|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
74-610 |
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: 1089.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 74 FRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAK 153
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 154 VLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPK 233
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 AAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIG 313
Cdd:cd05938 161 AARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 314 ELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIIT 393
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 394 YDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHEN 473
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 474 FIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSY 553
Cdd:cd05938 401 FLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAY 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 554 ARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIY 610
Cdd:cd05938 481 ARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
30-620 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 736.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 30 IGYFLKVAAVGRRVRSYGKRR---PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDC 106
Cdd:PRK08279 11 LPRRLPDLPGILRGLKRTALItpdSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAA-RGVGKGDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 107 VALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKkDDVSIYYVSRTS 186
Cdd:PRK08279 90 VALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLA-RPPRLWVAGGDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 187 NTD--GIDSFLDKVDEVSTEPipESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRI--WYGT--GLTfvsGLKADDVI 260
Cdd:PRK08279 169 LDDpeGYEDLAAAAAGAPTTN--PASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWlkAMGGfgGLL---RLTPDDVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 261 YITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG 340
Cdd:PRK08279 244 YCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 341 LRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKiiTYDLIKYDVEKDEPVRDENGYCVRVPKG 420
Cdd:PRK08279 324 LRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRCIKVKPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 421 EVGLLVCKITQLTPFNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADT 500
Cdd:PRK08279 402 EVGLLIGRITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 501 VGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 580
Cdd:PRK08279 481 LSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 308153494 581 EGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL 620
Cdd:PRK08279 561 EGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
76-585 |
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: 736.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 LVspelqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfsTPALYIYTSGTTGLPKAA 235
Cdd:cd05940 80 VV------------------------------------------------------------DAALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 236 MITHQRIWYGTGLTFVSGL-KADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGE 314
Cdd:cd05940 100 IISHRRAWRGGAFFAGSGGaLPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 315 LLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITY 394
Cdd:cd05940 180 LCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 395 DLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMVDHENF 474
Cdd:cd05940 260 ALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 475 IYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYA 554
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYA 418
|
490 500 510
....*....|....*....|....*....|.
gi 308153494 555 RPRFLRIQDTIEITGTFKHRKMTLVEEGFNP 585
Cdd:cd05940 419 RPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
76-585 |
2.73e-171 |
|
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: 495.79 E-value: 2.73e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQA-QGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 LVS--PELQAAVEEILPSLkkDDVSiyyvsrtsntdgidsFLDKVdevstepipeswrsevtfstpaLYIYTSGTTGLPK 233
Cdd:cd05939 80 IFNllDPLLTQSSTEPPSQ--DDVN---------------FRDKL----------------------FYIYTSGTTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 AAMITHQR-IWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYI 312
Cdd:cd05939 121 AAVIVHSRyYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 313 GELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKII 392
Cdd:cd05939 201 GEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 393 TYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTP---FNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMV 469
Cdd:cd05939 281 PIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 470 DHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENhEFDGKKLFQHIADY 549
Cdd:cd05939 360 DELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPER-KVDLDRFSAVLAKS 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 308153494 550 LPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNP 585
Cdd:cd05939 439 LPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
74-585 |
5.97e-159 |
|
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: 464.21 E-value: 5.97e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 74 FRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAK 153
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 154 VLLVSPElqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfsTPALYIYTSGTTGLPK 233
Cdd:cd05937 81 FVIVDPD---------------------------------------------------------DPAILIYTSGTTGLPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 AAMITHQRIWygTGLTFVS---GLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQ 310
Cdd:cd05937 104 AAAISWRRTL--VTSNLLShdlNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 311 YIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYAR---KVGAVGRVNYL 387
Cdd:cd05937 182 YVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdfGAGAIGHHGLI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 388 QKKIITYD--LIKYDVEKDEPVRD-ENGYCVRVPKGEVGLLVCKITQ--LTPFNGYAGAKAQTEKKKLRDVFKKGDLYFN 462
Cdd:cd05937 262 RRWKFENQvvLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVPFknREAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 463 SGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENH----EFD 538
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSavptEFT 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 308153494 539 GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNP 585
Cdd:cd05937 422 KSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-581 |
6.48e-94 |
|
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: 296.34 E-value: 6.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 56 LRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:COG0318 1 LADLLRRaAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 NYNIRAKSLLHCFQCCGAKVLLVspelqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsev 214
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 215 tfstpALYIYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFS 293
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLAnAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 294 ASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATEGN-IG 370
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGYGLTETSpVV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 371 FMN----YARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTE 446
Cdd:COG0318 257 TVNpedpGERRPGSVGRP-----------LPGVEVR----IVDEDG--RELPPGEVGEIVVRGPNVMK--GYWNDPEATA 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 447 KkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGRIGM 526
Cdd:COG0318 318 E-----AFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 527 ASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEE 581
Cdd:COG0318 390 AFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-578 |
9.04e-90 |
|
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: 284.57 E-value: 9.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP 159
Cdd:cd05934 5 TYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 160 elqaaveeilpslkkddVSIyyvsrtsntdgidsfldkvdevstepipeswrsevtfstpalyIYTSGTTGLPKAAMITH 239
Cdd:cd05934 84 -----------------ASI-------------------------------------------LYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 240 -QRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRY 318
Cdd:cd05934 104 aNLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 319 LCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATEGNIGFMN---YARKVGAVGRVNYLqkkiityd 395
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGprdEPRRPGSIGRPAPG-------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 396 likYDVEkdepVRDENGYcvRVPKGEVGLLVCKITQ-LTPFNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENF 474
Cdd:cd05934 255 ---YEVR----IVDDDGQ--ELPAGEPGELVIRGLRgWGFFKGYYNMPEATAE-----AMRNG--WFHTGDLGYRDADGF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 475 IYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYA 554
Cdd:cd05934 319 FYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEV-KAVVVLRPGETLDPEELFAFCEGQLAYFK 397
|
490 500
....*....|....*....|....
gi 308153494 555 RPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05934 398 VPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
35-586 |
2.27e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 258.53 E-value: 2.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 35 KVAAVGRRVRSYGKRRPARTILRAFLE-KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGN 113
Cdd:PRK06155 2 EPLGAGLAARAVDPLPPSERTLPAMLArQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 114 EPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPS-LKKDDVSIyyvsrtsntdgid 192
Cdd:PRK06155 81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWL------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 193 sfldkVDEVSTEPIPESWR-------------SEVTFSTPALYIYTSGTTGLPKAAMITH-QRIWYGTGLTFVSGLKADD 258
Cdd:PRK06155 148 -----LDAPASVSVPAGWStaplppldapapaAAVQPGDTAAILYTSGTTGPSKGVCCPHaQFYWWGRNSAEDLEIGADD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 259 VIYITLPFYHSAALLIGIHGcIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALG 338
Cdd:PRK06155 223 VLYTTLPLFHTNALNAFFQA-LLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 339 NGLRGDVWRQFVKRFGdICIYEFYAATEGN--IGFMNYARKVGAVGRvnyLQKKIITYdlikydvekdepVRDENGycVR 416
Cdd:PRK06155 302 PGVPAALHAAFRERFG-VDLLDGYGSTETNfvIAVTHGSQRPGSMGR---LAPGFEAR------------VVDEHD--QE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 417 VPKGEVGLLVCKITQltPF---NGYAGAKAQTekkklrdVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVA 493
Cdd:PRK06155 364 LPDGEPGELLLRADE--PFafaTGYFGMPEKT-------VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENIS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 494 TTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKH 573
Cdd:PRK06155 435 SFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
|
570
....*....|...
gi 308153494 574 RKMTLVEEGFNPA 586
Cdd:PRK06155 514 QKFVLREQGVTAD 526
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
68-586 |
8.11e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 224.56 E-value: 8.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 68 HKPFLLFRDETLTYAQVDRRSNQVARALHDHLGlRQGDC-VALLMGNEPAYVwLWLGLVKL-GCAMACLNYNIRAKSLLH 145
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLD-PTRPPhVGVLLDNTPEFS-LLLGAAALsGIVPVGLNPTRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 146 CFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGIDSFLDkvdevstEPIPeswRSEVTFSTPALYIYT 225
Cdd:PRK07867 96 DIAHADCQLVLTESAHAELLDGLDP-----GVRVINVDSPAWADELAAHRD-------AEPP---FRVADPDDLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 226 SGTTGLPKAAMITHQRIwYGTGLTFVS--GLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRK 303
Cdd:PRK07867 161 SGTSGDPKAVRCTHRKV-ASAGVMLAQrfGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 304 YNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGN-GLRGDVWRqFVKRFGdiC-IYEFYAATEGNIGFmnyARK---- 377
Cdd:PRK07867 240 YGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDIAR-FARRFG--CvVVDGFGSTEGGVAI---TRTpdtp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 378 VGAVGRvnylqkkiITYDLIKYDVEKDEP----VRDENGycvRVPKGE-VGLLVcKITQLTPFNGYAGaKAQTEKKKLRD 452
Cdd:PRK07867 314 PGALGP--------LPPGVAIVDPDTGTEcppaEDADGR---LLNADEaIGELV-NTAGPGGFEGYYN-DPEADAERMRG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 453 vfkkGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKM 531
Cdd:PRK07867 381 ----G--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYA--VPDpVVGDQVMAALVL 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 532 KENHEFDGKKL--FQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPA 586
Cdd:PRK07867 453 APGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
59-488 |
9.38e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 216.02 E-value: 9.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLL-FRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEvtfs 217
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 TPALYIYTSGTTGLPKAAMITHQ-----RIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKF 292
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRnlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 293 SA---SQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATEG 367
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 368 NIGFMNY------ARKVGAVGR-VNYLQKKIItydlikyDVEKDEPvrdengycvrVPKGEVGLLVCKITQLTPfnGYAG 440
Cdd:pfam00501 315 TGVVTTPlpldedLRSLGSVGRpLPGTEVKIV-------DDETGEP----------VPPGEPGELCVRGPGVMK--GYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 308153494 441 AKAQTEKkklrdVFKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWK 488
Cdd:pfam00501 376 DPELTAE-----AFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
63-615 |
5.07e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 206.42 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQ---VARALHDHLGLRQgdcVALLMGNEPAYVwLWLGLVKLGCAMAC-LNYNI 138
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREVLAEAAAraaALIALADPDRPLH---VGVLLGNTPEML-FWLAAAALGGYVLVgLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPELQAaveeILPSLKKDDVSIYYVSRtsntdgiDSFLDKVDEV-STEPIPEswrseVTFS 217
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTDAEHRP----LLDGLDLPGVRVLDVDT-------PAYAELVAAAgALTPHRE-----VDAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 TPALYIYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQ 296
Cdd:PRK13388 151 DPFMLIFTSGTTGAPKAVRCSHGRLAFaGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 297 FWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdiC-IYEFYAATEGNIgfmNYA 375
Cdd:PRK13388 231 FLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG--CqVEDGYGSSEGAV---IVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 376 RK----VGAVGRVnylqkkiiTYDLIKYDVEKDEP----VRDENGYcVRVPKGEVGLLVCKiTQLTPFNGYAGAKAQTEk 447
Cdd:PRK13388 306 REpgtpPGSIGRG--------APGVAIYNPETLTEcavaRFDAHGA-LLNADEAIGELVNT-AGAGFFEGYYNNPEATA- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 448 KKLRDvfkkGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGM 526
Cdd:PRK13388 375 ERMRH----GMYW--SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA--VPDeRVGDQVM 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 527 ASIKMKENHEFDGKKL--FQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFnpAVIKDALYFLDDTAKMYVP 604
Cdd:PRK13388 447 AALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW--ATGDPVTLWVRRGGPAYRL 524
|
570
....*....|.
gi 308153494 605 MTEDIYNAISA 615
Cdd:PRK13388 525 MSEPAKAALAA 535
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
63-575 |
8.47e-58 |
|
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: 200.53 E-value: 8.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRA-LGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLvspelqaaveeilpslkkDDvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfstPALY 222
Cdd:cd17631 84 VAYILADSGAKVLF------------------DD------------------------------------------LALL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITH-QRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDC 301
Cdd:cd17631 104 MYTSGTTGRPKGAMLTHrNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 302 RKYNVTVIQYIGELLRYLCNSPQkPNDRDH-KVRLALGNG--LRGDVWRQFVKRfgDICIYEFYAATE--GNIGFM---N 373
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPR-FATTDLsSLRAVIYGGapMPERLLRALQAR--GVKFVQGYGMTEtsPGVTFLspeD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 374 YARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkklrdV 453
Cdd:cd17631 261 HRRKLGSAGRP-----------VFFVEVR----IVDPDG--REVPPGEVGEIVVRGPHVMA--GYWNRPEATAA-----A 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 454 FKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMK 532
Cdd:cd17631 317 FRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAVVVPR 392
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 308153494 533 ENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRK 575
Cdd:cd17631 393 PGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
218-572 |
8.67e-58 |
|
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: 197.51 E-value: 8.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 TPALYIYTSGTTGLPKAAMITHQRI-WYGTGLTFVSGLKADDVIYITLPFYHSAaLLIGIHGCIVAGATLALRTKFSASQ 296
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLlAAAAALAASGGLTEGDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 297 FWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKRFGDIcIYEFYAATEGNIGFM-- 372
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LVNGYGLTETGGTVAtg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 373 ---NYARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKItqLTPFNGYAGAKAQTEkkk 449
Cdd:cd04433 159 ppdDDARKPGSVGRP-----------VPGVEVR----IVDPDG--GELPPGEIGELVVRG--PSVMKGYWNNPEATA--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 450 lrdvFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMAS 528
Cdd:cd04433 217 ----AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVG--VPDPEwGERVVAV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 308153494 529 IKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd04433 291 VVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
63-563 |
1.18e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 194.38 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTsnTDGIDSFLDKVDEVSTEPIPESwRSEVTFSTPALY 222
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGG--REAPGGWLDFADWAEAGSVAEP-DVELADDDLAQI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITHQR-IWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDC 301
Cdd:PRK08316 177 LYTSGTESLPKGAMLTHRAlIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 302 RKYNV-------TViqYIGeLLRylcnSPqkpnDRDhKVRLAlgnGLR----------GDVWRQFVKRFGDICIYEFYAA 364
Cdd:PRK08316 257 EAERItsffappTV--WIS-LLR----HP----DFD-TRDLS---SLRkgyygasimpVEVLKELRERLPGLRFYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 365 TEgnIGFM-------NYARKVGAVGR-VNYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLTpfN 436
Cdd:PRK08316 322 TE--IAPLatvlgpeEHLRRPGSAGRpVLNVETRVV-----------DDDGND-------VAPGEVGEIVHRSPQLM--L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 437 GYAGAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVh 516
Cdd:PRK08316 380 GYWDDPEKTA-----EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 308153494 517 vpDHEGRIG--MASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQD 563
Cdd:PRK08316 452 --PDPKWIEavTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
55-572 |
4.23e-54 |
|
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: 191.24 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 55 ILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 NYNIRAKSLLHCFQCCGAKVLLVspelqaaveeilpslkkddvsiyyvsrtsntdgIDSFLDKVDEvstePIPESWRSEV 214
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV---------------------------------AVSFTDLLAA----GAPLGERVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 215 TFSTPALYIYTSGTTGLPKAAMITHQRIW---YGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTK 291
Cdd:cd05936 123 TPEDVAVLQYTSGTTGVPKGAMLTHRNLVanaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 292 FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKRFGDIcIYEFYAATE--- 366
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTEtsp 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 367 ---GNigFMNYARKVGAVGrvnylqkkiitYDLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKA 443
Cdd:cd05936 282 vvaVN--PLDGPRKPGSIG-----------IPLPGTEVK----IVDDDG--EELPPGEVGELWVRGPQV--MKGYWNRPE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 444 QTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGR 523
Cdd:cd05936 341 ETAE-----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYS-GE 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 308153494 524 IGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd05936 413 AVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGK 461
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
61-614 |
8.49e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 189.54 E-value: 8.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 61 EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGcAMACLnynIRA 140
Cdd:PRK07868 455 EQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIA-VGVRQGDRVGVLMETRPSALVAIAALSRLG-AVAVL---MPP 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 141 KSLLH-CFQCCGAKVLLVSPE-LQAAVEEILPSL-----KKDDVSIyyvsrTSNTDGIDsfLDKVDEVSTEpIPESWRSE 213
Cdd:PRK07868 530 DTDLAaAVRLGGVTEIITDPTnLEAARQLPGRVLvlgggESRDLDL-----PDDADVID--MEKIDPDAVE-LPGWYRPN 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 214 VTFSTPALYIYTSGTTGLPKAAMITHQRiW----YGTGLTfvSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALR 289
Cdd:PRK07868 602 PGLARDLAFIAFSTAGGELVAKQITNYR-WalsaFGTASA--AALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 290 TKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNI 369
Cdd:PRK07868 679 RGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 GFMNYA-RKVGAVGRVNYLQKKIityDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVckitqltpfnGYAGAKAQTEKK 448
Cdd:PRK07868 759 VLANVSgAKIGSKGRPLPGAGRV---ELAAYDPEHDLILEDDRGFVRRAEVNEVGVLL----------ARARGPIDPTAS 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 449 KLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEgrIGMAS 528
Cdd:PRK07868 826 VKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAA 903
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 529 IKMKENHEFDGKKLFQHIADyLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFnPAVIKDALYFLDDTAKmYVPMTED 608
Cdd:PRK07868 904 VTLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKPGRQAWYFDPETNR-YRRLTPA 980
|
....*.
gi 308153494 609 IYNAIS 614
Cdd:PRK07868 981 VRAELT 986
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
54-565 |
6.76e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.46 E-value: 6.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 134 LNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLkkDDVSIYYVsrtsNTDGidsflDKVDEVSTEPIPESWRS- 212
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQL--PTVRTVIV----EGDG-----PAAPLAPEVGEYEELLAa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 213 --------EVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLIGIHGcIVAG 283
Cdd:PRK06187 155 asdtfdfpDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSlAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 284 ATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqKPNDRD-HKVRLAL--GNGLRGDVWRQFVKRFGdICIYE 360
Cdd:PRK06187 234 AKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAP-RAYFVDfSSLRLVIygGAALPPALLREFKEKFG-IDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 361 FYAATE-GNIGFMNY--------ARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGYCVRVPKGEVGLLVCK--- 428
Cdd:PRK06187 312 GYGMTEtSPVVSVLPpedqlpgqWTKRRSAGRP-----------LPGVEAR----IVDDDGDELPPDGGEVGEIIVRgpw 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 429 ITQltpfnGYAGAKAQTEKKklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQ 508
Cdd:PRK06187 377 LMQ-----GYWNRPEATAET-----IDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 308153494 509 EVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 565
Cdd:PRK06187 445 EVAVIG--VPDeKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDEL 500
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
61-578 |
2.02e-46 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 171.40 E-value: 2.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 61 EKARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:PRK08008 15 DLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 136 YNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSlkkDDVSI--YYVSRTSN--TDGIDSFLDKVDEVSTEpipesWR 211
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQE---DATPLrhICLTRVALpaDDGVSSFTQLKAQQPAT-----LC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 212 SEVTFST--PALYIYTSGTTGLPKAAMITHQRIWYGTGLT-FVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLAL 288
Cdd:PRK08008 166 YAPPLSTddTAEILFTSGTTSRPKGVVITHYNLRFAGYYSaWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 289 RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVR-----LALGNGLRGDvwrqFVKRFGdICIYEFYA 363
Cdd:PRK08008 246 LEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 364 ATE---GNIG-FMNYARKVGAVGRVNylqkkiitydlIKYDVEkdepVRDENGYcvRVPKGEVGLLVCK-ITQLTPFNGY 438
Cdd:PRK08008 321 MTEtivGIIGdRPGDKRRWPSIGRPG-----------FCYEAE----IRDDHNR--PLPAGEIGEICIKgVPGKTIFKEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 439 AGAKAQTEKkklrdVFkKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVP 518
Cdd:PRK08008 384 YLDPKATAK-----VL-EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 519 DHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:PRK08008 458 IRDEAI-KAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
63-557 |
1.36e-43 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 164.51 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDE-----TLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEIL---PSLKKddvsIYYVSRTSNT---DGIDSFLDKVDEVS 202
Cdd:COG0365 98 FGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALeelPSLEH----VIVVGRTGADvpmEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 203 TEPIPEswrsEVTFSTPALYIYTSGTTGLPKAAMITHQ--RIWYGTGLTFVSGLKADDViyitlpfYHSAALL--IGIHG 278
Cdd:COG0365 174 AEFEPE----PTDADDPLFILYTSGTTGKPKGVVHTHGgyLVHAATTAKYVLDLKPGDV-------FWCTADIgwATGHS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 279 CIV-----AGATLAL---RTKF-SASQFWDDCRKYNVTViqyigellryLCNSP-----------QKPNDRD-HKVRLAL 337
Cdd:COG0365 243 YIVygpllNGATVVLyegRPDFpDPGRLWELIEKYGVTV----------FFTAPtairalmkagdEPLKKYDlSSLRLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 338 GNG--LRGDVWRQFVKRFGdICIYEFYAATEGNIGFMNYAR----KVGAVGRVNYLqkkiitydlikYDVEkdepVRDEN 411
Cdd:COG0365 313 SAGepLNPEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGKPVPG-----------YDVA----VVDED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 412 GycVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTeKKKLRDVFKkgDLYFnSGDLLMVDHENFIYFHDRVGDTFRWKGEN 491
Cdd:COG0365 377 G--NPVPPGEEGELVIKGPWPGMFRGYWNDPERY-RETYFGRFP--GWYR-TGDGARRDEDGYFWILGRSDDVINVSGHR 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 492 VATTEVADTVGLVDFVQEVNVygVHVPDHEGRIGM-ASIKMKENHEFDG---KKLFQHIADYLPSYARPR 557
Cdd:COG0365 451 IGTAEIESALVSHPAVAEAAV--VGVPDEIRGQVVkAFVVLKPGVEPSDelaKELQAHVREELGPYAYPR 518
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-553 |
5.62e-42 |
|
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: 158.14 E-value: 5.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 LVSPELQAAVEEILPSLKKDDvSIYYVsrTSNTDGIDSFLDKVDEVSTEPIP-ESWRSEVTFSTPALYIYTSGTTGLPKA 234
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKD-KIIVL--DDKPDGVLSIEDLLSPTLGEEDEdLPPPLKDGKDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 235 AMITHQRI---WYGTGLTFVSGLKADDVIYITLPFYHSAALLIgIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQY 311
Cdd:cd05911 164 VCLSHRNLianLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFT-TLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 312 IGELLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFV----KRFGDICIYEFYAATE-GNIGFMN--YARKVGAVGRV 384
Cdd:cd05911 243 VPPIAAALAKSPLLDKYDLSSLRVILSGG--APLSKELQellaKRFPNATIKQGYGMTEtGGILTVNpdGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 385 --NYlQKKIItydlikydvekDEPVRDENGYcvrvpkGEVGLLVCKITQLtpFNGY-----AGAKAQTEkkklrdvfkkg 457
Cdd:cd05911 321 lpNV-EAKIV-----------DDDGKDSLGP------NEPGEICVRGPQV--MKGYynnpeATKETFDE----------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 458 DLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGRIGMASIKMKENHEF 537
Cdd:cd05911 370 DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS-GELPRAYVVRKPGEKL 448
|
490
....*....|....*.
gi 308153494 538 DGKKLFQHIADYLPSY 553
Cdd:cd05911 449 TEKEVKDYVAKKVASY 464
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
51-565 |
1.98e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 148.90 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 131 MACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEI---LPSLKkddvSIYYVSRTSNTDGIDSFLDKVDEVSTEPIP 207
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAttrLPALE----HVVICETEEDDPHTEKMKTFTDFLAAGDPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 208 ESWRsEVTFSTPALYIYTSGTTGLPKAAMITHQ------RIWYGTGltfvsGLKADDVIYITLPFYHSAALLIGIHGCIV 281
Cdd:PRK07656 158 ERAP-EVDPDDVADILFTSGTTGRPKGAMLTHRqllsnaADWAEYL-----GLTEGDRYLAANPFFHVFGYKAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 282 AGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDV--WRQFVKRFGDICIY 359
Cdd:PRK07656 232 RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPValLERFESELGVDIVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 360 EFYAATEGN-IGFMNYA---RKVGA--VGRVnylqkkiitydlIKyDVEkdepVRDENGYCVRVPKGEVGLLVCKitqlt 433
Cdd:PRK07656 312 TGYGLSEASgVTTFNRLdddRKTVAgtIGTA------------IA-GVE----NKIVNELGEEVPVGEVGELLVR----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 434 PFN---GYAGAKAQTEKKKLRDvfkkGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEV 510
Cdd:PRK07656 370 GPNvmkGYYDDPEATAAAIDAD----GWLH--TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 308153494 511 NVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 565
Cdd:PRK07656 444 AVIG--VPDERlGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDEL 497
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
63-563 |
2.41e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 149.16 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLVSPELQ---AAVEEILPSLkkddvSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPeswrSEVTFSTP 219
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAALApvaTAVRDIVPLL-----STVVVAGGSSDDSVLGYEDLLAEAGPAHAP----VDIPNDSP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 220 ALYIYTSGTTGLPKAAMITHQRIwYGTGLTFVSGLKAD---DVIYITLPFYHSAALligihGCIVAGATLALRT------ 290
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADinsDVGFVGVPLFHIAGI-----GSMLPGLLLGAPTviyplg 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 291 KFSASQFWDDCRKYNVTVIQYIGELLRYLCnSPQKPNDRDHKVR-LALGNGLRGD-VWRQFVKRFGDICIYEFYAATEGN 368
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAVC-AEQQARPRDLALRvLSWGAAPASDtLLRQMAATFPEAQILAAFGQTEMS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 369 -IGFM----NYARKVGAVGRV-NYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLtpFNGYAGAK 442
Cdd:PRK07786 330 pVTCMllgeDAIRKLGSVGKViPTVAARVV-----------DENMND-------VPVGEVGEIVYRAPTL--MSGYWNNP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 443 AQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhvPDHE- 521
Cdd:PRK07786 390 EATA-----EAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG---RADEk 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 308153494 522 -GRIGMASIKMK-ENHEFDGKKLFQHIADYLPSYARPRFLRIQD 563
Cdd:PRK07786 460 wGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARYKHPKALEIVD 503
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
62-580 |
1.25e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 146.16 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 62 KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAK 141
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 142 SLLHCFQCCGAKVLLVSPELQAAVEEIlpslkkddVSIYYVSRTSNTDGIDSFLDKvdevstEPIPESWRSEvtfSTPAL 221
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSM--------QKVSYVQRVISITSLKEIEDR------KIDNFVEKNE---SASFI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 222 YIYTSGTTGLPKAAMITHQRI-WYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDD 300
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMfWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 301 CRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKR---FGdiciyEFYAATEGN-IGFM-- 372
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapCPEELMREFIDRgflFG-----QGFGMTETSpTVFMls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 373 --NYARKVGAVGR-VNYLQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKKk 449
Cdd:PRK06839 309 eeDARRKVGSIGKpVLFCDYELI----------------DENKN--KVEVGEVGELLIRGPNV--MKEYWNRPDATEET- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 450 LRDVfkkgdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMAS 528
Cdd:PRK06839 368 IQDG------WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHVKwGEIPIAF 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 308153494 529 IKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 580
Cdd:PRK06839 440 IVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-580 |
5.40e-37 |
|
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: 144.38 E-value: 5.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKV 154
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 155 LLV-----SPELQAAVEEILPSLkkdDVSIYYVSRTSNTDGID-SFLDKV-DEVSTEPIPESwrsevtfSTPALYIYTSG 227
Cdd:cd05926 90 VLTpkgelGPASRAASKLGLAIL---ELALDVGVLIRAPSAESlSNLLADkKNAKSEGVPLP-------DDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 228 TTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNV 306
Cdd:cd05926 160 TTGRPKGVPLTHRNLAAsATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 307 TVIQYIGELLRYLCNSPQ-KPNDRDHKVRLA--LGNGLRGDVWRQFVKRFGdICIYEFYAATEG---------NIGfmny 374
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEpNPESPPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTEAahqmtsnplPPG---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 375 ARKVGAVGRVNYLQKKIITydlikydvEKDEPVRDENgycvrvpKGEV---GLLVCKitqltpfnGYAGAKAQTekkklR 451
Cdd:cd05926 315 PRKPGSVGKPVGVEVRILD--------EDGEILPPGV-------VGEIclrGPNVTR--------GYLNNPEAN-----A 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 452 DVFKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIK 530
Cdd:cd05926 367 EAAFKDG-WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFG--VPDeKYGEEVAAAVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 308153494 531 MKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 580
Cdd:cd05926 444 LREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-578 |
7.18e-35 |
|
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: 138.27 E-value: 7.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 58 AFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPES-WRSEvtf 216
Cdd:cd05959 88 LTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAtHADD--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 stPALYIYTSGTTGLPKAAMITHQRIWYgTGLTF---VSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKF- 292
Cdd:cd05959 165 --PAFWLYSSGSTGRPKGVVHLHADIYW-TAELYarnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 293 SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATE-GNI 369
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDGIGSTEmLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 GFMNYARKV--GAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTek 447
Cdd:cd05959 321 FLSNRPGRVryGTTGKP-----------VPGYEVE----LRDEDG--GDVADGEPGELYVRGPSSAT--MYWNNRDKT-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 448 kklRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMA 527
Cdd:cd05959 380 ---RDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 308153494 528 SIKMKENHEFDGK---KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05959 454 FVVLRPGYEDSEAleeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
37-557 |
1.48e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 138.14 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 37 AAVGRRVRSYGkrrPARTILRAfleKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPA 116
Cdd:PRK07788 39 LRLAADIRRYG---PFAGLVAH---AARRAPDRAALIDERGTLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 117 YVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTD-GIDSFL 195
Cdd:PRK07788 112 FVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGsTDETLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 196 DKVDEVSTEPIPeswrsevTFSTPA-LYIYTSGTTGLPKAAMITHQriwygTGLTFVSGL------KADDVIYITLPFYH 268
Cdd:PRK07788 192 DLIAGSSTAPLP-------KPPKPGgIVILTSGTTGTPKGAPRPEP-----SPLAPLAGLlsrvpfRAGETTLLPAPMFH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 269 SAALLIGIHGCIVaGATLALRTKFSASQFWDDCRKYNVTVI----QYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGD 344
Cdd:PRK07788 260 ATGWAHLTLAMAL-GSTVVLRRRFDPEATLEDIAKHKATALvvvpVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 345 VWRQFVKRFGDIcIYEFYAATEgnIGFM------NYARKVGAVGRVnylqkkIITYDLIKYdvekdepvrDENGYcvRVP 418
Cdd:PRK07788 339 LATRALEAFGPV-LYNLYGSTE--VAFAtiatpeDLAEAPGTVGRP------PKGVTVKIL---------DENGN--EVP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 419 KGEVGLLVCKITqlTPFNGYAGAKaqtEKKKLRDVFKKGDL-YFNSGDLLMVDhenfiyfhDRVGDTFRWKGENVATTEV 497
Cdd:PRK07788 399 RGVVGRIFVGNG--FPFEGYTDGR---DKQIIDGLLSSGDVgYFDEDGLLFVD--------GRDDDMIVSGGENVFPAEV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 498 ADTVGLVDFVQEVNVYGVHVPDHEGRIGmASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:PRK07788 466 EDLLAGHPDVVEAAVIGVDDEEFGQRLR-AFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
63-565 |
1.80e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 134.24 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNtdgidsfldkvdevSTEPIPESWRSEVTfstpALY 222
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQ--------------GGLEIPPQAAVAPT----DLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 --IYTSGTTGLPKAAMITHQRI-WYGTGLTFVSGLKADDVIYITLPFYHSAAL-LIGIhGCIVAGATLALRTKFSASQFW 298
Cdd:PRK06145 153 rlMYTSGTTDRPKGVMHSYGNLhWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGI-AVLWVGGTLRIHREFDPEAVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 299 DDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVW--RQFVKRFGDICIYEFYAATEGNIG--FMNY 374
Cdd:PRK06145 232 AAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESriRDFTRVFTRARYIDAYGLTETCSGdtLMEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 375 AR---KVGAVGR-VNYLQKKIITydlikydvekdepvrDENGYCVRVPKGEVGLLVCKITQltpfnGYAGAKAQTEKKKL 450
Cdd:PRK06145 312 GReieKIGSTGRaLAHVEIRIAD---------------GAGRWLPPNMKGEICMRGPKVTK-----GYWKDPEKTAEAFY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 451 RDvfkkgdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIK 530
Cdd:PRK06145 372 GD-------WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERI-TAVVV 443
|
490 500 510
....*....|....*....|....*....|....*
gi 308153494 531 MKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 565
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDEL 478
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
76-521 |
3.57e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 133.49 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 LVSPELQAAVEEILPSLKKDdVSIYYVSRtSNTDGIDSFLDKVDEVSTEPIPESWRSevtfstpALYIYTSGTTGLPK-- 233
Cdd:PRK08276 88 IVSAALADTAAELAAELPAG-VPLLLVVA-GPVPGFRSYEEALAAQPDTPIADETAG-------ADMLYSSGTTGRPKgi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 ----------AAMITHQRIwygtgLTFVSGLKADDVIYITLPFYHSAALLIGIhGCIVAGATLALRTKFSASQFWDDCRK 303
Cdd:PRK08276 159 krplpgldpdEAPGMMLAL-----LGFGMYGGPDSVYLSPAPLYHTAPLRFGM-SALALGGTVVVMEKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 304 YNVTVIQYIgellrylcnspqkPNdrdHKVR-LALGNGLRG-------------------DVWRQFVKRFGDIcIYEFYA 363
Cdd:PRK08276 233 YRVTHSQLV-------------PT---MFVRmLKLPEEVRArydvsslrvaihaaapcpvEVKRAMIDWWGPI-IHEYYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 364 ATEGN-IGFMN---YARKVGAVGRVNYLQKKIItydlikydvekdepvrDENGycVRVPKGEVGLLVCKITQLtPFNgYA 439
Cdd:PRK08276 296 SSEGGgVTVITsedWLAHPGSVGKAVLGEVRIL----------------DEDG--NELPPGEIGTVYFEMDGY-PFE-YH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 440 GAKAQTEKKKLrdvfKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD 519
Cdd:PRK08276 356 NDPEKTAAARN----PHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG--VPD 427
|
..
gi 308153494 520 HE 521
Cdd:PRK08276 428 EE 429
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
51-514 |
1.58e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 132.53 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFLEKARQTPHKPFLLFRD----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAA-VEEI---LPSLKKddvsIYYVSRTSNTDG-----IDSFLDK 197
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDkLLEVrdeLPSLRH----IVVLDPRGLRDDprllsLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 198 VDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGi 276
Cdd:COG1022 164 GREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSnARALLERLPLGPGDRTLSFLPLAHVFERTVS- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 277 HGCIVAGATLAlrtkFSAS--QFWDDCRKYNVTVI-------------------------QYIGEL-----LRYLCNSPQ 324
Cdd:COG1022 243 YYALAAGATVA----FAESpdTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkRKLFRWalavgRRYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 325 -KPNDRDHKVRLALGNGLrgdVWRQFVKRFGD-----IC-------------------IYEFYAATE-GNIGFMNY--AR 376
Cdd:COG1022 319 gKSPSLLLRLKHALADKL---VFSKLREALGGrlrfaVSggaalgpelarffralgipVLEGYGLTEtSPVITVNRpgDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 377 KVGAVGRVnylqkkiitydlIKyDVEkdepvrdengycVRV-PKGEV---GLLVCKitqltpfnGYAGAKAQTEKkklrd 452
Cdd:COG1022 396 RIGTVGPP------------LP-GVE------------VKIaEDGEIlvrGPNVMK--------GYYKNPEATAE----- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 453 VFKKgDLYFNSGDLLMVDHENFIYFHDRVGDTFrwK---GENVATTEVADTVGLVDFVQEVNVYG 514
Cdd:COG1022 438 AFDA-DGWLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
57-581 |
3.99e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 121.22 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 57 RAFLekarqTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:PRK03640 11 RAFL-----TPDRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSlkkddvsiyyvsrtsntdgidsfldKVDEVSTEPIPE-SWRSEVT 215
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKLIPGISV-------------------------KFAELMNGPKEEaEIQEEFD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 216 FSTPALYIYTSGTTGLPKAAMITHQRIWY---GTGLTFvsGLKADDVIYITLPFYHSAALLIGIHGcIVAGATLALRTKF 292
Cdd:PRK03640 140 LDEVATIMYTSGTTGKPKGVIQTYGNHWWsavGSALNL--GLTEDDCWLAAVPIFHISGLSILMRS-VIYGMRVVLVEKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 293 SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATEG----- 367
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKG-IPVYQSYGMTETasqiv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 368 NIGFMNYARKVGAVGRVNY-LQKKIitydlikydvEKDEPVrdengycvrVPKGEVGLLVCKITQLTPfnGYAGAKAQTE 446
Cdd:PRK03640 296 TLSPEDALTKLGSAGKPLFpCELKI----------EKDGVV---------VPPFEEGEIVVKGPNVTK--GYLNREDATR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 447 KkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIG 525
Cdd:PRK03640 355 E-----TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVG--VPDDKwGQVP 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 526 MASIKMkeNHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK---HRKMTLVEE 581
Cdd:PRK03640 426 VAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKllrHELKQLVEE 482
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
67-425 |
1.06e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 120.38 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIyyvsRTSNTDGIDSFLDKVD--EVSTEPIPEswRSEVTFSTPALY-I 223
Cdd:PRK07798 96 LDDSDAVALVYEREFAPRVAEVLPRLPKLRTLV----VVEDGSGNDLLPGAVDyeDALAAGSPE--RDFGERSPDDLYlL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 224 YTSGTTGLPKAAMITHQRIWY--GTGLTFVSGLKADD--------------VIYITLPFYHSAALLIGIhGCIVAGATLA 287
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQEDIFRvlLGGRDFATGEPIEDeeelakraaagpgmRRFPAPPLMHGAGQWAAF-AALFSGQTVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 288 L--RTKFSASQFWDDCRKYNVTVIQYIGE-LLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFVKR-----FGDICIY 359
Cdd:PRK07798 249 LlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLLDALEARGPYDLSSLFAIASG--GALFSPSVKEallelLPNVVLT 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 360 EFYAATE-GNIGFMNYARKVGAVGRVnylqkkiitydliKYDVEKDEPVRDENGYCVRVPKGEVGLL 425
Cdd:PRK07798 327 DSIGSSEtGFGGSGTVAKGAVHTGGP-------------RFTIGPRTVVLDEDGNPVEPGSGEIGWI 380
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
67-568 |
6.73e-28 |
|
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: 116.86 E-value: 6.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSPElQAAveeilpslkkddvsiyYVsrtsntdgidsfldkvdevstepipeswrsevtfstpalyIYTS 226
Cdd:cd05930 80 LEDSGAKLVLTDPD-DLA----------------YV----------------------------------------IYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 227 GTTGLPKAAMITHQRI-----WygtgLTFVSGLKADDVIYITLPFYHSAALLiGIHGCIVAGATLAL---RTKFSASQFW 298
Cdd:cd05930 103 GSTGKPKGVMVEHRGLvnlllW----MQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAGATLVVlpeEVRKDPEALA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 299 DDCRKYNVTVIQYIGELLRYLCNSPQkpNDRDHKVRLAL--GNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGfmnyar 376
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQELE--LAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEATVD------ 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 377 kvgavgrvnylqkkiITYDLIKYDVEKDEP-------------VRDENGYCvrVPKGEVGLLVckIT--QLTpfNGYAGA 441
Cdd:cd05930 250 ---------------ATYYRVPPDDEEDGRvpigrpipntrvyVLDENLRP--VPPGVPGELY--IGgaGLA--RGYLNR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 442 KAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVgDT------FRwkgenVATTEVADTVGLVDFVQEVNVYGV 515
Cdd:cd05930 309 PELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAVVAR 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 308153494 516 HVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd05930 383 EDGDGEKRL-VAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
79-572 |
7.71e-28 |
|
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: 116.42 E-value: 7.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 159 PELqaaveeilpslkkDDVSIyyvsrtsntdgidsfldkvdevstepIPeswrsevtfstpalyiYTSGTTGLPKAAMIT 238
Cdd:cd05935 81 SEL-------------DDLAL--------------------------IP----------------YTSGTTGLPKGCMHT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 239 HQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLR 317
Cdd:cd05935 106 HFSAAANAlQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 318 YLCNSPqKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGdICIYEFYAATEgnigfmnyarkVGAVGRVN-YLQKKIIT 393
Cdd:cd05935 186 DLLATP-EFKTRDLSSLKVLTGGgapMPPAVAEKLLKLTG-LRFVEGYGLTE-----------TMSQTHTNpPLRPKLQC 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 394 YDLIKYDVekDEPVRD-ENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKKKLRDvfkKGDLYFNSGDLLMVDHE 472
Cdd:cd05935 253 LGIP*FGV--DARVIDiETG--RELPPNEVGEIVVRGPQI--FKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 473 NFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKEnhEFDGKKLFQHIADY-- 549
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVIS--VPDERvGEEVKAFIVLRP--EYRGKVTEEDIIEWar 399
|
490 500
....*....|....*....|....*
gi 308153494 550 --LPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd05935 400 eqMAAYKYPREVEFVDELPRSASGK 424
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
63-521 |
2.31e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 116.33 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKP-FLLFR-DETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRA 140
Cdd:PRK13391 7 AQTTPDKPaVIMAStGEVVTYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 141 KSLLHCFQCCGAKVLLVSP---ELQAAVEEILPSLKKDDVsiyyVSRTSNTDGIDSFLDKVDEVSTEPIPESWRsevtfS 217
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAaklDVARALLKQCPGVRHRLV----LDGDGELEGFVGYAEAVAGLPATPIADESL-----G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 TPALyiYTSGTTGLPKA--AMITHQRIWYGTGLTFVS----GLKADDVIYITLPFYHSAAL-LIGIhgCIVAGATLALRT 290
Cdd:PRK13391 157 TDML--YSSGTTGRPKGikRPLPEQPPDTPLPLTAFLqrlwGFRSDMVYLSPAPLYHSAPQrAVML--VIRLGGTVIVME 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 291 KFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDR-DH---KVRLALGNGLRGDVWRQFVKRFGDIcIYEFYAATE 366
Cdd:PRK13391 233 HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKyDLsslEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 367 GNiGFM-----NYARKVGAVGRVnylqkkiitydlikydVEKDEPVRDENGYcvRVPKGEVGLLVCKitQLTPFNgYAGA 441
Cdd:PRK13391 312 GL-GFTacdseEWLAHPGTVGRA----------------MFGDLHILDDDGA--ELPPGEPGTIWFE--GGRPFE-YLND 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 442 KAQTEKKKLRDvfkkGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE 521
Cdd:PRK13391 370 PAKTAEARHPD----GT-WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFG--VPNED 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
46-574 |
4.25e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 46 YGKRRPARTILRAFLEKARQTPHKP---FLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAY 117
Cdd:PRK07529 18 LAARDLPASTYELLSRAAARHPDAPalsFLLDADpldrpETWTYAELLADVTRTANLLHS-LGVGPGDVVAFLLPNLPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 118 VWLWLGLVKLGCAMAcLNYNIRAKSLLHCFQCCGAKVLL-VSPELQ-------AAVEEILPSLK------------KDDV 177
Cdd:PRK07529 97 HFALWGGEAAGIANP-INPLLEPEQIAELLRAAGAKVLVtLGPFPGtdiwqkvAEVLAALPELRtvvevdlarylpGPKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 178 SIYYVSRTSNTDGIDSFLDkvdEVSTEPIPESWRSE-VTFSTPALYIYTSGTTGLPKAAMITH-QRIWYGTGLTFVSGLK 255
Cdd:PRK07529 176 LAVPLIRRKAHARILDFDA---ELARQPGDRLFSGRpIGPDDVAAYFHTGGTTGMPKLAQHTHgNEVANAWLGALLLGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 256 ADDVIYITLPFYHSAALLIGIHGCIVAGATLAL------RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqkPNDR 329
Cdd:PRK07529 253 PGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVP--VDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 330 D-HKVRLALGNG--LRGDVWRQFVKRFGdICIYEFYAATEGN-IGFMNYA---RKVGAVG-RVNYLQKKIItydlikydv 401
Cdd:PRK07529 331 DiSSLRYALCGAapLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPdgeRRIGSVGlRLPYQRVRVV--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 402 ekdepVRDENGYCVR-VPKGEVGLLVckITQLTPFNGYagakaqTEKKKLRDVFKKGDlYFNSGDLLMVDHENFIYFHDR 480
Cdd:PRK07529 401 -----ILDDAGRYLRdCAVDEVGVLC--IAGPNVFSGY------LEAAHNKGLWLEDG-WLNTGDLGRIDADGYFWLTGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 481 VGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYAR-PRF 558
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVG--RPDaHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAvPKH 544
|
570
....*....|....*....
gi 308153494 559 LRIQDTIEITG---TFKHR 574
Cdd:PRK07529 545 VRILDALPKTAvgkIFKPA 563
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
63-572 |
8.02e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 114.34 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRD--ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEP-AYVWLWLGLvKLGCAMACLNYNIR 139
Cdd:PRK13390 7 AQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPeALVVLWAAL-RSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 140 AKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLkkdDVSIYYVSRtsnTDGIDSFlDKVDEVSTEPIPESwrsevtfSTP 219
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAAKVGADL---PLRLSFGGE---IDGFGSF-EAALAGAGPRLTEQ-------PCG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 220 ALYIYTSGTTGLPKAAMIT-HQRIWYGTGLTFVS------GLKADDVIYITLPFYHSAAL--LIGIHGCivaGATLALRT 290
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDlPGRDVDAPGDPIVAiarafyDISESDIYYSSAPIYHAAPLrwCSMVHAL---GGTVVLAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 291 KFSASQFWDDCRKYNVTVIQYIGEL-LRYLcnspqKPNDrDHKVRLALGNgLRG----------DVWRQFVKRFGDIcIY 359
Cdd:PRK13390 228 RFDAQATLGHVERYRITVTQMVPTMfVRLL-----KLDA-DVRTRYDVSS-LRAvihaaapcpvDVKHAMIDWLGPI-VY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 360 EFYAATEGN----IGFMNYARKVGAVGRvnylqkkiitydlikyDVEKDEPVRDENGYcvRVPKGEVGLLVCKITQLtPF 435
Cdd:PRK13390 300 EYYSSTEAHgmtfIDSPDWLAHPGSVGR----------------SVLGDLHICDDDGN--ELPAGRIGTVYFERDRL-PF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 436 NgYAGAKAQTEKKKlrdvFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGv 515
Cdd:PRK13390 361 R-YLNDPEKTAAAQ----HPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG- 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 516 hVPDHE-GRIGMASIKMKENheFDG-KKLFQHIADYLPS----YARPRFLRIQDTIEITGTFK 572
Cdd:PRK13390 435 -VPDPEmGEQVKAVIQLVEG--IRGsDELARELIDYTRSriahYKAPRSVEFVDELPRTPTGK 494
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-572 |
9.57e-27 |
|
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: 113.69 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 86 RRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC----LNYNIRAKSLLHCFQCCGAKVLLVSPEL 161
Cdd:cd05922 1 LGVSAAASALLEA-GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 162 QAAVEEILPSLKKDDVSIyyvsrtsNTDGIDSFLDKVDEVstEPIPESwrsevtfstPALYIYTSGTTGLPKAAMITHQR 241
Cdd:cd05922 80 ADRLRDALPASPDPGTVL-------DADGIRAARASAPAH--EVSHED---------LALLLYTSGSTGSPKLVRLSHQN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 242 IWYGT-GLTFVSGLKADDVIYITLPFYHSAAL-LIGIHgcIVAGATLALRTKFSASQ-FWDDCRKYNVT---VIQYIGEL 315
Cdd:cd05922 142 LLANArSIAEYLGITADDRALTVLPLSYDYGLsVLNTH--LLRGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 316 -------------LRYLCNSpqkpndrdhkvrlalGNGLRGDVWRQFVKRFGDICIYEFYAATEGNiGFMNY------AR 376
Cdd:cd05922 220 ltrlgfdpaklpsLRYLTQA---------------GGRLPQETIARLRELLPGAQVYVMYGQTEAT-RRMTYlpperiLE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 377 KVGAVGRVnyLQKKIITydlikydvekdepVRDENGYcvRVPKGEVGLLVckITQLTPFNGYAGAKAQTEKKKLrdvfKK 456
Cdd:cd05922 284 KPGSIGLA--IPGGEFE-------------ILDDDGT--PTPPGEPGEIV--HRGPNVMKGYWNDPPYRRKEGR----GG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 457 GDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKEnhe 536
Cdd:cd05922 341 GVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKI--- 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 308153494 537 fDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd05922 416 -DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGK 450
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
76-562 |
3.96e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 112.48 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGL-AALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 LVSPELQAAVEEILPSlkkddvSIYYVSRTSNTDGIDSFldKVDEVSTEPIP-----ESWRSEVTFST------PALYIY 224
Cdd:PRK12406 88 IAHADLLHGLASALPA------GVTVLSVPTPPEIAAAY--RISPALLTPPAgaidwEGWLAQQEPYDgppvpqPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 225 TSGTTGLPK----AAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGcIVAGATLALRTKFSASQFWDD 300
Cdd:PRK12406 160 TSGTTGHPKgvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 301 CRKYNVTVIQYIGELLRYLCNSPQkpndrdhKVRLALG-NGLR----------GDVWRQFVKRFGDIcIYEFYAATE-GN 368
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPE-------EVRAKYDvSSLRhvihaaapcpADVKRAMIEWWGPV-IYEYYGSTEsGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 369 IGFMN---YARKVGAVGRVNY-LQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVCKITQLTPFNgYAGakaq 444
Cdd:PRK12406 311 VTFATsedALSHPGTVGKAAPgAELRFV----------------DEDGR--PLPQGEIGEIYSRIAGNPDFT-YHN---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 445 tEKKKLRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GR 523
Cdd:PRK12406 368 -KPEKRAEIDRGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGE 442
|
490 500 510
....*....|....*....|....*....|....*....
gi 308153494 524 IGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQ 562
Cdd:PRK12406 443 ALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
79-578 |
8.05e-26 |
|
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: 110.50 E-value: 8.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVs 158
Cdd:cd05972 1 WSFRELKRESAKAANVLAKL-GLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 159 pelqaaveeilpslkkddvsiyyvsrtsntdgidsflDKVDevstepipeswrsevtfstPALYIYTSGTTGLPKAAMIT 238
Cdd:cd05972 79 -------------------------------------DAED-------------------PALIYFTSGTTGLPKGVLHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 239 HqRIWYGTGLT--FVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGAT--LALRTKFSASQFWDDCRKYNVTViqyige 314
Cdd:cd05972 103 H-SYPLGHIPTaaYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATvfVYEGPRFDAERILELLERYGVTS------ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 315 llryLCNSP--------QKPNDRDHK-VRLALGNG--LRGDVWRQFVKRFGdICIYEFYAATEGNIGFMNYAR---KVGA 380
Cdd:cd05972 176 ----FCGPPtayrmlikQDLSSYKFShLRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTETGLTVGNFPDmpvKPGS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 381 VGRVnylqkkiitydLIKYDVEkdepVRDENGYcvRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKkklrdvFKKGDlY 460
Cdd:cd05972 251 MGRP-----------TPGYDVA----IIDDDGR--ELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEA------SIRGD-Y 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 461 FNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTvgLVDF--VQEVNVygVHVPDHE-GRIGMASIKMKENHEF 537
Cdd:cd05972 307 YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESA--LLEHpaVAEAAV--VGSPDPVrGEVVKAFVVLTSGYEP 382
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 308153494 538 D---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05972 383 SeelAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
68-580 |
7.29e-25 |
|
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: 107.76 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 68 HKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVwlwlgLVKLGCAMAclnyniraksllhcf 147
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYV-----VAQLAIWRA--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 148 qccGAKVLLVSPelQAAVEEILPSLKKDDVSIyyvsrtsntdgidsFLDkvdevstepipeswrsevtfstPALYIYTSG 227
Cdd:cd05941 61 ---GGVAVPLNP--SYPLAELEYVITDSEPSL--------------VLD----------------------PALILYTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 228 TTGLPKAAMITHQRIwygtgLTFVSGL------KADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDC 301
Cdd:cd05941 100 TTGRPKGVVLTHANL-----AANVRALvdawrwTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 302 RKYNVTVIQ-----YIgELLRYLcnsPQKPNDRDHKVRLALGN---------GLRGDVWRQFVKRFGDIcIYEFYAATEG 367
Cdd:cd05941 175 LMPSITVFMgvptiYT-RLLQYY---EAHFTDPQFARAAAAERlrlmvsgsaALPVPTLEEWEAITGHT-LLERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 368 NIGFMNYA---RKVGAVGR----VnylQKKIitydlikydvekdepVRDENGycVRVPKGEVGLLVCKITQLtpFNGY-- 438
Cdd:cd05941 250 GMALSNPLdgeRRPGTVGMplpgV---QARI---------------VDEETG--EPLPRGEVGEIQVRGPSV--FKEYwn 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 439 ---AGAKAQTEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVG-DTFRWKGENVATTEVADTVGLVDFVQEVNVYG 514
Cdd:cd05941 308 kpeATKEEFTD-----------DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIG 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308153494 515 vhVPDHE-GRIGMASIKMKEN-HEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 580
Cdd:cd05941 377 --VPDPDwGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
54-557 |
8.60e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 108.93 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 134 LNYNIRAKSLLHCFQCCGAKVLLV----SPELQ-----AAVEEI--------------------LPSLKKddvsiyyvSR 184
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVwdkvAPTVErlrrtTPLETIvsvnmiaampllqrlalrlpIPALRK--------AR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 185 TSNTDGIDSFLDKVDEVSTEPIPESWRS---EVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGT--GLTFVSGL-KADD 258
Cdd:PRK05605 184 AALTGPAPGTVPWETLVDAAIGGDGSDVshpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqGKAWVPGLgDGPE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 259 VIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALG 338
Cdd:PRK05605 264 RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 339 NG--LRGDVWRQFVKRFGDICIyEFYAATE------GNIgfMNYARKVGAVG--------RVnylqkkiitydlikydVE 402
Cdd:PRK05605 344 GAmaLPVSTVELWEKLTGGLLV-EGYGLTEtspiivGNP--MSDDRRPGYVGvpfpdtevRI----------------VD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 403 KDEPVRDengycvrVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVG 482
Cdd:PRK05605 405 PEDPDET-------MPDGEEGELLVRGPQV--FKGYWNRPEETAK-----SFLDG--WFRTGDVVVMEEDGFIRIVDRIK 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 483 DTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:PRK05605 469 ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV-VAAVVLEPGAALDPEGLRAYCREHLTRYKVPR 542
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
56-557 |
2.12e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.43 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 56 LRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK07470 9 LAHFLRQaARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 NYNIRAKSLLHCFQCCGAKVLLVS---PELQAAVEEILPSLKKDdVSIyyvsrtSNTDGIDSFLDKVDEVSTEPIPESwr 211
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHadfPEHAAAVRAASPDLTHV-VAI------GGARAGLDYEALVARHLGARVANA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 212 sEVTFSTPALYIYTSGTTGLPKAAMITHqriwyGTgLTFV---------SGLKADDVIYITLPFYHSAalliGIHG-CIV 281
Cdd:PRK07470 159 -AVDHDDPCWFFFTSGTTGRPKAAVLTH-----GQ-MAFVitnhladlmPGTTEQDASLVVAPLSHGA----GIHQlCQV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 282 A-GATLALRT--KFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNdRDH-KVRLALGNG---LRGDVWRQfVKRFG 354
Cdd:PRK07470 228 ArGAATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDR-YDHsSLRYVIYAGapmYRADQKRA-LAKLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 355 DIcIYEFYAATE--GNIGFMNYA---------RKVGAVGrvnylqkkiitYDLIKYDVEkdepVRDENGYcvRVPKGEVG 423
Cdd:PRK07470 306 KV-LVQYFGLGEvtGNITVLPPAlhdaedgpdARIGTCG-----------FERTGMEVQ----IQDDEGR--ELPPGETG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 424 llvcKITQLTP--FNGY-----AGAKAqtekkklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 496
Cdd:PRK07470 368 ----EICVIGPavFAGYynnpeANAKA----------FRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPRE 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308153494 497 VADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:PRK07470 432 IEEKLLTHPAVSEVAVLG--VPDPVwGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
56-581 |
2.55e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.43 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 56 LRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK06710 26 LHKYVEQmASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 NYNIRAKSLLHCFQCCGAKVLL----VSPEL---QAA----------VEEILPsLKKDDVSIYYVSRTSNtdgidsFLDK 197
Cdd:PRK06710 105 NPLYTERELEYQLHDSGAKVILcldlVFPRVtnvQSAtkiehvivtrIADFLP-FPKNLLYPFVQKKQSN------LVVK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 198 VDEVSTEPIPESWRSEVTFSTP---------ALYIYTSGTTGLPKAAMITHQRIWYGT--GLTFVSGLK-ADDVIYITLP 265
Cdd:PRK06710 178 VSESETIHLWNSVEKEVNTGVEvpcdpendlALLQYTGGTTGFPKGVMLTHKNLVSNTlmGVQWLYNCKeGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 266 FYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRG 343
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 344 DVWRQFVKRFGDICIyEFYAATEGNigfmnyarkvgAVGRVNYLQKKIITYDL-IKYDVEKDEPVRDENGYCVrvPKGEV 422
Cdd:PRK06710 338 EVQEKFETVTGGKLV-EGYGLTESS-----------PVTHSNFLWEKRVPGSIgVPWPDTEAMIMSLETGEAL--PPGEI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 423 GLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVG 502
Cdd:PRK06710 404 GEIVVKGPQI--MKGYWNKPEETAA-----VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 503 LVDFVQEVNVYGVHVPdHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEE 581
Cdd:PRK06710 475 EHEKVQEVVTIGVPDP-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-366 |
3.51e-24 |
|
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: 108.41 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAm 131
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEMVVALLAVLKAGAA- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 aclnY-----NIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSLKKDDVSiyyvsrtsntdgidsfldkVDEVSTEPI 206
Cdd:COG1020 553 ----YvpldpAYPAERLAYMLEDAGARLVLT----QSALAARLPELGVPVLA-------------------LDALALAAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 207 PESW-RSEVTFSTPAlY-IYTSGTTGLPKAAMITHQriwygtGLT-FVS------GLKADDVIYITLPFYHSAALLiGIH 277
Cdd:COG1020 606 PATNpPVPVTPDDLA-YvIYTSGSTGRPKGVMVEHR------ALVnLLAwmqrryGLGPGDRVLQFASLSFDASVW-EIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 278 GCIVAGATLALRTK---FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRdhkVRLAL--GNGLRGDVWRQFVKR 352
Cdd:COG1020 678 GALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPS---LRLVLvgGEALPPELVRRWRAR 754
|
330
....*....|....
gi 308153494 353 FGDICIYEFYAATE 366
Cdd:COG1020 755 LPGARLVNLYGPTE 768
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
53-481 |
4.81e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 106.20 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLE-KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK08314 9 ETSLFHNLEvSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELqaaVEEILPSLKKDDVSIYYVSRtsntdgidsFLDKVDEVSTEPIPE--- 208
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSEL---APKVAPAVGNLRLRHVIVAQ---------YSDYLPAEPEIAVPAwlr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 209 --------------SWRS-----------EVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYI 262
Cdd:PRK08314 157 aepplqalapggvvAWKEalaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAvGSVLWSNSTPESVVLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 263 TLPFYHSAALLIGIHGCIVAGATLALRTKfsasqfWD-----DC-RKYNVTVIQYIGELLRYLCNSPqKPNDRDHKVRLA 336
Cdd:PRK08314 237 VLPLFHVTGMVHSMNAPIYAGATVVLMPR------WDreaaaRLiERYRVTHWTNIPTMVVDFLASP-GLAERDLSSLRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 337 LGNG---LRGDVWRQFVKRFGdICIYEFYAATEgNIGF--MN-YAR-KVGAVGrvnylqkkIITYDLikydvekDEPVRD 409
Cdd:PRK08314 310 IGGGgaaMPEAVAERLKELTG-LDYVEGYGLTE-TMAQthSNpPDRpKLQCLG--------IPTFGV-------DARVID 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 410 -ENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKK--GDLYFNSGDLLMVDHENFIYFHDRV 481
Cdd:PRK08314 373 pETL--EELPPGEVGEIVVHGPQV--FKGYWNRPEATAE-----AFIEidGKRFFRTGDLGRMDEEGYFFITDRL 438
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
49-572 |
5.78e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 106.00 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 49 RRPARTILRAFLEKARQTPHKPFLLfrDE--TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLI--DElgTLTWRELDERSDALAAALQ-ALPIGEPRVVGIMCRNHRGFVEALLAANR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSpelqaavEEILPSLKKDDVSIYYVSRTSN-TDGIDSFLdkVDEVSTEP 205
Cdd:PRK13382 116 IGADILLLNTSFAGPALAEVVTREGVDTVIYD-------EEFSATVDRALADCPQATRIVAwTDEDHDLT--VEVLIAAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 206 IPEswRSEVTFSTPALYIYTSGTTGLPKAAmithQRIWYGTGLTFVSGL-----KADDVIYITLPFYH----SAALLIGI 276
Cdd:PRK13382 187 AGQ--RPEPTGRKGRVILLTSGTTGTPKGA----RRSGPGGIGTLKAILdrtpwRAEEPTVIVAPMFHawgfSQLVLAAS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 277 HGCivagaTLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDH----KVRLALGNGLRGDVWRQFVKR 352
Cdd:PRK13382 261 LAC-----TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSgrslRFAAASGSRMRPDVVIAFMDQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 353 FGDIcIYEFYAATE-GNIGFMNYARkvgavgrvnyLQKKIITYDliKYDVEKDEPVRDENGYcvRVPKGEVG-LLVCKIT 430
Cdd:PRK13382 336 FGDV-IYNNYNATEaGMIATATPAD----------LRAAPDTAG--RPAEGTEIRILDQDFR--EVPTGEVGtIFVRNDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 431 QltpFNGYAGAKAQTekkklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEV 510
Cdd:PRK13382 401 Q---FDGYTSGSTKD--------FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEA 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 511 NVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:PRK13382 468 AVIG--VDDEQyGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-578 |
5.85e-24 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 104.85 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 69 KPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 149 CCGAKVLLVSpelqaaveeilpslkKDDVsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfstpALYIYTSGT 228
Cdd:cd05919 80 DCEARLVVTS---------------ADDI------------------------------------------AYLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 229 TGLPKAAMITHqRIWYGTGLTF---VSGLKADDVIY--------------ITLPFYHSAALLIgIHGCIVAGATLALRTK 291
Cdd:cd05919 103 TGPPKGVMHAH-RDPLLFADAMareALGLTPGDRVFssakmffgyglgnsLWFPLAVGASAVL-NPGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 292 FSASQFwddcrkYNVTVIqyigelLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFG-DICiyEFYAATEgn 368
Cdd:cd05919 181 FRPTVL------YGVPTF------YANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFGgPIL--DGIGATE-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 369 IGFMNYARKVGAVgRVNYLQKKIITYDLikydvekdePVRDENGYcvRVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKK 448
Cdd:cd05919 245 VGHIFLSNRPGAW-RLGSTGRPVPGYEI---------RLVDEEGH--TIPPGEEGDLLVRGPSAAV--GYWNNPEKSRAT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 449 klrdvFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHEGRIGM-A 527
Cdd:cd05919 311 -----FNGGWYR--TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLtA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 308153494 528 SIKMKENHEFDGK---KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05919 382 FVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
60-496 |
9.46e-24 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 105.01 E-value: 9.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 60 LEKARQTPHKPFLLfrD----ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:cd05904 12 FLFASAHPSRPALI--DaatgRALTYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 136 YNIRAKSLLHCFQCCGAKVLLVSPELQAAVEE------ILPSLkkDDVSIYYVSRTSNTDGidsfldkvDEVSTEPIPES 209
Cdd:cd05904 89 PLSTPAEIAKQVKDSGAKLAFTTAELAEKLASlalpvvLLDSA--EFDSLSFSDLLFEADE--------AEPPVVVIKQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 210 wrsevtfSTPALyIYTSGTTGLPKAAMITHQRIwygtgLTFVSGLKA--------DDVIYITLPFYHSAALLIGIHGCIV 281
Cdd:cd05904 159 -------DVAAL-LYSSGTTGRSKGVMLTHRNL-----IAMVAQFVAgegsnsdsEDVFLCVLPMFHIYGLSSFALGLLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 282 AGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGDICI 358
Cdd:cd05904 226 LGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSP-IVDKYDLSSLRQIMSGaapLGKELIEAFRAKFPNVDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 359 YEFYAATE-GNIGFMNYA-----RKVGAVGRV--NyLQKKIItydlikyDVE--KDEPVRDENGYCVRVPKgevgllVCK 428
Cdd:cd05904 305 GQGYGMTEsTGVVAMCFApekdrAKYGSVGRLvpN-VEAKIV-------DPEtgESLPPNQTGELWIRGPS------IMK 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308153494 429 itqltpfnGYAGAKAQTEkkklRDVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 496
Cdd:cd05904 371 --------GYLNNPEATA----ATIDKEGWLH--TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAE 424
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
80-578 |
1.53e-23 |
|
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: 104.63 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNynIR------AKSLLHCfqccGAK 153
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN--PRlfpeqiAYIINHA----EDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 154 VLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNT-DGIDSFLDKVDEVSTEPIPESWrSEVTFSTPALYIYTSGTTGLP 232
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPePAGVGVLAYEELLAAESPEYDW-PDFDENTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 233 KAAMITHQRIW---YGTGLTFVSGLKADDVIYITLPFYHSAALliGI-HGCIVAGATLALRTKF----SASQFWDdcrKY 304
Cdd:cd12119 179 KGVVYSHRSLVlhaMAALLTDGLGLSESDVVLPVVPMFHVNAW--GLpYAAAMVGAKLVLPGPYldpaSLAELIE---RE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 305 NVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFVKRFGD--ICIYEFYAATE-GNIGFMNY----ARK 377
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGG--SAVPRSLIEAFEErgVRVIHAWGMTEtSPLGTVARppseHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 378 VGAVGRVNYLQKkiITYDLIKYDVEkdepVRDENGycVRVPK--GEVGLLVCK---ITQltpfnGYAGAKAQTEkkklrd 452
Cdd:cd12119 332 LSEDEQLALRAK--QGRPVPGVELR----IVDDDG--RELPWdgKAVGELQVRgpwVTK-----SYYKNDEESE------ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 453 vFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvpDHE--GRIGMASIK 530
Cdd:cd12119 393 -ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGV---PHPkwGERPLAVVV 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 308153494 531 MKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd12119 469 LKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
78-557 |
2.12e-23 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 102.81 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLhcFQccgakvllv 157
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELA--FQ--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 spelqaaveeilpsLKKDDVsiyyvsrtsntdgidsfldKVDEVSTepipeswrsevtfstpalYIYTSGTTGLPKAAMI 237
Cdd:cd05912 69 --------------LKDSDV-------------------KLDDIAT------------------IMYTSGTTGKPKGVQQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 238 THQRIWY---GTGLTFvsGLKADDVIYITLPFYHSAALLIGIHGcIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGE 314
Cdd:cd05912 98 TFGNHWWsaiGSALNL--GLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 315 LLRYLC---NSPQKPNDRdhkvRLALGNG-LRGDVWRQFVKRfgDICIYEFYAATEG-----NIGFMNYARKVGAVGRvn 385
Cdd:cd05912 175 MLQRLLeilGEGYPNNLR----CILLGGGpAPKPLLEQCKEK--GIPVYQSYGMTETcsqivTLSPEDALNKIGSAGK-- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 386 ylqkkiityDLIKYDVEkdepVRDENGycvrvPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkklrdVFKKGdlYFNSGD 465
Cdd:cd05912 247 ---------PLFPVELK----IEDDGQ-----PPYEVGEILLKGPNVTK--GYLNRPDATEE-----SFENG--WFKTGD 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 466 LLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKEnhEFDGKKLFQ 544
Cdd:cd05912 300 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG--IPDDKwGQVPVAFVVSER--PISEEELIA 375
|
490
....*....|...
gi 308153494 545 HIADYLPSYARPR 557
Cdd:cd05912 376 YCSEKLAKYKVPK 388
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-466 |
6.63e-23 |
|
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: 101.57 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEP-AYVWLwLGLVKLGCA---------MACLNYNIRAksllhcfqc 149
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAeLVVAI-LAVLKAGAAyvpldpaypAERLAFILED--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 150 CGAKVLLVSPELQAAVEEILPSlkkddvsIYYVSRTSNTDGIDSFLDKVDEVSTEPipeswrsevtfSTPALYIYTSGTT 229
Cdd:TIGR01733 71 AGARLLLTDSALASRLAGLVLP-------VILLDPLELAALDDAPAPPPPDAPSGP-----------DDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 230 GLPKAAMITHQRIwygtgLTFVS------GLKADDVIYITLPFYHSAALLiGIHGCIVAGATLAL------RTKFSASQF 297
Cdd:TIGR01733 133 GRPKGVVVTHRSL-----VNLLAwlarryGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVppedeeRDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 298 WDdcRKYNVTVIQYIGELLRYLcnSPQKPNDRDHKVRLALGnG--LRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYa 375
Cdd:TIGR01733 207 LI--AEHPVTVLNLTPSLLALL--AAALPPALASLRLVILG-GeaLTPALVDRWRARGPGARLINLYGPTETTVWSTAT- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 376 rkvgavgrvnylqkkiiTYDLIKYDVEKDEP-----------VRDENGYcvRVPKGEVGLLVCKITQLTPfnGYAGAKAQ 444
Cdd:TIGR01733 281 -----------------LVDPDDAPRESPVPigrplantrlyVLDDDLR--PVPVGVVGELYIGGPGVAR--GYLNRPEL 339
|
410 420
....*....|....*....|....*
gi 308153494 445 TEKKKLRDVFKKGD---LYFnSGDL 466
Cdd:TIGR01733 340 TAERFVPDPFAGGDgarLYR-TGDL 363
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
57-288 |
1.37e-22 |
|
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: 101.51 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkddvsiyyvsrtsntdgidsFLDKVDEVSTEPiPESWRSEVTF 216
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-----------------------AVVIDEALDAGP-AGNPAVPVSP 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 217 STPALYIYTSGTTGLPKAAMITHQRI-------WYGTgltfvsgLKADDVIYITLPFYHSAALLiGIHGCIVAGATLAL 288
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVAVTHRGVvrlvkntNYVT-------LGPDDRVLQTSPLAFDASTF-EIWGALLNGARLVL 206
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
53-572 |
2.34e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.11 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMA 132
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 133 CLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGID----SFLDKVDEVSTEPIPE 208
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIA-----DTPVKQVITTGLGDMLGfpkaALVNFVVKYVKKLVPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 209 -------SWRSEVTF----STPALYI---------YTSGTTGLPKAAMITHQRI---------WYGTGLTFVSGlkaDDV 259
Cdd:PRK08751 180 yringaiRFREALALgrkhSMPTLQIepddiaflqYTGGTTGVAKGAMLTHRNLvanmqqahqWLAGTGKLEEG---CEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 260 IYITLPFYHSAALLI-GIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALG 338
Cdd:PRK08751 257 VITALPLYHIFALTAnGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 339 NGLRgdVWRQFVKRFGDIC---IYEFYAATEGN----IGFMNYARKVGAVGRvnylqkKIITYDLIkydvekdepVRDEN 411
Cdd:PRK08751 337 GGMA--VQRSVAERWKQVTgltLVEAYGLTETSpaacINPLTLKEYNGSIGL------PIPSTDAC---------IKDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 412 GYCvrVPKGEVGLLVCKITQLtpFNGYagAKAQTEKKKLRDvfkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGEN 491
Cdd:PRK08751 400 GTV--LAIGEIGELCIKGPQV--MKGY--WKRPEETAKVMD----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 492 VATTEVADTVGLVDFVQEVNVYGvhVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTF 571
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVG--VPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVG 547
|
.
gi 308153494 572 K 572
Cdd:PRK08751 548 K 548
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
60-308 |
3.32e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.44 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 60 LEKARQTPHKPFLLfrD----ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:PLN02246 30 FERLSEFSDRPCLI--DgatgRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 136 YNIRAKSLLHCFQCCGAKVLLVSPelqAAVEEILPSLKKDDVSIyyVSRTSNTDGIDSF--LDKVDEvstEPIPESwrsE 213
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQS---CYVDKLKGLAEDDGVTV--VTIDDPPEGCLHFseLTQADE---NELPEV---E 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 214 VTFSTPALYIYTSGTTGLPKAAMITHQriwygtGL-TFVS----------GLKADDVIYITLPFYH----SAALLIGIHg 278
Cdd:PLN02246 176 ISPDDVVALPYSSGTTGLPKGVMLTHK------GLvTSVAqqvdgenpnlYFHSDDVILCVLPMFHiyslNSVLLCGLR- 248
|
250 260 270
....*....|....*....|....*....|
gi 308153494 279 civAGATLALRTKFSASQFWDDCRKYNVTV 308
Cdd:PLN02246 249 ---VGAAILIMPKFEIGALLELIQRHKVTI 275
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
78-572 |
9.84e-22 |
|
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: 98.94 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDhlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK--MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 SPELQAAVEEILPSLKKDDVSIYYVSRTSNTDgidSFLDKVDEVSTEPIPESW------RSEVTFSTPALYIYTSGTTGL 231
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDARIVYLEDLRAKI---SKADKCKAFLAGKFPPKWllrifgVAPVQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 232 PKAAMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHS--------AALLIGIHgciVAGATLALRTKfsasQFWDDCR 302
Cdd:cd05909 162 PKGVVLSHKNLLANVeQITAIFDPNPEDVVFGALPFFHSfgltgclwLPLLSGIK---VVFHPNPLDYK----KIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 303 KYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATEG----NIGFMNYARKV 378
Cdd:cd05909 235 DKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTECspviSVNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 379 GAVGR-VNYLQKKIItydlikyDVEKDEPvrdengycvrVPKGEVGLLVCKITQLtpFNGYAGAKAQTekkklrdVFKKG 457
Cdd:cd05909 314 GTVGRpLPGMEVKIV-------SVETHEE----------VPIGEGGLLLVRGPNV--MLGYLNEPELT-------SFAFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 458 DLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVdFVQEVNVYGVHVPDheGRIGMASIKMKENHEF 537
Cdd:cd05909 368 DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI-LPEDNEVAVVSVPD--GRKGEKIVLLTTTTDT 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 308153494 538 DGKKLFQHI-ADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd05909 445 DPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGK 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
49-581 |
2.57e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 98.19 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 49 RRPARTILRAFlekARQTPHKPFLLFRDETLTYAQVDRRSNQVArALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLG 128
Cdd:PRK06178 32 ERPLTEYLRAW---ARERPQRPAIIFYGHVITYAELDELSDRFA-ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 129 CAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGI---------DSF----- 194
Cdd:PRK06178 108 AVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRA-----ETSLRHVIVTSLADVLpaeptlplpDSLraprl 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 195 -----LDKVDEVSTEPIPESWRSeVTFSTPALYIYTSGTTGLPKAAMITHQRIWYgTGLTFVS---GLKADDVIYITLPF 266
Cdd:PRK06178 183 aaagaIDLLPALRACTAPVPLPP-PALDALAALNYTGGTTGMPKGCEHTQRDMVY-TAAAAYAvavVGGEDSVFLSFLPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 267 YHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVT----VIQYIGELLrylcnspQKPNDRDHKVR-------- 334
Cdd:PRK06178 261 FWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTrtvmLVDNAVELM-------DHPRFAEYDLSslrqvrvv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 335 ---LALGNGLRGDvWRQFVkrfGDICIYEFYAATEGN------IGF----MNYARKVGAVG-RVNYLQKKIItydlikyD 400
Cdd:PRK06178 334 sfvKKLNPDYRQR-WRALT---GSVLAEAAWGMTETHtcdtftAGFqdddFDLLSQPVFVGlPVPGTEFKIC-------D 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 401 VEKDE--PVRDENGYCVRVPkgevgllvckitqlTPFNGYAGaKAQTEKKKLRDvfkkGdlYFNSGDLLMVDHENFIYFH 478
Cdd:PRK06178 403 FETGEllPLGAEGEIVVRTP--------------SLLKGYWN-KPEATAEALRD----G--WLHTGDIGKIDEQGFLHYL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 479 DRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:PRK06178 462 GRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG--RPDpDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE 539
|
570 580
....*....|....*....|....
gi 308153494 558 fLRIQDTIEITGTFKHRKMTLVEE 581
Cdd:PRK06178 540 -IRIVDALPMTATGKVRKQDLQAL 562
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
53-578 |
8.60e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 96.00 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGlrQGDCVALLMGNEPAYVWLWLGLVKLGCAma 132
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWT-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 133 CLNYNIRAKsllhcfqccgakvllvspelQAAVEEILpSLKKDDVSI---YYVSRTSNTDGIDSFLDKVDEVSTEPIPES 209
Cdd:PRK07638 77 CVPLDIKWK--------------------QDELKERL-AISNADMIVterYKLNDLPDEEGRVIEIDEWKRMIEKYLPTY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 210 WRSEVTFSTPALYIYTSGTTGLPKAAMITHQRiWYG----TGLTFvsGLKADDVIYITLPFYHSAALLIGIHGCIVaGAT 285
Cdd:PRK07638 136 APIENVQNAPFYMGFTSGSTGKPKAFLRAQQS-WLHsfdcNVHDF--HMKREDSVLIAGTLVHSLFLYGAISTLYV-GQT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 286 LALRTKFSASQFWDDCRKYNVTVIQYIGELLrylcNSPQKPND-RDHKVRLALGnglrGDVW-----RQFVKRFGDICIY 359
Cdd:PRK07638 212 VHLMRKFIPNQVLDKLETENISVMYTVPTML----ESLYKENRvIENKMKIISS----GAKWeaeakEKIKNIFPYAKLY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 360 EFYAATEgnIGFMNY------ARKVGAVGR-VNYLQKKIitydlikydvekdepvRDENGycVRVPKGEVGLLVCKITQL 432
Cdd:PRK07638 284 EFYGASE--LSFVTAlvdeesERRPNSVGRpFHNVQVRI----------------CNEAG--EEVQKGEIGTVYVKSPQF 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 433 tpFNGYAGAKAQTEKKKLrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNV 512
Cdd:PRK07638 344 --FMGYIIGGVLARELNA-------DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVV 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 513 YGvhVPD-HEGRIGMASIKMKENHefdgKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:PRK07638 415 IG--VPDsYWGEKPVAIIKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
69-578 |
1.38e-20 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 94.85 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 69 KPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 149 CCGAKVLLVSPELQAAveeilpslkkDDVsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfstpALYIYTSGT 228
Cdd:cd05958 81 KARITVALCAHALTAS----------DDI------------------------------------------CILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 229 TGLPKAAMITHqRIWYGTGLTF---VSGLKADDVIYITLPFYHSAAL---LIGIHGcivAGATLALRTKFSASQFWDDCR 302
Cdd:cd05958 109 TGAPKATMHFH-RDPLASADRYavnVLRLREDDRFVGSPPLAFTFGLggvLLFPFG---VGASGVLLEEATPDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 303 KYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGDICI---------YEFYAATEGNIgf 371
Cdd:cd05958 185 RYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATGIPIIdgigstemfHIFISARPGDA-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 372 mnyarKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGYcvRVPKGEVGLLVCKitqltpfnGYAGAKAQTEKKKlR 451
Cdd:cd05958 263 -----RPGATGKP-----------VPGYEAK----VVDDEGN--PVPDGTIGRLAVR--------GPTGCRYLADKRQ-R 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 452 DVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIK 530
Cdd:cd05958 312 TYVQGGWNI--TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVG--HPDESrGVVVKAFVV 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 308153494 531 MKENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05958 388 LRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
82-580 |
1.84e-20 |
|
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: 94.75 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 82 AQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYV-WLWLGLvklGCAMACLNYNIRAKSLLH---CFQCCGAKVLLV 157
Cdd:cd05929 1 LEARDLDRAQVFHQRR-LLLLDVYSIALNRNARAAAAeGVWIAD---GVYIYLINSILTVFAAAAawkCGACPAYKSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 SPELQAAVEEILPSLKkdDVSIYYVSRTSntDGIDSFLDKVDEVSTEPIPESWRsevtfstPALYIYTSGTTGLPK---- 233
Cdd:cd05929 77 PRAEACAIIEIKAAAL--VCGLFTGGGAL--DGLEDYEAAEGGSPETPIEDEAA-------GWKMLYSGGTTGRPKgikr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 -----AAMITHQRIWygtglTFVSGLKADDVIYITLPFYHSAALlIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTV 308
Cdd:cd05929 146 glpggPPDNDTLMAA-----ALGFGPGADSVYLSPAPLYHAAPF-RWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 309 IQYIGELLRYLCNSPQKPNDRDH--KVRLALGNGLRGDVW--RQFVKRFGDIcIYEFYAATEGN----IGFMNYARKVGA 380
Cdd:cd05929 220 AQFVPTMFVRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWvkEQWIDWGGPI-IWEYYGGTEGQgltiINGEEWLTHPGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 381 VGRVnylqkkiitydlikydVEKDEPVRDENGYcvRVPKGEVGLLVCKITQ-LTPFNGYAGAKAQTEKKKLRDVfkkgdl 459
Cdd:cd05929 299 VGRA----------------VLGKVHILDEDGN--EVPPGEIGEVYFANGPgFEYTNDPEKTAAARNEGGWSTL------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 460 yfnsGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASI---KMKENH 535
Cdd:cd05929 355 ----GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVVqpaPGADAG 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 308153494 536 EFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 580
Cdd:cd05929 429 TALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
53-581 |
2.44e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 94.73 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLL-FRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTaVRLgtgapRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS--------PELQAAVEEILPSLKKddvsIYYVsrtsNTDGIDSFldkv 198
Cdd:PRK13295 103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVPktfrgfdhAAMARRLRPELPALRH----VVVV----GGDGADSF---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 199 DEVSTEPIPESWRSE---VTFSTP-----ALYIYTSGTTGLPKAAMITHQRIW-----YGTGLtfvsGLKADDVIYITLP 265
Cdd:PRK13295 171 EALLITPAWEQEPDApaiLARLRPgpddvTQLIYTSGTTGEPKGVMHTANTLManivpYAERL----GLGADDVILMASP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 266 FYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPnDRDH---KVRLALGNGLR 342
Cdd:PRK13295 247 MAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKES-GRPVsslRTFLCAGAPIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 343 GDVWRQFVKRFGdICIYEFYAATEgnigfmNYARKVGAVGRVNylqKKIITYDliKYDVEKDE-PVRDENGycVRVPKGE 421
Cdd:PRK13295 326 GALVERARAALG-AKIVSAWGMTE------NGAVTLTKLDDPD---ERASTTD--GCPLPGVEvRVVDADG--APLPAGQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 422 VGLLVckITQLTPFNGYAGakaqteKKKLRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTV 501
Cdd:PRK13295 392 IGRLQ--VRGCSNFGGYLK------RPQLNGTDADG--WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 502 GLVDFVQEVNVygVHVPDHegRIG---MASIKMKENHEFDgkklFQHIADYLPS--YAR---PRFLRIQDTIEITGTFKH 573
Cdd:PRK13295 462 YRHPAIAQVAI--VAYPDE--RLGeraCAFVVPRPGQSLD----FEEMVEFLKAqkVAKqyiPERLVVRDALPRTPSGKI 533
|
....*...
gi 308153494 574 RKMTLVEE 581
Cdd:PRK13295 534 QKFRLREM 541
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
54-580 |
6.61e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 93.68 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDETL--TYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELQ-----AAVEEILPSLKKDD--------------VSIYYVSRTSNTDGID 192
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFKtsdyhAMLQELLPGLAEGQpgalacerlpelrgVVSLAPAPPPGFLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 193 SFLDKVDEVSTEPIPESwRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVS-GLKADDVIYITLPFYHSAA 271
Cdd:PRK12583 178 ELQARGETVSREALAER-QASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESlGLTEHDRLCVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 272 LLIGIHGCIVAGATL--------ALRTKFSASQfwDDCRKYNVTVIQYIGELlrylcNSPQKPNDRDHKVRLALGNGlrG 343
Cdd:PRK12583 257 MVLANLGCMTVGACLvypneafdPLATLQAVEE--ERCTALYGVPTMFIAEL-----DHPQRGNFDLSSLRTGIMAG--A 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 344 DVWRQFVKR------FGDICIYefYAATEGN-IGFMNYA-----RKVGAVGRVN-YLQKKIItydlikydvekdepvrDE 410
Cdd:PRK12583 328 PCPIEVMRRvmdemhMAEVQIA--YGMTETSpVSLQTTAaddleRRVETVGRTQpHLEVKVV----------------DP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 411 NGycVRVPKGEVGLLvCkitqltpFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGE 490
Cdd:PRK12583 390 DG--ATVPRGEIGEL-C-------TRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 491 NVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITG 569
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFG--VPDEKyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTV 537
|
570
....*....|.
gi 308153494 570 TFKHRKMTLVE 580
Cdd:PRK12583 538 TGKVQKFRMRE 548
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
221-572 |
2.92e-19 |
|
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: 89.00 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 221 LYI-YTSGTTGLPKAAMITHQRiWYGtglTFVSG-----LKADDVIYITLPFYHSAALligiHGCIVA---GATLALRTK 291
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSERS-WIE---SFVCNedlfnISGEDAILAPGPLSHSLFL----YGAISAlylGGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 292 FSASQFWDDCRKYNVTVIQYIGELLRYLCNSpqkpNDRDHKVRLAL--GNGLRGDVWRQFVKRFGDICIYEFYAATEGNi 369
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSELS- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 gFMNY-----ARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycvrvpkGEVGLLVCKITQLtpFNGYAGAKAQ 444
Cdd:cd17633 150 -FITYnfnqeSRPPNSVGRP-----------FPNVEIE----IRNADG-------GEIGKIFVKSEMV--FSGYVRGGFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 445 TEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GR 523
Cdd:cd17633 205 NP-----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG--IPDARfGE 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 308153494 524 IGMASIKMKenhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd17633 272 IAVALYSGD---KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
79-572 |
3.38e-19 |
|
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: 90.64 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 159 PELqaaveeilpslkkddvsiyyvsrtsntdgidsfLDKVDevstepiPEswrsevtfsTPALYIYTSGTTGLPKA---- 234
Cdd:cd05969 80 EEL---------------------------------YERTD-------PE---------DPTLLHYTSGTTGTPKGvlhv 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 235 --AMITHqriwYGTGlTFVSGLKADDVI-------YITLPFYHS-AALLIGIHGCIVAGatlalrtKFSASQFWDDCRKY 304
Cdd:cd05969 111 hdAMIFY----YFTG-KYVLDLHPDDIYwctadpgWVTGTVYGIwAPWLNGVTNVVYEG-------RFDAESWYGIIERV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 305 NVTVIQYIGELLRYLCNS---PQKPNDRDH-KVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATE-GNIGFMNYAR--- 376
Cdd:cd05969 179 KVTVWYTAPTAIRMLMKEgdeLARKYDLSSlRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSIMIANYPCmpi 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 377 KVGAVGR-VNYLQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVCKITQLTPFNGYAGakaqtEKKKLRDVFK 455
Cdd:cd05969 258 KPGSMGKpLPGVKAAVV----------------DENGN--ELPPGTKGILALKPGWPSMFRGIWN-----DEERYKNSFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 456 KGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADtvGLVDF--VQEVNVYGvhVPDHE-GRIGMASIKMK 532
Cdd:cd05969 315 DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES--ALMEHpaVAEAGVIG--KPDPLrGEIIKAFISLK 388
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 308153494 533 ENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd05969 389 EGFEPSdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
56-563 |
3.67e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.09 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 56 LRAFLEKARQTPHKPFLLFRD-ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK07514 5 LFDALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 NYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVsiyyvsRTSNTDGIDSFLDKVDEVST--EPIPeswRS 212
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV------ETLDADGTGSLLEAAAAAPDdfETVP---RG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 213 EvtfSTPALYIYTSGTTGLPKAAMITH----------QRIWygtgltfvsGLKADDVIYITLPFYHSAALLIGIHGCIVA 282
Cdd:PRK07514 155 A---DDLAAILYTSGTTGRSKGAMLSHgnllsnaltlVDYW---------RFTPDDVLIHALPIFHTHGLFVATNVALLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 283 GATLALRTKFSASQFWDDCRKynVTVIQ-----YIgellRYLcnspQKPN-DRDH--KVRLAL-GNG-LRGDVWRQFVKR 352
Cdd:PRK07514 223 GASMIFLPKFDPDAVLALMPR--ATVMMgvptfYT----RLL----QEPRlTREAaaHMRLFIsGSApLLAETHREFQER 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 353 FGDiCIYEFYAATEGNigfMN----Y--ARKVGAVG--------RVNylqkkiitydlikyDVEKDEPvrdengycvrVP 418
Cdd:PRK07514 293 TGH-AILERYGMTETN---MNtsnpYdgERRAGTVGfplpgvslRVT--------------DPETGAE----------LP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 419 KGEVGLLVCKitqlTP--FNGYAGAKAQTeKKKLRDvfkkgDLYFNSGDLLMVDHENfiYFHdRVGdtfRWK------GE 490
Cdd:PRK07514 345 PGEIGMIEVK----GPnvFKGYWRMPEKT-AEEFRA-----DGFFITGDLGKIDERG--YVH-IVG---RGKdliisgGY 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 491 NVATTEVADTVGLVDFVQEVNVYGVHVPDHeGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQD 563
Cdd:PRK07514 409 NVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-591 |
3.91e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.46 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 220 ALYIYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLAL------RTKF 292
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYnAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 293 SASQFWDDCRKYNVTVIQYIGELLRYLCnspQKPNDRD-HKVRLALGNG--LRGDVWRQFVKRFGdICIYEFYAATEGNI 369
Cdd:cd05944 85 LFDNFWKLVERYRITSLSTVPTVYAALL---QVPVNADiSSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 G----FMNYARKVGAVG-RVNYLQKKIITYDlikydvekdepvrDENGYCVRVPKGEVGLLVckITQLTPFNGYagakAQ 444
Cdd:cd05944 161 LvavnPPDGPKRPGSVGlRLPYARVRIKVLD-------------GVGRLLRDCAPDEVGEIC--VAGPGVFGGY----LY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 445 TEKKKLRDVfkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGR 523
Cdd:cd05944 222 TEGNKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVG--QPDaHAGE 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 524 IGMASIKMKENHEFDGKKLFQHIADYLPSYAR-PRFLRIQDTIEITGtfkhrkmtlVEEGFNPAVIKDA 591
Cdd:cd05944 297 LPVAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTA---------VGKVFKPALRADA 356
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
57-568 |
1.53e-18 |
|
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: 88.92 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTsntdgidsfldkvdevSTEPIpeswrseVTF 216
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESE----------------NLEPV-------SKS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 STPALYIYTSGTTGLPKAAMITHQR----IWyGTGLTFVSGLKADDVIYITLPFYHS-----AALLIGIHGCIVAGATLA 287
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEHRGvvnlVE-WANKVIYQGEHLRVALFASISFDASvteifASLLSGNTLYIVRKETVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 288 LRTKFSASqfwddCRKYNVTVIQYIGELLRYLcNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDIC-IYEFYAATE 366
Cdd:cd17655 216 DGQALTQY-----IRQNRITIIDLTPAHLKLL-DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 367 GNIGFMNYarkvgavgrvnylqkkiitydliKYDVEKDEPVR---------------DENGYCvrVPKGEVGLL------ 425
Cdd:cd17655 290 TTVDASIY-----------------------QYEPETDQQVSvpigkplgntriyilDQYGRP--QPVGVAGELyiggeg 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 426 VCKitqltpfnGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVD 505
Cdd:cd17655 345 VAR--------GYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 506 FVQEVNVygVHVPDHEGRIGMASIKMKENhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd17655 417 DIKEAVV--IARKDEQGQNYLCAYIVSEK-ELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-557 |
2.10e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 87.96 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVs 158
Cdd:cd05973 1 LTFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 159 pelqaaveeilpslkkddvsiyyvsrtsNTDGidsfLDKVDevstepipeswrsevtfSTPALYIYTSGTTGLPKAAMIT 238
Cdd:cd05973 79 ----------------------------DAAN----RHKLD-----------------SDPFVMMFTSGTTGLPKGVPVP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 239 HQRIW-YGTGLTFVSGLKADDViyitlpFYHSA------ALLIGIHGCIVAG-ATLALRTKFSASQFWDDCRKYNVTVIQ 310
Cdd:cd05973 110 LRALAaFGAYLRDAVDLRPEDS------FWNAAdpgwayGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 311 YIGELLRYL----CNSPQKPNDRDHKVRLAlGNGLRGDVWRQFVKRFGdICIYEFYAATEGNIGFMNY-----ARKVGAV 381
Cdd:cd05973 184 GSPTAYRLLmaagAEVPARPKGRLRRVSSA-GEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHhalehPVHAGSA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 382 GRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKI--TQLTPFNGYAGAKAQTekkklrdvfKKGDl 459
Cdd:cd05973 262 GRA-----------MPGWRVA----VLDDDG--DELGPGEPGRLAIDIanSPLMWFRGYQLPDTPA---------IDGG- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 460 YFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFD 538
Cdd:cd05973 315 YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG--VPDPErTEVVKAFVVLRGGHEGT 392
|
490 500
....*....|....*....|..
gi 308153494 539 ---GKKLFQHIADYLPSYARPR 557
Cdd:cd05973 393 palADELQLHVKKRLSAHAYPR 414
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
55-519 |
2.43e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.50 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 55 ILRAFlekaRQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAyVWLWLGlvkLGCAMACl 134
Cdd:PRK06188 18 LVSAL----KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPE-VLMAIG---AAQLAGL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 nyniRAKSLL-------HCFQC--CGAKVLLVSP----ELQAAVEEILPSLKKddvsIYYVSRTSntDGIDsFLDKVDEV 201
Cdd:PRK06188 88 ----RRTALHplgslddHAYVLedAGISTLIVDPapfvERALALLARVPSLKH----VLTLGPVP--DGVD-LLAAAAKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 202 STEPIpeswRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWygtglTFVSGLKAD-----DVIY-ITLPFYHSAALLig 275
Cdd:PRK06188 157 GPAPL----VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIA-----TMAQIQLAEwewpaDPRFlMCTPLSHAGGAF-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 276 IHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQkPNDRD--------------HKVRLALGngl 341
Cdd:PRK06188 226 FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPD-LRTRDlssletvyygaspmSPVRLAEA--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 342 rgdvwrqfVKRFGDIcIYEFYAATEgnigfmnyarkvgAVGRVNYLQKKiitydlikyDVEKDEPVR------------- 408
Cdd:PRK06188 302 --------IERFGPI-FAQYYGQTE-------------APMVITYLRKR---------DHDPDDPKRltscgrptpglrv 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 409 ---DENGYcvRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTF 485
Cdd:PRK06188 351 allDEDGR--EVAQGEVGEICVRGPLV--MDGYWNRPEETAE-----AFRDGWLH--TGDVAREDEDGFYYIVDRKKDMI 419
|
490 500 510
....*....|....*....|....*....|....
gi 308153494 486 RWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD 519
Cdd:PRK06188 420 VTGGFNVFPREVEDVLAEHPAVAQVAVIG--VPD 451
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
72-514 |
2.55e-18 |
|
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: 88.67 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 72 LLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCG 151
Cdd:cd17632 61 LLPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 152 AKVLLVSPE-LQAAVEEIL--PSLKKDDVSIYYVSRTSNTDGIDSFLDK--------------VDEVSTEPIPESWRSEV 214
Cdd:cd17632 141 PRLLAVSAEhLDLAVEAVLegGTPPRLVVFDHRPEVDAHRAALESARERlaavgipvttltliAVRGRDLPPAPLFRPEP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 215 TFSTPALYIYTSGTTGLPKAAMITHQRI---WygtgLTFVSGLKADDVIYITL---PFYHSAALLIgIHGCIVAGATLAL 288
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVatfW----LKVSSIQDIRPPASITLnfmPMSHIAGRIS-LYGTLARGGTAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 289 RTKFSASQFWDD---CRKYNVTVIQYIGELL--RYL------CNSPQKPNDRDHKVRLALGNGLRG-------------- 343
Cdd:cd17632 296 AAASDMSTLFDDlalVRPTELFLVPRVCDMLfqRYQaeldrrSVAGADAETLAERVKAELRERVLGgrllaavcgsapls 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 344 DVWRQFVKRFGDICIYEFYAATEGnigfmnyarkvGAVGRVNYLQK-KIITYDLIkydvekDEPvrdENGYCVR---VPK 419
Cdd:cd17632 376 AEMKAFMESLLDLDLHDGYGSTEA-----------GAVILDGVIVRpPVLDYKLV------DVP---ELGYFRTdrpHPR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 420 GEvgLLVcKITQLTPfnGYAGAKAQTEkkklrDVFKKgDLYFNSGDLLM-VDHENFIYFhDRVGDTFRW-KGENVATTEV 497
Cdd:cd17632 436 GE--LLV-KTDTLFP--GYYKRPEVTA-----EVFDE-DGFYRTGDVMAeLGPDRLVYV-DRRNNVLKLsQGEFVTVARL 503
|
490
....*....|....*..
gi 308153494 498 ADTVGLVDFVQEVNVYG 514
Cdd:cd17632 504 EAVFAASPLVRQIFVYG 520
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
59-557 |
3.63e-18 |
|
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: 87.74 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd12118 9 FLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQaaVEEILPSLKKDDVSIYyvsrtsntdgidsfldKVDEvsTEPIpeswrsevtfs 217
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREFE--YEDLLAEGDPDFEWIP----------------PADE--WDPI----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 tpALYiYTSGTTGLPKAAMITHQRIW---YGTGLTFvsGLKADDVIYITLPFYHSA--------ALLIGIHGCivagatl 286
Cdd:cd12118 137 --ALN-YTSGTTGRPKGVVYHHRGAYlnaLANILEW--EMKQHPVYLWTLPMFHCNgwcfpwtvAAVGGTNVC------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 287 aLRtKFSASQFWDDCRKYNVTviQYIGE--LLRYLCNSPqkPNDR---DHKVRLALGNGLRGDVWRQFVKRFGdICIYEF 361
Cdd:cd12118 205 -LR-KVDAKAIYDLIEKHKVT--HFCGAptVLNMLANAP--PSDArplPHRVHVMTAGAPPPAAVLAKMEELG-FDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 362 YAATE--GNIGFMNY------------ARKVGAVGrVNYLQKKIItyDLIKYDVEKDEPvRDenGYCVrvpkGEV---GL 424
Cdd:cd12118 278 YGLTEtyGPATVCAWkpewdelpteerARLKARQG-VRYVGLEEV--DVLDPETMKPVP-RD--GKTI----GEIvfrGN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 425 LVCKitqltpfnGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLV 504
Cdd:cd12118 348 IVMK--------GYLKNPEATAE-----AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKH 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 308153494 505 DFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:cd12118 413 PAVLEAAVVA--RPDeKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPK 464
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
78-574 |
9.14e-18 |
|
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: 86.11 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLwlglvklgcAMACLnyniraksllhcfqCCGAkvlLV 157
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIA---------DLAIL--------------AIGA---VP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 SPelqaaveeILPSLKKDDVSiyYVSRTSNTDGIdsFLDKVDEVSTepipeswrsevtfstpalYIYTSGTTGLPKAAMI 237
Cdd:cd05907 58 VP--------IYPTSSAEQIA--YILNDSEAKAL--FVEDPDDLAT------------------IIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 238 THQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATL--ALRTK--------------FSASQFWDd 300
Cdd:cd05907 108 SHRNILSNAlALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIyfASSAEtllddlsevrptvfLAVPRVWE- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 301 cRKYNVTVIQYIGELLRYLcnspqkpndrdhkVRLALGNGLR----G------DVWRQFVKrFGdICIYEFYAATE-GNI 369
Cdd:cd05907 187 -KVYAAIKVKAVPGLKRKL-------------FDLAVGGRLRfaasGgaplpaELLHFFRA-LG-IPVYEGYGLTEtSAV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 GFMNY--ARKVGAVGRVnylqkkiitydlikydvekdepvrdenGYCVRVPKGEVGLLVCKITQLtpFNGYAGAKAQTek 447
Cdd:cd05907 251 VTLNPpgDNRIGTVGKP---------------------------LPGVEVRIADDGEILVRGPNV--MLGYYKNPEAT-- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 448 kklRDVFKKgDLYFNSGDLLMVDHENFIYFHDRVGDTFRW-KGENVATTEVADTVGLVDFVQEVNVYGVH--------VP 518
Cdd:cd05907 300 ---AEALDA-DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIGDGrpflvaliVP 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 519 DHEGRIGMASIKMKENHEFDG----KKLFQHIADY-------LPSYARPRFLRI------QDTIEITGTFKHR 574
Cdd:cd05907 376 DPEALEAWAEEHGIAYTDVAElaanPAVRAEIEAAveaanarLSRYEQIKKFLLlpepftIENGELTPTLKLK 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-370 |
9.35e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMA 132
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 133 CLNYNIRAKSLLHCFQCCGAKVLLVSPEL--QAAVEEILPSLKKDDVsiyyvsrtsntdgiDSFLDKVDEVSTEPI--PE 208
Cdd:PRK12467 591 PLDPEYPQDRLAYMLDDSGVRLLLTQSHLlaQLPVPAGLRSLCLDEP--------------ADLLCGYSGHNPEVAldPD 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 209 SWrsevtfstpALYIYTSGTTGLPKAAMITHQRIW-YGTGLTFVSGLKADDVIYITLPFyhsAALLIG--IHGCIVAGAT 285
Cdd:PRK12467 657 NL---------AYVIYTSGSTGQPKGVAISHGALAnYVCVIAERLQLAADDSMLMVSTF---AFDLGVteLFGALASGAT 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 286 LALRTK---FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQfVKRFGDIC-IYEF 361
Cdd:PRK12467 725 LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLAR-VRALGPGArLINH 803
|
....*....
gi 308153494 362 YAATEGNIG 370
Cdd:PRK12467 804 YGPTETTVG 812
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
77-579 |
9.72e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 85.95 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 vspelqaaveeilpslkkddvsiyyvsrtsnTDGIDSfldkvdevstepipeswrsevtfstPALYIYTSGTTGLPKAAM 236
Cdd:cd05971 84 -------------------------------TDGSDD-------------------------PALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 237 ITHqRIWYG--TGLTFVSGL--KADDVIYITLPFYHSAALLIGI-----HGCIVagatLALR-TKFSASQFWDDCRKYNV 306
Cdd:cd05971 108 HAH-RVLLGhlPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLlpslyFGVPV----LAHRmTKFDPKAALDLMSRYGV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 307 TVIQYIGELLRYLCNSPQKPNDRDHKVR-LALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMN----YARKVGAV 381
Cdd:cd05971 183 TTAFLPPTALKMMRQQGEQLKHAQVKLRaIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNcsalFPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 382 GRvnylqkkiityDLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKklrdvfKKGDlYF 461
Cdd:cd05971 263 GK-----------PIPGHRVA----IVDDNG--TPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKK------MAGD-WL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 462 NSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTvgLVDFVQEVNVYGVHVPDHE-GRIGMASIKMKENHEFD-- 538
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEC--LLKHPAVLMAAVVGIPDPIrGEIVKAFVVLNPGETPSda 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 308153494 539 -GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLV 579
Cdd:cd05971 397 lAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
51-522 |
1.20e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 86.34 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFL-EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGC 129
Cdd:PRK06164 7 PRADTLASLLdAHARARPDAVALIDEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 130 AMACLNYNIRAKSLLHCFQCCGAKVLLVSP-----ELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEV--- 201
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFalp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 202 STEPIPESWRSEVTFSTPALYIYTSGTTGLPK------AAMITHQRIwygtgLTFVSGLKADDVIYITLPF---YHSAAL 272
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSGPKlvlhrqATLLRHARA-----IARAYGYDPGAVLLAALPFcgvFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 273 LIGIHGcivaGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRylcnspqkpndrdhkvRLALGNGLRGDVWRqfVKR 352
Cdd:PRK06164 241 LGALAG----GAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLR----------------RILDTAGERADFPS--ARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 353 FGdiciyeFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIkYDVEKDEPVRDENGYC-------VRV-------- 417
Cdd:PRK06164 299 FG------FASFAPALGELAALARARGVPLTGLYGSSEVQALVAL-QPATDPVSVRIEGGGRpaspearVRArdpqdgal 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 418 -PKGEVGLLvcKITQLTPFNGY-----AGAKAQTEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGEN 491
Cdd:PRK06164 372 lPDGESGEI--EIRAPSLMRGYldnpdATARALTD-----------DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFL 438
|
490 500 510
....*....|....*....|....*....|.
gi 308153494 492 VATTEVADTVGLVDFVQEVNVYGVhvpDHEG 522
Cdd:PRK06164 439 VNPAEIEHALEALPGVAAAQVVGA---TRDG 466
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
59-568 |
1.88e-17 |
|
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: 85.47 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPELQ--AAVEEILPSLkkddvsiyyvsrtsntdgIDSFLDkVDEVSTEPIPESWRSEvtf 216
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAgeLAVELVAVTL------------------LDQPGA-AAGADAEPDPALDADD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 stPALYIYTSGTTGLPKAAMITHQRI-----WygtgLTFVSGLKADD--VIYITLPFYHSAAlliGIHGCIVAGATLALR 289
Cdd:cd17651 138 --LAYVIYTSGSTGRPKGVVMPHRSLanlvaW----QARASSLGPGArtLQFAGLGFDVSVQ---EIFSTLCAGATLVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 290 T---KFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVW---RQFVKRFGDICIYEFYA 363
Cdd:cd17651 209 PeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTedlREFCAGLPGLRLHNHYG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 364 ATEGNI-------GFMNYARKVGAVGRVnylqkkIITYDLIKYDvEKDEPvrdengycvrVPKGEVGLLVCKITQLTPfn 436
Cdd:cd17651 289 PTETHVvtalslpGDPAAWPAPPPIGRP------IDNTRVYVLD-AALRP----------VPPGVPGELYIGGAGLAR-- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 437 GYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVH 516
Cdd:cd17651 350 GYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARE 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 308153494 517 VPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd17651 430 DRPGEKRL-VAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLT 480
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
75-308 |
1.99e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 85.72 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKV 154
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 155 LLVSPEL-QAAVEEILPSLKK-----DDVSiyyvsrtsNTDGIDSFLDKVDEVSTEPIPESWRSEvtfsTPALYIYTSGT 228
Cdd:PRK04319 149 LITTPALlERKPADDLPSLKHvllvgEDVE--------EGPGTLDFNALMEQASDEFDIEWTDRE----DGAILHYTSGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 229 TGLPKA------AMITHqriwYGTGLtFVSGLKADDVIYITL-P----------FyhsAALLIGIHGCIVAGatlalrtK 291
Cdd:PRK04319 217 TGKPKGvlhvhnAMLQH----YQTGK-YVLDLHEDDVYWCTAdPgwvtgtsygiF---APWLNGATNVIDGG-------R 281
|
250
....*....|....*..
gi 308153494 292 FSASQFWDDCRKYNVTV 308
Cdd:PRK04319 282 FSPERWYRILEDYKVTV 298
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
63-568 |
8.74e-17 |
|
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: 83.07 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLVSPelqaaveeilpslkkDDVsiYYVsrtsntdgidsfldkvdevstepipeswrsevtfstpaly 222
Cdd:cd05945 80 IREILDAAKPALLIADG---------------DDN--AYI---------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITHQRIwygtgLTFVSG------LKADDVIYITLPFyhSAAL-LIGIHGCIVAGATLALRTKfsas 295
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNL-----VSFTNWmlsdfpLGPGDVFLNQAPF--SFDLsVMDLYPALASGATLVPVPR---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 296 qfwddcrkynvTVIQYIGELLRYLcnspqkpndRDHKV----------RLALGNG---------LR-----GDVW----- 346
Cdd:cd05945 172 -----------DATADPKQLFRFL---------AEHGItvwvstpsfaAMCLLSPtftpeslpsLRhflfcGEVLphkta 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 347 RQFVKRFGDICIYEFYAATEGNIgfmnyarkvgAVGRVNYLQKKIITYD-----LIKYDVEKDepVRDENGYCvrVPKGE 421
Cdd:cd05945 232 RALQQRFPDARIYNTYGPTEATV----------AVTYIEVTPEVLDGYDrlpigYAKPGAKLV--ILDEDGRP--VPPGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 422 VGLLVckITQLTPFNGYAGAKAQTEKKKLRDvfkKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTV 501
Cdd:cd05945 298 KGELV--ISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAAL 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 502 GLVDFVQEVNVygVHVPDHEGRIGM-ASIKMKENHEF-DGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd05945 373 RQVPGVKEAVV--VPKYKGEKVTELiAFVVPKPGAEAgLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
55-557 |
1.06e-16 |
|
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: 83.69 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 55 ILRAFLEK-ARQTPHKPFLLFRDE-----TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLG 128
Cdd:cd05968 62 IVEQLLDKwLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 129 CAMACLNYNIRAKSLLHCFQCCGAKVLLVS-------------PELQAAVEEiLPSLKKddvsIYYVSRTSNTDGIDSFL 195
Cdd:cd05968 141 GIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQ-CPTVEK----VVVVRHLGNDFTPAKGR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 196 DK-VDEVSTEPIPESWRSEVtfSTPALYIYTSGTTGLPKAAMITHQ--RIWYGTGLTFVSGLKADDVIYitlpFYHSAAL 272
Cdd:cd05968 216 DLsYDEEKETAGDGAERTES--EDPLMIIYTSGTTGKPKGTVHVHAgfPLKAAQDMYFQFDLKPGDLLT----WFTDLGW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 273 LIG---IHGCIVAGATLALRTKF----SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHK--VRLALGNG--L 341
Cdd:cd05968 290 MMGpwlIFGGLILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLssLRVLGSTGepW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 342 RGDVWRQFVKRFGDiciyefyaateGNIGFMNYARKVGAVGRV--NYLQKKI--ITYDLIKYDVEKDepVRDENGYCVRv 417
Cdd:cd05968 370 NPEPWNWLFETVGK-----------GRNPIINYSGGTEISGGIlgNVLIKPIkpSSFNGPVPGMKAD--VLDESGKPAR- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 418 pkGEVGLLVCkitqLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEV 497
Cdd:cd05968 436 --PEVGELVL----LAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEI 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308153494 498 ADTVGLVDFVQEVNVYGvhVPDH-EGRIGMASIKMKENHEFDG---KKLFQHIADYLPSYARPR 557
Cdd:cd05968 510 ESVLNAHPAVLESAAIG--VPHPvKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPE 571
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
51-286 |
1.23e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.56 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFLEKARQTPHKPFLLFRD------ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGL 124
Cdd:PRK12582 47 YPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLD-LGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 125 VKLGCAMACL--NYNI----RAKsLLHCFQCCGAKVLLVspELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKV 198
Cdd:PRK12582 126 MQAGVPAAPVspAYSLmshdHAK-LKHLFDLVKPRVVFA--QSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 199 DEVSTEPIPESwRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIwyGTGLTFVSGLKADD------VIYITLPFYHSAAL 272
Cdd:PRK12582 203 ATPPTAAVAAA-IAAITPDTVAKYLFTSGSTGMPKAVINTQRMM--CANIAMQEQLRPREpdppppVSLDWMPWNHTMGG 279
|
250
....*....|....
gi 308153494 273 LIGIHGCIVAGATL 286
Cdd:PRK12582 280 NANFNGLLWGGGTL 293
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
63-581 |
1.41e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 82.87 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLfrDET---LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIR 139
Cdd:PRK06087 33 ARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 140 AKSLLHCFQCCGAKVLL-------VSPELQA-AVEEILPSLKKDdVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESwr 211
Cdd:PRK06087 110 EAELVWVLNKCQAKMFFaptlfkqTRPVDLIlPLQNQLPQLQQI-VGVDKLAPATSSLSLSQIIADYEPLTTAITTHG-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 212 SEVtfstpALYIYTSGTTGLPKAAMITHQRI-----WYGTGLtfvsGLKADDVIYITLPFYHSAALLIGIHGCIVAGATL 286
Cdd:PRK06087 187 DEL-----AAVLFTSGTEGLPKGVMLTHNNIlaserAYCARL----NLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 287 ALRTKFSASQFWDDCRKYNVT----VIQYIGELlryLCNSPQKPNDRDhKVRLALGNG--LRGDVWRQFVKRfgDICIYE 360
Cdd:PRK06087 258 VLLDIFTPDACLALLEQQRCTcmlgATPFIYDL---LNLLEKQPADLS-ALRFFLCGGttIPKKVARECQQR--GIKLLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 361 FYAATEGNIGFM-----NYARKVGAVGR-VNYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLtp 434
Cdd:PRK06087 332 VYGSTESSPHAVvnlddPLSRFMHTDGYaAAGVEIKVV-----------DEARKT-------LPPGCEGEEASRGPNV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 435 FNGYAGAKAQTEkKKLRDvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYG 514
Cdd:PRK06087 392 FMGYLDEPELTA-RALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 515 vhVPDHE--GRIGMASIKMKENHEFDGKKLFQHIAD-YLPSYARPRFLRIQDTIEITGTFKHRKMTLVEE 581
Cdd:PRK06087 466 --MPDERlgERSCAYVVLKAPHHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
217-572 |
1.70e-16 |
|
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: 81.15 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 STPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVSGLK--ADDVIYITLPFYHSAALL----IGIHG--CIVAGATLAL 288
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNwvVGDVTYLPLPATHIGGLWwiltCLIHGglCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 289 RTKFSASQFwddcrkYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLR---GDVwrQFVKRFGDICIYEFYAAT 365
Cdd:cd17635 81 KSLFKILTT------NAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRaiaADV--RFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 366 E-GNIGFMNYAR---KVGAVGRvnylqkkiiTYDLIkyDVEkdepVRDENGycVRVPKGEVGLLVCKitqlTPFN--GYA 439
Cdd:cd17635 153 EtGTALCLPTDDdsiEINAVGR---------PYPGV--DVY----LAATDG--IAGPSASFGTIWIK----SPANmlGYW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 440 GAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYgvHVPD 519
Cdd:cd17635 212 NNPERTA-----EVLIDG--WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISD 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 520 HE--GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd17635 283 EEfgELVGLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGK 337
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
63-307 |
1.79e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 82.63 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDE--TLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRA 140
Cdd:PRK05852 26 ATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 141 KSLLHCFQCCGAKVLLVSPElqAAVEEILPSLKKDDVSiyyVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPA 220
Cdd:PRK05852 105 AEQRVRSQAAGARVVLIDAD--GPHDRAEPTTRWWPLT---VNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 221 LYIYTSGTTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLAL--RTKFSASQF 297
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVrAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRFSAHTF 259
|
250
....*....|
gi 308153494 298 WDDCRKYNVT 307
Cdd:PRK05852 260 WDDIKAVGAT 269
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
53-286 |
2.06e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 82.55 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRDETL--TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 131 MACLNYNIRAKSLLHCFQCCGAKVLL----------------VSPELQAAV-----EEILPSLKkddvSIYYV--SRTSN 187
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIaadgfkdsdyvamlyeLAPELATCEpgqlqSARLPELR----RVIFLgdEKHPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 188 TDGIDSFLDKVDEVSTEPIPESwRSEVTFSTPALYIYTSGTTGLPKAAMITHQRI-----WYGTGLtfvsGLKADDVIYI 262
Cdd:PRK08315 171 MLNFDELLALGRAVDDAELAAR-QATLDPDDPINIQYTSGTTGFPKGATLTHRNIlnngyFIGEAM----KLTEEDRLCI 245
|
250 260
....*....|....*....|....
gi 308153494 263 TLPFYHSAALLIGIHGCIVAGATL 286
Cdd:PRK08315 246 PVPLYHCFGMVLGNLACVTHGATM 269
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-578 |
3.55e-16 |
|
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: 80.40 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 224 YTSGTTGLPKAAMITHQRIW---YGTGLTFvsGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTK-FSASQFWD 299
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnngYFIGERL--GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 300 DCRKYNVTVIQ-----YIGELlrylcNSPQKPNDRDHKVR--LALGNGLRGDVWRQFVKRFG--DICIYefYAATEGN-I 369
Cdd:cd05917 87 AIEKEKCTALHgvptmFIAEL-----EHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNmkDVTIA--YGMTETSpV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 GFMNYA-----RKVGAVGRV-NYLQKKIItydlikydvekdepvrDENGYCVrVPKGEVGLLVCKITQLTpfNGYAGAKA 443
Cdd:cd05917 160 STQTRTddsieKRVNTVGRImPHTEAKIV----------------DPEGGIV-PPVGVPGELCIRGYSVM--KGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 444 QTEKKKLRDVFKKgdlyfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-G 522
Cdd:cd05917 221 KTAEAIDGDGWLH------TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VPDERyG 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 308153494 523 RIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd05917 293 EEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-556 |
5.45e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.31 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK12316 510 QRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSLKKDDVSIYyvsrtsntDGIDSFLDKvdeVSTEPiPEswr 211
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLS----QSHLGRKLPLAAGVQVLDL--------DRPAAWLEG---YSEEN-PG--- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 212 SEVTFSTPALYIYTSGTTGLPKAAMITHQRI-----WYGTGLtfvsGLKADDVIYITLPFYHSAALLIgIHGCIVAGATL 286
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTGKPKGAGNRHRALsnrlcWMQQAY----GLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGARL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 287 ALRTK---FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYA 363
Cdd:PRK12316 725 VVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYG 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 364 ATEGNIGFMNYA-RKVGA----VGR-VNYLQKKIITYDLikydvekdEPvrdengycvrVPKGEVGLLVCKITQLTpfNG 437
Cdd:PRK12316 805 PTEAAIDVTHWTcVEEGGdsvpIGRpIANLACYILDANL--------EP----------VPVGVLGELYLAGRGLA--RG 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 438 YAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhv 517
Cdd:PRK12316 865 YHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-- 942
|
490 500 510
....*....|....*....|....*....|....*....
gi 308153494 518 pdhEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARP 556
Cdd:PRK12316 943 ---DGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVP 978
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
63-291 |
6.71e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.30 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLglvklgcamACLNyniraks 142
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYL---------ALLQ------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 llhcfqcCGAKVLLVSPELQAA-VEEILPSLKKDdvSIYYVSRTSNTDGIDSFLdkVDEVSTEPiPESWRSEvtfsTPAL 221
Cdd:PRK09029 76 -------CGARVLPLNPQLPQPlLEELLPSLTLD--FALVLEGENTFSALTSLH--LQLVEGAH-AVAWQPQ----RLAT 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308153494 222 YIYTSGTTGLPKAAMITHQriwygTGLTFVSGL------KADDVIYITLPFYHSAALLIgIHGCIVAGATLALRTK 291
Cdd:PRK09029 140 MTLTSGSTGLPKAAVHTAQ-----AHLASAEGVlslmpfTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDK 209
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
59-334 |
1.30e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 79.99 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PRK08162 23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALA-RRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGidsflDKVDEVSTEPIPESWRSEVTFS 217
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGG-----RFIGALDYEAFLASGDPDFAWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 218 TP-----ALYI-YTSGTTGLPKaAMITHQRiwyGTGLTFVSGLKADDV----IYI-TLPFYH--------SAALLIGIHG 278
Cdd:PRK08162 177 LPadewdAIALnYTSGTTGNPK-GVVYHHR---GAYLNALSNILAWGMpkhpVYLwTLPMFHcngwcfpwTVAARAGTNV 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 279 CivagatlaLRtKFSASQFWDDCRKYNVTviQYIGE--LLRYLCNSPQKPND-RDHKVR 334
Cdd:PRK08162 253 C--------LR-KVDPKLIFDLIREHGVT--HYCGApiVLSALINAPAEWRAgIDHPVH 300
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-369 |
1.34e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.98 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGA 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 131 MACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDS-FLDKVDEVSTEPIPES 209
Cdd:PRK12467 1651 YVPLDPEYPRERLAYMIEDSGIELLLT----QSHLQARLPL----------------PDGLRSlVLDQEDDWLEGYSDSN 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 210 WRSEVTFSTPALYIYTSGTTGLPKAAMITHQ---RIWYGTGLTFvsGLKADDVIYITLPFYHSAALLiGIHGCIVAGATL 286
Cdd:PRK12467 1711 PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGalvNRLCATQEAY--QLSAADVVLQFTSFAFDVSVW-ELFWPLINGARL 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 287 ALR---TKFSASQFWDDCRKYNVTVIQYIGELLR-YLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFY 362
Cdd:PRK12467 1788 VIAppgAHRDPEQLIQLIERQQVTTLHFVPSMLQqLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLY 1867
|
....*..
gi 308153494 363 AATEGNI 369
Cdd:PRK12467 1868 GPTETAV 1874
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
57-562 |
1.61e-15 |
|
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: 79.28 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMaclny 136
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 niraksllhcfqccgakvllvspelqAAVEEILPSLKKDdvsiyYVSRTSNTDgIDSFLDKVDEVstepipeswrsevtf 216
Cdd:cd17653 75 --------------------------VPLDAKLPSARIQ-----AILRTSGAT-LLLTTDSPDDL--------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 stpALYIYTSGTTGLPKAAMITHQRI-----WYGTGLTFVSGLKADDVIYITlpFYHSAALligIHGCIVAGATLALRTk 291
Cdd:cd17653 108 ---AYIIFTSGSTGIPKGVMVPHRGVlnyvsQPPARLDVGPGSRVAQVLSIA--FDACIGE---IFSTLCNGGTLVLAD- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 292 fSASQFWDDCRKYNVTVIQyiGELLRYLcnspqKPNDRDHKVRLALGN-----GLRgDVWRqfvkrfGDICIYEFYAATE 366
Cdd:cd17653 179 -PSDPFAHVARTVDALMST--PSILSTL-----SPQDFPNLKTIFLGGeavppSLL-DRWS------PGRRLYNAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 367 GNIGfmnyarkvgavgrVNYLQKKIITYDLIKYdvekdePVRdeNGYCV-------RVPKGEVGLLVCKITQLTPfnGYA 439
Cdd:cd17653 244 CTIS-------------STMTELLPGQPVTIGK------PIP--NSTCYildadlqPVPEGVVGEICISGVQVAR--GYL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 440 GAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLvdfvQEVNVYGVHVPD 519
Cdd:cd17653 301 GNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ----SQPEVTQAAAIV 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 308153494 520 HEGRIGM----ASIkmkenhefDGKKLFQHIADYLPSYARP-RFLRIQ 562
Cdd:cd17653 377 VNGRLVAfvtpETV--------DVDGLRSELAKHLPSYAVPdRIIALD 416
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
67-369 |
1.65e-15 |
|
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: 79.24 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAA-GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSpelqaaveeiLPSLKKDDvsiyyvsrtsntDGIDSFLDKVDEVSTEPIPESwrSEVTFSTPALYIYTS 226
Cdd:cd12114 80 LADAGARLVLTD----------GPDAQLDV------------AVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 227 GTTGLPKAAMITHQRIWyGTGLTFVS--GLKADDVIYITLPFYHSAALLiGIHGCIVAGATLAL----RTKfSASQFWDD 300
Cdd:cd12114 136 GSTGTPKGVMISHRAAL-NTILDINRrfAVGPDDRVLALSSLSFDLSVY-DIFGALSAGATLVLpdeaRRR-DPAHWAEL 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 301 CRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALgngLRGDvW------RQFVKRFGDICIYEFYAATEGNI 369
Cdd:cd12114 213 IERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVL---LSGD-WipldlpARLRALAPDARLISLGGATEASI 283
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
63-288 |
2.26e-15 |
|
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: 79.20 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLF------RDETLTYAQVDRRSNQVARALHDHLglRQGDCVALLMGNEPAYVwlwLGLvkLGCAMACL-- 134
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFV---AAF--LGCLYAGAia 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 ------NYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILpslkkddvsiyyvsRTSNTDGIDSFLDkVDEVSTEPiPE 208
Cdd:cd05931 76 vplpppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFA--------------ASRPAAGTPRLLV-VDLLPDTS-AA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 209 SWR-SEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVS-GLKADDVIYITLPFYHSAALLIGIHGCIVAGATL 286
Cdd:cd05931 140 DWPpPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAyGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
..
gi 308153494 287 AL 288
Cdd:cd05931 220 VL 221
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
75-557 |
2.80e-15 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 78.70 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQccgakv 154
Cdd:cd05923 25 RGLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIE------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 155 llvSPELQAAV-EEILPSLKKDDVSIYYVSRTSNTDGidsflDKVDEVSTEPIPESWRSEvtfSTPALYIYTSGTTGLPK 233
Cdd:cd05923 98 ---RGEMTAAViAVDAQVMDAIFQSGVRVLALSDLVG-----LGEPESAGPLIEDPPREP---EQPAFVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 AAMITHQ----RIWYgtgLTFVSGLK--ADDVIYITLPFYHSaallIGIHGCIVA----GATLALRTKFSASQFWDDCRK 303
Cdd:cd05923 167 GAVIPQRaaesRVLF---MSTQAGLRhgRHNVVLGLMPLYHV----IGFFAVLVAalalDGTYVVVEEFDPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 304 YNVT----VIQYIGELLRYLCNSPQKPNDRDHkvrLALGNGLRGDVWRQFVKRFGDICIYEFYAATEG-NIGFMNYARKv 378
Cdd:cd05923 240 ERVTslfaTPTHLDALAAAAEFAGLKLSSLRH---VTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAmNSLYMRDART- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 379 GAVGRVNYLQKKIItydlikydvekdepVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGaKAQTEKKKLRDVfkkgd 458
Cdd:cd05923 316 GTEMRPGFFSEVRI--------------VRIGGSPDEALANGEEGELIVAAAADAAFTGYLN-QPEATAKKLQDG----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 459 lYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENhEF 537
Cdd:cd05923 376 -WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIG--VADERwGQSVTACVVPREG-TL 451
|
490 500
....*....|....*....|.
gi 308153494 538 DGKKLFQH-IADYLPSYARPR 557
Cdd:cd05923 452 SADELDQFcRASELADFKRPR 472
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
52-557 |
3.26e-15 |
|
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: 78.72 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 52 ARTILRAFLEKARQTPHKpfLLFRD----ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKL 127
Cdd:cd17642 16 AGEQLHKAMKRYASVPGT--IAFTDahtgVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 128 GCAMACLN--YNIRakSLLHCFQCCGAKVLLVSpelQAAVEEILPSLKKDDVSIYYVSRTSNTD-----GIDSFLDKVDE 200
Cdd:cd17642 93 GVGVAPTNdiYNER--ELDHSLNISKPTIVFCS---KKGLQKVLNVQKKLKIIKTIIILDSKEDykgyqCLYTFITQNLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 201 VSTEP---IPESWRSEvtfSTPALYIYTSGTTGLPKAAMITHQ----RIWYGTGLTFVSGLKADDVIYITLPFYHSAALL 273
Cdd:cd17642 168 PGFNEydfKPPSFDRD---EQVALIMNSSGSTGLPKGVQLTHKnivaRFSHARDPIFGNQIIPDTAILTVIPFHHGFGMF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 274 IGIhGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSP-QKPNDRDHKVRLALGNG-LRGDVWRQFVK 351
Cdd:cd17642 245 TTL-GYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 352 RFGDICIYEFYAATEGNIGFM---NYARKVGAVGRVnylqKKIITYDLIKYDVEKDEPVRDENGYCVRvpkgevGLLVCK 428
Cdd:cd17642 324 RFKLPGIRQGYGLTETTSAILitpEGDDKPGAVGKV----VPFFYAKVVDLDTGKTLGPNERGELCVK------GPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 429 itqltpfnGYAGAKAQTekKKLRDvfKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQ 508
Cdd:cd17642 394 --------GYVNNPEAT--KALID--KDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 308153494 509 EVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 557
Cdd:cd17642 460 DAGVAG--IPDEDaGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
59-561 |
5.17e-15 |
|
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: 77.70 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVsiyyvsrtsntdGIDSFLDKVDEVSTEPipeswrsevtfST 218
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDE------------ALAAPPATPPLVPPRP-----------DN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 219 PALYIYTSGTTGLPKAAMITHQRI-----W----YGTGLTFVSGLKA----DDVIY-ITLPFYHSAALLI---GIHGciV 281
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGIvnrllWmqdeYPLGPGDRVLQKTplsfDVSVWeLFWPLVAGARLVVarpGGHR--D 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 282 AGATLALrtkfsasqfwddCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICIYEF 361
Cdd:cd17646 218 PAYLAAL------------IREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG-AELHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 362 YAATEGNIGfmnyarkvgavgrvnylqkkiITYDliKYDVEKDEP--------------VRDENGYcvRVPKGEVGLLVC 427
Cdd:cd17646 285 YGPTEAAID---------------------VTHW--PVRGPAETPsvpigrpvpntrlyVLDDALR--PVPVGVPGELYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 428 KITQLTpfNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFV 507
Cdd:cd17646 340 GGVQLA--RGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 508 QEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARP-RFLRI 561
Cdd:cd17646 418 THAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERLPEYMVPaAFVVL 472
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
63-575 |
1.33e-14 |
|
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: 76.77 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDET-----LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd05970 27 AKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPE--LQAAVEEILPSLKKDDVSIYYvsRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVT 215
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWV--GDPVPEGWIDFRKLIKNASPDFERPTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 216 FSTPALYIYTSGTTGLPKaaMITHQRIW-YGTGLT--FVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLAL--RT 290
Cdd:cd05970 184 GEDILLVYFSSGTTGMPK--MVEHDFTYpLGHIVTakYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVydYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 291 KFSASQFWDDCRKYNVTVIQYIGELLRYLCNspQKPNDRD-HKVRLAL--GNGLRGDVWRQFvKRFGDICIYEFYAATE- 366
Cdd:cd05970 262 KFDPKALLEKLSKYGVTTFCAPPTIYRFLIR--EDLSRYDlSSLRYCTtaGEALNPEVFNTF-KEKTGIKLMEGFGQTEt 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 367 ----GNIGFMNyaRKVGAVGRVNylqkkiitydlIKYDVEkdepVRDENGYcvRVPKGEVGLLVCKITQLTP---FNGYA 439
Cdd:cd05970 339 tltiATFPWME--PKPGSMGKPA-----------PGYEID----LIDREGR--SCEAGEEGEIVIRTSKGKPvglFGGYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 440 GAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD 519
Cdd:cd05970 400 KDAEKTA-----EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTG--VPD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 520 H-EGRIGMASIKMKENHEFDG---KKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRK 575
Cdd:cd05970 471 PiRGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
60-515 |
1.51e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 76.63 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 60 LEKA-RQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN--Y 136
Cdd:PRK08974 29 FEQAvARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNplY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 NIRakSLLHCFQCCGAKVLLVSPELQAAVEEILpslkkDDVSIYYVSRTSNTD----GIDSFLDKVDEVSTEPIPE---- 208
Cdd:PRK08974 109 TPR--ELEHQLNDSGAKAIVIVSNFAHTLEKVV-----FKTPVKHVILTRMGDqlstAKGTLVNFVVKYIKRLVPKyhlp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 209 ---SWRS-------------EVTFSTPALYIYTSGTTGLPKAAMITHQRIwygtgltfVSGLKADDVIY----------- 261
Cdd:PRK08974 182 daiSFRSalhkgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNM--------LANLEQAKAAYgpllhpgkelv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 262 -ITLPFYHSAAL----LIGIHgciVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLA 336
Cdd:PRK08974 254 vTALPLYHIFALtvncLLFIE---LGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 337 LGNGLrgDVWRQFVKRFGDIC---IYEFYAATEGNigfmnyarkvgavgrvnylqkKIIT---YDLIKYDVEKDEPV--- 407
Cdd:PRK08974 331 VGGGM--AVQQAVAERWVKLTgqyLLEGYGLTECS---------------------PLVSvnpYDLDYYSGSIGLPVpst 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 408 ----RDENGYcvRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGD 483
Cdd:PRK08974 388 eiklVDDDGN--EVPPGEPGELWVKGPQV--MLGYWQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKD 456
|
490 500 510
....*....|....*....|....*....|..
gi 308153494 484 TFRWKGENVATTEVADTVGLVDFVQEVNVYGV 515
Cdd:PRK08974 457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
53-497 |
2.18e-14 |
|
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: 75.95 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA-M 131
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLnYNIRAKSLLHCFQCCGAKVLLVSP--------ELQAAVEEILPSLKKddvsIYYVSRTSNTDGIDSFLDK-VDEVS 202
Cdd:COG1021 104 FAL-PAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVPSLRH----VLVVGDAGEFTSLDALLAApADLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 203 TEPIPESwrsevtfstPALYIYTSGTTGLPKaaMI--THQRIWYgtglTF-----VSGLKADDVIYITLPFYHSAALLI- 274
Cdd:COG1021 179 PRPDPDD---------VAFFQLSGGTTGLPK--LIprTHDDYLY----SVrasaeICGLDADTVYLAALPAAHNFPLSSp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 275 GIHGCIVAGATLALRTKFSAsqfwDDC----RKYNVTVIQYIGELLRYLCNSPQKpNDRD-------------------H 331
Cdd:COG1021 244 GVLGVLYAGGTVVLAPDPSP----DTAfpliERERVTVTALVPPLALLWLDAAER-SRYDlsslrvlqvggaklspelaR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 332 KVRLALGNGLrgdvwrQFVkrFGdiciyefyaATEGNIgfmNYAR-------KVGAVGRvnylqkKIITYDLIKydvekd 404
Cdd:COG1021 319 RVRPALGCTL------QQV--FG---------MAEGLV---NYTRlddpeevILTTQGR------PISPDDEVR------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 405 epVRDENGycVRVPKGEVGLLVCKitqlTP--FNGYAGAKAQTEKkklrdVFKKgDLYFNSGDLLMVDHENFIYFHDRVG 482
Cdd:COG1021 367 --IVDEDG--NPVPPGEVGELLTR----GPytIRGYYRAPEHNAR-----AFTP-DGFYRTGDLVRRTPDGYLVVEGRAK 432
|
490
....*....|....*
gi 308153494 483 DTFRWKGENVATTEV 497
Cdd:COG1021 433 DQINRGGEKIAAEEV 447
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
80-578 |
4.09e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 75.23 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNiraksllhcfqccgakvlLVSP 159
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR------------------LSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 160 ELQAAVEEILPSLKKDDVSIYyVSRTSNTDgIDSFLDKVDEVS---TEPIPESwrsevtfsTPALYIYTSGTTGLPKAAM 236
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVA-AGRTDVED-LAAFIASADALEpadTPSIPPE--------RVSLILFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 237 ITHQRIwYGTGLTF-VSG-LKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIG- 313
Cdd:PRK09088 155 LSERNL-QQTAHNFgVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 314 -ELLRYLCNSPQ-KPNDRDHKVRLALGNG------LRGdvWRQfvkrfGDICIYEFYAATE-GNIGFMNY-----ARKVG 379
Cdd:PRK09088 234 pQMAQAFRAQPGfDAAALRHLTALFTGGAphaaedILG--WLD-----DGIPMVDGFGMSEaGTVFGMSVdcdviRAKAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 380 AVG-RVNYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLTPfnGY-----AGAKAQTekkklrdv 453
Cdd:PRK09088 307 AAGiPTPTVQTRVV-----------DDQGND-------CPAGVPGELLLRGPNLSP--GYwrrpqATARAFT-------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 454 fkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVaDTVgLVDF--VQEVNVYGvhVPDHE-GRIGMASIK 530
Cdd:PRK09088 359 ---GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEI-EAV-LADHpgIRECAVVG--MADAQwGEVGYLAIV 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 308153494 531 MKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:PRK09088 432 PADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
67-568 |
5.68e-14 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 74.27 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRA-EGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSPElQAAveeilpslkkddvsiyYVsrtsntdgidsfldkvdevstepipeswrsevtfstpalyIYTS 226
Cdd:cd17643 80 LADSGPSLLLTDPD-DLA----------------YV----------------------------------------IYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 227 GTTGLPKAAMITHQ---RIWYGTGLTFvsGLKADDViyITLpfYHSAAL---LIGIHGCIVAGATLAL---RTKFSASQF 297
Cdd:cd17643 103 GSTGRPKGVVVSHAnvlALFAATQRWF--GFNEDDV--WTL--FHSYAFdfsVWEIWGALLHGGRLVVvpyEVARSPEDF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 298 WDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGDIC--IYEFYAATEGNIgFMN 373
Cdd:cd17643 177 ARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTV-HVT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 374 Y---------ARKVGAVGRVnylqkkiiTYDLIKYdvekdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQ 444
Cdd:cd17643 256 FrpldaadlpAAAASPIGRP--------LPGLRVY-------VLDADG--RPVPPGVVGELYVSGAGVAR--GYLGRPEL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 445 TEKKKLRDVFKK-GDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEV-ADTVGLVDFVQevnvygVHVPDHEG 522
Cdd:cd17643 317 TAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIeAALATHPSVRD------AAVIVRED 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 308153494 523 RIG----MASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd17643 391 EPGdtrlVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
78-572 |
7.68e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 74.41 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 SPELQAAVEEILPslkKDDVSIYYVSRTSNTDG------IDSFLDKVDE-VSTEPIPES----------WRSEVTFSTP- 219
Cdd:PRK05677 129 LANMAHLAEKVLP---KTGVKHVIVTEVADMLPplkrllINAVVKHVKKmVPAYHLPQAvkfndalakgAGQPVTEANPq 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 220 ----ALYIYTSGTTGLPKAAMITHQRIWygTGLTFVSGLKADDV-----IYIT-LPFYH--------SAALLIGIHGCIV 281
Cdd:PRK05677 206 addvAVLQYTGGTTGVAKGAMLTHRNLV--ANMLQCRALMGSNLnegceILIApLPLYHiyaftfhcMAMMLIGNHNILI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 282 AGATlalrtkfSASQFWDDCRKYNVTVIQYIGELLRYLCNSP--QKPNDRDHKVRLALGNGLRGDVWRQFVKRFG-DICi 358
Cdd:PRK05677 284 SNPR-------DLPAMVKELGKWKFSGFVGLNTLFVALCNNEafRKLDFSALKLTLSGGMALQLATAERWKEVTGcAIC- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 359 yEFYAATEgnigfmnyARKVGAVGRVNYLQKKII----TYDLIKydvekdepVRDENGycVRVPKGEVGLLVCKITQLtp 434
Cdd:PRK05677 356 -EGYGMTE--------TSPVVSVNPSQAIQVGTIgipvPSTLCK--------VIDDDG--NELPLGEVGELCVKGPQV-- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 435 FNGYagAKAQTEKKKLRDvfkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYG 514
Cdd:PRK05677 415 MKGY--WQRPEATDEILD----SDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIG 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 515 vhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:PRK05677 489 --VPDEKsGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-369 |
9.63e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPELQAAveeiLPSlkKDDVSIYYVSRTSNTDGidsFLDKVDEVSTEPipeswrsevtfST 218
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQR----LPI--PDGLASLALDRDEDWEG---FPAHDPAVRLHP-----------DN 4695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 219 PALYIYTSGTTGLPKAAMITHQR-----IWYGTGLtfvsGLKADDVIYITLPFYHSAALLiGIHGCIVAGATLALRtkfs 293
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSlvnhlHATGERY----ELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIR---- 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 294 ASQFWDDCRKY------NVTVIQYIGELLRYLCNSPqkPNDRDH-KVRLAL--GNGLRGDVWRQFVKRFGDICIYEFYAA 364
Cdd:PRK12316 4767 DDSLWDPERLYaeihehRVTVLVFPPVYLQQLAEHA--ERDGEPpSLRVYCfgGEAVAQASYDLAWRALKPVYLFNGYGP 4844
|
....*
gi 308153494 365 TEGNI 369
Cdd:PRK12316 4845 TETTV 4849
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
58-308 |
1.20e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 58 AFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDSF-LDKVDEVSTEPI--PESwrsEV 214
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT----QRHLLERLPL----------------PAGVARLpLDRDAEWADYPDtaPAV---QL 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 215 TFSTPALYIYTSGTTGLPKAAMITH----QRIwYGTGLTFvsGLKADDVIYITLPFYHSAAlligIHGC---IVAGATLA 287
Cdd:PRK12316 2144 AGENLAYVIYTSGSTGLPKGVAVSHgalvAHC-QAAGERY--ELSPADCELQFMSFSFDGA----HEQWfhpLLNGARVL 2216
|
250 260
....*....|....*....|...
gi 308153494 288 LR--TKFSASQFWDDCRKYNVTV 308
Cdd:PRK12316 2217 IRddELWDPEQLYDEMERHGVTI 2239
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
58-497 |
2.78e-13 |
|
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: 72.50 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 58 AFLEKARQTPHKPFLLFRDET-----LTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYvwlWLglVKLGCAMA 132
Cdd:cd05928 16 ADKEKAGKRPPNPALWWVNGKgdevkWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW---WL--VNVACIRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 133 CLNY-----NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEIL---PSLKkddvSIYYVSRTSnTDGIDSFLDKVDEVSTE 204
Cdd:cd05928 91 GLVFipgtiQLTAKDILYRLQASKAKCIVTSDELAPEVDSVAsecPSLK----TKLLVSEKS-RDGWLNFKELLNEASTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 205 PIPESWRSEvtfsTPALYIYTSGTTGLPKaaMITHQRIWYGTGLT----FVSGLKADDVIYITLPFYHSAALLIGIHGCI 280
Cdd:cd05928 166 HHCVETGSQ----EPMAIYFTSGTTGSPK--MAEHSHSSLGLGLKvngrYWLDLTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 281 VAGATLALR--TKFSASQFWDDCRKYNVTVIQYIGELLRYLC----NSPQKPNDRDHkvrLALGNGLRGDVWRQFVKRFG 354
Cdd:cd05928 240 IQGACVFVHhlPRFDPLVILKTLSSYPITTFCGAPTVYRMLVqqdlSSYKFPSLQHC---VTGGEPLNPEVLEKWKAQTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 355 dICIYEFYAATEGNIGFMNYAR---KVGAVGRVNylqkkiitydlIKYDVEkdepVRDENGYCvrVPKGEVGLLVCKITQ 431
Cdd:cd05928 317 -LDIYEGYGQTETGLICANFKGmkiKPGSMGKAS-----------PPYDVQ----IIDDNGNV--LPPGTEGDIGIRVKP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 432 LTP---FNGYAGAKAQTEKKklrdvfKKGDLYfNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEV 497
Cdd:cd05928 379 IRPfglFSGYVDNPEKTAAT------IRGDFY-LTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
77-557 |
4.08e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 72.18 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPElqaAVEEiLPSLKkddVSIYYVSRTSNTDGIDSFLDKVDEV---STEPIPeswRSEVTFSTPALYIYTSGTTGLPK 233
Cdd:PLN02574 145 TSPE---NVEK-LSPLG---VPVIGVPENYDFDSKRIEFPKFYELikeDFDFVP---KPVIKQDDVAAIMYSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 234 AAMITHqRIWYGTGLTFV---------SGlkADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKY 304
Cdd:PLN02574 215 GVVLTH-RNLIAMVELFVrfeasqyeyPG--SDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 305 NVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGDICIYEFYAATEGNigfmnyarkvgAV 381
Cdd:PLN02574 292 KVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGaapLSGKFIQDFVQTLPHVDFIQGYGMTEST-----------AV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 382 GRVNYLQKKIITYD---LIKYDVEKdEPVRDENGYCvrVPKGEVGLLVckitqltpFNGYAGAKAQTEKKKLRDVFKKGD 458
Cdd:PLN02574 361 GTRGFNTEKLSKYSsvgLLAPNMQA-KVVDWSTGCL--LPPGNCGELW--------IQGPGVMKGYLNNPKATQSTIDKD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 459 LYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTvgLVDFVQEVNVYGVHVPDHE-GRIGMASIKMKENHEF 537
Cdd:PLN02574 430 GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV--LISHPEIIDAAVTAVPDKEcGEIPVAFVVRRQGSTL 507
|
490 500
....*....|....*....|
gi 308153494 538 DGKKLFQHIADYLPSYARPR 557
Cdd:PLN02574 508 SQEAVINYVAKQVAPYKKVR 527
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
77-565 |
5.02e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 71.93 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPELQAAVEEI-LPSLKKDDVSIyyvsrtSNTDGIDSFLDKVDEVSTEPIPEswrsEVTFSTPALYIYTSGTTGLPKAA 235
Cdd:PLN02330 133 TNDTNYGKVKGLgLPVIVLGEEKI------EGAVNWKELLEAADRAGDTSDNE----EILQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 236 MITHQRI-------WYGTGLTFVSGLKADDVIyitlPFYHsaalLIGIHGCIVA-----GATLALrTKFSASQFWDDCRK 303
Cdd:PLN02330 203 MLTHRNLvanlcssLFSVGPEMIGQVVTLGLI----PFFH----IYGITGICCAtlrnkGKVVVM-SRFELRTFLNALIT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 304 YNVTVIQYIGELLRYLCNSPQKPNDRDHKVRL----ALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVG 379
Cdd:PLN02330 274 QEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 380 AVGrvnYLQKKIITYDLIKYDVEKDEPvrdENGycVRVPKGEVGlLVCKITQLTpFNGYAGAKAQTEkkklRDVFKKGdl 459
Cdd:PLN02330 354 GHG---IAKKNSVGFILPNLEVKFIDP---DTG--RSLPKNTPG-ELCVRSQCV-MQGYYNNKEETD----RTIDEDG-- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 460 YFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHE-GRIGMASIKMKENHEFD 538
Cdd:PLN02330 418 WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKES 495
|
490 500
....*....|....*....|....*..
gi 308153494 539 GKKLFQHIADYLPSYARPRFLRIQDTI 565
Cdd:PLN02330 496 EEDILNFVAANVAHYKKVRVVQFVDSI 522
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
54-369 |
5.38e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 71.31 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 134 LNYNIRAKSLLHCFQCCGAKVLLVSPElqaaveeilpslkkddvSIYYVsrtsntdgidsfldkvdevstepipeswrse 213
Cdd:cd17644 80 LDPNYPQERLTYILEDAQISVLLTQPE-----------------NLAYV------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 214 vtfstpalyIYTSGTTGLPKAAMITHQRIW-YGTGLTFVSGLKADDVIYITLPFYHSAALLiGIHGCIVAGATLALRTK- 291
Cdd:cd17644 112 ---------IYTSGSTGKPKGVMIEHQSLVnLSHGLIKEYGITSSDRVLQFASIAFDVAAE-EIYVTLLSGATLVLRPEe 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 292 --FSASQFWDDCRKYNVTVI--------QYIGELLRYLCNSPQKPndrdhKVRLALGNGLRGDVWRQFVKRFGD-ICIYE 360
Cdd:cd17644 182 mrSSLEDFVQYIQQWQLTVLslppaywhLLVLELLLSTIDLPSSL-----RLVIVGGEAVQPELVRQWQKNVGNfIQLIN 256
|
....*....
gi 308153494 361 FYAATEGNI 369
Cdd:cd17644 257 VYGPTEATI 265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-556 |
8.09e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK12316 3056 ERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELqaaveeilpslkkddvsiyyvsRTSNTDGIDSF-LDKVDEVSTEPIPEsw 210
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLLSQSHL----------------------RLPLAQGVQVLdLDRGDENYAEANPA-- 3190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 211 rSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLiGIHGCIVAGATLALR 289
Cdd:PRK12316 3191 -IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLcWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLA 3268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 290 tkfsASQFWDDCRKY-------NVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFvkrFGDICIYEFY 362
Cdd:PRK12316 3269 ----GPEDWRDPALLvelinseGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLY 3341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 363 AATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVrdenGYCVRVPKGEVGLLvckitqltpfNGYAGAK 442
Cdd:PRK12316 3342 GPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPV----GALGELYLGGEGLA----------RGYHNRP 3407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 443 AQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvpdhEG 522
Cdd:PRK12316 3408 GLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV-----DG 3482
|
490 500 510
....*....|....*....|....*....|....
gi 308153494 523 RIGMASIKMKENHEFDGKKLFQHIADYLPSYARP 556
Cdd:PRK12316 3483 RQLVAYVVPEDEAGDLREALKAHLKASLPEYMVP 3516
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
64-515 |
1.16e-12 |
|
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: 70.68 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 64 RQTPHKPFLLFRDE------TLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd17634 64 RENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEILPSLKKDDVSIYYVSRTSNTDGID--SFLDKVDEVSTEPi 206
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQegRDLWWRDLIAKAS- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 207 PESWRSEVTFSTPALYIYTSGTTGLPKAAMITH--QRIWYGTGLTFVSGLKADDVIYITlpfyHSAALLIG----IHGCI 280
Cdd:cd17634 222 PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCT----ADVGWVTGhsylLYGPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 281 VAGATLALRTKF----SASQFWDDCRKYNVTVIQYIGELLRYLcnSPQKPN-----DRDH-KVRLALGNGLRGDVWRQFV 350
Cdd:cd17634 298 ACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDaiegtDRSSlRILGSVGEPINPEAYEWYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 351 KRFGDI-C-IYEFYAATEGNiGFMNYARKVgavgrVNYLQKKIITYDLIKYDVEkdepVRDENGYcvRVPKGEVGLLVck 428
Cdd:cd17634 376 KKIGKEkCpVVDTWWQTETG-GFMITPLPG-----AIELKAGSATRPVFGVQPA----VVDNEGH--PQPGGTEGNLV-- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 429 ITqlTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQ 508
Cdd:cd17634 442 IT--DPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
....*..
gi 308153494 509 EVNVYGV 515
Cdd:cd17634 520 EAAVVGI 526
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-572 |
2.30e-12 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 68.51 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 219 PALYIYTSGTTGLPKAAMITHQRIWY---GTGlTFVsGLKADDVIYITLPFYHSAALLIgIHGCIVAGATLALRTKFSAS 295
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLAsaaGLH-SRL-GFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 296 QfwDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDhKVRLALGNGlrGDVWRQFVKRFGD--ICIYEFYAATE--GNIGF 371
Cdd:cd17630 79 A--EDLAPPGVTHVSLVPTQLQRLLDSGQGPAALK-SLRAVLLGG--APIPPELLERAADrgIPLYTTYGMTEtaSQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 372 MNYAR-KVGAVGRVNylqkkiityDLIKYDVEKDEpvRDEngycvrvPKGEvgllvckitqlTPFNGYAGAKAQtekkkl 450
Cdd:cd17630 154 KRPDGfGRGGVGVLL---------PGRELRIVEDG--EIW-------VGGA-----------SLAMGYLRGQLV------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 451 RDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASI 529
Cdd:cd17630 199 PEFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDEElGQRPVAVI 274
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 308153494 530 KMkeNHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd17630 275 VG--RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGK 315
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
43-572 |
2.43e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 70.34 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 43 VRSYGKRRPAR-TILRAFLEKARQTPHKpfLLFRDET---LTYAQVDRRSNQVARALHDHLGLRQgdCVALLMGNEPAYV 118
Cdd:PRK08633 604 FDSWKSRKEALpPLAEAWIDTAKRNWSR--LAVADSTggeLSYGKALTGALALARLLKRELKDEE--NVGILLPPSVAGA 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 119 WLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSpelqAAVEEILPSLKKD-----DVSIYYV----SRTSNTD 189
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITS----RKFLEKLKNKGFDlelpeNVKVIYLedlkAKISKVD 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 190 GIDSFLdkvdevSTEPIPESW-----RSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYIT 263
Cdd:PRK08633 756 KLTALL------AARLLPARLlkrlyGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIeQISDVFNLRNDDVILSS 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 264 LPFYHSAALLIG-----IHGCIVA-------GATLAlrtkfsasqfwDDCRKYNVTVIQYIGELLR-YLCNSPQKPNDRD 330
Cdd:PRK08633 830 LPFFHSFGLTVTlwlplLEGIKVVyhpdptdALGIA-----------KLVAKHRATILLGTPTFLRlYLRNKKLHPLMFA 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 331 hKVRLALGNG--LRGDVWRQFVKRFGdICIYEFYAATEG------NI-------GFMNYARKVGAVGR------Vnylqk 389
Cdd:PRK08633 899 -SLRLVVAGAekLKPEVADAFEEKFG-IRILEGYGATETspvasvNLpdvlaadFKRQTGSKEGSVGMplpgvaV----- 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 390 KIItydlikyDVEKDEPvrdengycvrVPKGEVGLLVCKITQLtpFNGYAGAKAQTeKKKLRDVFKKGdlYFNSGDLLMV 469
Cdd:PRK08633 972 RIV-------DPETFEE----------LPPGEDGLILIGGPQV--MKGYLGDPEKT-AEVIKDIDGIG--WYVTGDKGHL 1029
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 470 DHENFIYFHDR------VGdtfrwkGENVATTEVADTVGLVDFVQEVNVYGVHVPDHegRIGMASIKMKENHEFDGKKLF 543
Cdd:PRK08633 1030 DEDGFLTITDRysrfakIG------GEMVPLGAVEEELAKALGGEEVVFAVTAVPDE--KKGEKLVVLHTCGAEDVEELK 1101
|
570 580 590
....*....|....*....|....*....|
gi 308153494 544 QHIAD-YLPSYARPRFLRIQDTIEITGTFK 572
Cdd:PRK08633 1102 RAIKEsGLPNLWKPSRYFKVEALPLLGSGK 1131
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
72-309 |
2.53e-12 |
|
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: 69.39 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 72 LLFRDETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCG 151
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 152 AKVLLVSpelqaaveeilpslKKDDVsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfstpALYIYTSGTTGL 231
Cdd:cd05914 80 AKAIFVS--------------DEDDV------------------------------------------ALINYTSGTTGN 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 232 PKAAMITHQRIWYG-TGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFwDDCRKYNVTVI 309
Cdd:cd05914 104 SKGVMLTYRNIVSNvDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-IALAFAQVTPT 181
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-273 |
3.24e-12 |
|
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: 69.23 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYV-WLWLGL------VKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIpAFWACVlagfvpAPLTVPPTYDEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 149 CCGAKVLLVSPELQAAVEEILpslkkddvsiyyvsrtsNTDGIDSF-LDKVDEVSTEPIPESWRsEVTFSTPALYIYTSG 227
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLE-----------------TLSGLPGIrVLSIEELLDTAADHDLP-QSRPDDLALLMLTSG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 308153494 228 TTGLPKAAMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALL 273
Cdd:cd05906 178 STGFPKAVPLTHRNILARSaGKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
67-239 |
4.58e-12 |
|
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: 68.43 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAAR-GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSPElqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfsTPALYIYTS 226
Cdd:cd17652 80 LADARPALLLTTPD---------------------------------------------------------NLAYVIYTS 102
|
170
....*....|...
gi 308153494 227 GTTGLPKAAMITH 239
Cdd:cd17652 103 GSTGRPKGVVVTH 115
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
62-297 |
6.09e-12 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 68.23 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 62 KARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN- 135
Cdd:cd05921 4 WARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 136 -YNIRAKS---LLHCFQCCGAKVLLVS--PELQAAVEEILPslkkDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPES 209
Cdd:cd05921 83 aYSLMSQDlakLKHLFELLKPGLVFAQdaAPFARALAAIFP----LGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 210 wRSEVTFSTPALYIYTSGTTGLPKaAMITHQRIWYGT--GLTFVSGLKADD--VIYITLPFYHSAALLIGIHGCIVAGAT 285
Cdd:cd05921 159 -FAAVGPDTVAKFLFTSGSTGLPK-AVINTQRMLCANqaMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250
....*....|...
gi 308153494 286 LAL-RTKFSASQF 297
Cdd:cd05921 237 LYIdDGKPMPGGF 249
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
77-285 |
6.65e-12 |
|
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: 68.54 E-value: 6.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPELQA----AVEEILPSLK-----KDDVSiyyvSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALyIYTSG 227
Cdd:cd05933 86 VENQKQLqkilQIQDKLPHLKaiiqyKEPLK----EKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTL-IYTSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 228 TTGLPKAAMITHQRI-WYGTGLTFVSGLKADDV----IYITLPFYHSAALLIGIHGCIVAGAT 285
Cdd:cd05933 161 TTGMPKGVMLSHDNItWTAKAASQHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQ 223
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-566 |
7.72e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 67.02 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 217 STPALYI-YTSGTTGLPKAAMITHQRIW--YGTGLTFVSGLKADD-------------VIYITLPFYHSAALLIGIHGCI 280
Cdd:cd05924 2 SADDLYIlYTGGTTGMPKGVMWRQEDIFrmLMGGADFGTGEFTPSedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 281 VAGATLALRTKFSASQFWDDCRKYNVTVIQYIGE-LLRYLCNSPQKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGDI 356
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 357 CIYEFYAATEGniGFMNYARkvgAVGRVNYLQKKIItydlikydVEKDEPVRDENGYCVRVPKGEVGLLVCKitQLTPfN 436
Cdd:cd05924 162 TLVDAFGSSET--GFTGSGH---SAGSGPETGPFTR--------ANPDTVVLDDDGRVVPPGSGGVGWIARR--GHIP-L 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 437 GYAGAKAQTeKKKLRDVfkKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvh 516
Cdd:cd05924 226 GYYGDEAKT-AETFPEV--DGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVG-- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 308153494 517 VPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIE 566
Cdd:cd05924 301 RPDERwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIE 351
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
59-256 |
7.94e-12 |
|
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: 67.95 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLR-SLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPELQAAveeilpslkkddvsiyYVsrtsntdgidsfldkvdevstepipeswrsevtfst 218
Cdd:cd05918 84 PLQRLQEILQDTGAKVVLTSSPSDAA----------------YV------------------------------------ 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 308153494 219 palyIYTSGTTGLPKAAMITHQriwygtglTFVSGLKA 256
Cdd:cd05918 112 ----IFTSGSTGKPKGVVIEHR--------ALSTSALA 137
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
78-560 |
1.14e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 67.54 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 SPELQAAVEEILPslkkdDVSIYYVSRTSNTDG--------IDSFLDKVDE-VSTEPIPE--SWRS-------------E 213
Cdd:PRK12492 129 LNMFGKLVQEVLP-----DTGIEYLIEAKMGDLlpaakgwlVNTVVDKVKKmVPAYHLPQavPFKQalrqgrglslkpvP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 214 VTFSTPALYIYTSGTTGLPKAAMITH-------QRIWYGTGLTFVSGLK----ADDVIYITLPFYHSAALLIGIHGCIVA 282
Cdd:PRK12492 204 VGLDDIAVLQYTGGTTGLAKGAMLTHgnlvanmLQVRACLSQLGPDGQPlmkeGQEVMIAPLPLYHIYAFTANCMCMMVS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 283 GATLALRTK-FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQ-KPNDRDH-KVRLALGNGL---RGDVWRQFVKrfgdi 356
Cdd:PRK12492 284 GNHNVLITNpRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGfKDLDFSAlKLTNSGGTALvkaTAERWEQLTG----- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 357 C-IYEFYAATEGNI-----GFMNYARkVGAVG-RVNYLQKKIItydlikydvekdepvrDENGycVRVPKGEVGLLVCKI 429
Cdd:PRK12492 359 CtIVEGYGLTETSPvastnPYGELAR-LGTVGiPVPGTALKVI----------------DDDG--NELPLGERGELCIKG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 430 TQLtpFNGYAGAKAQTEKKklrdvfKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVglVDFVQE 509
Cdd:PRK12492 420 PQV--MKGYWQQPEATAEA------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV--MAHPKV 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308153494 510 VNVYGVHVPDH-------------EGRIGMASIKM--KENheFDGKKLFQHIA--DYLPSYARPRFLR 560
Cdd:PRK12492 490 ANCAAIGVPDErsgeavklfvvarDPGLSVEELKAycKEN--FTGYKVPKHIVlrDSLPMTPVGKILR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
78-499 |
1.61e-11 |
|
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: 66.64 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 spelqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepiPESWRSEVTFSTP---ALYIYTSGTTGLPKA 234
Cdd:cd05903 80 -------------------------------------------------PERFRQFDPAAMPdavALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 235 AMITHQRIWYGT-GLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIG 313
Cdd:cd05903 111 VMHSHNTLSASIrQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 314 ELLRYLCNSPQKPNDR--DHKVRLALGNGLRGDVWRQFVKRFGDIcIYEFYAATEgnigfmnyarKVGAVGRVN-YLQKK 390
Cdd:cd05903 191 PFLTDLLNAVEEAGEPlsRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTE----------CPGAVTSITpAPEDR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 391 IITYD---LIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKAQTekkklRDVFKKGdlYFNSGDLL 467
Cdd:cd05903 260 RLYTDgrpLPGVEIK----VVDDTG--ATLAPGVEGELLSRGPSV--FLGYLDRPDLT-----ADAAPEG--WFRTGDLA 324
|
410 420 430
....*....|....*....|....*....|..
gi 308153494 468 MVDHENFIYFHDRVGDTFRWKGENVATTEVAD 499
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVED 356
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-559 |
1.88e-11 |
|
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: 65.75 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKADDVIYITLPFYHSAALLIGIhGCIVAGATLALRTKFSASQFWDDC 301
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAaNLQLIHAMGLTEADVYLNMLPLFHIAGLNLAL-ATFHAGGANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 302 RKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALgnGLRG-DVwrqfVKRFGDICIYEFYAA-----TEGNIGFMNYA 375
Cdd:cd17637 85 EEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL--GLDApET----IQRFEETTGATFWSLygqteTSGLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 376 RKVGAVGRVNYLQKKIITYDLikydvekDEPvrdengycvrVPKGEVGLLVCKitqlTP--FNGYAGAKAQTEKkklrdV 453
Cdd:cd17637 159 ERPGSAGRPGPLVRVRIVDDN-------DRP----------VPAGETGEIVVR----GPlvFQGYWNLPELTAY-----T 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 454 FKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWK--GENVATTEVADTVGLVDFVQEVNVYGvhVPDHEGRIGM-ASIK 530
Cdd:cd17637 213 FRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIG--VPDPKWGEGIkAVCV 288
|
330 340
....*....|....*....|....*....
gi 308153494 531 MKENHEFDGKKLFQHIADYLPSYARPRFL 559
Cdd:cd17637 289 LKPGATLTADELIEFVGSRIARYKKPRYV 317
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
56-559 |
2.07e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 66.58 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 56 LRAFLEKA-RQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK07059 25 LADLLEESfRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 135 N--YNIRakSLLHCFQCCGAKVLLVSPELQAAVEEILPSlkkddVSIYYVSRTSNTD--GIDSFL-----DKVDE-VSTE 204
Cdd:PRK07059 104 NplYTPR--ELEHQLKDSGAEAIVVLENFATTVQQVLAK-----TAVKHVVVASMGDllGFKGHIvnfvvRRVKKmVPAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 205 PIPESWR--------SEVTFSTP-------ALYIYTSGTTGLPKAAMITHQRI---------WYGTGLTfvSGLKADDVI 260
Cdd:PRK07059 177 SLPGHVRfndalaegARQTFKPVklgpddvAFLQYTGGTTGVSKGATLLHRNIvanvlqmeaWLQPAFE--KKPRPDQLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 261 YIT-LPFYHSAAL----LIGIHgciVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRL 335
Cdd:PRK07059 255 FVCaLPLYHIFALtvcgLLGMR---TGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 336 ALGNGL--RGDVWRQFVKRFGdiC-IYEFYAATEgnigfmnyarkVGAVGRVNYLQKK----IITYDLIKYDVEkdepVR 408
Cdd:PRK07059 332 ANGGGMavQRPVAERWLEMTG--CpITEGYGLSE-----------TSPVATCNPVDATefsgTIGLPLPSTEVS----IR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 409 DENGYcvRVPKGEVGLLVCKITQLTPfnGY-----AGAKAQTEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGD 483
Cdd:PRK07059 395 DDDGN--DLPLGEPGEICIRGPQVMA--GYwnrpdETAKVMTA-----------DGFFRTGDVGVMDERGYTKIVDRKKD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 484 TFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvPD-HEGRIGMASIkMKENHEFDGKKLFQHIADYLPSYARPRFL 559
Cdd:PRK07059 460 MILVSGFNVYPNEIEEVVASHPGVLEVAAVGV--PDeHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
77-265 |
3.72e-11 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 65.91 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPELQA-AVEEILPSLKKDDVSIYYVSR-TSNTDgiDSFLDKVDEVSTEPI------PESWRSEVTFSTP---ALYIYT 225
Cdd:cd17641 89 AEDEEQVdKLLEIADRIPSVRYVIYCDPRgMRKYD--DPRLISFEDVVALGRaldrrdPGLYEREVAAGKGedvAVLCTT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 308153494 226 SGTTGLPKAAMITHQR-IWYGTGLTFVSGLKADD--VIYITLP 265
Cdd:cd17641 167 SGTTGKPKLAMLSHGNfLGHCAAYLAADPLGPGDeyVSVLPLP 209
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
67-369 |
8.24e-11 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 64.31 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRAL-GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLvspelqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevSTEPipeswrsevtfSTPALYIYTS 226
Cdd:cd17649 80 LEDSGAGLLL---------------------------------------------THHP-----------RQLAYVIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 227 GTTGLPKAAMITHQRI-WYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIvAGATLALRtkfsASQFWDD----- 300
Cdd:cd17649 104 GSTGTPKGVAVSHGPLaAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLI-CGACVVLR----PDELWASadela 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 301 --CRKYNVTVIQ----YIGELLRYLCNSPQkpnDRDHKVRLAL--GNGLRGDVWRQFVKrfGDICIYEFYAATEGNI 369
Cdd:cd17649 179 emVRELGVTVLDlppaYLQQLAEEADRTGD---GRPPSLRLYIfgGEALSPELLRRWLK--APVRLFNAYGPTEATV 250
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
496-572 |
8.56e-11 |
|
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: 58.32 E-value: 8.56e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 496 EVADTVGLVDFVQEVNVYGVHVPDhEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDEL-KGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
51-243 |
1.44e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.13 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFLEKARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLV 125
Cdd:PRK08180 37 YPRRLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 126 KLGCAMACLN--YNIRAKS---LLHCFQCCGAKVLLVS--PELQAAVEEILPslkkDDVSIYYVSRTSNTDGIDSFLDKV 198
Cdd:PRK08180 116 YAGVPYAPVSpaYSLVSQDfgkLRHVLELLTPGLVFADdgAAFARALAAVVP----ADVEVVAVRGAVPGRAATPFAALL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 308153494 199 DEVSTEPIPESWRSeVTFSTPALYIYTSGTTGLPKAAmITHQRIW 243
Cdd:PRK08180 192 ATPPTAAVDAAHAA-VGPDTIAKFLFTSGSTGLPKAV-INTHRML 234
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-239 |
2.40e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 51 PARTILRAFL-EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGC 129
Cdd:PRK05691 1128 PAQAWLPELLnEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 130 AMACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDSF-LDKVDevstepiPE 208
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLLT----QSHLLERLPQ----------------AEGVSAIaLDSLH-------LD 1259
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 308153494 209 SWRSevtfSTPALY---------IYTSGTTGLPKAAMITH 239
Cdd:PRK05691 1260 SWPS----QAPGLHlhgdnlayvIYTSGSTGQPKGVGNTH 1295
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
59-578 |
2.65e-10 |
|
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: 62.96 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGK-GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPElqaaveeilpslkkddvSIYYVsrtsntdgidsfldkvdevstepipeswrsevtfst 218
Cdd:cd17645 83 PGERIAYMLADSSAKILLTNPD-----------------DLAYV------------------------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 219 palyIYTSGTTGLPKAAMITHQRI-----WYGTglTFVSGLKADDVIYITLPFYHSAallIGIHGCIVAGATLAL---RT 290
Cdd:cd17645 110 ----IYTSGSTGLPKGVMIEHHNLvnlceWHRP--YFGVTPADKSLVYASFSFDASA---WEIFPHLTAGAALHVvpsER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 291 KFSASQFWDDCRKYNVTviqyIGELLRYLCNspQKPNDRDHKVRLALGNglrGDVWRQFVKRfgDICIYEFYAATEGNIg 370
Cdd:cd17645 181 RLDLDALNDYFNQEGIT----ISFLPTGAAE--QFMQLDNQSLRVLLTG---GDKLKKIERK--GYKLVNNYGPTENTV- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 371 fmnyarkVGAVGRVNYLQKKIITYDLIkyDVEKDEPVRDENGYCvrvPKGEVGLLVCKITQLTpfNGYAGAKAQTEKKKL 450
Cdd:cd17645 249 -------VATSFEIDKPYANIPIGKPI--DNTRVYILDEALQLQ---PIGVAGELCIAGEGLA--RGYLNRPELTAEKFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 451 RDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIK 530
Cdd:cd17645 315 VHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL-VAYVT 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 308153494 531 MKEnhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 578
Cdd:cd17645 394 APE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
98-534 |
3.48e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.89 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 98 HLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNiraksllHCFQCCGAKVLLVSPELQAAVEEI--------- 168
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR-------WSFEEAKSAMLLVRPVMLVTDETCsswyeelqn 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 169 --LPSLKkddvsiYYVSRTSNTDgiDSFLDKVDEVSTEPIpesWRSEVTFSTP---------ALYIYTSGTTGLPKAAMI 237
Cdd:PLN02860 124 drLPSLM------WQVFLESPSS--SVFIFLNSFLTTEML---KQRALGTTELdyawapddaVLICFTSGTTGRPKGVTI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 238 THqriwygTGLTFVS-------GLKADDVIYITLPFYH----SAALLIgihgcIVAGATLALRTKFSASQFWDDCRKYNV 306
Cdd:PLN02860 193 SH------SALIVQSlakiaivGYGEDDVYLHTAPLCHigglSSALAM-----LMVGACHVLLPKFDAKAALQAIKQHNV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 307 T----VIQYIGELLRYlcNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGDICIYEFYAATEG--NIGFMnyarkv 378
Cdd:PLN02860 262 TsmitVPAMMADLISL--TRKSMTWKVFPSVRKILngGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcsSLTFM------ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 379 gavgRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVC--------KITQLTP--FNGYAGAKAQTEKK 448
Cdd:PLN02860 334 ----TLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGldessrvgRILTRGPhvMLGYWGQNSETASV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 449 KLRDVfkkgdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVaDTVgLVDFVQEVNVYGVHVPDHE-GRIGMA 527
Cdd:PLN02860 410 LSNDG------WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEV-EAV-LSQHPGVASVVVVGVPDSRlTEMVVA 481
|
....*..
gi 308153494 528 SIKMKEN 534
Cdd:PLN02860 482 CVRLRDG 488
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
66-568 |
3.75e-10 |
|
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: 62.49 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 66 TPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLH 145
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 146 CFQCCGAKVLLVSPELqaaveeilPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEvstepipeswrsevtfSTPALY-IY 224
Cdd:cd17656 80 IMLDSGVRVVLTQRHL--------KSKLSFNKSTILLEDPSISQEDTSNIDYINN----------------SDDLLYiIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 225 TSGTTGLPKAAMITHQRIwygTGL-----TFVSGLKADDVI-YITLPF---YHSaalligIHGCIVAGATLAL---RTKF 292
Cdd:cd17656 136 TSGTTGKPKGVQLEHKNM---VNLlhferEKTNINFSDKVLqFATCSFdvcYQE------IFSTLLSGGTLYIireETKR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 293 SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGdICIYEFYAATEGNI 369
Cdd:cd17656 207 DVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGeqlVITNEFKEMLHEHN-VHLHNHYGPSETHV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 370 GFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDepvrdengycvRVPKGEVGLLVckITQLTPFNGYAGAKAQTEKKK 449
Cdd:cd17656 286 VTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQ-----------LQPQGIVGELY--ISGASVARGYLNRQELTAEKF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 450 LRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQE--VNVYGvhvpDHEGRIGMA 527
Cdd:cd17656 353 FPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEavVLDKA----DDKGEKYLC 428
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 308153494 528 SIKMKEnHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 568
Cdd:cd17656 429 AYFVME-QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLT 468
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
77-514 |
3.79e-10 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. 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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 62.38 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAmaclnyNIRAKSllhcfqccgakvll 156
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAV------DVVRGS-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 vspelQAAVEEILPSLKKDDVSIYYVSRTSntdgidsfldkvDEVSTepipeswrsevtfstpalYIYTSGTTGLPKAAM 236
Cdd:cd17640 63 -----DSSVEELLYILNHSESVALVVENDS------------DDLAT------------------IIYTSGTTGNPKGVM 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 237 ITHQRIWYGTG--LTFVSGLKADDVIYItLPFYHSAALLIGiHGCIVAGATLALRtkfSASQFWDDCRKYNVTVIQYIGE 314
Cdd:cd17640 108 LTHANLLHQIRslSDIVPPQPGDRFLSI-LPIWHSYERSAE-YFIFACGCSQAYT---SIRTLKDDLKRVKPHYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 315 LLRYLCNSPQKPNDRDHKVR------LALGNGLR-----GDVWRQFVKRFGD---ICIYEFYAATE-GNIGFMNYARK-- 377
Cdd:cd17640 183 LWESLYSGIQKQVSKSSPIKqflflfFLSGGIFKfgisgGGALPPHVDTFFEaigIEVLNGYGLTEtSPVVSARRLKCnv 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 378 VGAVGRvnylqkkIITYDLIKydvekdepVRDENGYCVrVPKGEVGLLVCKITQLTpfNGYAGAKAQTeKKKLRDvfkkg 457
Cdd:cd17640 263 RGSVGR-------PLPGTEIK--------IVDPEGNVV-LPPGEKGIVWVRGPQVM--KGYYKNPEAT-SKVLDS----- 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 308153494 458 DLYFNSGDLLMVDHENFIYFHDRVGDTFRWK-GENVATTEVADTVGLVDFVQEVNVYG 514
Cdd:cd17640 319 DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
54-260 |
4.14e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 63.14 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMgnePAYVWLWLGLVKLgcama 132
Cdd:PRK10252 458 TTLSALVAQqAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVAL---PRSVFLTLALHAI----- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 133 clnynIRAksllhcfqccGAKVLLVSPE-----LQAAVEEILPSL--KKDDVSiyyvSRTSntDGIDSFLDKVDEVSTEP 205
Cdd:PRK10252 529 -----VEA----------GAAWLPLDTGypddrLKMMLEDARPSLliTTADQL----PRFA--DVPDLTSLCYNAPLAPQ 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308153494 206 IPESWRSEVTfSTPALYIYTSGTTGLPKAAMITHQRI-----W----YgtgltfvsGLKADDVI 260
Cdd:PRK10252 588 GAAPLQLSQP-HHTAYIIFTSGSTGRPKGVMVGQTAIvnrllWmqnhY--------PLTADDVV 642
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
59-518 |
2.38e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 60.03 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PLN03102 19 FLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDD-------VSIYYVSRTSNTDGIDSFLDKVDEvSTEPIPESW 210
Cdd:PLN03102 98 LDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDsnlnlpvIFIHEIDFPKRPSSEELDYECLIQ-RGEPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 211 RSEVTFST---PALYIYTSGTTGLPKAAMITHQRIWYGTgLTFVSGLKADDV-IYI-TLPFYHSAALLIGIHGCIVAGAT 285
Cdd:PLN03102 177 ARMFRIQDehdPISLNYTSGTTADPKGVVISHRGAYLST-LSAIIGWEMGTCpVYLwTLPMFHCNGWTFTWGTAARGGTS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 286 LALRtKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQkpNDRDHK---VRLALGNGLRGDVWRQFVKRFGdICIYEFY 362
Cdd:PLN03102 256 VCMR-HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNS--LDLSPRsgpVHVLTGGSPPPAALVKKVQRLG-FQVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 363 AATE--GNIGFMNYARKVGAVGRVNYLQKK----IITYDLIKYDVEKDEPVRDengycvrVPKG--EVGLLVCKITQLtp 434
Cdd:PLN03102 332 GLTEatGPVLFCEWQDEWNRLPENQQMELKarqgVSILGLADVDVKNKETQES-------VPRDgkTMGEIVIKGSSI-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 435 FNGY-AGAKAQTEkkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVY 513
Cdd:PLN03102 403 MKGYlKNPKATSE------AFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVV 474
|
....*
gi 308153494 514 GVHVP 518
Cdd:PLN03102 475 AMPHP 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
67-572 |
4.15e-09 |
|
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: 59.02 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 147 FQCCGAKVLLVSPElqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfsTPALYIYTS 226
Cdd:cd17650 80 LEDSGAKLLLTQPE---------------------------------------------------------DLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 227 GTTGLPKAAMITHQriwygtglTFVSGLKADDVIYITLPFYHSAALLIGIH---------GCIVAGATLAL---RTKFSA 294
Cdd:cd17650 103 GTTGKPKGVMVEHR--------NVAHAAHAWRREYELDSFPVRLLQMASFSfdvfagdfaRSLLNGGTLVIcpdEVKLDP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 295 SQFWDDCRKYNVTVIQYIGELLR----YLCNSPQKPNDRDhkvRLALGNGLRGDVW-RQFVKRFGD-ICIYEFYAATEGN 368
Cdd:cd17650 175 AALYDLILKSRITLMESTPALIRpvmaYVYRNGLDLSAMR---LLIVGSDGCKAQDfKTLAARFGQgMRIINSYGVTEAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 369 IGFMNYARKVGAVGRVNY--LQKKIITYDLIKYDvEKDEPvrdengycvrVPKGEVGLL------VCKitqltpfnGYAG 440
Cdd:cd17650 252 IDSTYYEEGRDPLGDSANvpIGRPLPNTAMYVLD-ERLQP----------QPVGVAGELyiggagVAR--------GYLN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 441 AKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHvpDH 520
Cdd:cd17650 313 RPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRE--DK 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 308153494 521 EGRIGMASIKMKEnHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 572
Cdd:cd17650 391 GGEARLCAYVVAA-ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-533 |
4.62e-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: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 74 FRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAK 153
Cdd:cd05915 20 GEVHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 154 VLLVSPELQAAVEEILPSLKkddvsiyyvSRTSNTDGIDSFLDKVDEVST-----EPIpeswrSEVTFSTPALYIYTSGT 228
Cdd:cd05915 99 VLLFDPNLLPLVEAIRGELK---------TVQHFVVMDEKAPEGYLAYEEalgeeADP-----VRVPERAACGMAYTTGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 229 TGLPKAAMITHQRIWY---GTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYN 305
Cdd:cd05915 165 TGLPKGVVYSHRALVLhslAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 306 VTVIQYIGELLRYLCNSPQKPNDR-DHKVRLALGNGLRGDVWRQfVKRFGDICIYEFYAATE----GNIGFM-------- 372
Cdd:cd05915 245 VTFTAGVPTVWLALADYLESTGHRlKTLRRLVVGGSAAPRSLIA-RFERMGVEVRQGYGLTEtspvVVQNFVkshlesls 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 373 -NYARKVGAVGRVNYLQKKIITYDLIKYDVEKDepvrdenGYCVRvpkgevgllVCKITQLTPFNGYAGAKAQTEKKKLR 451
Cdd:cd05915 324 eEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKD-------GKALG---------EVQLKGPWITGGYYGNEEATRSALTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 452 dvfkkGDLYFnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIK 530
Cdd:cd05915 388 -----DGFFR-TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA--IPHPKwQERPLAVVV 459
|
...
gi 308153494 531 MKE 533
Cdd:cd05915 460 PRG 462
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
77-287 |
8.39e-09 |
|
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: 58.25 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05932 5 VEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VS-----PELQAAVEEILPSlkkddVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESwrsevtfSTPALYIYTSGTTGL 231
Cdd:cd05932 84 VGklddwKAMAPGVPEGLIS-----ISLPPPSAANCQYQWDDLIAQHPPLEERPTRFP-------EQLATLIYTSGTTGQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 232 PKAAMITHQRI-WYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLA 287
Cdd:cd05932 152 PKGVMLTFGSFaWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA 208
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-242 |
1.09e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 47 GKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK05691 2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILK 2260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEiLPSlkkddvsiyYVSRTSNTDgiDSFLdkVDEVSTEPI 206
Cdd:PRK05691 2261 AGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE-LPA---------GVARWCLED--DAAA--LAAYSDAPL 2326
|
170 180 190
....*....|....*....|....*....|....*....
gi 308153494 207 PeswrsevTFSTP---ALYIYTSGTTGLPKAAMITHQRI 242
Cdd:PRK05691 2327 P-------FLSLPqhqAYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
223-575 |
1.61e-08 |
|
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: 56.74 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITH-QRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDC 301
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHrQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 302 RKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFVKR----FGDICIYEFYAATEGNIGFMnyark 377
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGA--ATVPVELVRRmrseLGFETVLTAYGLTEAGVATM----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 378 vgavgrvnylqkkiitydlikydVEKDEPVRDENGYCVR---------VPKGEVGLLVCKITQltpfnGYAGAKAQTEKK 448
Cdd:cd17638 159 -----------------------CRPGDDAETVATTCGRacpgfevriADDGEVLVRGYNVMQ-----GYLDDPEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 449 klrdvfKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMA 527
Cdd:cd17638 211 ------IDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKA 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 308153494 528 SIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRK 575
Cdd:cd17638 283 FVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
52-256 |
2.38e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 57.11 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 52 ARTILRAflekarQTPHKPFLLFRDET-----LTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK03584 89 AENLLRH------RRDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNIPETVVAMLATAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP---------ELQAAVEEI---LPSLKKDdVSIYYVSRTSNTDGIDSF 194
Cdd:PRK03584 162 LGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELraaLPSLEHV-VVVPYLGPAAAAAALPGA 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153494 195 LDKVDEVSTEPIPESWRSEVTFSTPaLYI-YTSGTTGLPKAamITHqriwyGTGLTFVSGLKA 256
Cdd:PRK03584 241 LLWEDFLAPAEAAELEFEPVPFDHP-LWIlYSSGTTGLPKC--IVH-----GHGGILLEHLKE 295
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-561 |
2.63e-08 |
|
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: 56.42 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAyvwLW---LGLVKLGCAMaclnynIRAKSLLHcfqccgakvl 155
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVE---LWeamLAAMKLGAVV------IPATTLLT---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 156 lvspelqaaveeilPSLKKDDVSIYYVSRTSntdgidsfldkVDEVSTEpipeswrsevtfSTPALYIYTSGTTGLPKAA 235
Cdd:cd05974 61 --------------PDDLRDRVDRGGAVYAA-----------VDENTHA------------DDPMLLYFTSGTTSKPKLV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 236 MITHQRIWYGTGLT-FVSGLKADDV-IYITLPFYHSAALligihGCIVA----GATLAL--RTKFSASQFWDDCRKYNVT 307
Cdd:cd05974 104 EHTHRSYPVGHLSTmYWIGLKPGDVhWNISSPGWAKHAW-----SCFFApwnaGATVFLfnYARFDAKRVLAALVRYGVT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 308 VIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQfVKRFGDICIYEFYAATEGNIGFMN---YARKVGAVGRv 384
Cdd:cd05974 179 TLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQ-VRRAWGLTIRDGYGQTETTALVGNspgQPVKAGSMGR- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 385 nylqkkiityDLIKYDVEKDEPVRDEngycvrVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKkklrdvfKKGDLYFNSG 464
Cdd:cd05974 257 ----------PLPGYRVALLDPDGAP------ATEGEVALDLGDTRPVGLMKGYAGDPDKTAH-------AMRGGYYRTG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 465 DLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHEgRIGM--ASIKMKENHEFD---G 539
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPDPV-RLSVpkAFIVLRAGYEPSpetA 390
|
490 500
....*....|....*....|..
gi 308153494 540 KKLFQHIADYLPSYARPRFLRI 561
Cdd:cd05974 391 LEIFRFSRERLAPYKRIRRLEF 412
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
67-268 |
3.40e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.54 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 67 PHKPFllfrdeTLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNE----PAYVWLWLglvkLGCAMACLNYNIR--- 139
Cdd:PRK07768 24 PDAPV------RHTWGEVHERARRIAGGLAAA-GVGPGDAVAVLAGAPveiaPTAQGLWM----RGASLTMLHQPTPrtd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 140 ----AKSLLHCFQCCGAKVLLVSPELQAAVeeilPSLKKDDVSIYYVSrtsntdgidsflDKVDEVSTEPIpeswrsEVT 215
Cdd:PRK07768 93 lavwAEDTLRVIGMIGAKAVVVGEPFLAAA----PVLEEKGIRVLTVA------------DLLAADPIDPV------ETG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 216 FSTPALYIYTSGTTGLPKAAMITHQRIWY-GTGLTFVSGLKAD-DVIYITLPFYH 268
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYAnAEAMFVAAEFDVEtDVMVSWLPLFH 205
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
77-268 |
4.23e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 56.33 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPELQAAVEEILPSLKK---------DDVSIYYVSRTSNTDgIDSFLDKVDEVSTEpipESWrSEVTFSTPALYIYTSG 227
Cdd:PRK05620 117 ADPRLAEQLGEILKECPCvravvfigpSDADSAAAHMPEGIK-VYSYEALLDGRSTV---YDW-PELDETTAAAICYSTG 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 308153494 228 TTGLPKAAMITHQRIWYGTgltfvSGLKADDVIYIT--------LPFYH 268
Cdd:PRK05620 192 TTGAPKGVVYSHRSLYLQS-----LSLRTTDSLAVThgesflccVPIYH 235
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
77-281 |
5.11e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 55.68 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMgnepAYVWLWLgLVKLGCAM-----ACLNYNIRAKSLLHCFQCCG 151
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLV-ELGLKPGDKVAIFA----ETRAEWL-ITALGCWSqnipiVTVYATLGEDALIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 152 AKVLLVSPelqaaveeilpslKKDDVsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfstpALYIYTSGTTGL 231
Cdd:cd17639 78 CSAIFTDG-------------KPDDL------------------------------------------ACIMYTSGSTGN 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 232 PKAAMITHQRIWYG-TGLTF-VSGLKADDVIYIT-LPFYH----SAALLIGIHGCIV 281
Cdd:cd17639 103 PKGVMLTHGNLVAGiAGLGDrVPELLGPDDRYLAyLPLAHifelAAENVCLYRGGTI 159
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
54-578 |
1.05e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.01 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDET--LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQ-SVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKddVSIYYVSRTSNTDGIDSFLDkVDEVSTEPipeswr 211
Cdd:PRK05857 94 VMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHS--IPVIAVDIAAVTRESEHSLD-AASLAGNA------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 212 sEVTFSTPALYIYTSGTTGLPKAAMITHQR------IWYGTGLTFVSGLkADDVIYITLPFYHSAAL---LIGI-HG--C 279
Cdd:PRK05857 165 -DQGSEDPLAMIFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWV-VGETTYSPLPATHIGGLwwiLTCLmHGglC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 280 IVAGA-TLALRTKFSASQFWDDCrkynvtviqYIGELLRYLCNSPQKPNDRDHKVRLALGNGLR---GDVwrQFVKRFGd 355
Cdd:PRK05857 243 VTGGEnTTSLLEILTTNAVATTC---------LVPTLLSKLVSELKSANATVPSLRLVGYGGSRaiaADV--RFIEATG- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 356 ICIYEFYAATE------------GNIGFMnyarKVGAVGRVnylQKKIITYdlikydvekdepVRDENGYCVRVPKG--- 420
Cdd:PRK05857 311 VRTAQVYGLSEtgctalclptddGSIVKI----EAGAVGRP---YPGVDVY------------LAATDGIGPTAPGAgps 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 421 -EVGLLVCKitqlTPFN--GYAGAKAQTekkklRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEV 497
Cdd:PRK05857 372 aSFGTLWIK----SPANmlGYWNNPERT-----AEVLIDG--WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 498 ADTVGLVDFVQEVNVYgvHVPDHE--GRIGMASIKMKENHEFDGKKLFQHIADYL----PSYARPRFLRIQDTIEITGTF 571
Cdd:PRK05857 441 DRIAEGVSGVREAACY--EIPDEEfgALVGLAVVASAELDESAARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSG 518
|
....*..
gi 308153494 572 KHRKMTL 578
Cdd:PRK05857 519 KVMRASL 525
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
80-271 |
1.37e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 54.37 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP 159
Cdd:PRK06018 41 TYAQIHDRALKVSQAL-DRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 160 ELQAAVEEILPSLKKDDVSIYYVSRT-------SNTDGIDSFLDKVDEVStepipeSWRsevTF--STPALYIYTSGTTG 230
Cdd:PRK06018 120 TFVPILEKIADKLPSVERYVVLTDAAhmpqttlKNAVAYEEWIAEADGDF------AWK---TFdeNTAAGMCYTSGTTG 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 308153494 231 LPKAAMITHQRIWYGTGLTF---VSGLKADDVIYITLPFYHSAA 271
Cdd:PRK06018 191 DPKGVLYSHRSNVLHALMANngdALGTSAADTMLPVVPLFHANS 234
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
63-256 |
1.68e-07 |
|
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: 54.20 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDET-----LTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd05943 78 RHADADDPAAIYAAEDgerteVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLL-------------VSPELQAAVEEiLPSLKKDdVSIYYVSRTSNTDG--IDSFLDKVDEVS 202
Cdd:cd05943 157 FGVPGVLDRFGQIEPKVLFavdaytyngkrhdVREKVAELVKG-LPSLLAV-VVVPYTVAAGQPDLskIAKALTLEDFLA 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 203 TEPIPESWRSEVTFSTPaLYI-YTSGTTGLPKAamITHqriwyGTGLTFVSGLKA 256
Cdd:cd05943 235 TGAAGELEFEPLPFDHP-LYIlYSSGTTGLPKC--IVH-----GAGGTLLQHLKE 281
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
59-239 |
1.94e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 53.86 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 139 RAKSLLHCFQCCGAKVLLVSPElqaaveeilpslkkddvsiyyvsrtsntdgidsfldkvdevstepipeswrsevtfsT 218
Cdd:cd12115 84 PPERLRFILEDAQARLVLTDPD---------------------------------------------------------D 106
|
170 180
....*....|....*....|.
gi 308153494 219 PALYIYTSGTTGLPKAAMITH 239
Cdd:cd12115 107 LAYVIYTSGSTGRPKGVAIEH 127
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
54-283 |
2.82e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 54 TILRAFLEKARQTPHKPFLLFRDET------LTYAQVDRRSNQVARALHDHLGLrqGDCVALLMGNEPAYVWLWLGLVKL 127
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 128 GcAMACLNYNIRA------KSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVsrtsntDGIDSFLdkvdev 201
Cdd:PRK05691 88 G-VIAVPAYPPESarrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCV------DTLDPAL------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 202 stepiPESWRS-EVTFSTPALYIYTSGTTGLPKAAMITH-------QRIWYGTGLTfvsgLKADDVIYITLPFYHSAALL 273
Cdd:PRK05691 155 -----AEAWQEpALQPDDIAFLQYTSGSTALPKGVQVSHgnlvaneQLIRHGFGID----LNPDDVIVSWLPLYHDMGLI 225
|
250
....*....|
gi 308153494 274 IGIHGCIVAG 283
Cdd:PRK05691 226 GGLLQPIFSG 235
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
59-323 |
3.14e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 53.31 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PLN02479 25 FLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEE---ILPSLKKDDVS----IYYVSRTSNTDGI-----------DSFLDKVD 199
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEalkILAEKKKSSFKppllIVIGDPTCDPKSLqyalgkgaieyEKFLETGD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 200 -EVSTEPIPESWRSevtfstPALYiYTSGTTGLPKAAMITHqRIWYGTGLT--FVSGLKADDVIYITLPFYHSAALLIGI 276
Cdd:PLN02479 184 pEFAWKPPADEWQS------IALG-YTSGTTASPKGVVLHH-RGAYLMALSnaLIWGMNEGAVYLWTLPMFHCNGWCFTW 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 308153494 277 HGCIVAGATLALRtKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSP 323
Cdd:PLN02479 256 TLAALCGTNICLR-QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAP 301
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
63-308 |
3.26e-07 |
|
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: 53.33 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLF------RDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd05966 63 LKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 137 NIRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEIL---PSLKKDDVsiyyVSRTSN----TDGIDSFLDK-VD 199
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALekcPSVEKVLV----VKRTGGevpmTEGRDLWWHDlMA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 200 EVSTEPIPESWRSEvtfsTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTF--VSGLKADDVI-------YITlpfYHSa 270
Cdd:cd05966 218 KQSPECEPEWMDSE----DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFkyVFDYHPDDIYwctadigWIT---GHS- 289
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 308153494 271 allIGIHGCIVAGATLALR----TKFSASQFWDDCRKYNVTV 308
Cdd:cd05966 290 ---YIVYGPLANGATTVMFegtpTYPDPGRYWDIVEKHKVTI 328
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
204-286 |
1.24e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 51.14 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 204 EPIPESwrsevtfstPALYIYTSGTTGLPKAAMITHQRIWYG-TGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVA 282
Cdd:PRK07787 124 EPDPDA---------PALIVYTSGTTGPPKGVVLSRRAIAADlDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRI 194
|
....
gi 308153494 283 GATL 286
Cdd:PRK07787 195 GNRF 198
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
80-288 |
1.71e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.86 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 80 TYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP 159
Cdd:PRK07008 41 TYRDCERRAKQLAQAL-AALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 160 ELQAAVEEILPSLKkddvsiyyvsrtsNTDGIDSFLDKvDEVSTEPIP----ESW--RSEVTFSTPAL-------YIYTS 226
Cdd:PRK07008 120 TFLPLVDALAPQCP-------------NVKGWVAMTDA-AHLPAGSTPllcyETLvgAQDGDYDWPRFdenqassLCYTS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308153494 227 GTTGLPKAAMITHQRIW---YGTGLTFVSGLKADDVIYITLPFYHSAALliGI-HGCIVAGATLAL 288
Cdd:PRK07008 186 GTTGNPKGALYSHRSTVlhaYGAALPDAMGLSARDAVLPVVPMFHVNAW--GLpYSAPLTGAKLVL 249
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
76-521 |
4.45e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 49.90 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMgnePAYVWL---WLGLVKLGCAMACLNYNIRAKSLLHCFQCCGA 152
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKD-VGVKKGDAVVIYL---PMLMELpiaMLACARIGAVHSVVFAGFSAESLAQRIVDCKP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 153 KVLLVSP---------ELQAAVEEILPSLKKDDVSIYYVSRTSN-----------TDGIDSFLDkvDEVSTEPI--PESW 210
Cdd:PLN02654 194 KVVITCNavkrgpktiNLKDIVDAALDESAKNGVSVGICLTYENqlamkredtkwQEGRDVWWQ--DVVPNYPTkcEVEW 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 211 rseVTFSTPALYIYTSGTTGLPKAAMITH--QRIWYGTGLTFVSGLKADDVIYITLP----FYHSAAlligIHGCIVAGA 284
Cdd:PLN02654 272 ---VDAEDPLFLLYTSGSTGKPKGVLHTTggYMVYTATTFKYAFDYKPTDVYWCTADcgwiTGHSYV----TYGPMLNGA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 285 TLAL----RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRL----ALGNGLRGDVWRQFVKRFGDI 356
Cdd:PLN02654 345 TVLVfegaPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLrvlgSVGEPINPSAWRWFFNVVGDS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 357 -C-IYEFYAATEGNiGFM------NYARKVGAVGRVNYLQKKIITydlikydvekDEPVRDENGYCvrvpkgeVGLLVCK 428
Cdd:PLN02654 425 rCpISDTWWQTETG-GFMitplpgAWPQKPGSATFPFFGVQPVIV----------DEKGKEIEGEC-------SGYLCVK 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 429 ITQLTPFNGYAGAKAQTEKKklrdVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQ 508
Cdd:PLN02654 487 KSWPGAFRTLYGDHERYETT----YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCA 562
|
490
....*....|...
gi 308153494 509 EVNVYGVhvpDHE 521
Cdd:PLN02654 563 EAAVVGI---EHE 572
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
53-283 |
2.95e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKPFLLFRD---------ETLTYAQVDRRSNQVARALHDHLglRQGDCVALLMGNEPAYVWLWLG 123
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 124 LVKLGCAMACLN---YNIRAKSLLHCFQCCGAKVLLVSpelqAAVEeilpslkkDDVSIYYVSRTSNTDG----IDSF-L 195
Cdd:PRK05850 79 ALQAGLIAVPLSvpqGGAHDERVSAVLRDTSPSVVLTT----SAVV--------DDVTEYVAPQPGQSAPpvieVDLLdL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 196 DKVDEVSTEPIPESWrsevtfstPALYIYTSGTTGLPKAAMITHQ----------RIWYG-------TGLTFVSglkadd 258
Cdd:PRK05850 147 DSPRGSDARPRDLPS--------TAYLQYTSGSTRTPAGVMVSHRnvianfeqlmSDYFGdtggvppPDTTVVS------ 212
|
250 260
....*....|....*....|....*
gi 308153494 259 viyiTLPFYHSAALLIGIHGCIVAG 283
Cdd:PRK05850 213 ----WLPFYHDMGLVLGVCAPILGG 233
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
63-370 |
4.18e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.53 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRL-TRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 143 LLHCFQCCGAKVLLVSPElqaaveeilpslkkddvsiyYVSRTSNTDgiDSFLdkVDEVSTEPIPESWRSEVTFSTPALY 222
Cdd:PRK13383 124 LAAALRAHHISTVVADNE--------------------FAERIAGAD--DAVA--VIDPATAGAEESGGRPAVAAPGRIV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 223 IYTSGTTGLPKAAMITHQ-RIWYGTGLTFV--SGLKADDVIYITLPFYHSAALLIgIHGCIVAGATLALRTKFSASQFWD 299
Cdd:PRK13383 180 LLTSGTTGKPKGVPRAPQlRSAVGVWVTILdrTRLRTGSRISVAMPMFHGLGLGM-LMLTIALGGTVLTHRHFDAEAALA 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308153494 300 DCRKYNVTVIQYIGELLRYLCNSPQKPNDRD--HKVRLALGNGLRGD--VWRQFVKRFGDIcIYEFYAATEGNIG 370
Cdd:PRK13383 259 QASLHRADAFTAVPVVLARILELPPRVRARNplPQLRVVMSSGDRLDptLGQRFMDTYGDI-LYNGYGSTEVGIG 332
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
79-268 |
4.61e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.63 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEP----------AY----VWLW--LG------------LVKLGCA 130
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLV-QHGIPKGACVGLYFINRPewlivdhacsAYsyvsVPLYdtLGpdavkfivnhaeVAAIFCV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 131 MACLNynirakSLLHCF-QCCGAKVLLVSpelqAAVEEILPSL-KKDDVSIYYVSRTSNtdgidsfldkvdevstepipE 208
Cdd:PLN02736 158 PQTLN------TLLSCLsEIPSVRLIVVV----GGADEPLPSLpSGTGVEIVTYSKLLA--------------------Q 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153494 209 SWRSEVTFSTP-----ALYIYTSGTTGLPKAAMITHQR-IWYGTGLTFVSGLKADDViYIT-LPFYH 268
Cdd:PLN02736 208 GRSSPQPFRPPkpedvATICYTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDV-HISyLPLAH 273
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
77-288 |
4.62e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 46.65 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAyvWLwLGLvklgcaMACLNYNIRA---------KSLLHCF 147
Cdd:PLN02387 105 EWITYGQVFERVCNFASGLV-ALGHNKEERVAIFADTRAE--WL-IAL------QGCFRQNITVvtiyaslgeEALCHSL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 148 Q-------CCGAKvllvspELQ--AAVEEILPSLKK-----DDVSIYYVSRTSNTDGIDSFLDKVDEVSTE-PIPESWRS 212
Cdd:PLN02387 175 NetevttvICDSK------QLKklIDISSQLETVKRviymdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKEnPVDPDLPS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 213 EvtfSTPALYIYTSGTTGLPKAAMITHQRIWYGTG--LTFVSGLKADDVIYITLPFYH-----SAALLIGIHGCIVAGAT 285
Cdd:PLN02387 249 P---NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgvMTVVPKLGKNDVYLAYLPLAHilelaAESVMAAVGAAIGYGSP 325
|
...
gi 308153494 286 LAL 288
Cdd:PLN02387 326 LTL 328
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
79-242 |
5.06e-05 |
|
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: 46.05 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 79 LTYAQVDRRSNQVARALHdHLGLRQ--GDCVALLMGNEPayvwLWLGlvklgCAMACLNYNIRAKSLLHCfqccgakvll 156
Cdd:cd05927 6 ISYKEVAERADNIGSALR-SLGGKPapASFVGIYSINRP----EWII-----SELACYAYSLVTVPLYDT---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 157 VSPElqaAVEEILpslKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPeswrsevtfSTP---ALYIYTSGTTGLPK 233
Cdd:cd05927 66 LGPE---AIEYIL---NHAEISIVFCDAGVKVYSLEEFEKLGKKNKVPPPP---------PKPedlATICYTSGTTGNPK 130
|
....*....
gi 308153494 234 AAMITHQRI 242
Cdd:cd05927 131 GVMLTHGNI 139
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
78-239 |
6.49e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.12 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDhLGLRQGDCVALlmgnepaYV---WLWLGLVkLGC----AMACLNY-NIRAKSLLHCFQ- 148
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAE-LGLTKGSNVAI-------YEetrWEWLASI-YGIwsqsMVAATVYaNLGEDALAYALRe 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 149 -------CCGAKV-----LLVSPELQAAV----EEILPSLKKDDVSIYyvsrtsntdgidSFLDKVD----EVSTEPIPE 208
Cdd:PTZ00216 192 teckaivCNGKNVpnllrLMKSGGMPNTTiiylDSLPASVDTEGCRLV------------AWTDVVAkghsAGSHHPLNI 259
|
170 180 190
....*....|....*....|....*....|.
gi 308153494 209 SWRSEVTfstpALYIYTSGTTGLPKAAMITH 239
Cdd:PTZ00216 260 PENNDDL----ALIMYTSGTTGDPKGVMHTH 286
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
53-275 |
3.22e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 43.80 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 53 RTILRAFLEKARQTPHKpFLLFRD---ETLTYAQVDRRSNQVARALHDhlGLRQGDCVALLMGNEPAYVWLWLGLVKLGC 129
Cdd:PRK06814 631 RTLFEALIEAAKIHGFK-KLAVEDpvnGPLTYRKLLTGAFVLGRKLKK--NTPPGENVGVMLPNANGAAVTFFALQSAGR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 130 AMACLNYNIRAKSLLHCFQCCGAKVLLVSPEL--QAAVEEILPSLKKDdVSIYYVSRTSNtdGIdSFLDKVDEVSTepip 207
Cdd:PRK06814 708 VPAMINFSAGIANILSACKAAQVKTVLTSRAFieKARLGPLIEALEFG-IRIIYLEDVRA--QI-GLADKIKGLLA---- 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308153494 208 eSWRSEVTFST-----PALYIYTSGTTGLPKAAMITHQRIWYGTG-LTFVSGLKADDVIYITLPFYHSAALLIG 275
Cdd:PRK06814 780 -GRFPLVYFCNrdpddPAVILFTSGSEGTPKGVVLSHRNLLANRAqVAARIDFSPEDKVFNALPVFHSFGLTGG 852
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| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
78-279 |
6.92e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 42.72 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 78 TLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLv 157
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAL- 92
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153494 158 spelqaAVEEILPSLKKDdvsiyyVSRTSNTDGIDSFLD--KVDEVSTepIPESWRSEVTFSTP---------ALYIYTS 226
Cdd:cd05905 93 ------TVEACLKGLPKK------LLKSKTAAEIAKKKGwpKILDFVK--IPKSKRSKLKKWGPhpptrdgdtAYIEYSF 158
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 308153494 227 GTTG------LPKAAMITHQRIwygtgLTFVSGLKADDVIYITLPFYHSAALligIHGC 279
Cdd:cd05905 159 SSDGslsgvaVSHSSLLAHCRA-----LKEACELYESRPLVTVLDFKSGLGL---WHGC 209
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