAIalnYTSGTTGNPK-GVVYHHRGAYLNALSNIlAWGMPKHPVYLWTLPMFHC--N----GWCfpwtvaARAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLRkKFSASRFWDDCVKYNCT------VVQYIgeicryLLRQPVRDVE-RRHHVRLAVGNGLRPAIWEEFTQRFGVR 384
Cdd:PRK08162 250 TNVCLR-KVDPKLIFDLIREHGVThycgapIVLSA------LINAPAEWRAgIDHPVHAMVAGAAPPAAVIAKMEEIGFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 385 qIGEFYGATECNcsianmdGKVGSC---------------GFNSRilTHV-YPIR--LVKVNEDTMEPL-RDSQGLcipc 445
Cdd:PRK08162 323 -LTHVYGLTETY-------GPATVCawqpewdalplderaQLKAR--QGVrYPLQegVTVLDPDTMQPVpADGETI---- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 446 qpGE---PGLLVgqinqqdplrrFDGYVSdsatNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 522
Cdd:PRK08162 389 --GEimfRGNIV-----------MKGYLK----NPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 523 STTEVEAVLSRLLGQTDVAVygVAVPG----------VEGKAGMAAIADphnqldpnsmyqEL----QKVLASYAQP--I 586
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAV--VAKPDpkwgevpcafVELKDGASATEE------------EIiahcREHLAGFKVPkaV 515
|
570 580
....*....|....*....|....
gi 564388681 587 FLRLLPQvdtTGTFKIQKTRLQRE 610
Cdd:PRK08162 516 VFGELPK---TSTGKIQKFVLREQ 536
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
79-316 |
9.54e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 79 DTIPRIFQAVAQRQPERLALV----DASSGICWTFAQLDTYSNAVANLfLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRfladDPGEGVVLSYRDLDLRARTIAAA-LQARASFGDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVAA---------------LLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkfcsgdlgPESVLPD 219
Cdd:PRK05691 88 GVIAVpayppesarrhhqerLLSIIADAEPRLLLTVADLRDSLLQMEELAAANA-------------------PELLCVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 220 TqlLDPMLAEApttplAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAN--DVLYDCLPLYHS 297
Cdd:PRK05691 149 T--LDPALAEA-----WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHD 221
|
250
....*....|....*....
gi 564388681 298 AGNIMGVGQCIIYGLTVVL 316
Cdd:PRK05691 222 MGLIGGLLQPIFSGVPCVL 240
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
126-586 |
2.27e-12 |
|
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: 69.80 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 126 LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYG-----GEMAAAVAEvseqlg 200
Cdd:cd05932 26 LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGklddwKAMAPGVPE------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 201 ksllKFCSGDLGPESVLPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSY 280
Cdd:cd05932 100 ----GLISISLPPPSAANCQYQWDDLIAQHP--PLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 281 SMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTV------------VLRKK----FSASRFWddcVKYNCTVVQYIG-EI 343
Cdd:cd05932 174 GTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRLW---TKFQQGVQDKIPqQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 344 CRYLLRQPV--RDVERR-------HHVRLAVGNG--LRPAIWEEFtQRFGVrQIGEFYGATEcNCSIANM----DGKVGS 408
Cdd:cd05932 251 LNLLLKIPVvnSLVKRKvlkglglDQCRLAGCGSapVPPALLEWY-RSLGL-NILEAYGMTE-NFAYSHLnypgRDKIGT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 409 CGFNsrilthvYPIRLVKVNEDTmEPLRDSqglcipcqpgePGLLVGQinqqdplrrfdgYVSDSATNkkiahSVFRKgD 488
Cdd:cd05932 328 VGNA-------GPGVEVRISEDG-EILVRS-----------PALMMGY------------YKDPEATA-----EAFTA-D 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 489 SAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEavlsRLLGQTDvAVYGVAVPGvEGKAGMAAIADPHNQLD 567
Cdd:cd05932 371 GFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIE----NKLAEHD-RVEMVCVIG-SGLPAPLALVVLSEEAR 444
|
490
....*....|....*....
gi 564388681 568 PNSMYQELQKVLASYAQPI 586
Cdd:cd05932 445 LRADAFARAELEASLRAHL 463
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
50-607 |
5.87e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 68.48 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 50 VCKTARRDLFGLSVLI----RVRLELRRHRRAGDTIPRIFQAV-AQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFL 124
Cdd:PRK13383 1 VAPTAARALVRSGLLNppspRAVLRLLREASRGGTNPYTLLAVtAARWPGRTAIIDDDGAL--SYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 125 QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksll 204
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGAD-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 205 kfcsgdlgpESVLpdtqLLDPMLA---EAPTTPLAQAPGKgmddrlFYIYTSGTTGLPKAaivVHSRYYRIAAFG----- 276
Cdd:PRK13383 151 ---------DAVA----VIDPATAgaeESGGRPAVAAPGR------IVLLTSGTTGKPKG---VPRAPQLRSAVGvwvti 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 277 HHSYSMRANDVLYDCLPLYHSAGNIMGVgQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRdVE 356
Cdd:PRK13383 209 LDRTRLRTGSRISVAMPMFHGLGLGMLM-LTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPR-VR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 357 RRH-----HVRLAVGNGLRPAIWEEFTQRFGvRQIGEFYGATECN----CSIANMD------GK-VGSCgfnsrilthvy 420
Cdd:PRK13383 287 ARNplpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGigalATPADLRdapetvGKpVAGC----------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 421 PIRLVKVNEDtmeplrdsqglciPCQPGEPGLLV--GQINQqdplrrfDGYVSDSAtnKKIAHSVFRKGDSAYLsgdvlv 498
Cdd:PRK13383 355 PVRILDRNNR-------------PVGPRVTGRIFvgGELAG-------TRYTDGGG--KAVVDGMTSTGDMGYL------ 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 499 mDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAGMAAIADPHNQLDPNSMYQELQKV 578
Cdd:PRK13383 407 -DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR 485
|
570 580
....*....|....*....|....*....
gi 564388681 579 LASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:PRK13383 486 VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
93-607 |
8.03e-12 |
|
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: 67.72 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvAALLNVNLR--REPL 170
Cdd:cd17643 1 PEAVAVVDEDRRL--TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAypVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 171 AFCLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapTTPlaqapgkgmDDRLFYI 250
Cdd:cd17643 77 AFILADSGPSLLL------------------------------------------------TDP---------DDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 251 YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYdclpLYHSAG------NIMGVgqcIIYGLTVVLRKKF---S 321
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 322 ASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVR--QIGEFYGATEcnc 397
Cdd:cd17643 173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDrpQLVNMYGITE--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 398 sianmdgkvgscgfnSRILTHVYPIRLVKVNEDTMEP-----------LRDSQGLCIPcqPGEPGLLV--------GQIN 458
Cdd:cd17643 250 ---------------TTVHVTFRPLDAADLPAAAASPigrplpglrvyVLDADGRPVP--PGVVGELYvsgagvarGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 459 QQD-PLRRFdgyVSDSATNkkiahsvfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQ 537
Cdd:cd17643 313 RPElTAERF---VANPFGG---------PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSV 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564388681 538 TDVAVygVAVPGVEGKAGMAA--IADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd17643 381 RDAAV--IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-531 |
1.39e-11 |
|
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: 66.82 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaallnvnlrreplafclgtsaakaliygge 187
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 maaavaevseqlgksllkfcsgdlgpesVLPDTQLLDP-----MLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKaa 262
Cdd:cd05974 52 ----------------------------VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 263 IVVHSryYRIAAFGHHS----YSMRANDVLYDClplyHSAGNIMGVGQCII----YGLTVVL--RKKFSASRFWDDCVKY 332
Cdd:cd05974 102 LVEHT--HRSYPVGHLStmywIGLKPGDVHWNI----SSPGWAKHAWSCFFapwnAGATVFLfnYARFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 333 NCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRPAIWEEFTQRFGvRQIGEFYGATECNCSIANMDGKVGSCGFN 412
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTALVGNSPGQPVKAGSM 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 413 SRILTHvYPIRLVkvnedtmeplrDSQGLciPCQPGEPGLLVGQINqqdPLRRFDGYVSDSAtnkKIAHSVfrkGDSAYL 492
Cdd:cd05974 255 GRPLPG-YRVALL-----------DPDGA--PATEGEVALDLGDTR---PVGLMKGYAGDPD---KTAHAM---RGGYYR 311
|
410 420 430
....*....|....*....|....*....|....*....
gi 564388681 493 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVL 531
Cdd:cd05974 312 TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-615 |
1.52e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.27 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 77 AGDTIPRIFQAVAQRQPERLALVdaSSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEF-VGLwLGLAKAG 155
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 156 VVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSeqlgksllkfcsgdlGPESVLPDTQLLDPMLAEAPTTPL 235
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE---------------GVSAIALDSLHLDSWPSQAPGLHL 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 236 AqapgkgmDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSagniMGVGQC---IIYG 311
Cdd:PRK05691 1271 H-------GDNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD----VSVWECfwpLITG 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 312 LTVVLR---KKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPvrDVERRHHVRLAV--GNGLRPAIWEEFTQRFGVRQI 386
Cdd:PRK05691 1340 CRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP--LAAACTSLRRLFsgGEALPAELRNRVLQRLPQVQL 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 GEFYGATEC-------NCSIAnmDGKVGSCGfnsRILTHVypirLVKVNEDTMEPLrdsqglcipcQPGEPG-LLVGQIN 458
Cdd:PRK05691 1418 HNRYGPTETainvthwQCQAE--DGERSPIG---RPLGNV----LCRVLDAELNLL----------PPGVAGeLCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 459 qqdpLRRfdGYVSDSATNKK--IAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAvlsRLLG 536
Cdd:PRK05691 1479 ----LAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQA---RLLA 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 537 QTDVAVYGVAVPgvEGKAGMAAI----ADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL----- 607
Cdd:PRK05691 1550 QPGVAQAAVLVR--EGAAGAQLVgyytGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepvw 1627
|
....*....
gi 564388681 608 -QREGFDPR 615
Cdd:PRK05691 1628 qQREHVEPR 1636
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
81-607 |
1.56e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 67.34 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAvAQRQPERLAL--VDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVA 158
Cdd:PRK05857 17 LDRVFEQ-ARQQPEAIALrrCDGTSAL--RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 159 ALLNVNLRREPLA-FCLGTSAAKALIY-GGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLdpmlaeapttplA 236
Cdd:PRK05857 94 VMADGNLPIAAIErFCQITDPAAALVApGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASL------------A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 237 QAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIA----AFGHHSYSMRANDVLYDCLPLYHSAG------NIMGVGQ 306
Cdd:PRK05857 162 GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPdilqKEGLNWVTWVVGETTYSPLPATHIGGlwwiltCLMHGGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 307 CIIYG-LTVVLRKKFSASRfwddcVKYNCTVVQYIGEICrYLLRQPVRDVERrhhVRLAVGNGLRpAIWEE--FTQRFGV 383
Cdd:PRK05857 242 CVTGGeNTTSLLEILTTNA-----VATTCLVPTLLSKLV-SELKSANATVPS---LRLVGYGGSR-AIAADvrFIEATGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 384 RQiGEFYGATECNCSIANMDGKVGSCgfnSRI----LTHVYPirLVKVNedtmepLRDSQGLCIPCQPGEPGLLVGQINQ 459
Cdd:PRK05857 312 RT-AQVYGLSETGCTALCLPTDDGSI---VKIeagaVGRPYP--GVDVY------LAATDGIGPTAPGAGPSASFGTLWI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 460 QDPLRRFdGYVSDSATNKKIAhsvfrkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTD 539
Cdd:PRK05857 380 KSPANML-GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVRE 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388681 540 VAVYGVAVPGVEGKAGMAAIadPHNQLDPNSMYQELQKVLASY-------AQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:PRK05857 453 AACYEIPDEEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
93-607 |
2.48e-11 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 66.24 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPE-FVGLwLGLAKAGVVAALLNVNLRREPLA 171
Cdd:cd17649 1 PDAVALVFG--DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 172 FCLGTSAAKALiyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttpLAQAPgkgmdDRLFY-I 250
Cdd:cd17649 78 YMLEDSGAGLL----------------------------------------------------LTHHP-----RQLAYvI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 251 YTSGTTGLPKAAIVVHsryyriAAFGHHS------YSMRANDVLYDCLPLYHSAGnIMGVGQCIIYGLTVVLRKK---FS 321
Cdd:cd17649 101 YTSGSTGTPKGVAVSH------GPLAAHCqataerYGLTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLRPDelwAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 322 ASRFWDDCVKYNCTVVQ----YIGEICRYLLRQPVRdveRRHHVRLAV--GNGLRPAIWEEfTQRFGVRQIGEfYGATEC 395
Cdd:cd17649 174 ADELAEMVRELGVTVLDlppaYLQQLAEEADRTGDG---RPPSLRLYIfgGEALSPELLRR-WLKAPVRLFNA-YGPTEA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 NCSIANMDGKVG-SCGFNSRILTHVYPIRLVKVNEdtmEPLRdsqglciPCQPGEPG-LLVGqinqQDPLRRfdGYVSDS 473
Cdd:cd17649 249 TVTPLVWKCEAGaARAGASMPIGRPLGGRSAYILD---ADLN-------PVPVGVTGeLYIG----GEGLAR--GYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 474 ATNKK--IAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVAVPGVE 551
Cdd:cd17649 313 ELTAErfVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV--VALDGAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 552 GK---AGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd17649 391 GKqlvAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
93-548 |
2.64e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 66.58 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGICWTfaqlDTYSNA--VANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 170
Cdd:PLN03102 28 PNRTSIIYGKTRFTWP----QTYDRCcrLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 171 AFCLGTSAAKALIYGGEMAAAVAEVSeqlgkSLLKFCSGDLGPESVL---------PDTQLLD--PMLAEAPTTPLAQAp 239
Cdd:PLN03102 104 AAILRHAKPKILFVDRSFEPLAREVL-----HLLSSEDSNLNLPVIFiheidfpkrPSSEELDyeCLIQRGEPTPSLVA- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 240 gkgmddRLFYI----------YTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCII 309
Cdd:PLN03102 178 ------RMFRIqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 310 YGLTVVLRkKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHH-VRLAVGNGLRPAIWEEFTQRFGVrQIGE 388
Cdd:PLN03102 252 GGTSVCMR-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGSPPPAALVKKVQRLGF-QVMH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 389 FYGATECNcsianmdGKVGSCGFNSrilthvypiRLVKVNEDTMEPLRDSQGLCI-----------PCQPGEP--GLLVG 455
Cdd:PLN03102 330 AYGLTEAT-------GPVLFCEWQD---------EWNRLPENQQMELKARQGVSIlgladvdvknkETQESVPrdGKTMG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 456 QINQQDPLrRFDGYVSdsatNKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRL 534
Cdd:PLN03102 394 EIVIKGSS-IMKGYLK----NPKATSEAFKHG---WLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY 465
|
490
....*....|....
gi 564388681 535 LGQTDVAVygVAVP 548
Cdd:PLN03102 466 PKVLETAV--VAMP 477
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
93-267 |
4.45e-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: 65.39 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDasSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIYGGEMAAAvaevseqlgksllkfcsgdlgpesvLPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFY-IY 251
Cdd:cd12116 79 ILEDAEPALVLTDDALPDR-------------------------LPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYvIY 133
|
170
....*....|....*.
gi 564388681 252 TSGTTGLPKAAIVVHS 267
Cdd:cd12116 134 TSGSTGRPKGVVVSHR 149
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
84-545 |
5.10e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 65.46 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRQPERLALVDAssGICWTFAQLDTYSNAVAnLFLQ--LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAalL 161
Cdd:PRK08974 28 MFEQAVARYADQPAFINM--GEVMTFRKLEERSRAFA-AYLQngLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV--V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 162 NVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVSEQ----------LGKSL-----------LKFCSGdLGPESVLP 218
Cdd:PRK08974 103 NVNPLYTPreLEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkhviltrMGDQLstakgtlvnfvVKYIKR-LVPKYHLP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 219 DtqlldpmlaeAPTTPLAQAPGKGM---------DDRLFYIYTSGTTGLPKAAIVVHSRYyrIA----AFGHHSYSMR-A 284
Cdd:PRK08974 182 D----------AISFRSALHKGRRMqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNM--LAnleqAKAAYGPLLHpG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 285 NDVLYDCLPLYHsagnimgvgqciIYGLTVvlrkkfsasrfwddcvkyNCTVVQYIGeICRYLLRQPvRDVE------RR 358
Cdd:PRK08974 250 KELVVTALPLYH------------IFALTV------------------NCLLFIELG-GQNLLITNP-RDIPgfvkelKK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 359 H---------------------------HVRLAVGNGL--RPAI---WEEFTqrfGVRQIgEFYGATECN----CSIANM 402
Cdd:PRK08974 298 YpftaitgvntlfnallnneefqeldfsSLKLSVGGGMavQQAVaerWVKLT---GQYLL-EGYGLTECSplvsVNPYDL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 403 DGKVGSCGFnsrilthvyPIrlvkvnEDTMEPLRDSQGLCIPcqPGEPGLLVG---QINQ---QDPlrrfdgyvsdSATN 476
Cdd:PRK08974 374 DYYSGSIGL---------PV------PSTEIKLVDDDGNEVP--PGEPGELWVkgpQVMLgywQRP----------EATD 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 477 KkiahsVFRKGdsaYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK08974 427 E-----VIKDG---WLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
89-607 |
5.78e-11 |
|
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: 64.96 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNvnlrre 168
Cdd:cd05945 1 AAANPDRPAVVEG--GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 plafclGTSAAkaliyggEMAAAVAEVSeqlgksllkfcsgdlGPESVLPDtqlldpmlaeapttplaqapgkgmDDRLF 248
Cdd:cd05945 73 ------ASSPA-------ERIREILDAA---------------KPALLIAD------------------------GDDNA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YI-YTSGTTGLPKAaiVVHSrYYRIAAFGHHS---YSMRANDVLYdCLPLYHSAGNIMGVGQCIIYGLTVV-LRKKFSAS 323
Cdd:cd05945 101 YIiFTSGSTGRPKG--VQIS-HDNLVSFTNWMlsdFPLGPGDVFL-NQAPFSFDLSVMDLYPALASGATLVpVPRDATAD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 324 --RFWDDCVKYNCTV---VQYIGEICrylLRQPVRDVERRHHVRLAVGNGlrpaiwEEFT--------QRFGVRQIGEFY 390
Cdd:cd05945 177 pkQLFRFLAEHGITVwvsTPSFAAMC---LLSPTFTPESLPSLRHFLFCG------EVLPhktaralqQRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 391 GATECN--CSIANMDGKVgsCGFNSRIlthvyPIRLVKVNEDTMepLRDSQGLCIPcqPGEPG--LLVGQinqqdplRRF 466
Cdd:cd05945 248 GPTEATvaVTYIEVTPEV--LDGYDRL-----PIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP-------SVS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 467 DGYVSDSATNKKIAHSVfrKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVygVA 546
Cdd:cd05945 310 KGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VP 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388681 547 VPGVEGKAGMAAIADPH---NQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRL 607
Cdd:cd05945 386 KYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-592 |
7.06e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 83 RIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLN 162
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGEQRL--SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 163 VNLRREPLAFCLGTSAAKALiyggemaaavaevseqLGKSLLKfcsgdlgpesvLPDTQLLDPMLAEAPTTPLAQA--PG 240
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLL----------------LSQSHLR-----------LPLAQGVQVLDLDRGDENYAEAnpAI 3191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 241 KGMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLydclpLYHSAGNIMGVGQCIIYGLTVVLRKK 319
Cdd:PRK12316 3192 RTMPENLAYvIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-----LQFTTFSFDVFVEELFWPLMSGARVV 3266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 320 FSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVE----RRHHVRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATEC 395
Cdd:PRK12316 3267 LAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEeedaHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEA 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 396 NCSIANMDgkVGSCGFNSRILTHVYPIRLVKVNEDTMEPlrDSQGLCIPCQPGEPGLLVGQINQQDplrrfdgyvsdsAT 475
Cdd:PRK12316 3347 TITVTHWQ--CVEEGKDAVPIGRPIANRACYILDGSLEP--VPVGALGELYLGGEGLARGYHNRPG------------LT 3410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 476 NKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgQTDVAVYGVAVPGVEGKAG 555
Cdd:PRK12316 3411 AERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL-----LEHPWVREAVVLAVDGRQL 3485
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564388681 556 MAAIADPHNQLD-PNSMYQELQKVLASY---AQPIFLRLLP 592
Cdd:PRK12316 3486 VAYVVPEDEAGDlREALKAHLKASLPEYmvpAHLLFLERMP 3526
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-286 |
1.17e-10 |
|
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: 64.10 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRQPERLAlVDASSGiCWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNV 163
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 164 NLrrePLAFclgtsaakaliyggemaaaVAEVSEQLGKSLlkfcsgdlgpesvlpdtqlldpMLAEAPttplaqapgkgm 243
Cdd:cd05918 82 SH---PLQR-------------------LQEILQDTGAKV----------------------VLTSSP------------ 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRAND 286
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGRALGLTS 146
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
86-267 |
1.18e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 64.43 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 86 QAVAQRQPERLALVDAS-SGI--CWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPE-FVGLwlgLAKA------- 154
Cdd:PRK03584 91 NLLRHRRDDRPAIIFRGeDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPEtVVAM---LATAslgaiws 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 ------GVVAALlnvnlRReplafcLGTSAAKALI------YGG---EMAAAVAEVSEQLgKSLLKFCS----GDLGPES 215
Cdd:PRK03584 168 scspdfGVQGVL-----DR------FGQIEPKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAA 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564388681 216 VLPDTQLLDPMLAEAPTTPLAQAPGkGMDDRLFYIYTSGTTGLPKAaiVVHS 267
Cdd:PRK03584 236 ALPGALLWEDFLAPAEAAELEFEPV-PFDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-544 |
1.71e-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: 63.60 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 94 ERLALVDAS---SGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPL 170
Cdd:cd05915 9 GRKEVVSRLhtgEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 171 AFCLGTSAAKALIYGGEMAAaVAEVSEQLGKSLLKfcsgdlGPESVLPDTQLLDPMLAEAPTTplaqAPGKGMD--DRLF 248
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLP-LVEAIRGELKTVQH------FVVMDEKAPEGYLAYEEALGEE----ADPVRVPerAACG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 YIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHSYSMRANDVLYDC-LPLYHSAgnimgvGQCIIY------GLTVVLRKKF 320
Cdd:cd05915 158 MAYTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPvVPMFHVN------AWCLPYaatlvgAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 321 SASRFWDDCVKYNCTvvQYIGEICRYLLRQPVRDVERRHH---VRLAVGNGLRPAIWEEFtQRFGVRQIGEFYGATEcnc 397
Cdd:cd05915 232 DPASLVELFDGEGVT--FTAGVPTVWLALADYLESTGHRLktlRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 398 sianMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSQGLCIPCQPGEPGllVGQINQQDPLRR---FDGYVSDSA 474
Cdd:cd05915 306 ----TSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEE 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 475 TNKKIAhsvFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYG 544
Cdd:cd05915 380 ATRSAL---TPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
89-287 |
1.95e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 64.30 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDAssGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEgRPEFVGLWL-GLAKAGvvAALLNVNLRR 167
Cdd:PRK10252 468 AAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAIVEAG--AAWLPLDTGY 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 168 --EPLAFCLGTSAAKALIyggemaaavaEVSEQLGKsllkfcsgdlgpesvLPDTQLLDPMLAEAPTTPLAQAPGKGM-- 243
Cdd:PRK10252 543 pdDRLKMMLEDARPSLLI----------TTADQLPR---------------FADVPDLTSLCYNAPLAPQGAAPLQLSqp 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDV 287
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDV 641
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
109-299 |
1.97e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.87 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 109 FAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVnlrrePLAF------------CLGT 176
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL-----PMGFggresyiaqlrgMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 177 SAAKALIYGGEMAAAVAEVSEqlGKSLLKfcsgdlgpesVLPDTQLldpMLAEAPTTPLAQA-PgkgmDDRLFYIYTSGT 255
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATH--GNPLLH----------VLSHAWF---KALPEADVALPRPtP----DDIAYLQYSSGS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564388681 256 TGLPKAAIVVH-SRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAG 299
Cdd:PRK09192 188 TRFPRGVIITHrALMANLRAISHDGLKVRPGDRCVSWLPFYHDMG 232
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
250-548 |
1.22e-09 |
|
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: 60.36 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 250 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGniMGVGQCIIY--GLTVVLRKkFSASRFWD 327
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 328 DCVKYNCTVVQYIGEICRYLLrqpvrDVERRHHVRLAvgnGLR-------PaiweEFTQRFGVRQIGEF---YGATECNC 397
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLL-----DAAEKSGVDLS---SLRhvlgldaP----ETIQRFEETTGATFwslYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 398 --SIANMDGKVGSCGfnsRILthvyPIRLVKVNEDTMEPLRdsqglcipcqPGEPGllvgQINQQDPLRrFDGYVSDSAT 475
Cdd:cd17637 151 lvTLSPYRERPGSAG---RPG----PLVRVRIVDDNDRPVP----------AGETG----EIVVRGPLV-FQGYWNLPEL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564388681 476 NkkiAHSvFRKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVP 548
Cdd:cd17637 209 T---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP 277
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
108-610 |
1.33e-09 |
|
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: 61.11 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 187
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MAAAVAEVSEQL--GKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPttPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVV 265
Cdd:cd12119 107 FLPLLEAIAPRLptVEHVVVMTDDAAMPEPAGVGVLAYEELLAAES--PEYDWPDFDENTAAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 266 HSRYYriaafgHHSYSMRANDVLY----D----CLPLYHsaGNIMGVG-QCIIYGLTVVLRKKF----SASRFWDdcvKY 332
Cdd:cd12119 185 HRSLV------LHAMAALLTDGLGlsesDvvlpVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYldpaSLAELIE---RE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 333 NCTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFTQRfGVRQIgEFYGATE-CNCSIAN-----MDG 404
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER-GVRVI-HAWGMTEtSPLGTVArppseHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 405 KVGSCGFNSRILTHvYPIRLVK---VNEDTMEPLRDSQGLcipcqpGE-----PGLLVGQINQQDPLRRF--DGYvsdsa 474
Cdd:cd12119 332 LSEDEQLALRAKQG-RPVPGVElriVDDDGRELPWDGKAV------GElqvrgPWVTKSYYKNDEESEALteDGW----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 475 tnkkiahsvFRkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPgvegKA 554
Cdd:cd12119 400 ---------LR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP----KW 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388681 555 G---MAAI-ADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKIQKTRLqRE 610
Cdd:cd12119 460 GerpLAVVvLKEGATVTAEELLEFLADKVAKWWLPddvVFVDEIPK---TSTGKIDKKAL-RE 518
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
80-545 |
2.26e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 60.42 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaa 159
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 LLNVNLRREP--LAFCLGTSAAKALIYGGEMAAAVAEVseqLGKSLLKF----CSGD-LG-----------------PES 215
Cdd:PRK07059 100 VVNVNPLYTPreLEHQLKDSGAEAIVVLENFATTVQQV---LAKTAVKHvvvaSMGDlLGfkghivnfvvrrvkkmvPAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 216 VLPDTQLLDPMLAEAPTTPLaQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAAFGHHSYSMRAND--VLY 289
Cdd:PRK07059 177 SLPGHVRFNDALAEGARQTF-KPVKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 290 DC-LPLYH----SAGNIMGVGQCiiyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLA 364
Cdd:PRK07059 256 VCaLPLYHifalTVCGLLGMRTG---GRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 365 VGNGL---RPAI--WEEFTQRFgvrqIGEFYGATECN----CSIANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepL 435
Cdd:PRK07059 333 NGGGMavqRPVAerWLEMTGCP----ITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS------I 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 436 RDSQGLCIPC-QPGE-----PGLLVGQINQQDPLRRF---DGYvsdsatnkkiahsvFRkgdsaylSGDVLVMDELGYMY 506
Cdd:PRK07059 394 RDDDGNDLPLgEPGEicirgPQVMAGYWNRPDETAKVmtaDGF--------------FR-------TGDVGVMDERGYTK 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 564388681 507 FRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGV 545
Cdd:PRK07059 453 IVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
93-274 |
6.31e-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: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 93 PERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAF 172
Cdd:cd17652 1 PDAPAVVFGDETL--TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 173 CLGTSAAKALIyggemaaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapTTPlaqapgkgmdDRLFY-IY 251
Cdd:cd17652 79 MLADARPALLL------------------------------------------------TTP----------DNLAYvIY 100
|
170 180
....*....|....*....|...
gi 564388681 252 TSGTTGLPKAAIVVHSRYYRIAA 274
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAA 123
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
89-317 |
8.79e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 58.34 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVdaSSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRRE 168
Cdd:PRK09029 13 AQVRPQAIALR--LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 169 PLafclgtsaakaliyggemaaavAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQAPgkgMddrlf 248
Cdd:PRK09029 91 LL----------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLAT---M----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 249 yIYTSGTTGLPKAaiVVHSryyriaaFGHHSYSmrANDVL----YDC-------LPLYHsagnimgV-GQCIIY-----G 311
Cdd:PRK09029 141 -TLTSGSTGLPKA--AVHT-------AQAHLAS--AEGVLslmpFTAqdswllsLPLFH-------VsGQGIVWrwlyaG 201
|
....*.
gi 564388681 312 LTVVLR 317
Cdd:PRK09029 202 ATLVVR 207
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-267 |
1.99e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAVAQRQPERLALVDASSGIcwTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 160
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEETL--DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 161 LNVNLRREPLAFCLGTSAAKALIyggemaaavaevSEQlgksllkfcsgDLGPEsvLPDTQLLDPMLAEAPTTPLA---- 236
Cdd:PRK12316 591 LDPEYPAERLAYMLEDSGVQLLL------------SQS-----------HLGRK--LPLAAGVQVLDLDRPAAWLEgyse 645
|
170 180 190
....*....|....*....|....*....|...
gi 564388681 237 QAPGKGMD-DRLFY-IYTSGTTGLPKAAIVVHS 267
Cdd:PRK12316 646 ENPGTELNpENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
92-608 |
3.26e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.78 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 92 QPERLALVDASSGICWtfaqLDTYSNA--VANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREP 169
Cdd:PLN02479 33 HPTRKSVVHGSVRYTW----AQTYQRCrrLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 170 LAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDL----GPESVLPDT-------------QLL---DPMLAE 229
Cdd:PLN02479 109 IAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSFKPPLliviGDPTCDPKSlqyalgkgaieyeKFLetgDPEFAW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 230 APTTPLAQAPGKGmddrlfyiYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCII 309
Cdd:PLN02479 189 KPPADEWQSIALG--------YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 310 YGLTVVLRKkFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRD----VERRHHVRLAvGNGLRPAIWEEFTQRfGVRq 385
Cdd:PLN02479 261 CGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtilpLPRVVHVMTA-GAAPPPSVLFAMSEK-GFR- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 386 IGEFYGATECNcsianmdGKVGSCGF---------------NSRI-LTHVYPIRLVKVNEDTMEPLrdsqglcipcqPGE 449
Cdd:PLN02479 337 VTHTYGLSETY-------GPSTVCAWkpewdslppeeqarlNARQgVRYIGLEGLDVVDTKTMKPV-----------PAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 450 pGLLVGQInqqdpLRRFDGYVSDSATNKKIAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEA 529
Cdd:PLN02479 399 -GKTMGEI-----VMRGNMVMKGYLKNPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 530 VLSRLLGQTDVAVygVAVPGV---EGKAGMAAIADPHNQLDPNSMYQELQKV----LASYAQP--IFLRLLPQvdtTGTF 600
Cdd:PLN02479 471 VVYTHPAVLEASV--VARPDErwgESPCAFVTLKPGVDKSDEAALAEDIMKFcrerLPAYWVPksVVFGPLPK---TATG 545
|
....*...
gi 564388681 601 KIQKTRLQ 608
Cdd:PLN02479 546 KIQKHVLR 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
80-610 |
3.42e-08 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 56.42 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 80 TIPRIFQAVAQRQPERLALvdASSGICWTFAQLDTYSNAVANLFL-QLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVa 158
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAY--HSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 159 aLLNVNLRREP--LAFCLGTSAAKALI----YGGEMAAAVAE------VSEQLGkSLLKFCSGDL------GPESVLPDT 220
Cdd:PRK08751 103 -VVNVNPLYTPreLKHQLIDSGASVLVvidnFGTTVQQVIADtpvkqvITTGLG-DMLGFPKAALvnfvvkYVKKLVPEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 221 QLLDPM-------LAEAPTTPLAQ-APgkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYS-----MRANDV 287
Cdd:PRK08751 181 RINGAIrfrealaLGRKHSMPTLQiEP----DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 288 LYDCLPLYH----SAGNI--MGVGqciiyGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHV 361
Cdd:PRK08751 257 VITALPLYHifalTANGLvfMKIG-----GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 362 RLAVGNGL--RPAIWEEFTQRFGVRQIgEFYGATECNcsianmdgkVGSCgfnsrilthVYPIRLVKVNEDTMEPLrDSQ 439
Cdd:PRK08751 332 KMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTETS---------PAAC---------INPLTLKEYNGSIGLPI-PST 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 440 GLCIPCQPGEpGLLVGQINQ---QDPlRRFDGYVSDSATNKKIAHSvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFR 516
Cdd:PRK08751 392 DACIKDDAGT-VLAIGEIGElciKGP-QVMKGYWKRPEETAKVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 517 WRGENVSTTEVEAVLSRLLGQTDVAvyGVAVPGVE-GKAGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVD 595
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEVA--AVGVPDEKsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELP 542
|
570
....*....|....*
gi 564388681 596 TTGTFKIqktrLQRE 610
Cdd:PRK08751 543 KTNVGKI----LRRE 553
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
127-559 |
4.03e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.58 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 127 GFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAevseqlgksllkf 206
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQ------------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 207 csgdlgPESVLPDTQLldpmLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-IAAFGHHSYSMRAN 285
Cdd:PRK06060 118 ------PSRVAEAAEL----MSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTfVDAMCRKALRLTPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 286 DVLYDCLPLYHSagniMGVGQCIIYGL-----TVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHH 360
Cdd:PRK06060 188 DTGLCSARMYFA----YGLGNSVWFPLatggsAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 361 VRLAVGNGLRPAIWEEFTQRFGVRQIGEFYGATECNCS-IANM--DGKVGSCGfnsRILTHvYPIRLVKVNEDTMEPlrd 437
Cdd:PRK06060 264 CVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTfVSNRvdEWRLGTLG---RVLPP-YEIRVVAPDGTTAGP--- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 438 sqglcipcqPGEPGLLVgqinqQDPlrrfdgyvsdsatnkKIAHSVFRKGDSAYLSGDVL------VMDELGYMYFRDRS 511
Cdd:PRK06060 337 ---------GVEGDLWV-----RGP---------------AIAKGYWNRPDSPVANEGWLdtrdrvCIDSDGWVTYRCRA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564388681 512 GDTFRWRGENVSTTEVEavlsRLLGQTDvAVYGVAVPGVEGKAGMAAI 559
Cdd:PRK06060 388 DDTEVIGGVNVDPREVE----RLIIEDE-AVAEAAVVAVRESTGASTL 430
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
81-275 |
6.79e-08 |
|
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: 55.84 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 81 IPRIFQAVAQRQPERLALVDASSGIC-------WTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAK 153
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 154 AGVVAALLNVNLRREPLAFCLGTSAAKALIyggemaaaVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAE---- 229
Cdd:TIGR03443 318 AGATFSVIDPAYPPARQTIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELELRTEIPALALQDDGSLVggsl 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 230 --------APTTPLAQAPGK---GMDDRLFYIYTSGTTGLPKAaivVHSRYYRIAAF 275
Cdd:TIGR03443 390 eggetdvlAPYQALKDTPTGvvvGPDSNPTLSFTSGSEGIPKG---VLGRHFSLAYY 443
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
84-427 |
9.33e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.36 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQ----RQPERLALVDASSGICwTFAQLDTYSNAVANLfLQLGFAPGDVVAVFLegrPEFVGL---WLGLAKAGV 156
Cdd:PRK06814 633 LFEALIEaakiHGFKKLAVEDPVNGPL-TYRKLLTGAFVLGRK-LKKNTPPGENVGVML---PNANGAavtFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 157 VAALLN-----VNLrrepLAFCLGTS-----AAKALIYGGEMAAAVAEVSEQLGKSLLkfcsgdlgpESVLPDTQLLDPM 226
Cdd:PRK06814 708 VPAMINfsagiANI----LSACKAAQvktvlTSRAFIEKARLGPLIEALEFGIRIIYL---------EDVRAQIGLADKI 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 227 LAE-APTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRIAA---FGhhsysmrANDVLYDCLPLYHSA 298
Cdd:PRK06814 775 KGLlAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFHSF 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 299 GNIMGVGQCIIYGLTVVLRKK-------------------FSASRFWDDcvkYNCTVVQYIGEICRYLL--RQPVRDVER 357
Cdd:PRK06814 848 GLTGGLVLPLLSGVKVFLYPSplhyriipeliydtnatilFGTDTFLNG---YARYAHPYDFRSLRYVFagAEKVKEETR 924
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564388681 358 RhhvrlavgnglrpaIWEEftqRFGVRqIGEFYGATECNCSIA-N--MDGKVGSCGfnsRILTHVYPiRLVKV 427
Cdd:PRK06814 925 Q--------------TWME---KFGIR-ILEGYGVTETAPVIAlNtpMHNKAGTVG---RLLPGIEY-RLEPV 975
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
79-610 |
1.71e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 54.38 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 79 DTIPRIfQAVAQRQPERLALVDASS--GICWTFAQLDTYSNAVAnLFLQ--LGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:PRK05677 21 DEYPNI-QAVLKQSCQRFADKPAFSnlGKTLTYGELYKLSGAFA-AWLQqhTDLKPGDRIAVQLPNVLQYPVAVFGAMRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVaaLLNVN---LRREpLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGP-------ESV------- 216
Cdd:PRK05677 99 GLI--VVNTNplyTARE-MEHQFNDSGAKALVCLANMAHLAEKVLPKTGvKHVIVTEVADMLPplkrlliNAVvkhvkkm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 217 -----LPDTQLLDPMLAEAPTTPLAQAPGKGmDDRLFYIYTSGTTGLPKAAIVVHSRYyrIAAFGHHSYSMRAN-----D 286
Cdd:PRK05677 176 vpayhLPQAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLQCRALMGSNlnegcE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 287 VLYDCLPLYH------SAGNIMGVGQCIIY--------GLTVVLRK-KFSAsrFwddcVKYNCTVVQyigeICRyllRQP 351
Cdd:PRK05677 253 ILIAPLPLYHiyaftfHCMAMMLIGNHNILisnprdlpAMVKELGKwKFSG--F----VGLNTLFVA----LCN---NEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 352 VRDVE-RRHHVRLAVGNGLRPAIWEEFTQRFGVrQIGEFYGATECN--CSIANMDG-KVGSCGFNsrilthvYPIRLVKV 427
Cdd:PRK05677 320 FRKLDfSALKLTLSGGMALQLATAERWKEVTGC-AICEGYGMTETSpvVSVNPSQAiQVGTIGIP-------VPSTLCKV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 428 NEDTME--PLRDSQGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKIAHSVFRKgdsaylSGDVLVMDELGYM 505
Cdd:PRK05677 392 IDDDGNelPLGEVGELCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIALIQEDGYM 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 506 YFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AIADPHNQLDPNSMYQELQKVLAS 581
Cdd:PRK05677 450 RIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEHMRANLTG 525
|
570 580
....*....|....*....|....*....
gi 564388681 582 YAQPIFLRLLPQVDTTGTFKIQKTRLQRE 610
Cdd:PRK05677 526 YKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
245-545 |
1.76e-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: 53.54 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVHSRYYRI----AAFGHHSYSM-------RAND---VLYDCLPLYHSAGNIMGVGQcIIY 310
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMlmggADFGTGEFTPsedahkaAAAAagtVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 311 GLTVVL-RKKFSASRFWDDCVKYNCTVVQYIGEIcrylLRQPVRDVERRHHVR-----LAVGNG---LRPAIWEEFTQRF 381
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVTSMTIVGDA----MARPLIDALRDAGPYdlsslFAISSGgalLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 382 GVRQIGEFYGATEcncSIANMDGKVGSCGFNSRILTHVYPiRLVKVNEDTMEPLRDSQGlcipcqpgepgllVGQINQQD 461
Cdd:cd05924 159 PNITLVDAFGSSE---TGFTGSGHSAGSGPETGPFTRANP-DTVVLDDDGRVVPPGSGG-------------VGWIARRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 462 --PLrrfdGYVSDSatnKKIAHSVFRKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQT 538
Cdd:cd05924 222 hiPL----GYYGDE---AKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVY 294
|
....*..
gi 564388681 539 DVAVYGV 545
Cdd:cd05924 295 DVLVVGR 301
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
75-286 |
2.40e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 75 RRAGDTIPRIFQAVAQRQPERLALVDASSGICwtFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKA 154
Cdd:PRK05691 2184 ARLDQTLHGLFAAQAARTPQAPALTFAGQTLS--YAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 155 GVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEvseqLGKSLLKFCsgdlgpesvLPDTQlldPMLAEAPTTP 234
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE----LPAGVARWC---------LEDDA---AALAAYSDAP 2325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 235 LAQAPGKgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGhhsysMRAND 286
Cdd:PRK05691 2326 LPFLSLP--QHQAYLIYTSGSTGKPKGVVVSHGEIAMhcqavIERFG-----MRADD 2375
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
526-601 |
2.83e-07 |
|
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: 48.31 E-value: 2.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 526 EVEAVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFK 601
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
108-302 |
4.01e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.44 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 187
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 maaAVAEVSEQLGKSLLKFCS----GDLgPESV-------LPDTQLLDPMLAEAPTTPLaqaPGKGMDDRLFYI-YTSGT 255
Cdd:PTZ00216 203 ---NVPNLLRLMKSGGMPNTTiiylDSL-PASVdtegcrlVAWTDVVAKGHSAGSHHPL---NIPENNDDLALImYTSGT 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 256 TGLPKAaiVVHSryYRIAAFGHHSYSMRANDVL--------YdC--LPLYHsagnIM 302
Cdd:PTZ00216 276 TGDPKG--VMHT--HGSLTAGILALEDRLNDLIgppeedetY-CsyLPLAH----IM 323
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
108-592 |
5.50e-07 |
|
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: 52.70 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGvvaallnvnlrreplafclgtsAAKALIYGGE 187
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIG----------------------AIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPL-------------AQAPGKGMD---------- 244
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKPHhvlvlnrpqvpadLTKPGRDLDwsellakaep 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 ---------DRLFYIYTSGTTGLPKAaIVVHSRYYRIAAfghhSYSMRAndvLYDCLP--LYHSAGNImG--VG-QCIIY 310
Cdd:cd05967 222 vdcvpvaatDPLYILYTSGTTGKPKG-VVRDNGGHAVAL----NWSMRN---IYGIKPgdVWWAASDV-GwvVGhSYIVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 311 G------LTVVLRKKFS----ASRFWDDCVKYNCTVVQYIGEICRYLLRQP-----VR--DVERRHHVRLAvGNGLRPAI 373
Cdd:cd05967 293 GpllhgaTTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKkyDLSSLRTLFLA-GERLDPPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 374 WEEFTQRFGVRQIgEFYGATE------CNCS-IANMDGKVGSC-----GFNsrilthvypirlVKVNEDTMEPLR-DSQG 440
Cdd:cd05967 372 LEWAENTLGVPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPgkpvpGYQ------------VQVLDEDGEPVGpNELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 441 -LCIPCqPGEPGLLVGQINQQDplrRF-DGYVSDSatnkkiahsvfrkgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 518
Cdd:cd05967 439 nIVIKL-PLPPGCLLTLWKNDE---RFkKLYLSKF--------------PGYYDTGDAGYKDEDGYLFIMGRTDDVINVA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 519 GENVSTTEVEAVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AIADPHNQLDPNSMYQELQKV-------LASYAQPIFLRL 590
Cdd:cd05967 501 GHRLSTGEMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKELVALvreqigpVAAFRLVIFVKR 579
|
..
gi 564388681 591 LP 592
Cdd:cd05967 580 LP 581
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
108-607 |
6.02e-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: 52.46 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIygGE 187
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI--GI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 maaavaevseqlgksllkfcsgdlgpesvlpdtqlldpmlaeapttPLAqapgkgmDDRLFYIYTSGTTGLPKAAIVVHS 267
Cdd:cd05910 82 ----------------------------------------------PKA-------DEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 268 RYY-RIAAFgHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCI-----IYGLTVVLRKKFSASRfwddcvKYNCTVV---- 337
Cdd:cd05910 109 TFAaQIDAL-RQLYGIRPGEVDLATFPLFALFGPALGLTSVIpdmdpTRPARADPQKLVGAIR------QYGVSIVfgsp 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 338 QYIGEICRYLLRQ--PVRDVERrhhvRLAVGNGLRPAIWEEFtqRFGVRQIGEF---YGATEC--NCSIANMD------- 403
Cdd:cd05910 182 ALLERVARYCAQHgiTLPSLRR----VLSAGAPVPIALAARL--RKMLSDEAEIltpYGATEAlpVSSIGSREllattta 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 404 ---GKVGSCgfnsriLTHVYPIRLVKVNEDTMEPLRDSQG-LCIPcqPGEpgllVGQINQQDPLrrfdgyVSDSATNKKI 479
Cdd:cd05910 256 atsGGAGTC------VGRPIPGVRVRIIEIDDEPIAEWDDtLELP--RGE----IGEITVTGPT------VTPTYVNRPV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 480 AHSVFRKGDSA----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKAG 555
Cdd:cd05910 318 ATALAKIDDNSegfwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388681 556 ----MAAIADPHNQLdpnsmYQELQKVLASYAQP-IFLRLL----PQVDTTGTFKIQKTRL 607
Cdd:cd05910 398 cvepLPGTITPRARL-----EQELRALAKDYPHTqRIGRFLihpsFPVDIRHNAKIFREKL 453
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
107-311 |
7.99e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.43 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 W-TFAQ-LDTYSNAVANLfLQLGFAPGDVVAVFLEGRPEfvglWL----GLAKAGVVAALLNVNLRREPLAFCLGTSAAK 180
Cdd:PLN02387 106 WiTYGQvFERVCNFASGL-VALGHNKEERVAIFADTRAE----WLialqGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 181 ALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLA----------EAPTTPLAQAPgkgmDDRLFYI 250
Cdd:PLN02387 181 TVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSsfseveklgkENPVDPDLPSP----NDIAVIM 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564388681 251 YTSGTTGLPKAAIVVHSRYY-RIAAFGHHSYSMRANDVLYDCLPLYH----SAGNIM-GVGQCIIYG 311
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVaTVAGVMTVVPKLGKNDVYLAYLPLAHilelAAESVMaAVGAAIGYG 323
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
107-296 |
2.11e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.87 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 107 W-TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 185
Cdd:PLN02736 78 WmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE----WLIVDHACSAYSYVSV-----PLYDTLGPDAVKFIVNH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 186 GEMAAAVaeVSEQLGKSLLKFCS------------GDLGPESVLPDTQ-----LLDPMLAEAPTTPLAQAPGKGmDDRLF 248
Cdd:PLN02736 149 AEVAAIF--CVPQTLNTLLSCLSeipsvrlivvvgGADEPLPSLPSGTgveivTYSKLLAQGRSSPQPFRPPKP-EDVAT 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564388681 249 YIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYH 296
Cdd:PLN02736 226 ICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
62-301 |
2.12e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.81 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 62 SVLIRVRLELRRHRRagdTIPRIFQAVAQRQPER--LALVDASSGiCW---TFAQLDTYSNAVANLFLQLGFAPGDVVAV 136
Cdd:PRK12582 35 SIVIKSRHPLGPYPR---SIPHLLAKWAAEAPDRpwLAQREPGHG-QWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 137 fLEGRP-EFVGLWLGLAKAGVVAA-------LLNVNLRRepLAFCLgTSAAKALIY---GGEMAAAVAEVSEQlGKSLLk 205
Cdd:PRK12582 111 -LSGNSiEHALMTLAAMQAGVPAApvspaysLMSHDHAK--LKHLF-DLVKPRVVFaqsGAPFARALAALDLL-DVTVV- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 206 FCSGDLGPESVLPdtqlLDPMLAEAPTTPLAQAPGK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRA 284
Cdd:PRK12582 185 HVTGPGEGIASIA----FADLAATPPTAAVAAAIAAiTPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREP 260
|
250 260
....*....|....*....|.
gi 564388681 285 ND---VLYDCLPLYH-SAGNI 301
Cdd:PRK12582 261 DPpppVSLDWMPWNHtMGGNA 281
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
244-609 |
2.54e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 50.67 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 244 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRIAAFgHHSYSMRANDVLY---DClplyhsaGNIMGVGQC----IIYGLTV 314
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITGHSYVtygpMLNGATV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 315 VLRKKF----SASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVER--RHHVRL--AVGNGLRPAIWEEFTQRFGvrqi 386
Cdd:PLN02654 347 LVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRhsRKSLRVlgSVGEPINPSAWRWFFNVVG---- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 387 gefygatECNCSIANMDGKVGSCGFNSRILTHVYP------------IRLVKVNEDTMEPLRDSQG-LCIPCQ-PGEPGL 452
Cdd:PLN02654 423 -------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCVKKSwPGAFRT 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 453 LVGQINQQDP--LRRFDGYvsdsatnkkiahsvfrkgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAV 530
Cdd:PLN02654 496 LYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 531 LSRLLGQTDVAVYGV--AVPGvEGKAGMAAIAD--PHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTR 606
Cdd:PLN02654 555 LVSHPQCAEAAVVGIehEVKG-QGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRI 633
|
...
gi 564388681 607 LQR 609
Cdd:PLN02654 634 LRK 636
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
79-302 |
6.13e-06 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 49.20 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 79 DTIPRIFQAVAQRQPERLALV------DASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFV-GLWlGL 151
Cdd:cd05906 6 EGAPRTLLELLLRAAERGPTKgityidADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIpAFW-AC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 152 AKAGVVAALLNV-------NLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEqlgksllkfcsgdlgpESVLPDTQLLd 224
Cdd:cd05906 85 VLAGFVPAPLTVpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLET----------------LSGLPGIRVL- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 225 pMLAEAPTTP-LAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVH-SRYYRIAAFGHHsYSMRANDVLYDCLPLYHSAGNIM 302
Cdd:cd05906 148 -SIEELLDTAaDHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHrNILARSAGKIQH-NGLTPQDVFLNWVPLDHVGGLVE 225
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
245-604 |
6.33e-06 |
|
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: 48.80 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 245 DRLFYIYTSGTTGLPKAAIVVHSRYYriAAFGH---HSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFS 321
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 322 ASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHHVRLAVGNGLRP-AIWEEFTQRFGVRQIGEFYGATECN--CS 398
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSETGtaLC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 399 IANMDG--KVGSCGfnsriltHVYPIRLVKV-NEDTMEPLRDSQGLCIPCQPgepgllvgqinqqdplRRFDGYVSdsat 475
Cdd:cd17635 160 LPTDDDsiEINAVG-------RPYPGVDVYLaATDGIAGPSASFGTIWIKSP----------------ANMLGYWN---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 476 NKKIAHSVFRKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvAVPGVEGKA 554
Cdd:cd17635 213 NPERTAEVLIDG---WVnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISDEEFGE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564388681 555 GMAAIADPHNQLDPNSMYQELQKV---LASYAQPIFLRLLPQVDTTGTFKIQK 604
Cdd:cd17635 288 LVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-264 |
9.18e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 83 RIFQAVAQRQPERLAL--VDASsgicWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAAL 160
Cdd:PRK05691 3724 RLFEAQVAAHPQRIAAscLDQQ----WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLP 3799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 161 LNVNLRREPLAFCLGTSAAKALIyggeMAAAVAEvseqLGKSLLKFCSGDLGPesvlpdtQLLdpMLAEAPTTPLAQA-P 239
Cdd:PRK05691 3800 LDPGLPAQRLQRIIELSRTPVLV----CSAACRE----QARALLDELGCANRP-------RLL--VWEEVQAGEVASHnP 3862
|
170 180
....*....|....*....|....*..
gi 564388681 240 G--KGMDDRLFYIYTSGTTGLPKAAIV 264
Cdd:PRK05691 3863 GiySGPDNLAYVIYTSGSTGLPKGVMV 3889
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
89-563 |
1.14e-05 |
|
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: 48.33 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALV----DASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVN 164
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 165 LRREPLAFCLGTSAAKALIY------GGEMAAAVAEVSEQLGKSLlkfcsgdlGPESVL---------PDTQ----LLDP 225
Cdd:cd05966 143 FSAESLADRINDAQCKLVITadggyrGGKVIPLKEIVDEALEKCP--------SVEKVLvvkrtggevPMTEgrdlWWHD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 226 MLAEAPTtplaQAPGKGMD--DRLFYIYTSGTTGLPKAaiVVHS----------------------RYYRIAAFG---HH 278
Cdd:cd05966 215 LMAKQSP----ECEPEWMDseDPLFILYTSGSTGKPKG--VVHTtggyllyaattfkyvfdyhpddIYWCTADIGwitGH 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 279 SYsmrandVLYDclPLyhsagnimgvgqciIYGLTVVLrkkF-------SASRFWDDCVKYNCTVVQYIGEICRYLLRQP 351
Cdd:cd05966 289 SY------IVYG--PL--------------ANGATTVM---FegtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 352 VRDVER--RHHVRL--AVGNGLRPAIWEEFTqrfgvRQIGEFygatecNCS--------------IANMDG----KVGSC 409
Cdd:cd05966 344 DEWVKKhdLSSLRVlgSVGEPINPEAWMWYY-----EVIGKE------RCPivdtwwqtetggimITPLPGatplKPGSA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 410 GFnsrilthvyP---IRLVKVNEDTMEPLRDSQG-LCIPcQPGePGLLVGQINqqDPLRRFDGYvsdsatnkkiahsvFR 485
Cdd:cd05966 413 TR---------PffgIEPAILDEEGNEVEGEVEGyLVIK-RPW-PGMARTIYG--DHERYEDTY--------------FS 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564388681 486 KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgqtdvavygVAVPGVegkAGMAAIADPH 563
Cdd:cd05966 466 KFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVGRPH 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
84-531 |
1.59e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 47.89 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 84 IFQAVAQRQPERLALvdASSGICWTFAQLDTYSNAVANlFLQ--LGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVaaLL 161
Cdd:PRK12492 29 VFERSCKKFADRPAF--SNLGVTLSYAELERHSAAFAA-YLQqhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLI--VV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 162 NVN---LRREpLAFCLGTSAAKALIYGGEMAAAVAEVSEQLG-KSLLKFCSGDLGP--ESVLPDTqLLDPMLAEAPTTPL 235
Cdd:PRK12492 104 NTNplyTARE-MRHQFKDSGARALVYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLPaaKGWLVNT-VVDKVKKMVPAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 236 AQAPG-----------------KGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-----IAAFGH-----HSYSMRANDVL 288
Cdd:PRK12492 182 PQAVPfkqalrqgrglslkpvpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvRACLSQlgpdgQPLMKEGQEVM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 289 YDCLPLYHsagnimgvgqciIYGLT-------------VVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQP-VRD 354
Cdd:PRK12492 262 IAPLPLYH------------IYAFTancmcmmvsgnhnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPgFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 355 VERRH-HVRLAVGNGLRPAIWEEFTQRFGVRqIGEFYGATECN-CSIANMDGKVgscgfnSRILTHVYPI--RLVKV-NE 429
Cdd:PRK12492 330 LDFSAlKLTNSGGTALVKATAERWEQLTGCT-IVEGYGLTETSpVASTNPYGEL------ARLGTVGIPVpgTALKViDD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 430 DTME-PLRDSQGLCIPcqpgEPGLLVGQINQQDplrrfdgyvsdsATNKKI-AHSVFRkgdsaylSGDVLVMDELGYMYF 507
Cdd:PRK12492 403 DGNElPLGERGELCIK----GPQVMKGYWQQPE------------ATAEALdAEGWFK-------TGDIAVIDPDGFVRI 459
|
490 500
....*....|....*....|....
gi 564388681 508 RDRSGDTFRWRGENVSTTEVEAVL 531
Cdd:PRK12492 460 VDRKKDLIIVSGFNVYPNEIEDVV 483
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
222-528 |
1.61e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 48.17 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 222 LLDPMLAEAPTTPlaqapgkgmDDRLFYIYTSGTTGLPKAaiVVHS---------RYYRIAAFghhsysmRANDVLYDCL 292
Cdd:PRK08043 352 LLMPRLAQVKQQP---------EDAALILFTSGSEGHPKG--VVHShksllanveQIKTIADF-------TPNDRFMSAL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 293 PLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCV-KYNCTVV----QYIGEICR-------YLLRQPVRDVER-RH 359
Cdd:PRK08043 414 PLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNYARfanpydfARLRYVVAGAEKlQE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 360 HVRlavgnglrpAIWEEftqRFGVRqIGEFYGATECNCSIA---NMDGKVGSCGfnsRILTHVyPIRLVKVNEDTmeplr 436
Cdd:PRK08043 494 STK---------QLWQD---KFGLR-ILEGYGVTECAPVVSinvPMAAKPGTVG---RILPGM-DARLLSVPGIE----- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 437 dsQGLCIpcQPGEPGLLVGQINQQDPlrrfDGYVSDSATNkkiAHSVFRKGdsAYLSGDVLVMDELGYMYFRDRSGDTFR 516
Cdd:PRK08043 552 --QGGRL--QLKGPNIMNGYLRVEKP----GVLEVPTAEN---ARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAK 618
|
330
....*....|..
gi 564388681 517 WRGENVSTTEVE 528
Cdd:PRK08043 619 IAGEMVSLEMVE 630
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
108-612 |
1.63e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.82 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE 187
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 188 MAAAVAEVSEQLgKSLLKFCSgdLGPESVLPDTQLLDpmlAEAPTTPLAQAPG----KGMDDRLF--YIYTSGTTGLPKA 261
Cdd:PRK06018 121 FVPILEKIADKL-PSVERYVV--LTDAAHMPQTTLKN---AVAYEEWIAEADGdfawKTFDENTAagMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 262 AI------VVHSryyrIAAFGHHSYSMRANDVLYDCLPLYHSagNIMGVGQ-CIIYGLTVVLR-KKFSASRFWDDCVKYN 333
Cdd:PRK06018 195 VLyshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA--NSWGIAFsAPSMGTKLVMPgAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 334 CTVVQYIGEICRYLLRQPVRDVERRHHVRLAV--GNGLRPAIWEEFtQRFGVrQIGEFYGATECN--CSIANMDGKVGSC 409
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVcgGSAMPRSMIKAF-EDMGV-EVRHAWGMTEMSplGTLAALKPPFSKL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 410 GFNSRI---LTHVYPIRLVKVNedtmepLRDSQGLCIPCQPGEPGLLVgqinqqdplrrfdgyVSDSAtnkkIAHSVFRK 486
Cdd:PRK06018 347 PGDARLdvlQKQGYPPFGVEMK------ITDDAGKELPWDGKTFGRLK---------------VRGPA----VAAAYYRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 487 GDSA------YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE--AVlsrllGQTDV---AVYGVAVPGVEGKAG 555
Cdd:PRK06018 402 DGEIldddgfFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnlAV-----GHPKVaeaAVIGVYHPKWDERPL 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 556 MAAIADPHNQLDPNSMYQELQKVLASYAQP---IFLRLLPQvdtTGTFKIQKTRLqREGF 612
Cdd:PRK06018 477 LIVQLKPGETATREEILKYMDGKIAKWWMPddvAFVDAIPH---TATGKILKTAL-REQF 532
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
89-407 |
2.26e-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: 47.43 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 89 AQRQPERLALVDASSGICW---TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAA------ 159
Cdd:cd05921 5 ARQAPDRTWLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAApvspay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 160 -LLNVNLRRepLAFCLGTsAAKALIY---GGEMAAAVAEVsEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPttpl 235
Cdd:cd05921 85 sLMSQDLAK--LKHLFEL-LKPGLVFaqdAAPFARALAAI-FPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVD---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 236 AQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRAND--VLYDCLPLYHSAGNIMGVGQCIIYGLT 313
Cdd:cd05921 157 AAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 314 VVL-RKKFSASRFwDDCVK--------YNCTVVQYIGEICRYLLRQPV--RDVERRHHVRLAVGNGLRPAIWEEFtQRFG 382
Cdd:cd05921 237 LYIdDGKPMPGGF-EETLRnlreisptVYFNVPAGWEMLVAALEKDEAlrRRFFKRLKLMFYAGAGLSQDVWDRL-QALA 314
|
330 340 350
....*....|....*....|....*....|....*..
gi 564388681 383 VRQIGE------FYGATE-----CNCS-IANMDGKVG 407
Cdd:cd05921 315 VATVGEripmmaGLGATEtaptaTFTHwPTERSGLIG 351
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
90-284 |
4.83e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.52 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 90 QRQPERLALVDASSGicWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGV--VAALLNVNlRR 167
Cdd:PRK10946 34 HAASDAIAVICGERQ--FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVapVNALFSHQ-RS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 168 EPLAFC-------LGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGpesvlpdtqLLDPMLAEAPTTPLAQAPG 240
Cdd:PRK10946 111 ELNAYAsqiepalLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHS---------LDDAINHPAEDFTATPSPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564388681 241 kgmDDRLFYIYTSGTTGLPKAAIVVHSRYYriaafghhsYSMRA 284
Cdd:PRK10946 182 ---DEVAFFQLSGGSTGTPKLIPRTHNDYY---------YSVRR 213
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
75-301 |
1.26e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 45.14 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 75 RRAGDTIPRIFQAVAQRQPERLAL-------------VDASSGICW-----TFAQLDTYSNAVANLF-LQLGFAPGDVVA 135
Cdd:cd17632 18 RRPGLRLAQIIATVMTGYADRPALgqratelvtdpatGRTTLRLLPrfetiTYAELWERVGAVAAAHdPEQPVRPGDFVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 136 VFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGE-MAAAVAEVSEQLG-KSLLKFcsgDLGP 213
Cdd:cd17632 98 VLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEhLDLAVEAVLEGGTpPRLVVF---DHRP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 214 E------------SVLPDT----QLLDPMLAEAPTTPLAQAPGKGMD-DRL-FYIYTSGTTGLPKAAIVVHSryyRIAAF 275
Cdd:cd17632 175 EvdahraalesarERLAAVgipvTTLTLIAVRGRDLPPAPLFRPEPDdDPLaLLIYTSGSTGTPKGAMYTER---LVATF 251
|
250 260 270
....*....|....*....|....*....|
gi 564388681 276 GHHSYSMRAND----VLYDCLPLYHSAGNI 301
Cdd:cd17632 252 WLKVSSIQDIRppasITLNFMPMSHIAGRI 281
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
151-611 |
1.73e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 44.60 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 151 LAKAGVVAALlnvnlRREPLAFCLGTSAAkaLIYGgemaAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEA 230
Cdd:PRK07787 42 VAGARRVAVL-----ATPTLATVLAVVGA--LIAG----VPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 231 PTTPLAQA----PGKGMDDRLFYIYTSGTTGLPKAaiVVHSRyyRIAAFG----HHSYSMRANDVLYDCLPLYHSAGNIM 302
Cdd:PRK07787 111 PVRLHARSwhryPEPDPDAPALIVYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 303 GVGQCIIYGLTVVLRKKFSASRFWDDCvKYNCTVvqYIGeicryllrqpVRDVERRHHVRLAVGNGLRPA---------- 372
Cdd:PRK07787 187 GVLGPLRIGNRFVHTGRPTPEAYAQAL-SEGGTL--YFG----------VPTVWSRIAADPEAARALRGArllvsgsaal 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 373 ---IWEEFTQRFGVRQIgEFYGATEC--NCSI-ANMDGKVGSCGFnsrilthvyPIRLVKVNedtmepLRDSQGLCIPCQ 446
Cdd:PRK07787 254 pvpVFDRLAALTGHRPV-ERYGMTETliTLSTrADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 447 pGEPgllVGQINQQDPLrRFDGYVsdsatNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTT 525
Cdd:PRK07787 318 -GET---VGELQVRGPT-LFDGYL-----NRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 526 EVEAVlsrLLGQTDVAvyGVAVPGVE----GKAGMAAIAdPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFK 601
Cdd:PRK07787 388 EIETA---LLGHPGVR--EAAVVGVPdddlGQRIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGK 461
|
490
....*....|
gi 564388681 602 IQKTRLQREG 611
Cdd:PRK07787 462 VLKKQLLSEG 471
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
483-602 |
1.95e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 44.26 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 483 VFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYgvavPGVEGKAG--MAAIA 560
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGerVKAKV 360
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564388681 561 DPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKI 602
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
103-296 |
3.35e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 43.74 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 103 SGICW-TFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKA 181
Cdd:cd17639 1 GEYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 182 LiyggemaaavaevseqlgksllkFCSGDlgpesvlpdtqlldpmlaeapttplaqapgkgMDDRLFYIYTSGTTGLPKA 261
Cdd:cd17639 81 I-----------------------FTDGK--------------------------------PDDLACIMYTSGSTGNPKG 105
|
170 180 190
....*....|....*....|....*....|....*..
gi 564388681 262 AIVVHSRYYR-IAAFGHHSYS-MRANDVLYDCLPLYH 296
Cdd:cd17639 106 VMLTHGNLVAgIAGLGDRVPElLGPDDRYLAYLPLAH 142
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
493-612 |
4.67e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 43.16 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 493 SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLsrllgqtdvavygVAVPGVegkAGMAAIADPHNQLDPNSMY 572
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVA-------------VAHPAV---AEAACIACAHPKWDERPLL 476
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 573 ------------QELQKV----LASYAQP---IFLRLLPQvdtTGTFKIQKTRLqREGF 612
Cdd:PRK07008 477 vvvkrpgaevtrEELLAFyegkVAKWWIPddvVFVDAIPH---TATGKLQKLKL-REQF 531
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-296 |
4.72e-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: 43.36 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 108 TFAQLDTYSNAVANLFLQLGF--APGDVVAVFLEGRPEfvglWLGLAKAGVVAALLNVnlrrePLAFCLGTSAAKALIYG 185
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPE----WIISELACYAYSLVTV-----PLYDTLGPEAIEYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388681 186 GEMaaavaevseqlgkSLLkFCSGDLgpeSVLPDTQLLDpMLAEAPTTPLAQAPgkgmdDRLFYI-YTSGTTGLPKAAIV 264
Cdd:cd05927 78 AEI-------------SIV-FCDAGV---KVYSLEEFEK-LGKKNKVPPPPPKP-----EDLATIcYTSGTTGNPKGVML 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 564388681 265 VH----SRYYRIAAFGHHSYSMRANDVLYDCLPLYH 296
Cdd:cd05927 135 THgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
250-314 |
6.76e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 42.73 E-value: 6.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388681 250 IYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDC----LPLYHSAGNIMGVGQCIIYGLTV 314
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| |
