|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
32-541 |
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: 723.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYss 111
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 elsegvkeilgelkdiklyilnkskegeetnlgeaiDLKKGLAEVSKANL--IDEVNAgkpRDKLLFIYTSGTTGLPKAA 189
Cdd:cd05939 82 ------------------------------------NLLDPLLTQSSTEPpsQDDVNF---RDKLFYIYTSGTTGLPKAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 190 VINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGE 269
Cdd:cd05939 123 VIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 270 ICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNIDNKVGCVGFVPRLAGPVYPV 349
Cdd:cd05939 203 ICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 350 VLLKVDKDTEEPIRNSKGFCIRCQPGEPGICVGKINSKQTISTFLGYADKVESEKKILKNVFKKGDNYFNSGDILVMDDY 429
Cdd:cd05939 283 RLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 430 GYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSY 509
Cdd:cd05939 363 GYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPY 442
|
490 500 510
....*....|....*....|....*....|..
gi 242022874 510 ARPLFVRIIKNLPLTGTYKLKKKELQMEGFNI 541
Cdd:cd05939 443 ARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-576 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 668.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEETNLgeAIDLKKGLAEVSKANLiDEVN 166
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEG--YEDLAAAAAGAPTTNP-ASRS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKK 246
Cdd:PRK08279 195 GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNL 326
Cdd:PRK08279 275 FSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 327 VNIDNKVGCVGFVPRLAGpvYPVVLLKVDKDTEEPIRNSKGFCIRCQPGEPGICVGKINSKQtisTFLGYADKVESEKKI 406
Cdd:PRK08279 355 INVFNFDGTVGRVPLWLA--HPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRG---PFDGYTDPEASEKKI 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 407 LKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAI 486
Cdd:PRK08279 430 LRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAI 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 487 H-DVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEGFNITKIKDPVYFYDNRSQKFELLSSLL 565
Cdd:PRK08279 510 VlADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAEL 589
|
570
....*....|.
gi 242022874 566 YNDILNGVLKL 576
Cdd:PRK08279 590 YAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
32-540 |
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: 587.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYss 111
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 elsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevnagkprDKLLFIYTSGTTGLPKAAVI 191
Cdd:cd05940 82 ------------------------------------------------------------DAALYIYTSGTTGLPKAAII 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 192 NNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEIC 271
Cdd:cd05940 102 SHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 272 RYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNIDNKVGCVGFVPRLAGPVYPVVL 351
Cdd:cd05940 182 RYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 352 LKVDKDTEEPIRNSKGFCIRCQPGEPGICVGKINSKQtisTFLGYADKVESEKKILKNVFKKGDNYFNSGDILVMDDYGY 431
Cdd:cd05940 262 VKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLE---PFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 432 FSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHD-VDESVNLQEFDEKLKKMLPSYA 510
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLqPNEEFDLSALAAHLEKNLPGYA 418
|
490 500 510
....*....|....*....|....*....|
gi 242022874 511 RPLFVRIIKNLPLTGTYKLKKKELQMEGFN 540
Cdd:cd05940 419 RPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
31-566 |
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: 571.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIY 109
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 110 SSELSEGVKEILGELKD--IKLYILNKSKEGEET-NLGEAIDlkkglAEVSKANLIDEVNAGKPRDKLLFIYTSGTTGLP 186
Cdd:cd05938 85 APELQEAVEEVLPALRAdgVSVWYLSHTSNTEGViSLLDKVD-----AASDEPVPASLRAHVTIKSPALYIYTSGTTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 187 KAAVINNNRYLFISiGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACY 266
Cdd:cd05938 160 KAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNIDNKVGCVGFVPRLAGPV 346
Cdd:cd05938 239 IGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 347 YPVVLLKVDKDTEEPIRNSKGFCIRCQPGEPGICVGKINSKqtiSTFLGYA-DKVESEKKILKNVFKKGDNYFNSGDILV 425
Cdd:cd05938 319 FPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQ---SPFLGYAgDKEQTEKKLLRDVFKKGDVYFNTGDLLV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 426 MDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDEsvnlQEFD-----E 500
Cdd:cd05938 396 QDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPG----HEFDgkklyQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 501 KLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEGFNITKIKDPVYFYDNRSQKFELLSSLLY 566
Cdd:cd05938 472 HVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
28-538 |
1.21e-142 |
|
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: 420.69 E-value: 1.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 28 ENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNA 106
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 107 LIYSselsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevnagkPRDKLLFIYTSGTTGLP 186
Cdd:cd05937 82 VIVD-----------------------------------------------------------PDDPAILIYTSGTTGLP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 187 KAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACY 266
Cdd:cd05937 103 KAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNI---DNKVGCVGFvprlA 343
Cdd:cd05937 183 VGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAGAIGH----H 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 344 GPVY------PVVLLKVDKDTEEPIR-NSKGFCIRCQPGEPGICVGKINSKqTISTFLGY-ADKVESEKKILKNVFKKGD 415
Cdd:cd05937 259 GLIRrwkfenQVVLVKMDPETDDPIRdPKTGFCVRAPVGEPGEMLGRVPFK-NREAFQGYlHNEDATESKLVRDVFRKGD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 416 NYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDESV-- 493
Cdd:cd05937 338 IYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAvp 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 242022874 494 ---NLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEG 538
Cdd:cd05937 418 tefTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEG 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
32-535 |
3.16e-83 |
|
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: 266.08 E-value: 3.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIyss 111
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 elsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlIDEVNagkprdkllFIYTSGTTGLPKAAVI 191
Cdd:cd05934 81 --------------------------------------------------VDPAS---------ILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 192 NNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEIC 271
Cdd:cd05934 102 THANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 272 RYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKqIGEFYGATEGNSNLVN---IDNKVGCVGfvprLAGPVYP 348
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGSIG----RPAPGYE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 349 VVLlkVDKDTEEpirnskgfcirCQPGEPG-ICvgkINSKQTISTFLGYADKVESEKKILKNVFkkgdnyFNSGDILVMD 427
Cdd:cd05934 257 VRI--VDDDGQE-----------LPAGEPGeLV---IRGLRGWGFFKGYYNMPEATAEAMRNGW------FHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 428 DYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLP 507
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 242022874 508 SYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
8-535 |
5.45e-74 |
|
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: 242.79 E-value: 5.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 8 VAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALIN 87
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 88 TNLRNQSFLHSLKAAKCNALIYSselsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevna 167
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVTA--------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 168 gkprdklLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKF 247
Cdd:COG0318 104 -------LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 248 SASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIkQIGEFYGATEGNSN 325
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGV-RIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LV-----NIDNKVGCVGFvprlagPVYPVVLLKVDKDTEEpirnskgfcirCQPGEPG-ICVgkinskQTISTFLGYADK 399
Cdd:COG0318 256 VTvnpedPGERRPGSVGR------PLPGVEVRIVDEDGRE-----------LPPGEVGeIVV------RGPNVMKGYWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 400 VESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVeG 479
Cdd:COG0318 313 PEATAEAFR------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-G 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 480 KAGMVAIH-DVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:COG0318 386 ERVVAFVVlRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-539 |
1.13e-64 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 220.79 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEIL-GELKDIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKANLidev 165
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAALLAALEAADpGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 166 nagKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAgQSILSGITVVIRK 245
Cdd:PRK06155 178 ---QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFF-QALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 246 KFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIgEFYGATEGNS- 324
Cdd:PRK06155 254 RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLL-DGYGSTETNFv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 325 -NLVNIDNKVGCVGfvpRLAGPVYPVVllkVDK-DTEEPirnskgfcircqPGEPGICVgkINSKQTISTFLGYADKVES 402
Cdd:PRK06155 333 iAVTHGSQRPGSMG---RLAPGFEARV---VDEhDQELP------------DGEPGELL--LRADEPFAFATGYFGMPEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 403 EKKILKNVfkkgdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAg 482
Cdd:PRK06155 393 TVEAWRNL------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV- 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 483 MVAIHDVD-ESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEGF 539
Cdd:PRK06155 466 MAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-445 |
1.90e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.10 E-value: 1.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 12 FQEICEKNYDKIAF-HQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNL 90
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 91 RNQSFLHSLKAAKCNALIYSSELS-EGVKEILGELKDIKLYILNKSKEGEETNLGEAidlkkglAEVSKANLIDEVNAGK 169
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKlEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE-------EAKPADVPPPPPPPPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFIYTSGTTGLPKAAVI--NN--NRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRK 245
Cdd:pfam00501 154 PDDLAYIIYTSGTTGKPKGVMLthRNlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 246 KFSA---SNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFqIKQIGEFYGAT 320
Cdd:pfam00501 234 GFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELF-GGALVNGYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 321 EGNSNLVNIDNKVGCVGFVPRlAGPVYPVVLLK-VDKDTEEPIRnskgfcircqPGEPG-ICVGkinskqTISTFLGYAD 398
Cdd:pfam00501 313 ETTGVVTTPLPLDEDLRSLGS-VGRPLPGTEVKiVDDETGEPVP----------PGEPGeLCVR------GPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 242022874 399 KVESEKKilknVFKKGDnYFNSGDILVMDDYGYFSFKDRTGDTFRWK 445
Cdd:pfam00501 376 DPELTAE----AFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
174-530 |
9.69e-56 |
|
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: 191.34 E-value: 9.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 174 LLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIvGAGQSILSGITVVIRKKFSASNFW 253
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 254 QDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERFQIK---QIGEFYGATEGNS-----N 325
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGG--APLPPELLERFEEApgiKLVNGYGLTETGGtvatgP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVNIDNKVGCVGfvprLAGPVYPVVLlkVDKDTEEpirnskgfcirCQPGEPG-ICVgkinskQTISTFLGYADKVEsek 404
Cdd:cd04433 160 PDDDARKPGSVG----RPVPGVEVRI--VDPDGGE-----------LPPGEIGeLVV------RGPSVMKGYWNNPE--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 405 kilKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPhVEGKAGMV 484
Cdd:cd04433 214 ---ATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 242022874 485 AIHDVD-ESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLK 530
Cdd:cd04433 290 VVVLRPgADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
59-551 |
1.35e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 185.27 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 59 IALYMENSIEyMCIWLGLAKL-GIVSALINTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKdiklyILNKSKE 137
Cdd:PRK07867 57 VGVLLDNTPE-FSLLLGAAALsGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVR-----VINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 138 GEETNLGEAIDLKKGLAEVSkanlidevnagkPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYN 217
Cdd:PRK07867 131 AWADELAAHRDAEPPFRVAD------------PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 218 SLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLK 297
Cdd:PRK07867 199 SMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 298 AQIWEKFVERFQIKQIgEFYGATEGNsnlVNI----DNKVGCVGfvpRLAGPVYpvvllKVDKDTEEPirnskgfcirCQ 373
Cdd:PRK07867 279 PGDIARFARRFGCVVV-DGFGSTEGG---VAItrtpDTPPGALG---PLPPGVA-----IVDPDTGTE----------CP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 374 PGEPGiCVGKINSKQTI---------STFLGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRW 444
Cdd:PRK07867 337 PAEDA-DGRLLNADEAIgelvntagpGGFEGYYNDPEADAERMR------GGVYWSGDLAYRDADGYAYFAGRLGDWMRV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 445 KGENVATSEVEAVISNIIGYKDAIVFGVEVPHVeGKAGMVAIHDVDESVNLQE-FDEKL-------KKMLPSYarplfVR 516
Cdd:PRK07867 410 DGENLGTAPIERILLRYPDATEVAVYAVPDPVV-GDQVMAALVLAPGAKFDPDaFAEFLaaqpdlgPKQWPSY-----VR 483
|
490 500 510
....*....|....*....|....*....|....*
gi 242022874 517 IIKNLPLTGTYKLKKKELQMEGFNITkikDPVYFY 551
Cdd:PRK07867 484 VCAELPRTATFKVLKRQLSAEGVDCA---DPVWWI 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
31-529 |
1.90e-51 |
|
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: 183.57 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS 110
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSEGVKEILGEL-KDIKLYILNKSKEGeetnLGEAIDLKKGLAEVSKANLIDEVNAGKprDKLLFI-YTSGTTGLPKA 188
Cdd:cd05911 90 PDGLEKVKEAAKELgPKDKIIVLDDKPDG----VLSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAIlYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 AVINNNRYLFISIGVKILLKLHD--DDILYNSLPLYHTSGVIvGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACY 266
Cdd:cd05911 164 VCLSHRNLIANLSQVQTFLYGNDgsNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRYLLAVPE-KSHDKQHKIRLMFGNG-LKAQIWEKFVERFQIKQIGEFYGATEGNSNL---VNIDNKVGCVGfvpR 341
Cdd:cd05911 243 VPPIAAALAKSPLlDKYDLSSLRVILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILtvnPDGDDKPGSVG---R 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 342 LAgpvyPVVLLK-VDKDTEEPirnskgfcirCQPGEPG-ICVgKINSKqtistFLGYADKVESekkiLKNVFKKgDNYFN 419
Cdd:cd05911 320 LL----PNVEAKiVDDDGKDS----------LGPNEPGeICV-RGPQV-----MKGYYNNPEA----TKETFDE-DGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 420 SGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV------EVPhvegkAGMVAIHDvDESV 493
Cdd:cd05911 375 TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIpdevsgELP-----RAYVVRKP-GEKL 448
|
490 500 510
....*....|....*....|....*....|....*...
gi 242022874 494 NLQEFDEKLKKMLPSYARpLF--VRIIKNLPLTGTYKL 529
Cdd:cd05911 449 TEKEVKDYVAKKVASYKQ-LRggVVFVDEIPKSASGKI 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
29-534 |
7.52e-45 |
|
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: 165.95 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 29 NISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALI 108
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 109 ----YSSELSEGVKEILGELKDIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKAnlidevnagKPRDKLLFIYTSGTTG 184
Cdd:cd05926 92 tpkgELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVP---------LPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 185 LPKAaVINNNRYLFISI-GVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTV 263
Cdd:cd05926 163 RPKG-VPLTHRNLAASAtNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 264 ACYIGEICRYLLAVPEkSHDKQHKIRLMF----GNGLKAQIWEKFVERFQIKQIgEFYGATEG----NSNLVNID-NKVG 334
Cdd:cd05926 242 YTAVPTIHQILLNRPE-PNPESPPPKLRFirscSASLPPAVLEALEATFGAPVL-EAYGMTEAahqmTSNPLPPGpRKPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 335 CVGFvprlagpvyPVVllkvdkdTEEPIRNSKGfcIRCQPGEPG-ICV-GKINSKqtistflGYADKVESEKkilKNVFK 412
Cdd:cd05926 320 SVGK---------PVG-------VEVRILDEDG--EILPPGVVGeICLrGPNVTR-------GYLNNPEANA---EAAFK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 413 kgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDES 492
Cdd:cd05926 372 --DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 242022874 493 VNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05926 450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
59-551 |
9.43e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 166.36 E-value: 9.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 59 IALYMENSIEyMCIWLGLAKL-GIVSALINTNLRNQSFLHSLKAAKCNALIYSSE---LSEGVkeilgELKDIKLYIlnk 134
Cdd:PRK13388 55 VGVLLGNTPE-MLFWLAAAALgGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEhrpLLDGL-----DLPGVRVLD--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 135 skegeeTNLGEAIDLKKGLAEVSKANLIDevnagkPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDI 214
Cdd:PRK13388 126 ------VDTPAYAELVAAAGALTPHREVD------AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 215 LYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGN 294
Cdd:PRK13388 194 CYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGN 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 295 GLKAQIWEKFVERFQIkQIGEFYGATEGNSNLVNIDnkvgcvGFVPRLAGPVYPVVLLkVDKDTEEPirnskgfCIRCQP 374
Cdd:PRK13388 274 EASPRDIAEFSRRFGC-QVEDGYGSSEGAVIVVREP------GTPPGSIGRGAPGVAI-YNPETLTE-------CAVARF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 375 GEPGI------CVGKINSKQTISTFLGY-------ADKVEsekkilknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDT 441
Cdd:PRK13388 339 DAHGAllnadeAIGELVNTAGAGFFEGYynnpeatAERMR-------------HGMYWSGDLAYRDADGWIYFAGRTADW 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 442 FRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVeGKAGMVAI--HDvDESVNLQEFDEKLKKM--LPSYARPLFVRI 517
Cdd:PRK13388 406 MRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV-GDQVMAALvlRD-GATFDPDAFAAFLAAQpdLGTKAWPRYVRI 483
|
490 500 510
....*....|....*....|....*....|....
gi 242022874 518 IKNLPLTGTYKLKKKELQMEGfniTKIKDPVYFY 551
Cdd:PRK13388 484 AADLPSTATNKVLKRELIAQG---WATGDPVTLW 514
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
7-534 |
4.05e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 164.20 E-value: 4.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEETN--LGEAIDLKKGLAEVSKANLIDE 164
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLApeVGEYEELLAAASDTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 165 vnagkpRDKLLFIYTSGTTGLPKAAVInNNRYLFI-SIGVKILLKLHDDDILYNSLPLYH--TSGVIVGAgqsILSGITV 241
Cdd:PRK06187 167 ------NDAAAMLYTSGTTGHPKGVVL-SHRNLFLhSLAVCAWLKLSRDDVYLVIVPMFHvhAWGLPYLA---LMAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 242 VIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIkQIGEFYGA 319
Cdd:PRK06187 237 VIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGI-DLVQGYGM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 320 TEgNSNLVNI---DNKVGCVGFVPRLAGPVYPVVLLKVDKDTEEPIRNSKGfcircQPGEpgICVgkinskQTISTFLGY 396
Cdd:PRK06187 316 TE-TSPVVSVlppEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGG-----EVGE--IIV------RGPWLMQGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 397 -ADKVESEKKILknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV--- 472
Cdd:PRK06187 382 wNRPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpde 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 473 ---EVPH--VEGKAGmvaiHDVDEsvnlQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK06187 455 kwgERPVavVVLKPG----ATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
8-535 |
1.41e-42 |
|
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: 158.88 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 8 VAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALIN 87
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 88 TNLRNQSFLHSLKAAKCNALIysselsegvkeilgelkdiklyilnkskegeeTNLGEAIDLKKGLAEVSKANLidevna 167
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALI--------------------------------VAVSFTDLLAAGAPLGERVAL------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 168 gKPRDKLLFIYTSGTTGLPKAAVINNnRYLFISI-GVKILLK--LHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIR 244
Cdd:cd05936 123 -TPEDVAVLQYTSGTTGVPKGAMLTH-RNLVANAlQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 245 KKFSASNFWQDCIKYNCTVAC-----YIGeicryLLAVPEKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKqIGEFY 317
Cdd:cd05936 201 PRFRPIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 318 GATE----GNSNLVNIDNKVGCVGFvprlagPVyPVVLLK-VDKDTEEPirnskgfcircQPGEPG-ICV-GKinskqti 390
Cdd:cd05936 275 GLTEtspvVAVNPLDGPRKPGSIGI------PL-PGTEVKiVDDDGEEL-----------PPGEVGeLWVrGP------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 391 STFLGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVF 470
Cdd:cd05936 330 QVMKGYWNRPEETAEAFV------DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVV 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242022874 471 GV------EVPHVegkagMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05936 404 GVpdpysgEAVKA-----FVVLKE-GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
7-535 |
8.75e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.54 E-value: 8.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENI-----SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGI 81
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 82 VSALINTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGE----LKDIklyILNKSKEGEETNlgeAIDLKKGLAEvs 157
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdatpLRHI---CLTRVALPADDG---VSSFTQLKAQ-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 158 KANLIDEVNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILS 237
Cdd:PRK08008 160 QPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 238 GITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIR-LMFGNGLKAQIWEKFVERFQIKQIGEf 316
Cdd:PRK08008 240 GATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLReVMFYLNLSDQEKDAFEERFGVRLLTS- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEgnsnlvnidNKVGCVGfvprlagpvypvvllkvDKDTEE---PIRNSKGFCIRCQ----------PGEPG-ICVG 382
Cdd:PRK08008 319 YGMTE---------TIVGIIG-----------------DRPGDKrrwPSIGRPGFCYEAEirddhnrplpAGEIGeICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 383 KINSKqTIstFLGYADKVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNII 462
Cdd:PRK08008 373 GVPGK-TI--FKEYYLDPKATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHP 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 463 GYKDAIVFGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK08008 445 KIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
21-531 |
2.79e-41 |
|
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: 154.69 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLrnqsflhslk 100
Cdd:cd17631 10 DRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 aakcnaliysselseGVKEILgelkdiklYILNKSKegeetnlgeaidlkkglAEVskanLIDevnagkprDKLLFIYTS 180
Cdd:cd17631 80 ---------------TPPEVA--------YILADSG-----------------AKV----LFD--------DLALLMYTS 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 181 GTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYN 260
Cdd:cd17631 108 GTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 261 CTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNG------LKAQIWEKFVErfqikqIGEFYGATE---GNSNLVNIDN 331
Cdd:cd17631 188 VTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapmperLLRALQARGVK------FVQGYGMTEtspGVTFLSPEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 332 --KVGCVGFvprlagPVYPVVLLKVDKDTEEpirnskgfcirCQPGEPG-ICVgkinskQTISTFLGYADKVESEKKILK 408
Cdd:cd17631 262 rrKLGSAGR------PVFFVEVRIVDPDGRE-----------VPPGEVGeIVV------RGPHVMAGYWNRPEATAAAFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 409 nvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVE-GKAGMvAIH 487
Cdd:cd17631 319 ------DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVV-AVV 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 242022874 488 DVDESVNL--QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKK 531
Cdd:cd17631 390 VPRPGAELdeDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
21-547 |
4.20e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 156.43 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQEN-----ISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSF 95
Cdd:COG0365 24 DKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 96 LHSLKAAKCNALIYSSELSEG---------VKEILGELKDIKLYILNKsKEGEETNLGEAIDLKKGLAEVSKANLIDEVN 166
Cdd:COG0365 104 ADRIEDAEAKVLITADGGLRGgkvidlkekVDEALEELPSLEHVIVVG-RTGADVPMEGDLDWDELLAAASAEFEPEPTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPrdklLFI-YTSGTTGLPKAAVINNNRYL-FISIGVKILLKLHDDDILYNSLPL---YHTSGVIVGAgqsILSGITV 241
Cdd:COG0365 183 ADDP----LFIlYTSGTTGKPKGVVHTHGGYLvHAATTAKYVLDLKPGDVFWCTADIgwaTGHSYIVYGP---LLNGATV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 242 VI---RKKF-SASNFWQDCIKYNCTVAC----YIgeicRYLLAVPE---KSHDKQHkIRLMFGNG--LKAQIWEKFVERF 308
Cdd:COG0365 256 VLyegRPDFpDPGRLWELIEKYGVTVFFtaptAI----RALMKAGDeplKKYDLSS-LRLLGSAGepLNPEVWEWWYEAV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 309 QIkQIGEFYGATEGN----SNLVNIDNKVGCVGfvprLAGPVYPVVLlkVDKDTEEpirnskgfcirCQPGEPG-ICVgk 383
Cdd:COG0365 331 GV-PIVDGWGQTETGgifiSNLPGLPVKPGSMG----KPVPGYDVAV--VDEDGNP-----------VPPGEEGeLVI-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 384 inSKQTISTFLGYADKvesEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIG 463
Cdd:COG0365 391 --KGPWPGMFRGYWND---PERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 464 YKDAIVFGveVPHVEGKAGMVAI------HDVDESV--NLQEFdekLKKMLPSYARPLFVRIIKNLPLTGT-----YKLK 530
Cdd:COG0365 466 VAEAAVVG--VPDEIRGQVVKAFvvlkpgVEPSDELakELQAH---VREELGPYAYPREIEFVDELPKTRSgkimrRLLR 540
|
570
....*....|....*..
gi 242022874 531 KKELQMEGFNITKIKDP 547
Cdd:COG0365 541 KIAEGRPLGDTSTLEDP 557
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
21-534 |
7.61e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 137.40 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIE-YMCIwLGLAKLGIVSALINTNLRNQSFLHSL 99
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEmILVI-HALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 100 KAAKCNALI----YSSELSEGVKEILGELKDiklyilnksKEGEETNLGEAIDLkkglaevskanliDEVNAgkprdkll 175
Cdd:PRK03640 96 DDAEVKCLItdddFEAKLIPGISVKFAELMN---------GPKEEAEIQEEFDL-------------DEVAT-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 176 FIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVgAGQSILSGITVVIRKKFSASNFWQD 255
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLVEKFDAEKINKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 256 CIKYNCTVACYIGEICRYLLAVPEKSHDKQHkIRLMF-GNGLKAQiweKFVERFQIKQIGEF--YGATEGNSNLVNID-- 330
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLERLGEGTYPSS-FRCMLlGGGPAPK---PLLEQCKEKGIPVYqsYGMTETASQIVTLSpe 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 331 ---NKVGCVGfvprlaGPVYPVVLlKVDKDTEEpirnskgfcirCQPGEPG-ICVgkinskQTISTFLGYADKVESEKKI 406
Cdd:PRK03640 301 dalTKLGSAG------KPLFPCEL-KIEKDGVV-----------VPPFEEGeIVV------KGPNVTKGYLNREDATRET 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 407 LKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEvphvEGKAGMVAI 486
Cdd:PRK03640 357 FQ------DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVP----DDKWGQVPV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 242022874 487 HDV--DESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK03640 427 AFVvkSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
32-534 |
1.21e-34 |
|
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: 135.93 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSS 111
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 ElsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevnagkprDKLLFIYTSGTTGLPKAaVI 191
Cdd:cd05972 81 E-----------------------------------------------------------DPALIYFTSGTTGLPKG-VL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 192 NNNRYLFISI-GVKILLKLHDDDILYNSlplyHTSGVIVGAGQSILS----GITVVI--RKKFSASNFWQDCIKYNCTVA 264
Cdd:cd05972 101 HTHSYPLGHIpTAAYWLGLRPDDIHWNI----ADPGWAKGAWSSFFGpwllGATVFVyeGPRFDAERILELLERYGVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 265 CYIGEICRYLLAVPEKSHDKQHkIRLMFGNG--LKAQIWEKFVERFQIKqIGEFYGATEGN---SNLVNIDNKVGCVGFv 339
Cdd:cd05972 177 CGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATGLP-IRDGYGQTETGltvGNFPDMPVKPGSMGR- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 340 prlAGPVYPVVLLkvDKDTEEpirnskgfcirCQPGEPG-ICVgKINskqTISTFLGYA-DKVESEKKIlknvfkkGDNY 417
Cdd:cd05972 254 ---PTPGYDVAII--DDDGRE-----------LPPGEEGdIAI-KLP---PPGLFLGYVgDPEKTEASI-------RGDY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 418 FNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPhVEG---KAGMVAIHDVDESVN 494
Cdd:cd05972 307 YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGevvKAFVVLTSGYEPSEE 385
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 242022874 495 L-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05972 386 LaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
33-562 |
1.24e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 136.77 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNlrnqsflhslkaakcnaliysSE 112
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD---------------------TD 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKeiLGELKDIKlyilnkskeGEETNLGEAIDL-----------KKGLAEVSKANLID---------------EVN 166
Cdd:PRK07868 533 LAAAVR--LGGVTEII---------TDPTNLEAARQLpgrvlvlgggeSRDLDLPDDADVIDmekidpdavelpgwyRPN 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPRDkLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKK 246
Cdd:PRK07868 602 PGLARD-LAFIAFSTAGGELVAKQITNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRG 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNL 326
Cdd:PRK07868 681 LDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVL 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 327 VNIDN-KVGCVGfvPRLAGPVyPVVLLKVDKDTEEPIRNSKGFCIRCQPGEPGICVGKINskqtistflGYADKVESekk 405
Cdd:PRK07868 761 ANVSGaKIGSKG--RPLPGAG-RVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARAR---------GPIDPTAS--- 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 406 ILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVA 485
Cdd:PRK07868 826 VKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAAVT 905
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 486 IHDvDESVNLQEFDEKLKKMLPSYaRPLFVRIIKNLPLTGTYKLKKKELQMEGfnITKIKDPVYFYDNRSQKFELLS 562
Cdd:PRK07868 906 LRP-GAAITAADLTEALASLPVGL-GPDIVHVVPEIPLSATYRPTVSALRAAG--IPKPGRQAWYFDPETNRYRRLT 978
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
21-534 |
1.97e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 133.45 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSL 99
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 100 KAAKCNALIYSSELSEGVKEILGElkdiklyilnkskegeeTNLGEAIDLKkGLAEVSKANLIDEVNAGKPRdKLLFIYT 179
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKV-----------------SYVQRVISIT-SLKEIEDRKIDNFVEKNESA-SFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 180 SGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKY 259
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 260 NCTVACYIGEICRYLLAVPEKSHDKQHKIRlMFGNGlKAQIWEKFVERFQIK--QIGEFYGATEGNSNLVNIDN-----K 332
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFETTNLQSVR-WFYNG-GAPCPEELMREFIDRgfLFGQGFGMTETSPTVFMLSEedarrK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 333 VGCVGfvprlagpvYPVVLLKVdkdteEPIRNSKGfciRCQPGEpgicVGKINSKQTiSTFLGYADKVESEKKILKnvfk 412
Cdd:PRK06839 316 VGSIG---------KPVLFCDY-----ELIDENKN---KVEVGE----VGELLIRGP-NVMKEYWNRPDATEETIQ---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 413 kgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVegKAGMVAIHDV--- 489
Cdd:PRK06839 370 --DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHV--KWGEIPIAFIvkk 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 242022874 490 -DESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK06839 444 sSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
31-534 |
1.43e-30 |
|
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: 124.00 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRnqsflhslkaakcnaliys 110
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLT------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 selsegVKEILGELKDiklyilnkskegeetnlgeaidlkkglAEVSKanliDEVNAgkprdkllFIYTSGTTGLPKAAV 190
Cdd:cd05912 62 ------PNELAFQLKD---------------------------SDVKL----DDIAT--------IMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 INNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSG--VIVgagQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIG 268
Cdd:cd05912 97 QTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGlsILM---RSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 269 EICRYLLAV-PEKSHDKQHKIrLMFGNGLKAQIWEKFVER-FQIKQIgefYGATEGNSNLVNID-----NKVGCVGfvpr 341
Cdd:cd05912 174 TMLQRLLEIlGEGYPNNLRCI-LLGGGPAPKPLLEQCKEKgIPVYQS---YGMTETCSQIVTLSpedalNKIGSAG---- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 342 laGPVYPVVLlKVDKDTEEPIrnskgfcircQPGEpgICVGKINSKQtistflGYADKVESEKKILKNvfkkgdNYFNSG 421
Cdd:cd05912 246 --KPLFPVEL-KIEDDGQPPY----------EVGE--ILLKGPNVTK------GYLNRPDATEESFEN------GWFKTG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 422 DILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGvevpHVEGKAGMVAIHDV--DESVNLQEFD 499
Cdd:cd05912 299 DIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG----IPDDKWGQVPVAFVvsERPISEEELI 374
|
490 500 510
....*....|....*....|....*....|....*
gi 242022874 500 EKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05912 375 AYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
6-534 |
3.20e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 124.66 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 6 STVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSAL 85
Cdd:PRK08316 11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 INTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEETnlGEAIDLKKGLAEVSKANLIDEV 165
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAP--GGWLDFADWAEAGSVAEPDVEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 166 NAGkprDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRK 245
Cdd:PRK08316 169 ADD---DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 246 KFSASNFWQDCIKYNC-------TVacYIGeicryLLAVPE-KSHDKQHKIRLMFGNG-LKAQIWEKFVERFQIKQIGEF 316
Cdd:PRK08316 246 APDPELILRTIEAERItsffappTV--WIS-----LLRHPDfDTRDLSSLRKGYYGASiMPVEVLKELRERLPGLRFYNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEgnsnlvnidnkVGCVGFV---------PRLAG-PVYPVVLLKVDKDTEEPIrnskgfcircqPGEPGICVGKinS 386
Cdd:PRK08316 319 YGQTE-----------IAPLATVlgpeehlrrPGSAGrPVLNVETRVVDDDGNDVA-----------PGEVGEIVHR--S 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 387 KQTIstfLGYADKVESEKKilknVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKD 466
Cdd:PRK08316 375 PQLM---LGYWDDPEKTAE----AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242022874 467 AIVFGVEVPH-VEGKAGMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK08316 446 VAVIGLPDPKwIEAVTAVVVPKA-GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
175-534 |
1.39e-27 |
|
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: 115.46 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 175 LFIYTSGTTGLPKAAV-----INNNrylfisigVKILLKL---HDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKK 246
Cdd:cd05941 93 LILYTSGTTGRPKGVVlthanLAAN--------VRALVDAwrwTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKsHDKQ---------HKIRLMF-GNG-LKAQIWEKFVERFQiKQIGE 315
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEA-HFTDpqfaraaaaERLRLMVsGSAaLPVPTLEEWEAITG-HTLLE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 316 FYGATEGN---SNLVNIDNKVGCVGFvPrLAGpvypVVLLKVDKDTEEPIRNSKgfcircqPGEpgICVgkinskQTIST 392
Cdd:cd05941 243 RYGMTEIGmalSNPLDGERRPGTVGM-P-LPG----VQARIVDEETGEPLPRGE-------VGE--IQV------RGPSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 393 FLGYADKVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTG-DTFRWKGENVATSEVEAVISNIIGYKDAIVFG 471
Cdd:cd05941 302 FKEYWNKPEATKEEF-----TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIG 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 472 veVPHV---EGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05941 377 --VPDPdwgERVVAVVVLRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
7-537 |
4.32e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.23 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQEN-ISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSAL 85
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 INTNLRNQSFLHSLKaaKCNALIY-------SSELSEGVKEILGELKDIKlYILNKSKEGEETNlgeAIDLKKGLAevSK 158
Cdd:PRK06087 104 LLPSWREAELVWVLN--KCQAKMFfaptlfkQTRPVDLILPLQNQLPQLQ-QIVGVDKLAPATS---SLSLSQIIA--DY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 159 ANLIDEVNAGKprDKLLFI-YTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILS 237
Cdd:PRK06087 176 EPLTTAITTHG--DELAAVlFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 238 GITVVIRKKFSASNfwqdCI----KYNCTvaCYIGE--ICRYLLAVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERFQIK 311
Cdd:PRK06087 254 GARSVLLDIFTPDA----CLalleQQRCT--CMLGAtpFIYDLLNLLEKQPADLSALRFFLCGG--TTIPKKVARECQQR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 312 QIG--EFYGATEGNSN-LVNIDNkvgCVGFVPRLAGPVYPVVLLKVDKDTEEPIrnskgfcircQPGEPGicvgkinskQ 388
Cdd:PRK06087 326 GIKllSVYGSTESSPHaVVNLDD---PLSRFMHTDGYAAAGVEIKVVDEARKTL----------PPGCEG---------E 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 389 TIS----TFLGYADKVESEKKILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGY 464
Cdd:PRK06087 384 EASrgpnVFMGYLDEPELTARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 465 KDAIVFGVEVPHV-EGKAGMVAIHDVDESVNLQEFDEKL-KKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQME 537
Cdd:PRK06087 459 HDACVVAMPDERLgERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
21-534 |
6.59e-27 |
|
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: 114.39 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLK 100
Cdd:cd05959 19 DKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKAnlidevNAGKPRDKLLFIYTS 180
Cdd:cd05959 99 DSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKP------AATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 181 GTTGLPKAAV-INNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVivgaGQSIL----SGITVVIRKKFSASNFWQD 255
Cdd:cd05959 173 GSTGRPKGVVhLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGL----GNSLTfplsVGATTVLMPERPTPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 256 CIK-YNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIkQIGEFYGATEGN----SNLVN 328
Cdd:cd05959 249 RIRrYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGIGSTEMLhiflSNRPG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 329 iDNKVGCVGfvprLAGPVYPVVLlkVDKDTEEpirnskgfcirCQPGEPGICVGKINSKQTistflGYADKVESEKKilk 408
Cdd:cd05959 328 -RVRYGTTG----KPVPGYEVEL--RDEDGGD-----------VADGEPGELYVRGPSSAT-----MYWNNRDKTRD--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 409 nVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPH--VEGKAGMVAI 486
Cdd:cd05959 382 -TFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDglTKPKAFVVLR 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 242022874 487 HDVDESVNLQ-EFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05959 459 PGYEDSEALEeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
7-535 |
3.47e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 109.22 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEETNLGEaIDLKKGLAEVSKANLIDEVN 166
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKM-KTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPRDkllFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKK 246
Cdd:PRK07656 165 PDDVAD---ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKQIGEFYGATE--G 322
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSEasG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 323 NSNLVNIDNKVGCvgfVPRLAGPVYPVVLLKVDKDTEEPIrnskgfcircQPGEPG-ICVGKINSKQtistflGY-ADKV 400
Cdd:PRK07656 322 VTTFNRLDDDRKT---VAGTIGTAIAGVENKIVNELGEEV----------PVGEVGeLLVRGPNVMK------GYyDDPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 401 ESEKKIlknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV------EV 474
Cdd:PRK07656 383 ATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVpderlgEV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 475 phveGKAGMVAIH--DVDESVNLQEFDEKLKKmlpsYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK07656 457 ----GKAYVVLKPgaELTEEELIAYCREHLAK----YKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
21-535 |
2.71e-24 |
|
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: 106.81 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAF-----HQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSF 95
Cdd:cd05970 32 DKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 96 LHSLKAAKCNALIYSSE--LSEGVKEILGEL--KDIKLYILNKSKEGeetnlgeAIDLKKGLAEVSKANLIDEVNAGKPR 171
Cdd:cd05970 112 VYRIESADIKMIVAIAEdnIPEEIEKAAPECpsKPKLVWVGDPVPEG-------WIDFRKLIKNASPDFERPTANSYPCG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIY-TSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDIlynslplyHTSGVIVGAGQSI--------LSGITVV 242
Cdd:cd05970 185 EDILLVYfSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGL--------HLTVADTGWGKAVwgkiygqwIAGAAVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 I--RKKFSASNFWQDCIKYNCTVACYIGEICRYLlaVPEK-SHDKQHKIR--LMFGNGLKAQIWEKFVERFQIKqIGEFY 317
Cdd:cd05970 257 VydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFL--IREDlSRYDLSSLRycTTAGEALNPEVFNTFKEKTGIK-LMEGF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 318 GATEGN---SNLVNIDNKVGCVGfvprLAGPVYPVVLLKVDKDTeepirnskgfcirCQPGEPGICVGKINSKQTISTFL 394
Cdd:cd05970 334 GQTETTltiATFPWMEPKPGSMG----KPAPGYEIDLIDREGRS-------------CEAGEEGEIVIRTSKGKPVGLFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 395 GYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEV 474
Cdd:cd05970 397 GYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 475 PhVEG---KAGMVAIHDVDESVNL-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05970 471 P-IRGqvvKATIVLAKGYEPSEELkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
31-534 |
3.59e-24 |
|
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: 105.25 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS 110
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevnagkprDKLLFIYTSGTTGLPKAAV 190
Cdd:cd05935 81 SELD---------------------------------------------------------DLALIPYTSGTTGLPKGCM 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 INNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEI 270
Cdd:cd05935 104 HTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 271 CRYLLAVPEKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKQIgEFYGATEGNSNL-VN--IDNKVGCVGFvprlagP 345
Cdd:cd05935 184 LVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTETMSQThTNppLRPKLQCLGI------P 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 346 VYPVVLLKVDKDTEEPIrnskgfcircQPGEPGICVgkINSKQtisTFLGYADKVESEKKILknVFKKGDNYFNSGDILV 425
Cdd:cd05935 257 *FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQ---IFKGYWNRPEETEESF--IEIKGRRFFRTGDLGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 426 MDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHV--EGKAGMVAIHDVDESVNLQEFDEKLK 503
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVgeEVKAFIVLRPEYRGKVTEEDIIEWAR 399
|
490 500 510
....*....|....*....|....*....|.
gi 242022874 504 KMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05935 400 EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
22-535 |
5.74e-24 |
|
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: 104.85 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 22 KIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKA 101
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 102 AKCNALIYSSElsegvkeilgelkdiklyilnkskegeetnlgeaidlkkglaevskanlidevnagkprDKLLFIYTSG 181
Cdd:cd05919 81 CEARLVVTSAD-----------------------------------------------------------DIAYLLYSSG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 182 TTGLPKAAV-INNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVivgaGQSIL----SGITVVIRKKF-SASNFWQD 255
Cdd:cd05919 102 TTGPPKGVMhAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGL----GNSLWfplaVGASAVLNPGWpTAERVLAT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 256 CIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIkQIGEFYGATEgnsnlvnidnkV 333
Cdd:cd05919 178 LARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGG-PILDGIGATE-----------V 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 334 GCVgFVPRLAGPVYPVVLLKVDKDTEEPIRNSKGFCIrcQPGEPGICVGKinskqTISTFLGYADKVESEKKILKnvfkk 413
Cdd:cd05919 246 GHI-FLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTI--PPGEEGDLLVR-----GPSAAVGYWNNPEKSRATFN----- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 414 gDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfgVEVPHVEG----KAGMVAIHDV 489
Cdd:cd05919 313 -GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGlsrlTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 242022874 490 DESVNL-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05919 390 APQESLaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
54-535 |
1.40e-23 |
|
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: 104.34 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 54 KKGDTIALYMENSIEYMCIWLGLAKLGIVSALIN--TNLRNQsfLHSLKAAKCNALIYSSELSEGVKEILGE--LKDIKL 129
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKVPVMLNytAGLREL--RACIKLAGIKTVLTSKQFIEKLKLHHLFdvEYDARI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 130 YILNKSKEgeetNLGEAIDLKKGLA---EVSKANLIDEVNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKIL 206
Cdd:cd05909 107 VYLEDLRA----KISKADKCKAFLAgkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 207 LKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRkkfsasnfwqdcikYNCTVACYIGEI-----CRYLLAVP--- 278
Cdd:cd05909 183 FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH--------------PNPLDYKKIPELiydkkATILLGTPtfl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 279 ----EKSHDKQHK-IRLMF--GNGLKAQIWEKFVERFQIkQIGEFYGATEGNS----NLVNIDNKVGCVGfvprlaGPVY 347
Cdd:cd05909 249 rgyaRAAHPEDFSsLRLVVagAEKLKDTLRQEFQEKFGI-RILEGYGTTECSPvisvNTPQSPNKEGTVG------RPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 348 PVVLLKVDKDTEEPIRNskgfcircqpGEPGICVGKINSKqtistFLGYADKVEsekkilKNVFKKGDNYFNSGDILVMD 427
Cdd:cd05909 322 GMEVKIVSVETHEEVPI----------GEGGLLLVRGPNV-----MLGYLNEPE------LTSFAFGDGWYDTGDIGKID 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 428 DYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGyKDAIVFGVEVPHveGKAG--MVAIHDvDESVNLQEFDEKLKKM 505
Cdd:cd05909 381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILP-EDNEVAVVSVPD--GRKGekIVLLTT-TTDTDPSSLNDILKNA 456
|
490 500 510
....*....|....*....|....*....|.
gi 242022874 506 -LPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05909 457 gISNLAKPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-548 |
6.61e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.54 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDK--IAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSA 84
Cdd:PRK12583 19 TIGDAFDATVARFPDReaLVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 85 LINTNLRNQSFLHSLKAAKCNALIY-----SSELSEGVKEILGELKDIKLYILNKSK----------EGEETNLGEAIDL 149
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGALACERlpelrgvvslAPAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 150 KKGLAEVSKANLIDEVNAGKPRDKLLFI-YTSGTTGLPKAAV-----INNNRYLfisigVKILLKLHDDDILYNSLPLYH 223
Cdd:PRK12583 179 LQARGETVSREALAERQASLDRDDPINIqYTSGTTGFPKGATlshhnILNNGYF-----VAESLGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 224 TSGVIVGAGQSILSGITVVIRkkfsasnfwQDCIKYNCTVACYIGEICRYLLAVP-----EKSHDKQHKIRL-------M 291
Cdd:PRK12583 254 CFGMVLANLGCMTVGACLVYP---------NEAFDPLATLQAVEEERCTALYGVPtmfiaELDHPQRGNFDLsslrtgiM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 292 FGNGLKAQIWEKFVERFQIKQIGEFYGATEGN--SNLV----NIDNKVGCVGFV-PRLAGPVypvvllkVDKDTEEpirn 364
Cdd:PRK12583 325 AGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSpvSLQTtaadDLERRVETVGRTqPHLEVKV-------VDPDGAT---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 365 skgfcirCQPGEPG-ICVgkinskQTISTFLGYADKVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFR 443
Cdd:PRK12583 394 -------VPRGEIGeLCT------RGYSVMKGYWNNPEATAESI-----DEDGWMHTGDLATMDEQGYVRIVGRSKDMII 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 444 WKGENVATSEVEAVISNIIGYKDAIVFGV-EVPHVEGKAGMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLP 522
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFGVpDEKYGEEIVAWVRLHP-GHAASEEELREFCKARIAHFKVPRYFRFVDEFP 534
|
570 580
....*....|....*....|....*.
gi 242022874 523 LTGTYKLKKkeLQMEGFNITKIKDPV 548
Cdd:PRK12583 535 MTVTGKVQK--FRMREISIEELALPV 558
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
32-534 |
1.00e-22 |
|
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: 100.97 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIyss 111
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 elsegvkeilgelkdiklyilnkskegeeTNLgeaidlkkglaevskanlidevnagkPRDKLLFIYTSGTTGLPKAAVi 191
Cdd:cd05971 84 -----------------------------TDG--------------------------SDDPALIIYTSGTTGPPKGAL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 192 NNNRYLFISI-GVKILLKL--HDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRK--KFSASNFWQDCIKYNCTVACY 266
Cdd:cd05971 108 HAHRVLLGHLpGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRmtKFDPKAALDLMSRYGVTTAFL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQI--WEKfvERFQIkQIGEFYGATEGN----SNLVNIDNKVGCVGf 338
Cdd:cd05971 188 PPTALKMMRQQGEQLKHAQVKLRAIAtgGESLGEELlgWAR--EQFGV-EVNEFYGQTECNlvigNCSALFPIKPGSMG- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 339 vprLAGPVYPVVLLKvDKDTEEPirnskgfcircqPGEPG-ICVGKINSKQtistFLGYADKVE-SEKKIlknvfkKGDn 416
Cdd:cd05971 264 ---KPIPGHRVAIVD-DNGTPLP------------PGEVGeIAVELPDPVA----FLGYWNNPSaTEKKM------AGD- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 417 YFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPhVEG---KAGMV---AIHDVD 490
Cdd:cd05971 317 WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP-IRGeivKAFVVlnpGETPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242022874 491 E-SVNLQEFdekLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05971 396 AlAREIQEL---VKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
6-534 |
3.83e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 100.09 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 6 STVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSAL 85
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 INTNLRNQSFLHSLKAAKCNALI----YSSELSE-----GVKEI----LGELKDIKLYILN-----KSKEGEETNLGEAI 147
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVvlenFATTVQQvlaktAVKHVvvasMGDLLGFKGHIVNfvvrrVKKMVPAWSLPGHV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 148 DLKKGLAEVSKANLiDEVNAGkPRDKLLFIYTSGTTGLPKAA------VINNNRYLFISIGVKILLKLHDDDILY-NSLP 220
Cdd:PRK07059 183 RFNDALAEGARQTF-KPVKLG-PDDVAFLQYTGGTTGVSKGAtllhrnIVANVLQMEAWLQPAFEKKPRPDQLNFvCALP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 221 LYHTSGVIVGAGQSI-LSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQ 299
Cdd:PRK07059 261 LYHIFALTVCGLLGMrTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 300 iwEKFVERFQIKQ---IGEFYGATE----GNSNLVNIDNKVGCVGFvprlagpvyPVvllkvdKDTEEPIRNSKGfciRC 372
Cdd:PRK07059 341 --RPVAERWLEMTgcpITEGYGLSEtspvATCNPVDATEFSGTIGL---------PL------PSTEVSIRDDDG---ND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 373 QP-GEPG-ICvgkINSKQTIStflGYADKVESEKKILKnvfkkGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVA 450
Cdd:PRK07059 401 LPlGEPGeIC---IRGPQVMA---GYWNRPDETAKVMT-----ADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 451 TSEVEAVISNIIGYKDAIVFGVEVPHvEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLK 530
Cdd:PRK07059 470 PNEIEEVVASHPGVLEVAAVGVPDEH-SGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKIL 548
|
....
gi 242022874 531 KKEL 534
Cdd:PRK07059 549 RREL 552
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
7-471 |
2.13e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 98.25 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQEN----ISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIV 82
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 83 SALINTNLRNQSFLHSLKAAKCNALIYSS-ELSEGVKEILGELKDIK-LYILNKSKEGEETNLGEAIDLKKGLAEVSKAN 160
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLRhIVVLDPRGLRDDPRLLSLDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 161 LIDE-VNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQsILSGI 239
Cdd:COG1022 172 ELEArRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 240 TVvirkkfsasNFWQDcIKyncTVACYIGEIcR--YLLAVP---EKSHDK------------------------QHKIRL 290
Cdd:COG1022 251 TV---------AFAES-PD---TLAEDLREV-KptFMLAVPrvwEKVYAGiqakaeeagglkrklfrwalavgrRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 291 MFGNG------LKAQIWEKFV-----ERF--QIK-----------QIGEF-----------YGATEgNSNLVNI----DN 331
Cdd:COG1022 317 LAGKSpslllrLKHALADKLVfsklrEALggRLRfavsggaalgpELARFfralgipvlegYGLTE-TSPVITVnrpgDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 332 KVGCVgfvprlaGPVYPVVLLKVDKDTEepIrnskgfCIRcqpgepGICVgkinskqtistFLGYadkvesekkiLKN-- 409
Cdd:COG1022 396 RIGTV-------GPPLPGVEVKIAEDGE--I------LVR------GPNV-----------MKGY----------YKNpe 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242022874 410 ----VFKKgDNYFNSGDILVMDDYGYFSFKDRTGDTFrwK---GENVATSEVEAVI--SNIIgyKDAIVFG 471
Cdd:COG1022 434 ataeAFDA-DGWLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALkaSPLI--EQAVVVG 499
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-535 |
3.30e-21 |
|
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: 95.04 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 178 YTSGTTGLPKAAV-----INNNRYLfisIGvkILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVI-RKKFSASN 251
Cdd:cd05917 9 FTSGTTGSPKGATlthhnIVNNGYF---IG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 252 FWQDCIKYNCTV-----ACYIGEicrylLAVPEKSHDKQHKIR--LMFGNGLKAQIWEKFVERFQIKQIGEFYGATEgNS 324
Cdd:cd05917 84 VLEAIEKEKCTAlhgvpTMFIAE-----LEHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTE-TS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 325 NLV-------NIDNKVGCVgfvprlaGPVYPVVLLK-VDKDT-EEPIRNSKG-FCIRcqpgepGICVgkinskqtistFL 394
Cdd:cd05917 158 PVStqtrtddSIEKRVNTV-------GRIMPHTEAKiVDPEGgIVPPVGVPGeLCIR------GYSV-----------MK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 395 GY-ADKVESEKKIlknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGve 473
Cdd:cd05917 214 GYwNDPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG-- 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 474 VPHV---EGKAGMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05917 286 VPDErygEEVCAWIRLKE-GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
26-535 |
2.85e-20 |
|
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: 94.45 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 26 HQENISWTYKQVNEYSNGIGHYF-KSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKC 104
Cdd:cd05928 36 KGDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 105 NALIYSSELSEGVKEILGELKDI--KLYILNKSKEGeetnlgeAIDLKKGLAEVSKANLIDEVnagKPRDKLLFIYTSGT 182
Cdd:cd05928 116 KCIVTSDELAPEVDSVASECPSLktKLLVSEKSRDG-------WLNFKELLNEASTEHHCVET---GSQEPMAIYFTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 183 TGLPKAAVINNNRY-LFISIGVKILLKLHDDDILYNSlplyHTSGVIVGAGQSILS----GITVVIRK--KFSASNFWQD 255
Cdd:cd05928 186 TGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNT----SDTGWIKSAWSSLFEpwiqGACVFVHHlpRFDPLVILKT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 256 CIKYNCTVACYIGEICRYLLAVPEKSHDKQH-KIRLMFGNGLKAQIWEKFVERFQIkQIGEFYGATE-----GNSNLVNI 329
Cdd:cd05928 262 LSSYPITTFCGAPTVYRMLVQQDLSSYKFPSlQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTEtglicANFKGMKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 330 dnKVGCVGfvprLAGPVYPVVLLKVDKDTEEPirnskgfcirCQPGEPGIcvgKINSKQTISTFLGYADKVESEKKILKN 409
Cdd:cd05928 341 --KPGSMG----KASPPYDVQIIDDNGNVLPP----------GTEGDIGI---RVKPIRPFGLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 410 vfkkgdNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVE-------AVI-SNIIGYKDAI------VFGVEVP 475
Cdd:cd05928 402 ------DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVEsaliehpAVVeSAVVSSPDPIrgevvkAFVVLAP 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 476 HVEGkagmvaiHDVDESVnlQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05928 476 QFLS-------HDPEQLT--KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-534 |
3.13e-20 |
|
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: 93.66 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVgAGQSILSGITVVIRKKFS- 248
Cdd:cd05922 116 HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVl 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 249 ASNFWQDCIKYNCTVAC---YIGEICRYLLAVPEKSHdkqhKIRLM--FGNGLKAQIWEKFVERFQIKQIGEFYGATEGN 323
Cdd:cd05922 195 DDAFWEDLREHGATGLAgvpSTYAMLTRLGFDPAKLP----SLRYLtqAGGRLPQETIARLRELLPGAQVYVMYGQTEAT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 324 SNLV-----NIDNKVGCVGfvPRLAGpvypvvllkvdkdTEEPIRNSKGFciRCQPGEPGICVgkiNSKQTIStfLGYAD 398
Cdd:cd05922 271 RRMTylppeRILEKPGSIG--LAIPG-------------GEFEILDDDGT--PTPPGEPGEIV---HRGPNVM--KGYWN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 399 KvesEKKILKNVFKKGDNYfnSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVE 478
Cdd:cd05922 329 D---PPYRRKEGRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 479 GKAGMVAIHDVDEsvnLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05922 404 KLALFVTAPDKID---PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-537 |
3.94e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.80 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 18 KNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLH 97
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 98 SLKAAKCNALIYSSELSEGVKEIlgelkdIKLYILNKSKEGEETNLGEAidlkkGLAevskanlIDEVNAGKPRDKLLFI 177
Cdd:PRK06145 94 ILGDAGAKLLLVDEEFDAIVALE------TPKIVIDAAAQADSRRLAQG-----GLE-------IPPQAAVAPTDLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 178 YTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHtsgviVGA----GQSIL-SGITVVIRKKFSASNF 252
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYH-----VGAfdlpGIAVLwVGGTLRIHREFDPEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 253 WQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKA--QIWEKFVERFQIKQIGEFYGATE--GNSNLVN 328
Cdd:PRK06145 231 LAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpeSRIRDFTRVFTRARYIDAYGLTEtcSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 329 IDNKVGCVGFVPRlagpVYPVVLLKV-DKDTEEPIRNSKG-FCIRcqpgEPGICVGKIN-SKQTISTFLGyadkvesekk 405
Cdd:PRK06145 311 AGREIEKIGSTGR----ALAHVEIRIaDGAGRWLPPNMKGeICMR----GPKVTKGYWKdPEKTAEAFYG---------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 406 ilknvfkkgdNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVA 485
Cdd:PRK06145 373 ----------DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 242022874 486 IHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQME 537
Cdd:PRK06145 443 VLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
31-534 |
7.73e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 92.66 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS 110
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSEGVKEILGELKD--IKLYILNKSKEGEEtnlgeaiDLKKGLAEVSKANLIDEVnagkPRDKLLfiYTSGTTGLPKa 188
Cdd:PRK08276 91 AALADTAAELAAELPAgvPLLLVVAGPVPGFR-------SYEEALAAQPDTPIADET----AGADML--YSSGTTGRPK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 avinnnrylfisiGVKILL--------------------KLHDDDILYNSLPLYHTSgVIVGAGQSILSGITVVIRKKFS 248
Cdd:PRK08276 157 -------------GIKRPLpgldpdeapgmmlallgfgmYGGPDSVYLSPAPLYHTA-PLRFGMSALALGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 249 ASNFWQDCIKYNCTVACYIGEICRYLLAVPEK---SHDKQhKIRLMFGNG------LKAQI---WEKFVErfqikqigEF 316
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKLPEEvraRYDVS-SLRVAIHAAapcpveVKRAMidwWGPIIH--------EY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEGN-SNLVNIDN---KVGCVGfvprlaGPVYPVVLLkVDKDTEEpirnskgfcirCQPGEPGIcvgkINSKQTIST 392
Cdd:PRK08276 294 YASSEGGgVTVITSEDwlaHPGSVG------KAVLGEVRI-LDEDGNE-----------LPPGEIGT----VYFEMDGYP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 393 FLGYADkvesEKKILKNVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGv 472
Cdd:PRK08276 352 FEYHND----PEKTAAARNPHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG- 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 473 eVPHVE-G---KAgMVAIHD-VDESVNL-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK08276 425 -VPDEEmGervKA-VVQPADgADAGDALaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
33-472 |
8.92e-20 |
|
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: 92.57 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLrnqsflhslKAAKCNALIYSSE 112
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRL---------KAAELAELIERGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGV----KEILGELKDIKLYILNKSKE---GEETNLGEAIdlkkglaevskanlidEVNAGKPRDKLLFIYTSGTTGL 185
Cdd:cd05923 101 MTAAViavdAQVMDAIFQSGVRVLALSDLvglGEPESAGPLI----------------EDPPREPEQPAFVFYTSGTTGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 186 PKAAVINN----NRYLFISIGVKILLKLHddDILYNSLPLYHTSGVI-VGAGQSILSGITVVIRkKFSASNfwqdcikyn 260
Cdd:cd05923 165 PKGAVIPQraaeSRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIGFFaVLVAALALDGTYVVVE-EFDPAD--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 261 cTVACYIGEICRYLLAVPEKSHDKQHKI-----------RLMFGNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNI 329
Cdd:cd05923 233 -ALKLIEQERVTSLFATPTHLDALAAAAefaglklsslrHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 330 DNKVGCVG---------FVPRLAGPVYPVvllkvdkdteepirnskgfcircQPGEPGICVGKINSKqtiSTFLGYADKV 400
Cdd:cd05923 312 DARTGTEMrpgffsevrIVRIGGSPDEAL-----------------------ANGEEGELIVAAAAD---AAFTGYLNQP 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242022874 401 ESEKKilknvfKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV 472
Cdd:cd05923 366 EATAK------KLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
7-535 |
3.78e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSAL 85
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 INTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEI-------------LGELKDI-KLYILN-----KSKEGEETNLGEA 146
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQViadtpvkqvittgLGDMLGFpKAALVNfvvkyVKKLVPEYRINGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 147 IDLKKGLAEVSKANL----IDevnagkPRDKLLFIYTSGTTGLPKAAVINNNRYL--------FISIGVKILlklHDDDI 214
Cdd:PRK08751 186 IRFREALALGRKHSMptlqIE------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGTGKLE---EGCEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 215 LYNSLPLYHTSGVIV-GAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFG 293
Cdd:PRK08751 257 VITALPLYHIFALTAnGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 294 NGLKAQiwEKFVERFqiKQIG-----EFYGATEGNS----NLVNIDNKVGCVGF-VPRLAgpvypvVLLKVDKDTEEPIR 363
Cdd:PRK08751 337 GGMAVQ--RSVAERW--KQVTgltlvEAYGLTETSPaaciNPLTLKEYNGSIGLpIPSTD------ACIKDDAGTVLAIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 364 NSKGFCIRcqpgepGICVGKinskqtistflGYADKVESEKKILKnvfkkGDNYFNSGDILVMDDYGYFSFKDRTGDTFR 443
Cdd:PRK08751 407 EIGELCIK------GPQVMK-----------GYWKRPEETAKVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMIL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 444 WKGENVATSEVEAVISNIIGYKDaiVFGVEVPHVE-GKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLP 522
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLE--VAAVGVPDEKsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELP 542
|
570
....*....|...
gi 242022874 523 LTGTYKLKKKELQ 535
Cdd:PRK08751 543 KTNVGKILRRELR 555
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
52-537 |
4.81e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 90.63 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 52 GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSELSE-GVKEILGELKDIKLY 130
Cdd:PLN02860 53 GLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSwYEELQNDRLPSLMWQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 131 ILNKSKEGE---ETNLGEAIDLKKGLAEVSKanLIDEVNAgkPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILL 207
Cdd:PLN02860 133 VFLESPSSSvfiFLNSFLTTEMLKQRALGTT--ELDYAWA--PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 208 KLHDDDILYNSLPLYHTSGvIVGAGQSILSGITVVIRKKFSASNFWqDCIKYNCtVACYIG--EICRYLLAVPEKSHDKQ 285
Cdd:PLN02860 209 GYGEDDVYLHTAPLCHIGG-LSSALAMLMVGACHVLLPKFDAKAAL-QAIKQHN-VTSMITvpAMMADLISLTRKSMTWK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 286 --HKIRLMF--GNGLKAQIWEKFVERFQIKQIGEFYGATEGNSNLVNIdnkvgcVGFVPRLAGPvyPVVLLKVDKDTEEP 361
Cdd:PLN02860 286 vfPSVRKILngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFM------TLHDPTLESP--KQTLQTVNQTKSSS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 362 IRNSKGFCIrcqpGEP------GIC------VGKINSKQTiSTFLGYADKVESEKKILKNvfkkgDNYFNSGDILVMDDY 429
Cdd:PLN02860 358 VHQPQGVCV----GKPaphvelKIGldessrVGRILTRGP-HVMLGYWGQNSETASVLSN-----DGWLDTGDIGWIDKA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 430 GYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV-EVPHVEGKAGMVAIHD---------VDESVNLQEFD 499
Cdd:PLN02860 428 GNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVpDSRLTEMVVACVRLRDgwiwsdnekENAKKNLTLSS 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 242022874 500 EKLK-----KMLPSYARP-LFVRIIKNLPLTGTYKLKKKELQME 537
Cdd:PLN02860 508 ETLRhhcreKNLSRFKIPkLFVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
7-545 |
7.69e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 89.45 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGyKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIysselsegvkeilgelkdIKLYILNKSkEGEETNLGEaIDLKKGLAEVSKANLIDEVN 166
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIV------------------TERYKLNDL-PDEEGRVIE-IDEWKRMIEKYLPTYAPIEN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPRDKLLFiyTSGTTGLPKAAVINNNRYL--FISIGVKILLKlHDDDI-----LYNSLPLYhtsgvivGAGQSILSGI 239
Cdd:PRK07638 141 VQNAPFYMGF--TSGSTGKPKAFLRAQQSWLhsFDCNVHDFHMK-REDSVliagtLVHSLFLY-------GAISTLYVGQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 240 TVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLL---AVPEKSHdkqhKIrLMFGNGLKAQIWEKFVERFQIKQIGEF 316
Cdd:PRK07638 211 TVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYkenRVIENKM----KI-ISSGAKWEAEAKEKIKNIFPYAKLYEF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEGN--SNLVNIDNKVGcvgfvPRLAG-PVYPVVLlkvdkdteePIRNSKGfcIRCQPGEpgicVGKINSKQTIStF 393
Cdd:PRK07638 286 YGASELSfvTALVDEESERR-----PNSVGrPFHNVQV---------RICNEAG--EEVQKGE----IGTVYVKSPQF-F 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 394 LGYadKVESEKKILKNVfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVE 473
Cdd:PRK07638 345 MGY--IIGGVLARELNA----DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVP 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242022874 474 VPHVEGKagMVAIhdVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEGFNITKIK 545
Cdd:PRK07638 419 DSYWGEK--PVAI--IKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIY 486
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
10-537 |
1.28e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 89.32 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 10 KVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLG-LAKLGIVsalINT 88
Cdd:PRK06710 28 KYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGtLLAGGIV---VQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 89 N-------LRNQSFLHSLKAAKCNALIY--------SSELSEGVKEILGELKDIKLYILNKSKEGEETNLgeaidlkkgL 153
Cdd:PRK06710 105 NplytereLEYQLHDSGAKVILCLDLVFprvtnvqsATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNL---------V 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 154 AEVSKANLI-------DEVNAG-----KPRDKL-LFIYTSGTTGLPKAAVINNNRYLFISI-GVKILLKLHD-DDILYNS 218
Cdd:PRK06710 176 VKVSESETIhlwnsveKEVNTGvevpcDPENDLaLLQYTGGTTGFPKGVMLTHKNLVSNTLmGVQWLYNCKEgEEVVLGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 219 LPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNG--L 296
Cdd:PRK06710 256 LPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 297 KAQIWEKFvERFQIKQIGEFYGATEGN----SNLVNIDNKVGCVGfVPrlagpvYPvvllkvdkDTEEPIRN-SKGFCIR 371
Cdd:PRK06710 336 PVEVQEKF-ETVTGGKLVEGYGLTESSpvthSNFLWEKRVPGSIG-VP------WP--------DTEAMIMSlETGEALP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 372 cqPGEPGICVgkINSKQTIStflGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVAT 451
Cdd:PRK06710 400 --PGEIGEIV--VKGPQIMK---GYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 452 SEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKK 531
Cdd:PRK06710 467 REVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
|
....*.
gi 242022874 532 KELQME 537
Cdd:PRK06710 547 RVLIEE 552
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
7-535 |
1.39e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 89.11 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVsaL 85
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLI--V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 INTN--LRNQSFLHSLKAAKCNALIYSSELSEGVKEILGE-----LKDIKLYILNKSKEGEETN--------------LG 144
Cdd:PRK12492 103 VNTNplYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDtgieyLIEAKMGDLLPAAKGWLVNtvvdkvkkmvpayhLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 145 EAIDLKKGLAEvSKANLIDEVNAGKpRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDD----------I 214
Cdd:PRK12492 183 QAVPFKQALRQ-GRGLSLKPVPVGL-DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 215 LYNSLPLYHTSGVIVGAGQSILSGI-TVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPE-KSHDKQH-KIRLM 291
Cdd:PRK12492 261 MIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGfKDLDFSAlKLTNS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 292 FGNGL---KAQIWEKFVErfqiKQIGEFYGATE----GNSNLVNIDNKVGCVGFvprlagPVyPVVLLKV--DKDTEEPI 362
Cdd:PRK12492 341 GGTALvkaTAERWEQLTG----CTIVEGYGLTEtspvASTNPYGELARLGTVGI------PV-PGTALKVidDDGNELPL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 363 RNSKGFCIRcqpgepGICVGKinskqtistflGYADKVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTF 442
Cdd:PRK12492 410 GERGELCIK------GPQVMK-----------GYWQQPEATAEAL-----DAEGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 443 RWKGENVATSEVEAVISNIIGYKDAIVFGVEvPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLP 522
Cdd:PRK12492 468 IVSGFNVYPNEIEDVVMAHPKVANCAAIGVP-DERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLP 546
|
570
....*....|...
gi 242022874 523 LTGTYKLKKKELQ 535
Cdd:PRK12492 547 MTPVGKILRRELR 559
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
17-473 |
2.57e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.45 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 17 EKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFL 96
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 97 HSLKAAKCNALIYSSELSEGVKEILGELkdIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKANLidevnAGKPRDKLLF 176
Cdd:PRK07788 140 EVAAREGVKALVYDDEFTDLLSALPPDL--GRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPL-----PKPPKPGGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 177 IYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVivgaGQSILS---GITVVIRKKFSASNFW 253
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGW----AHLTLAmalGSTVVLRRRFDPEATL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 254 QDCIKYNCTVACYIGEICRYLLAVPEKSHDKQ--HKIRLMFGNGlkAQIWEKFVERFQiKQIGE----FYGATEgnsnlv 327
Cdd:PRK07788 289 EDIAKHKATALVVVPVMLSRILDLGPEVLAKYdtSSLKIIFVSG--SALSPELATRAL-EAFGPvlynLYGSTE------ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 328 nidnkvgcVGFV-----------PRLAGPvyPVVLLKV----DKDTEEPirnskgfcircqPGEPG-ICVGkiNSkqtiS 391
Cdd:PRK07788 360 --------VAFAtiatpedlaeaPGTVGR--PPKGVTVkildENGNEVP------------RGVVGrIFVG--NG----F 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 392 TFLGYADKveSEKKILknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFG 471
Cdd:PRK07788 412 PFEGYTDG--RDKQII-------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
..
gi 242022874 472 VE 473
Cdd:PRK07788 483 VD 484
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
178-529 |
3.53e-18 |
|
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: 85.53 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 178 YTSGTTGLPKAAVINNNRYL-FISIGVKILLkLHDDDILYNSLPLYHtSGVIVGAGQSILSGITVVIRKKFSASNFWQDC 256
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIeSFVCNEDLFN-ISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 257 IKYNCTVacyigeicryLLAVPEKSH------DKQHKIRLMF--GNGLKAQIWEKFVERFQIKQIGEFYGATEGN---SN 325
Cdd:cd17633 85 NQYNATV----------IYLVPTMLQalartlEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSELSfitYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVNIDNKVGCVGfvprlagPVYPVVLLKvdkdteepIRNSKGfcircqpGEPG-ICVgkiNSKQTistFLGYADKVESEK 404
Cdd:cd17633 155 FNQESRPPNSVG-------RPFPNVEIE--------IRNADG-------GEIGkIFV---KSEMV---FSGYVRGGFSNP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 405 kilknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVEGKAGMV 484
Cdd:cd17633 207 ----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG--IPDARFGEIAV 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 242022874 485 AIHDVDEsVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKL 529
Cdd:cd17633 275 ALYSGDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
31-536 |
4.13e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 88.09 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQ----VNEYSNgighYFKSQGYKKGDTIALYMENSIE-YMCIWLGLAKlGIVSAlINTNLRNQSFLHSLKAAKCN 105
Cdd:PRK07529 58 TWTYAElladVTRTAN----LLHSLGVGPGDVVAFLLPNLPEtHFALWGGEAA-GIANP-INPLLEPEQIAELLRAAGAK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 106 ALIY-----SSELSEGVKEILGELKDIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKANLIDEVnAGKPRDKLLF---- 176
Cdd:PRK07529 132 VLVTlgpfpGTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFDAEL-ARQPGDRLFSgrpi 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 177 --------IYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVI----- 243
Cdd:PRK07529 211 gpddvaayFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatpqg 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 244 -RKKFSASNFWQDCIKYNCTvaCYIGEICRY--LLAVPEKSHDkqhkI-RLMFGNGLKAQIWEKFVERFQIK---QIGEF 316
Cdd:PRK07529 291 yRGPGVIANFWKIVERYRIN--FLSGVPTVYaaLLQVPVDGHD----IsSLRYALCGAAPLPVEVFRRFEAAtgvRIVEG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEGNS----NLVNIDNKVGCVGFvpRLagPVYPVVLLKVDKDteepirnskGFCIR-CQPGEPG-ICVGKINskqti 390
Cdd:PRK07529 365 YGLTEATCvssvNPPDGERRIGSVGL--RL--PYQRVRVVILDDA---------GRYLRdCAVDEVGvLCIAGPN----- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 391 sTFLGYADkVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVE-------AV-ISNII 462
Cdd:PRK07529 427 -VFSGYLE-AAHNKGLW-----LEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEeallrhpAVaLAAAV 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 463 GYKDAivFGVEVP--HVEGKAGMvaihdvdeSVNLQEFDEKLKKMLPSYAR-PLFVRIIKNLPLTGTYKLKKKELQM 536
Cdd:PRK07529 500 GRPDA--HAGELPvaYVQLKPGA--------SATEAELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
32-187 |
6.27e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 86.86 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVsaLINTNLR--NQSFLHSLKAAKCNALIY 109
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV--PVNVNYRyvEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 110 SSELSEGVKEILGELKDIKLYILnKSKEGEETNLGEAIDLKKGLAEVSKANLIDEVNAgkprDKLLFIYTSGTTGLPK 187
Cdd:PRK07798 107 EREFAPRVAEVLPRLPKLRTLVV-VEDGSGNDLLPGAVDYEDALAAGSPERDFGERSP----DDLYLLYTGGTTGMPK 179
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
33-535 |
7.40e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 86.94 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSS 111
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 ELSEGVKEILGELK-----------------DIKLY-ILNKSKEGEETNLGEAIDLKKGLAEVSKANlidEVNAGkPRDK 173
Cdd:PRK08314 117 ELAPKVAPAVGNLRlrhvivaqysdylpaepEIAVPaWLRAEPPLQALAPGGVVAWKEALAAGLAPP---PHTAG-PDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 174 LLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKfsasnfW 253
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------W 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 254 Q-----DCI-KYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKQIgEFYGATEGNS- 324
Cdd:PRK08314 267 DreaaaRLIeRYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERLKELTGLDYV-EGYGLTETMAq 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 325 NLVNIDN--KVGCVGFvprlagPVYPVVLLKVDKDTEEPIrnskgfcircQPGEPGICVgkINSKQTistFLGYADKVES 402
Cdd:PRK08314 346 THSNPPDrpKLQCLGI------PTFGVDARVIDPETLEEL----------PPGEVGEIV--VHGPQV---FKGYWNRPEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 403 EKKilknVFKK--GDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHV--E 478
Cdd:PRK08314 405 TAE----AFIEidGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRgeT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 479 GKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK08314 481 VKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQ 537
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
32-534 |
7.44e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 86.40 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALIntnlrnqsflhslkaakcnaliYSS 111
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL----------------------FSA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 ELSEGVKEILgELKDIKLYILNKSkegeetnLGEAIDlkkglaevskanlidevnagkPRDKLLFIYTSGTTGLPKAAVI 191
Cdd:cd05969 59 FGPEAIRDRL-ENSEAKVLITTEE-------LYERTD---------------------PEDPTLLHYTSGTTGTPKGVLH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 192 NNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRK-KFSASNFWQDCIKYNCTVACYIGEI 270
Cdd:cd05969 110 VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 271 CRYLL---AVPEKSHDKQHkIRLMFGNG--LKAQIWEKFVERFQIKqIGEFYGATEGNS----NLVNIDNKVGCVGfvpr 341
Cdd:cd05969 190 IRMLMkegDELARKYDLSS-LRFIHSVGepLNPEAIRWGMEVFGVP-IHDTWWQTETGSimiaNYPCMPIKPGSMG---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 342 laGPVYPVVLLKVDKDTEEPIRNSKGFcIRCQPGEPgicvgkinskqtiSTFLGYADkvESEKkiLKNVFKKGdnYFNSG 421
Cdd:cd05969 264 --KPLPGVKAAVVDENGNELPPGTKGI-LALKPGWP-------------SMFRGIWN--DEER--YKNSFIDG--WYLTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 422 DILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPhVEG---KAGMVAIHDVDESVNLQ-E 497
Cdd:cd05969 322 DLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGeiiKAFISLKEGFEPSDELKeE 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 242022874 498 FDEKLKKMLPSYARPLFVRIIKNLPLTGTYK-----LKKKEL 534
Cdd:cd05969 401 IINFVRQKLGAHVAPREIEFVDNLPKTRSGKimrrvLKAKEL 442
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
12-534 |
1.94e-17 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 85.46 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 12 FQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLR 91
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 92 NQSFLHSLKAAKCNALIYSSELSEGvkeilgeLKDIKLYILNKSKEGEEtnlGEAIDLKkglaevskanlidevNAGKPR 171
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPP-------IAFIGLIDLLDEDTIYH---EESENLE---------------PVSKSD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIYTSGTTGLPKAAVIN----NNryLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVgagQSILSGITVVIRKKF 247
Cdd:cd17655 138 DLAYVIYTSGSTGKPKGVMIEhrgvVN--LVEWANKVIYQGEHLRVALFASISFDASVTEIF---ASLLSGNTLYIVRKE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 248 SASN---FWQDCIKYNCTVacyIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIK-QIGEFYGATE 321
Cdd:cd17655 213 TVLDgqaLTQYIRQNRITI---IDLTPAHLKLLDAADDSEGLSLKHLIvgGEALSTELAKKIIELFGTNpTITNAYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 322 gnsnlvnidNKVGCVgfvprlagpVYPVVLLKVDKDT---EEPIRNSKGFCI----RCQP-GEPG-ICVGKINSKQtist 392
Cdd:cd17655 290 ---------TTVDAS---------IYQYEPETDQQVSvpiGKPLGNTRIYILdqygRPQPvGVAGeLYIGGEGVAR---- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 393 flGYADKVE-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfg 471
Cdd:cd17655 348 --GYLNRPElTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV-- 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242022874 472 VEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARP-LFVRIIKnLPLTGTYKLKKKEL 534
Cdd:cd17655 424 IARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPsYFIKLDE-IPLTPNGKVDRKAL 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
30-535 |
2.42e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 84.86 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 30 ISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLrnqsflhslKAAKCNALIY 109
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL---------SASELDALLQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 110 SSElsegVKEILGElkdiklyilnkskEGEETNLGEAIDLKKGLAEVSKANLIDEVNAgkPRDKL-LFIYTSGTTGLPKA 188
Cdd:PRK09088 92 DAE----PRLLLGD-------------DAVAAGRTDVEDLAAFIASADALEPADTPSI--PPERVsLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 AVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACYIG 268
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 269 --EICRYLLAVPEKSHDKQHKIRLMFGNG-----------LKAQIweKFVERFQIKQIGEFYGATegnSNLVNIDNKVGC 335
Cdd:PRK09088 233 vpQMAQAFRAQPGFDAAALRHLTALFTGGaphaaedilgwLDDGI--PMVDGFGMSEAGTVFGMS---VDCDVIRAKAGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 336 VGfvprLAGPvyPVVLLKVDKDTEEpirnskgfcirCQPGEPGICVGKINSkqtisTFLGYADKVESEKKILKnvfkkGD 415
Cdd:PRK09088 308 AG----IPTP--TVQTRVVDDQGND-----------CPAGVPGELLLRGPN-----LSPGYWRRPQATARAFT-----GD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 416 NYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHvEGKAGMVAIHDVDES-VN 494
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ-WGEVGYLAIVPADGApLD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 242022874 495 LQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK09088 440 LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
21-472 |
2.50e-17 |
|
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: 85.27 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAF---HQEnISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLH 97
Cdd:cd17642 32 GTIAFtdaHTG-VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 98 SLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEgeetNLGEAIDLKKGLAEVSKANLIDE----VNAGKPRDK 173
Cdd:cd17642 111 SLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKE----DYKGYQCLYTFITQNLPPGFNEYdfkpPSFDRDEQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 174 LLFIYTSGTTGLPKAAVINNNRYL--FIS-----IGVKILlklhDDDILYNSLPLYHTSGVIVGAGQSILsGITVVIRKK 246
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIVarFSHardpiFGNQII----PDTAILTVIPFHHGFGMFTTLGYLIC-GFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCIKYNCTVACYIGEICRYLLAVP--EKsHDKQHKIRLMFGNG-LKAQIWEKFVERFQIKQIGEFYGATEGN 323
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlvDK-YDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 324 SNLV---NIDNKVGCVG-FVPRLAGPVypvvllkVDKDTEEPI-RNSKG-FCIRcqpgEPGICVGKINSKQTISTFLgya 397
Cdd:cd17642 341 SAILitpEGDDKPGAVGkVVPFFYAKV-------VDLDTGKTLgPNERGeLCVK----GPMIMKGYVNNPEATKALI--- 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 398 DKvesekkilknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV 472
Cdd:cd17642 407 DK---------------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
33-484 |
4.43e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 84.26 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKEiLGELKDIKLYILNKSKEG--EETNLGEAIDlkkglaevskaNLIDEVNAgKPRDKLLFIYTSGTTGLPKaAV 190
Cdd:PLN02246 132 YVDKLKG-LAEDDGVTVVTIDDPPEGclHFSELTQADE-----------NELPEVEI-SPDDVVALPYSSGTTGLPK-GV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 INNNRYLFISIGVKI-----LLKLHDDDILYNSLPLYHtsgviVGAGQSIL-----SGITVVIRKKFSASNFWQDCIKYN 260
Cdd:PLN02246 198 MLTHKGLVTSVAQQVdgenpNLYFHSDDVILCVLPMFH-----IYSLNSVLlcglrVGAAILIMPKFEIGALLELIQRHK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 261 CTVACYIGEIcryLLAV---PEKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKQIGEFYGATEGNSNLV-------- 327
Cdd:PLN02246 273 VTIAPFVPPI---VLAIaksPVVEKYDLSSIRMVLSGAapLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAmclafake 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 328 NIDNKVGCVGFVPRLAGpvypvvlLK-VDKDTEEPI-RNskgfcircQPGEpgICvgkINSKQTIStflGYADKVESEKK 405
Cdd:PLN02246 350 PFPVKSGSCGTVVRNAE-------LKiVDPETGASLpRN--------QPGE--IC---IRGPQIMK---GYLNDPEATAN 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242022874 406 ILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfgveVPHVEGKAGMV 484
Cdd:PLN02246 407 TIDK-----DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV----VPMKDEVAGEV 476
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-534 |
8.60e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 83.20 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKEILGELKDIKLYI-LNKSKEGEE-TNLGEAIdlkkglAEVSKANLIDEVNAGkprdklLFIYTSGTTGLPKAAV 190
Cdd:PRK13391 106 KLDVARALLKQCPGVRHRLvLDGDGELEGfVGYAEAV------AGLPATPIADESLGT------DMLYSSGTTGRPKGIK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 -------INNNRYLFisigvKILLKL--HDDDILYNS-LPLYHTSGV-IVGAGQSIlsGITVVIRKKFSASNFWQDCIKY 259
Cdd:PRK13391 174 rplpeqpPDTPLPLT-----AFLQRLwgFRSDMVYLSpAPLYHSAPQrAVMLVIRL--GGTVIVMEHFDAEQYLALIEEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 260 NCTVACYIGEICRYLLAVPEKSHDKQHKirlmfgNGLKAQIWEKFVERFQIKQ---------IGEFYGATEGNSNLVnID 330
Cdd:PRK13391 247 GVTHTQLVPTMFSRMLKLPEEVRDKYDL------SSLEVAIHAAAPCPPQVKEqmidwwgpiIHEYYAATEGLGFTA-CD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 331 N-----KVGCVGFVprLAGpvypvVLLKVDKDTEEpirnskgfcirCQPGEPGicvgkinskqTIstflgyadkvesekk 405
Cdd:PRK13391 320 SeewlaHPGTVGRA--MFG-----DLHILDDDGAE-----------LPPGEPG----------TI--------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 406 ilknVFKKGD--NYFN-----------------SGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKD 466
Cdd:PRK13391 357 ----WFEGGRpfEYLNdpaktaearhpdgtwstVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAD 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 467 AIVFGveVPH----VEGKAGMVAIHDVDESVNL-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK13391 433 AAVFG--VPNedlgEEVKAVVQPVDGVDPGPALaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
31-534 |
2.19e-16 |
|
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: 81.76 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRnqsflhslkaakcnaliy 109
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLR------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 110 SSELSegvkeilgelkdiklYILNKskegeetnlgeaidlkkglAEVSKANLIDEVNAGKprDKLLFIYTSGTTGLPKAA 189
Cdd:cd05958 72 PKELA---------------YILDK-------------------ARITVALCAHALTASD--DICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 190 VINNNRYLFIS--IGVKILlKLHDDDILYNSLPLYHTSGV--------IVGAgqsilsgiTVVIRKKFSASNFWQDCIKY 259
Cdd:cd05958 116 MHFHRDPLASAdrYAVNVL-RLREDDRFVGSPPLAFTFGLggvllfpfGVGA--------SGVLLEEATPDLLLSAIARY 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 260 NCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIKQIgEFYGATEgnsNL-VNIDNKVGCV 336
Cdd:cd05958 187 KPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTE---MFhIFISARPGDA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 337 GfvPRLAGPVYPVVLLKVDKDTEEPIrnskgfcircQPGEPGICVGKinsKQTISTFLgyADKVEsekkilKNVFKKGDN 416
Cdd:cd05958 263 R--PGATGKPVPGYEAKVVDDEGNPV----------PDGTIGRLAVR---GPTGCRYL--ADKRQ------RTYVQGGWN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 417 YfnSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPH--VEGKAGMVAIHDVDESVN 494
Cdd:cd05958 320 I--TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgVVVKAFVVLRPGVIPGPV 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 242022874 495 L-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05958 398 LaRELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
157-534 |
2.90e-16 |
|
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: 81.65 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 157 SKANLIDEVNAGKprdklLFIYTSGTTGLPK---AAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGq 233
Cdd:cd05929 116 SPETPIEDEAAGW-----KMLYSGGTTGRPKgikRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMT- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 234 SILSGITVVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQH--KIRLMFGNGLKAQIWekfVERFQIK 311
Cdd:cd05929 190 ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPW---VKEQWID 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 312 ----QIGEFYGATEGN-SNLVNIDNKVGCVGFVPRLAGPVYPVVllkvDKDTEEpirnskgfcirCQPGEPGicvgkins 386
Cdd:cd05929 267 wggpIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAVLGKVHIL----DEDGNE-----------VPPGEIG-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 387 kqTI-----STFLGYADKVESEKKIlknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNI 461
Cdd:cd05929 324 --EVyfangPGFEYTNDPEKTAAAR------NEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 462 IGYKDAIVFGveVPHVE-GKAGMVAIHDVDESVNLQEFDEKL----KKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05929 396 PKVLDAAVVG--VPDEElGQRVHAVVQPAPGADAGTALAEELiaflRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
6-537 |
4.71e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 81.25 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 6 STVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSA 84
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 85 LINTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGElKDIKLYILnkskegeeTNLGEAIDLKKG-LAE-------- 155
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFK-TPVKHVIL--------TRMGDQLSTAKGtLVNfvvkyikr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 156 -VSKANLIDEVN------AG------KP---RDKLLFI-YTSGTTGLPKAA------VINNnryLFISIGVKILLKLHDD 212
Cdd:PRK08974 174 lVPKYHLPDAISfrsalhKGrrmqyvKPelvPEDLAFLqYTGGTTGVAKGAmlthrnMLAN---LEQAKAAYGPLLHPGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 213 DILYNSLPLYHTSGVIVGAGQSILSGIT-VVIRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLM 291
Cdd:PRK08974 251 ELVVTALPLYHIFALTVNCLLFIELGGQnLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 292 FGNGLK-----AQIWEKFVErfqiKQIGEFYGATEGnSNLV-----NIDNKVGCVGFvprlagPVyPVVLLKV--DKDTE 359
Cdd:PRK08974 331 VGGGMAvqqavAERWVKLTG----QYLLEGYGLTEC-SPLVsvnpyDLDYYSGSIGL------PV-PSTEIKLvdDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 360 EPIrnskgfcircqpGEPGICVGKinSKQTIstfLGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTG 439
Cdd:PRK08974 399 VPP------------GEPGELWVK--GPQVM---LGYWQRPEATDEVIK------DGWLATGDIAVMDEEGFLRIVDRKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 440 DTFRWKGENVATSEVEAVISniIGYKDAIVFGVEVPH-VEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRII 518
Cdd:PRK08974 456 DMILVSGFNVYPNEIEDVVM--LHPKVLEVAAVGVPSeVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFR 533
|
570
....*....|....*....
gi 242022874 519 KNLPLTGTYKLKKKELQME 537
Cdd:PRK08974 534 DELPKSNVGKILRRELRDE 552
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
169-540 |
7.55e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 81.12 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 169 KPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVV------ 242
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVyhpdpt 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 ----IRKKfsasnfwqdCIKYNCTVACYIGEICR-YLlavpekSHDKQHKirLMFGN---------GLKAQIWEKFVERF 308
Cdd:PRK08633 860 dalgIAKL---------VAKHRATILLGTPTFLRlYL------RNKKLHP--LMFASlrlvvagaeKLKPEVADAFEEKF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 309 QIKqIGEFYGATE-------------GNSNLVNIDNKVGCVGFvprlagPVyPVVLLK-VDKDTEEPirnskgfcirCQP 374
Cdd:PRK08633 923 GIR-ILEGYGATEtspvasvnlpdvlAADFKRQTGSKEGSVGM------PL-PGVAVRiVDPETFEE----------LPP 984
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 375 GEPG-ICVGKINskqtisTFLGYADKVESEKKILKNVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSE 453
Cdd:PRK08633 985 GEDGlILIGGPQ------VMKGYLGDPEKTAEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 454 VEAVISNIIGYKDAIVFGVEVPhvEGKAG--MVAIHDVDEsvnlQEFDEKLKKM----LPSYARPLFVRIIKNLPLTGTY 527
Cdd:PRK08633 1057 VEEELAKALGGEEVVFAVTAVP--DEKKGekLVVLHTCGA----EDVEELKRAIkesgLPNLWKPSRYFKVEALPLLGSG 1130
|
410
....*....|....*.
gi 242022874 528 KL---KKKELQMEGFN 540
Cdd:PRK08633 1131 KLdlkGLKELALALLG 1146
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-534 |
1.25e-15 |
|
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: 79.49 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNL---RNQsflH 97
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYpaeRLA---Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 98 SLKAAKCNALIYSSElsegvkeilgelkdiklyilnkskegeetnlgeaidlkkGLAEVskanlidevnagkprdkllfI 177
Cdd:cd05930 79 ILEDSGAKLVLTDPD---------------------------------------DLAYV--------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 178 YTSGTTGLPKAAVINN----NRYLfisiGVKILLKLHDDDILynslpLYHTSGVIVGAGQSI----LSGITVVIRKKFSA 249
Cdd:cd05930 100 YTSGSTGKPKGVMVEHrglvNLLL----WMQEAYPLTPGDRV-----LQFTSFSFDVSVWEIfgalLAGATLVVLPEEVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 250 SN---FWQDCIKYNCTVACYIGEICRYLLAVPEKSHDkqHKIRLMF--GNGLKAQIWEKFVERFQIKQIGEFYGATE--G 322
Cdd:cd05930 171 KDpeaLADLLAEEGITVLHLTPSLLRLLLQELELAAL--PSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEatV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 323 NSNLVNIDNKVGCVGFVPrLAGPVYPVVLLkvdkdteepIRNSKGfciRCQP-GEPG-ICVGkinskqTISTFLGYADKV 400
Cdd:cd05930 249 DATYYRVPPDDEEDGRVP-IGRPIPNTRVY---------VLDENL---RPVPpGVPGeLYIG------GAGLARGYLNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 401 E-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTgDT------FRwkgenVATSEVEAVISNIIGYKDAIVFGVE 473
Cdd:cd05930 310 ElTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAVVARE 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 474 VPhvEGKAGMVA--IHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05930 384 DG--DGEKRLVAyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
32-522 |
2.29e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 78.76 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRN---QSFLHSLKAAkcnALI 108
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLaelDYFIGDAEPA---LVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 109 YSSELSEGVKEILGELKDIKLYILNKSKEGeeTNLGEAIDLKKGLAEVSKANliDEVNAgkprdkllFIYTSGTTGLPKA 188
Cdd:PRK07514 106 CDPANFAWLSKIAAAAGAPHVETLDADGTG--SLLEAAAAAPDDFETVPRGA--DDLAA--------ILYTSGTTGRSKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 AVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASnfwqDCIKY--NCTVacY 266
Cdd:PRK07514 174 AMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPD----AVLALmpRATV--M 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRY--LLAVPEKSHDKQHKIRLmFGNG---LKAQIWEKFVERFQiKQIGEFYGATEGN---SNLVNIDNKVGCVGF 338
Cdd:PRK07514 248 MGVPTFYtrLLQEPRLTREAAAHMRL-FISGsapLLAETHREFQERTG-HAILERYGMTETNmntSNPYDGERRAGTVGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 339 vPrLAGpvypVVLLKVDKDTEEPirnskgfcirCQPGEPG-ICVGKINskqtisTFLGY---ADKVESEkkilknvFkKG 414
Cdd:PRK07514 326 -P-LPG----VSLRVTDPETGAE----------LPPGEIGmIEVKGPN------VFKGYwrmPEKTAEE-------F-RA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 415 DNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVEGKAGMVAI------HD 488
Cdd:PRK07514 376 DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIG--VPHPDFGEGVTAVvvpkpgAA 453
|
490 500 510
....*....|....*....|....*....|....
gi 242022874 489 VDESVNLQEFDEKLKKmlpsYARPLFVRIIKNLP 522
Cdd:PRK07514 454 LDEAAILAALKGRLAR----FKQPKRVFFVDELP 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-476 |
5.56e-15 |
|
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: 77.66 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKE------ILGELKDIKLYILNKSKEGEETNLGEAIDlkkglaevskanlidevnagKPRDKLLFIYTSGTTGLP 186
Cdd:cd05904 114 LAEKLASlalpvvLLDSAEFDSLSFSDLLFEADEAEPPVVVI--------------------KQDDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 187 KAAVINNNRylFISIGVKIL----LKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCT 262
Cdd:cd05904 174 KGVMLTHRN--LIAMVAQFVagegSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 263 vacyigeicrYLLAVP-----------EKSHDKQHKIRLMFGNG-LKAQIWEKFVERFQIKQIGEFYGATE----GNSNL 326
Cdd:cd05904 252 ----------HLPVVPpivlalvkspiVDKYDLSSLRQIMSGAApLGKELIEAFRAKFPNVDLGQGYGMTEstgvVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 327 VNIDN--KVGCVGF-VPRLAGPVypvvllkVDKDTEEPIRnskgfciRCQPGE-----PGICVGKINSKQ-TISTFlgya 397
Cdd:cd05904 322 APEKDraKYGSVGRlVPNVEAKI-------VDPETGESLP-------PNQTGElwirgPSIMKGYLNNPEaTAATI---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 398 DKvesekkilknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAV-ISN-------IIGYKDAIv 469
Cdd:cd05904 384 DK---------------EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALlLSHpeildaaVIPYPDEE- 447
|
....*..
gi 242022874 470 FGvEVPH 476
Cdd:cd05904 448 AG-EVPM 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
171-531 |
6.23e-15 |
|
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: 76.15 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 171 RDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKI-LLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSA 249
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 250 SNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLM-FGNGLKAQIWEKFVERFQIKQIGEFYGATE-GNSNLV 327
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIgYGGSRAIAADVRFIEATGLTNTAQVYGLSEtGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 328 NIDNKVGCVGFVprlaGPVYPVVLLKVdKDTEEPIRNSKGFcircqpgepgicvGKINSKqTISTFLGYADKVESEKKIL 407
Cdd:cd17635 161 PTDDDSIEINAV----GRPYPGVDVYL-AATDGIAGPSASF-------------GTIWIK-SPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 408 KnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFgvEVPHVE-GK---AGM 483
Cdd:cd17635 222 I------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISDEEfGElvgLAV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 242022874 484 VAIHDVDESVnLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKK 531
Cdd:cd17635 294 VASAELDENA-IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-534 |
1.97e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 76.00 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIA--FHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSA 84
Cdd:PRK08315 17 TIGQLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 85 LINTNLRNQSFLHSLKAAKCNALIY-----SSELSEGVKEILGELKDIKLYILNKSKE---------GEETNLG--EAID 148
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELATCEPGQLQSARLpelrrviflGDEKHPGmlNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 149 LKKGLAEVSKANLiDEVNAG-KPRDKLLFIYTSGTTGLPKAAV-----INNNRYLfisIGVkiLLKLHDDDILYNSLPLY 222
Cdd:PRK08315 177 LLALGRAVDDAEL-AARQATlDPDDPINIQYTSGTTGFPKGATlthrnILNNGYF---IGE--AMKLTEEDRLCIPVPLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 223 HTSGVIVGAGQSILSGITVVirkkFSASNFwqDCIKYNCTVAcyiGEICRYLLAVP-----EKSHDKQHKIRL------- 290
Cdd:PRK08315 251 HCFGMVLGNLACVTHGATMV----YPGEGF--DPLATLAAVE---EERCTALYGVPtmfiaELDHPDFARFDLsslrtgi 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 291 MFGNGLKAQIWEKFVERFQIKQIGEFYGATEG----NSNLVN--IDNKVGCVGfvpRlagpVYPVVLLK-VDKDTEEPir 363
Cdd:PRK08315 322 MAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETspvsTQTRTDdpLEKRVTTVG---R----ALPHLEVKiVDPETGET-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 364 nskgfcirCQPGEPG-ICV-GKinskqtiSTFLGYADKVESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFkdrTGdt 441
Cdd:PRK08315 393 --------VPRGEQGeLCTrGY-------SVMKGYWNDPEKTAEAI-----DADGWMHTGDLAVMDEEGYVNI---VG-- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 442 fRWK------GENVATSEVEAVISNIIGYKDAIVFGveVPHVE-GKAGMVAI-----HDVDESvNLQEFdekLKKMLPSY 509
Cdd:PRK08315 448 -RIKdmiirgGENIYPREIEEFLYTHPKIQDVQVVG--VPDEKyGEEVCAWIilrpgATLTEE-DVRDF---CRGKIAHY 520
|
570 580
....*....|....*....|....*
gi 242022874 510 ARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK08315 521 KIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
176-535 |
2.87e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 74.44 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 176 FIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVI------RKKFSA 249
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 250 SNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIkQIGEFYGATEGNS----N 325
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL-PVVEGYGLTEATClvavN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVNIDNKVGCVGfvprLAGPVYPVVLLKVDKDTEepirnskgFCIRCQPGEPG-ICVgkinskQTISTFLGYADkveSEK 404
Cdd:cd05944 166 PPDGPKRPGSVG----LRLPYARVRIKVLDGVGR--------LLRDCAPDEVGeICV------AGPGVFGGYLY---TEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 405 KilKNVFkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVI--------SNIIGYKDAIVFGVEVPH 476
Cdd:cd05944 225 N--KNAF-VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALlrhpavafAGAVGQPDAHAGELPVAY 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 477 VEGKAGmvaihdvdESVNLQEFDEKLKKMLPSYAR-PLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05944 302 VQLKPG--------AVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
21-534 |
3.67e-14 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 74.82 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLK 100
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIYSSELSegvkeilgelkdiklyilNKSKEGEETNLGEAIDLKKGLAEvskaNLIDEVNAgkprDKLLF-IYT 179
Cdd:cd17656 83 DSGVRVVLTQRHLK------------------SKLSFNKSTILLEDPSISQEDTS----NIDYINNS----DDLLYiIYT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 180 SGTTGLPKA-AVINNNRYLFISIGVKILLKLHDDDILYNSLP----LYHTsgvIVGAgqsILSGITVVIRKKFSASNFWQ 254
Cdd:cd17656 137 SGTTGKPKGvQLEHKNMVNLLHFEREKTNINFSDKVLQFATCsfdvCYQE---IFST---LLSGGTLYIIREETKRDVEQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 255 --DCIKYNCT-VACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWEKFVERFQIKQIG--EFYGATEGNSnlvni 329
Cdd:cd17656 211 lfDLVKRHNIeVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHlhNHYGPSETHV----- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 330 dnkVGCVGFVPRLAGPVYPVVllkvdkdtEEPIRNSKGFCI----RCQP-GEPG-ICVGKINSKQtistflGYADKVE-S 402
Cdd:cd17656 286 ---VTTYTINPEAEIPELPPI--------GKPISNTWIYILdqeqQLQPqGIVGeLYISGASVAR------GYLNRQElT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 403 EKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEvpHVEGKAG 482
Cdd:cd17656 349 AEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA--DDKGEKY 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 242022874 483 MVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17656 427 LCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-534 |
6.79e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 74.35 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 48 FKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGElkDI 127
Cdd:PRK12406 28 LAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPA--GV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 128 KLYILNKSKEgeetnLGEAIDLKKGLAEVsKANLIDE---VNAGKPRDKLL------FIYTSGTTGLPK----------- 187
Cdd:PRK12406 106 TVLSVPTPPE-----IAAAYRISPALLTP-PAGAIDWegwLAQQEPYDGPPvpqpqsMIYTSGTTGHPKgvrraaptpeq 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 188 AAVINNNRYLFISI--GVKILLklhdddilynSLPLYHTSGVIVGAgQSILSGITVVIRKKFSASNFWQDCIKYNCTvac 265
Cdd:PRK12406 180 AAAAEQMRALIYGLkpGIRALL----------TGPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELLQLIERHRIT--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 266 yigeicrYLLAVPEKShdkqhkIRLMfgnGLKAQIWEKFVE---RF----------QIKQ---------IGEFYGATEgn 323
Cdd:PRK12406 246 -------HMHMVPTMF------IRLL---KLPEEVRAKYDVsslRHvihaaapcpaDVKRamiewwgpvIYEYYGSTE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 324 snlvnidnkVGCVGFV--------PRLAGPVYPVVLLKVDKDTEEPIrnskgfcircQPGEpgicVGKINSKQTISTFLG 395
Cdd:PRK12406 308 ---------SGAVTFAtsedalshPGTVGKAAPGAELRFVDEDGRPL----------PQGE----IGEIYSRIAGNPDFT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 396 YADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVP 475
Cdd:PRK12406 365 YHNKPEKRAEIDR------GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242022874 476 HVEGKAGMVAIHDVDESVNLQEFD--EKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATLDEADirAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
172-524 |
7.58e-14 |
|
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: 72.69 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKkFSASN 251
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK-FDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 252 FWQDCIKYNCTVacyIGE---ICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIwekfvERFQIKQIGEF---YGATEgNSN 325
Cdd:cd17637 80 ALELIEEEKVTL---MGSfppILSNLLDAAEKSGVDLSSLRHVLGLDAPETI-----QRFEETTGATFwslYGQTE-TSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVNI---DNKVGCvgfvprlAGPVYPVVLLKVDKDTEEPIRnskgfcircqPGEPG-ICVgkinskQTISTFLGYADKVE 401
Cdd:cd17637 151 LVTLspyRERPGS-------AGRPGPLVRVRIVDDNDRPVP----------AGETGeIVV------RGPLVFQGYWNLPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 402 SEKKilknVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWK--GENVATSEVEAVISNIIGYKDAIVFGVEVPHV-E 478
Cdd:cd17637 208 LTAY----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWgE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 242022874 479 G-KAgmVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLT 524
Cdd:cd17637 282 GiKA--VCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKT 326
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
33-471 |
9.77e-14 |
|
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: 73.57 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQsflhslkaakcnaliyssE 112
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREH------------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSegvkeilgelkdiklYILNKSKegeetnlgeaidlkkglaevSKANLIDEV-----NAGKPRDKLLFIYTSGTTGLPK 187
Cdd:cd05903 65 LA---------------FILRRAK--------------------AKVFVVPERfrqfdPAAMPDAVALLLFTSGTTGEPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 188 AAVINNNRyLFISIGVKIL-LKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTV--- 263
Cdd:cd05903 110 GVMHSHNT-LSASIRQYAErLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFmmg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 264 -ACYIGEICRyllaVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERFQ---IKQIGEFYGATEGNSNLVNIDNkvGCVGFV 339
Cdd:cd05903 189 aTPFLTDLLN----AVEEAGEPLSRLRTFVCGG--ATVPRSLARRAAellGAKVCSAYGSTECPGAVTSITP--APEDRR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 340 PRLAGPVYPVVLLKVDKDTEEPIrnskgfcircqpgePGICVGKINSKQTiSTFLGYADKVESEKKILKnvfkkgDNYFN 419
Cdd:cd05903 261 LYTDGRPLPGVEIKVVDDTGATL--------------APGVEGELLSRGP-SVFLGYLDRPDLTADAAP------EGWFR 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 242022874 420 SGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFG 471
Cdd:cd05903 320 TGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-534 |
2.22e-13 |
|
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: 72.66 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 23 IAFHQENISW---------TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQ 93
Cdd:cd12119 8 LHGDREIVSRthegevhryTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 94 SFLHSLKAAKCNALIYSSELSEGVKEILGELKDIKLYILNKSKEGEE----TNLGEAIDLKKGLAEVSKANLIDEvnagk 169
Cdd:cd12119 88 QIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPepagVGVLAYEELLAAESPEYDWPDFDE----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 pRDKLLFIYTSGTTGLPKaAVINNNRYLFI---SIGVKILLKLHDDDILYNSLPLYHT-------SGVIVGAGQsILSGi 239
Cdd:cd12119 163 -NTAAAICYTSGTTGNPK-GVVYSHRSLVLhamAALLTDGLGLSESDVVLPVVPMFHVnawglpyAAAMVGAKL-VLPG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 240 tvvirKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEK-SHDKQHKIRLMFGN-----GLKAQIWEKFVERFQIkqi 313
Cdd:cd12119 239 -----PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEAnGRDLSSLRRVVIGGsavprSLIEAFEERGVRVIHA--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 314 gefYGATEGNSnlvnidnkVGCVGFVP---------------RLAG-PVYPVVLLKVDKDTEEPIRNSKGFcircqpGE- 376
Cdd:cd12119 311 ---WGMTETSP--------LGTVARPPsehsnlsedeqlalrAKQGrPVPGVELRIVDDDGRELPWDGKAV------GEl 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 377 ----PGICVGKinskqtistflgYADKVESEkkilknvFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATS 452
Cdd:cd12119 374 qvrgPWVTKSY------------YKNDEESE-------ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 453 EVEAVISNIIGYKDAIVFGveVPH---VEGKAGMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKL 529
Cdd:cd12119 435 ELENAIMAHPAVAEAAVIG--VPHpkwGERPLAVVVLKE-GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKI 511
|
....*
gi 242022874 530 KKKEL 534
Cdd:cd12119 512 DKKAL 516
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
6-537 |
4.59e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 71.72 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 6 STVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQ-GYKKGDTIALYMENSIEYMCIWLGLAKLGIVsa 84
Cdd:PRK05677 24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 85 LINTN--LRNQSFLHSLKAAKCNALIYSSELSEGVKEIL----------GELKD----IKLYILNK-----SKEGEETNL 143
Cdd:PRK05677 102 VVNTNplYTAREMEHQFNDSGAKALVCLANMAHLAEKVLpktgvkhvivTEVADmlppLKRLLINAvvkhvKKMVPAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 144 GEAIDLKKGLAEvSKANLIDEVNAgKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILL--KLHDD-DILYNSLP 220
Cdd:PRK05677 182 PQAVKFNDALAK-GAGQPVTEANP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsNLNEGcEILIAPLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 221 LYHTSGVIVGAGQSILSGI-TVVIRKKFSASNFWQDCIKYNCTvaCYIGeiCRYLLAVPEKSHDKQH------KIRLMFG 293
Cdd:PRK05677 260 LYHIYAFTFHCMAMMLIGNhNILISNPRDLPAMVKELGKWKFS--GFVG--LNTLFVALCNNEAFRKldfsalKLTLSGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 294 NGLK---AQIWEKFVErfqiKQIGEFYGATEgNSNLVNID----NKVGCVGFvprlagPVyPVVLLKV--DKDTEEPIrn 364
Cdd:PRK05677 336 MALQlatAERWKEVTG----CAICEGYGMTE-TSPVVSVNpsqaIQVGTIGI------PV-PSTLCKVidDDGNELPL-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 365 skgfcircqpGEPG-ICVgkiNSKQTIStflGYADKVESEKKILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFR 443
Cdd:PRK05677 402 ----------GEVGeLCV---KGPQVMK---GYWQRPEATDEILDS-----DGWLKTGDIALIQEDGYMRIVDRKKDMIL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 444 WKGENVATSEVEAVISNIIGYKDAIVFGVEvphvEGKAG----MVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIK 519
Cdd:PRK05677 461 VSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGeaikVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRD 536
|
570
....*....|....*...
gi 242022874 520 NLPLTGTYKLKKKELQME 537
Cdd:PRK05677 537 ELPTTNVGKILRRELRDE 554
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
31-534 |
4.99e-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: 71.47 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSAlintnlrnqSFLHSLKAAKCNaliys 110
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---------PIYPTSSAEQIA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 selsegvkeilgelkdiklYILNKSKegeetnlgeaidlkkglAEVskanLIdevnAGKPRDKLLFIYTSGTTGLPKAAV 190
Cdd:cd05907 71 -------------------YILNDSE-----------------AKA----LF----VEDPDDLATIIYTSGTTGRPKGVM 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 INNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIrkKFSASNFWQDCIKYNCTvacyigei 270
Cdd:cd05907 107 LSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF--ASSAETLLDDLSEVRPT-------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 271 crYLLAVP---EKSHDkqhKIRLMFGNGLKAQIWE-------KF-----------VERFqIKQIG----EFYGATEgNSN 325
Cdd:cd05907 177 --VFLAVPrvwEKVYA---AIKVKAVPGLKRKLFDlavggrlRFaasggaplpaeLLHF-FRALGipvyEGYGLTE-TSA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVNI----DNKVGCVgfvprlaGPVYPVVLLKVDKDteepirnskgfcircqpGEpgICV-GKinskqtiSTFLGYADKV 400
Cdd:cd05907 250 VVTLnppgDNRIGTV-------GKPLPGVEVRIADD-----------------GE--ILVrGP-------NVMLGYYKNP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 401 ESEKKILknvfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRW-KGENVATSEVEAVI--SNIIGykDAIVFGVEVPHV 477
Cdd:cd05907 297 EATAEAL-----DADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALkaSPLIS--QAVVIGDGRPFL 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 478 -----------------EGKAGMVAIHDVDESVNLQEFDEKLKKM---LPSYARplfVRIIKNLP---------LTGTYK 528
Cdd:cd05907 370 valivpdpealeawaeeHGIAYTDVAELAANPAVRAEIEAAVEAAnarLSRYEQ---IKKFLLLPepftiengeLTPTLK 446
|
....*.
gi 242022874 529 LKKKEL 534
Cdd:cd05907 447 LKRPVI 452
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
177-535 |
5.47e-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: 70.05 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 177 IYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVgAGQSILSGITVVIRKKFSAsnFWQDC 256
Cdd:cd17630 6 ILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQA--LAEDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 257 IKYNCTVACYIGEICRYLLAVPEKShDKQHKIRLMFGNGlkAQIWEKFVERFQIKQIGEF--YGATEGNSNlvnIDNKVg 334
Cdd:cd17630 83 APPGVTHVSLVPTQLQRLLDSGQGP-AALKSLRAVLLGG--APIPPELLERAADRGIPLYttYGMTETASQ---VATKR- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 335 CVGFVPRLAGPVYPVVLLKVDKDTEepirnskgfcircqpgepgICVGkinskqTISTFLGYADKVesekkILKNVFKKG 414
Cdd:cd17630 156 PDGFGRGGVGVLLPGRELRIVEDGE-------------------IWVG------GASLAMGYLRGQ-----LVPEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 415 dnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVEGKAGMVAIHDVDESVN 494
Cdd:cd17630 206 --WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDEELGQRPVAVIVGRGPAD 281
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 242022874 495 LQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd17630 282 PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
10-534 |
9.28e-13 |
|
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: 70.28 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 10 KVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTN 89
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 90 lrnqsflhslkaakcnaliYSSELSEgvkeilgelkdiklYILNKSkegeetnlGEAIDLKKglaevskanlidevnagk 169
Cdd:cd17645 82 -------------------YPGERIA--------------YMLADS--------SAKILLTN------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFIYTSGTTGLPKAAVINNNRylfisigvkillklhdddiLYNSLPLYHTS-GVIVGAGQSILSGITvvirkkFS 248
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHN-------------------LVNLCEWHRPYfGVTPADKSLVYASFS------FD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 249 ASnFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFgngLKAQIWEKFVE-----------------RFQIK 311
Cdd:cd17645 158 AS-AWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISF---LPTGAAEQFMQldnqslrvlltggdklkKIERK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 312 --QIGEFYGATEGN--SNLVNIDNKVGCVGfvprLAGPVYPVVLLKVDKDTE-EPIRNSKGFCIrcqPGEpGICVGKINS 386
Cdd:cd17645 234 gyKLVNNYGPTENTvvATSFEIDKPYANIP----IGKPIDNTRVYILDEALQlQPIGVAGELCI---AGE-GLARGYLNR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 387 KQtistflgyadkvESEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKD 466
Cdd:cd17645 306 PE------------LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 467 AIVFGVEvpHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17645 374 AAVLAKE--DADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
33-535 |
1.27e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 70.46 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:PRK06178 60 TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKEILGE--------------LKDIKLYILNKSKEGEETNLGEAIDLKKGLAEVSKANL-----IDEVNAgkprdk 173
Cdd:PRK06178 140 LAPVVEQVRAEtslrhvivtsladvLPAEPTLPLPDSLRAPRLAAAGAIDLLPALRACTAPVPlpppaLDALAA------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 174 llFIYTSGTTGLPKAaVINNNRYL------FISIGVKillkLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKF 247
Cdd:PRK06178 214 --LNYTGGTTGMPKG-CEHTQRDMvytaaaAYAVAVV----GGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 248 SASNFWQDCIKYNCTVACYIGEICRYLLAVPeksHDKQHKIRlmfgnGLKAQIWEKFVERF--QIKQ---------IGEF 316
Cdd:PRK06178 287 DAVAFMAAVERYRVTRTVMLVDNAVELMDHP---RFAEYDLS-----SLRQVRVVSFVKKLnpDYRQrwraltgsvLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 -YGATEGNSnlvnidnkvgC----VGF---------VPRLAG-PVYPVVLLKVDKDTEEPIrnskgfcircqP-GEPG-I 379
Cdd:PRK06178 359 aWGMTETHT----------CdtftAGFqdddfdllsQPVFVGlPVPGTEFKICDFETGELL-----------PlGAEGeI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 380 CVgkinskQTISTFLGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVI- 458
Cdd:PRK06178 418 VV------RTPSLLKGYWNKPEATAEALR------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLg 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 459 -------SNIIGYKDAIVFGVEVPHVEGKAGmvaiHDVDESvNLQEFdekLKKMLPSYARPLfVRIIKNLPLTGTYKLKK 531
Cdd:PRK06178 486 qhpavlgSAVVGRPDPDKGQVPVAFVQLKPG----ADLTAA-ALQAW---CRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
....
gi 242022874 532 KELQ 535
Cdd:PRK06178 557 QDLQ 560
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-531 |
1.64e-12 |
|
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: 68.68 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 177 IYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDC 256
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 257 IKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERFQ----IKQIGEFYGATEGNsnlvnidnk 332
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGA--ATVPVELVRRMRselgFETVLTAYGLTEAG--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 333 vgcvgfVPRLAGPVYPVVLLKVDKDTEEPirnskGFCIRCQ-PGEpgICVGKINskqtisTFLGYADKVESEKKILKnvf 411
Cdd:cd17638 155 ------VATMCRPGDDAETVATTCGRACP-----GFEVRIAdDGE--VLVRGYN------VMQGYLDDPEATAEAID--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 412 kkGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV------EVphveGKAGMVA 485
Cdd:cd17638 213 --ADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpdermgEV----GKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 242022874 486 IHDVdeSVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKK 531
Cdd:cd17638 287 RPGV--TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
21-535 |
1.84e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 69.81 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLR--NQSFLhs 98
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTppEIAFL-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 99 lkAAKCNALIYSSE-----LSEGVKEILGELKdiklYILNKSKEGEETNLGeaidLKKGLAEVSKANLIDEVnagkPRDK 173
Cdd:PRK07786 110 --VSDCGAHVVVTEaalapVATAVRDIVPLLS----TVVVAGGSSDDSVLG----YEDLLAEAGPAHAPVDI----PNDS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 174 -LLFIYTSGTTGLPKAAVINNNRY------LFISIGVKIllklhDDDILYNSLPLYHTSGvIVGAGQSILSGITVVIR-- 244
Cdd:PRK07786 176 pALIMYTSGTTGRPKGAVLTHANLtgqamtCLRTNGADI-----NSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 245 KKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPeKSHDKQHKIRLMFGNGLKAQ--IWEKFVERFQIKQIGEFYGATEG 322
Cdd:PRK07786 250 GAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ-QARPRDLALRVLSWGAAPASdtLLRQMAATFPEAQILAAFGQTEM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 323 NSNLVNIDN-----KVGCVGFV-PRLAGPVypvvllkVDKDTEEpirnskgfcirCQPGEpgicVGKINSKQTiSTFLGY 396
Cdd:PRK07786 329 SPVTCMLLGedairKLGSVGKViPTVAARV-------VDENMND-----------VPVGE----VGEIVYRAP-TLMSGY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 397 ADKVESEKkilkNVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFG----- 471
Cdd:PRK07786 386 WNNPEATA----EAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGradek 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 472 -VEVPhvegkAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK07786 460 wGEVP-----VAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
32-535 |
2.21e-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: 69.42 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEY-MC---IWLGlaklGIVSALINTNLRNQSFLHSLKAAKCNAL 107
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWfITdlaIWMA----GHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 108 IYSS-ELSEGVKEILGElkDIKLYILNKSKEGEETNLGEAIdlkkglaeVSKANLIDEVNAGKPRDKLLFIYTSGTTGLP 186
Cdd:cd05932 83 FVGKlDDWKAMAPGVPE--GLISISLPPPSAANCQYQWDDL--------IAQHPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 187 KAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKkfSASNFWQDCIKYNCTVacy 266
Cdd:cd05932 153 KGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDVQRARPTL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 igeicryLLAVP-------EKSHDK--QHKIRLMfgngLKAQIWEKFVERFQIKQIG----------------------- 314
Cdd:cd05932 228 -------FFSVPrlwtkfqQGVQDKipQQKLNLL----LKIPVVNSLVKRKVLKGLGldqcrlagcgsapvppallewyr 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 315 -------EFYGATE--GNSNL-VNIDNKVGCVgfvprlaGPVYPVVLLKVDKDTEEPIRnSKGfcircqpgepgicvgki 384
Cdd:cd05932 297 slglnilEAYGMTEnfAYSHLnYPGRDKIGTV-------GNAGPGVEVRISEDGEILVR-SPA----------------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 385 nskqtisTFLGYADKVESEKKILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRW-KGENVATSEVE-------- 455
Cdd:cd05932 352 -------LMMGYYKDPEATAEAFTA-----DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIEnklaehdr 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 456 ----AVISNIIGYKDAIVFGVEVPHVEGKAGmvAIHDVDESvnLQEFDEKLKKMLPSYARPLFVRIIK------NLPLTG 525
Cdd:cd05932 420 vemvCVIGSGLPAPLALVVLSEEARLRADAF--ARAELEAS--LRAHLARVNSTLDSHEQLAGIVVVKdpwsidNGILTP 495
|
570
....*....|
gi 242022874 526 TYKLKKKELQ 535
Cdd:cd05932 496 TLKIKRNVLE 505
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
21-524 |
3.77e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.00 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLK 100
Cdd:PRK06164 25 DAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIY---------SSELSEGVKEILGELKDIKLyILNKSKEGEETNLGEAIDLKKGLAEVSKANLIDEvnAGKPR 171
Cdd:PRK06164 105 RGRARWLVVwpgfkgidfAAILAAVPPDALPPLRAIAV-VDDAADATPAPAPGARVQLFALPDPAPPAAAGER--AADPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIYTSGTTGLPK------AAVINNNRYLFISIGVKillklhDDDILYNSLPLyhtSGV--IVGAGQSILSGITVVI 243
Cdd:PRK06164 182 AGALLFTTSGTTSGPKlvlhrqATLLRHARAIARAYGYD------PGAVLLAALPF---CGVfgFSTLLGALAGGAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 244 RKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAqiWEKFVERFQIKQ--IGEFYGATE 321
Cdd:PRK06164 253 EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPA--LGELAALARARGvpLTGLYGSSE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 322 GNSnLVNIDNKVGCVGfVPRLAG--PVYPVVLLKVdKDTEEPirnskGFCIRCQPGEPGIcvgkinskQTISTFLGYADK 399
Cdd:PRK06164 331 VQA-LVALQPATDPVS-VRIEGGgrPASPEARVRA-RDPQDG-----ALLPDGESGEIEI--------RAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 400 VESEKKILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEvphVEG 479
Cdd:PRK06164 395 PDATARALTD-----DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT---RDG 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 242022874 480 KAGMVAIHDVDESVNLQEFDEK--LKKMLPSYARPLFVRIIKNLPLT 524
Cdd:PRK06164 467 KTVPVAFVIPTDGASPDEAGLMaaCREALAGFKVPARVQVVEAFPVT 513
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-543 |
6.80e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 68.08 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 11 VFQEIcEKNYDKIAFHQENI--SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINT 88
Cdd:PLN02330 34 VLQDA-ELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 89 NLRNQSFLHSLKAAKCNALIYSSELSEGVKEIlgELKDIKLyilnkskeGEETNLGeAIDLKKGLAEVSKANLIDEVNAG 168
Cdd:PLN02330 113 TALESEIKKQAEAAGAKLIVTNDTNYGKVKGL--GLPVIVL--------GEEKIEG-AVNWKELLEAADRAGDTSDNEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 169 KPRDKLLFIYTSGTTGLPKAAVINNNRYL------FISIGVKILLKLhdddILYNSLPLYHTSGVIVGAGQSILSGITVV 242
Cdd:PLN02330 182 LQTDLCALPFSSGTTGISKGVMLTHRNLVanlcssLFSVGPEMIGQV----VTLGLIPFFHIYGITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 IRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRL----MFGNGLKAQIWEKFVERFQIKQIGEFYG 318
Cdd:PLN02330 258 VMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 319 ATEGNS-NLVNIDNKVG-------CVGFVprlagpvYPVVLLK-VDKDTEEPI-RNSKG-FCIRCQpgepgiCVgkinsk 387
Cdd:PLN02330 338 LTEHSCiTLTHGDPEKGhgiakknSVGFI-------LPNLEVKfIDPDTGRSLpKNTPGeLCVRSQ------CV------ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 388 qtistFLGY-ADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKD 466
Cdd:PLN02330 399 -----MQGYyNNKEETDRTIDE------DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 467 AIVfgveVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPS----YARPLFVRIIKNLPLTGTYKLKKKELQMEGFNIT 542
Cdd:PLN02330 468 AAV----VPLPDEEAGEIPAACVVINPKAKESEEDILNFVAAnvahYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
.
gi 242022874 543 K 543
Cdd:PLN02330 544 K 544
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
31-535 |
9.13e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.48 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS 110
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSEGVKEILGELKDIKLYILNKSKEGEETNLGeAIDLKKGLAEVSKanlidevnagkPRDKLLFIYTSGTTGLPKAAV 190
Cdd:PRK13382 148 EEFSATVDRALADCPQATRIVAWTDEDHDLTVEV-LIAAHAGQRPEPT-----------GRKGRVILLTSGTTGTPKGAR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 191 INNNRYLFI--SIGVKILLKLHDDDILynSLPLYHTSGVivgaGQSILSGI---TVVIRKKFSASNFWQDCIKYNCTVAC 265
Cdd:PRK13382 216 RSGPGGIGTlkAILDRTPWRAEEPTVI--VAPMFHAWGF----SQLVLAASlacTIVTRRRFDPEATLDLIDRHRATGLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 266 YIGEICRYLLAVPEKSHDKQHKIRLMF----GNGLKAQIWEKFVERFQiKQIGEFYGATEgnsnlvnidnkvgcVGFV-- 339
Cdd:PRK13382 290 VVPVMFDRIMDLPAEVRNRYSGRSLRFaaasGSRMRPDVVIAFMDQFG-DVIYNNYNATE--------------AGMIat 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 340 ---------PRLAG-PVYPVVLLKVDKDTEEpirnskgfcirCQPGEpgicVGKI---NSKQtistFLGYADKveSEKKI 406
Cdd:PRK13382 355 atpadlraaPDTAGrPAEGTEIRILDQDFRE-----------VPTGE----VGTIfvrNDTQ----FDGYTSG--STKDF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 407 LknvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAI 486
Cdd:PRK13382 414 H-------DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 242022874 487 HDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK13382 487 LKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-534 |
1.15e-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: 66.89 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 17 EKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINT---NLRNQ 93
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAsspAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 94 SFLhslKAAKCNALIYS-SELSegvkeilgelkdiklYIlnkskegeetnlgeaidlkkglaevskanlidevnagkprd 172
Cdd:cd05945 82 EIL---DAAKPALLIADgDDNA---------------YI----------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 173 kllfIYTSGTTGLPKAAVIN-NNRYLFISIGVKiLLKLHDDDILYNSLP---------LYHTsgVIVGAGQSIL------ 236
Cdd:cd05945 103 ----IFTSGSTGRPKGVQIShDNLVSFTNWMLS-DFPLGPGDVFLNQAPfsfdlsvmdLYPA--LASGATLVPVprdata 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 237 -----------SGITVVirkkFSASNFWqdcikynctvacyigEICRYLLAVPEKSHDKqhkIRLMF--GNGLKAQIWEK 303
Cdd:cd05945 176 dpkqlfrflaeHGITVW----VSTPSFA---------------AMCLLSPTFTPESLPS---LRHFLfcGEVLPHKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 304 FVERFQIKQIGEFYGATEGN--SNLVNIDNKVgcVGFVPRLA-GPVYPVVLLKVDKDTEEPIrnskgfcircQPGEPG-I 379
Cdd:cd05945 234 LQQRFPDARIYNTYGPTEATvaVTYIEVTPEV--LDGYDRLPiGYAKPGAKLVILDEDGRPV----------PPGEKGeL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 380 CV-GKinskqtiSTFLGY---ADKVESekkilknVFKKGDNY--FNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSE 453
Cdd:cd05945 302 VIsGP-------SVSKGYlnnPEKTAA-------AFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEE 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 454 VEAVISNIIGYKDAIVfgVEVPHVEGKAGMVAI---HDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLK 530
Cdd:cd05945 368 IEAALRQVPGVKEAVV--VPKYKGEKVTELIAFvvpKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKID 445
|
....
gi 242022874 531 KKEL 534
Cdd:cd05945 446 RKAL 449
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
20-535 |
1.53e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 67.36 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 20 YDKIAFHQENISwTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLR--NQSFLH 97
Cdd:PRK06060 20 YDRPAFYAADVV-THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHrdDHALAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 98 SLKAAkcnALIYSSelsegvkeilGELKDiklyilnkskEGEETNLGEAIDLkkgLAEVSKANLID-EVNAGkprDKLLF 176
Cdd:PRK06060 99 RNTEP---ALVVTS----------DALRD----------RFQPSRVAEAAEL---MSEAARVAPGGyEPMGG---DALAY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 177 -IYTSGTTGLPKAAVINN-NRYLFISIGVKILLKLHDDDILYNSLPLYHTSGV-------IVGAGQSILSGITVVIRKKF 247
Cdd:PRK06060 150 aTYTSGTTGPPKAAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLgnsvwfpLATGGSAVINSAPVTPEAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 248 SASNFWQDCIKYNctVACYIGEIcryllaVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERFQIKQIGEFYGATEGNSN 325
Cdd:PRK06060 230 ILSARFGPSVLYG--VPNFFARV------IDSCSPDSFRSLRCVVsaGEALELGLAERLMEFFGGIPILDGIGSTEVGQT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 LVN--IDN-KVGCVGFVPrlagPVYPVVLLKVDKDTEEPirnskgfcircqPGEPGICVGKINSKQTistflgYADKVES 402
Cdd:PRK06060 302 FVSnrVDEwRLGTLGRVL----PPYEIRVVAPDGTTAGP------------GVEGDLWVRGPAIAKG------YWNRPDS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 403 ekkILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEvpHVEGKAG 482
Cdd:PRK06060 360 ---PVAN-----EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR--ESTGAST 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242022874 483 MVAI------HDVDESVnLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK06060 430 LQAFlvatsgATIDGSV-MRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
19-511 |
2.03e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 66.84 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 19 NYDKIAFHQE------NISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRN 92
Cdd:PLN02654 102 NGDKIAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 93 QSFLHSLKAAKCNALIYSSELSEGVKEILgeLKDIKLYILNKS-KEGEETNLGEAIDLKKGLAE---------------- 155
Cdd:PLN02654 182 ESLAQRIVDCKPKVVITCNAVKRGPKTIN--LKDIVDAALDESaKNGVSVGICLTYENQLAMKRedtkwqegrdvwwqdv 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 156 VSKANLIDEVNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYL-FISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQS 234
Cdd:PLN02654 260 VPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMvYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 235 ILSGITVVIRKkfSASNF------WQDCIKYNCTVACYIGEICRYLL---AVPEKSHDKQhKIRLM--FGNGLKAQIWEK 303
Cdd:PLN02654 340 MLNGATVLVFE--GAPNYpdsgrcWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRK-SLRVLgsVGEPINPSAWRW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 304 FVERFQIKQ--IGEFYGATEGNSNLVN-----IDNKVGCVGFvprlagPVYPVVLLKVDKDTEEPIRNSKGF-CIRcqPG 375
Cdd:PLN02654 417 FFNVVGDSRcpISDTWWQTETGGFMITplpgaWPQKPGSATF------PFFGVQPVIVDEKGKEIEGECSGYlCVK--KS 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 376 EPGIcvgkinskqtISTFLGYADKVESekkilkNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVE 455
Cdd:PLN02654 489 WPGA----------FRTLYGDHERYET------TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 456 AVISNIIGYKDAIVFGVEvPHVEGKaGMVAIHDVDESVnlqEFDEKLKKMLPSYAR 511
Cdd:PLN02654 553 SALVSHPQCAEAAVVGIE-HEVKGQ-GIYAFVTLVEGV---PYSEELRKSLILTVR 603
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
23-524 |
3.80e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 65.68 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 23 IAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAA 102
Cdd:PRK05852 35 LVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 103 KCNALIYSSElseGVKEilGELKDIKLYILNKSKEGEETNLGEAIDLKKGLAevSKANLIDEVNAGKPRDKLLFIYTSGT 182
Cdd:PRK05852 115 GARVVLIDAD---GPHD--RAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAA--TEPTPATSTPEGLRPDDAMIMFTGGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 183 TGLPKAAVINNNRylfISIGVKILL---KLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVI--RKKFSASNFWQDCI 257
Cdd:PRK05852 188 TGLPKMVPWTHAN---IASSVRAIItgyRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 258 KYNCTVACYIGEICRYLLAVP--EKSHDKQHKIRLMFGNG--LKAQIWEKFVERFQIKQIgEFYGATEGNSNLV--NID- 330
Cdd:PRK05852 265 AVGATWYTAVPTIHQILLERAatEPSGRKPAALRFIRSCSapLTAETAQALQTEFAAPVV-CAFGMTEATHQVTttQIEg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 331 -----NKVGCVGFVPRLAGPVYPVVllkvdkdteepirNSKGfcircQPGEPGiCVGKI--NSKQTISTFLGyadkvesE 403
Cdd:PRK05852 344 igqteNPVVSTGLVGRSTGAQIRIV-------------GSDG-----LPLPAG-AVGEVwlRGTTVVRGYLG-------D 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 404 KKILKNVFKkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPH-VEGKA- 481
Cdd:PRK05852 398 PTITAANFT--DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFG--VPDqLYGEAv 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242022874 482 GMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLT 524
Cdd:PRK05852 474 AAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHT 516
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
172-535 |
6.26e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 65.04 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKkFSASN 251
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 252 FWQDCIKYNCTVACYIGEICRYLLAvpEKSHDKQHK---IRLMFGNGLKAQIWEKFVERFQIkQIGEFYGATEGNSNLVN 328
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLK--GNSLDLSPRsgpVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEATGPVLF 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 329 ID-----NKVgcvgfvprlagPVYPVVLLKVDKD------TEEPIRNSKgfcirCQPGEP--GICVGKINSKQTiSTFLG 395
Cdd:PLN03102 343 CEwqdewNRL-----------PENQQMELKARQGvsilglADVDVKNKE-----TQESVPrdGKTMGEIVIKGS-SIMKG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 396 YAdkveSEKKILKNVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfgVEVP 475
Cdd:PLN03102 406 YL----KNPKATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV--VAMP 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242022874 476 H----------VEGKAGMVAIHDVDESVNLQEFD--EKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PLN03102 478 HptwgetpcafVVLEKGETTKEDRVDKLVTRERDliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
12-535 |
7.94e-11 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 64.25 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 12 FQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEymciWLgLAKLGIvsalintnlr 91
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLE----ML-VAILAI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 92 nqsflhsLKAAKCNALIysselsegvkeilgelkDIKLyilnkskegeetnlgeAIDLKKGLAEVSKANLIdeVNAGKPR 171
Cdd:cd17653 68 -------LKAGAAYVPL-----------------DAKL----------------PSARIQAILRTSGATLL--LTTDSPD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 DKLLFIYTSGTTGLPKA----------AVINNNRYLFISIGVKILLKLhdddilynSLPLYHTSGVIVGAgqsILSGITV 241
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGvmvphrgvlnYVSQPPARLDVGPGSRVAQVL--------SIAFDACIGEIFST---LCNGGTL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 242 VIRkkfSASNFWQDCIKynctvACYIGEICRYLLAV-PEKSHDKQHKIRLMfGNGLKAQIWEKFVERfqiKQIGEFYGAT 320
Cdd:cd17653 175 VLA---DPSDPFAHVAR-----TVDALMSTPSILSTlSPQDFPNLKTIFLG-GEAVPPSLLDRWSPG---RRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 321 EgnsnlvnidnkVGCVGFVPRLAgPVYPVVLLKvdkdteePIRNSKgfCIRCQP-------GEPG-ICVGKInskqtiST 392
Cdd:cd17653 243 E-----------CTISSTMTELL-PGQPVTIGK-------PIPNST--CYILDAdlqpvpeGVVGeICISGV------QV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 393 FLGY-ADKVESEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVatsEVEAVISNIIGYKDAIVFG 471
Cdd:cd17653 296 ARGYlGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI---NLEEIEEVVLQSQPEVTQA 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242022874 472 VEVPHVEGKAGMVAIHDVDESvNLQEFdekLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd17653 373 AAIVVNGRLVAFVTPETVDVD-GLRSE---LAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
21-214 |
1.15e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.15 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFH----QENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLG-IVSAL--------IN 87
Cdd:PRK04319 59 DKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGaIVGPLfeafmeeaVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 88 TNLRNqsflhslkaAKCNALIYSSELSEG-VKEILGELKDIKLYilnkskeGEETNLGEA-IDLKKGLAEVSKANLIDEV 165
Cdd:PRK04319 139 DRLED---------SEAKVLITTPALLERkPADDLPSLKHVLLV-------GEDVEEGPGtLDFNALMEQASDEFDIEWT 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 242022874 166 nagKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDI 214
Cdd:PRK04319 203 ---DREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDV 248
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
31-532 |
1.22e-10 |
|
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: 64.05 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS 110
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSEGVKEIlgELKDiklyILNKSKEGEET--------NLGEAIDLKKG----LAEVsKANLIDEVNAGKPRDKLLFIY 178
Cdd:cd05968 171 DGFTRRGREV--NLKE----EADKACAQCPTvekvvvvrHLGNDFTPAKGrdlsYDEE-KETAGDGAERTESEDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 179 TSGTTGLPKAAVINNNRY-LFISIGVKILLKLHDDDILYNSLPLYHTSG--VIVGagqSILSGITVVIRKKF----SASN 251
Cdd:cd05968 244 TSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGpwLIFG---GLILGATMVLYDGApdhpKADR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 252 FWQDCIKYNCTVACYIGEICRYLLA---VPEKSHDKQhKIRLMFGNG--LKAQIWEKFVERFQI--KQIGEFYGATEGNS 324
Cdd:cd05968 321 LWRMVEDHEITHLGLSPTLIRALKPrgdAPVNAHDLS-SLRVLGSTGepWNPEPWNWLFETVGKgrNPIINYSGGTEISG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 325 NLvnidnkVGCVgfvprLAGPVYPVVLLKVDKDTEEPIRNSKGFCIRCQPGEpgICVGKINSKQTISTFlgyadkvESEK 404
Cdd:cd05968 400 GI------LGNV-----LIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGE--LVLLAPWPGMTRGFW-------RDED 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 405 KILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPH-VEGKAGM 483
Cdd:cd05968 460 RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG--VPHpVKGEAIV 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 484 ---VAIHDVDESVNLQE-----FDEKLKKMLpsyaRPLFVRIIKNLPLTGTYKLKKK 532
Cdd:cd05968 538 cfvVLKPGVTPTEALAEelmerVADELGKPL----SPERILFVKDLPKTRNAKVMRR 590
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
170-535 |
1.36e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 63.87 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFIYTSGTTGLPKAAVINNnRYLFISIG-----VKILLKlhDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIR 244
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTH-RNLFANAAqgkawVPGLGD--GPERVLAALPMFHAYGLTLCLTLAVSIGGELVLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 245 KKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNG--LKAQI---WEKFVERFQIkqigEFYGA 319
Cdd:PRK05605 295 PAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAmaLPVSTvelWEKLTGGLLV----EGYGL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 320 TEGN----SNLVNIDNKVGCVGfVPrlagpvYPvvllkvdkDTEEPIRNSKGFCIRCQPGEPGICVgkINSKQTistFLG 395
Cdd:PRK05605 371 TETSpiivGNPMSDDRRPGYVG-VP------FP--------DTEVRIVDPEDPDETMPDGEEGELL--VRGPQV---FKG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 396 YADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDR------TGdtfrwkGENVATSEVEAVISNIIGYKDAIV 469
Cdd:PRK05605 431 YWNRPEETAKSFL------DGWFRTGDVVVMEEDGFIRIVDRikeliiTG------GFNVYPAEVEEVLREHPGVEDAAV 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 470 FGveVPHVEGKAGMVAIHDVDESVNLQE--FDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK05605 499 VG--LPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
170-534 |
1.40e-10 |
|
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: 63.64 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLhdDDILYNSLPLYHTSgVIVGAG---QSILSGITVVI--- 243
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYEL--DSFPVRLLQMASFS-FDVFAGdfaRSLLNGGTLVIcpd 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 244 RKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIR-LMFG-NGLKAQIWEKFVERF-QIKQIGEFYGAT 320
Cdd:cd17650 169 EVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGsDGCKAQDFKTLAARFgQGMRIINSYGVT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 321 EG---NSNLVNIDNKVGCVGFVPrLAGPVYPVVLLKVD-KDTEEPIRNSKGFCIrcqpGEPGICVGkinskqtistflgY 396
Cdd:cd17650 249 EAtidSTYYEEGRDPLGDSANVP-IGRPLPNTAMYVLDeRLQPQPVGVAGELYI----GGAGVARG-------------Y 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 397 ADKVE-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEvp 475
Cdd:cd17650 311 LNRPElTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRE-- 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 242022874 476 HVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17650 389 DKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
34-534 |
1.51e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.87 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 34 YKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSEL 113
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 114 SEGVKEILGELKDIKLYILNKSKEGEETNLGEAIDLKKGlaevskanlidEVNAGKPrDKLLFIYTSGTTGLPKAAVINN 193
Cdd:PRK05857 124 KMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG-----------NADQGSE-DPLAMIFTSGTTGEPKAVLLAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 194 NRYLFISigvKIL-------LKLHDDDILYNSLPLYHTSGV------IVGAGQSILSGITVVIRKKFSASNfwqdcikyN 260
Cdd:PRK05857 192 RTFFAVP---DILqkeglnwVTWVVGETTYSPLPATHIGGLwwiltcLMHGGLCVTGGENTTSLLEILTTN--------A 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 261 CTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWE-KFVERFQIKQiGEFYGATEGNSNLVNIDNKVGCVGFV 339
Cdd:PRK05857 261 VATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADvRFIEATGVRT-AQVYGLSETGCTALCLPTDDGSIVKI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 340 PRLA-GPVYP-VVLLKVDKDTEEPirNSKGfcircqpGEPGICVGKINSKQTiSTFLGYADKVESEKKILknvfkkGDNY 417
Cdd:PRK05857 340 EAGAvGRPYPgVDVYLAATDGIGP--TAPG-------AGPSASFGTLWIKSP-ANMLGYWNNPERTAEVL------IDGW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 418 FNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGM--VAIHDVDESVNL 495
Cdd:PRK05857 404 VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLavVASAELDESAAR 483
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 242022874 496 ---QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK05857 484 alkHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
7-534 |
1.03e-09 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 60.91 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSElsegvkeilgelkdiklyilnkskegeetNLgeaidlkkglaevskanlidevn 166
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQPE-----------------------------NL----------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 agkprdkLLFIYTSGTTGLPKAAVINNNRYLFISIGV-KILLKLHDDDILYNSLPLYHTSgvIVGAGQSILSGITVVIRK 245
Cdd:cd17644 109 -------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLiKEYGITSSDRVLQFASIAFDVA--AEEIYVTLLSGATLVLRP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 246 K---FSASNFWQDCIKYNCTV----ACYIGEIcryLLAVPEKSHDKQHKIRLMFGNG-----LKAQIWEKFVERFqiKQI 313
Cdd:cd17644 180 EemrSSLEDFVQYIQQWQLTVlslpPAYWHLL---VLELLLSTIDLPSSLRLVIVGGeavqpELVRQWQKNVGNF--IQL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 314 GEFYGATEGNsnlvnidnkvgcvgfvprLAGPVYPVVLLKVDKDTE----EPIRNSKGFCI-----RCQPGEPG-ICVGK 383
Cdd:cd17644 255 INVYGPTEAT------------------IAATVCRLTQLTERNITSvpigRPIANTQVYILdenlqPVPVGVPGeLHIGG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 384 INSKQtistflGYADKVE-SEKKILKNVF--KKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISN 460
Cdd:cd17644 317 VGLAR------GYLNRPElTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQ 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 461 IIGYKDAIVFGVEVPhvEGKAGMVA--IHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17644 391 HNDVKTAVVIVREDQ--PGNKRLVAyiVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
21-537 |
3.32e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 59.28 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVsaLINTNLRNQ----SFL 96
Cdd:PRK07470 22 DRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNFRQTpdevAYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 97 HSLKAAKcnALIYSSELSEGVKEILGELKDIKLYILNKSKEGEEtnlgeaidlkkGLAEVSKANLIDEV-NAGKPRDK-L 174
Cdd:PRK07470 100 AEASGAR--AMICHADFPEHAAAVRAASPDLTHVVAIGGARAGL-----------DYEALVARHLGARVaNAAVDHDDpC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 175 LFIYTSGTTGLPKAAVINNNRYLFIsigvkILLKLHD-------DDILYNSLPLYHtsgvivGAGQSILS----GITVVI 243
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQMAFV-----ITNHLADlmpgtteQDASLVVAPLSH------GAGIHQLCqvarGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 244 --RKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERfQIKQIG----EFY 317
Cdd:PRK07470 236 lpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG--APMYRADQKR-ALAKLGkvlvQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 318 GATEGNSNLVNI-----------DNKVGCVGFvPRLAgpvypvvllkvdkdTEEPIRNSKGfcIRCQPGEPG-ICV-GKi 384
Cdd:PRK07470 313 GLGEVTGNITVLppalhdaedgpDARIGTCGF-ERTG--------------MEVQIQDDEG--RELPPGETGeICViGP- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 385 nskqtiSTFLGYADKVESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGY 464
Cdd:PRK07470 375 ------AVFAGYYNNPEANAKAFR------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAV 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242022874 465 KDAIVFGVEVPhVEGKAG-MVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQME 537
Cdd:PRK07470 443 SEVAVLGVPDP-VWGEVGvAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
17-214 |
4.83e-09 |
|
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: 59.11 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 17 EKNYDKIAFHQE------NISWTY----KQVNEYSNGIghyfKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:cd05966 64 KERGDKVAIIWEgdepdqSRTITYrellREVCRFANVL----KSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 NTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEIlgELKDIKLYILNKSKEGEE----TNLGEAIDLKKG--------LA 154
Cdd:cd05966 140 FAGFSAESLADRINDAQCKLVITADGGYRGGKVI--PLKEIVDEALEKCPSVEKvlvvKRTGGEVPMTEGrdlwwhdlMA 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 155 EVSKANLIDEVNAGKPrdklLFI-YTSGTTGLPKAAVINNNRYLfisIGVKILLK----LHDDDI 214
Cdd:cd05966 218 KQSPECEPEWMDSEDP----LFIlYTSGSTGKPKGVVHTTGGYL---LYAATTFKyvfdYHPDDI 275
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
21-534 |
5.05e-09 |
|
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: 58.85 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLK 100
Cdd:cd12118 19 DRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIYSSELsegvkeilgelkdiklyilnkskEGEEtnlgeAIDLKKGLAEVSKANliDEvnagkpRDKLLFIYTS 180
Cdd:cd12118 99 HSEAKVLFVDREF-----------------------EYED-----LLAEGDPDFEWIPPA--DE------WDPIALNYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 181 GTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKkFSASNFWQDCIKYN 260
Cdd:cd12118 143 GTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRK-VDAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 261 CTVACYIGEICRYLLAVPEKSHDK-QHKIRLMFGNGLKAqiwekFVERFQIKQIG----EFYGATEG-----------NS 324
Cdd:cd12118 222 VTHFCGAPTVLNMLANAPPSDARPlPHRVHVMTAGAPPP-----AAVLAKMEELGfdvtHVYGLTETygpatvcawkpEW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 325 NLVNIDNKVGC-----VGFVPRLAGPVypvvllkVDKDTEEPIrnskgfcircqPGEpGICVGKINSKQTIsTFLGYADK 399
Cdd:cd12118 297 DELPTEERARLkarqgVRYVGLEEVDV-------LDPETMKPV-----------PRD-GKTIGEIVFRGNI-VMKGYLKN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 400 VESEKKILKnvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGV------E 473
Cdd:cd12118 357 PEATAEAFR------GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpdekwgE 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242022874 474 VPHvegkaGMVAIHDvDESVNLQEFDEKLKKMLPSYARPLFVrIIKNLPLTGTYKLKKKEL 534
Cdd:cd12118 431 VPC-----AFVELKE-GAKVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVL 484
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
21-534 |
5.59e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 58.84 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYsngIGHY---FKSQGYKKGDTIALYMENSIEYMCIwLGLAKLgivSALINTNLR------ 91
Cdd:PRK06188 27 DRPALVLGDTRLTYGQLADR---ISRYiqaFEALGLGTGDAVALLSLNRPEVLMA-IGAAQL---AGLRRTALHplgsld 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 92 NQSFLhsLKAAKCNALIYSS----ELSEGVKEILGELKDIkLYIlnkskeGEetnLGEAIDLKKGLAEVSKANLideVNA 167
Cdd:PRK06188 100 DHAYV--LEDAGISTLIVDPapfvERALALLARVPSLKHV-LTL------GP---VPDGVDLLAAAAKFGPAPL---VAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 168 GKPRDKLLFIYTSGTTGLPKAAVINNNrylfiSIGVKILLKLHD----DDILY-NSLPLYHTSGVIVGAgqSILSGITVV 242
Cdd:PRK06188 165 ALPPDIAGLAYTGGTTGKPKGVMGTHR-----SIATMAQIQLAEwewpADPRFlMCTPLSHAGGAFFLP--TLLRGGTVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 IRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFgNGLKAQIWEKFVErfQIKQIG----EFYG 318
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVY-YGASPMSPVRLAE--AIERFGpifaQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 319 ATEGNSNLVNIDNKVGCVGFVPRLAGPVYPVVLLKV---DKDTEEpirnskgfcirCQPGEPG-ICV-GKINSKqtistf 393
Cdd:PRK06188 315 QTEAPMVITYLRKRDHDPDDPKRLTSCGRPTPGLRVallDEDGRE-----------VAQGEVGeICVrGPLVMD------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 394 lGYADKVESEKKILKNvfkkgdNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGve 473
Cdd:PRK06188 378 -GYWNRPEETAEAFRD------GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG-- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242022874 474 VPHveGKAGMvAIHDV-----DESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK06188 449 VPD--EKWGE-AVTAVvvlrpGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
21-244 |
6.18e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 58.34 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTnlrnqSFLHSLK 100
Cdd:PRK09029 18 QAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-----QLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALiysselsegvkeilgelkDIKlYILNKSKEGEETNLGEAIdlkkglaevskANLIDEVNAGKPRDKLL--FIY 178
Cdd:PRK09029 93 EELLPSL------------------TLD-FALVLEGENTFSALTSLH-----------LQLVEGAHAVAWQPQRLatMTL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242022874 179 TSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSgvivgaGQSI-----LSGITVVIR 244
Cdd:PRK09029 143 TSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVS------GQGIvwrwlYAGATLVVR 207
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
17-190 |
3.18e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 56.52 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 17 EKNYDkIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFL 96
Cdd:PTZ00216 108 ERTME-VTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 97 HSLKAAKCNALIYSselSEGVKEILGELKDIKL------YI--LNKSKEGEETNLGEAID-LKKGLAEVSKANLIDEVNa 167
Cdd:PTZ00216 187 YALRETECKAIVCN---GKNVPNLLRLMKSGGMpnttiiYLdsLPASVDTEGCRLVAWTDvVAKGHSAGSHHPLNIPEN- 262
|
170 180
....*....|....*....|....
gi 242022874 168 gkpRDKLLFI-YTSGTTGLPKAAV 190
Cdd:PTZ00216 263 ---NDDLALImYTSGTTGDPKGVM 283
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
7-467 |
8.85e-08 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 55.06 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAF------HQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLG 80
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 81 IVSALINTNLRNQSFLHSLKAAKCNALIYSSE--------LSEGVKEILGELKDIklYILNkskeGEETNLGEAIDLKKG 152
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaaMARRLRPELPALRHV--VVVG----GDGADSFEALLITPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 153 LAEVSKANLIDEVNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAG 232
Cdd:PRK13295 179 WEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 233 QSILSGITVVIRKKFSASNFW----QDCIKYNCTVACYIGEICRyllAVPEKSHD-KQHKIRLMFGnglkAQIWEKFVER 307
Cdd:PRK13295 259 MPVMLGATAVLQDIWDPARAAelirTEGVTFTMASTPFLTDLTR---AVKESGRPvSSLRTFLCAG----APIPGALVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 308 FQIK---QIGEFYGATEgnsnlvNIDNKVGCVGFVPRLA----GPVYPVVLLKVDKDTEEPIrnskgfcircQPGEpgic 380
Cdd:PRK13295 332 ARAAlgaKIVSAWGMTE------NGAVTLTKLDDPDERAsttdGCPLPGVEVRVVDADGAPL----------PAGQ---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 381 VGKINSKQTiSTFLGYADKVEsekkiLKNVfkKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISN 460
Cdd:PRK13295 392 IGRLQVRGC-SNFGGYLKRPQ-----LNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYR 463
|
490
....*....|....*
gi 242022874 461 --------IIGYKDA 467
Cdd:PRK13295 464 hpaiaqvaIVAYPDE 478
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-191 |
9.05e-08 |
|
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: 55.25 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGivSAL- 85
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG--AAYv 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 86 -INTNLRNQSFLHSLKAAKCNALIYSSELSEgvkeilgELKDIKLYILnkskegeetnlgeAIDlKKGLAEVSKANLIDE 164
Cdd:COG1020 555 pLDPAYPAERLAYMLEDAGARLVLTQSALAA-------RLPELGVPVL-------------ALD-ALALAAEPATNPPVP 613
|
170 180
....*....|....*....|....*....
gi 242022874 165 VNagkPRDklL--FIYTSGTTGLPKAAVI 191
Cdd:COG1020 614 VT---PDD--LayVIYTSGSTGRPKGVMV 637
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
33-535 |
1.01e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.63 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LsEGVKEILGELKDIKLyilnkskegeetNLGEAIDlkkGLAEVSKAnlidEVNAGKPRDK----LLFIYTSGTTGLPKA 188
Cdd:PRK13390 106 L-DGLAAKVGADLPLRL------------SFGGEID---GFGSFEAA----LAGAGPRLTEqpcgAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 A-------VINNNRYLFISIGvKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGiTVVIRKKFSASNFWQDCIKYNC 261
Cdd:PRK13390 166 IqpdlpgrDVDAPGDPIVAIA-RAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGG-TVVLAKRFDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 262 TVACYIGEICRYLLAVPEKshdkqhkIRLMFG-NGLKAQIWEKFVERFQIKQ---------IGEFYGATEGNS-NLVNID 330
Cdd:PRK13390 244 TVTQMVPTMFVRLLKLDAD-------VRTRYDvSSLRAVIHAAAPCPVDVKHamidwlgpiVYEYYSSTEAHGmTFIDSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 331 NKVGCVGFVPRlagPVYPVVLLKVDKDTEEPirnskgfcircqPGEpgicVGKINSKQTISTFlGYADKVE--SEKKILK 408
Cdd:PRK13390 317 DWLAHPGSVGR---SVLGDLHICDDDGNELP------------AGR----IGTVYFERDRLPF-RYLNDPEktAAAQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 409 NVFkkgdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHV--EGKAGMVAI 486
Cdd:PRK13390 377 HPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMgeQVKAVIQLV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 242022874 487 HDVDESVNL-QEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK13390 452 EGIRGSDELaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
33-232 |
1.01e-07 |
|
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: 54.53 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIysse 112
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 lsegvkeilgelkdiklyilnkskegeeTNlgeaidlkkglaevskanlidevnaGKPRDKLLFIYTSGTTGLPKAAVIN 192
Cdd:cd17639 83 ----------------------------TD-------------------------GKPDDLACIMYTSGSTGNPKGVMLT 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 193 NnrYLFIS----IGVKILLKLHDDDILYNSLPLYH-----------TSGVIVGAG 232
Cdd:cd17639 110 H--GNLVAgiagLGDRVPELLGPDDRYLAYLPLAHifelaaenvclYRGGTIGYG 162
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
11-534 |
1.25e-07 |
|
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: 54.51 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 11 VFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNL 90
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 91 RNQSFLHSLKAAKCNALIysseLSEGVKEILGELKDIkLYILNKSKEGEETNLGEAIDlkkglaevskanlidevnagkP 170
Cdd:cd12117 82 PAERLAFMLADAGAKVLL----TDRSLAGRAGGLEVA-VVIDEALDAGPAGNPAVPVS---------------------P 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 171 RDKLLFIYTSGTTGLPKAA----------VINNNrylFISIGVkillklhDDDILYNSLPLYHTSGV-IVGAgqsILSGI 239
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVavthrgvvrlVKNTN---YVTLGP-------DDRVLQTSPLAFDASTFeIWGA---LLNGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 240 TVVIRKKfsasnfwqdcikyncTVACYIGEICRYLlavpekshdKQHKIRLMF-GNGLKAQIWEKFVERF-QIKQI---G 314
Cdd:cd12117 203 RLVLAPK---------------GTLLDPDALGALI---------AEEGVTVLWlTAALFNQLADEDPECFaGLRELltgG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 315 E---------------------FYGATEgnsnlvnidNKVGCVGFV---PRLAGPVYPVVLlkvdkdteePIRNSKGFCI 370
Cdd:cd12117 259 EvvspphvrrvlaacpglrlvnGYGPTE---------NTTFTTSHVvteLDEVAGSIPIGR---------PIANTRVYVL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 371 R-----CQPGEPG-ICVGKInskqtiSTFLGYADKVE-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFR 443
Cdd:cd12117 321 DedgrpVPPGVPGeLYVGGD------GLALGYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 444 WKGENVATSEVEAVISNIIGYKDAIVfgVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPL 523
Cdd:cd12117 395 IRGFRIELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPL 472
|
570
....*....|.
gi 242022874 524 TGTYKLKKKEL 534
Cdd:cd12117 473 TANGKVDRRAL 483
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
28-531 |
2.86e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 53.21 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 28 ENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENS----IEYMCIWlglAKLGIVSALintnlrnqsfLHSLKAak 103
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRpewgIAFFAIW---TYGAIAVPI----------LAEFTA-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 104 cnaliysselsegvkeilgelKDIKlYILNKSKegeetnlgeaidlkkglaevSKAnlideVNAGKPRDKLLFIYTSGTT 183
Cdd:cd05914 69 ---------------------DEVH-HILNHSE--------------------AKA-----IFVSDEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 184 GLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNF----------- 252
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIialafaqvtpt 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 253 ------WQ-DCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIR--LM--FGNGLKAQI-----WEKFVERFqIKQIG-- 314
Cdd:cd05914 182 lgvpvpLViEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFkkVHeaFGGNIKEFViggakINPDVEEF-LRTIGfp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 315 --EFYGATEgNSNLV--NIDNKvgcvgFVPRLAGPVYPVVLLKVDKDTEEPirnskgfcircQPGEPgICVGKinskqti 390
Cdd:cd05914 261 ytIGYGMTE-TAPIIsySPPNR-----IRLGSAGKVIDGVEVRIDSPDPAT-----------GEGEI-IVRGP------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 391 STFLGYADKVESEKKIlknvFKKgDNYFNSGDILVMDDYGYFSFKDRTGDTFRW-KGENVATSEVEAVISNIIGYKDAIV 469
Cdd:cd05914 316 NVMKGYYKNPEATAEA----FDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLV 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 470 FgveVPHVEGKAGMVAIHDVDESVNLQ----------EFDEKLKKMLPSYARPLFVRIIK-NLPLTGTYKLKK 531
Cdd:cd05914 391 V---VQEKKLVALAYIDPDFLDVKALKqrniidaikwEVRDKVNQKVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
52-241 |
3.05e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.43 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 52 GYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSELSEgvKEILGEL-----KD 126
Cdd:PRK06814 678 NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIE--KARLGPLiealeFG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 127 IKLYILNKSKEGeeTNLGEAIdlkKGLAEVSKANLidEVNAGKPRDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKIL 206
Cdd:PRK06814 756 IRIIYLEDVRAQ--IGLADKI---KGLLAGRFPLV--YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAAR 828
|
170 180 190
....*....|....*....|....*....|....*
gi 242022874 207 LKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITV 241
Cdd:PRK06814 829 IDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
29-535 |
3.15e-07 |
|
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: 53.20 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 29 NISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALI 108
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 109 YSSELSEGVKEILGELKDIKLYILNKSKEGEETNLgeaidLKKGLAEVSKANLIDEVnagkprDKLLFIYTSGTTGLPKA 188
Cdd:cd05915 102 FDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLA-----YEEALGEEADPVRVPER------AACGMAYTTGTTGLPKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 AVINN-NRYL-FISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVIRKKFSASNFWQDCIKYNCTVACY 266
Cdd:cd05915 171 VVYSHrALVLhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 267 IGEICRyLLAVPEKSHDKQH--KIRLMFGNGLKAQIwekfveRFQIKQIGEF-----YGATEgnsnlvNIDNKVGCVGFV 339
Cdd:cd05915 251 VPTVWL-ALADYLESTGHRLktLRRLVVGGSAAPRS------LIARFERMGVevrqgYGLTE------TSPVVVQNFVKS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 340 PRLAGPVYPVVLLKVDK---------DTEEPIRNS---KGFCIRcqpgepgicVGKINSKQTISTFlgYADKVESEkkil 407
Cdd:cd05915 318 HLESLSEEEKLTLKAKTglpiplvrlRVADEEGRPvpkDGKALG---------EVQLKGPWITGGY--YGNEEATR---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 408 KNVFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGveVPHVEGKAGMVAIH 487
Cdd:cd05915 383 SALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA--IPHPKWQERPLAVV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 242022874 488 DVDES-VNLQEFDEKLKKMLPSYAR-PLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:cd05915 459 VPRGEkPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
11-191 |
3.62e-07 |
|
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: 52.93 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 11 VFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNL 90
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 91 ---RNQSFLHSLKAakcnALIYSSELSegvkeilgelkDIkLYIlnkskegeetnlgeaidlkkglaevskanlidevna 167
Cdd:cd05918 84 plqRLQEILQDTGA----KVVLTSSPS-----------DA-AYV------------------------------------ 111
|
170 180
....*....|....*....|....
gi 242022874 168 gkprdkllfIYTSGTTGLPKAAVI 191
Cdd:cd05918 112 ---------IFTSGSTGKPKGVVI 126
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
10-187 |
4.91e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.59 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 10 KVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTN 89
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 90 LRNQSFLHSLKAAKCNALIYSSELSEGVKEIlgelKDIKLYILNKSKEGEETnlgeaidlkkglaevskanlIDEVNAGK 169
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLIIATEELPLEILGI----PVITLDELKDIFATGNP--------------------YDFDHAVK 141
|
170
....*....|....*...
gi 242022874 170 PRDKLLFIYTSGTTGLPK 187
Cdd:PRK04813 142 GDDNYYIIFTSGTTGKPK 159
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
7-534 |
5.43e-07 |
|
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: 52.33 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALI 86
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 87 ntnlrnqsfLHSLKAAKCNALIyssELSEGVkeilgelkdiklyilnkskegeetnlgeAIDLKKGLAEVSKANLIDEVN 166
Cdd:cd05920 96 ---------LPSHRRSELSAFC---AHAEAV----------------------------AYIVPDRHAGFDHRALARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 167 AGKPrDKLLFIYTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYH----TSGVIVGAgqsILSGITVV 242
Cdd:cd05920 136 ESIP-EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplACPGVLGT---LLAGGRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 IRKKFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLM------FGNGLKAQIWEKFVERFQikqigEF 316
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLqvggarLSPALARRVPPVLGCTLQ-----QV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEGNSNLVNIDnkvgcvgfvprlagpvypvvllkvdkDTEEPIRNSKGFCIR--------------CQPGEPGicvg 382
Cdd:cd05920 287 FGMAEGLLNYTRLD--------------------------DPDEVIIHTQGRPMSpddeirvvdeegnpVPPGEEG---- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 383 kinskQTIS----TFLGYADKVESEKKilknVFKKgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVI 458
Cdd:cd05920 337 -----ELLTrgpyTIRGYYRAPEHNAR----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 459 SNIIGYKDAIVfgVEVPH-VEGKAGMVAIHDVDESVNLQEFDEKLKKM-LPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd05920 407 LRHPAVHDAAV--VAMPDeLLGERSCAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
33-223 |
5.58e-07 |
|
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: 52.22 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDT--IALYMENSIEYMCIWLGLAKLGIVS-ALINTnLRNQSFLHSLKAAKCNALIY 109
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTvPLYDT-LGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 110 SselsegvkeilgelKDIKLYILNKskegeetnlgeaidlkkgLAEVSKANLIDeVNAGKPRDKLLFIYTSGTTGLPKAA 189
Cdd:cd05927 86 D--------------AGVKVYSLEE------------------FEKLGKKNKVP-PPPPKPEDLATICYTSGTTGNPKGV 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 242022874 190 VINN----NRYLFISIGVKILLKLHDDDILYNSLPLYH 223
Cdd:cd05927 133 MLTHgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
12-534 |
9.40e-07 |
|
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: 51.58 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 12 FQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLR 91
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 92 NQSFLHSLKAAKCNALIYSSELSEGVkeilgelkdiklyilnkskeGEETNLGEAIDLKKGLAEVSkANLIDEVNAGKPr 171
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGEL--------------------AVELVAVTLLDQPGAAAGAD-AEPDPALDADDL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 172 dkLLFIYTSGTTGLPKAAVINnnrylfiSIGVKILLKLHDDdiLYNSLPLYHTSGvIVGAG-----QSILS----GITVV 242
Cdd:cd17651 139 --AYVIYTSGSTGRPKGVVMP-------HRSLANLVAWQAR--ASSLGPGARTLQ-FAGLGfdvsvQEIFStlcaGATLV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 243 IRK---KFSASNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMFGNGLKAQIWE---KFVERFQIKQIGEF 316
Cdd:cd17651 207 LPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEdlrEFCAGLPGLRLHNH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 317 YGATEgnSNLVN---IDNKVGCVGFVPRLAGPVYPVVLLKVDKDtEEPirnskgfcirCQPGEPG-ICVGKInskqtiST 392
Cdd:cd17651 287 YGPTE--THVVTalsLPGDPAAWPAPPPIGRPIDNTRVYVLDAA-LRP----------VPPGVPGeLYIGGA------GL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 393 FLGYADKVE-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfg 471
Cdd:cd17651 348 ARGYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV-- 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 472 VEVPHVEGKAGMVA--IHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17651 426 LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
32-241 |
1.46e-06 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 50.88 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYS- 110
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SELSEGVKEILGELKDIKLYI------LNKSKEGEETNLGEAIDLKKGLAEVSKANLIDEVNAGKPRDKLLFIYTSGTTG 184
Cdd:cd17641 92 EEQVDKLLEIADRIPSVRYVIycdprgMRKYDDPRLISFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 185 LPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITV 241
Cdd:cd17641 172 KPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV 228
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
31-87 |
2.17e-06 |
|
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: 50.83 E-value: 2.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALIN 87
Cdd:TIGR03443 270 SFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVID 326
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
170-243 |
2.22e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 170 PRDKLLFI-YTSGTTGLPKAAVINN-----NRYLfISIGVKIllKLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVVI 243
Cdd:PRK05691 164 QPDDIAFLqYTSGSTALPKGVQVSHgnlvaNEQL-IRHGFGI--DLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL 240
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
31-242 |
3.92e-06 |
|
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: 49.54 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGyKKGDTIALYMENSIEYMCIWLG--LAKLGIVSALINTNLRNQSFLHSLkAAKCN--A 106
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGclYAGAIAVPLPPPTPGRHAERLAAI-LADAGprV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 107 LIYSSELSEGVKEILGELkdiklyilnkskEGEETNLGEAIDLkkglAEVSKANliDEVNAGKPRDKLLFI-YTSGTTGL 185
Cdd:cd05931 102 VLTTAAALAAVRAFAASR------------PAAGTPRLLVVDL----LPDTSAA--DWPPPSPDPDDIAYLqYTSGSTGT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 186 PKAAVIN------NNRYLFISIGvkillkLHDDDILYNSLPLYHTSGVIVGAGQSILSGITVV 242
Cdd:cd05931 164 PKGVVVThrnllaNVRQIRRAYG------LDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
453-528 |
6.14e-06 |
|
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: 44.46 E-value: 6.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 453 EVEAVISNIIGYKDAIVFGVEVPhVEGKAGMV-AIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYK 528
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
6-235 |
7.91e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.96 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 6 STVAKVFQEICEKNYDK--------IAFHQENIS--------------W-TYKQVNE----YSNGIGHYfksqGYKKGDT 58
Cdd:PLN02387 58 TTLAALFEQSCKKYSDKrllgtrklISREFETSSdgrkfeklhlgeyeWiTYGQVFErvcnFASGLVAL----GHNKEER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 59 IALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSELSEGVKEILGELKDIK--LYILNKSK 136
Cdd:PLN02387 134 VAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKrvIYMDDEGV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 137 EGEETNLGEAIDLKKGLAEVSKANLIDEVNAGKPR--DKLLFIYTSGTTGLPKAAVINNNRYLFISIGV-KILLKLHDDD 213
Cdd:PLN02387 214 DSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSpnDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVmTVVPKLGKND 293
|
250 260
....*....|....*....|....*..
gi 242022874 214 ILYNSLPLYH-----TSGVIVGAGQSI 235
Cdd:PLN02387 294 VYLAYLPLAHilelaAESVMAAVGAAI 320
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
395-534 |
1.04e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 48.08 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 395 GYADKVE-SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfgve 473
Cdd:cd12115 307 GYLGRPGlTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVV---- 382
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 474 VPHVEGKAG--MVA--IHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd12115 383 VAIGDAAGErrLVAyiVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
410-538 |
1.09e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 48.11 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 410 VFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPhVEG---KAGMVAI 486
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDP-VAGervKAKVISH 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 242022874 487 HDVDeSVNLQEFdekLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQMEG 538
Cdd:PRK08308 364 EEID-PVQLREW---CIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
33-535 |
1.24e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 48.21 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCNALIYSSE 112
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 113 LSEGVKEILGELKDIKLYILNKSKEG-EETNLGEAIDLKKGLAEVS---KANLIDEVNAGKprdkllFIYTSGTTGLPKA 188
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLTDAAHmPQTTLKNAVAYEEWIAEADgdfAWKTFDENTAAG------MCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 189 AVIN---NNRYLFISIGVKILlKLHDDDILYNSLPLYHT-------SGVIVGA----------GQSI---LSGITVVirk 245
Cdd:PRK06018 195 VLYShrsNVLHALMANNGDAL-GTSAADTMLPVVPLFHAnswgiafSAPSMGTklvmpgakldGASVyelLDTEKVT--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 246 kFSAS--NFWQdcikynctvacyigeicrYLLAVPEKSHDKQHKIRLMFGNGlkAQIWEKFVERFQIKQIGEF--YGATE 321
Cdd:PRK06018 271 -FTAGvpTVWL------------------MLLQYMEKEGLKLPHLKMVVCGG--SAMPRSMIKAFEDMGVEVRhaWGMTE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 322 GNSnlvnidnkVGCVGFVP----RLAG------------PVYPVVLLKVDKDTEEPIRNSKGFCiRCQPGEPGICvgkin 385
Cdd:PRK06018 330 MSP--------LGTLAALKppfsKLPGdarldvlqkqgyPPFGVEMKITDDAGKELPWDGKTFG-RLKVRGPAVA----- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 386 skqtistflgyADKVESEKKILKNvfkkgDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEavisNI-IGY 464
Cdd:PRK06018 396 -----------AAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLE----NLaVGH 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242022874 465 KD---AIVFGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKELQ 535
Cdd:PRK06018 456 PKvaeAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
31-223 |
1.27e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 48.17 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 31 SW-TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQS--FL--HS-LKAAKC 104
Cdd:PLN02736 77 KWmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAvkFIvnHAeVAAIFC 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 105 NALIYSSELSegvkeILGELKDIKLYILnksKEGEETNLGEaIDLKKGLAEVSKANLIDEVNAG-------KPRDKLLFI 177
Cdd:PLN02736 157 VPQTLNTLLS-----CLSEIPSVRLIVV---VGGADEPLPS-LPSGTGVEIVTYSKLLAQGRSSpqpfrppKPEDVATIC 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 242022874 178 YTSGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYH 223
Cdd:PLN02736 228 YTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
31-87 |
1.55e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.90 E-value: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 31 SWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALIN 87
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVID 76
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
404-534 |
1.64e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 47.63 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 404 KKILKN------VFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVIsniigYKD-AIVFGV---- 472
Cdd:PRK08162 400 KGYLKNpkateeAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL-----YRHpAVLVAAvvak 472
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 473 ------EVPH--VEGKAGMvaihdvdeSVNLQEFDEKLKKMLPSYARPLFVRiIKNLPLTGTYKLKKKEL 534
Cdd:PRK08162 473 pdpkwgEVPCafVELKDGA--------SATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
33-243 |
2.53e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.96 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHS-LK--AAKCN-ALI 108
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAkLKhlFDLVKpRVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 109 Y--SSELSEGVKEILGeLKDIKLYILNKSKEGEETnlgeaidlkKGLAEVSKANLIDEVNAGKPR------DKLLFiyTS 180
Cdd:PRK12582 162 FaqSGAPFARALAALD-LLDVTVVHVTGPGEGIAS---------IAFADLAATPPTAAVAAAIAAitpdtvAKYLF--TS 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242022874 181 GTTGLPKaAVINNNRYLFISIGVKILLKLHDDD----ILYNSLPLYHTSGVIVGAGQSILSGITVVI 243
Cdd:PRK12582 230 GSTGMPK-AVINTQRMMCANIAMQEQLRPREPDppppVSLDWMPWNHTMGGNANFNGLLWGGGTLYI 295
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-187 |
4.39e-05 |
|
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: 46.29 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 7 TVAKVFQEICEKNYDKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVS--A 84
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPvfA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 85 LINTNLRNQSFLHSLKAAKcnALIYSSELS-----EGVKEILGELKDIKLYILnkskegeetnLGEAIDLkKGLAEVSKA 159
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAV--AYIIPDRHRgfdyrALARELQAEVPSLRHVLV----------VGDAGEF-TSLDALLAA 172
|
170 180
....*....|....*....|....*...
gi 242022874 160 NLIDEVNAGKPRDKLLFIYTSGTTGLPK 187
Cdd:COG1021 173 PADLSEPRPDPDDVAFFQLSGGTTGLPK 200
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
21-534 |
4.43e-05 |
|
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: 46.11 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTnlrnqsflhSLK 100
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI---------DQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIYSSelseGVKEILGELKDIKLYILNkskegeETNLGEAIDLKKGLAEVSKANLidevnagKPRDKLLFIYTS 180
Cdd:cd12114 73 AARREAILADA----GARLVLTDGPDAQLDVAV------FDVLILDLDALAAPAPPPPVDV-------APDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 181 GTTGLPKAAVINN----------NRYLFISIGVKILL--KLHDDdilynsLPLYHTSGVIVgagqsilSGITVVI--RKK 246
Cdd:cd12114 136 GSTGTPKGVMISHraalntildiNRRFAVGPDDRVLAlsSLSFD------LSVYDIFGALS-------AGATLVLpdEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 247 FSASNFWQDCI-KYNCTVACYIGEICRYLLAVPEKSHDKQHKIR--LMFGN----GLKAQIWEKFVErfqikqiGEFY-- 317
Cdd:cd12114 203 RRDPAHWAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRlvLLSGDwiplDLPARLRALAPD-------ARLIsl 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 318 -GATEGN--SNLVNIDNKVGCVGFVPR---LAGPVYPVVllkvDKDTEEpirnskgfcirCQPGEPG-ICVGKINSKQti 390
Cdd:cd12114 276 gGATEASiwSIYHPIDEVPPDWRSIPYgrpLANQRYRVL----DPRGRD-----------CPDWVPGeLWIGGRGVAL-- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 391 stflGY-ADKVESEKKILKNvfKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIV 469
Cdd:cd12114 339 ----GYlGDPELTAARFVTH--PDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242022874 470 FGVEVPHVEGKAGMVAIHDVDESVNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd12114 413 VVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
404-535 |
5.53e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 45.99 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 404 KKILKN------VFKKGdnYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVIsniigYKDAIVFGVEV--- 474
Cdd:PLN02479 414 KGYLKNpkaneeAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV-----YTHPAVLEASVvar 486
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242022874 475 PHV---EGKAGMVAIHD----VDESVNLQEFDEKLKKMLPSYARPLFVrIIKNLPLTGTYKLKKKELQ 535
Cdd:PLN02479 487 PDErwgESPCAFVTLKPgvdkSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
32-228 |
5.82e-05 |
|
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: 45.74 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 WTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYM-----CIWLGL--AKLGIVSALINTNLRNQSFLHSLKAAKC 104
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIpafwaCVLAGFvpAPLTVPPTYDEPNARLRKLRHIWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 105 NALIYSSELSEGVKEIlgelkdiklyilnkskegeetnlgEAIDLKKGLAEVSKANLID-----EVNAGKPRDKLLFIYT 179
Cdd:cd05906 120 PVVLTDAELVAEFAGL------------------------ETLSGLPGIRVLSIEELLDtaadhDLPQSRPDDLALLMLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 242022874 180 SGTTGLPKAAVINNNRYLFISIGVKILLKLHDDDILYNSLPLYHTSGVI 228
Cdd:cd05906 176 SGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
33-223 |
6.18e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 45.78 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNLRNQSFLHSLKAAKCN-ALIYSS 111
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSiVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 112 ELSEGVKEILGELKDIKLYI----LNKSKEGEETNLGEAIDLKKGLAEVSKANLIDeVNAGKPRDKLLFIYTSGTTGLPK 187
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVsfggVSREQKEEAETFGLVIYAWDEFLKLGEGKQYD-LPIKKKSDICTIMYTSGTTGDPK 239
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 242022874 188 AAVINNNRYLFISIGVKILLK-----LHDDDILYNSLPLYH 223
Cdd:PLN02614 240 GVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAH 280
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
21-191 |
7.61e-05 |
|
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: 45.36 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGIVSALINTNL---RNQsflH 97
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpadRLR---Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 98 SLKAAKCNALIYSSELSEGVKEILGELkdiklyilnkskegeetnlgeaidlkkGLAEVSKANLIDEVNAGKPRDKLLF- 176
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLPVL---------------------------LLALAAAAAAPAAPRTPVSPDDLAYv 131
|
170
....*....|....*
gi 242022874 177 IYTSGTTGLPKAAVI 191
Cdd:cd12116 132 IYTSGSTGRPKGVVV 146
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
32-223 |
9.12e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 45.58 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 32 W-TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEymciWLGLAKLGIVSALINTNLRNqsflhSLKAAKCNALIYS 110
Cdd:PLN02430 76 WkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQ----WIVAMEACAAHSLICVPLYD-----TLGPGAVDYIVDH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 111 SEL------SEGVKEIL----GELKDIKLYILNKSKEGEETNLGEAIDLK----KGLAEVSKANlIDEVNAGKPRDKLLF 176
Cdd:PLN02430 147 AEIdfvfvqDKKIKELLepdcKSAKRLKAIVSFTSVTEEESDKASQIGVKtyswIDFLHMGKEN-PSETNPPKPLDICTI 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 242022874 177 IYTSGTTGLPKAAVINNNRYLFISIGVKILL-----KLHDDDILYNSLPLYH 223
Cdd:PLN02430 226 MYTSGTSGDPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAH 277
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-534 |
1.12e-03 |
|
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: 41.52 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 21 DKIAFHQENISWTYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYMCIWLGLAKLGivSALINTNLRNqsflhslk 100
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAY-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 101 AAKCNALIysselsegvkeilgeLKDIKLYILnkskegeetnLGEAIDLkkglAEVskanlidevnagkprdkllfIYTS 180
Cdd:cd17643 72 PVERIAFI---------------LADSGPSLL----------LTDPDDL----AYV--------------------IYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 181 GTTGLPKAAVIN--NNRYLFISIGVkiLLKLHDDDILYnslpLYHTSGV------IVGAgqsILSGITVVIRKKF---SA 249
Cdd:cd17643 103 GSTGRPKGVVVShaNVLALFAATQR--WFGFNEDDVWT----LFHSYAFdfsvweIWGA---LLHGGRLVVVPYEvarSP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 250 SNFWQDCIKYNCTVACYIGEICRYLLAVPEKSHDKQHKIRLMF--GNGLKAQIWEKFVERF--QIKQIGEFYGATEGnsn 325
Cdd:cd17643 174 EDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFglDRPQLVNMYGITET--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 326 lvnidnkvgCVgFVPrlagpVYPVVLLKVDKDTEEPI-RNSKGFCIRC-----QPGEPGIcVGKIN-SKQTIStfLGYAD 398
Cdd:cd17643 251 ---------TV-HVT-----FRPLDAADLPAAAASPIgRPLPGLRVYVldadgRPVPPGV-VGELYvSGAGVA--RGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 399 KVE--SEKKILKNVFKKGDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVfgveVPH 476
Cdd:cd17643 313 RPEltAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV----IVR 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242022874 477 vEGKAG---MVAIHDVDES--VNLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:cd17643 389 -EDEPGdtrLVAYVVADDGaaADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
33-259 |
3.34e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 40.21 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 33 TYKQVNEYSNGIGHYFKSQGYKKGDTIALYMENSIEYmciwlglaklgiVSALINTNLRNQSFL---HSLKAAKCNALIY 109
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEW------------IIAMEACNSQGITYVplyDTLGANAVEFIIN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 110 SSELS------EGVKEILGELKDIKLYILNKSKEGEETNL--GEAIDLKKGLAEVSKANLIDEVNAGKPR----DKLLFI 177
Cdd:PLN02861 147 HAEVSiafvqeSKISSILSCLPKCSSNLKTIVSFGDVSSEqkEEAEELGVSCFSWEEFSLMGSLDCELPPkqktDICTIM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 178 YTSGTTGLPKAAVINNNRYLFISIGVKILLKLHD-----DDILYNSLPLYHTSGVIVGagqsilsgiTVVIRKKfSASNF 252
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDrvateEDSYFSYLPLAHVYDQVIE---------TYCISKG-ASIGF 296
|
....*..
gi 242022874 253 WQDCIKY 259
Cdd:PLN02861 297 WQGDIRY 303
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
414-534 |
4.83e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 40.33 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242022874 414 GDNYFNSGDILVMDDYGYFSFKDRTGDTFRWKGENVATSEVEAVISNIIGYKDAIVFGVEVPHVEGKAGMVAIHDVDESV 493
Cdd:PRK12316 2379 GERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDL 2458
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 242022874 494 nLQEFDEKLKKMLPSYARPLFVRIIKNLPLTGTYKLKKKEL 534
Cdd:PRK12316 2459 -LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| |
