|
Name |
Accession |
Description |
Interval |
E-value |
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
107-634 |
0e+00 |
|
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: 810.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 107 FQLETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNIT 186
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 187 QVFIDPDasnpireseeeiknalpdvklnyleeqdlmhellnsqspeflqqdnvrtplgltdfKPSMLIYTSGTTGLPKS 266
Cdd:cd05937 81 FVIVDPD--------------------------------------------------------DPAILIYTSGTTGLPKA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 267 AIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVG 346
Cdd:cd05937 105 AAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 347 EVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDFGIGACRNYGTIIQW 426
Cdd:cd05937 185 ELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 427 FLSFQQTLVRMDPNDDSVIYRNSKGFCEVAPVGEPGEMLMRIFFpkKPETSFQGYLGNAKETKSKVVRDVFRRGDAWYRC 506
Cdd:cd05937 265 KFENQVVLVKMDPETDDPIRDPKTGFCVRAPVGEPGEMLGRVPF--KNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 507 GDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNkeQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAK 586
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHP--DIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEF 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41629676 587 TKLLNDSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQKLPK 634
Cdd:cd05937 421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
110-630 |
4.06e-146 |
|
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: 432.16 E-value: 4.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVF 189
Cdd:cd05940 2 EALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPdasnpireseeeiknalpdvklnyleeqdlmhellnsqspeflqqdnvrtplgltdfkpSMLIYTSGTTGLPKSAIM 269
Cdd:cd05940 81 VDA-----------------------------------------------------------ALYIYTSGTTGLPKAAII 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 270 SWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVC 349
Cdd:cd05940 102 SHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 350 RYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDFGIGACRNYGTiiqwfLS 429
Cdd:cd05940 182 RYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLR-----KV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 430 FQQTLVRMDPNDDSVIyRNSKGFCEVAPVGEPGEMLMRIffpkKPETSFQGYLGNAKETKsKVVRDVFRRGDAWYRCGDL 509
Cdd:cd05940 257 APLALVKYDLESGEPI-RDAEGRCIKVPRGEPGLLISRI----NPLEPFDGYTDPAATEK-KILRDVFKKGDAWFNTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 510 LKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIKVPKYEGRAGFAVIKLTDN-SLDITAKTK 588
Cdd:cd05940 331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAF--PGVEEANVYGVQVPGTDGRAGMAAIVLQPNeEFDLSALAA 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 41629676 589 LLNDslsrlNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:cd05940 409 HLEK-----NLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
75-669 |
1.63e-145 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 436.23 E-value: 1.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 75 RFQNWylfikqVQQNGDHLAIsytrpmaekgEFQLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLW 154
Cdd:PRK08279 42 VFEEA------AARHPDRPAL----------LFEDQSISYAELNARANRYAHWAA-ARGVGKGDVVALLMENRPEYLAAW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 155 LSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDPDasnpIRESEEEIKNALPDVKLNYLEEQD-----LMHELLNS 229
Cdd:PRK08279 105 LGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEE----LVEAFEEARADLARPPRLWVAGGDtlddpEGYEDLAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 230 QSPEFlQQDNVRTPLGLTDFKPSMLIYTSGTTGLPKSAIMS---WRKSSvgcQVFGHVLHMTNESTVFTAMPLFHSTAAL 306
Cdd:PRK08279 181 AAAGA-PTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMShmrWLKAM---GGFGGLLRLTPDDVLYCCLPLYHNTGGT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 307 LGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRF 386
Cdd:PRK08279 257 VAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 387 NIEVIGEFYAATEAPFATTTFqkgdFG-IGACrnyGtIIQWFLSFQQTLVRMDPNDDSVIyRNSKGFCEVAPVGEPGEML 465
Cdd:PRK08279 337 GIPRILEFYAASEGNVGFINV----FNfDGTV---G-RVPLWLAHPYAIVKYDVDTGEPV-RDADGRCIKVKPGEVGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 466 MRIfFPKKPetsFQGYlGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLT 545
Cdd:PRK08279 408 GRI-TDRGP---FDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 546 ASnkEQYAQVLVVGIKVPKYEGRAGFAVIKLTDN-SLDITAKTKLLNDslsrlNLPSYAMPLFVKFVDEIKMTDNHKilk 624
Cdd:PRK08279 483 GF--PGVEEAVVYGVEVPGTDGRAGMAAIVLADGaEFDLAALAAHLYE-----RLPAYAVPLFVRLVPELETTGTFK--- 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 41629676 625 kvYREQKLPK-GLD---GNDTIF-WLKNYKRYEVLTAADWEAIDAQTIKL 669
Cdd:PRK08279 553 --YRKVDLRKeGFDpskVDDPLYvLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
107-624 |
1.48e-119 |
|
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: 367.00 E-value: 1.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 107 FQLETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNIT 186
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 187 QVFIDPDasnpIRESEEEIKNALPD--VKLNYLEEQDLMH------ELLNSQSPEFLQQDnVRTPLGLTDfkPSMLIYTS 258
Cdd:cd05938 81 VLVVAPE----LQEAVEEVLPALRAdgVSVWYLSHTSNTEgvisllDKVDAASDEPVPAS-LRAHVTIKS--PALYIYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 259 GTTGLPKSAIMSWRKSsVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTG 338
Cdd:cd05938 154 GTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 339 ATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRF-NIEVIgEFYAATEAPFATTTFQKgdfGIGAC 417
Cdd:cd05938 233 VTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFgPIRIR-EFYGSTEGNIGFFNYTG---KIGAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 418 RNYGTIIQWFLSFQqtLVRMDPNDDSVIyRNSKGFCEVAPVGEPGEMLMRIffpkKPETSFQGYLGNAKETKSKVVRDVF 497
Cdd:cd05938 309 GRVSYLYKLLFPFE--LIKFDVEKEEPV-RDAQGFCIPVAKGEPGLLVAKI----TQQSPFLGYAGDKEQTEKKLLRDVF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 498 RRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQyaQVLVVGIKVPKYEGRAGFAVIKLT 577
Cdd:cd05938 382 KKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQ--EVNVYGVTVPGHEGRIGMAAVKLK 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41629676 578 DN-SLDITAKTKLLNDslsrlNLPSYAMPLFVKFVDEIKMTDNHKILK 624
Cdd:cd05938 460 PGhEFDGKKLYQHVRE-----YLPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
137-624 |
3.52e-112 |
|
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: 345.95 E-value: 3.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 137 GDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDPDAsnPIRESEEEIKNALPDVklny 216
Cdd:cd05939 28 GDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNLLD--PLLTQSSTEPPSQDDV---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 217 leeqdlmhellnsqspeflqqdnvrtplgltDFKPSML-IYTSGTTGLPKSAIMS----WRKSSVGCQVFGhvlhMTNES 291
Cdd:cd05939 102 -------------------------------NFRDKLFyIYTSGTTGLPKAAVIVhsryYRIAAGAYYAFG----MRPED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 292 TVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYG 371
Cdd:cd05939 147 VVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 372 NGLRPDIWQDFRKRFNIEVIGEFYAATEapfATTTFQKGDFGIGACrNYGTIIQWFLsFQQTLVRMDPNDDSVIyRNSKG 451
Cdd:cd05939 227 NGLRPQIWEQFVRRFGIPQIGEFYGATE---GNSSLVNIDNHVGAC-GFNSRILPSV-YPIRLIKVDEDTGELI-RDSDG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 452 FCEVAPVGEPGEMLMRIfFPKKPETSFQGYLgNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWK 531
Cdd:cd05939 301 LCIPCQPGEPGLLVGKI-IQNDPLRRFDGYV-NEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 532 SENVSTTEVEDQLtaSNKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAKTKLLNDSlsrlnLPSYAMPLFVKFV 611
Cdd:cd05939 379 GENVSTTEVEGIL--SNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKS-----LPPYARPQFIRLL 451
|
490
....*....|...
gi 41629676 612 DEIKMTDNHKILK 624
Cdd:cd05939 452 PEVDKTGTFKLQK 464
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
112-628 |
1.18e-70 |
|
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: 235.65 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 112 FTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLkisnitqvfid 191
Cdd:cd05934 4 WTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYII----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 192 pdasnpireseeeiknalpdvklnyleeqdlmhellnsqspeflqqDNVRTPLGLTDfkPSMLIYTSGTTGLPKSAIMSW 271
Cdd:cd05934 72 ----------------------------------------------DHSGAQLVVVD--PASILYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 272 RKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRY 351
Cdd:cd05934 104 ANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 352 LLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIeVIGEFYAATEAPFATTtfqkGDfgIGACRNYGTIIQWFLSFQ 431
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGV-RLLEGYGMTETIVGVI----GP--RDEPRRPGSIGRPAPGYE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 432 QTLVrmDPNDDSViyrnskgfcevaPVGEPGEMLMRiffPKKPETSFQGYLGNAKETkskvvRDVFRRGdaWYRCGDLLK 511
Cdd:cd05934 257 VRIV--DDDGQEL------------PAGEPGELVIR---GLRGWGFFKGYYNMPEAT-----AEAMRNG--WFHTGDLGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 512 ADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQyaQVLVVGIKVPKYEGRAGFAVIkltdnsldITAKTKLLN 591
Cdd:cd05934 313 RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVR--EAAVVAVPDEVGEDEVKAVVV--------LRPGETLDP 382
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 41629676 592 DSL---SRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYR 628
Cdd:cd05934 383 EELfafCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
81-630 |
5.06e-59 |
|
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: 205.43 E-value: 5.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 81 LFIKQVQQNGDHLAISYTRpmaekgefqlETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNI 160
Cdd:COG0318 4 LLRRAAARHPDRPALVFGG----------RRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 161 GAIPAFLNYNTKGTPLVHSLKISNITQVFIdpdasnpireseeeiknalpdvklnyleeqdlmhellnsqspeflqqdnv 240
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 241 rtplgltdfkpSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLA 320
Cdd:COG0318 103 -----------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 321 LSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAY--GNGLRPDIWQDFRKRFNIEVIgEFYAAT 398
Cdd:COG0318 172 LLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVRIV-EGYGLT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 399 EAPFATTT--FQKGDFGIGACrnyGTIIQWflsfqqTLVR-MDPNDdsviyrnskgfcEVAPVGEPGEMLMRiffpkkPE 475
Cdd:COG0318 251 ETSPVVTVnpEDPGERRPGSV---GRPLPG------VEVRiVDEDG------------RELPPGEVGEIVVR------GP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 476 TSFQGYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQV 555
Cdd:COG0318 304 NVMKGYWNDPEAT-----AEAFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH--PGVAEA 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 556 LVVGIKVPKYeGRAGFAVIKLTDNSlDITAKTklLNDSLSRlNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:COG0318 375 AVVGVPDEKW-GERVVAFVVLRPGA-ELDAEE--LRAFLRE-RLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
84-630 |
6.13e-53 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 191.12 E-value: 6.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 84 KQVQQNGDhlaisytRPMAEKGEFQletFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAI 163
Cdd:PRK06155 29 RQAERYPD-------RPLLVFGGTR---WTYAEAARAAAAAAHALA-AAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 164 PAFLNYNTKGTPLVHSLKISNITQVFIDPDASNPIrESEEEIKNALPDVKLnyLEEQDLMHELLNSQSPEFLQQDNVRTP 243
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAAL-EAADPGDLPLPAVWL--LDAPASVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 244 LGLTDFKPSMLIYTSGTTGLPKSAIMS------WRKSSvgcqvfGHVLHMTNESTVFTAMPLFHSTAALLGACAILsHGG 317
Cdd:PRK06155 175 AAVQPGDTAAILYTSGTTGPSKGVCCPhaqfywWGRNS------AEDLEIGADDVLYTTLPLFHTNALNAFFQALL-AGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 318 CLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIEVIgEFYAA 397
Cdd:PRK06155 248 TYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLL-DGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 398 TE--APFATTtfqkgdfgIGACRNyGTIIQWFLSFQQTLVrmDPNDDSViyrnskgfcevaPVGEPGEMLMRiffPKKPE 475
Cdd:PRK06155 327 TEtnFVIAVT--------HGSQRP-GSMGRLAPGFEARVV--DEHDQEL------------PDGEPGELLLR---ADEPF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 476 TSFQGYLGNAKETkskvvrdVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQV 555
Cdd:PRK06155 381 AFATGYFGMPEKT-------VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLS--HPAVAAA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 556 LVVGIKVPKYEGRAGFAVIKLTDNSLDITAktkLLNDSLSRlnLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDGTALEPVA---LVRHCEPR--LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
251-623 |
3.44e-42 |
|
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: 155.91 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHST--AALLGAcaiLSHGGCLALSHKFSAS 328
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGglFGLLGA---LLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 329 TFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIgEFYAATEAPFATTT 406
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIKLV-NGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 407 FQKGDF--GIGACrnyGTIIQWFlsfqQTLVRmDPNDDSViyrnskgfcevaPVGEPGEMLMRIffpkkpETSFQGYLGN 484
Cdd:cd04433 158 GPPDDDarKPGSV---GRPVPGV----EVRIV-DPDGGEL------------PPGEIGELVVRG------PSVMKGYWNN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 485 AKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIKVPK 564
Cdd:cd04433 212 PEAT-----AAVDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH--PGVAEAAVVGVPDPE 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 41629676 565 YeGRAGFAVIKLTDNSlDITAKTklLNDSLsRLNLPSYAMPLFVKFVDEIKMTDNHKIL 623
Cdd:cd04433 283 W-GERVVAVVVLRPGA-DLDAEE--LRAHV-RERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-531 |
1.48e-35 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 138.98 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 82 FIKQVQQNGDHLAIsytrpmaEKGEFQleTFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIG 161
Cdd:pfam00501 1 LERQAARTPDKTAL-------EVGEGR--RLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 162 AIPAFLNYNTKGTPLVHSLKISNITQVFIDpdaSNPIRESEEEIKNALPDVKLNYLEEQDLMHELLNSQSPEFLQQDNVR 241
Cdd:pfam00501 71 AVYVPLNPRLPAEELAYILEDSGAKVLITD---DALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 242 TPLGLTDFKPSMLIYTSGTTGLPKSAIMSWRksSVGCQVFG------HVLHMTNESTVFTAMPLFHSTAALLGACAILSH 315
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHR--NLVANVLSikrvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 316 GGCLALSHKFSA---STFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAY--GNGLRPDIWQDFRKRFNIEV 390
Cdd:pfam00501 226 GATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFGGAL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 391 IgEFYAATEAPFATTTfqkGDFGIGACRNYGTiIQWFLSFQQTLVRmDPNDDsviyrnskgfcEVAPVGEPGEMLMRiff 470
Cdd:pfam00501 306 V-NGYGLTETTGVVTT---PLPLDEDLRSLGS-VGRPLPGTEVKIV-DDETG-----------EPVPPGEPGELCVR--- 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41629676 471 pkKPETsFQGYLGNAKETKskvvrDVFRRGDaWYRCGDLLKADEYGLWYFLDRMGDTFRWK 531
Cdd:pfam00501 366 --GPGV-MKGYLNDPELTA-----EAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
253-657 |
7.90e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 135.96 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 253 MLIYTSGTTGLPKSAIMSWRK-SSVG---CQVFGHvlhmTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSAS 328
Cdd:PRK07867 156 MLIFTSGTSGDPKAVRCTHRKvASAGvmlAQRFGL----GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSAS 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 329 TFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGN-GLRPDIwQDFRKRFNIEVIgEFYAATEAPFATTTF 407
Cdd:PRK07867 232 GFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDI-ARFARRFGCVVV-DGFGSTEGGVAITRT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 408 QKGDFG-IGACRNYGTIIQwflsfQQTLVRMDPnddSVIYRNSKGFCEVApVGE------PGemlmriffpkkpetSFQG 480
Cdd:PRK07867 310 PDTPPGaLGPLPPGVAIVD-----PDTGTECPP---AEDADGRLLNADEA-IGElvntagPG--------------GFEG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 481 YLGNAKETKSkvvrdvfRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVLVVGI 560
Cdd:PRK07867 367 YYNDPEADAE-------RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERIL--LRYPDATEVAVYAV 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 561 KVPKYEGRAGFAVIKLTDNSLDITAKTKLLndsLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQklpkGLDGND 640
Cdd:PRK07867 438 PDPVVGDQVMAALVLAPGAKFDPDAFAEFL---AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE----GVDCAD 510
|
410
....*....|....*....
gi 41629676 641 TIFWLKN--YKRYEVLTAA 657
Cdd:PRK07867 511 PVWWIRRltPSDYAALADE 529
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
251-665 |
4.33e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 134.00 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSW----RKSSVGCQVFGHvlhmTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFS 326
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHgrlaFAGRALTERFGL----TRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFS 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 327 ASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIEVIgEFYAATEAPFATT- 405
Cdd:PRK13388 228 ASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVE-DGYGSSEGAVIVVr 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 406 --TFQKGDFGIGAcrnygtiiqwflsfqqtlvrmdpnDDSVIYrNSKGF--CEVAPVGEPGEMLmriffpkKPETS---- 477
Cdd:PRK13388 307 epGTPPGSIGRGA------------------------PGVAIY-NPETLteCAVARFDAHGALL-------NADEAigel 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 478 --------FQGYLGNAKETKSKVvrdvfRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNK 549
Cdd:PRK13388 355 vntagagfFEGYYNNPEATAERM-----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 550 eqYAQVLVVGikVPkyEGRAG----FAVIKLTDNSLDITAKTKLLNdslSRLNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:PRK13388 428 --INRVAVYA--VP--DERVGdqvmAALVLRDGATFDPDAFAAFLA---AQPDLGTKAWPRYVRIAADLPSTATNKVLKR 498
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 41629676 626 VYREQklpkGLDGNDTIF-WLKNYK-RYEVLTAADWEAIDAQ 665
Cdd:PRK13388 499 ELIAQ----GWATGDPVTlWVRRGGpAYRLMSEPAKAALAAE 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
111-625 |
8.79e-32 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 129.80 E-value: 8.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHiLHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFI 190
Cdd:PRK08008 37 RYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 191 DPDASNPIRESEEEIKNALPDVKL---NYLEEQDLMH--ELLNSQSPEFLQqdnvRTPLGLTDfkPSMLIYTSGTTGLPK 265
Cdd:PRK08008 116 SAQFYPMYRQIQQEDATPLRHICLtrvALPADDGVSSftQLKAQQPATLCY----APPLSTDD--TAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 266 SAIM------------SWRkssvgCQvfghvlhMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQ 333
Cdd:PRK08008 190 GVVIthynlrfagyysAWQ-----CA-------LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 334 VYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK-VAYGNGLRPDIWQDFRKRFNIEVIGEfYAATEapfaTTTFQKGDF 412
Cdd:PRK08008 258 VCKYRATITECIPMMIRTLMVQPPSANDRQHCLReVMFYLNLSDQEKDAFEERFGVRLLTS-YGMTE----TIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 413 GIGAcRNYGTIIQWFLSFQQTLVRMDPNDdsviyrnskgfcevAPVGEPGEMLMRiFFPKKpeTSFQGYLGNAKETkSKV 492
Cdd:PRK08008 333 PGDK-RRWPSIGRPGFCYEAEIRDDHNRP--------------LPAGEIGEICIK-GVPGK--TIFKEYYLDPKAT-AKV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 493 VrdvfrRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQyaQVLVVGIKVPkYEGRAGFA 572
Cdd:PRK08008 394 L-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQ--DIVVVGIKDS-IRDEAIKA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 41629676 573 VIKLTDNSlDITAKTKLlndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:PRK08008 466 FVVLNEGE-TLSEEEFF---AFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
81-630 |
9.88e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 126.84 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 81 LFIKQVQQNGDHLAISYTRpmaekgefqlETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNI 160
Cdd:PRK06187 11 ILRHGARKHPDKEAVYFDG----------RRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 161 GAIPAFLNYNTKGTPLVHSLKISNITQVFIDPDASNPIreseEEIKNALPDVKLNYLEEQDLM----------HELLNSQ 230
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLL----AAILPQLPTVRTVIVEGDGPAaplapevgeyEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 231 SPEFLQQDnvrtpLGLTDfkPSMLIYTSGTTGLPKSAIMSWRkssvgcQVFGHVLHM------TNESTVFTAMPLFHSTA 304
Cdd:PRK06187 156 SDTFDFPD-----IDEND--AAAMLYTSGTTGHPKGVVLSHR------NLFLHSLAVcawlklSRDDVYLVIVPMFHVHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 305 alLGAC-AILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK-VAYGNG-LRPDIWQD 381
Cdd:PRK06187 223 --WGLPyLALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRlVIYGGAaLPPALLRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 382 FRKRFNIEVIgEFYAATEapfaTTtfqkgdfGIGACR--NYGTIIQWFLSFQQTL------VR-MDPNDDsviyrnskgf 452
Cdd:PRK06187 301 FKEKFGIDLV-QGYGMTE----TS-------PVVSVLppEDQLPGQWTKRRSAGRplpgveARiVDDDGD---------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 453 cEVAPV-GEPGEMLMRiffpkKPETSfQGYLGNAKETKSKVVrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWK 531
Cdd:PRK06187 359 -ELPPDgGEVGEIIVR-----GPWLM-QGYWNRPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 532 SENVSTTEVEDQLtaSNKEQYAQVLVVGIKVPKYeGRAGFAVIKLTDNSlDITAKT--KLLNDSLSRlnlpsYAMPLFVK 609
Cdd:PRK06187 425 GENIYPRELEDAL--YGHPAVAEVAVIGVPDEKW-GERPVAVVVLKPGA-TLDAKElrAFLRGRLAK-----FKLPKRIA 495
|
570 580
....*....|....*....|.
gi 41629676 610 FVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK06187 496 FVDELPRTSVGKILKRVLREQ 516
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
110-624 |
2.01e-30 |
|
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: 124.64 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYntkgtplvhslkisnitqvf 189
Cdd:cd17631 19 RSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF-------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 idpdasnpiRESEEEIKnalpdvklnyleeqdlmhELLNSQSPEFLQQDnvrtplgltdfkPSMLIYTSGTTGLPKSAIM 269
Cdd:cd17631 78 ---------RLTPPEVA------------------YILADSGAKVLFDD------------LALLMYTSGTTGRPKGAML 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 270 SWRksSVGCQVFGHVLH--MTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGE 347
Cdd:cd17631 119 THR--NLLWNAVNALAAldLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 348 VCRYLLHTP-ISKYEKMHKVKVAYGNGLRPD----IWQDFRKRFnieviGEFYAATEAPFATTTFQKGDF--GIGACrny 420
Cdd:cd17631 197 MIQALLQHPrFATTDLSSLRAVIYGGAPMPErllrALQARGVKF-----VQGYGMTETSPGVTFLSPEDHrrKLGSA--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 421 GTIIqwflSFQQTLVRmDPNDDSViyrnskgfcevaPVGEPGEMLMRiffpkkPETSFQGYLGNAKETkskvvRDVFRrg 500
Cdd:cd17631 269 GRPV----FFVEVRIV-DPDGREV------------PPGEVGEIVVR------GPHVMAGYWNRPEAT-----AAAFR-- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 501 DAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVLVVGIKVPKYeGRAGFAVIKLTD-N 579
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVL--YEHPAVAEVAVIGVPDEKW-GEAVVAVVVPRPgA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 41629676 580 SLDITAKTKLLndslsRLNLPSYAMPLFVKFVDEIKMTDNHKILK 624
Cdd:cd17631 396 ELDEDELIAHC-----RERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
110-629 |
1.01e-29 |
|
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: 123.19 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVF 189
Cdd:cd05926 13 PALTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASNPIRESEEE----IKNALPDVKLNYLEEQDlmHELLNsqsPEFLQQDNVRTPLGLTDfKPSMLIYTSGTTGLPK 265
Cdd:cd05926 92 TPKGELGPASRAASKlglaILELALDVGVLIRAPSA--ESLSN---LLADKKNAKSEGVPLPD-DLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 266 SAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYV 345
Cdd:cd05926 166 GVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 346 GEVCRYLLHTPISKYEK-MHKVKVAY--GNGLRPDIWQDFRKRFNIEVIgEFYAATEAPFATTTFQKgdfgIGACRNYGT 422
Cdd:cd05926 246 PTIHQILLNRPEPNPESpPPKLRFIRscSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMTSNPL----PPGPRKPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 423 IiqwFLSFQQTLVRMDPNDdsviyrnskgfcEVAPVGEPGEMLMRiffpkkPETSFQGYLGNAKETKSKVVRdvfrrgDA 502
Cdd:cd05926 321 V---GKPVGVEVRILDEDG------------EILPPGVVGEICLR------GPNVTRGYLNNPEANAEAAFK------DG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 503 WYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasNKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLD 582
Cdd:cd05926 374 WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLL--SHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVT 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41629676 583 ITAKTKLLndslsRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd05926 452 EEELRAFC-----RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-628 |
4.65e-29 |
|
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: 121.13 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 79 WYLFIKQVQQNGDHLAIsytrpmaekgEFQLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLW 158
Cdd:cd05936 2 ADLLEEAARRFPDKTAL----------IFMGRKLTYRELDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 159 NIGAIPAflNYNTKGTP--LVHSLKISNITQVFIDpdasnpireseeeiknalpdvklnyLEEQDLMhellnsQSPEFLQ 236
Cdd:cd05936 71 KAGAVVV--PLNPLYTPreLEHILNDSGAKALIVA-------------------------VSFTDLL------AAGAPLG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 237 QDNVRTPlglTDfkPSMLIYTSGTTGLPKSAIMSWRK----SSVGCQVFGHVLHMtnESTVFTAMPLFHS---TAALLga 309
Cdd:cd05936 118 ERVALTP---ED--VAVLQYTSGTTGVPKGAMLTHRNlvanALQIKAWLEDLLEG--DDVVLAALPLFHVfglTVALL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 310 CAILShGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG--LRPDIWQDFRKRFN 387
Cdd:cd05936 189 LPLAL-GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 388 IEVIgEFYAATEA-PfaTTTFQKGDFGigacRNYGTIiqwFLSFQQTLVR-MDPNDdsviyrnskgfcEVAPVGEPGEML 465
Cdd:cd05936 268 VPIV-EGYGLTETsP--VVAVNPLDGP----RKPGSI---GIPLPGTEVKiVDDDG------------EELPPGEVGELW 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 466 MRiffpkKPETsFQGYLGNAKETKskvvrDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLT 545
Cdd:cd05936 326 VR-----GPQV-MKGYWNRPEETA-----EAFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLY 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 546 AsnKEQYAQVLVVGIKVPKYeGRAGFAVIKLTDNSlditaktKLLNDSL---SRLNLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd05936 393 E--HPAVAEAAVVGVPDPYS-GEAVKAFVVLKEGA-------SLTEEEIiafCREQLAGYKVPRQVEFRDELPKSAVGKI 462
|
....*.
gi 41629676 623 LKKVYR 628
Cdd:cd05936 463 LRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
111-623 |
2.14e-27 |
|
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: 116.16 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNY-NTKGTpLVHSLKISNITQVF 189
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPiYTADE-LAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASNPIRESEEEIKN----ALPDVKLNY-LEEQDLMHELLNSQSPEFLqqdnvrTPLGLTDFKPSMLIYTSGTTGLP 264
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPkdkiIVLDDKPDGvLSIEDLLSPTLGEEDEDLP------PPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 265 KSAIMSWRKSSVGC-QVFGHV-LHMTNESTVFTAMPLFHSTAALLGACAILsHGGCLALSHKFSASTFWK-----QVylt 337
Cdd:cd05911 162 KGVCLSHRNLIANLsQVQTFLyGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDSELFLDliekyKI--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 338 gaTHIQYVGEVCRYLLHTPISKYEKMHKVK-VAYGNG-LRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDFGIG 415
Cdd:cd05911 238 --TFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 416 ACrnyGTIIqwfLSFQQTLVrmdpNDDSviyrnskgfCEVAPVGEPGEMLMRiffpkkPETSFQGYLGNAKETKSKVVRd 495
Cdd:cd05911 316 SV---GRLL---PNVEAKIV----DDDG---------KDSLGPNEPGEICVR------GPQVMKGYYNNPEATKETFDE- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 496 vfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtASNKEqYAQVLVVGIKVPKYEGRAGfAVIK 575
Cdd:cd05911 370 -----DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVL-LEHPG-VADAAVIGIPDEVSGELPR-AYVV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41629676 576 LTDNSlDITAK--TKLLNDSLSrlnlPSYAMPLFVKFVDEIKMTDNHKIL 623
Cdd:cd05911 442 RKPGE-KLTEKevKDYVAKKVA----SYKQLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
86-630 |
5.24e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 115.39 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 86 VQQNGDHLAIsytrpmaekgEFQLETFTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPA 165
Cdd:PRK07656 15 ARRFGDKEAY----------VFGDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 166 FLNYNTKGTPLVHSLKISNITQVFidpdASNPIRESEEEIKNALPDVKL--NYLEEQDLMHELLNSQSPEFLQQ-DNVRT 242
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALF----VLGLFLGVDYSATTRLPALEHvvICETEEDDPHTEKMKTFTDFLAAgDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 243 PLGLTDFKPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHS---TAALLgACaiLSHGGCL 319
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVfgyKAGVN-AP--LMRGATI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 320 ALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIGEFYAA 397
Cdd:PRK07656 237 LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 398 TEA-PFATTTFQKGDFGIGAcrnyGTIiqwflsfqqtlvrmDPNDDSVIYRNSKGFCEVAPVGEPGEMLMRIFfpkkpeT 476
Cdd:PRK07656 317 SEAsGVTTFNRLDDDRKTVA----GTI--------------GTAIAGVENKIVNELGEEVPVGEVGELLVRGP------N 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 477 SFQGYLGNAKETKSKVvrdvfrRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQVL 556
Cdd:PRK07656 373 VMKGYYDDPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYE--HPAVAEAA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 557 VVGIKVPKYeGRAG--FAVIKltdNSLDITAKTKLlndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK07656 445 VIGVPDERL-GEVGkaYVVLK---PGAELTEEELI---AYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
110-629 |
3.23e-21 |
|
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: 96.98 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNyntkgtplvhslkisnitqvf 189
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLN--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 idpdASNPIREseeeiknalpdvklnyleeqdLMHELLNSQSPEFLqqdnvrtplgltdfKPSMLIYTSGTTGLPKSAIM 269
Cdd:cd05941 69 ----PSYPLAE---------------------LEYVITDSEPSLVL--------------DPALILYTSGTTGRPKGVVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 270 SWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLG-ACAILSHGGCLALShKFSASTFWKQVYLTGATHIQYVGEV 348
Cdd:cd05941 110 THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNAlLCPLFAGASVEFLP-KFDPKEVAISRLMPSITVFMGVPTI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 349 CRYLLHTPISKYEKMHKVKVAYGNGLR----------PDIWQDFRKRFNiEVIGEFYAATEAPFATTTFQKGDfgigacR 418
Cdd:cd05941 189 YTRLLQYYEAHFTDPQFARAAAAERLRlmvsgsaalpVPTLEEWEAITG-HTLLERYGMTEIGMALSNPLDGE------R 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 419 NYGTiIQWFLSFQQTLVRMDPNDdsviyrnskgfcEVAPVGEPGEMLMRiffpkkPETSFQGYLGNAKETKSKVvrdvfr 498
Cdd:cd05941 262 RPGT-VGMPLPGVQARIVDEETG------------EPLPRGEVGEIQVR------GPSVFKEYWNKPEATKEEF------ 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 499 RGDAWYRCGDLLKADEYGLWYFLDRMG-DTFRWKSENVSTTEVEDQLTASNkeQYAQVLVVGIKVPKYeGRAGFAVIKLT 577
Cdd:cd05941 317 TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHP--GVSECAVIGVPDPDW-GERVVAVVVLR 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41629676 578 DNSLDITAKTkLLNDSLSRlnLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd05941 394 AGAAALSLEE-LKEWAKQR--LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
110-630 |
3.72e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 97.31 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVF 189
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASNPIRESEEEIKNALPDVkLNYLEEQDLMHELLNSQspEFLQQDNVRTPL-GLTDFKPSMLIYTSGTTGLPKSAI 268
Cdd:PRK08316 114 VDPALAPTAEAALALLPVDTLIL-SLVLGGREAPGGWLDFA--DWAEAGSVAEPDvELADDDLAQILYTSGTESLPKGAM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 269 MSWRK---SSVGCQVfghVLHMTNESTVFTAMPLFHS--------TAALLGACAILSHGG----CLALSHK------FSA 327
Cdd:PRK08316 191 LTHRAliaEYVSCIV---AGDMSADDIPLHALPLYHCaqldvflgPYLYVGATNVILDAPdpelILRTIEAeritsfFAP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 328 STFWkqvyltgathiqyVGevcryLLHTP-ISKYEKMHKVKVAYGNGLRP-DIWQDFRKRF-NIEVIgEFYAATE-APFA 403
Cdd:PRK08316 268 PTVW-------------IS-----LLRHPdFDTRDLSSLRKGYYGASIMPvEVLKELRERLpGLRFY-NCYGQTEiAPLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 404 tTTFQKGDfgigACRNYGTIIQWFLSFQQTLVRMDPNDdsviyrnskgfceVAPvGEPGEMLMRiffpkkpetSFQ---G 480
Cdd:PRK08316 329 -TVLGPEE----HLRRPGSAGRPVLNVETRVVDDDGND-------------VAP-GEVGEIVHR---------SPQlmlG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 481 YLGNAKETKskvvrDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQVLVVGI 560
Cdd:PRK08316 381 YWDDPEKTA-----EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYT--HPAVAEVAVIGL 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 561 KVPKYeGRAGFAVIKLTDNSlDITAKTKLlndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK08316 452 PDPKW-IEAVTAVVVPKAGA-TVTEDELI---AHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
89-629 |
5.41e-20 |
|
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: 93.85 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 89 NGDHLAISYTrpmaekGEFQLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLN 168
Cdd:cd12119 9 HGDREIVSRT------HEGEVHRYTYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 169 yntkgtPLVHSLKISNITQ------VFIDPDASnPIREseeEIKNALPDVK-------LNYLEEQDLM-----HELLNSQ 230
Cdd:cd12119 82 ------PRLFPEQIAYIINhaedrvVFVDRDFL-PLLE---AIAPRLPTVEhvvvmtdDAAMPEPAGVgvlayEELLAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 231 SPEFlqqdnvrtplGLTDFK---PSMLIYTSGTTGLPKSAIMSWRKSsvgcqvfghVLH-----------MTNESTVFTA 296
Cdd:cd12119 152 SPEY----------DWPDFDentAAAICYTSGTTGNPKGVVYSHRSL---------VLHamaalltdglgLSESDVVLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 297 MPLFHS-------TAALLGAcailshggclalshkfsastfwKQVyLTGathiqyvgevcRYLlhTPISKYEKMHKVKVA 369
Cdd:cd12119 213 VPMFHVnawglpyAAAMVGA----------------------KLV-LPG-----------PYL--DPASLAELIEREGVT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 370 YGNGLrPDIWQDFRKRFNIE----------VIGefyaATEAPFA-TTTFQkgDFGIGACRNYG-------TIIQWFLSFQ 431
Cdd:cd12119 257 FAAGV-PTVWQGLLDHLEANgrdlsslrrvVIG----GSAVPRSlIEAFE--ERGVRVIHAWGmtetsplGTVARPPSEH 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 432 QTLvrmdPNDDSVIYRNSKG----FCEVAPVGEPGEMLmriffPKKPETS----------FQGYLGNAKETKskvvrdvF 497
Cdd:cd12119 330 SNL----SEDEQLALRAKQGrpvpGVELRIVDDDGREL-----PWDGKAVgelqvrgpwvTKSYYKNDEESE-------A 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 498 RRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKeqYAQVLVVGIKVPKYEGRAgFAVIKLT 577
Cdd:cd12119 394 LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPA--VAEAAVIGVPHPKWGERP-LAVVVLK 470
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 41629676 578 DNSlDITAKtkLLNDSLSRLnLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd12119 471 EGA-TVTAE--ELLEFLADK-VAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
110-629 |
1.20e-19 |
|
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: 92.98 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLN--YNTKgtPLVHSLKISNITQ 187
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNdiYNER--ELDHSLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 188 VFIDPDASNPIRESEEEIKNA----LPDVKLNYLEEQDlMHELLNSQSPEFLQQDNVRTPLGLTDFKPSMLIYTSGTTGL 263
Cdd:cd17642 120 VFCSKKGLQKVLNVQKKLKIIktiiILDSKEDYKGYQC-LYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 264 PKSAIMSWRKSsvgCQVFGHVLHMT------NESTVFTAMPLFHStaalLGACAILSHGGC---LALSHKFSASTFWKQV 334
Cdd:cd17642 199 PKGVQLTHKNI---VARFSHARDPIfgnqiiPDTAILTVIPFHHG----FGMFTTLGYLICgfrVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 335 YLTGATHIQYVGEVCRYLL-HTPISKYEKMHKVKVAYGNG-LRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDF 412
Cdd:cd17642 272 QDYKVQSALLVPTLFAFFAkSTLVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 413 GIGACrnyGTIIQWFLSfqqtlVRMDPNDDSVIYRNSKGFCEVApvgepGEMLMRiffpkkpetsfqGYLGNAKETKSKV 492
Cdd:cd17642 352 KPGAV---GKVVPFFYA-----KVVDLDTGKTLGPNERGELCVK-----GPMIMK------------GYVNNPEATKALI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 493 VRDvfrrgdAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQvlVVGIKVPKYEGRAGFA 572
Cdd:cd17642 407 DKD------GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG--VAGIPDEDAGELPAAV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 41629676 573 VIKLTDNSLDITAKTKLLNDSLSrlnlPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd17642 479 VVLEAGKTMTEKEVMDYVASQVS----TAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
252-633 |
4.25e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 252 SMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNE-----STVFTAMPLFHSTAALLGACAILSHGGCLAL-SHKF 325
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKIGGCNHLiSNPR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 326 SASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGL--RPDIWQDFRKRFNIEVIgEFYAATEAPFA 403
Cdd:PRK08751 291 DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTETSPA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 404 tttfqkgdfgigACRNYGTIIQWFLSFQQTLvrmdPNDDSVIyRNSKGfcEVAPVGEPGEMLMriffpKKPETsFQGYLG 483
Cdd:PRK08751 370 ------------ACINPLTLKEYNGSIGLPI----PSTDACI-KDDAG--TVLAIGEIGELCI-----KGPQV-MKGYWK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 484 NAKETkSKVVRdvfrrGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQVLVVGIKVP 563
Cdd:PRK08751 425 RPEET-AKVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAM--MPGVLEVAAVGVPDE 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41629676 564 KyEGRAGFAVIKLTDNSL---DITAKtkllndslSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQKLP 633
Cdd:PRK08751 497 K-SGEIVKVVIVKKDPALtaeDVKAH--------ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
110-631 |
4.36e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 90.69 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVF 189
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASNPIRESEEEIKNAlPDVKLNYLEEQdLMHELLNSQSPeflqqdnvrtplglTDFKPSMLIYTSGTTGLPKSAIM 269
Cdd:PRK06839 106 VEKTFQNMALSMQKVSYVQ-RVISITSLKEI-EDRKIDNFVEK--------------NESASFIICYTSGTTGKPKGAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 270 SWRkssvgcQVFGHVLH------MTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQ 343
Cdd:PRK06839 170 TQE------NMFWNALNntfaidLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 344 YVGEVCRYLLHTPISKYEKMHKVKVAYgNGLRP---DIWQDFRKRFNIevIGEFYAATEAPFATTTFQKGDFGigacRNY 420
Cdd:PRK06839 244 GVPTIHQALINCSKFETTNLQSVRWFY-NGGAPcpeELMREFIDRGFL--FGQGFGMTETSPTVFMLSEEDAR----RKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 421 GTIIQWFLSFQQTLVrmDPNDDSViyrnskgfcevaPVGEPGEMLMRiffpkKPETsFQGYLGNAKETKSKVvrdvfrrG 500
Cdd:PRK06839 317 GSIGKPVLFCDYELI--DENKNKV------------EVGEVGELLIR-----GPNV-MKEYWNRPDATEETI-------Q 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 501 DAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQyaQVLVVGIKVPKYeGRAGFAVIKLTDNS 580
Cdd:PRK06839 370 DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVY--EVAVVGRQHVKW-GEIPIAFIVKKSSS 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 41629676 581 LDITAKTKllndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQK 631
Cdd:PRK06839 447 VLIEKDVI----EHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
78-632 |
6.49e-19 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 90.56 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 78 NW--YLFIKQVQQNGDHLAISYTrpmAEKGEfqLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWL 155
Cdd:COG0365 9 NIayNCLDRHAEGRGDKVALIWE---GEDGE--ERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 156 SLWNIGAI--PAFLNYNTKGtpLVHSLKISNITQVFIDPDASNPIRESE-----EEIKNALPDVK----LNYLEEQDLM- 223
Cdd:COG0365 83 ACARIGAVhsPVFPGFGAEA--LADRIEDAEAKVLITADGGLRGGKVIDlkekvDEALEELPSLEhvivVGRTGADVPMe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 224 -----HELLNSQSPEFlqqDNVRTPLglTDfkPSMLIYTSGTTGLPK------SAIMSWRKSSvgcqvFGHVLHMTNEST 292
Cdd:COG0365 161 gdldwDELLAAASAEF---EPEPTDA--DD--PLFILYTSGTTGKPKgvvhthGGYLVHAATT-----AKYVLDLKPGDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 293 VFTAMPLF----HS---TAALL-GACAILSHGGCLALshkfSASTFWKQ-------VYLTGATHIqyvgevcRYLLH--- 354
Cdd:COG0365 229 FWCTADIGwatgHSyivYGPLLnGATVVLYEGRPDFP----DPGRLWELiekygvtVFFTAPTAI-------RALMKagd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 355 TPISKYeKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIgEFYAATE--APFATTtfqkgdFGIGACRnYGTIIQWFLSF 430
Cdd:COG0365 298 EPLKKY-DLSSLRLLGSAGepLNPEVWEWWYEAVGVPIV-DGWGQTEtgGIFISN------LPGLPVK-PGSMGKPVPGY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 431 QQTLVrmDPNDDSViyrnskgfcevaPVGEPGEMLMriffpKKPETS-FQGYLGNAKETKSKvvrdVFRRGDAWYRCGDL 509
Cdd:COG0365 369 DVAVV--DEDGNPV------------PPGEEGELVI-----KGPWPGmFRGYWNDPERYRET----YFGRFPGWYRTGDG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 510 LKADEYGLWYFLDRMGDTFrwKS--ENVSTTEVEDQLtasnkEQYAQVL---VVGIKVP-KYEGRAGFAVikLTDNSLDI 583
Cdd:COG0365 426 ARRDEDGYFWILGRSDDVI--NVsgHRIGTAEIESAL-----VSHPAVAeaaVVGVPDEiRGQVVKAFVV--LKPGVEPS 496
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 41629676 584 TAKTKLLNDSLSRlNLPSYAMPLFVKFVDEIKMTDNHKI----LKKVYREQKL 632
Cdd:COG0365 497 DELAKELQAHVRE-ELGPYAYPREIEFVDELPKTRSGKImrrlLRKIAEGRPL 548
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
111-544 |
6.73e-19 |
|
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: 90.37 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHILHFDYNVQaGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNyntkgtPLVHSLKISNitQVfi 190
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN------PLSTPAEIAK--QV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 191 dpDASNP-----IRESEEEIKNALPDVKLNYLEEQDLMHELLNSQSPEFLQQDNVRtpLGLTDfkPSMLIYTSGTTGLPK 265
Cdd:cd05904 101 --KDSGAklaftTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVV--IKQDD--VAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 266 SAIMSWRK--SSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQ 343
Cdd:cd05904 175 GVMLTHRNliAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 344 YVGEVCRYLLHTPI-SKYE--KMHKVKVAyGNGLRPDIWQDFRKRFNIEVIGEFYAATEA-PFATTTFQ--KGDFGIGAC 417
Cdd:cd05904 255 VVPPIVLALVKSPIvDKYDlsSLRQIMSG-AAPLGKELIEAFRAKFPNVDLGQGYGMTEStGVVAMCFApeKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 418 rnyGTIIqwflsfqqtlvrmdPNDDSVIYRNSKGfcEVAPVGEPGEMLMRiffpkKPETsFQGYLGNAKETKSKVvrdvf 497
Cdd:cd05904 334 ---GRLV--------------PNVEAKIVDPETG--ESLPPNQTGELWIR-----GPSI-MKGYLNNPEATAATI----- 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 41629676 498 rRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQL 544
Cdd:cd05904 384 -DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
251-622 |
2.04e-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: 86.69 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKS---AIMSWRKSSVgCQVfgHVLHMTNESTVFTAMPLFHStAALLGACAILSHGGCLALSHKFSA 327
Cdd:cd17633 2 PFYIGFTSGTTGLPKAyyrSERSWIESFV-CNE--DLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 328 STFWKQVYLTGATHIQYVGEvcryLLHTPISKYEKMHKVKVAY--GNGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATT 405
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 406 TFQkgdfgiGACRNYGTIIQWFlsfqqtlvrmdPNDDSVIyRNSKGfcevapvGEPGemlmRIFFpkKPETSFQGYlgna 485
Cdd:cd17633 154 NFN------QESRPPNSVGRPF-----------PNVEIEI-RNADG-------GEIG----KIFV--KSEMVFSGY---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 486 ketkskvVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIkvpKY 565
Cdd:cd17633 199 -------VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAI--PGIEEAIVVGI---PD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41629676 566 EGRAGFAVIKLTDNSLDITAKTKLLNDSLSRLNLPSYamplfVKFVDEIKMTDNHKI 622
Cdd:cd17633 267 ARFGEIAVALYSGDKLTYKQLKRFLKQKLSRYEIPKK-----IIFVDSLPYTSSGKI 318
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
73-630 |
2.76e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.60 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 73 RHRFQNWylfikqVQQNGDHlaiSYTRPMAEKGEFQLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVF 152
Cdd:PRK07786 13 LARRQNW------VNQLARH---ALMQPDAPALRFLGNTTTWRELDDRVAALAGALS-RRGVGFGDRVLILMLNRTEFVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 153 LWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDP---DASNPIRESEEEIKNAL------PDVKLNYleeqdlm 223
Cdd:PRK07786 83 SVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAalaPVATAVRDIVPLLSTVVvaggssDDSVLGY------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 224 HELLNSQSPEFlqqdnvrTPLGLTDFKPSMLIYTSGTTGLPKSAIMSwrKSSVGCQVFGHVLHM---TNESTVFTAMPLF 300
Cdd:PRK07786 156 EDLLAEAGPAH-------APVDIPNDSPALIMYTSGTTGRPKGAVLT--HANLTGQAMTCLRTNgadINSDVGFVGVPLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 301 H-------STAALLGACAILSHGGClalshkFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG 373
Cdd:PRK07786 227 HiagigsmLPGLLLGAPTVIYPLGA------FDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 374 LRPD-IWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDfgigACRNYGTIIQWFLSFQQTLVRMDPNDdsviyrnskgf 452
Cdd:PRK07786 301 PASDtLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGED----AIRKLGSVGKVIPTVAARVVDENMND----------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 453 cevAPVGEPGEMLMRiffpkkPETSFQGYLGNAKETKskvvrDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKS 532
Cdd:PRK07786 366 ---VPVGEVGEIVYR------APTLMSGYWNNPEATA-----EAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 533 ENVSTTEVEDQLTAsnKEQYAQVLVVGIKVPKYeGRAGFAVIKLT--DNSLDITAKTKLLNDSLSRlnlpsYAMPLFVKF 610
Cdd:PRK07786 430 ENIYCAEVENVLAS--HPDIVEVAVIGRADEKW-GEVPVAVAAVRndDAALTLEDLAEFLTDRLAR-----YKHPKALEI 501
|
570 580
....*....|....*....|
gi 41629676 611 VDEIKMTDNHKILKKVYREQ 630
Cdd:PRK07786 502 VDALPRNPAGKVLKTELRER 521
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
250-633 |
4.08e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 84.86 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 250 KPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKF--SA 327
Cdd:PRK09088 136 RVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFepKR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 328 STFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG---LRPDI--WQDFRKRFnieVIGefYAATEApf 402
Cdd:PRK09088 216 TLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGaphAAEDIlgWLDDGIPM---VDG--FGMSEA-- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 403 aTTTF-----------QKGDFGIGACrnygtiiqwflSFQQTLVRMDPNDdsviyrnskgfcevAPVGEPGEMLMRiffp 471
Cdd:PRK09088 289 -GTVFgmsvdcdviraKAGAAGIPTP-----------TVQTRVVDDQGND--------------CPAGVPGELLLR---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 472 kkPETSFQGYLGNAKETKskvvrDVFRrGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQ 551
Cdd:PRK09088 339 --GPNLSPGYWRRPQATA-----RAFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVL--ADHPG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 552 YAQVLVVGIKVPKYeGRAGFAVIKLTDnslditAKTKLLNDSLSRLN--LPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK09088 409 IRECAVVGMADAQW-GEVGYLAIVPAD------GAPLDLERIRSHLStrLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
....
gi 41629676 630 QKLP 633
Cdd:PRK09088 482 ALAA 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
134-631 |
7.08e-17 |
|
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: 84.08 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 134 VQAGDYVAIDCTNKPLFVFLWLSLWNIGA--IPAFLNYNTKGtpLVHSLKISNITQVFIDPDASNPireseEEIKNALPD 211
Cdd:cd05970 69 IGKGDTVMLTLKRRYEFWYSLLALHKLGAiaIPATHQLTAKD--IVYRIESADIKMIVAIAEDNIP-----EEIEKAAPE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 212 V----KLNYLEEQDL-----MHELLNSQSPEFlqqdnvRTPLGLTDFK---PSMLIYTSGTTGLPKSAimswrkSSVGCQ 279
Cdd:cd05970 142 CpskpKLVWVGDPVPegwidFRKLIKNASPDF------ERPTANSYPCgedILLVYFSSGTTGMPKMV------EHDFTY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 280 VFGHV-------------LHMTNESTVFTAMPLFHSTAALLGACAILSHGgclalSHKFSASTFWKQVYLTGATHIQYVG 346
Cdd:cd05970 210 PLGHIvtakywqnvreggLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYD-----YDKFDPKALLEKLSKYGVTTFCAPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 347 EVCRYLLHTPISKYE--KMHKVKVAyGNGLRPDIWQDFRKRFNIEVIgEFYAATEAPFATTTF-----QKGDFGIGAcRN 419
Cdd:cd05970 285 TIYRFLIREDLSRYDlsSLRYCTTA-GEALNPEVFNTFKEKTGIKLM-EGFGQTETTLTIATFpwmepKPGSMGKPA-PG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 420 YGTIIqwflsfqqtlvrMDPNDDSViyrnskgfcevaPVGEPGEMLMRIFfPKKPETSFQGYLGNAKETKSkvvrdVFRr 499
Cdd:cd05970 362 YEIDL------------IDREGRSC------------EAGEEGEIVIRTS-KGKPVGLFGGYYKDAEKTAE-----VWH- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 500 gDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasnkeQYAQVL---VVGIKVPKyEGRAGFAVIKL 576
Cdd:cd05970 411 -DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI-----QHPAVLecaVTGVPDPI-RGQVVKATIVL 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 577 TDNSLDITAKTKLLNDSLSRLNLPsYAMPLFVKFVDEIKMTDNHKILKKVYREQK 631
Cdd:cd05970 484 AKGYEPSEELKKELQDHVKKVTAP-YKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
106-616 |
1.31e-16 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 83.15 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 106 EFQLETFTYIETYNIVLRLSHILHfDYNVQaGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNI 185
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLA-KMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 186 TQV-----FIDPDASNPIRESEEeiknalpDVKLNYLEEqdlmheLLNSQS-PE---------FLQQDNVRTpLGLTDFK 250
Cdd:cd05909 80 KTVltskqFIEKLKLHHLFDVEY-------DARIVYLED------LRAKISkADkckaflagkFPPKWLLRI-FGVAPVQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 P---SMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHStaalLGacaiLSHGGCLALSHKFSA 327
Cdd:cd05909 146 PddpAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHS----FG----LTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 328 stfwkqVYLTGATHIQYVGEV-----CRYLLHTP---------ISKYE-KMHKVKVAYGNGLRPDIWQDFRKRFNIeVIG 392
Cdd:cd05909 218 ------VFHPNPLDYKKIPELiydkkATILLGTPtflrgyaraAHPEDfSSLRLVVAGAEKLKDTLRQEFQEKFGI-RIL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 393 EFYAATE-APFATTTFQKGDFGIGacrnygtiiqwflsfqqTLVRMDPNDDSVIYrNSKGFCEVaPVGEPGEMLMRifFP 471
Cdd:cd05909 291 EGYGTTEcSPVISVNTPQSPNKEG-----------------TVGRPLPGMEVKIV-SVETHEEV-PIGEGGLLLVR--GP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 472 KKpetsFQGYLGNAKETkskvvrdVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEq 551
Cdd:cd05909 350 NV----MLGYLNEPELT-------SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 552 yaQVLVVGIKVPkyEGRAGFAVIKL-TDNSLDITAktklLNDSLSRLNLPSYAMPLFVKFVDEIKM 616
Cdd:cd05909 418 --DNEVAVVSVP--DGRKGEKIVLLtTTTDTDPSS----LNDILKNAGISNLAKPSYIHQVEEIPL 475
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
251-622 |
1.68e-16 |
|
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: 82.58 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPK------SAIMS---WRKSSVGCQVFGHVLHMTneSTVFTAmplfhSTAALLGAcaiLSHGGCLAL 321
Cdd:cd05930 95 LAYVIYTSGSTGKPKgvmvehRGLVNlllWMQEAYPLTPGDRVLQFT--SFSFDV-----SVWEIFGA---LLAGATLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 322 ---SHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISkyEKMHKVKVAY--GNGLRPDIWQDFRKRFNIEVIGEFYA 396
Cdd:cd05930 165 lpeEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 397 ATEAPFATTTF--QKGDFG-----IGAC-RNYGTIIqwflsfqqtlvrMDPNDDSViyrnskgfcevaPVGEPGEM---- 464
Cdd:cd05930 243 PTEATVDATYYrvPPDDEEdgrvpIGRPiPNTRVYV------------LDENLRPV------------PPGVPGELyigg 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 465 --LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMgDT------FRwksenVS 536
Cdd:cd05930 299 agLAR------------GYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 537 TTEVEDQLTASnkEQYAQVLVVGIKVPKYEGR-AGFAVIKlTDNSLDITAktklLNDSLSRLnLPSYAMPLFVKFVDEIK 615
Cdd:cd05930 361 LGEIEAALLAH--PGVREAAVVAREDGDGEKRlVAYVVPD-EGGELDEEE----LRAHLAER-LPDYMVPSAFVVLDALP 432
|
....*..
gi 41629676 616 MTDNHKI 622
Cdd:cd05930 433 LTPNGKV 439
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
118-629 |
4.31e-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: 81.27 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 118 YNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLnynTKGTPLVHSLKISNITqvfidPDASNP 197
Cdd:cd05929 23 YSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYK---SSRAPRAEACAIIEIK-----AAALVC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 198 IRESEEEIKNALPDvklnYLEEQDLmhellnsqSPEFLQQDNVRtplgltdfkPSMLIYTSGTTGLPK------------ 265
Cdd:cd05929 95 GLFTGGGALDGLED----YEAAEGG--------SPETPIEDEAA---------GWKMLYSGGTTGRPKgikrglpggppd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 266 -SAIMSWrksSVGCQvfghvlhMTNESTVFTAMPLFHstAALLGACAI-LSHGGCLALSHKFSASTFWKQVYLTGATHIQ 343
Cdd:cd05929 154 nDTLMAA---ALGFG-------PGADSVYLSPAPLYH--AAPFRWSMTaLFMGGTLVLMEKFDPEEFLRLIERYRVTFAQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 344 YVGEVCRYLLHTP--ISKYEKMHKVKVAYGNGLRPDIWQdfrKRFNI----EVIGEFYAATEapfatttfqkgdfGIGAC 417
Cdd:cd05929 222 FVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAAPCPPWV---KEQWIdwggPIIWEYYGGTE-------------GQGLT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 418 RNYGTiiQWfLSFQQTLVRMDPNDDSVIYRNSKgfcEVAPvGEPGEMLMRiffPKKPETSFQGYLGNAKEtkskvvrdvf 497
Cdd:cd05929 286 IINGE--EW-LTHPGSVGRAVLGKVHILDEDGN---EVPP-GEIGEVYFA---NGPGFEYTNDPEKTAAA---------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 498 RRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKeqYAQVLVVGikVPKYE-GRAGFAVIKL 576
Cdd:cd05929 346 RNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPK--VLDAAVVG--VPDEElGQRVHAVVQP 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 41629676 577 TDNSLDITAKTKLLNDSLsRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd05929 422 APGADAGTALAEELIAFL-RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
252-637 |
8.78e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 80.85 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 252 SMLIYTSGTTGLPKSAIMSwRKSSVGCQVFG-HVLH--MTNESTVFTAMPLFHstaaLLGACAILS----HGGCLALSHK 324
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLT-HKNLVSNTLMGvQWLYncKEGEEVVLGVLPFFH----VYGMTAVMNlsimQGYKMVLIPK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 325 FSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAY-GNGLRPDIWQDFRKRFNIEVIGEFYAATEA-PF 402
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPVEVQEKFETVTGGKLVEGYGLTESsPV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 403 ATTTFqkgdfgIGACRNYGTI-IQWflsfqqtlvrmdPNDDSVIYRNSKGfcEVAPVGEPGEMLMriffpKKPETsFQGY 481
Cdd:PRK06710 364 THSNF------LWEKRVPGSIgVPW------------PDTEAMIMSLETG--EALPPGEIGEIVV-----KGPQI-MKGY 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 482 LGNAKETKSKVvrdvfrrGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQyaQVLVVGIK 561
Cdd:PRK06710 418 WNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ--EVVTIGVP 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 562 VPkYEGRAGFAVIKLTDNSldITAKTKLlnDSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQKLPKGLD 637
Cdd:PRK06710 489 DP-YRGETVKAFVVLKEGT--ECSEEEL--NQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-624 |
1.28e-15 |
|
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: 78.86 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 256 YTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLAL-SHKFSASTFWKQV 334
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 335 YLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK--VAYGNGLRPDIWQDFRKRFNIEVIGEFYAATEA-PFATTTFqKGD 411
Cdd:cd05917 89 EKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETsPVSTQTR-TDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 412 FGIGACRNYGTIiqwfLSFQQTLVrMDPNDdsviyrnskgfCEVAPVGEPGEMLMRIFfpkkpeTSFQGYLGNAKETKSK 491
Cdd:cd05917 168 SIEKRVNTVGRI----MPHTEAKI-VDPEG-----------GIVPPVGVPGELCIRGY------SVMKGYWNDPEKTAEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 492 VVRDVfrrgdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVlvVGIKVPKYeGRAGF 571
Cdd:cd05917 226 IDGDG------WLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQV--VGVPDERY-GEEVC 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 572 AVIKLTDNSlDITAKT--KLLNDSLSRLNLPSYamplfVKFVDEIKMTDNHKILK 624
Cdd:cd05917 297 AWIRLKEGA-ELTEEDikAYCKGKIAHYKVPRY-----VFFVDEFPLTVSGKIQK 345
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
113-625 |
1.37e-15 |
|
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: 79.86 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 113 TYIETYNIVLRLSHILHFDyNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDP 192
Cdd:cd05923 30 TYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 193 DASnPIRES-----EEEIKNALPDVKLNYleeqdlmhellnSQSPEFlqQDNVRTPLgltdfKPSMLIYTSGTTGLPKSA 267
Cdd:cd05923 109 DAQ-VMDAIfqsgvRVLALSDLVGLGEPE------------SAGPLI--EDPPREPE-----QPAFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 268 IMSWRKSSvgcqvfGHVLHMTNES--------TVFTAMPLFHST---AALLGACAIlshGGCLALSHKFSASTFWKQVYL 336
Cdd:cd05923 169 VIPQRAAE------SRVLFMSTQAglrhgrhnVVLGLMPLYHVIgffAVLVAALAL---DGTYVVVEEFDPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 337 TGATHIQYVGEVCRYLLHTPISKYEKMHKV-KVAYGNGLRPDiwqDFRKRFNIEVIGEF---YAATEApfATTTFQKGdf 412
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFAGLKLSSLrHVTFAGATMPD---AVLERVNQHLPGEKvniYGTTEA--MNSLYMRD-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 413 gigacrnygtiiqwflSFQQTLVRMDPNDDSVIYRNSKGFCEVAPVGEPGEMLMRiffpKKPETSFQGYLGNAKETKSKV 492
Cdd:cd05923 313 ----------------ARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVA----AAADAAFTGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 493 VrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIKVPKYeGRAGFA 572
Cdd:cd05923 373 Q-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRH--PGVTEVVVIGVADERW-GQSVTA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 41629676 573 VIKLTDNSLDITAKTKLLNDSlsrlNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd05923 443 CVVPREGTLSADELDQFCRAS----ELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
292-657 |
1.52e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 80.53 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 292 TVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYG 371
Cdd:PRK07868 648 TVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIG 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 372 NGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDFGIGACRNYGtiiqwflSFQQTLVRMDPNDDsVIYRNSKG 451
Cdd:PRK07868 728 SGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGAKIGSKGRPLPG-------AGRVELAAYDPEHD-LILEDDRG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 452 FCEVAPVGEPGEMLMRIFFPKKPETSfqgylgnaketkskVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWK 531
Cdd:PRK07868 800 FVRRAEVNEVGVLLARARGPIDPTAS--------------VKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTA 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 532 SENVSTTEVEDQLTASNkeQYAQVLVVGIKVPKYEgRAGFAVIKLTDNSLDITAktklLNDSLSRlnLPSYAMPLFVKFV 611
Cdd:PRK07868 866 RGPVYTEPVTDALGRIG--GVDLAVTYGVEVGGRQ-LAVAAVTLRPGAAITAAD----LTEALAS--LPVGLGPDIVHVV 936
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41629676 612 DEIKMTDNHKILKKVYREQKLPKglDGNDTIFWLKNYKRYEVLTAA 657
Cdd:PRK07868 937 PEIPLSATYRPTVSALRAAGIPK--PGRQAWYFDPETNRYRRLTPA 980
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
254-624 |
2.13e-15 |
|
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: 79.04 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 254 LIYTSGTTGLPKSAIMSWRKSSVGCQVFG-HVLHMTNESTVFTAMPLF------HSTAALL--GACAILSHG-----GCL 319
Cdd:cd05919 96 LLYSSGTTGPPKGVMHAHRDPLLFADAMArEALGLTPGDRVFSSAKMFfgyglgNSLWFPLavGASAVLNPGwptaeRVL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 320 ALSHKFSASTFWKqvyltgathiqyVGEVCRYLLHTPISKYEKMHKVK--VAYGNGLRPDIWQDFRKRFNIEVIgEFYAA 397
Cdd:cd05919 176 ATLARFRPTVLYG------------VPTFYANLLDSCAGSPDALRSLRlcVSAGEALPRGLGERWMEHFGGPIL-DGIGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 398 TEAPFATTTFQKGDFGIGACrnyGTIIQWFlsfQQTLVrmDPNDDSViyrnskgfcevaPVGEPGEMLMRIffpkkpETS 477
Cdd:cd05919 243 TEVGHIFLSNRPGAWRLGST---GRPVPGY---EIRLV--DEEGHTI------------PPGEEGDLLVRG------PSA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 478 FQGYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEdqLTASNKEQYAQVLV 557
Cdd:cd05919 297 AVGYWNNPEKS-----RATFNGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE--SLIIQHPAVAEAAV 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 558 VGikVPKYEGragfaVIKLTdnsLDITAKTKLLND-SLSRL-------NLPSYAMPLFVKFVDEIKMTDNHKILK 624
Cdd:cd05919 368 VA--VPESTG-----LSRLT---AFVVLKSPAAPQeSLARDihrhlleRLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
155-616 |
3.35e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 79.58 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 155 LSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQV-----FIDPdasnpiRESEEEIKNALPDVKLNYLEE--------QD 221
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVitsrkFLEK------LKNKGFDLELPENVKVIYLEDlkakiskvDK 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 222 LMHELLNSQSPEFLQQDNVRTPLGLTDfkPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFH 301
Cdd:PRK08633 757 LTALLAARLLPARLLKRLYGPTFKPDD--TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 302 S---TAALLgacailshggcLALSHKFSAstfwkqVYLTGATHIQYVGEVCR-----YLLHTP--ISKYEKMHKVK---- 367
Cdd:PRK08633 835 SfglTVTLW-----------LPLLEGIKV------VYHPDPTDALGIAKLVAkhratILLGTPtfLRLYLRNKKLHplmf 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 368 ------VAYGNGLRPDIWQDFRKRFNIEvIGEFYAATE-APFAT----------TTFQKGdfgigaCRNyGTIiqwFLSF 430
Cdd:PRK08633 898 aslrlvVAGAEKLKPEVADAFEEKFGIR-ILEGYGATEtSPVASvnlpdvlaadFKRQTG------SKE-GSV---GMPL 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 431 QQTLVRM-DPNDdsviyrnskgfCEVAPVGEPGEMLMriffpKKPETsFQGYLGNAKETkSKVVRDVFRRGdaWYRCGDL 509
Cdd:PRK08633 967 PGVAVRIvDPET-----------FEELPPGEDGLILI-----GGPQV-MKGYLGDPEKT-AEVIKDIDGIG--WYVTGDK 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 510 LKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVLVVGikVPkyEGRAGFAVIKLTDNSLDITAKtkl 589
Cdd:PRK08633 1027 GHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTA--VP--DEKKGEKLVVLHTCGAEDVEE--- 1099
|
490 500
....*....|....*....|....*..
gi 41629676 590 LNDSLSRLNLPSYAMPLFVKFVDEIKM 616
Cdd:PRK08633 1100 LKRAIKESGLPNLWKPSRYFKVEALPL 1126
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
112-636 |
3.38e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 78.91 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 112 FTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFID 191
Cdd:PLN03102 40 FTWPQTYDRCCRLAASL-ISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 192 PDASNPIRESEEEI--KNALPDVKLNYLEEQDLMHELLNSQSP-EFLQQDNVRTPLGLT-------DFKPSMLIYTSGTT 261
Cdd:PLN03102 119 RSFEPLAREVLHLLssEDSNLNLPVIFIHEIDFPKRPSSEELDyECLIQRGEPTPSLVArmfriqdEHDPISLNYTSGTT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 262 GLPKSAIMSWRKS--SVGCQVFGhvLHMTNESTVFTAMPLFHSTAALLgACAILSHGGCLALSHKFSASTFWKQVYLTGA 339
Cdd:PLN03102 199 ADPKGVVISHRGAylSTLSAIIG--WEMGTCPVYLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHVTAPEIYKNIEMHNV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 340 THIQYVGEVCRYLLHTpiSKYEKMHK---VKVAYGNGLRPDIWQDFRKRFNIEVIgEFYAATEA--PFATTTFQKgdfgi 414
Cdd:PLN03102 276 THMCCVPTVFNILLKG--NSLDLSPRsgpVHVLTGGSPPPAALVKKVQRLGFQVM-HAYGLTEAtgPVLFCEWQD----- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 415 gACRNYGTIIQWFLSFQQTLVRMDPNDDSViyRNSKGFCEVAPVGEP-GEMLMriffpkKPETSFQGYLGNAKETKskvv 493
Cdd:PLN03102 348 -EWNRLPENQQMELKARQGVSILGLADVDV--KNKETQESVPRDGKTmGEIVI------KGSSIMKGYLKNPKATS---- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 494 rDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasnkeQYAQVL---VVGIKVPKY-EGRA 569
Cdd:PLN03102 415 -EAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLY-----KYPKVLetaVVAMPHPTWgETPC 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41629676 570 GFAVIKLTDNSLDITAKTKLLND----SLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREqkLPKGL 636
Cdd:PLN03102 487 AFVVLEKGETTKEDRVDKLVTRErdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD--IAKGL 555
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
113-626 |
3.41e-15 |
|
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: 78.29 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 113 TYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIdp 192
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 193 dasnpirESEEEiknalpdvklnyleeqDLMhellnsqspeflqqdnvrtplgltdfkpsMLIYTSGTTGLPKSAIMSWR 272
Cdd:cd05935 80 -------GSELD----------------DLA-----------------------------LIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 273 K--SSVGCQVFGHVLhmTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCR 350
Cdd:cd05935 108 SaaANALQSAVWTGL--TPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 351 YLLHTPISKYEKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIgEFYAATEAPFATTTFQKGDFGIgacrnygtiiqwfl 428
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTETMSQTHTNPPLRPKL-------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 429 sfqQTLVRMDPNDDSVIYRNSKGfcEVAPVGEPGEMLMRiffpkKPETsFQGYLGNAKETKSKVVRDVFRRgdaWYRCGD 508
Cdd:cd05935 251 ---QCLGIP*FGVDARVIDIETG--RELPPNEVGEIVVR-----GPQI-FKGYWNRPEETEESFIEIKGRR---FFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 509 LLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVLVVGikVPkyEGRAGFAVIKLTdnSLDITAKTK 588
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL--YKHPAI*EVCVIS--VP--DERVGEEVKAFI--VLRPEYRGK 388
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41629676 589 LLNDSL---SRLNLPSYAMPLFVKFVDEIKMTDNHKILKKV 626
Cdd:cd05935 389 VTEEDIiewAREQMAAYKYPREVEFVDELPRSASGKILWRL 429
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
134-628 |
5.61e-15 |
|
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: 77.76 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 134 VQAGDYVAIDCTNKPLFVFLWLSLWNIGAIpaflnyntkGTPLVHSLKISNITQVFIDPDASNPIRESEEeiknalpdvk 213
Cdd:cd05972 22 LRKGDRVAVLLPRVPELWAVILAVIKLGAV---------YVPLTTLLGPKDIEYRLEAAGAKAIVTDAED---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 214 lnyleeqdlmhellnsqspeflqqdnvrtplgltdfkPSMLIYTSGTTGLPKSAIMSWRkssvgcQVFGHVLHMTN---- 289
Cdd:cd05972 83 -------------------------------------PALIYFTSGTTGLPKGVLHTHS------YPLGHIPTAAYwlgl 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 290 -ESTVF--TAMP-----LFHSTAA--LLGACAILSHGgclalsHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISK 359
Cdd:cd05972 120 rPDDIHwnIADPgwakgAWSSFFGpwLLGATVFVYEG------PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 360 YEKMH-KVKVAYGNGLRPDIWQDFRKRFNIEvIGEFYAATEapfatTTFQKGDFgigacrnygtiiQWFLSFQQTLVRMD 438
Cdd:cd05972 194 YKFSHlRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTE-----TGLTVGNF------------PDMPVKPGSMGRPT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 439 PNDDSVIYrNSKGfcEVAPVGEPGEMLMRIffpkKPETSFQGYLGNAKETKSKVvrdvfrRGDaWYRCGDLLKADEYGLW 518
Cdd:cd05972 256 PGYDVAII-DDDG--RELPPGEEGDIAIKL----PPPGLFLGYVGDPEKTEASI------RGD-YYLTGDRAYRDEDGYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 519 YFLDRMGDTFRWKSENVSTTEVEDQLTasnkeQYAQVL---VVGIKVPKYeGRAGFAVIKLTDNSLDITAKTKLLNDsLS 595
Cdd:cd05972 322 WFVGRADDIIKSSGYRIGPFEVESALL-----EHPAVAeaaVVGSPDPVR-GEVVKAFVVLTSGYEPSEELAEELQG-HV 394
|
490 500 510
....*....|....*....|....*....|...
gi 41629676 596 RLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYR 628
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
252-624 |
1.10e-14 |
|
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: 75.62 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 252 SMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFW 331
Cdd:cd17638 3 SDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 332 KQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIGEFYAATEAPFATTtfqk 409
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVATM---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 410 gdfgigaCRnygtiiqwflsfqqtlvrmdPNDDSVIYRNSKGFC----EVApVGEPGEMLMRiffpkkPETSFQGYLGNA 485
Cdd:cd17638 159 -------CR--------------------PGDDAETVATTCGRAcpgfEVR-IADDGEVLVR------GYNVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 486 KETKSKVvrdvfrRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasNKEQYAQVLVVGIKVPKY 565
Cdd:cd17638 205 EATAEAI------DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALA--EHPGVAQVAVIGVPDERM 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 41629676 566 eGRAGFAVIkLTDNSLDITAKTKLlndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILK 624
Cdd:cd17638 277 -GEVGKAFV-VARPGVTLTEEDVI---AWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
134-625 |
5.31e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 75.08 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 134 VQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITqVFIDPDASNPIRES-------EEEIK 206
Cdd:PRK06178 80 VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAE-VLLALDQLAPVVEQvraetslRHVIV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 207 NALPDV--KLNYLEEQDL----------MHELLNSqspefLQQDNVRTPLGLTDF-KPSMLIYTSGTTGLPKSAIMSWRK 273
Cdd:PRK06178 159 TSLADVlpAEPTLPLPDSlraprlaaagAIDLLPA-----LRACTAPVPLPPPALdALAALNYTGGTTGMPKGCEHTQRD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 274 SSVGCQVFGHVLHMTNESTVFTA-MPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATH-IQYVGEVCRY 351
Cdd:PRK06178 234 MVYTAAAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRtVMLVDNAVEL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 352 LLHTPISKYE--KMHKVKVA-YGNGLRPDIwqdfRKRFNI---EVIGEF-YAATEAPFA---TTTFQKGDFGigacrnyg 421
Cdd:PRK06178 314 MDHPRFAEYDlsSLRQVRVVsFVKKLNPDY----RQRWRAltgSVLAEAaWGMTETHTCdtfTAGFQDDDFD-------- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 422 tiiqwfLSFQQTLVRMD-PNDDSVIYRNSKGfcEVAPVGEPGEMLMRiffpkKPeTSFQGYLGNAKETKskvvrDVFRrg 500
Cdd:PRK06178 382 ------LLSQPVFVGLPvPGTEFKICDFETG--ELLPLGAEGEIVVR-----TP-SLLKGYWNKPEATA-----EALR-- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 501 DAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasnkeQYAQVLVVGIkVPKYEGRAG---FAVIKLT 577
Cdd:PRK06178 441 DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG-----QHPAVLGSAV-VGRPDPDKGqvpVAFVQLK 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 41629676 578 DNSlDITAktkllnDSLS---RLNLPSYAMPLfVKFVDEIKMTDNHKILKK 625
Cdd:PRK06178 515 PGA-DLTA------AALQawcRENMAVYKVPE-IRIVDALPMTATGKVRKQ 557
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
251-630 |
1.24e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 73.87 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRksSVGCQVfghVLHMTN-----ESTVFTAMPLFHSTAALLgaCAILSHGGCLALSHKF 325
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHR--SIATMA---QIQLAEwewpaDPRFLMCTPLSHAGGAFF--LPTLLRGGTVIVLAKF 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 326 SASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK-VAYG-NGLRPDiwqdfRKRFNIEVIG----EFYAATE 399
Cdd:PRK06188 243 DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLEtVYYGaSPMSPV-----RLAEAIERFGpifaQYYGQTE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 400 APFATTTFQKGDFG------IGACrnyGTIIQWFlsfqqTLVRMDPNDDSViyrnskgfcevaPVGEPGEMLMRiffpkK 473
Cdd:PRK06188 318 APMVITYLRKRDHDpddpkrLTSC---GRPTPGL-----RVALLDEDGREV------------AQGEVGEICVR-----G 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 474 PETSfQGYLGNAKETKskvvrDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYA 553
Cdd:PRK06188 373 PLVM-DGYWNRPEETA-----EAFRDG--WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE--HPAVA 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 554 QVLVVGIKVPKYeGRAGFAVIKL-TDNSLD---ITAKTKllndslSRLNlpSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK06188 443 QVAVIGVPDEKW-GEAVTAVVVLrPGAAVDaaeLQAHVK------ERKG--SVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
.
gi 41629676 630 Q 630
Cdd:PRK06188 514 R 514
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
134-630 |
1.40e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 73.77 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 134 VQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDPD-ASNPIRESEEEIKNALPDV 212
Cdd:PRK06145 49 IGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEfDAIVALETPKIVIDAAAQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 213 KLNYLEEQdlmHELLNSQSPEfLQQDNVRtplgltdfkpsmLIYTSGTTGLPKSAIMSWrkSSVGCQVFGHV--LHMTNE 290
Cdd:PRK06145 129 DSRRLAQG---GLEIPPQAAV-APTDLVR------------LMYTSGTTDRPKGVMHSY--GNLHWKSIDHViaLGLTAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 291 STVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQV---YLTGA-------THIQYVGEVCRYLLHT---PI 357
Cdd:PRK06145 191 ERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIerhRLTCAwmapvmlSRVLTVPDRDRFDLDSlawCI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 358 SKYEKMHKVKVaygnglrpdiwQDFRKRFNIEVIGEFYAATEAPFATTTFQKGdfgigacRNYGTIIQWFLSFQQTLVRM 437
Cdd:PRK06145 271 GGGEKTPESRI-----------RDFTRVFTRARYIDAYGLTETCSGDTLMEAG-------REIEKIGSTGRALAHVEIRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 438 DPNDDSVIyrnskgfcevaPVGEPGEMLMRiffpkKPETSfQGYLGNAKETKSKVVRDvfrrgdaWYRCGDLLKADEYGL 517
Cdd:PRK06145 333 ADGAGRWL-----------PPNMKGEICMR-----GPKVT-KGYWKDPEKTAEAFYGD-------WFRSGDVGYLDEEGF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 518 WYFLDRMGDTFRWKSENVSTTEVEDQLTasNKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAKtkllnDSLSRL 597
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIY--ELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEAL-----DRHCRQ 461
|
490 500 510
....*....|....*....|....*....|...
gi 41629676 598 NLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK06145 462 RLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
81-629 |
8.08e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 71.34 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 81 LFIKQVQQNGDHLAISYtRPMAEKgefqletFTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNI 160
Cdd:PRK12583 23 AFDATVARFPDREALVV-RHQALR-------YTWRQLADAVDRLARGL-LALGVQPGDRVGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 161 GAIPAFLNYNTKGTPLVHSLKISNITQVFIDP-----DASNPIRESEEEIKNA---------LPDVK-LNYLEEQD---- 221
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADafktsDYHAMLQELLPGLAEGqpgalacerLPELRgVVSLAPAPppgf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 222 -LMHELLNSQSPEFLQQDNVRTPlGLTDFKPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLF 300
Cdd:PRK12583 174 lAWHELQARGETVSREALAERQA-SLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 301 HSTAALLGACAILSHGGCLAL-SHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK--VAYGNGLRPD 377
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRtgIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 378 IWQDFRKRFNIEVIGEFYAATEA-PFATTTFQKGDFGIGAcrnygtiiqwflsfqQTLVRMDPNDDSVIYrNSKGfcEVA 456
Cdd:PRK12583 333 VMRRVMDEMHMAEVQIAYGMTETsPVSLQTTAADDLERRV---------------ETVGRTQPHLEVKVV-DPDG--ATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 457 PVGEPGEMLMRIFfpkkpeTSFQGYLGNAKETKSKVVRDvfrrgdAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVS 536
Cdd:PRK12583 395 PRGEIGELCTRGY------SVMKGYWNNPEATAESIDED------GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 537 TTEVEDQLTasNKEQYAQVLVVGIKVPKYeGRAGFAVIKL-TDNSLDITAKTKLLNDSLSRLNLPSYamplfVKFVDEIK 615
Cdd:PRK12583 463 PREIEEFLF--THPAVADVQVFGVPDEKY-GEEIVAWVRLhPGHAASEEELREFCKARIAHFKVPRY-----FRFVDEFP 534
|
570
....*....|....
gi 41629676 616 MTDNHKILKKVYRE 629
Cdd:PRK12583 535 MTVTGKVQKFRMRE 548
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
111-559 |
1.28e-12 |
|
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: 70.32 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPaflnyntkgTPLVHSLKISNITQVfi 190
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVP---------VPIYPTSSAEQIAYI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 191 dpdasnpIRESEeeiknalpdVKLNYLEEqdlmhellnsqsPEFLqqdnvrtplgltdfkpSMLIYTSGTTGLPKSAIMS 270
Cdd:cd05907 73 -------LNDSE---------AKALFVED------------PDDL----------------ATIIYTSGTTGRPKGVMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 271 WRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHK----------------FSASTFWKQV 334
Cdd:cd05907 109 HRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSaetllddlsevrptvfLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 335 YLtgATHIQYVGEVCRYLLHTPISKyekmhKVKVAYGNG--LRPDIWQDFRKrFNIEVIgEFYAATE--APFATTTFQKG 410
Cdd:cd05907 189 YA--AIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAELLHFFRA-LGIPVY-EGYGLTEtsAVVTLNPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 411 DFG-IGACrnygtiiqwflsfqqtlvrMDPnddsviyrnskgfCEVApVGEPGEMLMRiffpkkPETSFQGYLGNAKETK 489
Cdd:cd05907 260 RIGtVGKP-------------------LPG-------------VEVR-IADDGEILVR------GPNVMLGYYKNPEATA 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41629676 490 SKVVRdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKS-ENVSTTEVEDQLTASnkEQYAQVLVVG 559
Cdd:cd05907 301 EALDA------DGWLHTGDLGEIDEDGFLHITGRKKDLIITSGgKNISPEPIENALKAS--PLISQAVVIG 363
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
254-634 |
1.72e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 254 LIYTSGTTGLPKSAIMSWRK--SSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFW 331
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNlvANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 332 KQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKV----AYGNGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTF 407
Cdd:PLN02330 269 NALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTH 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 408 QKGDFGIG-ACRNYGTIIQWFLSFQqtlvRMDPNDDSVIYRNSkgfcevapvgePGEMLMRiffpkkPETSFQGYLGNAK 486
Cdd:PLN02330 349 GDPEKGHGiAKKNSVGFILPNLEVK----FIDPDTGRSLPKNT-----------PGELCVR------SQCVMQGYYNNKE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 487 ETKSKVVRDvfrrgdAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVlvvgIKVPKYE 566
Cdd:PLN02330 408 ETDRTIDED------GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV----VPLPDEE 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41629676 567 -GRAGFAVIKLTDNSLDitAKTKLLNDSLSrlNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQKLPK 634
Cdd:PLN02330 478 aGEIPAACVVINPKAKE--SEEDILNFVAA--NVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
252-634 |
2.04e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 70.08 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 252 SMLIYTSGTTGLPKSAIMSWRKSSVGCQ----VFGHVLHMTNESTVfTAMPLFHsTAALLGACAILSHGGCLAL------ 321
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEqakaAYGPLLHPGKELVV-TALPLYH-IFALTVNCLLFIELGGQNLlitnpr 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 322 ----------SHKFSAstfwkqvyLTGathiqyVGEVCRYLLHTPISKYEKMHKVKVAYGNGLR-----PDIWQDFRKRF 386
Cdd:PRK08974 287 dipgfvkelkKYPFTA--------ITG------VNTLFNALLNNEEFQELDFSSLKLSVGGGMAvqqavAERWVKLTGQY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 387 NIEviGefYAATE-APFATttfqkgdfgigaCRNY------GTIiqwFLSFQQTLVRMDPNDDSViyrnskgfcevAPVG 459
Cdd:PRK08974 353 LLE--G--YGLTEcSPLVS------------VNPYdldyysGSI---GLPVPSTEIKLVDDDGNE-----------VPPG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 460 EPGEMlmrifFPKKPETsFQGYLGNAKETKsKVVRDvfrrgdAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTE 539
Cdd:PRK08974 403 EPGEL-----WVKGPQV-MLGYWQRPEATD-EVIKD------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 540 VEDQLTASNKeqyaqVL-VVGIKVP-KYEGRA--GFAVIKltDNSLditAKTKLLNDSlsRLNLPSYAMPLFVKFVDEIK 615
Cdd:PRK08974 470 IEDVVMLHPK-----VLeVAAVGVPsEVSGEAvkIFVVKK--DPSL---TEEELITHC--RRHLTGYKVPKLVEFRDELP 537
|
410
....*....|....*....
gi 41629676 616 MTDNHKILKKVYREQKLPK 634
Cdd:PRK08974 538 KSNVGKILRRELRDEARAK 556
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
251-625 |
2.42e-12 |
|
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: 69.39 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHS-------TAALLGACAILSHGGCLalsh 323
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDyglsvlnTHLLRGATLVLTNDGVL---- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 324 kfsASTFWKQVYLTGATH---IQYVGEVCRYLLHTPIsKYEKMHKVKVAyGNGLRPDIWQDFRKRFNIEVIGEFYAATEA 400
Cdd:cd05922 195 ---DDAFWEDLREHGATGlagVPSTYAMLTRLGFDPA-KLPSLRYLTQA-GGRLPQETIARLRELLPGAQVYVMYGQTEA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 401 pFATTTFQKGDFGIGACRNYGTIIqwflsfqqtlvrmdPNDDSVIYRNSKGFCevaPVGEPGEMLMRIFFPKKpetsfqG 480
Cdd:cd05922 270 -TRRMTYLPPERILEKPGSIGLAI--------------PGGEFEILDDDGTPT---PPGEPGEIVHRGPNVMK------G 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 481 YLGNAKETKSKVvrdvfRRGDAWYrCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNkeQYAQVLVVGI 560
Cdd:cd05922 326 YWNDPPYRRKEG-----RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG--LIIEAAAVGL 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 561 KVPKYEGRAGFAVIKLTDNSLDITaktkllnDSLSRLnLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd05922 398 PDPLGEKLALFVTAPDKIDPKDVL-------RSLAER-LPPYKVPATVRVVDELPLTASGKVDYA 454
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
121-632 |
3.54e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.44 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 121 VLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNtkgtplvHSLKISNITQVFIDP-----DAS 195
Cdd:PLN02860 42 VLSLAAGL-LRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR-------WSFEEAKSAMLLVRPvmlvtDET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 196 npIRESEEEIKN-ALPDVKLNYLEEQD---LMHELLNSQSPEFLQQDNVRTPLGLTDFKPS--MLI-YTSGTTGLPKSAI 268
Cdd:PLN02860 114 --CSSWYEELQNdRLPSLMWQVFLESPsssVFIFLNSFLTTEMLKQRALGTTELDYAWAPDdaVLIcFTSGTTGRPKGVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 269 MSWR----KSSVGCQVFGHvlhmtNESTVF--TAmPLFHsTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHI 342
Cdd:PLN02860 192 ISHSalivQSLAKIAIVGY-----GEDDVYlhTA-PLCH-IGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 343 QYVGEVCRYLLHTPISK-----YEKMHKVkVAYGNGLRPDIWQDFRKRFNIEVIGEFYAATEApFATTTFQkgdfgigac 417
Cdd:PLN02860 265 ITVPAMMADLISLTRKSmtwkvFPSVRKI-LNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEA-CSSLTFM--------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 418 RNYGTIIQWFLSFQQTLVRmdPNDDSViyRNSKGFCevapVGEPGEML-MRIFFP----------KKPETsFQGYLGNAK 486
Cdd:PLN02860 334 TLHDPTLESPKQTLQTVNQ--TKSSSV--HQPQGVC----VGKPAPHVeLKIGLDessrvgriltRGPHV-MLGYWGQNS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 487 ETKSKVVRDvfrrgdAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVLVVGIKvpkyE 566
Cdd:PLN02860 405 ETASVLSND------GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL--SQHPGVASVVVVGVP----D 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 567 GRAG---FAVIKL------TDNSLDITAKTKLLNDSLSRL-----NLPSYAMP-LFVKFVDEIKMTDNHKILKKVYREQK 631
Cdd:PLN02860 473 SRLTemvVACVRLrdgwiwSDNEKENAKKNLTLSSETLRHhcrekNLSRFKIPkLFVQWRKPFPLTTTGKIRRDEVRREV 552
|
.
gi 41629676 632 L 632
Cdd:PLN02860 553 L 553
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
251-628 |
3.95e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 68.61 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRkssvgcqvfghVL--HMTNESTVFTAMP----LFHSTA------ALLGACAILSHGGC 318
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHR-----------VLlgHLPGVQFPFNLFPrdgdLYWTPAdwawigGLLDVLLPSLYFGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 319 LALSH---KFSASTFWKQVYLTGATH-------IQYVGEVCRYLLHTPIskyeKMHKVKVAyGNGLRPDIWQDFRKRFNI 388
Cdd:cd05971 159 PVLAHrmtKFDPKAALDLMSRYGVTTaflpptaLKMMRQQGEQLKHAQV----KLRAIATG-GESLGEELLGWAREQFGV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 389 EViGEFYAATEApfatttfqkgDFGIGACRNygtiiqWFLSFQQTLVRMDPNDDSVIYrNSKGfcEVAPVGEPGEMLMRI 468
Cdd:cd05971 234 EV-NEFYGQTEC----------NLVIGNCSA------LFPIKPGSMGKPIPGHRVAIV-DDNG--TPLPPGEVGEIAVEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 469 FFPkkpeTSFQGYLGNAKETKSKVVRDvfrrgdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasN 548
Cdd:cd05971 294 PDP----VAFLGYWNNPSATEKKMAGD-------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLL--K 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 549 KEQYAQVLVVGIKVP-KYEGRAGFAVIKLTDNSLDITAKtKLLNdsLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVY 627
Cdd:cd05971 361 HPAVLMAAVVGIPDPiRGEIVKAFVVLNPGETPSDALAR-EIQE--LVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
.
gi 41629676 628 R 628
Cdd:cd05971 438 R 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
242-546 |
5.32e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 68.76 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 242 TPLGLTDfKPSMLIYTSGTTGLPKsaIMSWRKSSVGCQVFGHV--LHMTNESTVFTAMPLFHS---TAALLgacAILSHG 316
Cdd:PRK05852 170 TPEGLRP-DDAMIMFTGGTTGLPK--MVPWTHANIASSVRAIItgYRLSPRDATVAVMPLYHGhglIAALL---ATLASG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 317 GCLALSH--KFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAY----GNGLRPDIWQDFRKRFNIEV 390
Cdd:PRK05852 244 GAVLLPArgRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFirscSAPLTAETAQALQTEFAAPV 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 391 IgEFYAATEAPFATTTFQKGDFGigacRNYGTIIQWFLSFQQTLVRMDpnddsvIYRNSKGFCevaPVGEPGEMLMRiff 470
Cdd:PRK05852 324 V-CAFGMTEATHQVTTTQIEGIG----QTENPVVSTGLVGRSTGAQIR------IVGSDGLPL---PAGAVGEVWLR--- 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 471 pkkPETSFQGYLGNAKETKSKVVrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTA 546
Cdd:PRK05852 387 ---GTTVVRGYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLAS 452
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
138-625 |
5.36e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.63 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 138 DYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFID--------------PDASNPIresee 203
Cdd:PRK13382 94 RVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDeefsatvdraladcPQATRIV----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 204 eiknALPDvklnylEEQDLMHELLnsqSPEFLQQDNVRTPLgltdfKPSMLIYTSGTTGLPKSAImswRKSSVGCQVFGH 283
Cdd:PRK13382 169 ----AWTD------EDHDLTVEVL---IAAHAGQRPEPTGR-----KGRVILLTSGTTGTPKGAR---RSGPGGIGTLKA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 284 VLHMT---NESTVFTAMPLFHSTA------ALLGACAILSHggclalsHKFSASTFWKQVYLTGATHIQYVGEVCRYLLH 354
Cdd:PRK13382 228 ILDRTpwrAEEPTVIVAPMFHAWGfsqlvlAASLACTIVTR-------RRFDPEATLDLIDRHRATGLAVVPVMFDRIMD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 355 TP---ISKYE-KMHKVKVAYGNGLRPDIWQDFRKRFNiEVIGEFYAATEAPFATTT----FQKGDFGIGACRNyGTIIQW 426
Cdd:PRK13382 301 LPaevRNRYSgRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAGMIATAtpadLRAAPDTAGRPAE-GTEIRI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 427 FlsfqqtlvrmDPNddsviyrnskgFCEVaPVGEPGemlmRIFFpkKPETSFQGYL-GNAKETKskvvrdvfrrgDAWYR 505
Cdd:PRK13382 379 L----------DQD-----------FREV-PTGEVG----TIFV--RNDTQFDGYTsGSTKDFH-----------DGFMA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 506 CGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQVLVVGIKVPKYEGR-AGFAVIKLTDNSLDIT 584
Cdd:PRK13382 420 SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLAT--HPDVAEAAVIGVDDEQYGQRlAAFVVLKPGASATPET 497
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41629676 585 AKTKLlndslsRLNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:PRK13382 498 LKQHV------RDNLANYKVPRDIVVLDELPRGATGKILRR 532
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
140-630 |
2.44e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 66.34 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 140 VAIDCTNKPLFVFLWLSLWNIG--AIPafLNYNTKGTPLVHSLKISNITQVFIDPDASNPIRESEEEIKnalpdvklnyl 217
Cdd:PRK07638 53 IAILLENRIEFLQLFAGAAMAGwtCVP--LDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVI----------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 218 eEQDLMHELLNSQSPEFLQQDNVRTPlgltdfkPSMLIYTSGTTGLPKSAI---MSWrKSSVGCQVfgHVLHMTNESTVF 294
Cdd:PRK07638 120 -EIDEWKRMIEKYLPTYAPIENVQNA-------PFYMGFTSGSTGKPKAFLraqQSW-LHSFDCNV--HDFHMKREDSVL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 295 TAMPLFHSTaALLGACAILSHGGCLALSHKFSASTFWKQ-------VYLTGATHIQYVGEVCRYLLH--TPIS---KYEK 362
Cdd:PRK07638 189 IAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVLDKletenisVMYTVPTMLESLYKENRVIENkmKIISsgaKWEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 363 MHKVKVAygnglrpDIWQdFRKRFnievigEFYAATEAPFATttfqkgdfgigacrnygtiiqwFLSFQQTLVRmdPN-- 440
Cdd:PRK07638 268 EAKEKIK-------NIFP-YAKLY------EFYGASELSFVT----------------------ALVDEESERR--PNsv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 441 -----DDSVIYRNSKGfcEVAPVGEPGemlmRIFFpkKPETSFQGYLGNAKETKSKVVrdvfrrgDAWYRCGDLLKADEY 515
Cdd:PRK07638 310 grpfhNVQVRICNEAG--EEVQKGEIG----TVYV--KSPQFFMGYIIGGVLARELNA-------DGWMTVRDVGYEDEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 516 GLWYFLDRMGDTFRWKSENVSTTEVEDQLtasnKEQYA--QVLVVGIKVPkYEGRAGFAVIKLTDNSLDItaKTKLLNds 593
Cdd:PRK07638 375 GFIYIVGREKNMILFGGINIFPEEIESVL----HEHPAvdEIVVIGVPDS-YWGEKPVAIIKGSATKQQL--KSFCLQ-- 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41629676 594 lsrlNLPSYAMPLFVKFVDEIKMTDNHKI----LKKVYREQ 630
Cdd:PRK07638 446 ----RLSSFKIPKEWHFVDEIPYTNSGKIarmeAKSWIENQ 482
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
251-560 |
2.49e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 66.56 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQ-----VFGhvLHMTNEsTVFTAMPLFHSTAALLGACAILSHGGCLALSHKF 325
Cdd:PRK05605 221 VALILYTSGTTGKPKGAQLTHRNLFANAAqgkawVPG--LGDGPE-RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 326 SASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG--LRPDI---WQDFRKRFNIEviGefYAATE- 399
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAmaLPVSTvelWEKLTGGLLVE--G--YGLTEt 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 400 APFATTTfqkgdfGIGACRNYGTIiqwFLSFQQTLVRM-DPNDDSviyrnskgfcEVAPVGEPGEMLMRiffpkKPETsF 478
Cdd:PRK05605 374 SPIIVGN------PMSDDRRPGYV---GVPFPDTEVRIvDPEDPD----------ETMPDGEEGELLVR-----GPQV-F 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 479 QGYLGNAKETKskvvrDVFRrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVLVV 558
Cdd:PRK05605 429 KGYWNRPEETA-----KSFL--DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL--REHPGVEDAAVV 499
|
..
gi 41629676 559 GI 560
Cdd:PRK05605 500 GL 501
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
252-629 |
2.94e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 66.49 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 252 SMLIYTSGTTGLPKSAIMSWRKS-SVGCQVFGHVLHMTNESTVFTAmPLFHSTaALLGACAILSHGGCLALSHKFSASTF 330
Cdd:PRK07788 210 GIVILTSGTTGTPKGAPRPEPSPlAPLAGLLSRVPFRAGETTLLPA-PMFHAT-GWAHLTLAMALGSTVVLRRRFDPEAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 331 WKQVYLTGATHIQYVGEVCRYLLHTP---ISKYEKMH-KVKVAYGNGLRPDIWQDFRKRFNiEVIGEFYAATEAPFATTT 406
Cdd:PRK07788 288 LEDIAKHKATALVVVPVMLSRILDLGpevLAKYDTSSlKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 407 FQK---------GDFGIGAcrnygtiiqwflsfqqTLVRMDPNDDSViyrnskgfcevaPVGEPGemlmRIFFpkKPETS 477
Cdd:PRK07788 367 TPEdlaeapgtvGRPPKGV----------------TVKILDENGNEV------------PRGVVG----RIFV--GNGFP 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 478 FQGYL-GNAKETKskvvrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLtaSNKEQYAQVL 556
Cdd:PRK07788 413 FEGYTdGRDKQII-----------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL--AGHPDVVEAA 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 557 VVGIKVPKYEGRAGFAVIKLTDNSLDitaktkllNDSLS---RLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK07788 480 VIGVDDEEFGQRLRAFVVKAPGAALD--------EDAIKdyvRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
81-559 |
3.60e-11 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 66.28 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 81 LFIKQVQQNGDHLAISYtrpmAEKGEFQleTFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNI 160
Cdd:COG1022 16 LLRRRAARFPDRVALRE----KEDGIWQ--SLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 161 GAIPAFLnYNTKgTP--LVHSLKISNITQVFIdpdasnpirESEE------EIKNALPDVKLNYLEEQDLMH-------- 224
Cdd:COG1022 89 GAVTVPI-YPTS-SAeeVAYILNDSGAKVLFV---------EDQEqldkllEVRDELPSLRHIVVLDPRGLRddprllsl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 225 -ELL----NSQSPEFLQQdnVRTPLGLTDfkPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPL 299
Cdd:COG1022 158 dELLalgrEVADPAELEA--RRAAVKPDD--LATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 300 FHStAALLGACAILSHGGCLAlshkFSASTfwKQVyltgathIQYVGEVcR--YLLHTP-IskYEKMHK----------- 365
Cdd:COG1022 234 AHV-FERTVSYYALAAGATVA----FAESP--DTL-------AEDLREV-KptFMLAVPrV--WEKVYAgiqakaeeagg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 366 ---------VKVAY------GNGLRPDIWQDF-------------RKRF--NIEV-----------IGEFYAA------- 397
Cdd:COG1022 297 lkrklfrwaLAVGRryararLAGKSPSLLLRLkhaladklvfsklREALggRLRFavsggaalgpeLARFFRAlgipvle 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 398 ----TEAPFATTTFQKGDFGIGACrnyGTIIqwflsfqqtlvrmdPNddsviyrnskgfCEVApVGEPGEMLMR---Iff 470
Cdd:COG1022 377 gyglTETSPVITVNRPGDNRIGTV---GPPL--------------PG------------VEVK-IAEDGEILVRgpnV-- 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 471 pkkpetsFQGYLGNAKETkskvvRDVFRRgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKS-ENVSTTEVEDQLTASnk 549
Cdd:COG1022 425 -------MKGYYKNPEAT-----AEAFDA-DGWLHTGDIGELDEDGFLRITGRKKDLIVTSGgKNVAPQPIENALKAS-- 489
|
570
....*....|.
gi 41629676 550 eQY-AQVLVVG 559
Cdd:COG1022 490 -PLiEQAVVVG 499
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
190-634 |
5.32e-11 |
|
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: 65.43 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASnpiresEEEIKNALPDVKLNY-LEEQDLMHELLNSQSPEFLQQDNVRTPlGLTDFKP-------SMLIYTSGTT 261
Cdd:cd17655 77 IDPDYP------EERIQYILEDSGADIlLTQSHLQPPIAFIGLIDLLDEDTIYHE-ESENLEPvsksddlAYVIYTSGST 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 262 GLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVftamPLFHS-----------TAALLGACAILSHGGCLALSHKFSASTF 330
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANKVIYQGEHLRV----ALFASisfdasvteifASLLSGNTLYIVRKETVLDGQALTQYIR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 331 WKQVYLTGAT--HIQYvgevcryLLHTPISKYEKMHKVKVAyGNGLRPDIWQDFRKRF--NIEVIGEfYAATEAPFATTT 406
Cdd:cd17655 226 QNRITIIDLTpaHLKL-------LDAADDSEGLSLKHLIVG-GEALSTELAKKIIELFgtNPTITNA-YGPTETTVDASI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 407 FQ-------KGDFGIGAcrnygtiiqwflsfqqtlvrmdPNDDSVIY-RNSKGfcEVAPVGEPGEMLMriffpkKPETSF 478
Cdd:cd17655 297 YQyepetdqQVSVPIGK----------------------PLGNTRIYiLDQYG--RPQPVGVAGELYI------GGEGVA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 479 QGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVLVv 558
Cdd:cd17655 347 RGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIA- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41629676 559 gikVPKYEGRAGFAVIKLTDNSLDITAktklLNDSLSRlNLPSYAMP-LFVKfVDEIKMTDNHKILKKvyreqKLPK 634
Cdd:cd17655 426 ---RKDEQGQNYLCAYIVSEKELPVAQ----LREFLAR-ELPDYMIPsYFIK-LDEIPLTPNGKVDRK-----ALPE 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
251-622 |
7.73e-11 |
|
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: 64.65 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPK---------SAIMSWRKSSVGCQVFGHVLHMTneSTVF--TAMPLFhstaallgacAILSHGGCL 319
Cdd:cd12115 107 LAYVIYTSGSTGRPKgvaiehrnaAAFLQWAAAAFSAEELAGVLAST--SICFdlSVFELF----------GPLATGGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 320 ALS----HKFSASTfwkqvyLTGATHIQYVGEVCRYLL-HTPISKYEKMhkVKVAyGNGLRPDIWQDFRKRFNIEVIGEF 394
Cdd:cd12115 175 VLAdnvlALPDLPA------AAEVTLINTVPSAAAELLrHDALPASVRV--VNLA-GEPLPRDLVQRLYARLQVERVVNL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 395 YAATEapfaTTTF---------QKGDFGIGACRnYGTiiqwflsfqQTLVrMDPNDDSViyrnskgfcevaPVGEPGEML 465
Cdd:cd12115 246 YGPSE----DTTYstvapvppgASGEVSIGRPL-ANT---------QAYV-LDRALQPV------------PLGVPGELY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 466 MriffpkKPETSFQGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLT 545
Cdd:cd12115 299 I------GGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 546 asNKEQYAQVLVVGIKVPKYEGR-AGFAViklTDNSLDItaktkLLNDSLSRL--NLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd12115 373 --SIPGVREAVVVAIGDAAGERRlVAYIV---AEPGAAG-----LVEDLRRHLgtRLPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
251-628 |
1.13e-10 |
|
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: 64.31 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFG-HVLHMTNESTVFTAMPLFHstAALLGACAI--LSHGG-CLALSHKFS 326
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAELYArNVLGIREDDVCFSAAKLFF--AYGLGNSLTfpLSVGAtTVLMPERPT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 327 ASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVK--VAYGNGLRPDIWQDFRKRFNIEV---IGefyaATEAP 401
Cdd:cd05959 243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRlcVSAGEALPAEVGERWKARFGLDIldgIG----STEML 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 402 --FATTTfqkgdfgIGACRnYGTIIQWFLSFQQTLVRMDPNDDsviyrnskgfcevaPVGEPGEMLMRiffpkkPETSFQ 479
Cdd:cd05959 319 hiFLSNR-------PGRVR-YGTTGKPVPGYEVELRDEDGGDV--------------ADGEPGELYVR------GPSSAT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 480 GYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTasnkeQYAQVL--- 556
Cdd:cd05959 371 MYWNNRDKT-----RDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALV-----QHPAVLeaa 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41629676 557 VVGIKVPkyEGRAGF-AVIKLTDNSLDITAKTKLLNDSLsRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYR 628
Cdd:cd05959 439 VVGVEDE--DGLTKPkAFVVLRPGYEDSEALEEELKEFV-KDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
99-346 |
1.20e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.52 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 99 RPMAEKGEfqlETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVH 178
Cdd:PRK07798 19 RVALVCGD---RRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 179 slkisnitqVFIDPDASNPIRESE-----EEIKNALPDVKL----------NYLEEQDLMHELLNSQSPEflqqdnvrtP 243
Cdd:PRK07798 95 ---------LLDDSDAVALVYEREfaprvAEVLPRLPKLRTlvvvedgsgnDLLPGAVDYEDALAAGSPE---------R 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 244 LGLTdfkPS----MLIYTSGTTGLPKsAIMsWRKSSVGCQVFGHVLHMTNE-----------------STVFTAMPLFHs 302
Cdd:PRK07798 157 DFGE---RSpddlYLLYTGGTTGMPK-GVM-WRQEDIFRVLLGGRDFATGEpiedeeelakraaagpgMRRFPAPPLMH- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41629676 303 TAALLGACAILSHGGCLAL--SHKFSASTFWKQVYLTGATHIQYVG 346
Cdd:PRK07798 231 GAGQWAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVG 276
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
111-625 |
1.70e-10 |
|
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: 63.52 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNyntkgtplvhslkisnitqvfi 190
Cdd:cd05912 1 SYTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 191 dpdasnpIRESEEEIKNALPDVKLnyleeqdlmhellnsqspeflQQDNVRTplgltdfkpsmLIYTSGTTGLPKSAIMS 270
Cdd:cd05912 58 -------TRLTPNELAFQLKDSDV---------------------KLDDIAT-----------IMYTSGTTGKPKGVQQT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 271 WRK---SSVGCQVfghVLHMTNESTVFTAMPLFHstaalLGACAILSHG---GCLALSH-KFSASTFWKQVYLTGATHIQ 343
Cdd:cd05912 99 FGNhwwSAIGSAL---NLGLTEDDNWLCALPLFH-----ISGLSILMRSviyGMTVYLVdKFDAEQVLHLINSGKVTIIS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 344 YVGEVCRYLLHTPISKYEKMHKvKVAYGNGLRPDIWQDFRKRFNIEVIgEFYAATEA--PFATTTFQKGDFGIGacrnyg 421
Cdd:cd05912 171 VVPTMLQRLLEILGEGYPNNLR-CILLGGGPAPKPLLEQCKEKGIPVY-QSYGMTETcsQIVTLSPEDALNKIG------ 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 422 tiiqwflSFQQTLvrmdPNDDSVIYRNSKgfcevaPVGEPGEMLMriffpKKPETSfQGYLGNAKETKSkvvrdVFRRGd 501
Cdd:cd05912 243 -------SAGKPL----FPVELKIEDDGQ------PPYEVGEILL-----KGPNVT-KGYLNRPDATEE-----SFENG- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 502 aWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIKVPKYeGRAGFAVIKLtdnSL 581
Cdd:cd05912 294 -WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSH--PAIKEAGVVGIPDDKW-GQVPVAFVVS---ER 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 41629676 582 DITAKTklLNDSLSRlNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd05912 367 PISEEE--LIAYCSE-KLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
111-629 |
3.04e-10 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 63.23 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNiTQVFI 190
Cdd:PRK06087 49 SYTYSALDHAASRLANWL-LAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQ-AKMFF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 191 DPDASNPIRESEE--EIKNALPdvklnYLEEQDLMHELLNSQSPEFLQQDNVRTPlGLTDFKP------SMLIYTSGTTG 262
Cdd:PRK06087 127 APTLFKQTRPVDLilPLQNQLP-----QLQQIVGVDKLAPATSSLSLSQIIADYE-PLTTAITthgdelAAVLFTSGTEG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 263 LPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQV------YL 336
Cdd:PRK06087 201 LPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLeqqrctCM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 337 TGAT--------HIQYVG---EVCRYLL--HTPISKyeKMhkVKVAYGNGLRpdiwqdfrkrfnievIGEFYAATEA-PF 402
Cdd:PRK06087 281 LGATpfiydllnLLEKQPadlSALRFFLcgGTTIPK--KV--ARECQQRGIK---------------LLSVYGSTESsPH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 403 ATTTFQKGdfgigacrnygtiIQWFLSFQQTL---VRMDPNDDsviYRNSkgfcevAPVGEPGEMLMRiffpkKPETsFQ 479
Cdd:PRK06087 342 AVVNLDDP-------------LSRFMHTDGYAaagVEIKVVDE---ARKT------LPPGCEGEEASR-----GPNV-FM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 480 GYLgNAKETKSKVVRDvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVlvvg 559
Cdd:PRK06087 394 GYL-DEPELTARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV---- 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41629676 560 IKVPkyEGRAG-----FAVIKLTDNSL---DITAktkllndSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK06087 464 VAMP--DERLGerscaYVVLKAPHHSLtleEVVA-------FFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
78-629 |
5.22e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 62.29 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 78 NWylFIKQVQQNGDHLAIsytrpmaekgEFQLETFTYIETYNIVLRLSHILhFDYNVQAGDYVAIDCTNKPLFVFLWLSL 157
Cdd:PRK03640 6 NW--LKQRAFLTPDRTAI----------EFEEKKVTFMELHEAVVSVAGKL-AALGVKKGDRVALLMKNGMEMILVIHAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 158 WNIGAIPAFLNynTKGTP--LVHSLKISNITQVFIDPDASNPIRESEEEIKNALPDVKLNYLEEQDLMHEllnsqspefl 235
Cdd:PRK03640 73 QQLGAVAVLLN--TRLSReeLLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 236 qqDNVRTplgltdfkpsmLIYTSGTTGLPKSAIMSWRK---SSVGCQVfghVLHMTNESTVFTAMPLFH-STAALLGACA 311
Cdd:PRK03640 141 --DEVAT-----------IMYTSGTTGKPKGVIQTYGNhwwSAVGSAL---NLGLTEDDCWLAAVPIFHiSGLSILMRSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 312 IlsHGGCLALSHKFSAStfwkqvyltgathiqyvgEVCRYLLH---TPISKYEKMHKVKVA-YGNGLRPDiwqDFR---- 383
Cdd:PRK03640 205 I--YGMRVVLVEKFDAE------------------KINKLLQTggvTIISVVSTMLQRLLErLGEGTYPS---SFRcmll 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 384 -------------KRFNIEVIgEFYAATEapfatTTFQkgdfgigacrnygtiiqwflsfqqtLVRMDPnDDSVIYRNSK 450
Cdd:PRK03640 262 gggpapkplleqcKEKGIPVY-QSYGMTE-----TASQ-------------------------IVTLSP-EDALTKLGSA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 451 G---F-CEV--------APVGEPGEMLMriffpKKPeTSFQGYLGNAKETKskvvrDVFRrgDAWYRCGDLLKADEYGLW 518
Cdd:PRK03640 310 GkplFpCELkiekdgvvVPPFEEGEIVV-----KGP-NVTKGYLNREDATR-----ETFQ--DGWFKTGDIGYLDEEGFL 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 519 YFLDRMGDTFRWKSENVSTTEVEDQLTAsnKEQYAQVLVVGI------KVPkyegrAGFAVI--KLTDNSLditaktkll 590
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLS--HPGVAEAGVVGVpddkwgQVP-----VAFVVKsgEVTEEEL--------- 440
|
570 580 590
....*....|....*....|....*....|....*....
gi 41629676 591 nDSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK03640 441 -RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
478-625 |
1.05e-09 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 61.11 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 478 FQGYLGNAKETKSKVVRDVFRRgdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkeQYAQVLV 557
Cdd:cd05945 309 SKGYLNNPEKTAAAFFPDEGQR---AYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQV---PGVKEAV 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41629676 558 VgikVPKYEGRAG---FAVIKLTDNSLDitAKTKLLNDSLSRlNLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd05945 383 V---VPKYKGEKVtelIAFVVPKPGAEA--GLTKAIKAELAE-RLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-622 |
1.90e-09 |
|
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: 60.25 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 81 LFIKQVQQNGDHLAISytrpmAEKGEFqletfTYIETYNIVLRLSHILHfDYNVQAGDYVAIdCTNKplfvflwlSLWni 160
Cdd:cd05918 4 LIEERARSQPDAPAVC-----AWDGSL-----TYAELDRLSSRLAHHLR-SLGVGPGVFVPL-CFEK--------SKW-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 161 gAIPAFLnyntkGTplvhsLKISNiTQVFIDPdasnpireseeeiknalpdvklnyleeqdlmhellnSQSPEFLQ---Q 237
Cdd:cd05918 62 -AVVAML-----AV-----LKAGG-AFVPLDP------------------------------------SHPLQRLQeilQ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 238 DnVRTPLGLTDfKPS---MLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFtampLFHS---TAALLGACA 311
Cdd:cd05918 94 D-TGAKVVLTS-SPSdaaYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVL----QFASytfDVSILEIFT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 312 ILSHGGCL----------ALSHKFSAstfwkqvylTGATHIQYVGEVCRYL-------LHTPISKYEKMHKVKVaygngl 374
Cdd:cd05918 168 TLAAGGCLcipseedrlnDLAGFINR---------LRVTWAFLTPSVARLLdpedvpsLRTLVLGGEALTQSDV------ 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 375 rpDIWQDFRKRFNievigeFYAATEAPFATTTFQKGDfgIGACRNYGTiiqwflSFQQTLVRMDPNDDsviyrnskgfCE 454
Cdd:cd05918 233 --DTWADRVRLIN------AYGPAECTIAATVSPVVP--STDPRNIGR------PLGATCWVVDPDNH----------DR 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 455 VAPVGEPGEMLMriffpkkpETSF--QGYLGNAKETKSKVVRD-------VFRRGDAWYRCGDLLKADEYGLWYFLDRMG 525
Cdd:cd05918 287 LVPIGAVGELLI--------EGPIlaRGYLNDPEKTAAAFIEDpawlkqeGSGRGRRLYRTGDLVRYNPDGSLEYVGRKD 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 526 DT-----FRW---------KSENVSTTEVEDQLTASNKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAKTKLLN 591
Cdd:cd05918 359 TQvkirgQRVelgeiehhlRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELR 438
|
570 580 590
....*....|....*....|....*....|.
gi 41629676 592 DSLSRlNLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd05918 439 SKLRQ-RLPSYMVPSVFLPLSHLPLTASGKI 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
110-541 |
3.23e-09 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 59.86 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVF 189
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 190 IDPDASnpirESEEEIKNALPDVKLNY-----LEEQDLMHELLnSQSPEFLqqdnVRTPLGLTDFKPSMliYTSGTTGLP 264
Cdd:PLN02574 145 TSPENV----EKLSPLGVPVIGVPENYdfdskRIEFPKFYELI-KEDFDFV----PKPVIKQDDVAAIM--YSSGTTGAS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 265 KSAIMSWRKSSVGCQVF-----GHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGA 339
Cdd:PLN02574 214 KGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 340 THIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRP---DIWQDFRKRF-NIEVIgEFYAATEapfATTTFQKGdFGIG 415
Cdd:PLN02574 294 THFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPlsgKFIQDFVQTLpHVDFI-QGYGMTE---STAVGTRG-FNTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 416 ACRNYGTIiqwflsfqqtlVRMDPNDDSVIYRNSKGFCevAPVGEPGEMLMRiffpkKPETsFQGYLGNAKETKSKVVRd 495
Cdd:PLN02574 369 KLSKYSSV-----------GLLAPNMQAKVVDWSTGCL--LPPGNCGELWIQ-----GPGV-MKGYLNNPKATQSTIDK- 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 41629676 496 vfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVE 541
Cdd:PLN02574 429 -----DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLE 469
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
254-628 |
3.69e-09 |
|
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: 59.25 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 254 LIYTSGTTGLPK---------SAIMSWRKSSVGCQVFGHVLHMTneSTVFTAmplfhSTAALLGAcaiLSHGGCLALSHk 324
Cdd:cd17653 110 IIFTSGSTGIPKgvmvphrgvLNYVSQPPARLDVGPGSRVAQVL--SIAFDA-----CIGEIFST---LCNGGTLVLAD- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 325 fSASTFwkqvyltgathiQYVGEVCRYLLHTP-------ISKYEKMHKVKVAyGNGLRPDI---WQDFRKRFNievigeF 394
Cdd:cd17653 179 -PSDPF------------AHVARTVDALMSTPsilstlsPQDFPNLKTIFLG-GEAVPPSLldrWSPGRRLYN------A 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 395 YAATEAPFATTTFQ--KGDF-GIG-ACRNYGTIIqwflsfqqtlvrMDPNDDSViyrnskgfcevaPVGEPGEM------ 464
Cdd:cd17653 239 YGPTECTISSTMTEllPGQPvTIGkPIPNSTCYI------------LDADLQPV------------PEGVVGEIcisgvq 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 465 LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQL 544
Cdd:cd17653 295 VAR------------GYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 545 TASNKE-QYAQVLVVGikvpkyegraGFAVIKLTDNSLDITAktklLNDSLSRLnLPSYAMPLFVKFVDEIKMTDNHKI- 622
Cdd:cd17653 363 LQSQPEvTQAAAIVVN----------GRLVAFVTPETVDVDG----LRSELAKH-LPSYAVPDRIIALDSFPLTANGKVd 427
|
....*.
gi 41629676 623 LKKVYR 628
Cdd:cd17653 428 RKALRE 433
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
251-622 |
6.05e-09 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 58.05 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHsTAALLGACAILSHGGCLALSHKFSAStf 330
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFH-IAGLNLALATFHAGGANVVMEKFDPA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 331 wKQVYLTGATHIQYVGEVCRYLlhTPISKYEKMHKVKVAygnGLR-------PDIWQDFRKRFNieviGEFYAA---TEA 400
Cdd:cd17637 79 -EALELIEEEKVTLMGSFPPIL--SNLLDAAEKSGVDLS---SLRhvlgldaPETIQRFEETTG----ATFWSLygqTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 401 PfATTTFQKGDFGIGACrnyGTIIQWflsfqqTLVR-MDPNDDSViyrnskgfcevaPVGEPGEMLMRiffpkKPeTSFQ 479
Cdd:cd17637 149 S-GLVTLSPYRERPGSA---GRPGPL------VRVRiVDDNDRPV------------PAGETGEIVVR-----GP-LVFQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 480 GYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKS--ENVSTTEVEDQLTAsnKEQYAQVLV 557
Cdd:cd17637 201 GYWNLPELT-----AYTFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKPggENVYPAEVEKVILE--HPAIAEVCV 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 558 VGIKVPKYeGRAGFAVIKLTDNSLdITAKtKLLNDSLSRlnLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd17637 272 IGVPDPKW-GEGIKAVCVLKPGAT-LTAD-ELIEFVGSR--IARYKKPRYVVFVEALPKTADGSI 331
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-621 |
8.25e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 57.78 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 254 LIYTSGTTGLPKsAIMsWRKSSVGCQVFGHVLHMTNE----------------STVFTAMPLFHSTAALLGACAILSHGG 317
Cdd:cd05924 8 ILYTGGTTGMPK-GVM-WRQEDIFRMLMGGADFGTGEftpsedahkaaaaaagTVMFPAPPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 318 CLALSHKFSASTFWKQVYLTGATHIQYVGEV-CRYLLH-------TPISKYekmhkvkVAYGNG---LRPDIWQDFRKRF 386
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAmARPLIDalrdagpYDLSSL-------FAISSGgalLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 387 NIEVIGEFYAATEAPFATTTFQKGdfgigacrnygtiiqwflSFQQTLVRMDPNDDSVIYRNSKGFCEVAPvGEPGEMLM 466
Cdd:cd05924 159 PNITLVDAFGSSETGFTGSGHSAG------------------SGPETGPFTRANPDTVVLDDDGRVVPPGS-GGVGWIAR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 467 RIFFPkkpetsfQGYLGNAKETKskvvrDVFRR--GDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQL 544
Cdd:cd05924 220 RGHIP-------LGYYGDEAKTA-----ETFPEvdGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEAL 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41629676 545 TAsnKEQYAQVLVVGIKVPKYeGRAGFAVIKLTDN-SLDITAKTKLLNDSLSRlnlpsYAMPLFVKFVDEIKMTDNHK 621
Cdd:cd05924 288 KS--HPAVYDVLVVGRPDERW-GQEVVAVVQLREGaGVDLEELREHCRTRIAR-----YKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
454-636 |
9.19e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 58.51 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 454 EVAPvGEPGEMLMRiffpkKPETsFQGYLGNAKETkskvvRDVFRrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSE 533
Cdd:PRK07470 360 ELPP-GETGEICVI-----GPAV-FAGYYNNPEAN-----AKAFR--DGWFRTGDLGHLDARGFLYITGRASDMYISGGS 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 534 NVSTTEVEDQLTASnkEQYAQVLVVGIKVPKYeGRAGFAVIKLTDnSLDITAKTklLNDSLSRlNLPSYAMPLFVKFVDE 613
Cdd:PRK07470 426 NVYPREIEEKLLTH--PAVSEVAVLGVPDPVW-GEVGVAVCVARD-GAPVDEAE--LLAWLDG-KVARYKLPKRFFFWDA 498
|
170 180
....*....|....*....|...
gi 41629676 614 IKMTDNHKILKKVYREQKLPKGL 636
Cdd:PRK07470 499 LPKSGYGKITKKMVREELEERGL 521
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
219-629 |
9.55e-09 |
|
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: 58.16 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 219 EQDLMHELLNSQSPEFLQQDNVR--TPLGLTDfKPSMLIYTSGTTGLPKSAIMSwrKSSVGCQVFGHVLHM--TNESTVF 294
Cdd:cd05903 62 EHELAFILRRAKAKVFVVPERFRqfDPAAMPD-AVALLLFTSGTTGEPKGVMHS--HNTLSASIRQYAERLglGPGDVFL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 295 TAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQ----YVGEVCRYLLH--TPISKYEKMhkvkV 368
Cdd:cd05903 139 VASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgatpFLTDLLNAVEEagEPLSRLRTF----V 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 369 AYGNGLRPDIWQDFRKRFnIEVIGEFYAATEAPFATTTFQKGDFGIGACRNyGTIiqwflsFQQTLVRMDPNDDSVIyrn 448
Cdd:cd05903 215 CGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD-GRP------LPGVEIKVVDDTGATL--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 449 skgfcevaPVGEPGEMLMRiffpkKPETsFQGYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTF 528
Cdd:cd05903 284 --------APGVEGELLSR-----GPSV-FLGYLDRPDLT-----ADAAPEG--WFRTGDLARLDEDGYLRITGRSKDII 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 529 RWKSENVSTTEVEDQLTASNKeqYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAktklLNDSLSRLNLPSYAMPLFV 608
Cdd:cd05903 343 IRGGENIPVLEVEDLLLGHPG--VIEAAVVALPDERLGERACAVVVTKSGALLTFDE----LVAYLDRQGVAKQYWPERL 416
|
410 420
....*....|....*....|.
gi 41629676 609 KFVDEIKMTDNHKILKKVYRE 629
Cdd:cd05903 417 VHVDDLPRTPSGKVQKFRLRE 437
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
251-632 |
2.11e-08 |
|
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: 57.13 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPK------SAIMSWRKSsvGCQVFGhvLHmtnESTVF--TAMP------LFHSTAALLGACAILSHG 316
Cdd:cd05969 91 PTLLHYTSGTTGTPKgvlhvhDAMIFYYFT--GKYVLD--LH---PDDIYwcTADPgwvtgtVYGIWAPWLNGVTNVVYE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 317 GclalshKFSASTFWK-------QVYLTGATHIQYVGEVCRYLLhtpiSKYEKMH-KVKVAYGNGLRPDIwqdfrKRFNI 388
Cdd:cd05969 164 G------RFDAESWYGiiervkvTVWYTAPTAIRMLMKEGDELA----RKYDLSSlRFIHSVGEPLNPEA-----IRWGM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 389 EVIGefyaateAPFATTTFQKGDFGIGACrNY-------GTIIQWFLSFQQTLVRMDPNDdsviyrnskgfcevAPVGEP 461
Cdd:cd05969 229 EVFG-------VPIHDTWWQTETGSIMIA-NYpcmpikpGSMGKPLPGVKAAVVDENGNE--------------LPPGTK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 462 GEMLMRIFFPkkpeTSFQGYLGNAKETKSKVVrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVE 541
Cdd:cd05969 287 GILALKPGWP----SMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 542 DQLTasNKEQYAQVLVVGIKVPkYEGRAGFAVIKLTDnslDITAKTKLLNDSLS--RLNLPSYAMPLFVKFVDEIKMTDN 619
Cdd:cd05969 356 SALM--EHPAVAEAGVIGKPDP-LRGEIIKAFISLKE---GFEPSDELKEEIINfvRQKLGAHVAPREIEFVDNLPKTRS 429
|
410
....*....|...
gi 41629676 620 HKILKKVYREQKL 632
Cdd:cd05969 430 GKIMRRVLKAKEL 442
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
251-622 |
5.47e-08 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 55.34 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKS-SVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSAST 329
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 330 FWKQVYLTGATHIqyvgevcrYLLHTPISKYEKMHKVKVAYGNGLRpdiwqdfrkrfNIEVIGEFYAATEAPFATTTfqk 409
Cdd:cd17635 83 LFKILTTNAVTTT--------CLVPTLLSKLVSELKSANATVPSLR-----------LIGYGGSRAIAADVRFIEAT--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 410 gdfgigacRNYGTIIQWFLSFQQTLVRMDPNDDS--------------VIYRNSKGFceVAPVGEPGEMLMriffpkKPE 475
Cdd:cd17635 141 --------GLTNTAQVYGLSETGTALCLPTDDDSieinavgrpypgvdVYLAATDGI--AGPSASFGTIWI------KSP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 476 TSFQGYLGNAKETKSKVVrdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVED--------QLTAS 547
Cdd:cd17635 205 ANMLGYWNNPERTAEVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERiaegvsgvQECAC 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41629676 548 NK---EQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSlditaktkllndslsrlNLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd17635 278 YEisdEEFGELVGLAVVASAELDENAIRALKHTIRR-----------------ELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
257-518 |
6.89e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 55.73 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 257 TSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALS------HKFSASTF 330
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgyrGPGVIANF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 331 WKQVYLTGATHIQYVGEVCRYLLHTPISKYEkMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIgEFYAATEAPFATTT-F 407
Cdd:PRK07529 301 WKIVERYRINFLSGVPTVYAALLQVPVDGHD-ISSLRYALCGAapLPVEVFRRFEAATGVRIV-EGYGLTEATCVSSVnP 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 408 QKGDFGIGAcrnygtiIQWFLSFQQT-LVRMDPNDDSViyRNskgfcevAPVGEPGEMLMRiffpkKPeTSFQGYLGNAK 486
Cdd:PRK07529 379 PDGERRIGS-------VGLRLPYQRVrVVILDDAGRYL--RD-------CAVDEVGVLCIA-----GP-NVFSGYLEAAH 436
|
250 260 270
....*....|....*....|....*....|...
gi 41629676 487 EtkskvvRDVFrRGDAWYRCGDLLKADEYG-LW 518
Cdd:PRK07529 437 N------KGLW-LEDGWLNTGDLGRIDADGyFW 462
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-630 |
9.95e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 54.97 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 113 TYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKisnitqvfiDP 192
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVT---------DS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 193 DASNPIRESE--EEIKNALPDVKL---------NYLEEQ--DLMHELLNSQSP-------------EFLQQDNVRTPL-- 244
Cdd:PRK08314 108 GARVAIVGSElaPKVAPAVGNLRLrhvivaqysDYLPAEpeIAVPAWLRAEPPlqalapggvvawkEALAAGLAPPPHta 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 245 GLTDFkpSMLIYTSGTTGLPKSAIMSWRksSVGCQVFGHVL--HMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALs 322
Cdd:PRK08314 188 GPDDL--AVLPYTSGTTGVPKGCMHTHR--TVMANAVGSVLwsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 323 hkfsaSTFWKQvyltgathiqyvgEVCRYLlhtpISKYEKMHkvkvaygnglrpdiWQ-------DFRKRFNIE------ 389
Cdd:PRK08314 263 -----MPRWDR-------------EAAARL----IERYRVTH--------------WTniptmvvDFLASPGLAerdlss 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 390 --VIGEFYAATeaPFATTTFQKGDFGIGACRNYG---TIIQwflsfqqtlVRMDPND--------------DSVIYRNSK 450
Cdd:PRK08314 307 lrYIGGGGAAM--PEAVAERLKELTGLDYVEGYGlteTMAQ---------THSNPPDrpklqclgiptfgvDARVIDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 451 GfcEVAPVGEPGEMLMRiffpkKPETsFQGYLGNAKETkskvvRDVF--RRGDAWYRCGDLLKADEYGLWYFLD---RMG 525
Cdd:PRK08314 376 L--EELPPGEVGEIVVH-----GPQV-FKGYWNRPEAT-----AEAFieIDGKRFFRTGDLGRMDEEGYFFITDrlkRMI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 526 DTFRWKsenVSTTEVEDQLTASNKEQyaQVLVVGIKVPkYEGRAGFAVIKLTDNSLDITAKTKLLndSLSRLNLPSYAMP 605
Cdd:PRK08314 443 NASGFK---VWPAEVENLLYKHPAIQ--EACVIATPDP-RRGETVKAVVVLRPEARGKTTEEEII--AWAREHMAAYKYP 514
|
570 580
....*....|....*....|....*
gi 41629676 606 LFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK08314 515 RIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
110-635 |
9.96e-08 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 54.99 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 110 ETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIpaflnyNTKGTPLVHSLKISN----- 184
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV------TTTANPFYTPAEIAKqakas 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 185 -----ITQ------------------VFIDPDASNPIRESE--EEIKNALPDVKLnyleeqdlmhellnsqSPEflqqDN 239
Cdd:PLN02246 122 gakliITQscyvdklkglaeddgvtvVTIDDPPEGCLHFSEltQADENELPEVEI----------------SPD----DV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 240 VRTPlgltdfkpsmliYTSGTTGLPKSAIMSWRK--SSVGCQVFGHV--LHMTNESTVFTAMPLFH--STAALLgACAiL 313
Cdd:PLN02246 182 VALP------------YSSGTTGLPKGVMLTHKGlvTSVAQQVDGENpnLYFHSDDVILCVLPMFHiySLNSVL-LCG-L 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 314 SHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYgNGLRP---DIWQDFRKRFNIEV 390
Cdd:PLN02246 248 RVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVL-SGAAPlgkELEDAFRAKLPNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 391 IGEFYAATEA-PFATTT--FQKGDFGI--GACrnyGTIIQwflsfQQTLVRMDPNDDSVIYRNskgfcevapvgEPGEML 465
Cdd:PLN02246 327 LGQGYGMTEAgPVLAMClaFAKEPFPVksGSC---GTVVR-----NAELKIVDPETGASLPRN-----------QPGEIC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 466 MRiffpkkPETSFQGYLGNAKETKSKVvrDVfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLT 545
Cdd:PLN02246 388 IR------GPQIMKGYLNDPEATANTI--DK----DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 546 ASNKEQYAQVlvvgikVPKYEGRAG-----FAV----IKLTDNSL-DITAKTKLLNDSLSRlnlpsyamplfVKFVDEIK 615
Cdd:PLN02246 456 SHPSIADAAV------VPMKDEVAGevpvaFVVrsngSEITEDEIkQFVAKQVVFYKRIHK-----------VFFVDSIP 518
|
570 580
....*....|....*....|
gi 41629676 616 MTDNHKILKKVYREqKLPKG 635
Cdd:PLN02246 519 KAPSGKILRKDLRA-KLAAG 537
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
226-546 |
1.15e-07 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 54.58 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 226 LLNSQSPEFLQQDNVRTPLGLTDFKPSML---IYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPL-F- 300
Cdd:TIGR01733 94 ILLDPLELAALDDAPAPPPPDAPSGPDDLayvIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLsFd 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 301 HSTAALLGAcaiLSHGGCLAL------SHKFSASTFWKQVYltGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAyGNGL 374
Cdd:TIGR01733 174 ASVEEIFGA---LLAGATLVVppedeeRDDAALLAALIAEH--PVTVLNLTPSLLALLAAALPPALASLRLVILG-GEAL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 375 RPDIWQDFRKRF-NIEVIGEfYAATEAPFATTTFqkgDFGIGACRNYGTI-IQWFLSFQQTLVRmDPNDdsviyrnskgf 452
Cdd:TIGR01733 248 TPALVDRWRARGpGARLINL-YGPTETTVWSTAT---LVDPDDAPRESPVpIGRPLANTRLYVL-DDDL----------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 453 cEVAPVGEPGEM------LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFR--RGDAWYRCGDLLKADEYGLWYFLDRM 524
Cdd:TIGR01733 312 -RPVPVGVVGELyiggpgVAR------------GYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
330 340
....*....|....*....|....*...
gi 41629676 525 gDT------FRwksenVSTTEVEDQLTA 546
Cdd:TIGR01733 379 -DDqvkirgYR-----IELGEIEAALLR 400
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
251-630 |
1.24e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 54.70 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKS---AIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAIlSHGGCLALSHKFSA 327
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAG-RLGGVLVLQPRFDP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 328 STFWKQVYLTGATHIQYVGEVCRYLLHTPiskyekmHKVKVAYG-NGLR----------PDIwqdfrKRFNIE----VIG 392
Cdd:PRK12406 233 EELLQLIERHRITHMHMVPTMFIRLLKLP-------EEVRAKYDvSSLRhvihaaapcpADV-----KRAMIEwwgpVIY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 393 EFYAATEApfATTTFQKGDfgiGACRNYGTIIQwfLSFQQTLVRMDPNDDSViyrnskgfcevaPVGEPGEMLMRIffPK 472
Cdd:PRK12406 301 EYYGSTES--GAVTFATSE---DALSHPGTVGK--AAPGAELRFVDEDGRPL------------PQGEIGEIYSRI--AG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 473 KPETSFQgylgNAKETKSKVVRdvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQY 552
Cdd:PRK12406 360 NPDFTYH----NKPEKRAEIDR------GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAV--PGV 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41629676 553 AQVLVVGIKVPKYeGRAGFAVIKLTDN-SLDITAKTKLLNDSLSRlnlpsYAMPLFVKFVDEIKMTDNHKILKKVYREQ 630
Cdd:PRK12406 428 HDCAVFGIPDAEF-GEALMAVVEPQPGaTLDEADIRAQLKARLAG-----YKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
90-629 |
1.48e-07 |
|
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: 54.23 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 90 GDHLAISYtrpmaekGEFQletFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNY 169
Cdd:cd12118 18 PDRTSIVY-------GDRR---YTWRQTYDRCRRLASALA-ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 170 NTKGTPLVHSLKISNITQVFIDpdasnpiRESEEEiknalpdvklnyleeqdlmhELLNSQSPEFLQQdnvrTPLGltDF 249
Cdd:cd12118 87 RLDAEEIAFILRHSEAKVLFVD-------REFEYE--------------------DLLAEGDPDFEWI----PPAD--EW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 250 KPSMLIYTSGTTGLPKSAIMSWRkssvGC--QVFGHVLH--MTNESTVFTAMPLFHSTaallGAC---AILSHGG---CL 319
Cdd:cd12118 134 DPIALNYTSGTTGRPKGVVYHHR----GAylNALANILEweMKQHPVYLWTLPMFHCN----GWCfpwTVAAVGGtnvCL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 320 alsHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKM-HKVKVAYGNGLRPdiwqdFRKRFNIEVIG----EF 394
Cdd:cd12118 206 ---RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLpHRVHVMTAGAPPP-----AAVLAKMEELGfdvtHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 395 YAATEA--PFATTTFQKGDFGIGACRNYGtiiqwfLSFQQTlVRM---------DPNDDSVIYRNSKGFCEVAPVGEpge 463
Cdd:cd12118 278 YGLTETygPATVCAWKPEWDELPTEERAR------LKARQG-VRYvgleevdvlDPETMKPVPRDGKTIGEIVFRGN--- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 464 MLMRiffpkkpetsfqGYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQ 543
Cdd:cd12118 348 IVMK------------GYLKNPEAT-----AEAFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 544 LTAsnkeqYAQVL---VVGIKVPKYeGRAGFAVIKLTDNSL----DITAktkllndsLSRLNLPSYAMPLFVKFvDEIKM 616
Cdd:cd12118 409 LYK-----HPAVLeaaVVARPDEKW-GEVPCAFVELKEGAKvteeEIIA--------FCREHLAGFMVPKTVVF-GELPK 473
|
570
....*....|...
gi 41629676 617 TDNHKILKKVYRE 629
Cdd:cd12118 474 TSTGKIQKFVLRD 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-546 |
1.98e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 53.64 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 256 YTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALS------HKFSAST 329
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyrNPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 330 FWKQVYLTGATHIQYVGEVCRYLLHTPISKyeKMHKVKVAYGNG--LRPDIWQDFRKRFNIEVIgEFYAATEAPFATT-T 406
Cdd:cd05944 89 FWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAapLPVELRARFEDATGLPVV-EGYGLTEATCLVAvN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 407 FQKGDFGIGACRnygtiiqwfLSFQQTLVRMDPNDDSVIYRNSKGfcevapVGEPGEMLMriffpkKPETSFQGYLGNAK 486
Cdd:cd05944 166 PPDGPKRPGSVG---------LRLPYARVRIKVLDGVGRLLRDCA------PDEVGEICV------AGPGVFGGYLYTEG 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 487 EtkskvvRDVFrRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTA 546
Cdd:cd05944 225 N------KNAF-VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
92-636 |
2.89e-07 |
|
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: 53.65 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 92 HLAISYTRP----MAEKGEfqLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAI--PA 165
Cdd:cd05968 70 WLADTRTRPalrwEGEDGT--SRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIvvPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 166 FLNYNTKgtPLVHSLKISN----ITQ-VFIDPDASNPIRESEEEIKNALPDVK----LNYLEEQDLMHELLNSQSPEFLQ 236
Cdd:cd05968 147 FSGFGKE--AAATRLQDAEakalITAdGFTRRGREVNLKEEADKACAQCPTVEkvvvVRHLGNDFTPAKGRDLSYDEEKE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 237 QDNVRTPLGLTDfKPSMLIYTSGTTGLPKSAIMSWRKSSV-GCQVFGHVLHMTNESTV--FTAM-----PLFHSTAALLG 308
Cdd:cd05968 225 TAGDGAERTESE-DPLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLtwFTDLgwmmgPWLIFGGLILG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 309 ACAILSHGgclALSHKfSASTFWKQVYLTGATHIQYVGEVCRYLL---HTPISKYEKMhKVKVAYGNG--LRPDIWqdfr 383
Cdd:cd05968 304 ATMVLYDG---APDHP-KADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLS-SLRVLGSTGepWNPEPW---- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 384 kRFNIEVIGEfyaaTEAPFAT----TTFQKGDFG------IGACrnygtiiqwflSFQQTLVRMDPN--DDsviyrnskg 451
Cdd:cd05968 375 -NWLFETVGK----GRNPIINysggTEISGGILGnvlikpIKPS-----------SFNGPVPGMKADvlDE--------- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 452 fcEVAPV-GEPGEMLMRIFFPKKPetsfQGYLGNAKetksKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRW 530
Cdd:cd05968 430 --SGKPArPEVGELVLLAPWPGMT----RGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 531 KSENVSTTEVEDQLTASNKEQYAQvlVVGIKVP-KYEGRAGFAVIKLTDNSLDITAKtKLLNDSLSRLNLPsyAMPLFVK 609
Cdd:cd05968 500 AGKRVGPAEIESVLNAHPAVLESA--AIGVPHPvKGEAIVCFVVLKPGVTPTEALAE-ELMERVADELGKP--LSPERIL 574
|
570 580
....*....|....*....|....*..
gi 41629676 610 FVDEIKMTDNHKILKKVYREQKLPKGL 636
Cdd:cd05968 575 FVKDLPKTRNAKVMRRVIRAAYLGKEL 601
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
217-634 |
3.87e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 217 LEEQDLMHELLNSQSPEFLQQDNvrTPLGLTDFKPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTA 296
Cdd:PRK12316 3166 LPLAQGVQVLDLDRGDENYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF 3243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 297 MPlFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYL---TGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNG 373
Cdd:PRK12316 3244 TT-FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELinsEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEA 3322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 374 LRPDIWQdfrKRFNIEVIGEFYAATEAPFATTTFQKGDFGIGacrnygtiiqwflsfQQTLVRMDPNDDSVIYRNSkgfC 453
Cdd:PRK12316 3323 LPADLQQ---QVFAGLPLYNLYGPTEATITVTHWQCVEEGKD---------------AVPIGRPIANRACYILDGS---L 3381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 454 EVAPVGEPGEMLMriffpkKPETSFQGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSE 533
Cdd:PRK12316 3382 EPVPVGALGELYL------GGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGF 3455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 534 NVSTTEVEDQLTASNKEQYAQVLVVgikvpkyEGRAGFAVIKLTDNSldiTAKTKLLNDSLsRLNLPSYAMPLFVKFVDE 613
Cdd:PRK12316 3456 RIELGEIEARLLEHPWVREAVVLAV-------DGRQLVAYVVPEDEA---GDLREALKAHL-KASLPEYMVPAHLLFLER 3524
|
410 420
....*....|....*....|.
gi 41629676 614 IKMTDNHKILKKVyreqkLPK 634
Cdd:PRK12316 3525 MPLTPNGKLDRKA-----LPR 3540
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
435-630 |
5.94e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 52.44 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 435 VRM-DPNDDSViyrnskgfcevAPVGEPGEMLMRiffpkKPeTSFQGYLGNAKETkskvvRDVFRRgDAWYRCGDLLKAD 513
Cdd:PRK06164 361 VRArDPQDGAL-----------LPDGESGEIEIR-----AP-SLMRGYLDNPDAT-----ARALTD-DGYFRTGDLGYTR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 514 EYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQvlVVGIKVPKYEGRAGFaVIKLTDNSLDITAKTKLLNDS 593
Cdd:PRK06164 418 GDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ--VVGATRDGKTVPVAF-VIPTDGASPDEAGLMAACREA 494
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41629676 594 LSrlnlpSYAMPLFVKFVDEIKMTDN---HKILKKVYREQ 630
Cdd:PRK06164 495 LA-----GFKVPARVQVVEAFPVTESangAKIQKHRLREM 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
113-633 |
7.53e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.45 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 113 TYIETYNIVLRLSHILHFDyNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNyntkgtPLVHSLKISNITQ----- 187
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVN------PRLFPEQIAWIINhaedr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 188 -VFIDPDASnPIRESeeeIKNALPDVKLnYLEEQDLMH----ELLNSQS-PEFLQQDNvrtplglTDFKPSM-------- 253
Cdd:PRK06018 114 vVITDLTFV-PILEK---IADKLPSVER-YVVLTDAAHmpqtTLKNAVAyEEWIAEAD-------GDFAWKTfdentaag 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 254 LIYTSGTTGLPKSAIMSWRKSSVGCQVF--GHVLHMTNESTVFTAMPLFHSTAALLGacailshggclalshkFSASTFW 331
Cdd:PRK06018 182 MCYTSGTTGDPKGVLYSHRSNVLHALMAnnGDALGTSAADTMLPVVPLFHANSWGIA----------------FSAPSMG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 332 KQVYLTGAthiQYVGEvcryllhtpiSKYEKMHKVKVAYGNGLrPDIW----QDFRK------RFNIEVIGefyaATEAP 401
Cdd:PRK06018 246 TKLVMPGA---KLDGA----------SVYELLDTEKVTFTAGV-PTVWlmllQYMEKeglklpHLKMVVCG----GSAMP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 402 FAT-TTFQKGD------FGIGACRNYGTIIQWFLSFQQTlvrmdPNDDSVIYRNSKGFcevAPVGepgeMLMRIFFPKKP 474
Cdd:PRK06018 308 RSMiKAFEDMGvevrhaWGMTEMSPLGTLAALKPPFSKL-----PGDARLDVLQKQGY---PPFG----VEMKITDDAGK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 475 ETSFQG-YLGNAKETKSKVVRDVFRRG------DAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDqlTAS 547
Cdd:PRK06018 376 ELPWDGkTFGRLKVRGPAVAAAYYRVDgeilddDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN--LAV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 548 NKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAKTKLLNDSLSRlnlpsYAMPLFVKFVDEIKMTDNHKILKKVY 627
Cdd:PRK06018 454 GHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAK-----WWMPDDVAFVDAIPHTATGKILKTAL 528
|
570
....*....|
gi 41629676 628 REQ----KLP 633
Cdd:PRK06018 529 REQfkdyKLP 538
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
439-625 |
8.02e-07 |
|
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: 51.79 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 439 PNDDSVIYRNSKGFcEVAPVGEPGEMLMriffpkKPETSFQGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLW 518
Cdd:cd17645 267 PIDNTRVYILDEAL-QLQPIGVAGELCI------AGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNI 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 519 YFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVLVVGIKvpkyEGRAGFAVIKLTDNSLDITAKTKLLNDSlsrln 598
Cdd:cd17645 340 EFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA----DGRKYLVAYVTAPEEIPHEELREWLKND----- 410
|
170 180
....*....|....*....|....*..
gi 41629676 599 LPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd17645 411 LPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
454-625 |
1.26e-06 |
|
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: 51.56 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 454 EVAPvGEPGEMLMRiffpkKPETsFQGYLgNAKETKSKVVRDvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSE 533
Cdd:cd05920 329 PVPP-GEEGELLTR-----GPYT-IRGYY-RAPEHNARAFTP-----DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 534 NVSTTEVEDQLTASNKEQYAqvLVVGIKVPkYEGRAGFAVIKLTDNSLDITAktklLNDSLSRLNLPSYAMPLFVKFVDE 613
Cdd:cd05920 396 KIAAEEVENLLLRHPAVHDA--AVVAMPDE-LLGERSCAFVVLRDPPPSAAQ----LRRFLRERGLAAYKLPDRIEFVDS 468
|
170
....*....|..
gi 41629676 614 IKMTDNHKILKK 625
Cdd:cd05920 469 LPLTAVGKIDKK 480
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
251-622 |
1.76e-06 |
|
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: 50.93 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKssvgcqvFGHVLHMTNESTVFTAMPLFHSTAALLGA-------CAILSHGGCLAL-- 321
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRN-------VAHAAHAWRREYELDSFPVRLLQMASFSFdvfagdfARSLLNGGTLVIcp 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 322 -SHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKV-AYGNGLRPDIW-QDFRKRFNIE-VIGEFYAA 397
Cdd:cd17650 168 dEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLlIVGSDGCKAQDfKTLAARFGQGmRIINSYGV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 398 TEAPFATTTFQKGDFGIGACRNygTIIQWFLSfQQTLVRMDPNDDSViyrnskgfcevaPVGEPGEMLMriffpkKPETS 477
Cdd:cd17650 248 TEATIDSTYYEEGRDPLGDSAN--VPIGRPLP-NTAMYVLDERLQPQ------------PVGVAGELYI------GGAGV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 478 FQGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAqvlV 557
Cdd:cd17650 307 ARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEA---V 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41629676 558 VGIKVPKyEGRAGFAVIKLTDNSLDITAKTKLLNDSLSRLNLPSYAMPLfvkfvDEIKMTDNHKI 622
Cdd:cd17650 384 VAVREDK-GGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQL-----DALPLTPNGKV 442
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
454-630 |
7.62e-06 |
|
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: 48.99 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 454 EVAPvGEPGEMLMRiffpkKPETsFQGYLGNAKETkskvvRDVFRRgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSE 533
Cdd:COG1021 374 PVPP-GEVGELLTR-----GPYT-IRGYYRAPEHN-----ARAFTP-DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 534 NVSTTEVEDQLTAsnKEQYAQVLVVGikVP-KYEGRAGFAVIKLTDNSLDITAktklLNDSLSRLNLPSYAMPLFVKFVD 612
Cdd:COG1021 441 KIAAEEVENLLLA--HPAVHDAAVVA--MPdEYLGERSCAFVVPRGEPLTLAE----LRRFLRERGLAAFKLPDRLEFVD 512
|
170
....*....|....*...
gi 41629676 613 EIKMTDNHKILKKVYREQ 630
Cdd:COG1021 513 ALPLTAVGKIDKKALRAA 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
455-622 |
3.45e-05 |
|
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: 46.81 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 455 VAPVGEPGEM------LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDT- 527
Cdd:cd12117 326 PVPPGVPGELyvggdgLAL------------GYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQv 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 528 ----FRwksenVSTTEVEDQLTAsnkeqyaqvlvvgikvpkYEGRAGFAVIKLTDNSLD------ITAKTKL----LNDS 593
Cdd:cd12117 394 kirgFR-----IELGEIEAALRA------------------HPGVREAVVVVREDAGGDkrlvayVVAEGALdaaeLRAF 450
|
170 180
....*....|....*....|....*....
gi 41629676 594 LSRlNLPSYAMPLFVKFVDEIKMTDNHKI 622
Cdd:cd12117 451 LRE-RLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-629 |
4.14e-05 |
|
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: 46.66 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 112 FTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFID 191
Cdd:cd05915 25 TTYAEVYQRARRLMGGLR-ALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 192 PDASNPIRESEEEIKNAL--PDVKLNYLEEQDLmhelLNSQSPEFlqqDNVRtPLGLTDfkPSMLIYTSGTTGLPKSAIM 269
Cdd:cd05915 104 PNLLPLVEAIRGELKTVQhfVVMDEKAPEGYLA----YEEALGEE---ADPV-RVPERA--ACGMAYTTGTTGLPKGVVY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 270 SWRKSSVGCQVFGHVLHMTNE--STVFTAMPLFHSTaallGAC---AILSHGGCLA-LSHKFSASTFWKQVYLTGATHIQ 343
Cdd:cd05915 174 SHRALVLHSLAASLVDGTALSekDVVLPVVPMFHVN----AWClpyAATLVGAKQVlPGPRLDPASLVELFDGEGVTFTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 344 YVGEVCRYLLHTPIS-KYEKMHKVKVAYGNGLRPDIWQDFRKrfnievIGEFYAATEapfatttfqkgdFGIGACRNYGT 422
Cdd:cd05915 250 GVPTVWLALADYLEStGHRLKTLRRLVVGGSAAPRSLIARFE------RMGVEVRQG------------YGLTETSPVVV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 423 IIQWFLSFqQTLvrmdPNDDSVIYRNSKG---FCEVAPVGEPGEM-------LMRIfFPKKPETSFQGYLGNAKETKSkv 492
Cdd:cd05915 312 QNFVKSHL-ESL----SEEEKLTLKAKTGlpiPLVRLRVADEEGRpvpkdgkALGE-VQLKGPWITGGYYGNEEATRS-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 493 vrDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTaSNKEQYaQVLVVGiKVPKYEGRAGFA 572
Cdd:cd05915 384 --ALTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALM-GHPKVK-EAAVVA-IPHPKWQERPLA 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 41629676 573 VIKLTDNSLDITAKTKLLNDSLSRLNLpsyaMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:cd05915 457 VVVPRGEKPTPEELNEHLLKAGFAKWQ----LPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
111-341 |
4.85e-05 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 46.31 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 111 TFTYIETYNIVLRLSHIL--HFDYNVQAgdyVAIDCTNKPLFVFLWLSLWNIGAipAFLnyntkgtplvhslkisnitqv 188
Cdd:cd17654 16 TVSYADLAEKISNLSNFLrkKFQTEERA---IGLRCDRGTESPVAILAILFLGA--AYA--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 189 FIDPDASnpiresEEEIKNALPDVKLNYLEEQDLMHELLNSQSPEfLQQDNVRTPLGLtdfkpSMLIYTSGTTGLPKSAI 268
Cdd:cd17654 70 PIDPASP------EQRSLTVMKKCHVSYLLQNKELDNAPLSFTPE-HRHFNIRTDECL-----AYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 269 MSWRKSSVGCQVFGHVLHMTNESTVFTAMPL-FH------STAALLGACAILSHGGCLALSHKFSASTF-WKQVYLTGAT 340
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSEDILFLTSPLtFDpsvveiFLSLSSGATLLIVPTSVKVLPSKLADILFkRHRITVLQAT 217
|
.
gi 41629676 341 H 341
Cdd:cd17654 218 P 218
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
454-622 |
5.45e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 46.11 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 454 EVAPVGEPGEM------LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDT 527
Cdd:cd17646 327 RPVPVGVPGELylggvqLAR------------GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 528 FRWKSENVSTTEVEDQLTASnkEQYAQVLVVGIKVPKYEGR-AGFAVIKLTDNSLDITAktklLNDSLSRLnLPSYAMPL 606
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAH--PAVTHAVVVARAAPAGAARlVGYVVPAAGAAGPDTAA----LRAHLAER-LPEYMVPA 467
|
170
....*....|....*.
gi 41629676 607 FVKFVDEIKMTDNHKI 622
Cdd:cd17646 468 AFVVLDALPLTANGKL 483
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
457-634 |
5.53e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 46.29 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 457 PVGEPGEMLMriffpKKPETsFQGYLGNAKETkSKVVRDvfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVS 536
Cdd:PRK05677 400 PLGEVGELCV-----KGPQV-MKGYWQRPEAT-DEILDS-----DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVY 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 537 TTEVEDQLTAsnKEQYAQVLVVGIKVPKY-EGRAGFAVIKLTDNsldITAKTKLlndSLSRLNLPSYAMPLFVKFVDEIK 615
Cdd:PRK05677 468 PNELEDVLAA--LPGVLQCAAIGVPDEKSgEAIKVFVVVKPGET---LTKEQVM---EHMRANLTGYKVPKAVEFRDELP 539
|
170
....*....|....*....
gi 41629676 616 MTDNHKILKKVYREQKLPK 634
Cdd:PRK05677 540 TTNVGKILRRELRDEELKK 558
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
251-326 |
1.13e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 44.98 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFS 326
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPT 205
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
457-622 |
1.93e-04 |
|
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: 44.59 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 457 PVGEPGEMLMriffpKKPETSfQGYLGNAKETKSKVVRDVFRRGDA-WYRCGDLLKADEYGLWYFLDRMGDTFRWKSENV 535
Cdd:cd12116 313 PPGVPGELYI-----GGDGVA-QGYLGRPALTAERFVPDPFAGPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 536 STTEVEDQLTASNkeQYAQVLVVGIKVPKYEGRAGFAVIKlTDNSLDITAKTKLLNDSLSRLNLPSYAMPLfvkfvDEIK 615
Cdd:cd12116 387 ELGEIEAALAAHP--GVAQAAVVVREDGGDRRLVAYVVLK-AGAAPDAAALRAHLRATLPAYMVPSAFVRL-----DALP 458
|
....*..
gi 41629676 616 MTDNHKI 622
Cdd:cd12116 459 LTANGKL 465
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
104-313 |
3.62e-04 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 43.50 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 104 KGEFQLETFTYIETYNIVLRLSHILHfDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPaflnyntkgTPLV-----H 178
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVL---------NPLMpifreR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 179 SL---------KISNITQVFIDPDASNPIREseeeIKNALPDVKLNYL---EEQDLMHELLnsQSPEFLQQDnvRTPLGL 246
Cdd:PRK13295 118 ELsfmlkhaesKVLVVPKTFRGFDHAAMARR----LRPELPALRHVVVvggDGADSFEALL--ITPAWEQEP--DAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 247 TDFKPS-----MLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHST--------AALLGACAIL 313
Cdd:PRK13295 190 ARLRPGpddvtQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTgfmyglmmPVMLGATAVL 269
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
108-303 |
5.36e-04 |
|
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: 43.23 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 108 QLETFTYIETYNIVLRL-SHILHFdyNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAI--PAF--LNYNTKGTPLVHS-LK 181
Cdd:cd05932 3 QVVEFTWGEVADKARRLaAALRAL--GLEPGSKIALISKNCAEWFITDLAIWMAGHIsvPLYptLNPDTIRYVLEHSeSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 182 ISNITQVFIDPDASNPIRESEEEIKNALPDVKLNYLEEQDLmhelLNSQSPefLQQDNVRTPLGLtdfkpSMLIYTSGTT 261
Cdd:cd05932 81 ALFVGKLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDL----IAQHPP--LEERPTRFPEQL-----ATLIYTSGTT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 41629676 262 GLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHST 303
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVT 191
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
483-629 |
5.62e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 43.23 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 483 GNAKETKSKVVRDVFRR--GDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASnkEQYAQVLVVGI 560
Cdd:PRK05620 409 GAASTFRGEDVEDANDRftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA--PEVVECAVIGY 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 561 KVPKYeGRAGFAVIKLTDNsLDITAKT-KLLNDSLsRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYRE 629
Cdd:PRK05620 487 PDDKW-GERPLAVTVLAPG-IEPTRETaERLRDQL-RDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
456-630 |
5.68e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 43.01 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 456 APVGEPGEMLMRIFFpkKPETSFQGYLGNAKETkskvvRDVFRRGdaWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENV 535
Cdd:PRK08162 379 QPVPADGETIGEIMF--RGNIVMKGYLKNPKAT-----EEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENI 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 536 STTEVEDQLTasnkeQYAQVL---VVGIKVPKYeGRAGFAVIKLTDNSL----DITAktkllndsLSRLNLPSYAMPLFV 608
Cdd:PRK08162 450 SSIEVEDVLY-----RHPAVLvaaVVAKPDPKW-GEVPCAFVELKDGASateeEIIA--------HCREHLAGFKVPKAV 515
|
170 180
....*....|....*....|..
gi 41629676 609 KFvDEIKMTDNHKILKKVYREQ 630
Cdd:PRK08162 516 VF-GELPKTSTGKIQKFVLREQ 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
251-622 |
6.38e-04 |
|
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: 42.72 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 251 PSMLIYTSGTTGLPKSAIMSWRksSVGCQVFGH--VLHMTNES-TVFTAMPLFH-STAALLGAcaiLSHGGCLAL---SH 323
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPHR--SLANLVAWQarASSLGPGArTLQFAGLGFDvSVQEIFST---LCAGATLVLppeEV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 324 KFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPiskyekmhKVKVAYGNGLR------------PDI-----WQDFRKRF 386
Cdd:cd17651 213 RTDPPALAAWLDEQRISRVFLPTVALRALAEHG--------RPLGVRLAALRylltggeqlvltEDLrefcaGLPGLRLH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 387 NievigeFYAATEAPFATTTFQKGDFG-------IGAcrnygtiiqwflsfqqtlvrmdPNDDSVIYRnSKGFCEVAPVG 459
Cdd:cd17651 285 N------HYGPTETHVVTALSLPGDPAawpapppIGR----------------------PIDNTRVYV-LDAALRPVPPG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 460 EPGEM------LMRiffpkkpetsfqGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSE 533
Cdd:cd17651 336 VPGELyiggagLAR------------GYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGF 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 534 NVSTTEVEDQLtasnkeqYAQVLVVGIKVPKYEGRAG----FAVIKLTDNSLDITAKtklLNDSLSRLnLPSYAMPLFVK 609
Cdd:cd17651 404 RIELGEIEAAL-------ARHPGVREAVVLAREDRPGekrlVAYVVGDPEAPVDAAE---LRAALATH-LPEYMVPSAFV 472
|
410
....*....|...
gi 41629676 610 FVDEIKMTDNHKI 622
Cdd:cd17651 473 LLDALPLTPNGKL 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
453-630 |
6.64e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 42.88 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 453 CEVAPVGEPGEMLMRIFfpkkpeTSFQGYLGNAKETKSkvVRDVfrrgDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKS 532
Cdd:PRK08315 390 GETVPRGEQGELCTRGY------SVMKGYWNDPEKTAE--AIDA----DGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGG 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 533 ENVSTTEVEDQLTASNKEQYAQVlvVGIKVPKYeGRAGFAVIKLTDNSlDITAK--TKLLNDSLSRLNLPSYamplfVKF 610
Cdd:PRK08315 458 ENIYPREIEEFLYTHPKIQDVQV--VGVPDEKY-GEEVCAWIILRPGA-TLTEEdvRDFCRGKIAHYKIPRY-----IRF 528
|
170 180
....*....|....*....|
gi 41629676 611 VDEIKMTDNHKILKKVYREQ 630
Cdd:PRK08315 529 VDEFPMTVTGKIQKFKMREM 548
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
155-307 |
7.37e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 43.03 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 155 LSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFidpdASNPIRES---EEEIKNALPDVKLNYLEE-------QDLMH 224
Cdd:PRK06814 700 FALQSAGRVPAMINFSAGIANILSACKAAQVKTVL----TSRAFIEKarlGPLIEALEFGIRIIYLEDvraqiglADKIK 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 225 ELLNSQSPEFlqQDNVRTPLgltdfKPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHS-- 302
Cdd:PRK06814 776 GLLAGRFPLV--YFCNRDPD-----DPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSfg 848
|
....*.
gi 41629676 303 -TAALL 307
Cdd:PRK06814 849 lTGGLV 854
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
479-633 |
8.49e-04 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 42.46 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 479 QGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVLVV 558
Cdd:cd17656 339 RGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDK 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41629676 559 GIKVPKYEGRAGF-AVIKLTDNSLditaKTKLLNDslsrlnLPSYAMPLFVKFVDEIKMTDNHKILKKvyreqKLP 633
Cdd:cd17656 419 ADDKGEKYLCAYFvMEQELNISQL----REYLAKQ------LPEYMIPSFFVPLDQLPLTPNGKVDRK-----ALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
479-625 |
1.08e-03 |
|
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: 41.87 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 479 QGYLGNAKETKSKVVRDvfRRGDAWYRCGDL--LKADeyGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVL 556
Cdd:cd12114 338 LGYLGDPELTAARFVTH--PDGERLYRTGDLgrYRPD--GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41629676 557 VVGIKVPKyeGRAGFAVIKLTDNSLDITAKTKLLNDSlsrlnLPSYAMPLFVKFVDEIKMTDNHKILKK 625
Cdd:cd12114 414 VLGDPGGK--RLAAFVVPDNDGTPIAPDALRAFLAQT-----LPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
203-318 |
1.97e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 41.19 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 203 EEIKNALPdvklNYLEEQDLMhELLNSQSPEflQQDNVrtplgLTDFKPS---MLIYTSGTTGLPKSAIMS-----WRKS 274
Cdd:cd05933 113 EPLKEKEP----NLYSWDEFM-ELGRSIPDE--QLDAI-----ISSQKPNqccTLIYTSGTTGMPKGVMLShdnitWTAK 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41629676 275 SVGcQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGC 318
Cdd:cd05933 181 AAS-QHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQ 223
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
457-629 |
2.34e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 40.96 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 457 PVGEPGEMLMriffpKKPETsFQGYLgNAKETKSKVVRdvfrrGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVS 536
Cdd:PRK12492 408 PLGERGELCI-----KGPQV-MKGYW-QQPEATAEALD-----AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 537 TTEVEDQLTASNKeqYAQVLVVGikVPkyEGRAGFAViKLTDNSLDITAKTKLLNdSLSRLNLPSYAMPLFVKFVDEIKM 616
Cdd:PRK12492 476 PNEIEDVVMAHPK--VANCAAIG--VP--DERSGEAV-KLFVVARDPGLSVEELK-AYCKENFTGYKVPKHIVLRDSLPM 547
|
170
....*....|...
gi 41629676 617 TDNHKILKKVYRE 629
Cdd:PRK12492 548 TPVGKILRRELRD 560
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
539-621 |
9.17e-03 |
|
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: 35.60 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 539 EVEDQLTASnkEQYAQVLVVGIKVPKyEGRAGFAVIKLTDNSLDITAKtklLNDSLSRlNLPSYAMPLFVKFVDEIKMTD 618
Cdd:pfam13193 1 EVESALVSH--PAVAEAAVVGVPDEL-KGEAPVAFVVLKPGVELLEEE---LVAHVRE-ELGPYAVPKEVVFVDELPKTR 73
|
...
gi 41629676 619 NHK 621
Cdd:pfam13193 74 SGK 76
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
256-319 |
9.30e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 39.02 E-value: 9.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 256 YTSGTTGLPKSAIMSWRK-----SSVG-CQVFghvlhmTNESTVFTAMPLFHSTAALLGACAILSHGGCL 319
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNilnngYFIGeAMKL------TEEDRLCIPVPLYHCFGMVLGNLACVTHGATM 269
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
250-324 |
9.98e-03 |
|
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: 39.12 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41629676 250 KPSML---IYTSGTTGLPKSAIMSWRK---SSVGCQVFGHVLHMTNESTV-FTAMPLFHSTAALLgACAILSHGGCLALS 322
Cdd:cd05927 112 KPEDLatiCYTSGTTGNPKGVMLTHGNivsNVAGVFKILEILNKINPTDVyISYLPLAHIFERVV-EALFLYHGAKIGFY 190
|
..
gi 41629676 323 HK 324
Cdd:cd05927 191 SG 192
|
|
| |
