|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
101-611 |
0e+00 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 859.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 181 FggemvaavaevsghlgkslikfcsgdlgpegilpdtHLLDPLLKEASTAPLAQIPsKGMDDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05939 81 F------------------------------------NLLDPLLTQSSTEPPSQDD-VNFRDKLFYIYTSGTTGLPKAAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEI 340
Cdd:cd05939 124 IVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 341 CRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR 420
Cdd:cd05939 204 CRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 421 LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSVFSKGDSAYLSGDVLVMDELG 500
Cdd:cd05939 284 LIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDSAFLSGDVLVMDELG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 501 YMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYA 580
Cdd:cd05939 364 YLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYA 443
|
490 500 510
....*....|....*....|....*....|.
gi 38524616 581 RPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05939 444 RPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
42-644 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 681.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFR 121
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQS--ISYAELNARANRYAHWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLI 201
Cdd:PRK08279 81 ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 202 KFCSGDlgPEGILPDTHL-LDPLLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR-MAAFGHhAYRM 279
Cdd:PRK08279 161 LWVAGG--DTLDDPEGYEdLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKaMGGFGG-LLRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 280 QAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVR 359
Cdd:PRK08279 238 TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 360 LAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHvyPIRLVKVNEDTMELLRDAQGLC 439
Cdd:PRK08279 318 LMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRC 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 440 IPCQAGEPGLLVGQINqqdPLRRFDGYVSESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENV 519
Cdd:PRK08279 396 IKVKPGEVGLLIGRIT---DRGPFDGYTDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 520 STTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAA-VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFK 598
Cdd:PRK08279 473 ATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAiVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFK 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 38524616 599 IQKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAF 644
Cdd:PRK08279 553 YRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKF 598
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
101-611 |
0e+00 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 650.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 181 FggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05940 81 V------------------------------------------------------------DAALYIYTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEI 340
Cdd:cd05940 101 ISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 341 CRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR 420
Cdd:cd05940 181 CRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 421 LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINqqdPLRRFDGYVSESATSKKIAHSVFSKGDSAYLSGDVLVMDELG 500
Cdd:cd05940 261 LVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRIN---PLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 501 YMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSL-LDPNAIYQELQKVLAPY 579
Cdd:cd05940 338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEeFDLSALAAHLEKNLPGY 417
|
490 500 510
....*....|....*....|....*....|..
gi 38524616 580 ARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05940 418 ARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
101-636 |
0e+00 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 599.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAL 179
Cdd:cd05938 3 GETYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 180 IFGGEMVAAVAEVSGHLGKSLIK--FCSGDLGPEGIlpdTHLLDpLLKEASTAPLAQ---IPSKGMDDRLfYIYTSGTTG 254
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSvwYLSHTSNTEGV---ISLLD-KVDAASDEPVPAslrAHVTIKSPAL-YIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 255 LPKAAIVVHSRYYRMAAFgHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVV 334
Cdd:cd05938 158 LPKAARISHLRVLQCSGF-LSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 335 QYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILP 414
Cdd:cd05938 237 QYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 415 HVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPlrrFDGYV-SESATSKKIAHSVFSKGDSAYLSGDV 493
Cdd:cd05938 317 LLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSP---FLGYAgDKEQTEKKLLRDVFKKGDVYFNTGDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 494 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAV--ADPHSlLDPNAIYQE 571
Cdd:cd05938 394 LVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVklKPGHE-FDGKKLYQH 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 572 LQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVY 636
Cdd:cd05938 473 VREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
101-611 |
8.19e-138 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 411.06 E-value: 8.19e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAL 179
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 180 IfggemvaavaevsghlgkslikfcsgdlgpegilpdthlLDPllkeastaplaqipskgmDDRLFYIYTSGTTGLPKAA 259
Cdd:cd05937 83 I---------------------------------------VDP------------------DDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 260 IVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGE 339
Cdd:cd05937 106 AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 340 ICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANM---DGKVGSCGFNSRILPHV 416
Cdd:cd05937 186 LCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnvgDFGAGAIGHHGLIRRWK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 417 Y--PIRLVKVNEDTMELLRDAQ-GLCIPCQAGEPGLLVGQINqQDPLRRFDGYV-SESATSKKIAHSVFSKGDSAYLSGD 492
Cdd:cd05937 266 FenQVVLVKMDPETDDPIRDPKtGFCVRAPVGEPGEMLGRVP-FKNREAFQGYLhNEDATESKLVRDVFRKGDIYFRTGD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 493 VLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVA-DPHSLLDPNAIYQE 571
Cdd:cd05937 345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITlEESSAVPTEFTKSL 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 38524616 572 LQKV----LAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDP 611
Cdd:cd05937 425 LASLarknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
78-607 |
3.14e-89 |
|
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: 284.78 E-value: 3.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG--RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 158 LNVNLRREPLAFCLGTSGAKALIFggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqips 237
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 238 kgmddrLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKF 317
Cdd:COG0318 103 ------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 318 SASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRqIGEFYGATECNCS 395
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGVR-IVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IA-----NMDGKVGSCGfnsRILPHVyPIRLVkvnedtmellrDAQGlcIPCQAGEPGLLVGQINQQdplrrFDGYV-SE 469
Cdd:COG0318 256 VTvnpedPGERRPGSVG---RPLPGV-EVRIV-----------DEDG--RELPPGEVGEIVVRGPNV-----MKGYWnDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 470 SATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEG 549
Cdd:COG0318 314 EATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE-KWG 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 550 KAGMAAV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:COG0318 386 ERVVAFVvLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
101-605 |
2.17e-87 |
|
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: 279.18 E-value: 2.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI 180
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 181 fggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeASTAPLaqipskgmddrlfyIYTSGTTGLPKAAI 260
Cdd:cd05934 81 ----------------------------------------------VDPASI--------------LYTSGTTGPPKGVV 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEI 340
Cdd:cd05934 101 ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 341 CRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECNCSIAN---MDGKVGSCGfnsrilphvY 417
Cdd:cd05934 181 LSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVR-LLEGYGMTETIVGVIGprdEPRRPGSIG---------R 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 418 PIRLVKVnedtmeLLRDAQGLciPCQAGEPGLLVgqINQQDPLRRFDGYVS-ESATSKKIAHSVFSKGDSAYlsgdvlvM 496
Cdd:cd05934 251 PAPGYEV------RIVDDDGQ--ELPAGEPGELV--IRGLRGWGFFKGYYNmPEATAEAMRNGWFHTGDLGY-------R 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 497 DELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVL 576
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQL 393
|
490 500
....*....|....*....|....*....
gi 38524616 577 APYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05934 394 AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
74-617 |
3.35e-81 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 266.62 E-value: 3.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGGTR--WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 154 EAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfcsgDLGPEGiLPDTHLLDPLLKEASTAPLA 233
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--------------DPGDLP-LPAVWLLDAPASVSVPAGWS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 234 QIPSKGMD-----------DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHS-AGNIIGv 301
Cdd:PRK06155 162 TAPLPPLDapapaaavqpgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALNAFF- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 302 gQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVR 381
Cdd:PRK06155 241 -QALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 382 QIgEFYGATECNCSIANM--DGKVGSCGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVGQINQqdP 459
Cdd:PRK06155 320 LL-DGYGSTETNFVIAVThgSQRPGSMG---RLAPG-FEARVV-----------DEHDQELP--DGEPGELLLRADE--P 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 LRRFDGYVSESATskkiahSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:PRK06155 380 FAFATGYFGMPEK------TVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 540 YGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPrQTSDR 617
Cdd:PRK06155 454 FPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA-DTWDR 530
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-515 |
2.16e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 215.64 E-value: 2.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 82 FQAVVQRQPERLALVDaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:pfam00501 1 LERQAARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPegilPDTHLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDP----VLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKF 317
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHrnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 318 SA---SRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVR--LAVGNGLRPAIWEEFTERFGvRQIGEFYGATEC 392
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 393 NCSIANMD------GKVGSCGfnsRILPHVypiRLVKVNEDTMELLRDaqglcipcqaGEPG-LLVGQINQqdplrrFDG 465
Cdd:pfam00501 315 TGVVTTPLpldedlRSLGSVG---RPLPGT---EVKIVDDETGEPVPP----------GEPGeLCVRGPGV------MKG 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 38524616 466 YV-SESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 515
Cdd:pfam00501 373 YLnDPELTAEAF------DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
242-600 |
1.13e-61 |
|
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: 208.29 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRKKFSASR 321
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 322 FWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEFYGATECNCSIA-- 397
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 398 ---NMDGKVGSCGfnsRILPHVYpIRLVkvNEDTmellrdaqglcIPCQAGEPGLLVGQINQqdplrRFDGYVsesatsK 474
Cdd:cd04433 159 ppdDDARKPGSVG---RPVPGVE-VRIV--DPDG-----------GELPPGEIGELVVRGPS-----VMKGYW------N 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMA 554
Cdd:cd04433 211 NPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVA 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 38524616 555 AV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ 600
Cdd:cd04433 290 VVvLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
86-610 |
5.20e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 196.02 E-value: 5.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALvdaGTGEC-WTFAQLDAYSNAVANLFRQLGFAPGDV-VAIFLEGRPEFVgLWLGLAKAGmEAALLNVNLR 163
Cdd:PRK13388 11 DRAGDDTIAV---RYGDRtWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEML-FWLAAAALG-GYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 164 REplafclgtsgakalifGGEMVAAVAEVSGHL------GKSLIKfcsgDLGpegiLPDTHLLD---PLLKE--ASTAPL 232
Cdd:PRK13388 86 RR----------------GAALAADIRRADCQLlvtdaeHRPLLD----GLD----LPGVRVLDvdtPAYAElvAAAGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 233 AQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-----FGHHayrmqAADVLYDCLPLYHSAGNIIGVGQCLIY 307
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRalterFGLT-----RDDVCYVSMPLFHSNAVMAGWAPAVAS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 308 GLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVrQIGEFY 387
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGC-QVEDGY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 388 GATECNCSIANMDGK-VGSCGfnsRILPHVypirlVKVNEDTMEllrdaqgLCIPCQAGEPGLL------VGQINQQDPL 460
Cdd:PRK13388 296 GSSEGAVIVVREPGTpPGSIG---RGAPGV-----AIYNPETLT-------ECAVARFDAHGALlnadeaIGELVNTAGA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 461 RRFDGYVS-ESATSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:PRK13388 361 GFFEGYYNnPEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAV 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 540 YGVAVPGVeGKAGMAAV--ADPHSlLDPNAIYQEL--QKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFD 610
Cdd:PRK13388 434 YAVPDERV-GDQVMAALvlRDGAT-FDPDAFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWA 506
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
241-610 |
2.29e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 188.74 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 241 DDRLFYIYTSGTTGLPKAAIVVHSRYY---RMAA--FGHhayrmQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK 315
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVAsagVMLAqrFGL-----GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 316 KFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIgEFYGATECNCS 395
Cdd:PRK07867 227 KFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVV-DGFGSTEGGVA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IANM-DGKVGSCGfnsrilPHVYPIRLvkVNEDTMEllrdaqgLCIPCQAGEPGLL-----VGQ-INQQDPlRRFDGYVS 468
Cdd:PRK07867 306 ITRTpDTPPGALG------PLPPGVAI--VDPDTGT-------ECPPAEDADGRLLnadeaIGElVNTAGP-GGFEGYYN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 469 -ESATSKKIAHSVFSKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGV 547
Cdd:PRK07867 370 dPEADAERMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 548 eGKAGMAAVA-DPHSLLDPNAIYQEL--QKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFD 610
Cdd:PRK07867 443 -GDQVMAALVlAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
77-607 |
8.15e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 181.54 E-value: 8.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 77 TIPRIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGksLIKFC--SGDLGPEGILPDTHLLDPLLKEASTAPLAq 234
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLP--TVRTVivEGDGPAAPLAPEVGEYEELLAAASDTFDF- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 235 iPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniIGVG-QCLIYGLTVVL 313
Cdd:PRK06187 162 -PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLPyLALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 314 RKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIgEFYGATE 391
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFGIDLV-QGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 392 CnCSIA----------NMDGKVGSCGfnsRILPHVYpIRLvkVNEDTMELlrdaqglciPCQAGEPGLLV--GQINQQdp 459
Cdd:PRK06187 318 T-SPVVsvlppedqlpGQWTKRRSAG---RPLPGVE-ARI--VDDDGDEL---------PPDGGEVGEIIvrGPWLMQ-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 lrrfdGYVS-ESATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:PRK06187 380 -----GYWNrPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38524616 539 VYGVAVPgvegKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLqRE 607
Cdd:PRK06187 448 VIGVPDE----KWGERPVAvvvlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
86-615 |
1.61e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 175.69 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:COG0365 19 AEGRGDKVALIwegEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 163 RREPLAFCLGTSGAKALI------FGGEMV---AAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEAS-TAPL 232
Cdd:COG0365 99 GAEALADRIEDAEAKVLItadgglRGGKVIdlkEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASaEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 233 AQIPSkgmDDRLFYIYTSGTTGLPKAaiVVHS-RYY--RMAAFGHHAYRMQAADVLYdCLP----LYHsAGNIIgVGQcL 305
Cdd:COG0365 179 EPTDA---DDPLFILYTSGTTGKPKG--VVHThGGYlvHAATTAKYVLDLKPGDVFW-CTAdigwATG-HSYIV-YGP-L 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 306 IYGLTVVL---RKKF-SASRFWDDCIKYNCTVvqyigeIC------RYLLKQPVREAERRHRVRL----AVGNGLRPAIW 371
Cdd:COG0365 250 LNGATVVLyegRPDFpDPGRLWELIEKYGVTV------FFtaptaiRALMKAGDEPLKKYDLSSLrllgSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 372 EEFTERFGVrQIGEFYGATECNCSIAN----MDGKVGSCGFnsrilphvyPIRLVKVnedtmELLrDAQGlcIPCQAGEP 447
Cdd:COG0365 324 EWWYEAVGV-PIVDGWGQTETGGIFISnlpgLPVKPGSMGK---------PVPGYDV-----AVV-DEDG--NPVPPGEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 448 GLLVgqINQQDP--LRRF----DGYVSesatskkiahSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVST 521
Cdd:COG0365 386 GELV--IKGPWPgmFRGYwndpERYRE----------TYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 522 TEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA--VADPHSLLDPnAIYQELQ----KVLAPYARP---IFLRLLPqvd 592
Cdd:COG0365 454 AEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAfvVLKPGVEPSD-ELAKELQahvrEELGPYAYPreiEFVDELP--- 527
|
570 580
....*....|....*....|....*
gi 38524616 593 TTGTFKIQKTRLQR--EGFDPRQTS 615
Cdd:COG0365 528 KTRSGKIMRRLLRKiaEGRPLGDTS 552
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
75-605 |
2.05e-47 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 174.49 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 75 GHTIPRIFQAVVQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIfesSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 152 GMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGpEGILPDTHLLDPLLKEAStAP 231
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVA-LPADDGVSSFTQLKAQQP-AT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 232 LAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHsryYRMAAFGHHAY---RMQAADVLYDCLPLYHSAGNIIGVGQCLIYG 308
Cdd:PRK08008 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSAwqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 309 LTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVR-----LAVGNGLRpaiwEEFTERFGVRQI 383
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEERFGVRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEfYGATEcncSIAnmdGKVGSCGFNSRILPHV------YPIRlvkvnedtmelLRDAQGLCIP-------CQAGEPGLL 450
Cdd:PRK08008 317 TS-YGMTE---TIV---GIIGDRPGDKRRWPSIgrpgfcYEAE-----------IRDDHNRPLPageigeiCIKGVPGKT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 451 VGQINQQDPlrrfdgyvseSATSKKI-AHSVFSKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLS 529
Cdd:PRK08008 379 IFKEYYLDP----------KATAKVLeADGWLHTGDTGY-------VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 530 RLLGQTDVAVYGVAVPgVEGKAGMAAVA-DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK08008 442 THPKIQDIVVVGIKDS-IRDEAIKAFVVlNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
94-600 |
2.55e-46 |
|
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: 170.86 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 94 ALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGT 173
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 174 SGAKALIFGGEMVAAVAEVSGHLG-KSLIkFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKgmDDRLFYIYTSGT 252
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGpKDKI-IVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 253 TGLPKAAIVVHSRYYRMA--AFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGqCLIYGLTVVLRKKFSASRFWDDCIKYN 330
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLA-SLLNGATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 331 CTVVQYIGEICRYLLKQPVREAERRHRVR-LAVGNG-LRPAIWEEFTERFGVRQIGEFYGATECNCSIA---NMDGKVGS 405
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDKYDLSSLRvILSGGApLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 406 CGfnsRILPHVypiRLVKVNEDTMELLRDaqglcipcqaGEPG-LLV--GQInqqdplrrFDGYVS-ESATSKKIAHsvf 481
Cdd:cd05911 317 VG---RLLPNV---EAKIVDDDGKDSLGP----------NEPGeICVrgPQV--------MKGYYNnPEATKETFDE--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 482 skgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVA-DPH 560
Cdd:cd05911 370 ---DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVrKPG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 38524616 561 SLLDPNAIYQELQKVLAPY----ARPIFLRLLPQvdtTGTFKIQ 600
Cdd:cd05911 446 EKLTEKEVKDYVAKKVASYkqlrGGVVFVDEIPK---SASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-601 |
8.44e-45 |
|
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: 165.48 E-value: 8.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd17631 5 ARRHPDRTALVFGG--RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmDDRLF 245
Cdd:cd17631 83 EVAYILADSGAKVLF------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 246 YIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG-NIIGVGQcLIYGLTVVLRKKFSASRFWD 324
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGlGVFTLPT-LLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 325 DCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFtERFGVRqIGEFYGATECNCSIANMD-- 400
Cdd:cd17631 182 LIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGVK-FVQGYGMTETSPGVTFLSpe 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 401 ---GKVGSCGfnsRILPHVyPIRLVKVNEDtmellrdaqglciPCQAGEpgllVGQINQQDPLrRFDGYVS-ESATSKKI 476
Cdd:cd17631 260 dhrRKLGSAG---RPVFFV-EVRIVDPDGR-------------EVPPGE----VGEIVVRGPH-VMAGYWNrPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 477 AhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVE-GKAGMAA 555
Cdd:cd17631 318 R-------DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAV 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 38524616 556 VA-DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17631 389 VVpRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
77-605 |
5.24e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 165.08 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 77 TIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAA 156
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGD--QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG--AV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLkeASTAPLAQ 234
Cdd:PRK07656 82 VVPLNTRYTAdeAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFL--AAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 235 IPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMA-AFGHHAyRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAaDWAEYL-GLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 314 RKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRQIGEFYGATE 391
Cdd:PRK07656 239 LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPVALLERFESELGVDIVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 392 CnCSIANM-----DGKV--GSCGfnsRILPHVyPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVgqinqqdpLRRFD 464
Cdd:PRK07656 319 A-SGVTTFnrlddDRKTvaGTIG---TAIAGV-ENKIV-----------NELGEEVP--VGEVGELL--------VRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 465 ---GYVS-ESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY 540
Cdd:PRK07656 373 vmkGYYDdPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 541 GVAVPGVeGKAGMA-AVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPqVDTTGtfKIQKTRLQ 605
Cdd:PRK07656 447 GVPDERL-GEVGKAyVVLKPGAELTEEELIAYCREHLAKYKVPrsiEFLDELP-KNATG--KVLKRALR 511
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
78-605 |
2.17e-42 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 159.65 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 158 LNVNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkSLIKFCSgdlgpegilpdthlldpLLKEASTAPLAQIPS 237
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALI------------------VAVSFTD-----------------LLAAGAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 238 KgmDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQaaDVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:cd05936 124 P--EDVAVLQYTSGTTGVPKGAMLTHrnlvANALQIKAWLEDLLEGD--DVVLAALPLFHVFGLTVALLLPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 314 RKKFSASRFWDDCIKYNCTVVQ-----YIGeicryLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEF 386
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 387 YGATECNCSIA-N-MDG--KVGSCGFnsrILPHVYpirlVKVnedtmellRDAQGLCIPCqaGEPGLLVgqinqqdpLR- 461
Cdd:cd05936 274 YGLTETSPVVAvNpLDGprKPGSIGI---PLPGTE----VKI--------VDDDGEELPP--GEVGELW--------VRg 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 462 --RFDGYVS-ESATSKkiahsVFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:cd05936 329 pqVMKGYWNrPEETAE-----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38524616 539 VYGVAVP--GVEGKAgmAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLQ 605
Cdd:cd05936 402 VVGVPDPysGEAVKA--FVVLKEGASLTEEEIIAFCREQLAGYKVPrqvEFRDELPK-SAVG--KILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-604 |
3.44e-40 |
|
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: 153.62 E-value: 3.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIkfcsgDLGPEGILPDTHLLD---PLLKEASTAPLAQIPSKGMDDRLFy 246
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAIL-----ELALDVGVLIRAPSAeslSNLLADKKNAKSEGVPLPDDLALI- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSryyRMAAFGHH---AYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFW 323
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHR---NLAASATNitnTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 324 DDCIKYNCTVVQYIGEICRYLLKQPVREAERRH---RVRLAVGNGLRPAIWEEFTERFGVRQIgEFYGATE------CNC 394
Cdd:cd05926 232 PDVRDYNATWYTAVPTIHQILLNRPEPNPESPPpklRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEaahqmtSNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 SIANMDgKVGSCGfnsriLPHVYPIRLvkVNEDtmellrdaqGLciPCQAGEpgllVGQINQQDPlRRFDGYVSESATSK 474
Cdd:cd05926 311 LPPGPR-KPGSVG-----KPVGVEVRI--LDED---------GE--ILPPGV----VGEICLRGP-NVTRGYLNNPEANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAhsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKA-GM 553
Cdd:cd05926 367 EAA-----FKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KYGEEvAA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 38524616 554 AAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRL 604
Cdd:cd05926 441 AVVLREGASVTEEELRAFCRKHLAAFKVPkkvYFVDELPK---TATGKIQRRKV 491
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
81-601 |
5.71e-40 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 153.80 E-value: 5.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 81 IFQAVVQRQPERLALV---DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAAL 157
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 158 LNVNLRREPLAFCLGTSGAKALIFGGE--MVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEAS---TAPL 232
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWID----FRKLIKNASpdfERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 233 AQIPSKGMDDRLFYiYTSGTTGLPKaaIVVHSRYYRMaafGHHAYRMQAADVLYDCLplyHSAGNIIGVGQCL---IYG- 308
Cdd:cd05970 178 ANSYPCGEDILLVY-FSSGTTGMPK--MVEHDFTYPL---GHIVTAKYWQNVREGGL---HLTVADTGWGKAVwgkIYGq 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 309 ------LTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVRE---AERRHRVrlAVGNGLRPAIWEEFTERFG 379
Cdd:cd05970 249 wiagaaVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRydlSSLRYCT--TAGEALNPEVFNTFKEKTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 380 VrQIGEFYGATECNCSIAN---MDGKVGSCGfnsRILPHvYPIRLVKVNEDtmellrdaqglciPCQAGEPGLLVGQINQ 456
Cdd:cd05970 327 I-KLMEGFGQTETTLTIATfpwMEPKPGSMG---KPAPG-YEIDLIDREGR-------------SCEAGEEGEIVIRTSK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 457 QDPLRRFDGYVSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTD 536
Cdd:cd05970 389 GKPVGLFGGYYKDAEKTAEVWH------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 537 VAVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd05970 463 CAVTGVPDP-IRGQVVKATIVLAKGYEPSEELKKELQdhvkKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
104-604 |
4.44e-39 |
|
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: 149.41 E-value: 4.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGG 183
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 EmvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05972 81 E---------------------------------------------------------DPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 264 SryyrmAAFGHHAYR-----MQAADVLY---DCLPLYHSAGNIIGVgqcLIYGLTVVL--RKKFSASRFWDDCIKYNCTV 333
Cdd:cd05972 104 S-----YPLGHIPTAaywlgLRPDDIHWniaDPGWAKGAWSSFFGP---WLLGATVFVyeGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 334 VQYIGEICRYLLKQPVrEAERRHRVRLAVGNG--LRPAIWEEFTERFGVrQIGEFYGATECNCSIAN---MDGKVGSCGf 408
Cdd:cd05972 176 FCGPPTAYRMLIKQDL-SSYKFSHLRLVVSAGepLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNfpdMPVKPGSMG- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 409 nsrilphvYPIRLVKVnedtmELLRDAQGLCIPcqaGEPGLLVGQINqqdPLRRFDGYVS-ESATSKKIahsvfskGDSA 487
Cdd:cd05972 253 --------RPTPGYDV-----AIIDDDGRELPP---GEEGDIAIKLP---PPGLFLGYVGdPEKTEASI-------RGDY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 488 YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLLDPNA 567
Cdd:cd05972 307 YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKAFVVLTSGYEPSEE 385
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 38524616 568 IYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05972 386 LAEELQghvkKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
69-609 |
1.51e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 149.70 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 69 RRHQRAG-HTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLG 147
Cdd:PRK08316 3 ERSTRARrQTIGDILRRSARRYPDKTALVFGD--RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 148 LAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVA---AVAEVSGHLGKSLIKFCSGDLGPEGILPdthLLDPLL 224
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPtaeAALALLPVDTLILSLVLGGREAPGGWLD---FADWAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 225 KEASTAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSryyrmaAFGH------HAYRMQAADVLYDCLPLYHSAGNI 298
Cdd:PRK08316 158 AGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHR------ALIAeyvsciVAGDMSADDIPLHALPLYHCAQLD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 299 IGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNC-------TVvqYIGeicryLLKQPVREaerrhRVRLAvgnGLRPA-- 369
Cdd:PRK08316 229 VFLGPYLYVGATNVILDAPDPELILRTIEAERItsffappTV--WIS-----LLRHPDFD-----TRDLS---SLRKGyy 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 370 --------IWEEFTERFGVRQIGEFYGATEcncsIA---------NMDGKVGSCG---FN--SRILphvypirlvkvned 427
Cdd:PRK08316 294 gasimpveVLKELRERLPGLRFYNCYGQTE----IAplatvlgpeEHLRRPGSAGrpvLNveTRVV-------------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 428 tmellrDAQGLCIPcqAGEPGLLVGQINQQdplrrFDGYV-SESATSKKIAHSVFSkgdsaylSGDVLVMDELGYMYFRD 506
Cdd:PRK08316 356 ------DDDGNDVA--PGEVGEIVHRSPQL-----MLGYWdDPEKTAEAFRGGWFH-------SGDLGVMDEEGYITVVD 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 507 RSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV-------AVPGVegkagmaAVADPHSLLDPNAIYQELQKVLAPY 579
Cdd:PRK08316 416 RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpdpkwieAVTAV-------VVPKAGATVTEDELIAHCRARLAGF 488
|
570 580 590
....*....|....*....|....*....|...
gi 38524616 580 ARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 609
Cdd:PRK08316 489 KVPkrvIFVDELPR-NPSG--KILKREL-RERY 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
105-605 |
5.65e-34 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 134.90 E-value: 5.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 MVAavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlFYIYTSGTTGLPKAAIVVHS 264
Cdd:cd05919 92 DIA---------------------------------------------------------YLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 265 RYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIYGL----TVVLRKKF-SASRFWDDCIKYNCTVVQYIG 338
Cdd:cd05919 115 DPLLFAdAMAREALGLTPGDRVFSSAKMFFG----YGLGNSLWFPLavgaSAVLNPGWpTAERVLATLARFRPTVLYGVP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 339 EICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVrQIGEFYGATEC-NCSIANMDGKV--GSCGfnsRIL 413
Cdd:cd05919 191 TFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGG-PILDGIGATEVgHIFLSNRPGAWrlGSTG---RPV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 414 PHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVGQINQQDPlrrfdGYVSESATSKKiahsvfSKGDSAYLSGDV 493
Cdd:cd05919 267 PG-YEIRLV-----------DEEGHTIP--PGEEGDLLVRGPSAAV-----GYWNNPEKSRA------TFNGGWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 494 LVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAAVADPHSLLDPN-----AI 568
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAFVVLKSPAAPQeslarDI 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 38524616 569 YQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05919 400 HRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
90-604 |
5.29e-33 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 133.26 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDaGTGECWtFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05959 18 GDKTAFID-DAGSLT-YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAEVSG---HLGKSLIKfcSGDLGPEGILPD-THLLD---PLLKEASTAPlaqipskgmDD 242
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAALTkseHTLVVLIV--SGGAGPEAGALLlAELVAaeaEQLKPAATHA---------DD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 243 RLFYIYTSGTTGLPKAAIVVHSRYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLRKKF 317
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFA----YGLGNSLTFplsvGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 318 -SASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVrQIGEFYGATEC-N 393
Cdd:cd05959 241 pTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFGL-DILDGIGSTEMlH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 394 CSIANMDGKV--GSCGfnsRILPHvYPIRLvkVNEDTMELlrdaqglcipcQAGEPGLL--------VGQINQQDPLRR- 462
Cdd:cd05959 320 IFLSNRPGRVryGTTG---KPVPG-YEVEL--RDEDGGDV-----------ADGEPGELyvrgpssaTMYWNNRDKTRDt 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 463 FDGYvsesatskkiahsvfskgdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLsrllgQTDVAVYGV 542
Cdd:cd05959 383 FQGE--------------------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL-----VQHPAVLEA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38524616 543 AVPGVEGKAGM---AAVADPHSLLDPNAIYQE-----LQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRL 604
Cdd:cd05959 438 AVVGVEDEDGLtkpKAFVVLRPGYEDSEALEEelkefVKDRLAPYKYPrwiVFVDELPK---TATGKIQRFKL 507
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
97-639 |
1.82e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 134.07 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 97 DAGTGECW-------TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNlrrEPLAF 169
Cdd:PRK07868 459 DAPKGEFLlfdgrvhTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD---TDLAA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAEVSGH---LGKSLIKFCSGDLGPEGIlpDTHLLDPllkEASTAPLAQIPSKGMDDRLFY 246
Cdd:PRK07868 536 AVRLGGVTEIITDPTNLEAARQLPGRvlvLGGGESRDLDLPDDADVI--DMEKIDP---DAVELPGWYRPNPGLARDLAF 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSRYyRMAAFG-HHAYRMQAADVLYdCL-PLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWD 324
Cdd:PRK07868 611 IAFSTAGGELVAKQITNYRW-ALSAFGtASAAALDRRDTVY-CLtPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQ 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 325 DCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDG-KV 403
Cdd:PRK07868 689 EVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaKI 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 404 GSCGfnsRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGqinqqdplrRFDGYVSESATSKKiahSVFSK 483
Cdd:PRK07868 769 GSKG---RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLA---------RARGPIDPTASVKR---GVFAP 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 484 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRlLGQTDVAV-YGVAVPGVEgkAGMAAVA-DPHS 561
Cdd:PRK07868 834 ADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGR-IGGVDLAVtYGVEVGGRQ--LAVAAVTlRPGA 910
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 562 LLDPNAIYQELQKvLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFdPRqTSDRLFFLDLKQGHYLPLNEAVYTRI 639
Cdd:PRK07868 911 AITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PK-PGRQAWYFDPETNRYRRLTPAVRAEL 985
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-593 |
9.62e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.05 E-value: 9.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 42 RFLRIVCKTARRDLFGLSVLIRVRLELRRHQRAGhtipRIFQAVVQRQPERLALVD-AGTgecWTFAQLDAYSNAVANLF 120
Cdd:PRK07788 19 HYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFA----GLVAHAARRAPDRAALIDeRGT---LTYAELDEQSNALARGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 121 RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSL 200
Cdd:PRK07788 92 LALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 201 IKFCSGDLGPEGIlPDTHLLDPLLKEASTAPLAQIPSKGMddrlFYIYTSGTTGLPKAAivVHSRYYRMAAFGHHAYRM- 279
Cdd:PRK07788 172 AWGGNPDDDEPSG-STDETLDDLIAGSSTAPLPKPPKPGG----IVILTSGTTGTPKGA--PRPEPSPLAPLAGLLSRVp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 280 -QAADVLYDCLPLYHSagniIGVGQCLI---YGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERR 355
Cdd:PRK07788 245 fRAGETTLLPAPMFHA----TGWAHLTLamaLGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 356 H----RVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECN-CSIANMD------GKVGScgfnsrilphvyPIRLVKV 424
Cdd:PRK07788 321 DtsslKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAfATIATPEdlaeapGTVGR------------PPKGVTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 425 nedtmELLrDAQGLCIPcqAGEPG-LLVGQINQqdplrrFDGYVseSATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMY 503
Cdd:PRK07788 388 -----KIL-DENGNEVP--RGVVGrIFVGNGFP------FEGYT--DGRDKQIIDGLLSSGDVGYF-------DEDGLLF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 504 FRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYAR 581
Cdd:PRK07788 445 VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEFGQRLRAfvVKAPGAALDEDAIKDYVRDNLARYKV 522
|
570
....*....|....*
gi 38524616 582 P---IFLRLLPQVDT 593
Cdd:PRK07788 523 PrdvVFLDELPRNPT 537
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
94-615 |
9.95e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 129.25 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 94 ALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGT 173
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 174 SGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEASTAPLA-QIPSKGMddrlfyIYTSGT 252
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPDTPIAdETAGADM------LYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 253 TGLPKA------AIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGvGQCLIYGLTVVLRKKFSASRFWDDC 326
Cdd:PRK08276 152 TGRPKGikrplpGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFG-MSALALGGTVVVMEKFDAEEALALI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 327 IKYNCTVVQYIGEICRYLLKQPvreAERRHR-----VRLAVGNG--LRPAIWEEFTERFGvRQIGEFYGATECN----CS 395
Cdd:PRK08276 231 ERYRVTHSQLVPTMFVRMLKLP---EEVRARydvssLRVAIHAAapCPVEVKRAMIDWWG-PIIHEYYASSEGGgvtvIT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IANMDGKVGSCGfnsriLPHVYPIRLVkvnedtmellrDAQGlcIPCQAGEPGLLVGQINQQDplrrFDGYVSESATSK- 474
Cdd:PRK08276 307 SEDWLAHPGSVG-----KAVLGEVRIL-----------DEDG--NELPPGEIGTVYFEMDGYP----FEYHNDPEKTAAa 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVEGKAGMA 554
Cdd:PRK08276 365 RNPHGWVTVGDVGYL-------DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG--VPDEEMGERVK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 555 AVADPHSLLDPN-AIYQEL----QKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLqREGFDPRQTS 615
Cdd:PRK08276 436 AVVQPADGADAGdALAAELiawlRGRLAHYKCPrsiDFEDELPR-TPTG--KLYKRRL-RDRYWEGRQR 500
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
99-606 |
7.51e-31 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 125.62 E-value: 7.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 99 GTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKA 178
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 179 LIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipSKGMDDRLFYIYTSGTTGLPKA 258
Cdd:cd05971 82 LV--------------------------------------------------------TDGSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 259 AIvvhsryyrmaafghHAYR--MQAADVLYDCLPLYHSAGN----------IIGVGQCLI----YGLTVVLRK--KFSAS 320
Cdd:cd05971 106 AL--------------HAHRvlLGHLPGVQFPFNLFPRDGDlywtpadwawIGGLLDVLLpslyFGVPVLAHRmtKFDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 321 RFWDDCIKYNCTVVqYIGEICRYLLKQpVREAERRHRVRL-AVGNGLRPAIWEEF---TERFGVrQIGEFYGATECNCSI 396
Cdd:cd05971 172 AALDLMSRYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLrAIATGGESLGEELLgwaREQFGV-EVNEFYGQTECNLVI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 397 AN----MDGKVGSCGfnsRILP-HVYPIrlvkVNEDTMELLRDAQG-LCipcqagepgllvgqINQQDPLrRFDGYV-SE 469
Cdd:cd05971 249 GNcsalFPIKPGSMG---KPIPgHRVAI----VDDNGTPLPPGEVGeIA--------------VELPDPV-AFLGYWnNP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 470 SATSKKIAHSVFskgdsayLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEG 549
Cdd:cd05971 307 SATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP-IRG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38524616 550 KAGMAAVADPHSLLDPNAIYQELQKV----LAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05971 379 EIVKAFVVLNPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-606 |
1.04e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.43 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVdaGTGECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLA 168
Cdd:PRK06839 16 PDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 169 FCLGTSGAKALIFGGEMVAAVAEVSGHLGkslikfcsgdlgpegILPDTHLLDPllKEASTAPLAQIPSKGMDDRLFYIY 248
Cdd:PRK06839 94 FQLKDSGTTVLFVEKTFQNMALSMQKVSY---------------VQRVISITSL--KEIEDRKIDNFVEKNESASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIK 328
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 329 YNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVgNGLRPA---IWEEFTERfGVRqIGEFYGATECNCS---IANMDG- 401
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFY-NGGAPCpeeLMREFIDR-GFL-FGQGFGMTETSPTvfmLSEEDAr 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 402 -KVGSCGfnsrilphvypiRLVKVNEdtMELLRDAQGLCIPcqaGEpgllVGQINQQDPLRRFDGYVSESATSKKIAHSV 480
Cdd:PRK06839 314 rKVGSIG------------KPVLFCD--YELIDENKNKVEV---GE----VGELLIRGPNVMKEYWNRPDATEETIQDGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 481 FSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPH 560
Cdd:PRK06839 373 LCTGDLARV-------DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 38524616 561 SLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLQR 606
Cdd:PRK06839 446 SVLIEKDVIEHCRLFLAKYKIPkeiVFLKELPK-NATG--KIQKAQLVN 491
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
86-607 |
1.16e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 122.76 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK03640 12 AFLTPDRTAIEFEE--KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfCSGDLGPegiLPDTHLLDPLLKEasTAPLAQIPSkgmddrlf 245
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPG-----------ISVKFAE---LMNGPKEEAEIQE--EFDLDEVAT-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 246 YIYTSGTTGLPKAAivvhsryyrMAAFGHHAYR---------MQAADVLYDCLPLYHSAGNIIGVGQcLIYGLTVVLRKK 316
Cdd:PRK03640 146 IMYTSGTTGKPKGV---------IQTYGNHWWSavgsalnlgLTEDDCWLAAVPIFHISGLSILMRS-VIYGMRVVLVEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 317 FSASRFWDDCIKYNCT---VVQyigeicrYLLKQPVREAERRH-----RVRLAVGNGLRPAIWEEFTER-FGVRQIgefY 387
Cdd:PRK03640 216 FDAEKINKLLQTGGVTiisVVS-------TMLQRLLERLGEGTypssfRCMLLGGGPAPKPLLEQCKEKgIPVYQS---Y 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 388 GATECNCSIANMD-----GKVGSCG---FNSRIlphvypirlvKVNEDTMEllrdaqglCIPCQAGE-----PGLLVGQI 454
Cdd:PRK03640 286 GMTETASQIVTLSpedalTKLGSAGkplFPCEL----------KIEKDGVV--------VPPFEEGEivvkgPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 455 NQqdplrrfdgyvsESATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQ 534
Cdd:PRK03640 348 NR------------EDATRETFQDGWFKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 535 TDVAVYGVAvpgvEGKAGMAAVAD--PHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLQRE 607
Cdd:PRK03640 409 AEAGVVGVP----DDKWGQVPVAFvvKSGEVTEEELRHFCEEKLAKYKVPkrfYFVEELPR---NASGKLLRHELKQL 479
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
88-606 |
2.84e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 123.14 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 88 RQPERLAL---VDAG---TGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeAALLNVN 161
Cdd:PRK07529 37 RHPDAPALsflLDADpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI-ANPINPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LRREPLAFCLGTSGAKALI-----FGGEMVAAVAEVSGHL--GKSLIKFCSGDLGPegilPDTHLLDPLLKEASTAP--- 231
Cdd:PRK07529 116 LEPEQIAELLRAAGAKVLVtlgpfPGTDIWQKVAEVLAALpeLRTVVEVDLARYLP----GPKRLAVPLIRRKAHARild 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 232 -LAQIpSKGMDDRLF------------YIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNI 298
Cdd:PRK07529 192 fDAEL-ARQPGDRLFsgrpigpddvaaYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 299 IGVGQCLIYGLTVVL------RKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVrEAERRHRVRLAVGNG--LRPAI 370
Cdd:PRK07529 271 VTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAapLPVEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 371 WEEFTERFGVRqIGEFYGATECNC--SIANMDG--KVGSCGFNsriLPHVYpIRLVKVNEDTmELLRDaqglcipCQAGE 446
Cdd:PRK07529 350 FRRFEAATGVR-IVEGYGLTEATCvsSVNPPDGerRIGSVGLR---LPYQR-VRVVILDDAG-RYLRD-------CAVDE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 447 PGLLVgqinQQDPlRRFDGYVSEsatskkiAHSVFSKGDSAYL-SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PRK07529 417 VGVLC----IAGP-NVFSGYLEA-------AHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 526 GVLSRLLGQTDVAVYG--------VAVPGVEGKAGmaAVADPHSLLDPNAiyqelQKVLAPYARPIFLRLLPQVDTTGTF 597
Cdd:PRK07529 485 EALLRHPAVALAAAVGrpdahageLPVAYVQLKPG--ASATEAELLAFAR-----DHIAERAAVPKHVRILDALPKTAVG 557
|
....*....
gi 38524616 598 KIQKTRLQR 606
Cdd:PRK07529 558 KIFKPALRR 566
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
86-572 |
5.17e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 121.34 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFcsgDLGPEGILPDTHLLDPLLKEASTAPLAQiPSKGMDdrlf 245
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEAVAGLPATPIAD-ESLGTD---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 246 YIYTSGTTGLPKAAivvhsryYR------------MAAFGHHAYRMQAADVLYDCLPLYHSA-GNIIGVGQCLiyGLTVV 312
Cdd:PRK13391 159 MLYSSGTTGRPKGI-------KRplpeqppdtplpLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL--GGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 LRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPvREAERRHRVrlavgNGLRPAIW----------EEFTERFGvRQ 382
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP-EEVRDKYDL-----SSLEVAIHaaapcppqvkEQMIDWWG-PI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 383 IGEFYGATECNcsianmdgkvGSCGFNSR-ILPHvyPIRLVKVNEDTMELLRDAQGlciPCQAGEPgllvGQI--NQQDP 459
Cdd:PRK13391 303 IHEYYAATEGL----------GFTACDSEeWLAH--PGTVGRAMFGDLHILDDDGA---ELPPGEP----GTIwfEGGRP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 LRRF-DGYVSESATSkkiAHSVFSKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:PRK13391 364 FEYLnDPAKTAEARH---PDGTWST------VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAA 434
|
490 500 510
....*....|....*....|....*....|....*
gi 38524616 539 VYGvaVPGVEGKAGMAAVADPHSLLDPN-AIYQEL 572
Cdd:PRK13391 435 VFG--VPNEDLGEEVKAVVQPVDGVDPGpALAAEL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
90-609 |
1.26e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 119.98 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALvDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PRK07514 16 RDAPFI-ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKfcsgDLGPEGIlpdthllDPLLKEASTAPLAQIP-SKGMDDRLFYIY 248
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKIAAAAGAPHVE----TLDADGT-------GSLLEAAAAAPDDFETvPRGADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSAsrfwDDCIK 328
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDP----DAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 329 Y--NCTVVqyIGEICRY--LLKQPV--REAERrhRVRLAVgNGLRPAIWE---EFTERFGVRqIGEFYGATECNCSIAN- 398
Cdd:PRK07514 240 LmpRATVM--MGVPTFYtrLLQEPRltREAAA--HMRLFI-SGSAPLLAEthrEFQERTGHA-ILERYGMTETNMNTSNp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 MDGK--VGSCGFNsriLPHVyPIRLvkVNEDTMEllrdaqglciPCQAGEpgllVGQINQQDPlRRFDGY--VSEsatsk 474
Cdd:PRK07514 314 YDGErrAGTVGFP---LPGV-SLRV--TDPETGA----------ELPPGE----IGMIEVKGP-NVFKGYwrMPE----- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAHSVfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVeGKAGMA 554
Cdd:PRK07514 368 KTAEEF--RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 555 AV-ADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvDTTGtfKIQKTRLqREGF 609
Cdd:PRK07514 445 VVvPKPGAALDEAAILAALKGRLARFKQPkrvFFVDELPR-NTMG--KVQKNLL-REQY 499
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
59-607 |
9.58e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 117.85 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 59 SVLIRVRLElrRHQRAGH----TIPRIFQAVVQRQPERLALVD--AGTGEC--WTFAQLDAYSNAVANLFRQLGFAPGDV 130
Cdd:PRK13295 5 AVLLPPRRA--ASIAAGHwhdrTINDDLDACVASCPDKTAVTAvrLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 131 VAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI----FGG----EMVAAVAEVSGHLGKslIK 202
Cdd:PRK13295 83 VSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktFRGfdhaAMARRLRPELPALRH--VV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 203 FCSGDlGPEGIlpDTHLLDPLLKEASTAP-LAQIPSKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRMAAFGHHAYRMQ- 280
Cdd:PRK13295 161 VVGGD-GADSF--EALLITPAWEQEPDAPaILARLRPGPDDVTQLIYTSGTTGEPKG--VMHTANTLMANIVPYAERLGl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 281 -AADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWD----DCIKYNCTVVQYIGEICRYllkqpVREAER- 354
Cdd:PRK13295 236 gADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAElirtEGVTFTMASTPFLTDLTRA-----VKESGRp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 355 --RHRVRLAVGNGLRPAIWEEFTERFGVRQIGEfYGATECNC-----------SIANMDGkvgscgfnsRILPHVyPIRL 421
Cdd:PRK13295 311 vsSLRTFLCAGAPIPGALVERARAALGAKIVSA-WGMTENGAvtltklddpdeRASTTDG---------CPLPGV-EVRV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 422 VkvnedtmellrDAQGLCIPcqAGEPGLLV--GQINqqdplrrFDGYVSESATSKKIAHSVFSKGDSAYLSGDvlvmdel 499
Cdd:PRK13295 380 V-----------DADGAPLP--AGQIGRLQvrGCSN-------FGGYLKRPQLNGTDADGWFDTGDLARIDAD------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 500 GYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAI--YQELQKVLA 577
Cdd:PRK13295 433 GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMveFLKAQKVAK 512
|
570 580 590
....*....|....*....|....*....|
gi 38524616 578 PYArPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK13295 513 QYI-PERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
82-605 |
9.78e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.22 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 82 FQAvvQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:PRK09088 3 FHA--RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LrreplafclgtsgakalifggemvaAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:PRK09088 81 L-------------------------SASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-FGHHAyRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSAS 320
Cdd:PRK09088 136 RVSLILFTSGTSGQPKGVMLSERNLQQTAHnFGVLG-RVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 321 RFWDDCIKYNCTVVQYIG--EICRYLLKQPVREAER-RHRVRLAVGNGLRPAI----WEE----FTERFGVRQIGEFYGA 389
Cdd:PRK09088 215 RTLGRLGDPALGITHYFCvpQMAQAFRAQPGFDAAAlRHLTALFTGGAPHAAEdilgWLDdgipMVDGFGMSEAGTVFGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 390 TeCNCSIanMDGKVGSCGFNSrilPHVYpIRLVkvnedtmellrDAQGLciPCQAGEPG--LLVGQinqqdplRRFDGYV 467
Cdd:PRK09088 295 S-VDCDV--IRAKAGAAGIPT---PTVQ-TRVV-----------DDQGN--DCPAGVPGelLLRGP-------NLSPGYW 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 468 SESATSKKiahsVFSkGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGv 547
Cdd:PRK09088 348 RRPQATAR----AFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ- 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 548 EGKAG-MAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK09088 422 WGEVGyLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
86-543 |
9.83e-28 |
|
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: 117.22 E-value: 9.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd05923 11 ASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFClgtsgakalIFGGEMVAAVAEVsGHLGKSLIKFCSGDLGPEGILPDTHLLDpllkeaSTAPLAQIPSKGMDDRLF 245
Cdd:cd05923 91 ELAEL---------IERGEMTAAVIAV-DAQVMDAIFQSGVRVLALSDLVGLGEPE------SAGPLIEDPPREPEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 246 YIYTSGTTGLPKAAIVVH-SRYYRMAAFGHHA-YRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFW 323
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQrAAESRVLFMSTQAgLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 324 DDCIKYNCT----VVQYIGEICRYLLKQPVREAERRHrVRLAvGNGLRPAIWEEFTERFGVRQIgEFYGATECNCSIANM 399
Cdd:cd05923 235 KLIEQERVTslfaTPTHLDALAAAAEFAGLKLSSLRH-VTFA-GATMPDAVLERVNQHLPGEKV-NIYGTTEAMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 400 DGKVGSC---GFNSRilphvypIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDplrrfdgyvsesATSKKI 476
Cdd:cd05923 312 DARTGTEmrpGFFSE-------VRIVRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPE------------ATAKKL 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 477 AhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVA 543
Cdd:cd05923 373 Q-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
90-604 |
1.18e-27 |
|
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: 116.47 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--REPL 167
Cdd:cd05930 1 PDAVAVVDGD--QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG--AAYVPLDPSypAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 168 AFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeasTAPlaqipskgmdDRLFY- 246
Cdd:cd05930 77 AYILEDSGAKLVL------------------------------------------------TDP----------DDLAYv 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAGNIIGVGQ---CLIYGLTVVLRKK---FSAS 320
Cdd:cd05930 99 IYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVL----QFTSFSFDVSVWEifgALLAGATLVVLPEevrKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 321 RFWDDCIKYNCTVVQYIGEICRYLLKQPvrEAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIGEFYGATEcnCSIAN 398
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTE--ATVDA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 MDGKVGSCGFNSRILPHVYPIRLVKVnedtmeLLRDAQGLCIPcqAGEPG-LLVG--QINQqdplrrfdGYV-SESATSK 474
Cdd:cd05930 251 TYYRVPPDDEEDGRVPIGRPIPNTRV------YVLDENLRPVP--PGVPGeLYIGgaGLAR--------GYLnRPELTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMA 554
Cdd:cd05930 315 RFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV--VAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 38524616 555 A--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05930 393 AyvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-607 |
2.70e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.80 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 75 GHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGme 154
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 155 AALLNVN--LRREPLAFCLGTSGAKALIF-----GGEMVAAVAEvsghLGKSLIKFCSGDLGPE-----------GILPD 216
Cdd:PRK12583 95 AILVNINpaYRASELEYALGQSGVRWVICadafkTSDYHAMLQE----LLPGLAEGQPGALACErlpelrgvvslAPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 217 THLL--DPLLKEA---STAPLAQI-PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLP 290
Cdd:PRK12583 171 PGFLawHELQARGetvSREALAERqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 291 LYHSAGNIIGVGQCLIYGLTVVL-RKKFSASRFWDDCIKYNCTVVQ-----YIGEicrylLKQPVREAERRHRVRLAV-- 362
Cdd:PRK12583 251 LYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAE-----LDHPQRGNFDLSSLRTGIma 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 363 GNGLRPAIWEEFTERFGVRQIGEFYGATECN------CSIANMDGKVGSCGfnsRILPHVYpirlVK-VNEDTMELLRDA 435
Cdd:PRK12583 326 GAPCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqtTAADDLERRVETVG---RTQPHLE----VKvVDPDGATVPRGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 436 QG-LCIpcqagePGLLVGQINQQDPlrrfdgyvseSATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRW 514
Cdd:PRK12583 399 IGeLCT------RGYSVMKGYWNNP----------EATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 515 RGENVSTTEVEGVLSRLLGQTDVAVYGVAvpgvEGKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQ 590
Cdd:PRK12583 457 GGENIYPREIEEFLFTHPAVADVQVFGVP----DEKYGEEIVAwvrlHPGHAASEEELREFCKARIAHFKVPRYFRFVDE 532
|
570
....*....|....*..
gi 38524616 591 VDTTGTFKIQKTRLqRE 607
Cdd:PRK12583 533 FPMTVTGKVQKFRM-RE 548
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
86-581 |
3.47e-26 |
|
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: 112.71 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN-VNLRR 164
Cdd:cd05904 15 ASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 165 EpLAFCLGTSGAKaLIFggeMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPllkeaSTAPLAQIPSkgmDDRL 244
Cdd:cd05904 95 E-IAKQVKDSGAK-LAF---TTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADE-----AEPPVVVIKQ---DDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAA--DVLYDCLPLYHSAG-NIIGVGQcLIYGLTVVLRKKFSASR 321
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMFHIYGlSSFALGL-LRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 322 FWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRlAVGNG---LRPAIWEEFTERFGVRQIGEFYGATECNCSIAN 398
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 MD------GKVGSCGfnsRILPHVYpirlVK-VNEDTMELLRdaqglciPCQAGE-----PGLLVGQINqqdplrrfdgy 466
Cdd:cd05904 320 CFapekdrAKYGSVG---RLVPNVE----AKiVDPETGESLP-------PNQTGElwirgPSIMKGYLN----------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 467 vSESATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPG 546
Cdd:cd05904 375 -NPEATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV--IPYPD 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 38524616 547 VE-GKAGMA-AVADPHSLLDPNAIYQELQKVLAPYAR 581
Cdd:cd05904 446 EEaGEVPMAfVVRKPGSSLTEDEIMDFVAKQVAPYKK 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-604 |
9.97e-26 |
|
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: 110.46 E-value: 9.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 91 ERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGF-APGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd05941 1 DRIAIVDDG--DSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmdDRLFYIYT 249
Cdd:cd05941 79 VITDSEPSLVL-------------------------------------------------------------DPALILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 250 SGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKY 329
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 330 NCTVVQ-----YIGEICRYLLKQPVREAERR---HRVRLAV-GNG-LRPAIWEEFTERFGVRqIGEFYGATECNCSIAN- 398
Cdd:cd05941 178 SITVFMgvptiYTRLLQYYEAHFTDPQFARAaaaERLRLMVsGSAaLPVPTLEEWEAITGHT-LLERYGMTEIGMALSNp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 MDG--KVGSCGFNsriLPHVyPIRLVKvNEDTMELLRDAQG-LCIpcqAGePGLlvgqinqqdplrrFDGYVSE-SATSK 474
Cdd:cd05941 257 LDGerRPGTVGMP---LPGV-QARIVD-EETGEPLPRGEVGeIQV---RG-PSV-------------FKEYWNKpEATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 475 KIAhsvfskGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGM 553
Cdd:cd05941 315 EFT------DDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDP-DWGERVV 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 554 AAVA--DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05941 388 AVVVlrAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
76-391 |
1.04e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 111.52 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 76 HTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeA 155
Cdd:PRK07798 3 WNIADLFEAVADAVPDRVALVCGD--RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 156 ALLNVNLR--REPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLA 233
Cdd:PRK07798 79 VPVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 234 QIPSKgmDDrLFYIYTSGTTGLPKAAIVVHSRYYRmAAFG--------------HHAYRMQAAD--VLYDCLPLYHSAGn 297
Cdd:PRK07798 159 GERSP--DD-LYLLYTGGTTGMPKGVMWRQEDIFR-VLLGgrdfatgepiedeeELAKRAAAGPgmRRFPAPPLMHGAG- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 298 IIGVGQCLIYGLTVVL--RKKFSASRFWDDCIKYNCTVVQYIGE-ICRYLLKqpvrEAERRHRVRL----AVGNG---LR 367
Cdd:PRK07798 234 QWAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLLD----ALEARGPYDLsslfAIASGgalFS 309
|
330 340
....*....|....*....|....
gi 38524616 368 PAIWEEFTERFGVRQIGEFYGATE 391
Cdd:PRK07798 310 PSVKEALLELLPNVVLTDSIGSSE 333
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
87-609 |
1.31e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.41 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGTGECWtfAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK07786 28 LMQPDAPALRFLGNTTTW--RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 167 LAFCLGTSGAKALIFGG---EMVAAVAEVSGHLGKSLIkfcSGDLGPEGILPdthlLDPLLKEASTA-PLAQIPSkgmDD 242
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAalaPVATAVRDIVPLLSTVVV---AGGSSDDSVLG----YEDLLAEAGPAhAPVDIPN---DS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 243 RLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQ-AADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLR--KKFSA 319
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 320 SRFWDDCIKYNCTVVQYIGEICRYLLKQPvREAERRHRVRlAVGNGLRPA---IWEEFTERFGVRQIGEFYGATECNCSI 396
Cdd:PRK07786 255 GQLLDVLEAEKVTGIFLVPAQWQAVCAEQ-QARPRDLALR-VLSWGAAPAsdtLLRQMAATFPEAQILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 397 ANMDG-----KVGSCGfnsRILPHVYpirlVKVNEDTMELLrdAQGlcipcQAGE-----PGLLVGQINqqdplrrfdgy 466
Cdd:PRK07786 333 CMLLGedairKLGSVG---KVIPTVA----ARVVDENMNDV--PVG-----EVGEivyraPTLMSGYWN----------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 467 vSESATSKKIAHSVFSkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPG 546
Cdd:PRK07786 388 -NPEATAEAFAGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38524616 547 -VEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLqREGF 609
Cdd:PRK07786 460 wGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERY 522
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
87-581 |
1.50e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 110.87 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLWLGLaKAGMEAALLNVNLRRE 165
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEaLVVLWAAL-RSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHL------GKSLIKFCSGDLGPEGILPdthlldpllkeastaPLAQIPSKG 239
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLplrlsfGGEIDGFGSFEAALAGAGP---------------RLTEQPCGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 240 MddrlfYIYTSGTTGLPKA------AIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAgNIIGVGQCLIYGLTVVL 313
Cdd:PRK13390 152 V-----MLYSSGTTGFPKGiqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 314 RKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQpvrEAERRHRVRLAvgnGLRPAIWEEFTERFGVRQ---------IG 384
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKL---DADVRTRYDVS---SLRAVIHAAAPCPVDVKHamidwlgpiVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 385 EFYGATECNcSIANMD-----GKVGSCGFNSRILPHVypirlvkVNEDTMELlrdaqglcipcQAGEPGLLVgqiNQQDP 459
Cdd:PRK13390 300 EYYSSTEAH-GMTFIDspdwlAHPGSVGRSVLGDLHI-------CDDDGNEL-----------PAGRIGTVY---FERDR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 LR-RFDGYVSESATSKKIAHSVFSKgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:PRK13390 358 LPfRYLNDPEKTAAAQHPAHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVA 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 38524616 539 VYGVAVP--GVEGKAGMAAVADphslLDPNaiyQELQKVLAPYAR 581
Cdd:PRK13390 432 VIGVPDPemGEQVKAVIQLVEG----IRGS---DELARELIDYTR 469
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-606 |
2.10e-25 |
|
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: 109.32 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLG--GSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VNLRREPLAFCLGTSGAKALIFggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeaSTAPlaqipskg 239
Cdd:cd17653 79 AKLPSARIQAILRTSGATLLLT----------------------------------------------TDSP-------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 240 mDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHayRM---------QAADVLYDClplyhSAGNIIGvgqCLIYGLT 310
Cdd:cd17653 105 -DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA--RLdvgpgsrvaQVLSIAFDA-----CIGEIFS---TLCNGGT 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 311 VVLRkkfSASRFWDDCIKyNCTVVQYIGEIcryLLKQPVREAERRHRVRLAvGNGLRPAIWEEFTERfgvRQIGEFYGAT 390
Cdd:cd17653 174 LVLA---DPSDPFAHVAR-TVDALMSTPSI---LSTLSPQDFPNLKTIFLG-GEAVPPSLLDRWSPG---RRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 391 ECNCSIAnmdgkvgscgfNSRILPHV-----YPIRLVKV---NEDTMELLRDAQG-LCIpcqAGePGLLVGQINQqdplr 461
Cdd:cd17653 243 ECTISST-----------MTELLPGQpvtigKPIPNSTCyilDADLQPVPEGVVGeICI---SG-VQVARGYLGN----- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 462 rfdgyvsESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQtdvaVYG 541
Cdd:cd17653 303 -------PALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE----VTQ 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 542 VAVPGVEGKagMAAVADPHSlLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd17653 372 AAAIVVNGR--LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
85-608 |
4.12e-25 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 109.54 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 85 VVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRR 164
Cdd:TIGR02262 14 VVEGRGGKTAFID--DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 165 EPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDlGPEGILPDTHLL---DPLLKEASTAPlaqipskgmD 241
Cdd:TIGR02262 92 DDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLateSEQFKPAATQA---------D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAA-FGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLR-K 315
Cdd:TIGR02262 162 DPAFWLYSSGSTGMPKGVVHTHSNPYWTAElYARNTLGIREDDVCFSAAKLFFA----YGLGNALTFpmsvGATTVLMgE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 316 KFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVrQIGEFYGATEC- 392
Cdd:TIGR02262 238 RPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTsaGEALPAEVGQRWQARFGV-DIVDGIGSTEMl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 393 NCSIANMDGKV--GSCGfnsrilphvypirlVKVNEDTMELLRDAQGlciPCQAGEPGLL--------VGQINQQDPLRR 462
Cdd:TIGR02262 317 HIFLSNLPGDVryGTSG--------------KPVPGYRLRLVGDGGQ---DVADGEPGELlisgpssaTMYWNNRAKSRD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 463 -FDGYVSESatskkiahsvfskgdsaylsGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLsrllgqtdvavyg 541
Cdd:TIGR02262 380 tFQGEWTRS--------------------GDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESAL------------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 542 VAVPGVEgKAGMAAVADPHSLLDPNA----------IYQELQK----VLAPYARPIFLRLLPQVDTTGTFKIQKTRLqRE 607
Cdd:TIGR02262 427 IQHPAVL-EAAVVGVADEDGLIKPKAfvvlrpgqtaLETELKEhvkdRLAPYKYPRWIVFVDDLPKTATGKIQRFKL-RE 504
|
.
gi 38524616 608 G 608
Cdd:TIGR02262 505 G 505
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-599 |
5.37e-25 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 108.97 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 82 FQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:cd17651 1 FERQAARTPDAPALVAEGR--RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LRREPLAFCLGTSGAKAlifggemVAAVAEVsghlgkslikfcSGDLGPEGILPdthLLDPLLKEASTAPLAQIPSKGMD 241
Cdd:cd17651 79 YPAERLAFMLADAGPVL-------VLTHPAL------------AGELAVELVAV---TLLDQPGAAAGADAEPDPALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSR-----YYRMAAFGHHAYR--MQAADVLYDClplyhSAGNIIGVgqcLIYGLTVVLR 314
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRSlanlvAWQARASSLGPGArtLQFAGLGFDV-----SVQEIFST---LCAGATLVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 K---KFSASRFWDDCIKYNCTVV----QYIGEICRYLLKQPVREAERRHRV----RLAVGNGLRpaiweEFTERFGVRQI 383
Cdd:cd17651 209 PeevRTDPPALAAWLDEQRISRVflptVALRALAEHGRPLGVRLAALRYLLtggeQLVLTEDLR-----EFCAGLPGLRL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEFYGATEcncsiaNMDGKVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQglciPCQAGEPG-LLVGqinqQDPLRR 462
Cdd:cd17651 284 HNHYGPTE------THVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR----PVPPGVPGeLYIG----GAGLAR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 463 fdGYVSESA-TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVyg 541
Cdd:cd17651 350 --GYLNRPElTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV-- 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 542 VAVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKI 599
Cdd:cd17651 426 LAREDRPGEKRLVAyvVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-605 |
1.68e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 108.20 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK06178 44 RERPQRPAIIFYGH--VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 167 LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCS-GDLGPEGI---LPDTHLLDPLLKE----------ASTAPl 232
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSlADVLPAEPtlpLPDSLRAPRLAAAgaidllpalrACTAP- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 233 AQIPSKGMDDRLFYIYTSGTTGLPKAaiVVHSR---YYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGL 309
Cdd:PRK06178 201 VPLPPPALDALAALNYTGGTTGMPKG--CEHTQrdmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 310 TVVLRKKFSASRFWDDCIKYNCT----VVQYIGEICRY---------LLKQP-----VRE--AERRHRVRLAVGNGLRPA 369
Cdd:PRK06178 279 TLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVELMDHprfaeydlsSLRQVrvvsfVKKlnPDYRQRWRALTGSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 370 IW--------EEFTERFgvrQIGEFygatecncsiaNMDGKVGSCGfnsriLPhVYPIRLVKVNEDTMELLrdaqglciP 441
Cdd:PRK06178 359 AWgmtethtcDTFTAGF---QDDDF-----------DLLSQPVFVG-----LP-VPGTEFKICDFETGELL--------P 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 442 C-QAGE-----PGLLVGQINQQDplrrfdgyvsesATSKKIAhsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR 515
Cdd:PRK06178 411 LgAEGEivvrtPSLLKGYWNKPE------------ATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 516 GENVSTTEVEGvlsrLLGQTDvAVYGVAVPGV--EGKaGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIfLRLLP 589
Cdd:PRK06178 472 GMSVFPSEVEA----LLGQHP-AVLGSAVVGRpdPDK-GQVPVAfvqlKPGADLTAAALQAWCRENMAVYKVPE-IRIVD 544
|
570
....*....|....*.
gi 38524616 590 QVDTTGTFKIQKTRLQ 605
Cdd:PRK06178 545 ALPMTATGKVRKQDLQ 560
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
104-606 |
9.55e-24 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 103.97 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKalifgg 183
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 emvaavaevsghlgkslikfcsgdlgpegiLPDTHLLdpllkeastaplaqipskgmddrlfyIYTSGTTGLPKAAIVvh 263
Cdd:cd05912 76 ------------------------------LDDIATI--------------------------MYTSGTTGKPKGVQQ-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 264 sryyrmaAFGHHAYRMQAADV---LYD------CLPLYHSAGNIIGVGQcLIYGLTVVLRKKFSASRFWDDCIKYNCTVV 334
Cdd:cd05912 98 -------TFGNHWWSAIGSALnlgLTEddnwlcALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 335 QYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTER-FGVRQIgefYGATE-----CNCSIANMDGKVGSCGf 408
Cdd:cd05912 170 SVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIPVYQS---YGMTEtcsqiVTLSPEDALNKIGSAG- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 409 nsRILPHVYpirlvkvnedtmelLRDAQGLCIPCQAGE-----PGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSK 483
Cdd:cd05912 246 --KPLFPVE--------------LKIEDDGQPPYEVGEillkgPNVTKGYLNRPD------------ATEESFENGWFKT 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 484 GDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPgvEGKAGMAAVA--DPHS 561
Cdd:cd05912 298 GDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV--VGIP--DDKWGQVPVAfvVSER 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 38524616 562 LLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLQR 606
Cdd:cd05912 367 PISEEELIAYCSEKLAKYKVPkkiYFVDELPR---TASGKLLRHELKQ 411
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-311 |
1.13e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 105.57 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALV--DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 152 GmeaaLLNV----NLRREPLAFCLGTSGAKALIFGG-EMVAAVAEVSGHLGkSLIKFCSGDLGPEGILPDTHLLDPLLKE 226
Cdd:COG1022 89 G----AVTVpiypTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELP-SLRHIVVLDPRGLRDDPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 227 ASTAPL-----AQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGV 301
Cdd:COG1022 164 GREVADpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSY 243
|
250
....*....|
gi 38524616 302 GqCLIYGLTV 311
Cdd:COG1022 244 Y-ALAAGATV 252
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
105-604 |
1.50e-23 |
|
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: 104.00 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI---- 180
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVvper 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 181 FGGEMVAAvaevsghlgkslikfcsgdlgpegiLPDThlldpllkeastapLAQIpskgmddrlfyIYTSGTTGLPKAai 260
Cdd:cd05903 83 FRQFDPAA-------------------------MPDA--------------VALL-----------LFTSGTTGEPKG-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 261 VVHSRYYRMAAFGHHAYRMQA--ADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQ--- 335
Cdd:cd05903 111 VMHSHNTLSASIRQYAERLGLgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMgat 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 336 -YIGEICRYLLKQPvrEAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECNcsianmdGKVGSC-------- 406
Cdd:cd05903 191 pFLTDLLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP-------GAVTSItpapedrr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 407 -GFNSRILPHVYpirlVKVNEDTMELLRdaqglciPCQAGE-----PGLLVGQINQQDPLRRFDgyvsesatskkiahsv 480
Cdd:cd05903 261 lYTDGRPLPGVE----IKVVDDTGATLA-------PGVEGEllsrgPSVFLGYLDRPDLTADAA---------------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 481 fskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPgvEGKAGMAAVA--- 557
Cdd:cd05903 314 ---PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV--VALP--DERLGERACAvvv 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 38524616 558 --DPHSL-LDPNAIYQELQKVlAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05903 387 tkSGALLtFDELVAYLDRQGV-AKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-582 |
2.66e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 79 PRIF---QAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEA 155
Cdd:PRK05852 16 PRIAdlvEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 156 ALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFcSGDLGPEGILPDTHLLDpllkEASTAPLAQI 235
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNV-GGDSGPSGGTLSVHLDA----ATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 236 PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRyyrMAAFGHH---AYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK05852 171 PEGLRPDDAMIMFTGGTTGLPKMVPWTHAN---IASSVRAiitGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 L--RKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL----AVGNGLRPAIWEEFTERFGVRQIgEF 386
Cdd:PRK05852 248 LpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrfirSCSAPLTAETAQALQTEFAAPVV-CA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 387 YGATECNCSIANMDGKVGSCGFNSRILPHVypirlvkVNEDTMELLRDAQGLCIPCQAGEpgllVGQINQQDP--LRrfd 464
Cdd:PRK05852 327 FGMTEATHQVTTTQIEGIGQTENPVVSTGL-------VGRSTGAQIRIVGSDGLPLPAGA----VGEVWLRGTtvVR--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 465 GYVSESA-TSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVA 543
Cdd:PRK05852 393 GYLGDPTiTAANFTDGWLRTGDLGSLSAA-------GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 38524616 544 vPGVEGKAgMAAVADPHSLLDPNA--IYQELQKVLAPYARP 582
Cdd:PRK05852 466 -DQLYGEA-VAAVIVPRESAPPTAeeLVQFCRERLAAFEIP 504
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
86-607 |
3.23e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.06 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVDaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:PRK06087 33 ARAMPDKIAVVD-NHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIFGG--------EMVAAVAEVSGHLGKSLIkfcSGDLGPEgilpdthLLDPLLKE--ASTAPLAQI 235
Cdd:PRK06087 112 ELVWVLNKCQAKMFFAPTlfkqtrpvDLILPLQNQLPQLQQIVG---VDKLAPA-------TSSLSLSQiiADYEPLTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 236 PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYrmaaFGHHAY----RMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTV 311
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL----ASERAYcarlNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 312 VLRKKFSAsrfwDDCI----KYNCTVVQ----YIGEICRYLLKQPVREAERrhRVRLAVGNGLRPAIWEEFTERfGVRqI 383
Cdd:PRK06087 258 VLLDIFTP----DACLalleQQRCTCMLgatpFIYDLLNLLEKQPADLSAL--RFFLCGGTTIPKKVARECQQR-GIK-L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEFYGATE-CNCSIANMDGKVGSCGFNSRILPHVYPIRLvkVNEDTMELLRDAQGLciPCQAGePGLLVGQINQQDplrr 462
Cdd:PRK06087 330 LSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKV--VDEARKTLPPGCEGE--EASRG-PNVFMGYLDEPE---- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 463 fdgyvsesATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygV 542
Cdd:PRK06087 401 --------LTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV--V 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38524616 543 AVP----GvEGKAGMAAVADPH---SLLDPNAIYQElqKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK06087 465 AMPderlG-ERSCAYVVLKAPHhslTLEEVVAFFSR--KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
86-577 |
4.80e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 103.81 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:cd17634 63 LRENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkSLIKFCSGDLGPEGILPDTHLL------------------DPL 223
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGGVRAGRSV------PLKKNVDDALNPNVTSVEHVIVlkrtgsdidwqegrdlwwRDL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 224 LKEAStaPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYRMQAADVLYDCLPLYHSAGNIIGVG 302
Cdd:cd17634 217 IAKAS--PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYWCTADVGWVTGHSYLLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 303 QCLIYGLTVVLRKKF----SASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL----AVGNGLRPAIWEEF 374
Cdd:cd17634 295 GPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLrilgSVGEPINPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 375 TERFGVRQigefygatecnCSIANMDGKVGSCGFNSRILPHVYPIR----LVKVNEDTMELLrDAQGLciPCQAGEPGLL 450
Cdd:cd17634 375 WKKIGKEK-----------CPVVDTWWQTETGGFMITPLPGAIELKagsaTRPVFGVQPAVV-DNEGH--PQPGGTEGNL 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 451 V------GQINQ--QDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTT 522
Cdd:cd17634 441 VitdpwpGQTRTlfGDHERFEQTY--------------FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 523 EVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQKVLA 577
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
106-604 |
8.10e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 102.47 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 106 FAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEM 185
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 186 VAAVAevsGHLGKSlIKFCSGDLGPEGI----LPDTHL--------LDPLLK--EASTAPLAQIPSKgmddrlfYIYTSG 251
Cdd:PRK12406 94 LHGLA---SALPAG-VTVLSVPTPPEIAaayrISPALLtppagaidWEGWLAqqEPYDGPPVPQPQS-------MIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 252 TTGLPK-----AAIVVHSRYY-RMAAfghHAYRMQAADVLYDCLPLYHSAGNIIGVgQCLIYGLTVVLRKKFSASRFWDD 325
Cdd:PRK12406 163 TTGHPKgvrraAPTPEQAAAAeQMRA---LIYGLKPGIRALLTGPLYHSAPNAYGL-RAGRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 326 CIKYNCTVVQYIGEICRYLLKQPvreAERRHRVRL----AVGNGLRPA---IWEEFTERFG-VrqIGEFYGATE------ 391
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLP---EEVRAKYDVsslrHVIHAAAPCpadVKRAMIEWWGpV--IYEYYGSTEsgavtf 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 392 CNCSIA-NMDGKVGscgfnsRILPHVypiRLVKVNEDTMELlrdaqglcipcQAGEPGLLVGQInQQDPLRRFDGYVSES 470
Cdd:PRK12406 314 ATSEDAlSHPGTVG------KAAPGA---ELRFVDEDGRPL-----------PQGEIGEIYSRI-AGNPDFTYHNKPEKR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 471 ATSKKiahsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVE-G 549
Cdd:PRK12406 373 AEIDR---------GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 550 KAGMAAV-ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK12406 442 EALMAVVePQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
74-392 |
1.43e-22 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 103.40 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGm 153
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFGD--QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 154 eAAL--LNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLgkslikfcsgdlgpegILPDTHLLDPllkEASTAP 231
Cdd:COG1020 551 -AAYvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPV----------------LALDALALAA---EPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 232 LAQIPSkgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVlydcLPLYHSAGNIIGVGQ---CLIY 307
Cdd:COG1020 611 PVPVTP----DDLAYvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR----VLQFASLSFDASVWEifgALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 308 GLTVVLRKK---FSASRFWDDCIKYNCTVVQYIGEICRYLLKQPvreAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQ 382
Cdd:COG1020 683 GATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLvgGEALPPELVRRWRARLPGAR 759
|
330
....*....|
gi 38524616 383 IGEFYGATEC 392
Cdd:COG1020 760 LVNLYGPTET 769
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
87-607 |
1.43e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 101.50 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--R 164
Cdd:PRK06145 13 RRTPDRAALVYRD--QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLG--AVFLPINYRlaA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 165 EPLAFCLGTSGAKALIFGGEMVAAVAEVSghlgkslikfcsgdlgPEGILPDTHLLDPLLKEASTAPLAQIPSKGMDDRL 244
Cdd:PRK06145 89 DEVAYILGDAGAKLLLVDEEFDAIVALET----------------PKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHsagniigVGQCLIYGLTVV-------LRKKF 317
Cdd:PRK06145 153 RLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYH-------VGAFDLPGIAVLwvggtlrIHREF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 318 SASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLR-PAI-WEEFTERFGVRQIGEFYGATECNCS 395
Cdd:PRK06145 226 DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKtPESrIRDFTRVFTRARYIDAYGLTETCSG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IANMDG-----KVGSCGfnsRILPHVypirlvkvnedTMELLRDAQGLCIPCQAGEPGLLVGQINQqdplrrfdGYVSES 470
Cdd:PRK06145 306 DTLMEAgreieKIGSTG---RALAHV-----------EIRIADGAGRWLPPNMKGEICMRGPKVTK--------GYWKDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 471 atsKKIAHSVFskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGK 550
Cdd:PRK06145 364 ---EKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGER 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 551 AGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK06145 438 ITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
72-606 |
1.90e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 101.37 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 72 QRAGHTIPRIFQAVVQRQPERLALVD-AGTgecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK 150
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDeLGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 151 AGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAevsghlgksliKFCSGDLGPEGILPDTHLLDPLLKEA-ST 229
Cdd:PRK13382 116 IGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD-----------RALADCPQATRIVAWTDEDHDLTVEVlIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 230 APLAQ-IPSKGMDDRLFyIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAgniiGVGQCLIYG 308
Cdd:PRK13382 185 AHAGQrPEPTGRKGRVI-LLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAW----GFSQLVLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 309 L---TVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPV----REAERRHRVRLAVGNGLRPAIWEEFTERFGvR 381
Cdd:PRK13382 260 SlacTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevrnRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-D 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 382 QIGEFYGATECN-CSIANMDgkvgscgfNSRILPHVYPirlvKVNEDTMELLRDAQGLCIPcqAGEpgllVGQINQQDPL 460
Cdd:PRK13382 339 VIYNNYNATEAGmIATATPA--------DLRAAPDTAG----RPAEGTEIRILDQDFREVP--TGE----VGTIFVRNDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 461 rRFDGYVseSATSKKIAHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY 540
Cdd:PRK13382 401 -QFDGYT--SGSTKDFHDGFMASGDVGYL-------DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVI 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 541 GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:PRK13382 471 GVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
99-607 |
2.19e-22 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 101.39 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 99 GTGE--CWTFAQLDAYSNAVANLFRQL-GFAPGDVVAIFLEGRPEFvglWLgLAKAGMEAALL----NVNLRREPLAFCL 171
Cdd:cd05928 35 GKGDevKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEW---WL-VNVACIRTGLVfipgTIQLTAKDILYRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 172 GTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPdthlLDPLLKEASTAPLAqIPSKGMDDRLFYiYTSG 251
Cdd:cd05928 111 QASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLN----FKELLNEASTEHHC-VETGSQEPMAIY-FTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 252 TTGLPKAAIVVHSRY-YRMAAFGHHAYRMQAADVLYdCLPLYHSAGNIIG-VGQCLIYGLTVVLRK--KFSASRFWDDCI 327
Cdd:cd05928 185 TTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMW-NTSDTGWIKSAWSsLFEPWIQGACVFVHHlpRFDPLVILKTLS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 328 KYNCTVVQYIGEICRYLLKQPVREAERRH-RVRLAVGNGLRPAIWEEFTERFGVrQIGEFYGATECNCSIANMDG---KV 403
Cdd:cd05928 264 SYPITTFCGAPTVYRMLVQQDLSSYKFPSlQHCVTGGEPLNPEVLEKWKAQTGL-DIYEGYGQTETGLICANFKGmkiKP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 404 GSCGFNSriLPhvYPIRLVKVNEDTMEllrdaqglciPCQAGEPGLlvgQINQQDPLRRFDGYVSE-SATSKKIahsvfs 482
Cdd:cd05928 343 GSMGKAS--PP--YDVQIIDDNGNVLP----------PGTEGDIGI---RVKPIRPFGLFSGYVDNpEKTAATI------ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 483 KGDsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAV--ADPH 560
Cdd:cd05928 400 RGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVVKAFVvlAPQF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 38524616 561 SLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:cd05928 478 LSHDPEQLTKELQqhvkSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
87-612 |
2.71e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 100.89 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLWlglAKAGMEAALLNVNLRRE 165
Cdd:PRK07470 18 RRFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQmFESMF---AAFRLGAVWVPTNFRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 P--LAFCLGTSGAKALIFGG---EMVAAVAEVSGHLgKSLIKFCSGDLGPEgilpdthlLDPLLKEASTAPlAQIPSKGM 240
Cdd:PRK07470 93 PdeVAYLAEASGARAMICHAdfpEHAAAVRAASPDL-THVVAIGGARAGLD--------YEALVARHLGAR-VANAAVDH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 241 DDRLFYIYTSGTTGLPKAAIVVHSryyRMaAF---GHHAYRMQA---ADVLYDCLPLYHSAGniigvgqclIYGLTVVLR 314
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHG---QM-AFvitNHLADLMPGtteQDASLVVAPLSHGAG---------IHQLCQVAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 ---------KKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGlrPAIWEEFTERfGVRQIG- 384
Cdd:PRK07470 230 gaatvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG--APMYRADQKR-ALAKLGk 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 385 ---EFYGATECNCSIANM--------DG---KVGSCGFnsrilphvypirlvkvnEDT-MEL-LRDAQGLciPCQAGEpg 448
Cdd:PRK07470 307 vlvQYFGLGEVTGNITVLppalhdaeDGpdaRIGTCGF-----------------ERTgMEVqIQDDEGR--ELPPGE-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 449 llVGQINQQDPlRRFDGYVSES-ATSKKIAHSVFSKGDSAYlsgdvlvMDELGYMYFRDRSGDTFRWRGENVSTTEVEGV 527
Cdd:PRK07470 366 --TGEICVIGP-AVFAGYYNNPeANAKAFRDGWFRTGDLGH-------LDARGFLYITGRASDMYISGGSNVYPREIEEK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 528 LSRLLGQTDVAVYGVAVPgVEGKAGMAA-VADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKtR 603
Cdd:PRK07470 436 LLTHPAVSEVAVLGVPDP-VWGEVGVAVcVARDGAPVDEAELLAWLDGKVARYKLPkrfFFWDALPK---SGYGKITK-K 510
|
....*....
gi 38524616 604 LQREGFDPR 612
Cdd:PRK07470 511 MVREELEER 519
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
68-551 |
2.80e-22 |
|
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: 101.41 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 68 LRRHQRAGHTiprifQAVVQRQPERlalvdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLG 147
Cdd:cd05968 67 LDKWLADTRT-----RPALRWEGED------GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 148 LAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSghLGKSLIKFCSGDLGPEGILPDTHLLDPLLK-- 225
Cdd:cd05968 136 VARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVN--LKEEADKACAQCPTVEKVVVVRHLGNDFTPak 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 226 -------EASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYRMQAADVLYDCLPLYHSAGN 297
Cdd:cd05968 214 grdlsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDmYFQFDLKPGDLLTWFTDLGWMMGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 298 IIGVGQcLIYGLTVVLRKKF----SASRFWDDCIKYNCTVVQYIGEICRYLL---KQPVReAERRHRVRLAVGNG--LRP 368
Cdd:cd05968 294 WLIFGG-LILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVN-AHDLSSLRVLGSTGepWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 369 AIWEEFTERFGVRQ--IGEFYGATECNCSI--ANMDGKVGSCGFNSrILPHVYPIRLvkvnedtmellrDAQGLCIPCQA 444
Cdd:cd05968 372 EPWNWLFETVGKGRnpIINYSGGTEISGGIlgNVLIKPIKPSSFNG-PVPGMKADVL------------DESGKPARPEV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 445 GE-------PGLLVGqiNQQDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 517
Cdd:cd05968 439 GElvllapwPGMTRG--FWRDEDRYLETY--------------WSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGK 502
|
490 500 510
....*....|....*....|....*....|....
gi 38524616 518 NVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKA 551
Cdd:cd05968 503 RVGPAEIESVLNAHPAVLESAAIGVPHP-VKGEA 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
243-599 |
3.28e-22 |
|
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: 97.86 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 243 RLFYI-YTSGTTGLPKAaivvhsrYYR-----MAAF--GHHAYRMQAADVLYDCLPLYHSaGNIIGVGQCLIYGLTVVLR 314
Cdd:cd17633 1 NPFYIgFTSGTTGLPKA-------YYRserswIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 KKFSASRFWDDCIKYNCTVVQYIGEicryLLKQPVREAERRHRVR--LAVGNGLRPAIWEEFTERFGVRQIGEFYGATEC 392
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 393 NCSIANMDG---KVGSCGfnsRILPHVyPIRLvkvnedtmellRDAQGlcipcqaGEPGLLVGQINQqdplrRFDGYVSE 469
Cdd:cd17633 149 SFITYNFNQesrPPNSVG---RPFPNV-EIEI-----------RNADG-------GEIGKIFVKSEM-----VFSGYVRG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 470 SATSKkiaHSVFSKGDSAYLsgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVEG 549
Cdd:cd17633 202 GFSNP---DGWMSVGDIGYV-------DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG--IPDARF 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 550 KAGMAAVADPHSLLDPNaIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKI 599
Cdd:cd17633 270 GEIAVALYSGDKLTYKQ-LKRFLKQKLSRYEIPkkiIFVDSLPY---TSSGKI 318
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
113-599 |
9.71e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 98.67 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 113 SNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAlifGGEMVAAVAEV 192
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADA---GGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 193 SGHLGKSLIKFCSGD--LGPEGILPDTHLLDpllkeastaplAQIPSKgmDDRLFYIYTSGTTGLPKAAIVVHsRYYRMA 270
Cdd:cd05922 80 ADRLRDALPASPDPGtvLDADGIRAARASAP-----------AHEVSH--EDLALLLYTSGSTGSPKLVRLSH-QNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 271 AFGHHAY-RMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRKKFSASR-FWDDCIKYNCT---VVQYIGEICRYLL 345
Cdd:cd05922 146 ARSIAEYlGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 346 KQPVREAERRHRVRlaVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDG-----KVGSCGfnsRILPhvypir 420
Cdd:cd05922 225 FDPAKLPSLRYLTQ--AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPerileKPGSIG---LAIP------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 421 lvkvnEDTMELLRDAQGLCIPcqaGEPGLLVgqinQQDPLRRFDGYVSESATSKKIAhsvfsKGDSAYlSGDVLVMDELG 500
Cdd:cd05922 294 -----GGEFEILDDDGTPTPP---GEPGEIV----HRGPNVMKGYWNDPPYRRKEGR-----GGGVLH-TGDLARRDEDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 501 YMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEgkaGMAAVADPHSLLDPNAIYQELQKVLAPYA 580
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDKIDPKDVLRSLAERLPPYK 432
|
490
....*....|....*....
gi 38524616 581 RPIFLRLLPQVDTTGTFKI 599
Cdd:cd05922 433 VPATVRVVDELPLTASGKV 451
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
104-545 |
1.12e-21 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 98.34 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIfgg 183
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 emvaavaevsghlgkslikfcsgdlgpegilpdTHlldPLLKEASTaplaqipskgMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05969 78 ---------------------------------TT---EELYERTD----------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 264 SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK-KFSASRFWDDCIKYNCTVVQYIGEICR 342
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 343 YLLK---QPVREAERRH-RVRLAVGNGLRPAI--WEEftERFGVRqIGEFYGATECNC-SIAN---MDGKVGSCGfnsRI 412
Cdd:cd05969 192 MLMKegdELARKYDLSSlRFIHSVGEPLNPEAirWGM--EVFGVP-IHDTWWQTETGSiMIANypcMPIKPGSMG---KP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 413 LPHVypiRLVKVNEDTMELLRDAQGLcIPCQAGEPGLLVGQINQQDplrRFDGYvsesatskkiahsvFSKGdsAYLSGD 492
Cdd:cd05969 266 LPGV---KAAVVDENGNELPPGTKGI-LALKPGWPSMFRGIWNDEE---RYKNS--------------FIDG--WYLTGD 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 493 VLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP 545
Cdd:cd05969 323 LAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP 375
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
101-604 |
1.59e-21 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 97.93 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGtsgaKAL 179
Cdd:cd05958 8 EREWTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 180 IfggemvaAVAevsghlgkslikfcsgdlgpegilpdthlldpLLKEASTAplaqipskgMDDRLFYIYTSGTTGLPKAA 259
Cdd:cd05958 84 I-------TVA--------------------------------LCAHALTA---------SDDICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 260 IVVHSRYYRMA-AFGHHAYRMQAADVLYDCLPLYHSagniIGVGQCLIY----GLTVVLRKKFSASRFWDDCIKYNCTVV 334
Cdd:cd05958 116 MHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFT----FGLGGVLLFpfgvGASGVLLEEATPDLLLSAIARYKPTVL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 335 QYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIgEFYGATEC-NCSIANMDG--KVGSCGfn 409
Cdd:cd05958 192 FTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPII-DGIGSTEMfHIFISARPGdaRPGATG-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 410 sRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPGLLVgqinqqdplrrfdgyvsesATSKKIAHSVFSKGDSAYL 489
Cdd:cd05958 269 -KPVPG-YEAKVV-----------DDEGNPVP--DGTIGRLA-------------------VRGPTGCRYLADKRQRTYV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 490 ------SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP--GVEGKAGMaaVADPHS 561
Cdd:cd05958 315 qggwniTGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDEsrGVVVKAFV--VLRPGV 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 38524616 562 LLDPnAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05958 393 IPGP-VLARELQdhakAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
75-312 |
1.59e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 95.65 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 75 GHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGme 154
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 155 AALLNVN--LRREPLAFCLGTSGAKALIFGG--------EMVAAVA-----EVSGHLG-------KSLIKFcsGDLGPEG 212
Cdd:PRK08315 93 AILVTINpaYRLSELEYALNQSGCKALIAADgfkdsdyvAMLYELApelatCEPGQLQsarlpelRRVIFL--GDEKHPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 213 ILPDTHLLDpLLKEASTAPLAQIPSK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPL 291
Cdd:PRK08315 171 MLNFDELLA-LGRAVDDAELAARQATlDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL 249
|
250 260
....*....|....*....|.
gi 38524616 292 YHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK08315 250 YHCFGMVLGNLACVTHGATMV 270
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
83-604 |
1.88e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 95.20 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 83 QAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:PRK06164 17 DAHARARPDAVALIDEDR--PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 163 RREPLAFCLGTSGAKALI----FGG----EMVAAVAEVSGHLGKSLIKFCSG-DLGPEGILPDTHLLDPLlkEASTAPLA 233
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVvwpgFKGidfaAILAAVPPDALPPLRAIAVVDDAaDATPAPAPGARVQLFAL--PDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 234 QIPSKGMDDRLFYIY-TSGTTGLPKaaIVVHsryyRMAAFGHH------AYRMQAADVLYDCLPLYHSAGnIIGVGQCLI 306
Cdd:PRK06164 173 AGERAADPDAGALLFtTSGTTSGPK--LVLH----RQATLLRHaraiarAYGYDPGAVLLAALPFCGVFG-FSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 307 YGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNgLRPAiWEEFTERfgVRQIGE- 385
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPA-LGELAAL--ARARGVp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 386 ---FYGATECncsIANMDGKVGSCGFNSRILPHVYPIR---LVKVnedtmellRDAQ--GLCIPCQAGE-----PGLLVG 452
Cdd:PRK06164 322 ltgLYGSSEV---QALVALQPATDPVSVRIEGGGRPASpeaRVRA--------RDPQdgALLPDGESGEieiraPSLMRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 453 QINQQDPLRRF---DGYvsesatskkiahsvFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLS 529
Cdd:PRK06164 391 YLDNPDATARAltdDGY--------------FRTGDLGYTRGD-------GQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 530 RLLGQTDVAVYGVAvpgVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPY---ARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK06164 450 ALPGVAAAQVVGAT---RDGKTVPVAfvIPTDGASPDEAGLMAACREALAGFkvpARVQVVEAFPVTESANGAKIQKHRL 526
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-542 |
7.52e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 93.51 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 71 HQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvglwlglAK 150
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVLGDTR--LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE--------VL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 151 AGMEAALLnVNLRREPL---------AFCLGTSGAKALIF--------GGEMVAAVAEVSGHLGkslikfcsgdLGPEGI 213
Cdd:PRK06188 77 MAIGAAQL-AGLRRTALhplgslddhAYVLEDAGISTLIVdpapfverALALLARVPSLKHVLT----------LGPVPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 214 LPDthlldpLLKEASTAPLAQIPSKGMDDRLFYI-YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLY 292
Cdd:PRK06188 146 GVD------LLAAAAKFGPAPLVAAALPPDIAGLaYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 293 HSAGNIIGVGqcLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQP-VREAERRHRVRLAVG-NGLRPAI 370
Cdd:PRK06188 220 HAGGAFFLPT--LLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPdLRTRDLSSLETVYYGaSPMSPVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 371 WEEFTERFGvrQI-GEFYGATECNCSIANMD---------GKVGSCGFnsrilphvyPIRLVKVnedtmELLrDAQGLCI 440
Cdd:PRK06188 298 LAEAIERFG--PIfAQYYGQTEAPMVITYLRkrdhdpddpKRLTSCGR---------PTPGLRV-----ALL-DEDGREV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 441 PcqAGEPgllvGQINQQDPLrRFDGYVSE-SATSKkiahsVFSKGdsaYL-SGDVLVMDELGYMYFRDRSGDTFRWRGEN 518
Cdd:PRK06188 361 A--QGEV----GEICVRGPL-VMDGYWNRpEETAE-----AFRDG---WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFN 425
|
490 500
....*....|....*....|....
gi 38524616 519 VSTTEVEGVLSRLLGQTDVAVYGV 542
Cdd:PRK06188 426 VFPREVEDVLAEHPAVAQVAVIGV 449
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
105-599 |
7.64e-20 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 92.54 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 mvaavaevsghlgkslikfcsgdlgpegiLPDthlldpllkeastapLAQIPskgmddrlfyiYTSGTTGLPKAAIVVHS 264
Cdd:cd05935 83 -----------------------------LDD---------------LALIP-----------YTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 265 RYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYL 344
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 345 LKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRQIgEFYGATEcNCSIANMDgkvgscgfnsrilPHVYPIR-- 420
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTGLRFV-EGYGLTE-TMSQTHTN-------------PPLRPKLqc 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 421 LVKVNEDTMELLRDAQGLcIPCQAGEpgllVGQINQQDPlRRFDGYVS-ESATSKKIahsVFSKGDSAYLSGDVLVMDEL 499
Cdd:cd05935 253 LGIP*FGVDARVIDIETG-RELPPNE----VGEIVVRGP-QIFKGYWNrPEETEESF---IEIKGRRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 500 GYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADP--HSLLDPNAIYQELQKVLA 577
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQMA 403
|
490 500
....*....|....*....|....*
gi 38524616 578 PYARP---IFLRLLPQvdtTGTFKI 599
Cdd:cd05935 404 AYKYPrevEFVDELPR---SASGKI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
105-539 |
1.56e-19 |
|
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: 91.17 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFA-PGDVVAIFLEGRPEFVGLWLGLAKAGmeAA--LLNVNLRREPLAFCLGTSGAKALIF 181
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAG--AAyvPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 182 GGEMVAAVAevsghlgkslikfcsgDLGPEGILPDThLLDPLLKEASTAPLAQIPSKGmDDRLFYIYTSGTTGLPKAAIV 261
Cdd:TIGR01733 79 DSALASRLA----------------GLVLPVILLDP-LELAALDDAPAPPPPDAPSGP-DDLAYVIYTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 262 VH----------SRYY------RMAAFGHHAYRMQAADVLydcLPLYHsagniigvGQCLIYGLTVVLRKKFSASRFWDD 325
Cdd:TIGR01733 141 THrslvnllawlARRYgldpddRVLQFASLSFDASVEEIF---GALLA--------GATLVVPPEDEERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 326 ciKYNCTVVQYIGEICRYLLKQPVREAERRHRVrLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNcsianmdgkVGS 405
Cdd:TIGR01733 210 --EHPVTVLNLTPSLLALLAAALPPALASLRLV-ILGGEALTPALVDRWRARGPGARLINLYGPTETT---------VWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 406 CGFnsrILPHVYPIRLVKVN-----EDTMELLRDAQGLciPCQAGEPG-LLVGQINqqdpLRRfdGYVS-ESATSKKIAH 478
Cdd:TIGR01733 278 TAT---LVDPDDAPRESPVPigrplANTRLYVLDDDLR--PVPVGVVGeLYIGGPG----VAR--GYLNrPELTAERFVP 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38524616 479 SVFSKGDSA--YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:TIGR01733 347 DPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
91-542 |
3.86e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.50 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 91 ERLAL--VDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLeGR-PEFVGLWLGLAKAGMEAALLNVNLRREPL 167
Cdd:PRK04319 59 DKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFM-PRiPELYFALLGALKNGAIVGPLFEAFMEEAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 168 AFCLGTSGAKALIFGGEMVA-AVAEVSGHLGKSLIkfcSGDLGPEGilPDTHLLDPLLKEASTAplAQIPSKGMDDRLFY 246
Cdd:PRK04319 138 RDRLEDSEAKVLITTPALLErKPADDLPSLKHVLL---VGEDVEEG--PGTLDFNALMEQASDE--FDIEWTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSryyrmAAFGHHA---YRM--QAADVlYDClplyhSA------GNIIGVGQCLIYGLT-VVLR 314
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHN-----AMLQHYQtgkYVLdlHEDDV-YWC-----TAdpgwvtGTSYGIFAPWLNGATnVIDG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 KKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRH----RVRLAVGNGLRP-AI-WEEftERFGVRqIGEFYG 388
Cdd:PRK04319 280 GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDlsslRHILSVGEPLNPeVVrWGM--KVFGLP-IHDNWW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 389 ATECNCS-IAN---MDGKVGSCGfnsRILPHVYpIRLVKVNEDtmELLRDAQG-LCIpcQAGEPGLLVGQINQQDplrRF 463
Cdd:PRK04319 357 MTETGGImIANypaMDIKPGSMG---KPLPGIE-AAIVDDQGN--ELPPNRMGnLAI--KKGWPSMMRGIWNNPE---KY 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 464 DGYvsesatskkiahsvFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlSRLLGQTDVAVYGV 542
Cdd:PRK04319 426 ESY--------------FAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE---SKLMEHPAVAEAGV 485
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
80-604 |
4.13e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 90.72 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 80 RIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLN 159
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS--LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG--AAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VNLR--REPLAFCLGTSGAKALIFGGEMVAAVAEvsghlgkslikfcsgdlgpegiLPDTHLLDPLLKEASTAPLAQIPS 237
Cdd:cd12117 77 LDPElpAERLAFMLADAGAKVLLTDRSLAGRAGG----------------------LEVAVVIDEALDAGPAGNPAVPVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 238 KgmDDRLFYIYTSGTTGLPKAAIV--------VHSRYYrmAAFGHHAYRMQAADVLYDClplyhSAGNIIGvgqCLIYGL 309
Cdd:cd12117 135 P--DDLAYVMYTSGSTGRPKGVAVthrgvvrlVKNTNY--VTLGPDDRVLQTSPLAFDA-----STFEIWG---ALLNGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 310 TVVLRKKfsasrfwddcikynctvvqyiGEIcryLLKQPVREAERRHRVR-LAVGNGLRPAIWEEFTERF-GVRQI---G 384
Cdd:cd12117 203 RLVLAPK---------------------GTL---LDPDALGALIAEEGVTvLWLTAALFNQLADEDPECFaGLRELltgG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 385 E---------------------FYGATE-----CNCSIANMDGKVGScgfnsriLPHVYPIRlvkvneDTMELLRDAQGl 438
Cdd:cd12117 259 EvvspphvrrvlaacpglrlvnGYGPTEnttftTSHVVTELDEVAGS-------IPIGRPIA------NTRVYVLDEDG- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 439 cIPCQAGEPG-LLVGqinqQDPLRRfdGYVSESA-TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRG 516
Cdd:cd12117 325 -RPVPPGVPGeLYVG----GDGLAL--GYLNRPAlTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 517 ENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA--VADPhsLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTT 594
Cdd:cd12117 398 FRIELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAyvVAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPLT 473
|
570
....*....|
gi 38524616 595 GTFKIQKTRL 604
Cdd:cd12117 474 ANGKVDRRAL 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-613 |
4.80e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.33 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 38 SGGWR-FLRIVCKTARRDLFGLSVLIRV--RLELRRHQRAGHTIPR------IFQAVVQRQPERLALVdAGtGECWTFAQ 108
Cdd:PRK12316 1956 DRHLLhLLEQMAEDAQAALGELALLDAGerQRILADWDRTPEAYPRgpgvhqRIAEQAARAPEAIAVV-FG-DQHLSYAE 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 109 LDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAkALIFGGEMVAA 188
Cdd:PRK12316 2034 LDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLTQRHLLE 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 189 VAEVSGHLgKSLikfcsgDLGPEGILPDThlldpllkeASTAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYR 268
Cdd:PRK12316 2113 RLPLPAGV-ARL------PLDRDAEWADY---------PDTAPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 269 MAAFGHHAYRMQAADVLYDCLPLYHSAgniiGVGQC---LIYGLTVVLR--KKFSASRFWDDCIKYNCTVVQYIGEicry 343
Cdd:PRK12316 2174 HCQAAGERYELSPADCELQFMSFSFDG----AHEQWfhpLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPV---- 2245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 344 LLKQPVREAER-RHRVRLAV----GNGLRPAIWEEFTERFGVRQIGEFYGATEcncsiANMDGKVGSCGFNSRILPHVYP 418
Cdd:PRK12316 2246 YLQQLAEHAERdGRPPAVRVycfgGEAVPAASLRLAWEALRPVYLFNGYGPTE-----AVVTPLLWKCRPQDPCGAAYVP 2320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 419 I------RLVKVNEDTMELLrdAQGLCIPCQAGEPGLLVGQINQQdplrrfdGYVSESATSKKIAHSvfskGDSAYLSGD 492
Cdd:PRK12316 2321 IgralgnRRAYILDADLNLL--APGMAGELYLGGEGLARGYLNRP-------GLTAERFVPDPFSAS----GERLYRTGD 2387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 493 VLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMA-AVADPHSLLDPNAIYQE 571
Cdd:PRK12316 2388 LARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAyVVPDDAAEDLLAELRAW 2465
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 38524616 572 LQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQ 613
Cdd:PRK12316 2466 LAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
241-545 |
4.98e-19 |
|
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: 90.47 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 241 DDRLFYIYTSGTTGLPKAAIVVHSRYY--RMAAFGHhaYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFS 318
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI--FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 319 ASRFWDDCI-KYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATEC----N 393
Cdd:cd05909 225 DYKKIPELIyDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECspviS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 394 CSIANMDGKVGSCGfnsRILPHVyPIRLVKVnedtmellrdaQGLCiPCQAGEPGLLVGQINQqdplrRFDGYVSESats 473
Cdd:cd05909 304 VNTPQSPNKEGTVG---RPLPGM-EVKIVSV-----------ETHE-EVPIGEGGLLLVRGPN-----VMLGYLNEP--- 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38524616 474 kkiAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQtDVAVYGVAVP 545
Cdd:cd05909 360 ---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE-DNEVAVVSVP 427
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-614 |
1.13e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.99 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 61 LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE 140
Cdd:PRK12467 497 RELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGE--QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 141 FVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAkALIFGGEMVAAVAEVsghlgkslikfcsgdlgPEGI--LPDTH 218
Cdd:PRK12467 575 MVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV-RLLLTQSHLLAQLPV-----------------PAGLrsLCLDE 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 219 LLDPLLKEASTAP-LAQIPskgmdDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAG 296
Cdd:PRK12467 637 PADLLCGYSGHNPeVALDP-----DNLAYvIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSML----MVSTFA 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 297 NIIGVGQ---CLIYGLTVVLRKK---FSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAI 370
Cdd:PRK12467 708 FDLGVTElfgALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 371 ---WEEFteRFGVRQIgEFYGATEcncsiANMDGKVGSCGFNSRILPHVyPIRLVKVNEDTMELLRDAQglciPCQAGEP 447
Cdd:PRK12467 788 larVRAL--GPGARLI-NHYGPTE-----TTVGVSTYELSDEERDFGNV-PIGQPLANLGLYILDHYLN----PVPVGVV 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 448 G-LLVGqinqQDPLRRfdGYVSESA-TSKKIAHSVFS-KGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEV 524
Cdd:PRK12467 855 GeLYIG----GAGLAR--GYHRRPAlTAERFVPDPFGaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEI 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 525 EgvlSRLLGQTDV--AVYgVAVPGVEGK--------AGMAAVADPHSLLDpnAIYQELQKVLAPYARPIFLRLLPQVDTT 594
Cdd:PRK12467 929 E---ARLLAQPGVreAVV-LAQPGDAGLqlvaylvpAAVADGAEHQATRD--ELKAQLRQVLPDYMVPAHLLLLDSLPLT 1002
|
570 580
....*....|....*....|.
gi 38524616 595 GTFKIQKTRL-QREGFDPRQT 614
Cdd:PRK12467 1003 PNGKLDRKALpKPDASAVQAT 1023
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
248-605 |
1.74e-18 |
|
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: 87.33 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL-RKKFSASRFWDDC 326
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 327 IKYNCTVVQ-----YIGEicrylLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIAN- 398
Cdd:cd05917 89 EKEKCTALHgvptmFIAE-----LEHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 -----MDGKVGSCGfnsRILPHVYpirlVK-VNEDTMELL-RDAQG-LCIpcqagePGLLVGQINQQDPLRrfdgyvses 470
Cdd:cd05917 164 rtddsIEKRVNTVG---RIMPHTE----AKiVDPEGGIVPpVGVPGeLCI------RGYSVMKGYWNDPEK--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 471 aTSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAvpgvEGK 550
Cdd:cd05917 222 -TAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP----DER 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 551 AGMAAVA----DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:cd05917 291 YGEEVCAwirlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
77-582 |
6.27e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 87.36 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 77 TIPRIFQAVVQRQPERLALVDAGTGEcwTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREPLAFCLGTSGAKALIFGgEMVAAVAE-----------VSGHLGKSL--------------IKFCSGDL--G 209
Cdd:PRK05605 111 EHNPLYTAHELEHPFEDHGARVAIVW-DKVAPTVErlrrttpletiVSVNMIAAMpllqrlalrlpipaLRKARAALtgP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 210 PEGILPDTHLLD-PLLKEASTAPLaqiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHH--------AYRMQ 280
Cdd:PRK05605 190 APGTVPWETLVDaAIGGDGSDVSH---PRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvpglgdgPERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 281 AAdvlydcLPLYHsagniigvgqclIYGLTVVLrkkfsasrfwddcikyncTVVQYIG------------EICRYLLKQP 348
Cdd:PRK05605 267 AA------LPMFH------------AYGLTLCL------------------TLAVSIGgelvllpapdidLILDAMKKHP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 349 -------------VREAERRHRVRLavgNGLRPAI-------------WEEFTERFGVrqigEFYGATECN----CSIAN 398
Cdd:PRK05605 311 ptwlpgvpplyekIAEAAEERGVDL---SGVRNAFsgamalpvstvelWEKLTGGLLV----EGYGLTETSpiivGNPMS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 MDGKVGSCGfnsriLPhvYP---IRLVkvNEDTMELLRDaqglciPCQAGEpgLLVgqinqQDPlRRFDGYVSESATSKK 475
Cdd:PRK05605 384 DDRRPGYVG-----VP--FPdteVRIV--DPEDPDETMP------DGEEGE--LLV-----RGP-QVFKGYWNRPEETAK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 476 IAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAA 555
Cdd:PRK05605 441 SFL------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV--VGLPREDGSEEVVA 512
|
570 580
....*....|....*....|....*....
gi 38524616 556 --VADPHSLLDPNAIYQELQKVLAPYARP 582
Cdd:PRK05605 513 avVLEPGAALDPEGLRAYCREHLTRYKVP 541
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-606 |
9.25e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 86.03 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIfgge 184
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 mvaavaevsghlgkslikfCSGDlgpegilpDTHLLDpllkeastaplaqipskgmDDRLFYIYTSGTTGLPKaAIVVHS 264
Cdd:cd05973 78 -------------------TDAA--------NRHKLD-------------------SDPFVMMFTSGTTGLPK-GVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 265 RYyrMAAFghHAYRMQAADVLYDclplyHSAGNIIGVGQCliYGL-------------TVVLRKKFSASRFWDDCIKYNC 331
Cdd:cd05973 111 RA--LAAF--GAYLRDAVDLRPE-----DSFWNAADPGWA--YGLyyaitgplalghpTILLEGGFSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 332 TVVQYIGEICRYLLKQPVrEAERRHRVRLAV----GNGLRPAIWEEFTERFGVrQIGEFYGATECNCSIANMDG-----K 402
Cdd:cd05973 180 TNLAGSPTAYRLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALGV-PIHDHYGQTELGMVLANHHAlehpvH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 403 VGSCGFnsrILPHvypIRLVKVNEDTMELLrdaqglcipcqAGEPGLLVGQINQQdPLRRFDGYvsesatskkiahsvFS 482
Cdd:cd05973 258 AGSAGR---AMPG---WRVAVLDDDGDELG-----------PGEPGRLAIDIANS-PLMWFRGY--------------QL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 483 KGDSA-----YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVA 557
Cdd:cd05973 306 PDTPAidggyYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP-ERTEVVKAFVV 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 558 DPHSLLDPNAIYQELQ----KVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05973 385 LRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
79-604 |
1.00e-17 |
|
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: 86.56 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 79 PRIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALL 158
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAG--AAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 159 NVN--LRREPLAFCLGTSGAKALIFGGEMVAAvaevsghlgkslikfcsgdlgPEGILPDTHLLDPLLKEASTAPLAQIP 236
Cdd:cd17646 77 PLDpgYPADRLAYMLADAGPAVVLTTADLAAR---------------------LPAGGDVALLGDEALAAPPATPPLVPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 237 skGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMaafgHHAYRMQAADVLYDCLPLyhsaGNIIGVGQC---LIYGL 309
Cdd:cd17646 136 --RPDNLAYVIYTSGSTGRPKGVMVTHagivNRLLWM----QDEYPLGPGDRVLQKTPL----SFDVSVWELfwpLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 310 TVVL------RKKFSASRFWDDcikYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRqI 383
Cdd:cd17646 206 RLVVarpgghRDPAYLAALIRE---HGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAE-L 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEFYGATEcnCSIANMDGKVgSCGFNSRILPHVYPI---RLVKVNEDtmelLRdaqglciPCQAGEPG-LLVGQInqqdP 459
Cdd:cd17646 282 HNLYGPTE--AAIDVTHWPV-RGPAETPSVPIGRPVpntRLYVLDDA----LR-------PVPVGVPGeLYLGGV----Q 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 LRRfdGYVSESA-TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:cd17646 344 LAR--GYLGRPAlTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 539 VygVAVPGVEGKAGMAA---VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17646 422 V--VARAAPAGAARLVGyvvPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
80-604 |
2.03e-17 |
|
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: 85.30 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 80 RIFQAVVQRQPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipsKG 239
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILL---------------------------------------------------------TN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 240 MDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAAD--VLYDCLPLYHSAGNIIgvgQCLIYGLTVVL---R 314
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADksLVYASFSFDASAWEIF---PHLTAGAALHVvpsE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 KKFSASRFWDDCIKYNCTVVQYIGEICryllKQPVREAERRHRVRLAVGNGLRPAIWEEFterfgvrQIGEFYGATECN- 393
Cdd:cd17645 180 RRLDLDALNDYFNQEGITISFLPTGAA----EQFMQLDNQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTENTv 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 394 -CSIANMDGKVGScgfnsriLPHVYPIRLVKV---NED-TMELLRDAQGLCIpcqAGEpGLLVGQINQQDplrrfdgyvs 468
Cdd:cd17645 249 vATSFEIDKPYAN-------IPIGKPIDNTRVyilDEAlQLQPIGVAGELCI---AGE-GLARGYLNRPE---------- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 469 esATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVE 548
Cdd:cd17645 308 --LTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDAD 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 549 GKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17645 384 GRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-391 |
2.15e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 85.78 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGTGecWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAgmEAALLNVN--LR 163
Cdd:PRK08314 21 RRYPDKTAIVFYGRA--ISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRA--NAVVVPVNpmNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 164 REPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDL---GPEGILPD----THLLDPL-------LKEAS 228
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYlpaEPEIAVPAwlraEPPLQALapggvvaWKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 229 TAPLAQIPSK-GMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIY 307
Cdd:PRK08314 177 AAGLAPPPHTaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 308 GLTVVLrkkfsASRfWD-----DCI-KYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNG--LRPAIWEEFTERFG 379
Cdd:PRK08314 257 GATVVL-----MPR-WDreaaaRLIeRYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERLKELTG 330
|
330
....*....|..
gi 38524616 380 VRQIgEFYGATE 391
Cdd:PRK08314 331 LDYV-EGYGLTE 341
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
69-257 |
1.03e-16 |
|
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: 83.66 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 69 RRHQRAGH----TIPRIFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGL 144
Cdd:COG1021 14 ARYREAGYwrgeTLGDLLRRRAERHPDRIAVVDGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 145 WLGLAKAGmeaaLLNVNL-----RREPLAFClGTSGAKALI----FGG----EMVAAVAEVSGHLGKSLIkfcSGDLGPE 211
Cdd:COG1021 92 FFALFRAG----AIPVFAlpahrRAEISHFA-EQSEAVAYIipdrHRGfdyrALARELQAEVPSLRHVLV---VGDAGEF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 38524616 212 gilpdtHLLDPLLKEASTAPLAQIPSkgmDDRLFYIYTSGTTGLPK 257
Cdd:COG1021 164 ------TSLDALLAAPADLSEPRPDP---DDVAFFQLSGGTTGLPK 200
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
83-607 |
2.08e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.77 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 83 QAVVQRQPERLALvdAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNL 162
Cdd:PRK06710 31 EQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 163 RREPLAFCLGTSGAKALIFGGEMVAAVAEV-SGHLGKSLIKFCSGDLGP---EGILP-----------------DTHLLD 221
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFPRVTNVqSATKIEHVIVTRIADFLPfpkNLLYPfvqkkqsnlvvkvseseTIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 222 PLLKEASTAplAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG-HHAYR-MQAADVLYDCLPLYHSAGNII 299
Cdd:PRK06710 189 SVEKEVNTG--VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQWLYNcKEGEEVVLGVLPFFHVYGMTA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 300 GVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV-GNGLRPAIWEEFTERF 378
Cdd:PRK06710 267 VMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 379 GVRQIGEFYGATECN-CSIANM--DGKV-GSCGfnsriLPhvYPirlvkvnedtmellrDAQGLCIPCQAGE---PGlLV 451
Cdd:PRK06710 347 TGGKLVEGYGLTESSpVTHSNFlwEKRVpGSIG-----VP--WP---------------DTEAMIMSLETGEalpPG-EI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 452 GQINQQDPlRRFDGYVSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRL 531
Cdd:PRK06710 404 GEIVVKGP-QIMKGYWNKPEETAAVLQ------DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 532 LGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
78-606 |
2.78e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.20 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAvvQRQPERLALVDAGTGECWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PLN02574 43 VSFIFSH--HNHNGDTALIDSSTGFSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNvnlrrePLAfclgtsgakALifgGEMVAAVAEVSGHLGKSLIKfCSGDLGPEGI----LPDTHLLDPLLKEAST--- 229
Cdd:PLN02574 121 TMN------PSS---------SL---GEIKKRVVDCSVGLAFTSPE-NVEKLSPLGVpvigVPENYDFDSKRIEFPKfye 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 230 ------APLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAA----FGHHAYRMQAADVLY-DCLPLYHSAGNI 298
Cdd:PLN02574 182 likedfDFVPK-PVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrFEASQYEYPGSDNVYlAALPMFHIYGLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 299 IGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPA---IWEEFT 375
Cdd:PLN02574 261 LFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLsgkFIQDFV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 376 ERFGVRQIGEFYGATEcncSIAnmdgkVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGE-----PGLL 450
Cdd:PLN02574 341 QTLPHVDFIQGYGMTE---STA-----VGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGElwiqgPGVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 451 VGQINqqdplrrfdgyvSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR 530
Cdd:PLN02574 413 KGYLN------------NPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 531 LLGQTDVAVYGVavpgVEGKAGMAAVA----DPHSLLDPNAIYQELQKVLAPYA---RPIFLRLLPQvdtTGTFKIQKTR 603
Cdd:PLN02574 475 HPEIIDAAVTAV----PDKECGEIPVAfvvrRQGSTLSQEAVINYVAKQVAPYKkvrKVVFVQSIPK---SPAGKILRRE 547
|
...
gi 38524616 604 LQR 606
Cdd:PLN02574 548 LKR 550
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
90-604 |
1.60e-15 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 79.43 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17650 1 PDAIAVSDATRQ--LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALifggemvaavaevsghlgkslikfcsgdlgpegilpdthLLDPllkeastaplaqipskgmDDRLFYIYT 249
Cdd:cd17650 79 MLEDSGAKLL---------------------------------------LTQP------------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 250 SGTTGLPKAAIVVHS----------RYYRMAAFGHHAyrMQAADVLYDClplyhSAGNIIgvgQCLIYGLTVVL---RKK 316
Cdd:cd17650 102 SGTTGKPKGVMVEHRnvahaahawrREYELDSFPVRL--LQMASFSFDV-----FAGDFA---RSLLNGGTLVIcpdEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 317 FSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVR-LAVGNGLRPAIW-EEFTERFGVR-QIGEFYGATECN 393
Cdd:cd17650 172 LDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFGQGmRIINSYGVTEAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 394 -------------CSIANMdgKVGSCGFNSRIL---PHVYPIRLVKVNEdtmellrdaqgLCIpcqaGEPGLLVGQINQQ 457
Cdd:cd17650 252 idstyyeegrdplGDSANV--PIGRPLPNTAMYvldERLQPQPVGVAGE-----------LYI----GGAGVARGYLNRP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 458 DplrrfdgyvsesATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDV 537
Cdd:cd17650 315 E------------LTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEA 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 538 AVygVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17650 383 VV--AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
90-545 |
2.55e-15 |
|
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: 78.88 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAAL--LNVNLRREPL 167
Cdd:cd12118 18 PDRTSIVYGDRR--YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG--AVLnaLNTRLDAEEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 168 AFCLGTSGAKALIFGGEmvaavaevsgHLGKSLIKfcSGDLGPEGILPDthlldpllKEASTAPLAqipskgmddrlfyi 247
Cdd:cd12118 94 AFILRHSEAKVLFVDRE----------FEYEDLLA--EGDPDFEWIPPA--------DEWDPIALN-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniigvgQCLIYGLT------VVLRKkFSASR 321
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG------WCFPWTVAavggtnVCLRK-VDAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 322 FWDDCIKYNctVVQYIGE--ICRYLLKQPVREAERR-HRVRLAVGNGLRPAIWEEFTERFGVRqIGEFYGATECNcsian 398
Cdd:cd12118 213 IYDLIEKHK--VTHFCGAptVLNMLANAPPSDARPLpHRVHVMTAGAPPPAAVLAKMEELGFD-VTHVYGLTETY----- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 399 mdGKVGSCGFN--SRILPhvypirlvkvnEDTMELLRDAQGLCIPcqaGEPGLLVGQINQQDPLRRfDG----------- 465
Cdd:cd12118 285 --GPATVCAWKpeWDELP-----------TEERARLKARQGVRYV---GLEEVDVLDPETMKPVPR-DGktigeivfrgn 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 466 ------YVSESATSKKIAHSVFskgdsayLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:cd12118 348 ivmkgyLKNPEATAEAFRGGWF-------HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
....*.
gi 38524616 540 ygVAVP 545
Cdd:cd12118 421 --VARP 424
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
90-557 |
2.68e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 79.25 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PLN02246 37 SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIfggEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLdpllkEASTAPLAQIpSKGMDDRLFYIYT 249
Cdd:PLN02246 117 QAKASGAKLII---TQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELT-----QADENELPEV-EISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 250 SGTTGLPKAAIVVH-----SRYYRMAAFGHHAYrMQAADVLYDCLPLYH--SAGNIIGVGqcLIYGLTVVLRKKFSASRF 322
Cdd:PLN02246 188 SGTTGLPKGVMLTHkglvtSVAQQVDGENPNLY-FHSDDVILCVLPMFHiySLNSVLLCG--LRVGAAILIMPKFEIGAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 323 WDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLaVGNGLRP---AIWEEFTERFGVRQIGEFYGATECNCSIAnM 399
Cdd:PLN02246 265 LELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPlgkELEDAFRAKLPNAVLGQGYGMTEAGPVLA-M 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 400 ---------DGKVGSCGFNSRilphvyPIRLVKVNEDT-MELLRDaqglcipcQAGE-----PGLLVGQINqqDPlrrfd 464
Cdd:PLN02246 343 clafakepfPVKSGSCGTVVR------NAELKIVDPETgASLPRN--------QPGEicirgPQIMKGYLN--DP----- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 465 gyvseSATSKKI-----AHSvfskGDSAYLSGDvlvmDElgyMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:PLN02246 402 -----EATANTIdkdgwLHT----GDIGYIDDD----DE---LFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465
|
490
....*....|....*...
gi 38524616 540 ygvaVPGVEGKAGMAAVA 557
Cdd:PLN02246 466 ----VPMKDEVAGEVPVA 479
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-604 |
3.15e-15 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 78.50 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNLR--REPL 167
Cdd:cd17643 1 PEAVAVVDED--RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG--GAYVPIDPAypVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 168 AFCLGTSGAKALIFGGEMVAAVaevsghlgkslikfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlfyI 247
Cdd:cd17643 77 AFILADSGPSLLLTDPDDLAYV---------------------------------------------------------I 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 248 YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYdclpLYHSAG------NIIGVgqcLIYGLTVVLRKKF---S 318
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfsvwEIWGA---LLHGGRLVVVPYEvarS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 319 ASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVR--QIGEFYGATECNC 394
Cdd:cd17643 173 PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDrpQLVNMYGITETTV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 -------SIANMDGKVGS-CGfnsRILPHvYPIRLVkvnedtmellrDAQGLCIPcqAGEPG-LLVG--QINQqdplrrf 463
Cdd:cd17643 253 hvtfrplDAADLPAAAASpIG---RPLPG-LRVYVL-----------DADGRPVP--PGVVGeLYVSgaGVAR------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 464 dGYVSESA--TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVyg 541
Cdd:cd17643 309 -GYLGRPEltAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV-- 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 542 VAVPGVEGKAGMAA--VADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17643 386 IVREDEPGDTRLVAyvVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
247-601 |
4.40e-15 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 76.77 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDC 326
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 327 IKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV-GNGLRPAIW-EEFTERFGVRQIGEFYGATECNC---------- 394
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELvRRMRSELGFETVLTAYGLTEAGVatmcrpgdda 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 -SIANMDGKvGSCGFNSRIlphvypirlvkvnEDTMELLrdAQGlcipcqagePGLLVGQINqqDPlrrfdgyvseSATS 473
Cdd:cd17638 166 eTVATTCGR-ACPGFEVRI-------------ADDGEVL--VRG---------YNVMQGYLD--DP----------EATA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 474 KKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVeGKAGM 553
Cdd:cd17638 209 EAI------DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGK 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 38524616 554 A-AVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17638 282 AfVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-606 |
4.56e-15 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 77.99 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvgLWlglakagmEAALLNVNLRreplafclgtsgakalifgge 184
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVE---LW--------EAMLAAMKLG--------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 mvaAVaevsghlgkslikfcsgdlgpegILPDTHLLDP-----LLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKaa 259
Cdd:cd05974 50 ---AV-----------------------VIPATTLLTPddlrdRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPK-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 260 IVVHSryYRMAAFGHHAYR----MQAADVLYDClplyHSAGNIIGVGQCLI----YGLTVVL--RKKFSASRFWDDCIKY 329
Cdd:cd05974 102 LVEHT--HRSYPVGHLSTMywigLKPGDVHWNI----SSPGWAKHAWSCFFapwnAGATVFLfnYARFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 330 NCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGvRQIGEFYGATECNCSIANMDGKVGSCGFN 409
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTALVGNSPGQPVKAGSM 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 410 SRILPHVypiRLVKVNEDTMELlrdAQG-LCIPCQAGEP-GLLVGQINQQDplrrfdgyvsesatskKIAHSVfskGDSA 487
Cdd:cd05974 255 GRPLPGY---RVALLDPDGAPA---TEGeVALDLGDTRPvGLMKGYAGDPD----------------KTAHAM---RGGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 488 YLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG------VAVPgvegKAGMAAVA---- 557
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPspdpvrLSVP----KAFIVLRAgyep 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 38524616 558 DPHSLLDpnaIYQELQKVLAPY--ARPIFLRLLPQvdtTGTFKIQKTRLQR 606
Cdd:cd05974 386 SPETALE---IFRFSRERLAPYkrIRRLEFAELPK---TISGKIRRVELRR 430
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
241-606 |
6.12e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 76.75 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 241 DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL------R 314
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 315 KKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVrQIGEFYGATECNC 394
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL-PVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 SIA----NMDGKVGSCGFNsriLPHVYpIRLVKVNEDTMELLRDAQGLCIP-CQAGePGLLVGQINQQDPLRRF--DGYV 467
Cdd:cd05944 161 LVAvnppDGPKRPGSVGLR---LPYAR-VRIKVLDGVGRLLRDCAPDEVGEiCVAG-PGVFGGYLYTEGNKNAFvaDGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 468 SesatskkiahsvfskgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSR--------LLGQTDVAV 539
Cdd:cd05944 236 N---------------------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRhpavafagAVGQPDAHA 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 540 YGVAVPGVEGKAGmaAVADPHSLLDPNAiyqelQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd05944 295 GELPVAYVQLKPG--AVVEEEELLAWAR-----DHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-634 |
9.41e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.46 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLN 159
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE--QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGkslikfcsgdlgpegiLPDTHLLDPLLKEASTAPLAQ--IPS 237
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLL-----------SQSHLR----------------LPLAQGVQVLDLDRGDENYAEanPAI 3191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 238 KGMDDRLFY-IYTSGTTGLPKAAIVVHsryyrmAAFGHHAYRM-QAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRK 315
Cdd:PRK12316 3192 RTMPENLAYvIYTSGSTGKPKGVGIRH------SALSNHLCWMqQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 316 KFSASRFWDDCIKY----NCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATE 391
Cdd:PRK12316 3266 VLAGPEDWRDPALLveliNSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTE 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 392 cncsiANMDGKVGSCgfnsrILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRfdgyvsESA 471
Cdd:PRK12316 3346 -----ATITVTHWQC-----VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNR------PGL 3409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 472 TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlSRLLGQTdvAVYGVAVPGVEGKA 551
Cdd:PRK12316 3410 TAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE---ARLLEHP--WVREAVVLAVDGRQ 3484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 552 GMAAVADPHSLLD-PNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLqregfdPRQTSDrlfflDLKQGHYLP 630
Cdd:PRK12316 3485 LVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL------PRPDAA-----LLQQDYVAP 3553
|
....
gi 38524616 631 LNEA 634
Cdd:PRK12316 3554 VNEL 3557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
74-612 |
1.40e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEF-VGLwLGLAKAG 152
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVWDG--GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLlVGL-LAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 153 MEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGhlgkslikFCSGDLgpegilpDTHLLDPLlkeASTAPL 232
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEG--------VSAIAL-------DSLHLDSW---PSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 233 AQIpskgMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSagniIGVGQC---LIYG 308
Cdd:PRK05691 1268 LHL----HGDNLAYvIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD----VSVWECfwpLITG 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 309 LTVVLR---KKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGE 385
Cdd:PRK05691 1340 CRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHN 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 386 FYGATEC-------NCSIAnmDGKVGSCGfnsRILPHVypirLVKVNEDTMELLrdaqglcipcQAGEPG-LLVGQINqq 457
Cdd:PRK05691 1420 RYGPTETainvthwQCQAE--DGERSPIG---RPLGNV----LCRVLDAELNLL----------PPGVAGeLCIGGAG-- 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 458 dpLRRfdGYVSESATSKK--IAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlSRLLGQT 535
Cdd:PRK05691 1479 --LAR--GYLGRPALTAErfVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ---ARLLAQP 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 536 DVAVYGVAVPgvEGKAGMAAV----ADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL------Q 605
Cdd:PRK05691 1552 GVAQAAVLVR--EGAAGAQLVgyytGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALpepvwqQ 1629
|
....*..
gi 38524616 606 REGFDPR 612
Cdd:PRK05691 1630 REHVEPR 1636
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
107-604 |
2.21e-14 |
|
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: 75.88 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 107 AQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaaLLNVNLRREPLAF---CLGTSGAKALIFGG 183
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIY---LINSILTVFAAAAawkCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 EMVAAVAEVsghlgKSLIKFCSGDLGPEGilpdthlLDPLlkEASTAPLAQIPSKGMDDRLFY---IYTSGTTGLPKA-- 258
Cdd:cd05929 79 AEACAIIEI-----KAAALVCGLFTGGGA-------LDGL--EDYEAAEGGSPETPIEDEAAGwkmLYSGGTTGRPKGik 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 259 ----AIVVHSRYYRMAAFGhhaYRMQAADVLYDCLPLYHSAGNIIGVGqCLIYGLTVVLRKKFSASRFWDDCIKYNCTVV 334
Cdd:cd05929 145 rglpGGPPDNDTLMAAALG---FGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 335 QYIGEICRYLLKQP--VREAERRHRVRLAVGNG--LRPAIWEEFTERFGVRqIGEFYGATECNcsianmdgkvGSCGFNS 410
Cdd:cd05929 221 QFVPTMFVRLLKLPeaVRNAYDLSSLKRVIHAAapCPPWVKEQWIDWGGPI-IWEYYGGTEGQ----------GLTIING 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 411 -RILPHvyPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGqinqqDPLRRFDGYVSESATSKKiaHSVFSKGDSAYL 489
Cdd:cd05929 290 eEWLTH--PGSVGRAVLGKVHILDEDGNEVPPGEIGEVYFANG-----PGFEYTNDPEKTAAARNE--GGWSTLGDVGYL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 490 sgdvlvmDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVE-GKAGMAAVaDPHSLLDPNAI 568
Cdd:cd05929 361 -------DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVV-QPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 38524616 569 YQE-----LQKVLAPYARP---IFLRLLPQVDTTgtfKIQKTRL 604
Cdd:cd05929 431 LAEeliafLRDRLSRYKCPrsiEFVAELPRDDTG---KLYRRLL 471
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
104-590 |
2.36e-14 |
|
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: 75.71 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGG 183
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 emvaavaevsghlgkslikfcsgdlgpegilPDThlldpllkeastapLAQIpskgmddrlfyIYTSGTTGLPKAAIVVH 263
Cdd:cd05907 86 -------------------------------PDD--------------LATI-----------IYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 264 SRYyrMAAFGHHAYRMQAA--DVLYDCLPLYHSAGNIIGVGQCLIYGLTVV-----------LRKK-----FSASRFWDd 325
Cdd:cd05907 110 RNI--LSNALALAERLPATegDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddLSEVrptvfLAVPRVWE- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 326 ciK-YNCTVVQYIGEICRYLLKQPVREaerrhRVRLAVGNG--LRPAIwEEFTERFGVrQIGEFYGATECnCSIANM--- 399
Cdd:cd05907 187 --KvYAAIKVKAVPGLKRKLFDLAVGG-----RLRFAASGGapLPAEL-LHFFRALGI-PVYEGYGLTET-SAVVTLnpp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 400 -DGKVGSCGfnsrilpHVYPIRLVKVNEDtmellrdaqglcipcqaGEpgLLV-GQINqqdplrrFDGYVSESATSKKIA 477
Cdd:cd05907 257 gDNRIGTVG-------KPLPGVEVRIADD-----------------GE--ILVrGPNV-------MLGYYKNPEATAEAL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 478 hsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWR-GENVSTTEVEGVL--SRLLGQtdVAVYGVAVPGV------- 547
Cdd:cd05907 304 -----DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALkaSPLISQ--AVVIGDGRPFLvalivpd 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 548 ------EGKAGMAAVADPHSLLDPNAIYQELQKV-------LAPYARPIFLRLLPQ 590
Cdd:cd05907 377 pealeaWAEEHGIAYTDVAELAANPAVRAEIEAAveaanarLSRYEQIKKFLLLPE 432
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
86-313 |
2.61e-14 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 76.12 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGfAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALL--- 158
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 159 --NVNLRRepLAFCLGTSGAKALIFGGEMVAAVAEVSghlgkslikfcsgdLGPEGILPDTHLLDPLLkEASTAPLAQIP 236
Cdd:cd05931 82 tpGRHAER--LAAILADAGPRVVLTTAAALAAVRAFA--------------ASRPAAGTPRLLVVDLL-PDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 237 SKGMDDRLFYIYTSGTTGLPKAAIVVHsryyrmAAFGH------HAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLT 310
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTH------RNLLAnvrqirRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
...
gi 38524616 311 VVL 313
Cdd:cd05931 219 SVL 221
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
69-604 |
3.51e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 75.44 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 69 RRHQRAGHTIPRIFQAV----VQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGL 144
Cdd:cd05920 4 RRYRAAGYWQDEPLGDLlarsAARHPDRIAVVDGDRR--LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 145 WLGLAKAGMEAAL-LNVNLRREPLAFClGTSGAKALIfggemvaavaevsghlgkslikfcsgdlGPEGILPDTHLldPL 223
Cdd:cd05920 82 FFALLRLGAVPVLaLPSHRRSELSAFC-AHAEAVAYI----------------------------VPDRHAGFDHR--AL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 224 LKEAstapLAQIPskgmdDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYH----SAGNII 299
Cdd:cd05920 131 AREL----AESIP-----EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplACPGVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 300 GVgqcLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEicryLLKQPVREAERR------HRVRLAVGNGLRPAIWEE 373
Cdd:cd05920 202 GT---LLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPA----LVSLWLDAAASRradlssLRLLQVGGARLSPALARR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 374 FTERFGVrQIGEFYGATE--CNCS--------IANMDGKVGSCGFNSRILphvypirlvkvnedtmellrDAQGLCIPcq 443
Cdd:cd05920 275 VPPVLGC-TLQQVFGMAEglLNYTrlddpdevIIHTQGRPMSPDDEIRVV--------------------DEEGNPVP-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 444 AGEPGLLvgqinqqdpLRR----FDGYV-SESATSKkiahsVFSKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGEN 518
Cdd:cd05920 332 PGEEGEL---------LTRgpytIRGYYrAPEHNAR-----AFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 519 VSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKAGMAAVADPHsllDPNAIYQELQKVL-----APYARPIFLRLLPQVDT 593
Cdd:cd05920 397 IAAEEVENLLLRHPAVHDAAV--VAMPDELLGERSCAFVVLR---DPPPSAAQLRRFLrerglAAYKLPDRIEFVDSLPL 471
|
570
....*....|.
gi 38524616 594 TGTFKIQKTRL 604
Cdd:cd05920 472 TAVGKIDKKAL 482
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-542 |
6.88e-14 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 74.49 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17642 31 PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKaLIF----GGEMVAAVAEVSGHLGKSLIKFCSGDLGpeGILPD----THLLDPLLKEASTAPlaqiPSKGMD 241
Cdd:cd17642 111 SLNISKPT-IVFcskkGLQKVLNVQKKLKIIKTIIILDSKEDYK--GYQCLytfiTQNLPPGFNEYDFKP----PSFDRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYI-YTSGTTGLPKAAIVVHSRYyrMAAFGH-----HAYRMQAADVLYDCLPLYHSAGNIIGVGQcLIYGLTVVLRK 315
Cdd:cd17642 184 EQVALImNSSGSTGLPKGVQLTHKNI--VARFSHardpiFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LICGFRVVLMY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 316 KFSASRFWDDCIKYNCTVVQYIGEICRYLLKQP-VREAERRHRVRLAVGNG-LRPAIWEEFTERFGVRQIGEFYGATECN 393
Cdd:cd17642 261 KFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 394 CSI---ANMDGKVGSCGfnsRILPHVYpirlVKV-NEDTMELLRdaqglciPCQAGE-----PGLLVGQINqqdplrrfd 464
Cdd:cd17642 341 SAIlitPEGDDKPGAVG---KVVPFFY----AKVvDLDTGKTLG-------PNERGElcvkgPMIMKGYVN--------- 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 465 gyvSESATSKKIAHsvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 542
Cdd:cd17642 398 ---NPEATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
90-263 |
7.13e-14 |
|
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: 74.23 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAALLNVNL-----RR 164
Cdd:cd12114 1 PDATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAG--AAYVPVDIdqpaaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 165 EPLafcLGTSGAKALIfggemvaavaevsghlgkslikFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPskGMDDRL 244
Cdd:cd12114 77 EAI---LADAGARLVL----------------------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDV--APDDLA 129
|
170
....*....|....*....
gi 38524616 245 FYIYTSGTTGLPKAAIVVH 263
Cdd:cd12114 130 YVIFTSGSTGTPKGVMISH 148
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
105-607 |
9.87e-14 |
|
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: 74.20 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 MVAAVAEVSGHL--GKSLIKFCSGDLGPEGILPDTHLLDPLLkeASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKA---- 258
Cdd:cd12119 107 FLPLLEAIAPRLptVEHVVVMTDDAAMPEPAGVGVLAYEELL--AAESPEYDWPDFDENTAAAICYTSGTTGNPKGvvys 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 259 --AIVVHSryyrMAAFGHHAYRMQAADVLYDCLPLYHsaGNIIGVG-QCLIYGLTVVLRKKFSASRFWDDCIK-YNCTVV 334
Cdd:cd12119 185 hrSLVLHA----MAALLTDGLGLSESDVVLPVVPMFH--VNAWGLPyAAAMVGAKLVLPGPYLDPASLAELIErEGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 335 QYIGEICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERfGVRQIgEFYGATE-CNCSIAN-----MDGKVGSC 406
Cdd:cd12119 259 AGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEER-GVRVI-HAWGMTEtSPLGTVArppseHSNLSEDE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 407 GFNSRILPHvYPIRLVK---VNEDTMELLRDAQglcipcQAGE-----PGLLVGQINQQDPLRRF--DGYVSesatskki 476
Cdd:cd12119 337 QLALRAKQG-RPVPGVElriVDDDGRELPWDGK------AVGElqvrgPWVTKSYYKNDEESEALteDGWLR-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 477 ahsvfskgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgvegKAG---M 553
Cdd:cd12119 402 -------------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP----KWGerpL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 554 A-AVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLqRE 607
Cdd:cd12119 465 AvVVLKEGATVTAEELLEFLADKVAKWWLPddvVFVDEIPK---TSTGKIDKKAL-RE 518
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
90-604 |
1.50e-13 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 73.17 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLwLGLAKAGMEAALLNVNLRREPLA 168
Cdd:cd17649 1 PDAVALVFGD--QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEmVVAL-LAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 169 FCLGTSGAKALIfggemvaavaevsGHLGKSLIkfcsgdlgpegilpdthlldpllkeastaplaqipskgmddrlFYIY 248
Cdd:cd17649 78 YMLEDSGAGLLL-------------THHPRQLA-------------------------------------------YVIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVHsryyrmAAFGHHA------YRMQAADVLYDCLPLYHSAGnIIGVGQCLIYGLTVVLRKK---FSA 319
Cdd:cd17649 102 TSGSTGTPKGVAVSH------GPLAAHCqataerYGLTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLRPDelwASA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 320 SRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRH-RVRLAV--GNGLRPAIWEEfTERFGVRQIGEfYGATEcncsi 396
Cdd:cd17649 175 DELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPpSLRLYIfgGEALSPELLRR-WLKAPVRLFNA-YGPTE----- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 397 ANMDGKVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQglciPCQAGEPG-LLVGqinqQDPLRRfdGYVSESATSKK 475
Cdd:cd17649 248 ATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN----PVPVGVTGeLYIG----GEGLAR--GYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 476 --IAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGK--- 550
Cdd:cd17649 318 rfVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV--VALDGAGGKqlv 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 38524616 551 AGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17649 396 AYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
90-607 |
2.24e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 73.06 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGECWtfAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAAL--LNVNLRREPL 167
Cdd:PRK08162 32 PDRPAVIHGDRRRTW--AETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG--AVLntLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 168 AFCLGTSGAKALI----FGGEMVAAVAEVSGhlgksLIKFCSGDLGPEgiLPDTHLLDPLLKEASTA----PLAQIPSKG 239
Cdd:PRK08162 108 AFMLRHGEAKVLIvdteFAEVAREALALLPG-----PKPLVIDVDDPE--YPGGRFIGALDYEAFLAsgdpDFAWTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 240 MDDRLFYIYTSGTTGLPKAaIVVHSR-YYRMAA-------FGHHAyrmqaadVLYDCLPLYHSagNiigvGQC------L 305
Cdd:PRK08162 181 EWDAIALNYTSGTTGNPKG-VVYHHRgAYLNALsnilawgMPKHP-------VYLWTLPMFHC--N----GWCfpwtvaA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 306 IYGLTVVLRKkFSASRFWDDCIKYNCT------VVQYIgeicryLLKQPvrEAERR---HRVRLAVGNGLRPAIWEEFTE 376
Cdd:PRK08162 247 RAGTNVCLRK-VDPKLIFDLIREHGVThycgapIVLSA------LINAP--AEWRAgidHPVHAMVAGAAPPAAVIAKME 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 377 RFGVRqIGEFYGATECNcsianmdGKVGSCGFNS--RILPHvypirlvkvneDTMELLRDAQGLCIPCQAG--------- 445
Cdd:PRK08162 318 EIGFD-LTHVYGLTETY-------GPATVCAWQPewDALPL-----------DERAQLKARQGVRYPLQEGvtvldpdtm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 446 EP----GLLVGQInqqdpLRR----FDGYV-SESATSKKIAHSVFSKGDSAylsgdvlVMDELGYMYFRDRSGDTFRWRG 516
Cdd:PRK08162 379 QPvpadGETIGEI-----MFRgnivMKGYLkNPKATEEAFAGGWFHTGDLA-------VLHPDGYIKIKDRSKDIIISGG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 517 ENVSTTEVEGVLSRLLGQTDVAVygVAVPG----------VEGKAGMAAVADphslldpnAIYQELQKVLAPYARP--IF 584
Cdd:PRK08162 447 ENISSIEVEDVLYRHPAVLVAAV--VAKPDpkwgevpcafVELKDGASATEE--------EIIAHCREHLAGFKVPkaVV 516
|
570 580
....*....|....*....|...
gi 38524616 585 LRLLPQvdtTGTFKIQKTRLQRE 607
Cdd:PRK08162 517 FGELPK---TSTGKIQKFVLREQ 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
242-606 |
2.57e-13 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 71.21 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIgVGQCLIYGLTVVLRKKFSASR 321
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 322 fwDDCIKYNCTVVQYIGEICRYLLKQP-VREAERRHRVRLaVGNGlrpAIWEEFTERFGVRQIGEF--YGATE---CNCS 395
Cdd:cd17630 80 --EDLAPPGVTHVSLVPTQLQRLLDSGqGPAALKSLRAVL-LGGA---PIPPELLERAADRGIPLYttYGMTEtasQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IANMDGKVGSCGfnsRILPHVypirlvkvnedtmELLRDAQGlCIpcQAGEPGLLVGQINQQDPLRRFDGyvsesatskk 475
Cdd:cd17630 154 KRPDGFGRGGVG---VLLPGR-------------ELRIVEDG-EI--WVGGASLAMGYLRGQLVPEFNED---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 476 iahSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgvegKAGMAA 555
Cdd:cd17630 205 ---GWFTTKDLGELHAD-------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE----ELGQRP 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 556 VA--DPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQR 606
Cdd:cd17630 271 VAviVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
69-545 |
5.55e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 72.26 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 69 RRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECwTFAQLDAYSNAVANLFRQLgFAPGDVVAIFLegrPEFVG---LW 145
Cdd:PRK08633 608 KSRKEALPPLAEAWIDTAKRNWSRLAVADSTGGEL-SYGKALTGALALARLLKRE-LKDEENVGILL---PPSVAgalAN 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 146 LGLAKAGMEAALLNVNLRREPLAFCLGTSGAKAlIFGGEMVAAVAEVSGHLGKSLIKfcSGDLGPEGILPDTHLLDPLLK 225
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKT-VITSRKFLEKLKNKGFDLELPEN--VKVIYLEDLKAKISKVDKLTA 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 226 --EASTAPLAQI-----PSKGMDDRLFYIYTSGTTGLPKAaiVVHSRYYRMAAFGH--HAYRMQAADVLYDCLPLYHSag 296
Cdd:PRK08633 760 llAARLLPARLLkrlygPTFKPDDTATIIFSSGSEGEPKG--VMLSHHNILSNIEQisDVFNLRNDDVILSSLPFFHS-- 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 297 niigvgqcliYGLTV----VLRKKFSASRFWDD---------CIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVG 363
Cdd:PRK08633 836 ----------FGLTVtlwlPLLEGIKVVYHPDPtdalgiaklVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVA 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 364 NG--LRPAIWEEFTERFGVRqIGEFYGATEC------NCSIANMDG-------KVGSCGfnsRILPHVyPIRLvkVNEDT 428
Cdd:PRK08633 906 GAekLKPEVADAFEEKFGIR-ILEGYGATETspvasvNLPDVLAADfkrqtgsKEGSVG---MPLPGV-AVRI--VDPET 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 429 MEllrdaqglciPCQAGEPGL-LVGQINqqdplrRFDGYVS-ESATSKKIAHsvfSKGDSAYLSGDVLVMDELGYMYFRD 506
Cdd:PRK08633 979 FE----------ELPPGEDGLiLIGGPQ------VMKGYLGdPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITD 1039
|
490 500 510
....*....|....*....|....*....|....*....
gi 38524616 507 RSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVP 545
Cdd:PRK08633 1040 RYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVP 1078
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
122-542 |
6.91e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 71.37 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEV-SGHLGKSL 200
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELqNDRLPSLM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 201 IKFCSGDLGPEGILPDTHLL--DPLLKEASTAPLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYY-----RMAAFG 273
Cdd:PLN02860 131 WQVFLESPSSSVFIFLNSFLttEMLKQRALGTTELD-YAWAPDDAVLICFTSGTTGRPKGVTISHSALIvqslaKIAIVG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 274 HhayrmQAADVLYDCLPLYH-----SAGNIIGVGQCLiygltvVLRKKFSASRFWdDCIKYNC-----TVVQYIGEICRY 343
Cdd:PLN02860 210 Y-----GEDDVYLHTAPLCHigglsSALAMLMVGACH------VLLPKFDAKAAL-QAIKQHNvtsmiTVPAMMADLISL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 344 LLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIRLVK 423
Cdd:PLN02860 278 TRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 424 VNEdtmellrdAQGLCIpcqaGEP------------GLLVGQINQQDP--LRRFDGYVSESATSKKiahsvfskgDSAYL 489
Cdd:PLN02860 358 VHQ--------PQGVCV----GKPaphvelkigldeSSRVGRILTRGPhvMLGYWGQNSETASVLS---------NDGWL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 38524616 490 -SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 542
Cdd:PLN02860 417 dTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-576 |
7.91e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 154 EAALLNVNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGKSLIKfcsgdlgPEGIlpDTHLLDPLlKEASTAPLA 233
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLL-----------TQSHLLQRLPI-------PDGL--ASLALDRD-EDWEGFPAH 4685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 234 QIPSKGMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPlYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK12316 4686 DPAVRLHPDNLAYvIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 LRKkfsaSRFWD------DCIKYNCTVVQYIGEICRYLLKQPVREAE-RRHRVRLAVGNGLRPAIWEEFTERFGVRQIGE 385
Cdd:PRK12316 4765 IRD----DSLWDperlyaEIHEHRVTVLVFPPVYLQQLAEHAERDGEpPSLRVYCFGGEAVAQASYDLAWRALKPVYLFN 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 386 FYGATECNCSIANMDGKVGS-CGfnsrilPHVYPIRLVKVNEDTMeLLRDAQGLCIPCQAGEpgLLVGqinqQDPLRRfd 464
Cdd:PRK12316 4841 GYGPTETTVTVLLWKARDGDaCG------AAYMPIGTPLGNRSGY-VLDGQLNPLPVGVAGE--LYLG----GEGVAR-- 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 465 GYVSESA-TSKKIAHSVFSK-GDSAYLSGDVL------VMDELGymyfrdRSGDTFRWRGENVSTTEVEgvlSRLLGQTD 536
Cdd:PRK12316 4906 GYLERPAlTAERFVPDPFGApGGRLYRTGDLAryradgVIDYLG------RVDHQVKIRGFRIELGEIE---ARLREHPA 4976
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 38524616 537 V--AVYgVAVPGVEGKAGMAAV--ADPHsLLDPNAIYQELQKVL 576
Cdd:PRK12316 4977 VreAVV-IAQEGAVGKQLVGYVvpQDPA-LADADEAQAELRDEL 5018
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-604 |
1.46e-12 |
|
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: 70.01 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd12116 1 PDATAVRDDD--RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAevsghlgkslikfcsgdlgpeGILPDTHLLDPLLKEASTAPLAQIPskgmDDRLFY-IY 248
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLP---------------------AGLPVLLLALAAAAAAPAAPRTPVS----PDDLAYvIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVH----------------SRYYRMAAFGHHAYRMQAADVLydcLPlyhsagniigvgqcLIYGLTVV 312
Cdd:cd12116 134 TSGSTGRPKGVVVSHrnlvnflhsmrerlglGPGDRLLAVTTYAFDISLLELL---LP--------------LLAGARVV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 LRKK---FSASRFWDDCIKYNCTVVQYIGEICRYLLKQpvrEAERRHRVRLAVG-NGLRPAIWEEFTERfgVRQIGEFYG 388
Cdd:cd12116 197 IAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDA---GWQGRAGLTALCGgEALPPDLAARLLSR--VGSLWNLYG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 389 ATECNcsianmdgkVGSCGfnSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPcqAGEPG-LLVGQIN-QQDPLRRfdgy 466
Cdd:cd12116 272 PTETT---------IWSTA--ARVTAAAGPIPIGRPLANTQVYVLDAALRPVP--PGVPGeLYIGGDGvAQGYLGR---- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 467 vsESATSKKIAHSVFSKGDS-AYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAvygVAVP 545
Cdd:cd12116 335 --PALTAERFVPDPFAGPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA---VVVR 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38524616 546 GVEGKAGMAAVADPH--SLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd12116 410 EDGGDRRLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
77-552 |
1.66e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 77 TIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREPLAFCLGTSGAKALIFGGemvAAVAEVSGhLGKSLIKFcsGDLGPEGILPDTHLLDPLLKEASTAPLAQIP 236
Cdd:PLN02330 109 GANPTALESEIKKQAEAAGAKLIVTND---TNYGKVKG-LGLPVIVL--GEEKIEGAVNWKELLEAADRAGDTSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 237 SKgmdDRLFYIYTSGTTGLPKAAIVVHsryyrmaafghhayRMQAADVlydCLPLYHSAGNIIGVGQCL-------IYGL 309
Cdd:PLN02330 183 QT---DLCALPFSSGTTGISKGVMLTH--------------RNLVANL---CSSLFSVGPEMIGQVVTLglipffhIYGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 310 T------------VVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVRE----AERRHRVRLAVGNGLRPAIWEE 373
Cdd:PLN02330 243 TgiccatlrnkgkVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 374 FTERFGVRQIGEFYGATECNC-SIANMD-------GKVGSCGFnsrILPHvypIRLVKVNEDT-MELLRDAQG-LCIPCQ 443
Cdd:PLN02330 323 FEAKFPGVQVQEAYGLTEHSCiTLTHGDpekghgiAKKNSVGF---ILPN---LEVKFIDPDTgRSLPKNTPGeLCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 444 AgepgLLVGQINQQDplrrfdgyvsesATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTE 523
Cdd:PLN02330 397 C----VMQGYYNNKE------------ETDRTI------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
490 500
....*....|....*....|....*....
gi 38524616 524 VEGVLSRLLGQTDVAVygvaVPGVEGKAG 552
Cdd:PLN02330 455 LEAILLTHPSVEDAAV----VPLPDEEAG 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
74-613 |
1.82e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.96 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 74 AGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM 153
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFGE--QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 154 EAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHlgKSLikfcsgdlgpegilpdthLLDPLLKEASTAPLA 233
Cdd:PRK12467 1650 AYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGL--RSL------------------VLDQEDDWLEGYSDS 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 234 QIPSKGMDDRLFY-IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPlYHSAGNIIGVGQCLIYGLTVV 312
Cdd:PRK12467 1710 NPAVNLAPQNLAYvIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 LRkKFSASRFWDDCIKYNC----TVVQYIGEICRYLLKQPVREAE-RRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFY 387
Cdd:PRK12467 1789 IA-PPGAHRDPEQLIQLIErqqvTTLHFVPSMLQQLLQMDEQVEHpLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 388 GATEC-------NCSIANMDGKVGScgfnsrilphvyPIRLVKVNEDTMELlrDAQGLCIPCQ-AGEpgLLVGqinqQDP 459
Cdd:PRK12467 1868 GPTETavdvthwTCRRKDLEGRDSV------------PIGQPIANLSTYIL--DASLNPVPIGvAGE--LYLG----GVG 1927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 LRRfdGYVSESA-TSKKIAHSVFSKGDS-AYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEgvlSRLLGQTDV 537
Cdd:PRK12467 1928 LAR--GYLNRPAlTAERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE---ARLREQGGV 2002
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 538 AvyGVAVPGVEGKAGMAAVA-----DPHSLLDPNAIY-------QELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK12467 2003 R--EAVVIAQDGANGKQLVAyvvptDPGLVDDDEAQValrailkNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALP 2080
|
....*...
gi 38524616 606 REgfDPRQ 613
Cdd:PRK12467 2081 AP--DASE 2086
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
89-605 |
2.08e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.81 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 89 QPERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPgDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLA 168
Cdd:PRK07638 14 QPNKIAIKE--NDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 169 FCLGTSGAkalifggEMVaaVAEvsghlgksliKFCSGDL-GPEGILPDTHLLDPLLKEASTAPLaqiPSKGMDDRLFYI 247
Cdd:PRK07638 91 ERLAISNA-------DMI--VTE----------RYKLNDLpDEEGRVIEIDEWKRMIEKYLPTYA---PIENVQNAPFYM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 248 -YTSGTTGLPKAAIVVHSRYyrMAAF--GHHAYRMQAADVLYDCLPLYHSAgNIIGVGQCLIYGLTVVLRKKFSASRFWD 324
Cdd:PRK07638 149 gFTSGSTGKPKAFLRAQQSW--LHSFdcNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 325 DCIKYNCTVVQYIGEICRYLLKQpvrEAERRHRVRLAVGNGLRPAIW-EEFTERFGVRQIGEFYGATECNCSIANMDGkv 403
Cdd:PRK07638 226 KLETENISVMYTVPTMLESLYKE---NRVIENKMKIISSGAKWEAEAkEKIKNIFPYAKLYEFYGASELSFVTALVDE-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 404 gscgfNSRILPHVY--PIRLVKVNedtmelLRDAQGlcIPCQAGEpgllVGQINQQDPLRrFDGYVSESATSKKIAhsvf 481
Cdd:PRK07638 301 -----ESERRPNSVgrPFHNVQVR------ICNEAG--EEVQKGE----IGTVYVKSPQF-FMGYIIGGVLARELN---- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 482 skgDSAYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgvegKAGMAAVADPH 560
Cdd:PRK07638 359 ---ADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS----YWGEKPVAIIK 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 38524616 561 SLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQ 605
Cdd:PRK07638 432 GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
80-604 |
2.93e-12 |
|
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: 69.28 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 80 RIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPE-FVGLwLGLAKAGMEAALL 158
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED--QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEmIVGI-LGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 159 NVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEvsghlgkslIKFCsgdlgpegilpdTHLLDPLLKEASTAPLAqIPSK 238
Cdd:cd17655 78 DPDYPEERIQYILEDSGADILLTQSHLQPPIAF---------IGLI------------DLLDEDTIYHEESENLE-PVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 239 GmDDRLFYIYTSGTTGLPKAAIVVHSryyrmaafGHHAYRMQAADVLY----DCLPLYHSAGNIIGVGQ---CLIYGLTV 311
Cdd:cd17655 136 S-DDLAYVIYTSGSTGKPKGVMIEHR--------GVVNLVEWANKVIYqgehLRVALFASISFDASVTEifaSLLSGNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 312 VLRKKFSASR---FWDDCIKYNCTVV-------QYIGEIcRYLLKQPVReaerrhrvRLAV-GNGLRPAIWEEFTERFGV 380
Cdd:cd17655 207 YIVRKETVLDgqaLTQYIRQNRITIIdltpahlKLLDAA-DDSEGLSLK--------HLIVgGEALSTELAKKIIELFGT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 381 -RQIGEFYGATEC--NCSIANMDGKvgscgfnSRILPHVyPIRLVKVNedTMELLRDAQGLCIPcqAGEPG-LLVGqinq 456
Cdd:cd17655 278 nPTITNAYGPTETtvDASIYQYEPE-------TDQQVSV-PIGKPLGN--TRIYILDQYGRPQP--VGVAGeLYIG---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 457 QDPLRRfdGYVS-ESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQT 535
Cdd:cd17655 342 GEGVAR--GYLNrPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIK 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38524616 536 DVAVygVAVPGVEGKAGMAA--VADPHslLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17655 420 EAVV--IARKDEQGQNYLCAyiVSEKE--LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
81-542 |
7.54e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 68.16 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 81 IFQAVVQRQPERLALVDagTGECWTFAQLDAYSNA-VANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAalLN 159
Cdd:PRK08974 28 MFEQAVARYADQPAFIN--MGEVMTFRKLEERSRAfAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV--VN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VNLRREP--LAFCLGTSGAKALI----FGG--EMVAAVAEVsghlgKSLIKFCSGDL--GPEGIL------------PDT 217
Cdd:PRK08974 104 VNPLYTPreLEHQLNDSGAKAIVivsnFAHtlEKVVFKTPV-----KHVILTRMGDQlsTAKGTLvnfvvkyikrlvPKY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 218 HLLDPL-LKEA-STAPLAQI--PSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYrmaafghhAYRMQA----ADVLYD-- 287
Cdd:PRK08974 179 HLPDAIsFRSAlHKGRRMQYvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNML--------ANLEQAkaayGPLLHPgk 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 288 -----CLPLYHsagniigvgqclIYGLTVvlrkkfsasrfwddcikyNCTVVQYIGeICRYLLKQP------VREAeRRH 356
Cdd:PRK08974 251 elvvtALPLYH------------IFALTV------------------NCLLFIELG-GQNLLITNPrdipgfVKEL-KKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 357 RV---------------------------RLAVGNGL--RPAI---WEEFTerfGVRQIgEFYGATECN----CSIANMD 400
Cdd:PRK08974 299 PFtaitgvntlfnallnneefqeldfsslKLSVGGGMavQQAVaerWVKLT---GQYLL-EGYGLTECSplvsVNPYDLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 401 GKVGSCGFnsrilPhvYPIRLVKVNEDTMELLrdAQGlcipcQAGE-----PGLLVGQINQQDplrrfdgyvsesATSKk 475
Cdd:PRK08974 375 YYSGSIGL-----P--VPSTEIKLVDDDGNEV--PPG-----EPGElwvkgPQVMLGYWQRPE------------ATDE- 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 476 iahsVFSKGdsaYLS-GDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGV 542
Cdd:PRK08974 428 ----VIKDG---WLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-279 |
1.30e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 67.18 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 81 IFQAVVQRQPERLAlVDAGTGEcWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeAA--LL 158
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDGS-LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG--GAfvPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 159 NVNLRREPLAFCLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeASTAplaqipsk 238
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVL----------------------------------------------TSSP-------- 105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 38524616 239 gmDDRLFYIYTSGTTGLPKAAIVVHSRYyrMAAFGHHAYRM 279
Cdd:cd05918 106 --SDAAYVIFTSGSTGKPKGVVIEHRAL--STSALAHGRAL 142
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
77-613 |
1.49e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 67.35 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 77 TIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaA 156
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKA--ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGY--V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGD-LGPEGI-----------------LP 215
Cdd:PRK07059 100 VVNVNPLYTPreLEHQLKDSGAEAIVVLENFATTVQQVLAKTAvKHVVVASMGDlLGFKGHivnfvvrrvkkmvpawsLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 216 DTHLLDPLLKEASTAPLAQiPSKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAAFGHHAYRMQAAD--VLYDC- 288
Cdd:PRK07059 180 GHVRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHrnivANVLQMEAWLQPAFEKKPRPdqLNFVCa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 289 LPLYHsagniigvgqclIYGLTVVLRKKFSA-------------SRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERR 355
Cdd:PRK07059 259 LPLYH------------IFALTVCGLLGMRTggrnilipnprdiPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 356 HRVRLAVGNGLrpAIWEEFTERFGVRQ---IGEFYGATECN----CSIANMDGKVGSCGFnsrilphvyPIRLVKVNedt 428
Cdd:PRK07059 327 SKLIVANGGGM--AVQRPVAERWLEMTgcpITEGYGLSETSpvatCNPVDATEFSGTIGL---------PLPSTEVS--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 429 melLRDAQGLCIPC-QAGE-----PGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSKgdsaylSGDVLVMDELGYM 502
Cdd:PRK07059 393 ---IRDDDGNDLPLgEPGEicirgPQVMAGYWNRPD------------ETAKVMTADGFFR------TGDVGVMDERGYT 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 503 YFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvavpgvegkagmaaVADPHS-----LL----DPNAIYQELQ 573
Cdd:PRK07059 452 KIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG--------------VPDEHSgeavkLFvvkkDPALTEEDVK 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 38524616 574 KV----LAPYARPIFLRLLPQVDTTGTFKIqktrLQREGFDPRQ 613
Cdd:PRK07059 518 AFckerLTNYKRPKFVEFRTELPKTNVGKI----LRRELRDGKA 557
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-604 |
2.02e-11 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 66.50 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALVdaGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRRE 165
Cdd:cd05945 1 AAANPDRPAVV--EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 166 PLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGK---------SLIKFCsgdlgpEGILPDThLLDPLLKEASTAPLAqip 236
Cdd:cd05945 79 RIREILDAAKPALLIADGDDNAYIIFTSGSTGRpkgvqishdNLVSFT------NWMLSDF-PLGPGDVFLNQAPFS--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 237 skgMDDRLFYIYTSGTTGlpkAAIVVHSRyyrmaafghhayrmqaaDVLYDCLPLYHSAGNiigvgqcliYGLTVVlrkk 316
Cdd:cd05945 149 ---FDLSVMDLYPALASG---ATLVPVPR-----------------DATADPKQLFRFLAE---------HGITVW---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 317 FSASRFWDDCIKY---------NCTVVQYIGEICryllkqPVREAERRHrvrlavgnglrpaiweeftERFGVRQIGEFY 387
Cdd:cd05945 193 VSTPSFAAMCLLSptftpeslpSLRHFLFCGEVL------PHKTARALQ-------------------QRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 388 GATECNCSIANMdgkvgscgfnsRILPHVY------PIRLVKVNEDTMelLRDAQGLCIPcqAGEPG--LLVGQinqqdp 459
Cdd:cd05945 248 GPTEATVAVTYI-----------EVTPEVLdgydrlPIGYAKPGAKLV--ILDEDGRPVP--PGEKGelVISGP------ 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 460 lRRFDGYVSESATSKKIAHSVfsKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV 539
Cdd:cd05945 307 -SVSKGYLNNPEKTAAAFFPD--EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 540 ygVAVPGVEGKAGMAAVADPH---SLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd05945 384 --VPKYKGEKVTELIAFVVPKpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
90-604 |
3.23e-11 |
|
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: 65.96 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDagTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17656 2 PDAVAVVF--ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALifggemvaaVAEVSghlgkslikfCSGDLGPEGILpdTHLLDPLLKEASTaplAQIPSKGMDDRLFY-IY 248
Cdd:cd17656 80 IMLDSGVRVV---------LTQRH----------LKSKLSFNKST--ILLEDPSISQEDT---SNIDYINNSDDLLYiIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVHSRYYRMAAFGH-HAYRMQAADVLYDCLP----LYHSagniigVGQCLIYGLTVVLRKKfSASRfw 323
Cdd:cd17656 136 TSGTTGKPKGVQLEHKNMVNLLHFEReKTNINFSDKVLQFATCsfdvCYQE------IFSTLLSGGTLYIIRE-ETKR-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 324 dDCIKYNCTVVQYIGEICRY---LLKQPVREAERRHR----VRLAVGNGLRPAIWEEFTERFGVRQIG--EFYGATECNC 394
Cdd:cd17656 207 -DVEQLFDLVKRHNIEVVFLpvaFLKFIFSEREFINRfptcVKHIITAGEQLVITNEFKEMLHEHNVHlhNHYGPSETHV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 sianmdgkVGSCGFNSRI-LPHVYPIRLVKVNEDTmeLLRDAQGLCIPCqaGEPG-LLVGQINqqdpLRRfdGYVS-ESA 471
Cdd:cd17656 286 --------VTTYTINPEAeIPELPPIGKPISNTWI--YILDQEQQLQPQ--GIVGeLYISGAS----VAR--GYLNrQEL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 472 TSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVPGVEGKA 551
Cdd:cd17656 348 TAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVV--LDKADDKGEK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 38524616 552 GMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:cd17656 426 YLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-605 |
6.44e-11 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 65.18 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALiFGG 183
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL-FVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 184 EMVAAVAEVSGhLGKSLIkfcSGDLGPEGILPDTHLLDPLLKEAstAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:cd05932 86 KLDDWKAMAPG-VPEGLI---SISLPPPSAANCQYQWDDLIAQH--PPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 264 SRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTV------------VLRKK----FSASRFWddcI 327
Cdd:cd05932 160 GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedVQRARptlfFSVPRLW---T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 328 KYNCTVVQYIG-EICRYLLKQPVREAERRHRV---------RLAVGNG--LRPAIWEEFtERFGVrQIGEFYGATEcNCS 395
Cdd:cd05932 237 KFQQGVQDKIPqQKLNLLLKIPVVNSLVKRKVlkglgldqcRLAGCGSapVPPALLEWY-RSLGL-NILEAYGMTE-NFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 396 IANM----DGKVGSCGFNsrilphvYPIRLVKVNEDTMELLRdaqglcipcqagEPGLLVGQinqqdplrrfdgYVSESA 471
Cdd:cd05932 314 YSHLnypgRDKIGTVGNA-------GPGVEVRISEDGEILVR------------SPALMMGY------------YKDPEA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 472 TSkkiahSVFSKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEGVLSR--------LLGQTDVAVYGV 542
Cdd:cd05932 363 TA-----EAFTA-DGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEhdrvemvcVIGSGLPAPLAL 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 543 AVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQ---VDT---TGTFKIQKTRLQ 605
Cdd:cd05932 437 VVLSEEARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDpwsIDNgilTPTLKIKRNVLE 505
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
69-604 |
6.74e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.03 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 69 RRHQRAGHTIPRIFQAVV---QRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLW 145
Cdd:PRK05857 4 KKFQAMPQLPSTVLDRVFeqaRQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 146 LGLAKAGMEAALLNVNLRREPLA-FCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSG-DLGPEGILPDThlldpl 223
Cdd:PRK05857 84 LACAKLGAIAVMADGNLPIAAIErFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAaVTRESEHSLDA------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 224 lkeastAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYR----MAAFGHHAYRMQAADVLYDCLPLYHsAGNII 299
Cdd:PRK05857 158 ------ASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdiLQKEGLNWVTWVVGETTYSPLPATH-IGGLW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 300 GVGQCLIYGLTVVLRKKFSASR---FWDDCIKYNCTVVQyigeicryLLKQPVREAERRHRV----RLAVGNGLRpAIWE 372
Cdd:PRK05857 231 WILTCLMHGGLCVTGGENTTSLleiLTTNAVATTCLVPT--------LLSKLVSELKSANATvpslRLVGYGGSR-AIAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 373 E--FTERFGVRQiGEFYGATECNC----------SIANMD-GKVGscgfnsRILP--HVYpirlvkvnedtmelLRDAQG 437
Cdd:PRK05857 302 DvrFIEATGVRT-AQVYGLSETGCtalclptddgSIVKIEaGAVG------RPYPgvDVY--------------LAATDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 438 LCIPCQAGEPGLLVGQINQQDPLRRFdGYVSESATSKKIAhsvfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGE 517
Cdd:PRK05857 361 IGPTAPGAGPSASFGTLWIKSPANML-GYWNNPERTAEVL------IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 518 NVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVadPHSLLDPNAIYQELQKVLAPY-------ARPIFLRLLPQ 590
Cdd:PRK05857 434 NIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV--ASAELDESAARALKHTIAARFrresepmARPSTIVIVTD 511
|
570
....*....|....
gi 38524616 591 VDTTGTFKIQKTRL 604
Cdd:PRK05857 512 IPRTQSGKVMRASL 525
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
78-292 |
7.15e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 64.92 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALVDAGTGECW--------TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLA 149
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADgklaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 150 KAGMEAALLNVNLRREPLAFCLGTSGAKALIfgGEMVAAVAEVSGHLGKSLIKF---CSGDLGPEGILPDTHLLDPLLKE 226
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI--GIPKAHLARRLFGWGKPSVRRlvtVGGRLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 227 ASTAPLAQipskgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLY 292
Cdd:PRK09274 166 FPMADLAP------DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF 225
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
76-542 |
8.54e-11 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 64.90 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 76 HTIPRIFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVAN-LFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMe 154
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGK--TITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 155 aALLNVNLRREP--LAFCLGTSGAKALI----FGGEMVAAVAEVSGhlgKSLIKFCSGDL--GPEGIL------------ 214
Cdd:PRK08751 102 -TVVNVNPLYTPreLKHQLIDSGASVLVvidnFGTTVQQVIADTPV---KQVITTGLGDMlgFPKAALvnfvvkyvkklv 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 215 PDTHLLDPL-LKEA------STAPLAQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHH-----AYRMQAA 282
Cdd:PRK08751 178 PEYRINGAIrFREAlalgrkHSMPTLQIEP---DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagtGKLEEGC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 283 DVLYDCLPLYH----SAGNIIGVGqclIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRV 358
Cdd:PRK08751 255 EVVITALPLYHifalTANGLVFMK---IGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 359 RLAVGNGL--RPAIWEEFTERFGVRQIgEFYGATECNCSIA----NMDGKVGSCGFnsrilphvyPIrlvkvnEDTMELL 432
Cdd:PRK08751 332 KMTLGGGMavQRSVAERWKQVTGLTLV-EAYGLTETSPAACinplTLKEYNGSIGL---------PI------PSTDACI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 433 RDAQGLCIPcqAGEpgllVGQINQQDPlRRFDGYVSESATSKKIAHSvfskgDSAYLSGDVLVMDELGYMYFRDRSGDTF 512
Cdd:PRK08751 396 KDDAGTVLA--IGE----IGELCIKGP-QVMKGYWKRPEETAKVMDA-----DGWLHTGDIARMDEQGFVYIVDRKKDMI 463
|
490 500 510
....*....|....*....|....*....|
gi 38524616 513 RWRGENVSTTEVEGVLSRLLGQTDVAVYGV 542
Cdd:PRK08751 464 LVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
86-603 |
1.42e-10 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 64.12 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 86 VQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK---------AG 152
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARigavhsvvfAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 153 MEAallnvnlrrEPLAFCLGTSGAKALIF------GGEMV-------AAVAE--------VSGHLGKSlIKFCSG-DLgp 210
Cdd:cd05966 143 FSA---------ESLADRINDAQCKLVITadggyrGGKVIplkeivdEALEKcpsvekvlVVKRTGGE-VPMTEGrDL-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 211 egilpdthLLDPLLKEASTaplaQIPSKGMD--DRLFYIYTSGTTGLPKAaiVVHSR--YYRMAAFGHH---AYRMQ--- 280
Cdd:cd05966 211 --------WWHDLMAKQSP----ECEPEWMDseDPLFILYTSGSTGKPKG--VVHTTggYLLYAATTFKyvfDYHPDdiy 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 281 --AADVlydclplyhsaGNIIG----VGQCLIYGLTVVLrkkF-------SASRFWDDCIKYNCTVVQYIGEICRYLLKQ 347
Cdd:cd05966 277 wcTADI-----------GWITGhsyiVYGPLANGATTVM---FegtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 348 PvREAERRH-----RVRLAVGNGLRPAIWEEFTERFGVRQ--IGEFYGATEC-NCSIANMDG----KVGSCGFNsriLPH 415
Cdd:cd05966 343 G-DEWVKKHdlsslRVLGSVGEPINPEAWMWYYEVIGKERcpIVDTWWQTETgGIMITPLPGatplKPGSATRP---FFG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 416 VYPirlVKVNEDTMELLRDAQG-LCIpcQAGEPGLLVGQINqqDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVL 494
Cdd:cd05966 419 IEP---AILDEEGNEVEGEVEGyLVI--KRPWPGMARTIYG--DHERYEDTY--------------FSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 495 VMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLsrllgqtdvavygVAVPGVegkAGMAAVADPHSlLDPNAIY----- 569
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL-------------VAHPAV---AEAAVVGRPHD-IKGEAIYafvtl 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 38524616 570 -----------QEL----QKVLAPYARP---IFLRLLPqvdttgtfkiqKTR 603
Cdd:cd05966 541 kdgeepsdelrKELrkhvRKEIGPIATPdkiQFVPGLP-----------KTR 581
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
83-264 |
2.84e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 63.28 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 83 QAVVQRQPERLALVDA---GTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGmeaALLN 159
Cdd:PRK03584 91 NLLRHRRDDRPAIIFRgedGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLG---AIWS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VnlrreplafC---LGTSGA---------KALI------FGG---EMVAAVAEVSGHLgKSLIKFCS----GDLGPEGIL 214
Cdd:PRK03584 168 S---------CspdFGVQGVldrfgqiepKVLIavdgyrYGGkafDRRAKVAELRAAL-PSLEHVVVvpylGPAAAAAAL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 38524616 215 PDTHLLDPLLKEASTAPL--AQIPskgMDDRLFYIYTSGTTGLPKAaiVVHS 264
Cdd:PRK03584 238 PGALLWEDFLAPAEAAELefEPVP---FDHPLWILYSSGTTGLPKC--IVHG 284
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
90-545 |
5.94e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 62.34 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGTGECWTfAQLDAYSNAVANLFrQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:PLN03102 28 PNRTSIIYGKTRFTWP-QTYDRCCRLAASLI-SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIFGGEMVAAVAEVSghlgkSLIKFCSGDLGPEGILpdTHLLD----PLLKEASTAPLAQI--PSKGMDDR 243
Cdd:PLN03102 106 ILRHAKPKILFVDRSFEPLAREVL-----HLLSSEDSNLNLPVIF--IHEIDfpkrPSSEELDYECLIQRgePTPSLVAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 244 LFYI----------YTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVL 313
Cdd:PLN03102 179 MFRIqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 314 RkKFSASRFWDDCIKYNCTVVQYIGEICRYLLK-QPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVrQIGEFYGATEC 392
Cdd:PLN03102 259 R-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 393 NcsianmdGKVGSCGFNSRI--LPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEP--GLLVGQINQQDPLrRFDGYVS 468
Cdd:PLN03102 337 T-------GPVLFCEWQDEWnrLPENQQMELKARQGVSILGLADVDVKNKETQESVPrdGKTMGEIVIKGSS-IMKGYLK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 469 E-SATSKKIAHSVFSkgdsaylSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVygVAVP 545
Cdd:PLN03102 409 NpKATSEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV--VAMP 477
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
70-284 |
9.34e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 61.98 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 70 RHQRAGHTIPRIFQAVVQRQPERLALVDAGTGecWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEgRPEFVGLWL-GL 148
Cdd:PRK10252 452 AVEIPETTLSALVAQQAAKTPDAPALADARYQ--FSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAI 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 149 AKAGmeAALLNVNLRR--EPLAFCLGTSGAKALIfggemvaAVAEVSGHlgkslikfcsgdlgpegiLPDTHLLDPLLKE 226
Cdd:PRK10252 529 VEAG--AAWLPLDTGYpdDRLKMMLEDARPSLLI-------TTADQLPR------------------FADVPDLTSLCYN 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 227 ASTAPlAQIPSKGM---DDRLFYIYTSGTTGLPKAAIVVH----SRYYRMaafgHHAYRMQAADV 284
Cdd:PRK10252 582 APLAP-QGAAPLQLsqpHHTAYIIFTSGSTGRPKGVMVGQtaivNRLLWM----QNHYPLTADDV 641
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-263 |
1.39e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 72 QRAGHTIPRIFQAVVQRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKA 151
Cdd:PRK05691 2184 ARLDQTLHGLFAAQAARTPQAPALTFAG--QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 152 GMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEvsghLGKSLIKFCSGDLGPegilpdthlldpLLKEASTAP 231
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE----LPAGVARWCLEDDAA------------ALAAYSDAP 2325
|
170 180 190
....*....|....*....|....*....|..
gi 38524616 232 LAQIpsKGMDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:PRK05691 2326 LPFL--SLPQHQAYLIYTSGSTGKPKGVVVSH 2355
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
242-601 |
1.68e-09 |
|
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: 59.97 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYrmAAFGH---HAYRMQAADVLYDCLPLYHSAGN------IIGVGQCLIYGLTVV 312
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF--AVPDIlqkEGLNWVVGDVTYLPLPATHIGGLwwiltcLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 313 LRKKFSASRFWDDCIkyNCTVVQYIGEICRyLLKQPVREAERrhrVRLAVGNGLRP-AIWEEFTERFGVRQIGEFYGATE 391
Cdd:cd17635 80 YKSLFKILTTNAVTT--TCLVPTLLSKLVS-ELKSANATVPS---LRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 392 CN--CSIANMDG--KVGSCGfnsrilpHVYPIRLVKVnedtmellRDAQGLCIPcqAGEPGLLVGQINqqdplRRFDGYV 467
Cdd:cd17635 154 TGtaLCLPTDDDsiEINAVG-------RPYPGVDVYL--------AATDGIAGP--SASFGTIWIKSP-----ANMLGYW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 468 SESA-TSKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYgvAVPG 546
Cdd:cd17635 212 NNPErTAEVLIDGWVNTGDLGERRED-------GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISD 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 547 VEGKAGMAAVADPHSLLDPNAIYQELQKV---LAPYARPIFLRLLPQVDTTGTFKIQK 601
Cdd:cd17635 283 EEFGELVGLAVVASAELDENAIRALKHTIrreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-264 |
1.90e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.13 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALVdagTGE-CWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAA 156
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALA---FGEeTLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREPLAFCLGTSGAKALIfggemvaavaeVSGHLGKSLikfcSGDLGPEGILPDThlLDPLLKEASTAPlaqiP 236
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLL-----------SQSHLGRKL----PLAAGVQVLDLDR--PAAWLEGYSEEN----P 648
|
170 180 190
....*....|....*....|....*....|
gi 38524616 237 SKGMD-DRLFY-IYTSGTTGLPKAAIVVHS 264
Cdd:PRK12316 649 GTELNpENLAYvIYTSGSTGKPKGAGNRHR 678
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
47-604 |
2.09e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 60.40 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 47 VCKTARRDLFGLSVLI----RVRLELRRHQRAGHTIPRIFQAVVQ-RQPERLALVDAGTGecWTFAQLDAYSNAVANLFR 121
Cdd:PRK13383 1 VAPTAARALVRSGLLNppspRAVLRLLREASRGGTNPYTLLAVTAaRWPGRTAIIDDDGA--LSYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 122 QLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlGKSLI 201
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGA----DDAVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 202 KfcsgdlgpegILPDTHLLDPLLKEASTAPLAQIpskgmddrlfYIYTSGTTGLPKAaivVHSRYYRMAAFG-----HHA 276
Cdd:PRK13383 155 V----------IDPATAGAEESGGRPAVAAPGRI----------VLLTSGTTGKPKG---VPRAPQLRSAVGvwvtiLDR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 277 YRMQAADVLYDCLPLYHSagniIGVGQCLI---YGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAE 353
Cdd:PRK13383 212 TRLRTGSRISVAMPMFHG----LGLGMLMLtiaLGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 354 RRH----RVRLAVGNGLRPAIWEEFTERFGvRQIGEFYGATECNcsianmdgkVGSCGfnsrilphvypirlvkvnedTM 429
Cdd:PRK13383 288 RNPlpqlRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVG---------IGALA--------------------TP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 430 ELLRDAqglciPCQAGEPglLVGQinqqdPLRRFDGY---VSESATSK-----KIAHSVFSKG------DSAYLSGDVLV 495
Cdd:PRK13383 338 ADLRDA-----PETVGKP--VAGC-----PVRILDRNnrpVGPRVTGRifvggELAGTRYTDGggkavvDGMTSTGDMGY 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 496 MDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKV 575
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR 485
|
570 580
....*....|....*....|....*....
gi 38524616 576 LAPYARPIFLRLLPQVDTTGTFKIQKTRL 604
Cdd:PRK13383 486 VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
78-607 |
3.62e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 59.78 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALvdAGTGECWTFAQLDAYSNAVANLFRQL-GFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaA 156
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAF--SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVN---LRREpLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDLG-------------------PEGI 213
Cdd:PRK05677 102 VVNTNplyTARE-MEHQFNDSGAKALVCLANMAHLAEKVLPKTGvKHVIVTEVADMLpplkrllinavvkhvkkmvPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 214 LPDTHLLDPLLKEASTAPLAQIPSKGmDDRLFYIYTSGTTGLPKAAIVVHSRyyrMAAFGHHAYRMQAADVLYDC----- 288
Cdd:PRK05677 181 LPQAVKFNDALAKGAGQPVTEANPQA-DDVAVLQYTGGTTGVAKGAMLTHRN---LVANMLQCRALMGSNLNEGCeilia 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 289 -LPLYH--------SAGNIIGVGQCLIY------GLTVVLRK-KFSAsrFwddcIKYNCTVVQyigeICRyllkqpvREA 352
Cdd:PRK05677 257 pLPLYHiyaftfhcMAMMLIGNHNILISnprdlpAMVKELGKwKFSG--F----VGLNTLFVA----LCN-------NEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 353 ER-----RHRVRLAVGNGLRPAIWEEFTERFGVrQIGEFYGATECN--CSIANMDG-KVGSCGfnsriLPhvYPIRLVKV 424
Cdd:PRK05677 320 FRkldfsALKLTLSGGMALQLATAERWKEVTGC-AICEGYGMTETSpvVSVNPSQAiQVGTIG-----IP--VPSTLCKV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 425 -NEDTMELLRDAQG-LCIPcqagEPGLLVGQINQQDplrrfdgyvsesATSKKIAHSVFSKgdsaylSGDVLVMDELGYM 502
Cdd:PRK05677 392 iDDDGNELPLGEVGeLCVK----GPQVMKGYWQRPE------------ATDEILDSDGWLK------TGDIALIQEDGYM 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 503 YFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAvpgvEGKAGMA----AVADPHSLLDPNAIYQELQKVLAP 578
Cdd:PRK05677 450 RIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSGEAikvfVVVKPGETLTKEQVMEHMRANLTG 525
|
570 580
....*....|....*....|....*....
gi 38524616 579 YARPIFLRLLPQVDTTGTFKIQKTRLQRE 607
Cdd:PRK05677 526 YKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
85-589 |
5.46e-09 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 59.25 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 85 VVQRQPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNV 160
Cdd:cd05967 60 VEAGRGDQIALIydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 161 NLRREPLAFCLGTSGAKALI---FGGE---------MVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLL-DPLLKEA 227
Cdd:cd05967 140 GFAAKELASRIDDAKPKLIVtasCGIEpgkvvpykpLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDLDwSELLAKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 228 STAPLAQIPSkgmDDRLFYIYTSGTTGLPKAaiVV-----HS--RYYRMAafghHAYRMQAADVLYdclplyhsAGNIIG 300
Cdd:cd05967 220 EPVDCVPVAA---TDPLYILYTSGTTGKPKG--VVrdnggHAvaLNWSMR----NIYGIKPGDVWW--------AASDVG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 301 --VGQCLI-YG------LTVVLRKKFS----ASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAE-RRH-----RVRLA 361
Cdd:cd05967 283 wvVGHSYIvYGpllhgaTTVLYEGKPVgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYiKKYdlsslRTLFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 362 VGNGLRPAIWEEFTERFGVRQIgEFYGATE------CNCS-IANMDGKVGSCGfnsriLPhvYPIRLVKVNEDTMEllrd 434
Cdd:cd05967 363 AGERLDPPTLEWAENTLGVPVI-DHWWQTEtgwpitANPVgLEPLPIKAGSPG-----KP--VPGYQVQVLDEDGE---- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 435 aqglciPCQAGEPGLLV-------GQINQ--QDPLRRFDGYvsesatskkiahsvFSKGDSAYLSGDVLVMDELGYMYFR 505
Cdd:cd05967 431 ------PVGPNELGNIViklplppGCLLTlwKNDERFKKLY--------------LSKFPGYYDTGDAGYKDEDGYLFIM 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 506 DRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVaVPGVEGKAGMA-AVADPHSLLDPNAIYQELQKV----LAPYA 580
Cdd:cd05967 491 GRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGV-RDELKGQVPLGlVVLKEGVKITAEELEKELVALvreqIGPVA 569
|
570
....*....|..
gi 38524616 581 RP---IFLRLLP 589
Cdd:cd05967 570 AFrlvIFVKRLP 581
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
116-541 |
6.23e-09 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 58.98 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 116 VANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAaVAEVSGH 195
Cdd:cd05915 37 LMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLP-LVEAIRG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 196 LGKSLIKFCSGDLGPEGILPDTHLLDPLLKeastaplaqiPSKGMD--DRLFYIYTSGTTGLPKAAIVVH-SRYYRMAAF 272
Cdd:cd05915 116 ELKTVQHFVVMDEKAPEGYLAYEEALGEEA----------DPVRVPerAACGMAYTTGTTGLPKGVVYSHrALVLHSLAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 273 GHHAYRMQAADVLYDC-LPLYHSAGniigvgQCLIY------GLTVVLRKKFSASRFWDDCIKYNCTvvQYIGEICRYLL 345
Cdd:cd05915 186 SLVDGTALSEKDVVLPvVPMFHVNA------WCLPYaatlvgAKQVLPGPRLDPASLVELFDGEGVT--FTAGVPTVWLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 346 KQPVREAERRH---RVRLAVGNGLRPAIWEEFtERFGVRQIGEFYGATEcncsianMDGKVGSCGFNSR--ILPHVYPIR 420
Cdd:cd05915 258 LADYLESTGHRlktLRRLVVGGSAAPRSLIAR-FERMGVEVRQGYGLTE-------TSPVVVQNFVKSHleSLSEEEKLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 421 LVKvnEDTMELLRDAQGLCIPCQAGEPGllVGQINQQDPLRR---FDGYVSESATSKKIAhsvFSKGdsAYLSGDVLVMD 497
Cdd:cd05915 330 LKA--KTGLPIPLVRLRVADEEGRPVPK--DGKALGEVQLKGpwiTGGYYGNEEATRSAL---TPDG--FFRTGDIAVWD 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 38524616 498 ELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYG 541
Cdd:cd05915 401 EEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-542 |
1.12e-08 |
|
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: 57.39 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 242 DRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFG--------------HHAYRMQAADVLYDCLPLYHSAGNIIGVGQcLIY 307
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGadfgtgeftpsedaHKAAAAAAGTVMFPAPPLMHGTGSWTAFGG-LLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 308 GLTVVL-RKKFSASRFWDDCIKYNCTVVQYIGEIcrylLKQPVREAERRHRVR-----LAVGNG---LRPAIWEEFTERF 378
Cdd:cd05924 83 GQTVVLpDDRFDPEEVWRTIEKHKVTSMTIVGDA----MARPLIDALRDAGPYdlsslFAISSGgalLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 379 GVRQIGEFYGATEC-NCSIANMDGKVGSCGFNSRILPhvypiRLVKVNEDTMELLRDAQGlcipcqagepgllVGQINQQ 457
Cdd:cd05924 159 PNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP-----DTVVLDDDGRVVPPGSGG-------------VGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 458 D--PLrrfdGYVSEsatSKKIAHSVFSKGDSAY-LSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQ 534
Cdd:cd05924 221 GhiPL----GYYGD---EAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV 293
|
....*...
gi 38524616 535 TDVAVYGV 542
Cdd:cd05924 294 YDVLVVGR 301
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
90-271 |
1.30e-08 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 57.65 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 90 PERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAF 169
Cdd:cd17652 1 PDAPAVVFGD--ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 170 CLGTSGAKALIfggemvaavaevsghlgkslikfcsgdlgpegilpdthlldpllkeasTAPlaqipskgmdDRLFY-IY 248
Cdd:cd17652 79 MLADARPALLL------------------------------------------------TTP----------DNLAYvIY 100
|
170 180
....*....|....*....|...
gi 38524616 249 TSGTTGLPKAAIVVHSRYYRMAA 271
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAA 123
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
87-314 |
1.40e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 57.57 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 87 QRQPERLALVDAGtgECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREP 166
Cdd:PRK09029 14 QVRPQAIALRLND--EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 167 LafclgtsgakalifggemvaavAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAP--LAQIpskgmddrl 244
Cdd:PRK09029 92 L----------------------EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPqrLATM--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 245 fyIYTSGTTGLPKAaiVVHSryyrmaafgHHAYRMQAADVL----YDC-------LPLYHSAGNIIgVGQCLIYGLTVVL 313
Cdd:PRK09029 141 --TLTSGSTGLPKA--AVHT---------AQAHLASAEGVLslmpFTAqdswllsLPLFHVSGQGI-VWRWLYAGATLVV 206
|
.
gi 38524616 314 R 314
Cdd:PRK09029 207 R 207
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
241-606 |
1.55e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 57.60 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 241 DDRLFYIYTSGTTGLPKAAIVVHSRY--YRMAAFgHHAYRMQAADVLY---DClplyhsaGNIIGVGQC----LIYGLTV 311
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmvYTATTF-KYAFDYKPTDVYWctaDC-------GWITGHSYVtygpMLNGATV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 312 VLRKKF----SASRFWDDCIKYNCTVVQYIGEICRYLLK---QPVREAERRH-RVRLAVGNGLRPAIWEEFTERFGvrqi 383
Cdd:PLN02654 347 LVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRdgdEYVTRHSRKSlRVLGSVGEPINPSAWRWFFNVVG---- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 gefygatECNCSIANMDGKVGSCGFNSRILPHVYP------------IRLVKVNEDTMELLRDAQG-LCIpcQAGEPGL- 449
Cdd:PLN02654 423 -------DSRCPISDTWWQTETGGFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGKEIEGECSGyLCV--KKSWPGAf 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 450 --LVGQINQQDP--LRRFDGYvsesatskkiahsvfskgdsaYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVE 525
Cdd:PLN02654 494 rtLYGDHERYETtyFKPFAGY---------------------YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 526 GVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVadphSLLDPNAIYQELQKVL--------APYARPIFLRLLPQVDTTGTF 597
Cdd:PLN02654 553 SALVSHPQCAEAAVVGIEHE-VKGQGIYAFV----TLVEGVPYSEELRKSLiltvrnqiGAFAAPDKIHWAPGLPKTRSG 627
|
....*....
gi 38524616 598 KIQKTRLQR 606
Cdd:PLN02654 628 KIMRRILRK 636
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
106-379 |
1.90e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.32 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 106 FAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVnlrrePLAF------------CLGT 173
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL-----PMGFggresyiaqlrgMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 174 SGAKALIFGGEMVAAVAEVSGHLGkslikfcsgdlGPEGILPDthllDPLLKEASTAPLAQI-PskgmDDRLFYIYTSGT 252
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNP-----------LLHVLSHA----WFKALPEADVALPRPtP----DDIAYLQYSSGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 253 TGLPKAAIVVHSRYyrMA---AFGHHAYRMQAADVLYDCLPLYHSAGnIIGvgqCLIYGLTVVLRKKFSASR-F------ 322
Cdd:PRK09192 188 TRFPRGVIITHRAL--MAnlrAISHDGLKVRPGDRCVSWLPFYHDMG-LVG---FLLTPVATQLSVDYLPTRdFarrplq 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 323 WDDCIKYNCTVVQY---IG-EICryllKQPVREAERRH----RVRLAvGNG---LRPAIWEEFTERFG 379
Cdd:PRK09192 262 WLDLISRNRGTISYsppFGyELC----ARRVNSKDLAEldlsCWRVA-GIGadmIRPDVLHQFAEAFA 324
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
105-264 |
1.96e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 57.29 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 MVAAVAEVSGHLG-KSLIKFCSGDLgPEG-------ILPDTHLLDPLLKEASTAPLAqIPSKGmDDRLFYIYTSGTTGLP 256
Cdd:PTZ00216 203 NVPNLLRLMKSGGmPNTTIIYLDSL-PASvdtegcrLVAWTDVVAKGHSAGSHHPLN-IPENN-DDLALIMYTSGTTGDP 279
|
....*...
gi 38524616 257 KAaiVVHS 264
Cdd:PTZ00216 280 KG--VMHT 285
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
523-598 |
2.67e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 51.01 E-value: 2.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38524616 523 EVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMA-AVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFK 598
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAfVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
247-556 |
5.23e-08 |
|
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: 55.35 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGniIGVGQCLIY--GLTVVLRKkFSASRFWD 324
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHagGANVVMEK-FDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 325 DCIKYNCTVVQYIGEICRYLLkqpvrEAERRHRVRLAvgnGLR-------PAIWEEFTERFGvrqiGEF---YGATECNC 394
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLL-----DAAEKSGVDLS---SLRhvlgldaPETIQRFEETTG----ATFwslYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 395 --SIANMDGKVGSCGfnsRILPHVyPIRLVKVNEDtmellrdaqglciPCQAGEPGllvgQINQQDPLRrFDGYVSESAT 472
Cdd:cd17637 151 lvTLSPYRERPGSAG---RPGPLV-RVRIVDDNDR-------------PVPAGETG----EIVVRGPLV-FQGYWNLPEL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 473 SkkiAHSvFSKGdsAYLSGDVLVMDELGYMYFRDRSG--DTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGvaVPGVEGK 550
Cdd:cd17637 209 T---AYT-FRNG--WHHTGDLGRFDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIG--VPDPKWG 280
|
....*.
gi 38524616 551 AGMAAV 556
Cdd:cd17637 281 EGIKAV 286
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
247-608 |
8.59e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 55.00 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 247 IYTSGTTGLPKAaiVVHSRyyRMAAFG----HHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRF 322
Cdd:PRK07787 134 VYTSGTTGPPKG--VVLSR--RAIAADldalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 323 WDDCiKYNCTVvqYIGEICRYL-LKQPVREAERRHRVRLAV-GNGLRPA-IWEEFTERFGVRQIgEFYGATEC--NCSI- 396
Cdd:PRK07787 210 AQAL-SEGGTL--YFGVPTVWSrIAADPEAARALRGARLLVsGSAALPVpVFDRLAALTGHRPV-ERYGMTETliTLSTr 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 397 ANMDGKVGSCGFnsrilphvyPIRLVKVNedtmelLRDAQGLCIPCQaGEPgllVGQINQQDPLrRFDGYVSE-SATSkk 475
Cdd:PRK07787 286 ADGERRPGWVGL---------PLAGVETR------LVDEDGGPVPHD-GET---VGELQVRGPT-LFDGYLNRpDATA-- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 476 iahSVFSkGDSAYLSGDVLVMDELGYMYFRDR-SGDTFRWRGENVSTTEVEGVlsrLLGQTDVAvyGVAVPGVE----GK 550
Cdd:PRK07787 344 ---AAFT-ADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETA---LLGHPGVR--EAAVVGVPdddlGQ 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 38524616 551 AGMAAVAdPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREG 608
Cdd:PRK07787 415 RIVAYVV-GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
81-424 |
1.64e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 54.59 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 81 IFQAVVQ----RQPERLALVDAGTGECwTFAQLDAYSNAVANLFRQlGFAPGDVVAIFLegrPEFVGL---WLGLAKAGM 153
Cdd:PRK06814 633 LFEALIEaakiHGFKKLAVEDPVNGPL-TYRKLLTGAFVLGRKLKK-NTPPGENVGVML---PNANGAavtFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 154 EAALLN-----VNLrrepLAFC-------LGTSgaKALIFGGEMVAAVAEVSGHLgkSLIKFcsgdlgpEGILPDTHLLD 221
Cdd:PRK06814 708 VPAMINfsagiANI----LSACkaaqvktVLTS--RAFIEKARLGPLIEALEFGI--RIIYL-------EDVRAQIGLAD 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 222 PLL-KEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVH----SRYYRMAA---FGhhayrmqAADVLYDCLPLYH 293
Cdd:PRK06814 773 KIKgLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHrnllANRAQVAAridFS-------PEDKVFNALPVFH 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 294 SAGNIIGVGQCLIYGLTVVLRKK-------------------FSASRFWDDcikYNCTVVQYIGEICRYLL--KQPVREA 352
Cdd:PRK06814 846 SFGLTGGLVLPLLSGVKVFLYPSplhyriipeliydtnatilFGTDTFLNG---YARYAHPYDFRSLRYVFagAEKVKEE 922
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 353 ERRhrvrlavgnglrpaIWeefTERFGVRqIGEFYGATECNCSIA-N--MDGKVGSCGfnsRILPHVYPiRLVKV 424
Cdd:PRK06814 923 TRQ--------------TW---MEKFGIR-ILEGYGVTETAPVIAlNtpMHNKAGTVG---RLLPGIEY-RLEPV 975
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-296 |
1.66e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 54.21 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 76 HTIPRIFQAVVQRQPERLALV------DAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFV-GLWlGL 148
Cdd:cd05906 6 EGAPRTLLELLLRAAERGPTKgityidADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIpAFW-AC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 149 AKAGMEAALLNV-------NLRREPLAFCLGTSGAKALIFGGEMVAAVAEVsghlgkslikfcsgdLGPEGILPDTHLLD 221
Cdd:cd05906 85 VLAGFVPAPLTVpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFAGL---------------ETLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38524616 222 PLLKEasTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG 296
Cdd:cd05906 150 EELLD--TAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-313 |
2.31e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 83 QAVVQR---QPERLALV----DAGTGECWTFAQLDAYSNAVANLFRQLGfAPGDVVAIFLEGRPEFVGLWLGLAKAGMEA 155
Cdd:PRK05691 13 QALQRRaaqTPDRLALRfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 156 A---------------LLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAevsghlgkslikfcsgdlgPEGILPDThlL 220
Cdd:PRK05691 92 VpayppesarrhhqerLLSIIADAEPRLLLTVADLRDSLLQMEELAAANA-------------------PELLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 221 DPLLKEASTAPlaQIPSkgmDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAA--DVLYDCLPLYHSAGNI 298
Cdd:PRK05691 151 DPALAEAWQEP--ALQP---DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLI 225
|
250
....*....|....*
gi 38524616 299 IGVGQCLIYGLTVVL 313
Cdd:PRK05691 226 GGLLQPIFSGVPCVL 240
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
105-294 |
3.53e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 53.22 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGE 184
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 185 MVAAVAEVSGHLG--KSLIKFCSGDLGPEGILPDTHLLDPLLKEAStaplAQIPSKGMDDRLF--YIYTSGTTGLPKAAI 260
Cdd:PRK06018 121 FVPILEKIADKLPsvERYVVLTDAAHMPQTTLKNAVAYEEWIAEAD----GDFAWKTFDENTAagMCYTSGTTGDPKGVL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 38524616 261 ------VVHSryyrMAAFGHHAYRMQAADVLYDCLPLYHS 294
Cdd:PRK06018 197 yshrsnVLHA----LMANNGDALGTSAADTMLPVVPLFHA 232
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-559 |
3.93e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 52.83 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 101 GECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALi 180
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 181 fggemvaavaevsghlgkslikFCSgdlgpegilpdthllDPllkeastaplaqipskgmDDRLFYIYTSGTTGLPKAAI 260
Cdd:cd05914 84 ----------------------FVS---------------DE------------------DDVALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 261 VVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSA-----------------SRFW 323
Cdd:cd05914 109 LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSakiialafaqvtptlgvPVPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 324 D-DCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAV--------------GNGLRPAIwEEFTERFGVRQIgEFYG 388
Cdd:cd05914 189 ViEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFKKVheafggnikefvigGAKINPDV-EEFLRTIGFPYT-IGYG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 389 ATECN---CSIANMDGKVGSCGFnsrilphvyPIRLVKVNEDtmellrdaqglcipcqAGEPGLLVGQINQQDPLRRFDG 465
Cdd:cd05914 267 MTETApiiSYSPPNRIRLGSAGK---------VIDGVEVRID----------------SPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 466 YVSESATSkkiahSVFSKgDSAYLSGDVLVMDELGYMYFRDRSGDTFRW-RGENVSTTEVEgvlSRLLGQTDVAVYGVAV 544
Cdd:cd05914 322 YKNPEATA-----EAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE---AKINNMPFVLESLVVV 392
|
490
....*....|....*
gi 38524616 545 pgVEGKAGMAAVADP 559
Cdd:cd05914 393 --QEKKLVALAYIDP 405
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
218-527 |
8.66e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.02 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 218 HLLDPLLkeastAPLAQIPskgmDDRLFYIYTSGTTGLPKAaiVVHSRYYRMAAFGH--HAYRMQAADVLYDCLPLYHSA 295
Cdd:PRK08043 351 HLLMPRL-----AQVKQQP----EDAALILFTSGSEGHPKG--VVHSHKSLLANVEQikTIADFTPNDRFMSALPLFHSF 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 296 GNIIGVGQCLIYGLTVVLRKKFSASRFWDDCI-KYNCTVV----QYIGEICRYllKQPVREAERRHRVrlAVGNGLRPAI 370
Cdd:PRK08043 420 GLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNYARF--ANPYDFARLRYVV--AGAEKLQEST 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 371 WEEFTERFGVRqIGEFYGATECNCSIA---NMDGKVGSCGfnsRILPHVyPIRLVKVNEDTmellrdaQGLCIpcQAGEP 447
Cdd:PRK08043 496 KQLWQDKFGLR-ILEGYGVTECAPVVSinvPMAAKPGTVG---RILPGM-DARLLSVPGIE-------QGGRL--QLKGP 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 448 GLLVGQINQQDPlrrfdgYVSESATSKKiAHSVFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGV 527
Cdd:PRK08043 562 NIMNGYLRVEKP------GVLEVPTAEN-ARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL 632
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
105-293 |
1.31e-06 |
|
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: 51.45 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGF--APGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNVnlrrePLafcLGTSGAKALIFg 182
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPE----WIISELACYAYSLVTV-----PL---YDTLGPEAIEY- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 183 gemVAAVAEVSghlgkslIKFCSGDLgpegilpDTHLLDPLLKEASTAPLAQIPSKGMDdrLFYI-YTSGTTGLPKAAIV 261
Cdd:cd05927 74 ---ILNHAEIS-------IVFCDAGV-------KVYSLEEFEKLGKKNKVPPPPPKPED--LATIcYTSGTTGNPKGVML 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 38524616 262 VH----SRYYRMAAFGHHAYRMQAADVLYDCLPLYH 293
Cdd:cd05927 135 THgnivSNVAGVFKILEILNKINPTDVYISYLPLAH 170
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
81-528 |
5.16e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.44 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 81 IFQAVVQRQPERLALVDAGTgeCWTFAQLDAYSNAVANLFRQ-LGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMeaALLN 159
Cdd:PRK12492 29 VFERSCKKFADRPAFSNLGV--TLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGL--IVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 160 VN---LRREpLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG-KSLIKFCSGDLGP--------------EGILPDTHL-- 219
Cdd:PRK12492 105 TNplyTARE-MRHQFKDSGARALVYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLPaakgwlvntvvdkvKKMVPAYHLpq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 220 ---LDPLLKEASTAPLAQIPsKGMDDRLFYIYTSGTTGLPKAAIVVHSR--------YYRMAAFGHHAYRM--QAADVLY 286
Cdd:PRK12492 184 avpFKQALRQGRGLSLKPVP-VGLDDIAVLQYTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLmkEGQEVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 287 DCLPLYHsagniigvgqclIYGLT-------------VVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAE 353
Cdd:PRK12492 263 APLPLYH------------IYAFTancmcmmvsgnhnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 354 RRHRVRL--AVGNGLRPAIWEEFTERFGVRqIGEFYGATECN-CSIANMDG---KVGSCGfnsriLPhvYPIRLVKV-NE 426
Cdd:PRK12492 331 DFSALKLtnSGGTALVKATAERWEQLTGCT-IVEGYGLTETSpVASTNPYGelaRLGTVG-----IP--VPGTALKViDD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 427 DTMELLRDAQG-LCIPcqagEPGLLVGQINQQDplrrfdgyvsesATSKKIahsvfsKGDSAYLSGDVLVMDELGYMYFR 505
Cdd:PRK12492 403 DGNELPLGERGeLCIK----GPQVMKGYWQQPE------------ATAEAL------DAEGWFKTGDIAVIDPDGFVRIV 460
|
490 500
....*....|....*....|...
gi 38524616 506 DRSGDTFRWRGENVSTTEVEGVL 528
Cdd:PRK12492 461 DRKKDLIIVSGFNVYPNEIEDVV 483
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
235-536 |
1.06e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 48.66 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 235 IPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG-NIIGV-----GQCLIYG 308
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfNSCTLfpllsGVPVVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 309 LTVVLRKKFSasRFWDDcikyncTVVQYIGE---ICRYLLKQPVREAERRHRVRLAV--GNGLRPAIWEEFTERFGVRQI 383
Cdd:PRK06334 257 YNPLYPKKIV--EMIDE------AKVTFLGStpvFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEFYGATECN--CSIANMDG-KVGSCgfnsrilphvypirlVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQdpl 460
Cdd:PRK06334 329 RQGYGTTECSpvITINTVNSpKHESC---------------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL--- 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38524616 461 rrFDGYVSESATSKKIAHSvfskGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTD 536
Cdd:PRK06334 391 --FSGYLGEDFGQGFVELG----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNA 460
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
78-272 |
1.58e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.14 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 78 IPRIFQAVVQRQPERLALVDAGTGEC-------WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAK 150
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 151 AGmeaALLNVNLRREPLA---FCLGTSGAKALIfggemvaaVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDP----- 222
Cdd:TIGR03443 318 AG---ATFSVIDPAYPPArqtIYLSVAKPRALI--------VIEKAGTLDQLVRDYIDKELELRTEIPALALQDDgslvg 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 223 -LLKEASTAPLAQIPSK---------GMDDRLFYIYTSGTTGLPKAaivVHSRYYRMAAF 272
Cdd:TIGR03443 387 gSLEGGETDVLAPYQALkdtptgvvvGPDSNPTLSFTSGSEGIPKG---VLGRHFSLAYY 443
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
73-355 |
6.67e-05 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 45.91 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 73 RAGHTIPRIFQAVVQRQPERLAL--------VDAGTG----------ECWTFAQLDAYSNAVANLFR-QLGFAPGDVVAI 133
Cdd:cd17632 19 RPGLRLAQIIATVMTGYADRPALgqratelvTDPATGrttlrllprfETITYAELWERVGAVAAAHDpEQPVRPGDFVAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 134 FLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMV-AAVAEVSGHLG-KSLIKFcsgDLGPE 211
Cdd:cd17632 99 LGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLdLAVEAVLEGGTpPRLVVF---DHRPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 212 GilpDTH-------------------LLDPLLKEASTAPLAQIPSKGMD-DRL-FYIYTSGTTGLPKAAIVVHSRYYRM- 269
Cdd:cd17632 176 V---DAHraalesarerlaavgipvtTLTLIAVRGRDLPPAPLFRPEPDdDPLaLLIYTSGSTGTPKGAMYTERLVATFw 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 270 -AAFGHHAYRMQAADVLyDCLPLYHSAGNIIGVGQcLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQP 348
Cdd:cd17632 253 lKVSSIQDIRPPASITL-NFMPMSHIAGRISLYGT-LARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRY 330
|
....*..
gi 38524616 349 VREAERR 355
Cdd:cd17632 331 QAELDRR 337
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
84-528 |
6.76e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 45.99 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 84 AVVQrqPERLALVDAGTGECW--TFAQLDAYSNAVANlfRQLGfaPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVN 161
Cdd:PLN02479 30 AVVH--PTRKSVVHGSVRYTWaqTYQRCRRLASALAK--RSIG--PGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 162 LRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKS---------LIKFCSGDLGPEGIlpdTHLL-------DPLLK 225
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKkkssfkpplLIVIGDPTCDPKSL---QYALgkgaieyEKFLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 226 EASTApLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCL 305
Cdd:PLN02479 181 TGDPE-FAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 306 IYGLTVVLRKkFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREA--ERRHRVRLAVGNGLRPAIWEEFTERFGVRqI 383
Cdd:PLN02479 260 LCGTNICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHVMTAGAAPPPSVLFAMSEKGFR-V 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 384 GEFYGATECNcsianmdGKVGSCGFNSRI--LPhvyPIRLVKVNEDTMELLRDAQGL-CIPCQAGEP----GLLVGQInq 456
Cdd:PLN02479 338 THTYGLSETY-------GPSTVCAWKPEWdsLP---PEEQARLNARQGVRYIGLEGLdVVDTKTMKPvpadGKTMGEI-- 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38524616 457 qdpLRRFDGYVSESATSKKIAHSVFSKGdsAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVL 528
Cdd:PLN02479 406 ---VMRGNMVMKGYLKNPKANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
484-599 |
9.11e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 45.41 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 484 GDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPgVEGKAGMAAVADPHSLl 563
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDP-VAGERVKAKVISHEEI- 366
|
90 100 110
....*....|....*....|....*....|....*.
gi 38524616 564 DPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKI 599
Cdd:PRK08308 367 DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
88-263 |
1.10e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.49 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 88 RQPERLALvdaGTGECWTFAQ-LDAYSNAVANLFrQLGFAPGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNV----NL 162
Cdd:PLN02387 94 RKFEKLHL---GEYEWITYGQvFERVCNFASGLV-ALGHNKEERVAIFADTRAE----WLIALQGCFRQNITVVtiyaSL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 163 RREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLG--KSLIkfCSGDLGPEGILPDTHL-------LDPLLKEASTAPL- 232
Cdd:PLN02387 166 GEEALCHSLNETEVTTVICDSKQLKKLIDISSQLEtvKRVI--YMDDEGVDSDSSLSGSsnwtvssFSEVEKLGKENPVd 243
|
170 180 190
....*....|....*....|....*....|.
gi 38524616 233 AQIPSKgmDDRLFYIYTSGTTGLPKAAIVVH 263
Cdd:PLN02387 244 PDLPSP--NDIAVIMYTSGSTGLPKGVMMTH 272
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-293 |
1.91e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 44.70 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 W-TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEfvglWLGLAKAGMEAALLNVnlrrePLAFCLGTSGAKALIFG 182
Cdd:PLN02736 78 WmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPE----WLIVDHACSAYSYVSV-----PLYDTLGPDAVKFIVNH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 183 GEmVAAVAEVSGHLgKSLIKFCSgDL----------GPEGILPDTHL--------LDPLLKEASTAPLAQIPSKGmDDRL 244
Cdd:PLN02736 149 AE-VAAIFCVPQTL-NTLLSCLS-EIpsvrlivvvgGADEPLPSLPSgtgveivtYSKLLAQGRSSPQPFRPPKP-EDVA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 38524616 245 FYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYH 293
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH 273
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
89-264 |
1.99e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); 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. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 44.57 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 89 QPERLALVDAGTGEC--WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGM----------EAA 156
Cdd:cd05943 82 ADDPAAIYAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwsscspdfgVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 157 LLNVNLRREP--LAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKS-LIKFCSGDLGPE-GILPDTHLLDPLLKEASTAPL 232
Cdd:cd05943 162 VLDRFGQIEPkvLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVvVVPYTVAAGQPDlSKIAKALTLEDFLATGAAGEL 241
|
170 180 190
....*....|....*....|....*....|....
gi 38524616 233 --AQIPskgMDDRLFYIYTSGTTGLPKAaiVVHS 264
Cdd:cd05943 242 efEPLP---FDHPLYILYSSGTTGLPKC--IVHG 270
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
104-609 |
3.29e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 43.54 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 104 WTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAkaGMEAALLNVNLRREP--LAFCLGTSGAKALIF 181
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVS--GSGAVCHTINPRLFPeqIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 182 GGEMVAAVAEVSGHLG--KSLIKFCSGDLGPEGILP-----------DTHLLDPLLKEASTAPLAqipskgmddrlfyiY 248
Cdd:PRK07008 118 DLTFLPLVDALAPQCPnvKGWVAMTDAAHLPAGSTPllcyetlvgaqDGDYDWPRFDENQASSLC--------------Y 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 249 TSGTTGLPKAAIVVHsRYYRMAAFGH---HAYRMQAADVLYDCLPLYHS-------AGNIIGV-----GQCL----IYGL 309
Cdd:PRK07008 184 TSGTTGNPKGALYSH-RSTVLHAYGAalpDAMGLSARDAVLPVVPMFHVnawglpySAPLTGAklvlpGPDLdgksLYEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 310 TVVLRKKFSASRfwddcikynCTVVQyigeicryLLKQPVREAERRH---RVRLAVGNGLRPAIWEEFTERFGVRQIgEF 386
Cdd:PRK07008 263 IEAERVTFSAGV---------PTVWL--------GLLNHMREAGLRFstlRRTVIGGSACPPAMIRTFEDEYGVEVI-HA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 387 YGATEcncsianMDGKVGSCGFNSRILphvypirlvKVNEDTMELLRDAQGLCIpcqAGEPGLLVGQINQQDPlrrFDGY 466
Cdd:PRK07008 325 WGMTE-------MSPLGTLCKLKWKHS---------QLPLDEQRKLLEKQGRVI---YGVDMKIVGDDGRELP---WDGK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 467 VSESATSKK--IAHSVFsKGDSAYL------SGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVA 538
Cdd:PRK07008 383 AFGDLQVRGpwVIDRYF-RGDASPLvdgwfpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38524616 539 VYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARP---IFLRLLPQvdtTGTFKIQKTRLqREGF 609
Cdd:PRK07008 462 CIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPddvVFVDAIPH---TATGKLQKLKL-REQF 531
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
247-311 |
5.70e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.11 E-value: 5.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38524616 247 IYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDC----LPLYHSAGNIIGVGQCLIYGLTV 311
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQV 224
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
105-298 |
7.93e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 42.29 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIfLEGRPEFV-----GLWLglakAGMEAALLNVNLRREPLAF-------CLG 172
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVEIaptaqGLWM----RGASLTMLHQPTPRTDLAVwaedtlrVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 173 TSGAKALIFGGEMVAAVAEVSGHlgkslikfcsgdlgpeGILPDThlldplLKEASTAPLAQIPSKGMDDRLFYIYTSGT 252
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK----------------GIRVLT------VADLLAADPIDPVETGEDDLALMQLTSGS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 38524616 253 TGLPKAAIVVHSRYYRMAAFGHHAYRMQAA-DVLYDCLPLYHSAGNI 298
Cdd:PRK07768 164 TGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMV 210
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
220-582 |
5.75e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.59 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 220 LDPLLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIvvHS-RYYRMAAFGHHAYRMQAADVLYDCLPLYHSAG-- 296
Cdd:PRK07445 99 LDQLKLSHPPPLPSQGILPNLETGWIMIPTGGSSGQIRFAI--HTwETLTASVQGFQRYFQLQQVNSFCVLPLYHVSGlm 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 297 ----NIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQ---------PV----REAERRHRVR 359
Cdd:PRK07445 177 qfmrSFLTGGKLVILPYKRLKSGQELPPNPSDFFLSLVPTQLQRLLQLRPQWLAQfrtillggaPAwpslLEQARQLQLR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 360 LAvgnglrPAiweefterfgvrqigefYGATECNCSIANM------DGKVgSCGfnsRILPHvypirlvkvnedtmellr 433
Cdd:PRK07445 257 LA------PT-----------------YGMTETASQIATLkpddflAGNN-SSG---QVLPH------------------ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 434 dAQgLCIPCQAgepgllVGQINQQDPlRRFDGYVSEsatsKKIAHSVFSKGDSAYLSGDvlvmdelGYMYFRDRSGDTFR 513
Cdd:PRK07445 292 -AQ-ITIPANQ------TGNITIQAQ-SLALGYYPQ----ILDSQGIFETDDLGYLDAQ-------GYLHILGRNSQKII 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 514 WRGENVSTTEVEGV-LSRLLGQtDVAVYGVAVPgVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARP 582
Cdd:PRK07445 352 TGGENVYPAEVEAAiLATGLVQ-DVCVLGLPDP-HWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQP 419
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-197 |
5.95e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 39.75 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38524616 105 TFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI--FG 182
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIgiPK 83
|
90
....*....|....*
gi 38524616 183 GEMVAAVAEVSGHLG 197
Cdd:cd05910 84 ADEPAAILFTSGSTG 98
|
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