|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
138-592 |
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: 798.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 138 PGAGSVTFGELDARACQAAWALKAELGdpasLCAGEPTALLVLASQAvpALCMWLGLAKLGCPTAWINPHGRGMPLAHSV 217
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAG----LRPGDTVALLLGNEPA--FLWIWLGLAKLGCPVAFLNTNIRSKSLLHCF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 218 LSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSG 297
Cdd:cd05938 75 RCCGAKVLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 298 TTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVT 377
Cdd:cd05938 155 TTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 378 VILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCL 457
Cdd:cd05938 235 VIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 458 LRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVL 537
Cdd:cd05938 315 YKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 538 AMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGRHG 592
Cdd:cd05938 395 VQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEG 449
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
87-593 |
1.63e-167 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 490.16 E-value: 1.63e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 87 LPADVIFLAKILhLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQ-AAWALKAELGd 165
Cdd:PRK08279 11 LPRRLPDLPGIL-RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFED---QSISYAELNARANRyAHWAAARGVG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 166 paslcAGEPTALLVLASqavPALCM-WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQA 244
Cdd:PRK08279 86 -----KGDVVALLMENR---PEYLAaWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 245 ENIRCFYLSHTSPTP-GVGALGAALDAAPSHPVPAdlRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS- 322
Cdd:PRK08279 158 PPRLWVAGGDTLDDPeGYEDLAAAAAGAPTTNPAS--RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 323 GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHT 402
Cdd:PRK08279 236 RLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 403 VRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKmsCLLRMLSPFELVQFDMEAAEPVRDNQG 482
Cdd:PRK08279 316 LRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGR--VPLWLAHPYAIVKYDVDTGEPVRDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 483 FCIPVGLGEPGLLLTKVVSQQPFVGYRGPrELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENV 562
Cdd:PRK08279 394 RCIKVKPGEVGLLIGRITDRGPFDGYTDP-EASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENV 472
|
490 500 510
....*....|....*....|....*....|.
gi 768006055 563 STHEVEGVLSQVDFLQQVNVYGVCVPGrHGG 593
Cdd:PRK08279 473 ATTEVENALSGFPGVEEAVVYGVEVPG-TDG 502
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
144-592 |
5.76e-150 |
|
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: 439.87 E-value: 5.76e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAElgdpaSLCAGEPTALLVLASQAVPALcmWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGAR 223
Cdd:cd05940 5 TYAELDAMANRYARWLKSL-----GLKPGDVVALFMENRPEYVLL--WLGLVKIGAVAALINYNLRGESLAHCLNVSSAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 224 VLVVDpdlresleeilpklqaeniRCFYlshtsptpgvgalgaaldaapshpvpadlragitwrspalfIYTSGTTGLPK 303
Cdd:cd05940 78 HLVVD-------------------AALY-----------------------------------------IYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 304 PAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYV 382
Cdd:cd05940 98 AAIISHRRAWRGGAFFaGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 383 GELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLS 462
Cdd:cd05940 178 GELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 463 PFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRElSERKLVRNVRQSGDVYYNTGDVLAMDRE 542
Cdd:cd05940 258 PLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGE 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006055 543 GFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGRHG 592
Cdd:cd05940 337 GFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDG 386
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
144-592 |
1.53e-131 |
|
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: 393.71 E-value: 1.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAElgdpaSLCAGEPTALLVLASQAVPALcmWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGAR 223
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQ-----GYRSGDVVALFMENRLEFVAL--WLGLAKIGVETALINSNLRLESLLHCITVSKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 224 VLVVD--PDLRESLEEILPKLQAENircfylshtsptpgvgalgaaldaapshpvpadlragitWRSPALFIYTSGTTGL 301
Cdd:cd05939 78 ALIFNllDPLLTQSSTEPPSQDDVN---------------------------------------FRDKLFYIYTSGTTGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 302 PKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVIL 380
Cdd:cd05939 119 PKAAVIVHSRYYRIAAGAYYAfGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 381 YVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRM 460
Cdd:cd05939 199 YIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 461 LSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQP---FVGYRGPRElSERKLVRNVRQSGDVYYNTGDVL 537
Cdd:cd05939 279 VYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGA-TNKKIARDVFKKGDSAFLSGDVL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 538 AMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGRHG 592
Cdd:cd05939 358 VMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEG 412
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
144-592 |
6.60e-109 |
|
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: 335.17 E-value: 6.60e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAELGdpasLCAGEPTALLVLASqavPALCM-WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGA 222
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLG----VQAGDFVAIDLTNS---PEFVFlWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 223 RVLVVDPDlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragitwrSPALFIYTSGTTGLP 302
Cdd:cd05937 80 RFVIVDPD---------------------------------------------------------DPAILIYTSGTTGLP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 303 KPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILY 381
Cdd:cd05937 103 KAAAISWRRTLVTSNLLShDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 382 VGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNY-VG--RCGALGKMSCLL 458
Cdd:cd05937 183 VGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGdfGAGAIGHHGLIR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 459 RMLSPFE--LVQFDMEAAEPVRDNQ-GFCIPVGLGEPGLLLTKV--VSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNT 533
Cdd:cd05937 263 RWKFENQvvLVKMDPETDDPIRDPKtGFCVRAPVGEPGEMLGRVpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 534 GDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGRHG 592
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDG 401
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
116-585 |
1.84e-67 |
|
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: 226.62 E-value: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 116 FVDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALkAELGdpasLCAGEPTAllVLASQAVPALCMWLGLA 195
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG---RRLTYAELDARARRLAAAL-RALG----VGPGDRVA--LLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 196 KLGCPTAWINPHGRGMPLAHSVLSSGARVLVVdpdlresleeilpklqaenircfylshtsptpgvgalgaaldaapshp 275
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 276 vpadlragitwrspALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGA 354
Cdd:COG0318 103 --------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAlGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 355 TCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVY 432
Cdd:COG0318 169 TLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 433 GSTEGNM--------GLVNYVGRCGalgkmscllrmlspfeLVQFDMEAAepVRDNQGfcIPVGLGEPGLLLTKvvSQQP 504
Cdd:COG0318 248 GLTETSPvvtvnpedPGERRPGSVG----------------RPLPGVEVR--IVDEDG--RELPPGEVGEIVVR--GPNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 505 FVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:COG0318 306 MKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVG 378
|
.
gi 768006055 585 V 585
Cdd:COG0318 379 V 379
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-585 |
2.23e-65 |
|
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: 220.24 E-value: 2.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALkAELGDPaslcagEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGAR 223
Cdd:cd05934 5 TYAELLRESARIAAAL-AALGIR------PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 224 VLVVDPdlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragitwrspALFIYTSGTTGLPK 303
Cdd:cd05934 78 LVVVDP------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 304 PAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYV 382
Cdd:cd05934 98 GVVITHANLTFAGYySARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 383 GELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVGrcGALGKMSCLLRMls 462
Cdd:cd05934 178 GAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGPRD--EPRRPGSIGRPA-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 463 pfelvqFDMEAAepVRDNQGFCIPVglGEPG-LLLTKVVSQQPFVGYRGpRELSERKLVRNvrqsgdVYYNTGDVLAMDR 541
Cdd:cd05934 253 ------PGYEVR--IVDDDGQELPA--GEPGeLVIRGLRGWGFFKGYYN-MPEATAEAMRN------GWFHTGDLGYRDA 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 768006055 542 EGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAV 359
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
121-585 |
1.39e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 207.69 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 121 ERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLvlASQAVPALCMWLGLAKLGCP 200
Cdd:PRK06155 28 ARQAERYPDRPLLVF---GGTRWTYAEAARAAAAAAHALAA-----AGVKRGDRVALM--CGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 201 TAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAenIRCFYLSHTSPTPGVGALGAALDAAPS-HPVPAd 279
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLP--LPAVWLLDAPASVSVPAGWSTAPLPPLdAPAPA- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 lrAGITWRSPALFIYTSGTTGLPKPAILTHERV----LQMSKMLslsGATADDVVYTVLPLYHVMGLVVGILGCLDlGAT 355
Cdd:PRK06155 175 --AAVQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDL---EIGADDVLYTTLPLFHTNALNAFFQALLA-GAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 356 CVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGST 435
Cdd:PRK06155 249 YVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 436 EGN--MGLVNYVGRCGALGkmscllRMLSPFELVQFDmEAAEPVRDnqgfcipvglGEPGLLLtkVVSQQPFV---GYRG 510
Cdd:PRK06155 328 ETNfvIAVTHGSQRPGSMG------RLAPGFEARVVD-EHDQELPD----------GEPGELL--LRADEPFAfatGYFG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 511 PRElserKLVRNVRqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK06155 389 MPE----KTVEAWR---NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
120-558 |
6.87e-54 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 189.06 E-value: 6.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRAllVWTGPGAGSVTFGELDARACQAAWALKA---ELGDPASLCAgEPTALLVLAsqavpalcmWLGLAK 196
Cdd:pfam00501 1 LERQAARTPDKT--ALEVGEGRRLTYRELDERANRLAAGLRAlgvGKGDRVAILL-PNSPEWVVA---------FLACLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 197 LGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLR-ESLEEILPKLQAenIRCFYLSHTSPTPGVGALGAALDAAPSHP 275
Cdd:pfam00501 69 AGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKlEELLEALGKLEV--VKLVLVLDRDPVLKEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 276 VPADLRAGitwRSPALFIYTSGTTGLPKPAILTHE----RVLQMSKM-LSLSGATADDVVYTVLPLYHVMGLVVGILGCL 350
Cdd:pfam00501 147 PPPPPPDP---DDLAYIIYTSGTTGKPKGVMLTHRnlvaNVLSIKRVrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 351 DLGATCVLAPKFSTSC---FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGP 425
Cdd:pfam00501 224 LAGATVVLPPGFPALDpaaLLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 426 iRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKvvSQQPF 505
Cdd:pfam00501 304 -ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPP----------GEPGELCVR--GPGVM 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 768006055 506 VGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWK 558
Cdd:pfam00501 371 KGYLNDPELTAEAFDE------DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
289-585 |
3.35e-50 |
|
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: 177.09 E-value: 3.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVmGLVVGILGCLDLGATCVLAPKFSTSCF 367
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAaLAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 368 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGN-----MG 440
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPG-IKLVNGYGLTETGgtvatGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 441 LVNYVGRCGALGKmscllrmlsPFELVQFDmeaaepVRDNQGfcIPVGLGEPGLLLTKvvSQQPFVGYRGPRELSERKLv 520
Cdd:cd04433 160 PDDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVR--GPSVMKGYWNNPEATAAVD- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 521 rnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd04433 220 ------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGV 278
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-585 |
9.03e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 172.56 E-value: 9.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 150 ARACQAAWALKAELGDPaslcaGEPTALLVLaSQAVPALCMWLGLAKL-GCPTAWINPHGRGMPLAHSVLSSGARVLVVD 228
Cdd:PRK07867 35 IRGSAARAAALRARLDP-----TRPPHVGVL-LDNTPEFSLLLGAAALsGIVPVGLNPTRRGAALARDIAHADCQLVLTE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 229 PDLRESLEEILPKLQAENIRC-FYLSHTSPTPGVGALgaaldaaPSHPVPADLragitwrspALFIYTSGTTGLPKPAIL 307
Cdd:PRK07867 109 SAHAELLDGLDPGVRVINVDSpAWADELAAHRDAEPP-------FRVADPDDL---------FMLIFTSGTSGDPKAVRC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 308 THERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELL 386
Cdd:PRK07867 173 THRKVASAGVMLAQRfGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 387 RYLCNIPQQPEDRTHTVRLAMGN-GLRADVwETFQQRFGpIRIWEVYGSTEGNMGLVNYVG-RCGALGKMSCLLRMLSPf 464
Cdd:PRK07867 253 SYVLATPERPDDADNPLRIVYGNeGAPGDI-ARFARRFG-CVVVDGFGSTEGGVAITRTPDtPPGALGPLPPGVAIVDP- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 465 elvqfdmEAAEPvrdnqgfCIPVGLGEPGLL--------LTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNtgdv 536
Cdd:PRK07867 330 -------DTGTE-------CPPAEDADGRLLnadeaigeLVNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYR---- 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768006055 537 lamDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK07867 392 ---DADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
185-595 |
2.36e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 157.50 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 185 VPALCMWLGLAKL-GCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEI-LPKLQaenircfYLSHTSPtpgvG 262
Cdd:PRK13388 62 TPEMLFWLAAAALgGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLdLPGVR-------VLDVDTP----A 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 263 ALGAALDAAPSHPVPAdlragITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMG 341
Cdd:PRK13388 131 YAELVAAAGALTPHRE-----VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERfGLTRDDVCYVSMPLFHSNA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 342 LVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQ 421
Cdd:PRK13388 206 VMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 422 RFGpIRIWEVYGSTEGNMGLVNYVGR-CGALGKmscllrmlsPFE-LVQFDMEAAEPvrdnqgfCIPVGLGEPGLLLT-- 497
Cdd:PRK13388 286 RFG-CQVEDGYGSSEGAVIVVREPGTpPGSIGR---------GAPgVAIYNPETLTE-------CAVARFDAHGALLNad 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 498 ----KVVSQQ---PFVGY-RGPRELSERklVRNvrqsGDvyYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEG 569
Cdd:PRK13388 349 eaigELVNTAgagFFEGYyNNPEATAER--MRH----GM--YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420
|
410 420
....*....|....*....|....*.
gi 768006055 570 VLSQVDFLQQVNVYGvcVPGRHGGHQ 595
Cdd:PRK13388 421 ILLRHPAINRVAVYA--VPDERVGDQ 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
116-585 |
8.37e-38 |
|
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: 145.78 E-value: 8.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 116 FVDAFERRARAQPGRALLVWTGPgagSVTFGELDARACQAAWALKA---ELGDPASLCAgePTALLVLASqavpalcmWL 192
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGR---KLTYRELDALAEAFAAGLQNlgvQPGDRVALML--PNCPQFPIA--------YF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 193 GLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDpdlrESLEEILpklqaenircfylshtsptpgvgalgaaldaap 272
Cdd:cd05936 68 GALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA----VSFTDLL--------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 273 SHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVL---QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGC 349
Cdd:cd05936 111 AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVanaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 350 LDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIR 427
Cdd:cd05936 191 LALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG-VP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 428 IWEVYGSTE------GNmgLVNYVGRCGALGKmscllrmlsPFElvqfDMEAAepVRDNQGfcIPVGLGEPGLLLTKvvS 501
Cdd:cd05936 270 IVEGYGLTEtspvvaVN--PLDGPRKPGSIGI---------PLP----GTEVK--IVDDDG--EELPPGEVGELWVR--G 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 502 QQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVN 581
Cdd:cd05936 329 PQVMKGYWNRPEETAEAFV-------DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA 401
|
....
gi 768006055 582 VYGV 585
Cdd:cd05936 402 VVGV 405
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-585 |
2.42e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 142.63 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 111 QPPDTFVDAFERRARAQPGRALLVWTGPGagsVTFGELDARACQAAWALKAelgdpASLCAGEPTALLVLASQAvpALCM 190
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRR---TTYAELDERVNRLANALRA-----LGVKKGDRVAVFDWNSHE--YLEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 191 WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLqaENIRCFYLSHTSPTPGVGALGAA--- 267
Cdd:PRK06187 73 YFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQL--PTVRTVIVEGDGPAAPLAPEVGEyee 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 268 -LDAAPSHPVPADLRAgitwRSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVG 345
Cdd:PRK06187 151 lLAAASDTFDFPDIDE----NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLaVCAWLKLSRDDVYLVIVPMFHVHAWGLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 346 ILGcLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRF 423
Cdd:PRK06187 227 YLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 424 GpIRIWEVYGSTEgnmglvnyvgrCGALgkMSCLL----------RMLS---PFELVqfdmEAAepVRDNQGFCIPVGLG 490
Cdd:PRK06187 306 G-IDLVQGYGMTE-----------TSPV--VSVLPpedqlpgqwtKRRSagrPLPGV----EAR--IVDDDGDELPPDGG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 491 EPGLLLTKvvSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:PRK06187 366 EVGEIIVR--GPWLMQGYWNRPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDA 436
|
490
....*....|....*
gi 768006055 571 LSQVDFLQQVNVYGV 585
Cdd:PRK06187 437 LYGHPAVAEVAVIGV 451
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
142-585 |
4.32e-36 |
|
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: 141.58 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 142 SVTFGELDARACQAAWALKAEL---GDPASLCAGEPTALLVLAsqavpalcmwLGLAKLGCPTAWINPHGRGMPLAHSVL 218
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGlkkGDVVGIISPNSTYYPPVF----------LGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPD----LRESLEEILPKlqaENIRCFYlSHTSPTPGVGALGAALDAAPSHPVPADLRAGITwrSPALFIY 294
Cdd:cd05911 80 ISKPKVIFTDPDglekVKEAAKELGPK---DKIIVLD-DKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKD--DTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 295 TSGTTGLPKPAILTHERVLQMSKMLSLS---GATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFWDDC 371
Cdd:cd05911 154 SSGTTGLPKGVCLSHRNLIANLSQVQTFlygNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 372 RQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEG------NMGLVN 443
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILsgGAPLSKELQELLAKRFPNATIKQGYGMTETggiltvNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 444 YVGRCGalgkmscllRMLSPFELVQFDMEaaepvrDNQGfcipVGLGEPGLLLTKvvSQQPFVGY-RGPRELSERklvrn 522
Cdd:cd05911 313 KPGSVG---------RLLPNVEAKIVDDD------GKDS----LGPNEPGEICVR--GPQVMKGYyNNPEATKET----- 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006055 523 vrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05911 367 --FDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGI 427
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
120-585 |
4.90e-34 |
|
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: 134.66 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALkAELGdpasLCAGEPTALLVLASQAvpALCMWLGLAKLGC 199
Cdd:cd17631 1 LRRRARRHPDRTALVFGG---RSLTYAELDERVNRLAHAL-RALG----VAKGDRVAVLSKNSPE--FLELLFAAARLGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 200 PTAWINPHGRGMPLAHSVLSSGARVLVVDPdlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpad 279
Cdd:cd17631 71 VFVPLNFRLTPPEVAYILADSGAKVLFDDL-------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 lragitwrspALFIYTSGTTGLPKPAILTHERVLQMS-KMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 358
Cdd:cd17631 101 ----------ALLMYTSGTTGRPKGAMLTHRNLLWNAvNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 APKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFqQRFGPiRIWEVYGSTE 436
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGV-KFVQGYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 GNMGLV-----NYVGRCGALGK--MSCLLRMLSPfelvqfDMEAAEPvrdnqgfcipvglGEPGLLLtkvvsqqpfvgYR 509
Cdd:cd17631 249 TSPGVTflspeDHRRKLGSAGRpvFFVEVRIVDP------DGREVPP-------------GEVGEIV-----------VR 298
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 510 GPRELSE--RKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17631 299 GPHVMAGywNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGV 376
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
111-585 |
4.35e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 127.33 E-value: 4.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 111 QPPDTFVDAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKA---ELGDPASLCAGEpTALLVLASqavpa 187
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVF---GDQRLTYAELNARVRRAAAALAAlgiGKGDRVAIWAPN-SPHWVIAA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 188 lcmwLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLqaENIRCFYLSHTSPTPGVGALGAA 267
Cdd:PRK07656 73 ----LGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL--PALEHVVICETEEDDPHTEKMKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 268 LDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGI 346
Cdd:PRK07656 147 FTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAAdWAEYLGLTEGDRYLAANPFFHVFGYKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 347 LGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGlrADV----WETFQQR 422
Cdd:PRK07656 227 NAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGA--ASMpvalLERFESE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 423 FGPIRIWEVYGSTEgnmglvnyvgrcgALGkMSCLLRMLSPFELVQ----FDMEAAE-PVRDNQGfcIPVGLGEPGLLLT 497
Cdd:PRK07656 305 LGVDIVLTGYGLSE-------------ASG-VTTFNRLDDDRKTVAgtigTAIAGVEnKIVNELG--EEVPVGEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 498 KvvsqQPFV--GYRG-PRELSErklvrNVRQSGDVYynTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQV 574
Cdd:PRK07656 369 R----GPNVmkGYYDdPEATAA-----AIDADGWLH--TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH 437
|
490
....*....|.
gi 768006055 575 DFLQQVNVYGV 585
Cdd:PRK07656 438 PAVAEAAVIGV 448
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-585 |
7.93e-29 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 120.11 E-value: 7.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 130 RALLVwtGPGAGSVTFGELDARACQAAWALkAELGdpasLCAGEPTALlVLASqAVPALCMWLGLAKLGCPTAWINPHGR 209
Cdd:cd05926 4 PALVV--PGSTPALTYADLAELVDDLARQL-AALG----IKKGDRVAI-ALPN-GLEFVVAFLAAARAGAVVAPLNPAYK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 210 GMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRcfyLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSP 289
Cdd:cd05926 75 KAEFEFYLADLGSKLVLTPKGELGPASRAASKLGLAILE---LALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLqmSKMLSLSGA---TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 366
Cdd:cd05926 152 ALILHTSGTTGRPKGVPLTHRNLA--ASATNITNTyklTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVTVILYVGELLRYLCNIPQ-QPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEgnmglvn 443
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKLRFIRscSASLPPAVLEALEATFG-APVLEAYGMTE------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 444 yvgrcgALGKMSCllrmlSPFelvqfdmeaaEPVRDNQG-FCIPVG-----LGEPGLLLT-----KVVSQQPFV--GYRG 510
Cdd:cd05926 302 ------AAHQMTS-----NPL----------PPGPRKPGsVGKPVGvevriLDEDGEILPpgvvgEICLRGPNVtrGYLN 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 511 PRElserklVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05926 361 NPE------ANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGV 429
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
118-585 |
9.92e-29 |
|
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: 120.17 E-value: 9.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALkAELGdpasLCAGEPTALLVLASQAVPALcmWLGLAKL 197
Cdd:cd05959 8 LVDLNLNEGRGDKTAFID---DAGSLTYAELEAEARRVAGAL-RALG----VKREERVLLIMLDTVDFPTA--FLGAIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 198 GCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRcfyLSHTSPTPGVGALGAALDAAPSHPvp 277
Cdd:cd05959 78 GIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVV---LIVSGGAGPEAGALLLAELVAAEA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 278 ADLRAGITWR-SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGA 354
Cdd:cd05959 153 EQLKPAATHAdDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYArnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 355 TCVLAPKFST-SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEV 431
Cdd:cd05959 233 TTVLMPERPTpAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 432 YGSTE-GNMGLVNYVG--RCGALGKMscllrmlSPFELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKVVSQQPfvGY 508
Cdd:cd05959 312 IGSTEmLHIFLSNRPGrvRYGTTGKP-------VPGYEVELRDEDGGDVAD----------GEPGELYVRGPSSAT--MY 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 509 RGPRELSerklvRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05959 373 WNNRDKT-----RDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGV 442
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
191-585 |
2.72e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 119.02 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 191 WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPK--LQAENIrCFYLSHTSPTPGVGALGAAL 268
Cdd:PRK08008 79 WFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdaTPLRHI-CLTRVALPADDGVSSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 269 DAapsHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGA-TADDVVYTVLPLYHVMGLVVGIL 347
Cdd:PRK08008 158 AQ---QPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCAlRDDDVYLTVMPAFHIDCQCTAAM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 348 GCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR-----LAMGNGLRadvwETFQQR 422
Cdd:PRK08008 235 AAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEER 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 423 FGpIRIWEVYGSTEGNMGLVN----------YVGRCGalgkmscllrmlspfelvqFDMEAAepVRDNQGFCIPVGL--- 489
Cdd:PRK08008 311 FG-VRLLTSYGMTETIVGIIGdrpgdkrrwpSIGRPG-------------------FCYEAE--IRDDHNRPLPAGEige 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 490 ----GEPGLLLTKvvsqqpfvGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTH 565
Cdd:PRK08008 369 icikGVPGKTIFK--------EYYLDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCV 434
|
410 420
....*....|....*....|
gi 768006055 566 EVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK08008 435 ELENIIATHPKIQDIVVVGI 454
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-585 |
6.43e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 117.73 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALkAELGdpasLCAGEPTALLVLASQAVPALcmWLGLAKL 197
Cdd:PRK08316 15 DILRRSARRYPDKTALVF---GDRSWTYAELDAAVNRVAAAL-LDLG----LKKGDRVAALGHNSDAYALL--WLACARA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 198 GCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVP 277
Cdd:PRK08316 85 GAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 278 AdlrAGITWRSPALFIYTSGTTGLPKPAILTHERVLQ--MSKMLSLsGATADDVVYTVLPLYHVMGLVVGILGCLDLGAT 355
Cdd:PRK08316 165 D---VELADDDLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVAG-DMSADDIPLHALPLYHCAQLDVFLGPYLYVGAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 356 CVLAPKFSTSCFWDDCRQHGVTVI-----LYVGeLLRYlcnipqqPEDRTHTVRlamgnGLR----------ADVWETFQ 420
Cdd:PRK08316 241 NVILDAPDPELILRTIEAERITSFfapptVWIS-LLRH-------PDFDTRDLS-----SLRkgyygasimpVEVLKELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 421 QRFGPIRIWEVYGSTEgnMGLVNYV-------GRCGALGKMScllrmlspfelvqFDMEAAepVRDNQGFCIPVglGEPG 493
Cdd:PRK08316 308 ERLPGLRFYNCYGQTE--IAPLATVlgpeehlRRPGSAGRPV-------------LNVETR--VVDDDGNDVAP--GEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 494 llltKVV--SQQPFVGYRGPRELSERKLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PRK08316 369 ----EIVhrSPQLMLGYWDDPEKTAEAF-------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEAL 437
|
490
....*....|....
gi 768006055 572 SQVDFLQQVNVYGV 585
Cdd:PRK08316 438 YTHPAVAEVAVIGL 451
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
289-592 |
8.16e-28 |
|
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: 117.05 E-value: 8.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVL----QMSKMLSlsgATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK-FS 363
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLanveQITAIFD---PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 364 TSCFWDDCRQHGVTVILYVGELLRYLCNiPQQPEDrTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEG---- 437
Cdd:cd05909 226 YKKIPELIYDKKATILLGTPTFLRGYAR-AAHPED-FSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECspvi 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 438 NMGLVNYVGRCGALGKmscllrmlsPFELVQFDMEAAEPVrdnqgfcIPVGLGEPGLLLTKVVSQqpFVGYRGPRELSER 517
Cdd:cd05909 303 SVNTPQSPNKEGTVGR---------PLPGMEVKIVSVETH-------EEVPIGEGGLLLVRGPNV--MLGYLNEPELTSF 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006055 518 KLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVdFLQQVNVYGVCVP-GRHG 592
Cdd:cd05909 365 AF-------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI-LPEDNEVAVVSVPdGRKG 432
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
272-585 |
1.30e-27 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 115.85 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 272 PSHPvPADLRAGIT------WRSPALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVV 344
Cdd:cd05941 69 PSYP-LAELEYVITdsepslVLDPALILYTSGTTGRPKGVVLTHANLAANVRALvDAWRWTEDDVLLHVLPLHHVHGLVN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 345 GILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYV----GELLRYLCNIPQQPEDRT----HTVRLAM-GNG-LRAD 414
Cdd:cd05941 148 ALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVptiyTRLLQYYEAHFTDPQFARaaaaERLRLMVsGSAaLPVP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 415 VWETFQQRFGPiRIWEVYGSTEGNMGLVN-YVG--RCGALGkmscllrmlSPFELVQfdmeaAEPVRDNQGfcIPVGLGE 491
Cdd:cd05941 228 TLEEWEAITGH-TLLERYGMTEIGMALSNpLDGerRPGTVG---------MPLPGVQ-----ARIVDEETG--EPLPRGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 492 PGLLLTKvvSQQPFVGYRGPRELSERKLVrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLG-DTFRWKGENVSTHEVEGV 570
Cdd:cd05941 291 VGEIQVR--GPSVFKEYWNKPEATKEEFT------DDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERV 362
|
330
....*....|....*
gi 768006055 571 LSQVDFLQQVNVYGV 585
Cdd:cd05941 363 LLAHPGVSECAVIGV 377
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
112-575 |
2.11e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 116.75 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 112 PPDTF---VDAFERRARAQPGRALLVWTG-PGAG-SVTFGELDARACQAAWALKAeLGdpasLCAGEptALLVLASQAVP 186
Cdd:COG0365 4 VGGRLniaYNCLDRHAEGRGDKVALIWEGeDGEErTLTYAELRREVNRFANALRA-LG----VKKGD--RVAIYLPNIPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 187 ALCMWLGLAKLGCPTAWINPhgrGM---PLAHSVLSSGARVLVVDP---------DLRESLEEILPKLQA-ENIRCF-YL 252
Cdd:COG0365 77 AVIAMLACARIGAVHSPVFP---GFgaeALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSlEHVIVVgRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 253 SHTSPTPGVGALGAALDAAPSHPVPADLRAGitwrSPALFIYTSGTTGLPKPAILTHeR--VLQMSKMLSLS-GATADDV 329
Cdd:COG0365 154 GADVPMEGDLDWDELLAAASAEFEPEPTDAD----DPLFILYTSGTTGKPKGVVHTH-GgyLVHAATTAKYVlDLKPGDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 330 VYTVLPLYHVMGLVVGILGCLDLGATCVL---APKFST-SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTH--TV 403
Cdd:COG0365 229 FWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFPDpGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlsSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 404 RLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVG----RCGALGKmscllrmlsPFelvqFDMEAAepV 477
Cdd:COG0365 309 RLLGSAGepLNPEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGK---------PV----PGYDVA--V 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 478 RDNQGfcIPVGLGEPGLLltkVVsQQP----FVGYRGPRElserKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGD 553
Cdd:COG0365 373 VDEDG--NPVPPGEEGEL---VI-KGPwpgmFRGYWNDPE----RYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDD 442
|
490 500
....*....|....*....|..
gi 768006055 554 TFRWKGENVSTHEVEGVLSQVD 575
Cdd:COG0365 443 VINVSGHRIGTAEIESALVSHP 464
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
292-591 |
4.40e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 110.58 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 292 FIYTSGTTGLPKPAILTHERvLQMSKMLSLSGATAD--DVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWD 369
Cdd:PRK07868 610 FIAFSTAGGELVAKQITNYR-WALSAFGTASAAALDrrDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQ 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 370 DCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGrcg 449
Cdd:PRK07868 689 EVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSG--- 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 450 alGKMSCLLRML---SPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVvsqqpfvgyRGPRELSErKLVRNVRQS 526
Cdd:PRK07868 766 --AKIGSKGRPLpgaGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARA---------RGPIDPTA-SVKRGVFAP 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 527 GDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGRH 591
Cdd:PRK07868 834 ADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ 898
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
141-586 |
3.08e-23 |
|
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: 102.93 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 141 GSVTFGELDARACQAAWALKAeLGDPAslcaGEPTALLVLASQAVPalCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSS 220
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRN-LGVSS----GDRVLLLMLDSPELV--QLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 221 GARVLVVDpdlresleeilpklqAENIrCFYLshtsptpgvgalgaaldaapshpvpadlragitwrspalfiYTSGTTG 300
Cdd:cd05919 82 EARLVVTS---------------ADDI-AYLL-----------------------------------------YSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 301 LPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFST-SCFWDDCRQHGVT 377
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAreALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTaERVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 378 VILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTE-GNMGLVNYVG--RCGALG 452
Cdd:cd05919 185 VLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATEvGHIFLSNRPGawRLGSTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 453 kmscllRMLSPFELvqfdmeaaePVRDNQGFCIPVGlgEPGLLLTKVVSQqpFVGYRGPRELSERKLVrnvrqsgDVYYN 532
Cdd:cd05919 264 ------RPVPGYEI---------RLVDEEGHTIPPG--EEGDLLVRGPSA--AVGYWNNPEKSRATFN-------GGWYR 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 533 TGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVC 586
Cdd:cd05919 318 TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP 371
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
124-571 |
3.30e-22 |
|
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: 100.39 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVwTGPGAGSVTFGELDARACQAAWALKAELGDPaslcaGEPTALLVLASQAVPALCmwLGLAKLGCPTAW 203
Cdd:cd05904 15 ASAHPSRPALI-DAATGRALTYAELERRVRRLAAGLAKRGGRK-----GDVVLLLSPNSIEFPVAF--LAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 204 INPHGRGMPLAHSVLSSGARVLVVDPDLresleeiLPKLQAENIRCFYLShtSPTPGVGALGAALDAAPSHPVPadlRAG 283
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAKLAFTTAEL-------AEKLASLALPVVLLD--SAEFDSLSFSDLLFEADEAEPP---VVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 284 ITWRSPALFIYTSGTTGLPKPAILTHERV---LQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 360
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLiamVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGPIRIWEVYGSTE-G 437
Cdd:cd05904 235 RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAapLGKELIEAFRAKFPNVDLGQGYGMTEsT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 438 NMGLVNYVGRCGALGKMSCllRMLSPfelvqfDMEaAEPVRDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELSER 517
Cdd:cd05904 315 GVVAMCFAPEKDRAKYGSV--GRLVP------NVE-AKIVDPETGESLPP--NQTGELWIR--GPSIMKGYLNNPEATAA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 518 KLVrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd05904 382 TID------KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
110-553 |
8.18e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 99.64 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 110 RQPPDTFVDAFERRARAQPGR-ALLVWTGPG----AGSVTFGELDARACQAAWALkaelgdpASLCAGEPTA---LLVLA 181
Cdd:PRK07529 21 RDLPASTYELLSRAAARHPDApALSFLLDADpldrPETWTYAELLADVTRTANLL-------HSLGVGPGDVvafLLPNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 182 SQAVPALcmWLG-LAKLGCPtawINPHGRGMPLAHSVLSSGARVLVV-----DPDLRESLEEILPklQAENIRCFYLSHT 255
Cdd:PRK07529 94 PETHFAL--WGGeAAGIANP---INPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLA--ALPELRTVVEVDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 256 SPTPGVGALGAALDAAPSHPV------------PAD-LRAG--ITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKML- 319
Cdd:PRK07529 167 ARYLPGPKRLAVPLIRRKAHArildfdaelarqPGDrLFSGrpIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGa 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 320 SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP------KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIP 393
Cdd:PRK07529 247 LLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrgPGVIANFWKIVERYRINFLSGVPTVYAALLQVP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 394 QQPEDRThTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNMGL-VNYVG---RCGALGkmsclLRMlsPFE-- 465
Cdd:PRK07529 327 VDGHDIS-SLRYALCGAapLPVEVFRRFEAATG-VRIVEGYGLTEATCVSsVNPPDgerRIGSVG-----LRL--PYQrv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 466 -LVQFDmEAAEPVRDnqgfCIPvglGEPGLLLTkvvsQQP--FVGYRGPRElsERKLVrnvrqSGDVYYNTGDVLAMDRE 542
Cdd:PRK07529 398 rVVILD-DAGRYLRD----CAV---DEVGVLCI----AGPnvFSGYLEAAH--NKGLW-----LEDGWLNTGDLGRIDAD 458
|
490
....*....|.
gi 768006055 543 GFLYFRDRLGD 553
Cdd:PRK07529 459 GYFWLTGRAKD 469
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
115-585 |
2.70e-21 |
|
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: 97.58 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPGRALLVWTGPGAgSVTFGELDARACQAAWALKAELGDPASLCAgeptallVLASQAVPALCMWLGL 194
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGL-RLTYSELRARIEAVAARLHARGLRPGQRVA-------VVLPNSVEAVIALLAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 195 AKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLresleeilPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSH 274
Cdd:cd05923 74 HRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDA--------QVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 PV-PADlragitwrsPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLSGAtADDVVYTVLPLYHVMGLVVGILGC 349
Cdd:cd05923 146 PRePEQ---------PAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQAGLRHG-RHNVVLGLMPLYHVIGFFAVLVAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 350 LDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR------LAMGNGLRADVwetfqQRF 423
Cdd:cd05923 216 LALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRhvtfagATMPDAVLERV-----NQH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 424 GPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCllrmlspFELVQFdmeaaepVRDNQGFCIPVGLGEPGLLLTKVVSQQ 503
Cdd:cd05923 291 LPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGF-------FSEVRI-------VRIGGSPDEALANGEEGELIVAAAADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 504 PFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVY 583
Cdd:cd05923 357 AFTGYLNQPEATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
..
gi 768006055 584 GV 585
Cdd:cd05923 430 GV 431
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-573 |
1.05e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 95.97 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 114 DTFVDAFERRARAQPGRALLVwTGPGAgSVTFGELD-ARACQAAWALKA--ELGDpaslcageptallVLASQaVPALC- 189
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVV-DNHGA-SYTYSALDhAASRLANWLLAKgiEPGD-------------RVAFQ-LPGWCe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 190 ---MWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLV-------VDP-DLRESLEEILPKLQaeniRCFYLSHTSP- 257
Cdd:PRK06087 87 ftiIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlfkqTRPvDLILPLQNQLPQLQ----QIVGVDKLAPa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 258 TPGVGALGAALDAAP-SHPVPADlragitWRSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLP 335
Cdd:PRK06087 163 TSSLSLSQIIADYEPlTTAITTH------GDELAAVLFTSGTEGLPKGVMLTHNNILASERaYCARLNLTWQDVFMMPAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 336 LYHVMGLVVGILGCLDLGATCVLAPKFSTS----------CFWddcrQHGVTVILYvgellRYLCNIPQQPEDRThTVRL 405
Cdd:PRK06087 237 LGHATGFLHGVTAPFLIGARSVLLDIFTPDaclalleqqrCTC----MLGATPFIY-----DLLNLLEKQPADLS-ALRF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 406 AMGNG--LRADVWETFQQRfgPIRIWEVYGSTEGN-MGLVNyvgrcgaLGKmsCLLRMlspfelVQFDMEAAEPVR---- 478
Cdd:PRK06087 307 FLCGGttIPKKVARECQQR--GIKLLSVYGSTESSpHAVVN-------LDD--PLSRF------MHTDGYAAAGVEikvv 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 479 DNQGFCIPVG-LGEPgllltkvVSQQP--FVGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTF 555
Cdd:PRK06087 370 DEARKTLPPGcEGEE-------ASRGPnvFMGYLDEPELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDII 436
|
490
....*....|....*...
gi 768006055 556 RWKGENVSTHEVEGVLSQ 573
Cdd:PRK06087 437 VRGGENISSREVEDILLQ 454
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
293-585 |
1.55e-20 |
|
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: 93.10 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 293 IYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVGiLGCLDLGATCVLAPKFSTSCFWDD 370
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIaaNLQLIHAM-GLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 371 CRQHGVTVIlyvGELLRYLCNIPQQPEDrtHTVRLAmgnGLRA----DVWETFQ--QRFGPIRIWEVYGSTEgNMGLVN- 443
Cdd:cd17637 84 IEEEKVTLM---GSFPPILSNLLDAAEK--SGVDLS---SLRHvlglDAPETIQrfEETTGATFWSLYGQTE-TSGLVTl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 444 --YVGRCGALGKMScllrMLSPFELVQFDmeaaepvrDNqgfciPVGLGEPGllltKVVSQQP--FVGYRGPRELSERKL 519
Cdd:cd17637 155 spYRERPGSAGRPG----PLVRVRIVDDN--------DR-----PVPAGETG----EIVVRGPlvFQGYWNLPELTAYTF 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 520 vRNvrqsGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWK--GENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17637 214 -RN----G--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGV 274
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
112-584 |
1.01e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 93.24 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 112 PPDTFVDAFERRARAQPGRALLVWTGPGAG-SVTFGELDARACQAAWALKAeLGdpasLCAGEPTALL-------VLASQ 183
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIWqSLTWAEFAERVRALAAGLLA-LG----VKPGDRVAILsdnrpewVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 184 AVpalcMWLGLAklGCP---------TAWInphgrgmpLAHSvlssGARVLVV-DPDLRESLEEILPKLQA-ENIRCFYL 252
Cdd:COG1022 84 AI----LAAGAV--TVPiyptssaeeVAYI--------LNDS----GAKVLFVeDQEQLDKLLEVRDELPSlRHIVVLDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 253 SHTSPTPGVGALGAALDAAPSHPVPADL---RAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADD 328
Cdd:COG1022 146 RGLRDDPRLLSLDELLALGREVADPAELearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALlERLPLGPGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 329 VVYTVLPLYHVMGLVVGIlGCLDLGATCVLAPKFSTscFWDDCRQHGVTVILYV----------------------GELL 386
Cdd:COG1022 226 RTLSFLPLAHVFERTVSY-YALAAGATVAFAESPDT--LAEDLREVKPTFMLAVprvwekvyagiqakaeeagglkRKLF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 387 RYLCNI-----PQQPEDRTHTVRLAMGNGLrAD--VWETFQQRFGP------------------------IRIWEVYGST 435
Cdd:COG1022 303 RWALAVgrryaRARLAGKSPSLLLRLKHAL-ADklVFSKLREALGGrlrfavsggaalgpelarffralgIPVLEGYGLT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 436 E-GNMGLVNYVGRC--GALGKmscllrmlspfelvqfdmeaaePVRDNQgfcipVGLGEPGLLLTKvvSQQPFVGYRGPR 512
Cdd:COG1022 382 EtSPVITVNRPGDNriGTVGP----------------------PLPGVE-----VKIAEDGEILVR--GPNVMKGYYKNP 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 513 ELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFrwK---GENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:COG1022 433 EATAEAFDA------DGWLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
142-585 |
1.32e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.63 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 142 SVTFGELDARACQAAWALKAELgdpaSLCAGEPTALLVLASQAVPALCmwLGLAKLGCPTAWINPHGRGMPLAHSVLSSG 221
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGEL----QLKKGDRVALMMPNCLQYPIAT--FGVLRAGLTVVNVNPLYTPRELKHQLIDSG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 222 ARVLVVDPDLRESLEEIL-------------------PKLQAENIRCFYLSHTSPT---PGVGALGAALDAAPSHPVPAd 279
Cdd:PRK08751 124 ASVLVVIDNFGTTVQQVIadtpvkqvittglgdmlgfPKAALVNFVVKYVKKLVPEyriNGAIRFREALALGRKHSMPT- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 lrAGITWRSPALFIYTSGTTGLPKPAILTHERVL----QMSKMLSLSGATAD--DVVYTVLPLYHVMGLVVGILGCLDLG 353
Cdd:PRK08751 203 --LQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqQAHQWLAGTGKLEEgcEVVITALPLYHIFALTANGLVFMKIG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 354 ATCVLA--PKfSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGL--RADVWETFQQRFGpIRIW 429
Cdd:PRK08751 281 GCNHLIsnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTG-LTLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 430 EVYGSTEGNMGlvnyvgrcgalgkmSCLlrmlSPFELVQFDMEAAEPV-------RDNQGFCIPvgLGEPGLLLTKvvSQ 502
Cdd:PRK08751 359 EAYGLTETSPA--------------ACI----NPLTLKEYNGSIGLPIpstdaciKDDAGTVLA--IGEIGELCIK--GP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 503 QPFVGY-RGPRELSERklvrnvrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVN 581
Cdd:PRK08751 417 QVMKGYwKRPEETAKV-------MDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVA 489
|
....
gi 768006055 582 VYGV 585
Cdd:PRK08751 490 AVGV 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
290-585 |
1.88e-19 |
|
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: 91.00 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHeRVLQMSKMLSL--SGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCF 367
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTH-FSAAANALQSAvwTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 368 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEG-NMGLVNY 444
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTNP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 445 VGRCgalgKMSCLLRMLSPFELVQFDMEAAEPVRDNQgfcipvgLGEpgllltkVVSQQP--FVGY-RGPRELSERKlvr 521
Cdd:cd05935 245 PLRP----KLQCLGIP*FGVDARVIDIETGRELPPNE-------VGE-------IVVRGPqiFKGYwNRPEETEESF--- 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 522 nVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05935 304 -IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISV 366
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
112-585 |
2.06e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 91.99 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 112 PPDTFVDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKAeLGdpasLCAGEPTALlVLAS--QAVPALC 189
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPALDFFG---ATTTYAELGKQVRRAAAGLRA-LG----VRPGDRVAI-VLPNcpQHIVAFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 190 MWLglaKLGCPTAWINPHGRGMPLAHSVLSSGARVLVV----DPDLRE-----SLEEI--------LPKLQ-------AE 245
Cdd:PRK05605 101 AVL---RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvAPTVERlrrttPLETIvsvnmiaaMPLLQrlalrlpIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 246 NIRCFYLSHTSPTPG-------VGALGAALDAAPSHPVPadlragiTWRSPALFIYTSGTTGLPKPAILTHERV---LQM 315
Cdd:PRK05605 178 ALRKARAALTGPAPGtvpwetlVDAAIGGDGSDVSHPRP-------TPDDVALILYTSGTTGKPKGAQLTHRNLfanAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 316 SKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRylcNIPQQ 395
Cdd:PRK05605 251 GKAWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYE---KIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 396 PEDR---THTVRLAMGNG--LRADVWETFQQRFGPiRIWEVYGSTE------GNMglVNYVGRCGALGkmscllrmlSPF 464
Cdd:PRK05605 328 AEERgvdLSGVRNAFSGAmaLPVSTVELWEKLTGG-LLVEGYGLTEtspiivGNP--MSDDRRPGYVG---------VPF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 465 ELVqfDMEAAEPvrDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGF 544
Cdd:PRK05605 396 PDT--EVRIVDP--EDPDETMPD--GEEGELLVR--GPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 768006055 545 LYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK05605 461 IRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
121-606 |
3.55e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 90.69 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 121 ERRARAQPGRALLVWTgpgAGSVTFGELDARACQAAWALKAELGdpasLCAGEPTAllVLASQAVPALCMWLGLAKLGCP 200
Cdd:PRK06839 9 EKRAYLHPDRIAIITE---EEEMTYKQLHEYVSKVAAYLIYELN----VKKGERIA--ILSQNSLEYIVLLFAIAKVECI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 201 TAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIrcfyLSHTSPTpgvgalgAALDAAPSHPVPADL 280
Cdd:PRK06839 80 AVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRV----ISITSLK-------EIEDRKIDNFVEKNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 281 RAgitwrsPALFIYTSGTTGLPKPAILTHERVL--QMSKMLSLSgATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK06839 149 SA------SFIICYTSGTTGKPKGAVLTQENMFwnALNNTFAID-LTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 APKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA--DVWETFQQRfgPIRIWEVYGSTE 436
Cdd:PRK06839 222 PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCpeELMREFIDR--GFLFGQGFGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 GNMGLV-----NYVGRCGALGK--MSCLLRMLSPfelvqfdmeaaepvrdNQGfciPVGLGEPGLLLTkvvsqqpfvgyR 509
Cdd:PRK06839 300 TSPTVFmlseeDARRKVGSIGKpvLFCDYELIDE----------------NKN---KVEVGEVGELLI-----------R 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 510 GPRELSE----RKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK06839 350 GPNVMKEywnrPDATEETIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGR 427
|
490 500
....*....|....*....|.
gi 768006055 586 cvpgrhgghQHVQTDEDPVGA 606
Cdd:PRK06839 428 ---------QHVKWGEIPIAF 439
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
290-585 |
4.08e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.01 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFW 368
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLS-SALAMLMVGACHVLLPKFDAKAAL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 369 DDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVR--LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGnmglvny 444
Cdd:PLN02860 254 QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRkiLNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEA------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 445 vgrCGALGKMSCLLRMLSPFE--LVQFDMEAAEPVRDNQGFCipVGLGEPGLLLTKVVSQQPFVG---YRGP----RELS 515
Cdd:PLN02860 327 ---CSSLTFMTLHDPTLESPKqtLQTVNQTKSSSVHQPQGVC--VGKPAPHVELKIGLDESSRVGrilTRGPhvmlGYWG 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 516 ERKLVRNVRQSgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PLN02860 402 QNSETASVLSN-DGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
290-585 |
6.13e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 90.50 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLqmSKMLSLSGATA------DDVVYTVLPLYHVMGLVVGILGCLDLGATCVLA--PK 361
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNML--ANLEQAKAAYGpllhpgKELVVTALPLYHIFALTVNCLLFIELGGQNLLItnPR 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 362 fSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLR-----ADVWETFQQRfgpiRIWEVYGSTE 436
Cdd:PRK08974 287 -DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAvqqavAERWVKLTGQ----YLLEGYGLTE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 gnmglvnyvgrCGALgkMSCllrmlSPFELVQFDMEAAEPV-------RDNQGFCIPvgLGEPGLLLTKvvSQQPFVGY- 508
Cdd:PRK08974 362 -----------CSPL--VSV-----NPYDLDYYSGSIGLPVpsteiklVDDDGNEVP--PGEPGELWVK--GPQVMLGYw 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 509 RGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK08974 420 QRPEATDE------VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
115-436 |
8.34e-19 |
|
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: 91.07 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLVLAS-QAVPALcmwLG 193
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVF---GDQSLTYAELNARANRLAHHLRA-----LGVGPGDLVGVCLERSlEMVVAL---LA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 194 LAKLGCptAWI-----NPHGRgmpLAHSVLSSGARVLVVDPDLRESLEEilpklqaenircfylshtSPTPGVGALGAAL 268
Cdd:COG1020 546 VLKAGA--AYVpldpaYPAER---LAYMLEDAGARLVLTQSALAARLPE------------------LGVPVLALDALAL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 269 DAAPSHPVPADLRAGitwrSPALFIYTSGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVV 344
Cdd:COG1020 603 AAEPATNPPVPVTPD----DLAYVIYTSGSTGRPKGVMVEHRalvnLLAWMQRRYGL---GPGDRVLQFASLSFDAS-VW 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 345 GILGCLDLGATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVrLAMGNGLRADVWETFQQ 421
Cdd:COG1020 675 EIFGALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLV-LVGGEALPPELVRRWRA 753
|
330
....*....|....*
gi 768006055 422 RFGPIRIWEVYGSTE 436
Cdd:COG1020 754 RLPGARLVNLYGPTE 768
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
290-573 |
8.48e-19 |
|
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: 88.94 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFSTSCF 367
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWwsAIGSALNL-GLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 368 WDDCRQHGVTVILYVGELLRYLcnIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRfgPIRIWEVYGSTEGNMGLVNYV 445
Cdd:cd05912 158 LHLINSGKVTIISVVPTMLQRL--LEILGEGYPNNLRCILlgGGPAPKPLLEQCKEK--GIPVYQSYGMTETCSQIVTLS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 446 GRcGALGKMSCLLRMLSPFELvqfdmeaaEPVRDNQGfciPVGLGEpgllltkVVSQQPFV--GYRGPRELSERKLVRNv 523
Cdd:cd05912 234 PE-DALNKIGSAGKPLFPVEL--------KIEDDGQP---PYEVGE-------ILLKGPNVtkGYLNRPDATEESFENG- 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 768006055 524 rqsgdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQ 573
Cdd:cd05912 294 ------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
144-582 |
1.62e-18 |
|
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: 88.09 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAELGdpasLCAGEPTAllVLASQAVPALCMWLGLAKLGCptAW--INPHgrgMP---LAHSVL 218
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG----VGPGDRVA--VLLERSAELVVAILAVLKAGA--AYvpLDPA---YPaerLAFILE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDLRESLEEIlpklqaenircfylshtsPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGT 298
Cdd:TIGR01733 70 DAGARLLLTDSALASRLAGL------------------VLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 299 TGLPKPAILTHERVLQM-SKMLSLSGATADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPKFSTSC---FWDDC-RQ 373
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVNLlAWLARRYGLDPDDRVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDdaaLLAALiAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 374 HGVTVILYVGELLRYLCniPQQPEDRTH--TVRLAmGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGlvnyvgrcgal 451
Cdd:TIGR01733 211 HPVTVLNLTPSLLALLA--AALPPALASlrLVILG-GEALTPALVDRWRARGPGARLINLYGPTETTVW----------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 452 gkmscllrmlSPFELVQFDMEAAEPVR------DNQGFCI------PVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKL 519
Cdd:TIGR01733 277 ----------STATLVDPDDAPRESPVpigrplANTRLYVldddlrPVPVGVVGELY--IGGPGVARGYLNRPELTAERF 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 520 VRNVRQSGD--VYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 582
Cdd:TIGR01733 345 VPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-585 |
1.80e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 87.33 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL-APKFS-----TSC 366
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERlGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDplavlEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQ-HGVTVIlYVGELlrylcNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGN----M 439
Cdd:cd05917 89 EKEKCTAlHGVPTM-FIAEL-----EHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpvstQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 440 GL--------VNYVGRcgalgkmscllrmLSPF-ELVQFDMEAaepvrdnqgfCIPVGLGEPGLLLTKVVSQQpfVGYRG 510
Cdd:cd05917 163 TRtddsiekrVNTVGR-------------IMPHtEAKIVDPEG----------GIVPPVGVPGELCIRGYSVM--KGYWN 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 511 PRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd05917 218 DPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV 286
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
290-590 |
2.19e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 88.94 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSKM---LSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 366
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTLMgvqWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGPiRIWEVYGSTEGN-MGLVN 443
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKFETVTGG-KLVEGYGLTESSpVTHSN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 444 YVGRCGALGKMSCllrmlsPF---ELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKvvSQQPFVGY-RGPRELSErkl 519
Cdd:PRK06710 368 FLWEKRVPGSIGV------PWpdtEAMIMSLETGEALPP----------GEIGEIVVK--GPQIMKGYwNKPEETAA--- 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006055 520 vrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:PRK06710 427 ---VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
144-588 |
5.86e-18 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 86.73 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAElgdpaSLCAGEPTALLvlaSQAVPALCMWL-GLAKLGCPTAWINPHgrgMP--LAHSVLSS 220
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ-----GIRSGSRVALV---GQNSIEMVLLLhACLLLGAEIAMLNTR---LTenERTNQLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 221 GARVLVVDPDLresLEEilPKLQAENIRCFYLSHTSPTpgvgalgaaldaapshpvpaDLRAGITWRSPALFIYTSGTTG 300
Cdd:TIGR01923 70 LDVQLLLTDSL---LEE--KDFQADSLDRIEAAGRYET--------------------SLSASFNMDQIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 301 LPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFSTscFWDDCRQHGVTVI 379
Cdd:TIGR01923 125 KPKAVPHTFRNHYASAVGSKENlGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--LLEMIANERVTHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 380 LYVGELL-RYLcnipqQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIriWEVYGSTEgnmglvnyvgrcgalgkmsc 456
Cdd:TIGR01923 202 SLVPTQLnRLL-----DEGGHNENLRkiLLGGSAIPAPLIEEAQQYGLPI--YLSYGMTE-------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 457 llrMLSPFELVQFDMEAAEP----VRDNQGFCIPV-GLGEPGLLLTKvvSQQPFVGYRGPRELSERklvrnVRQSGdvYY 531
Cdd:TIGR01923 255 ---TCSQVTTATPEMLHARPdvgrPLAGREIKIKVdNKEGHGEIMVK--GANLMKGYLYQGELTPA-----FEQQG--WF 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 532 NTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVnvygVCVP 588
Cdd:TIGR01923 323 NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEA----VVVP 375
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
289-573 |
6.44e-18 |
|
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: 86.62 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL--APKFSTS 365
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLgHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 366 CFWDDCRQHGVTVILYVGELLRYLcnIPQQPEDRT-HTVRLAMGNG--LRADVWETFQQRFG-PIRiwEVYGSTEGNMGL 441
Cdd:cd05972 163 RILELLERYGVTSFCGPPTAYRML--IKQDLSSYKfSHLRLVVSAGepLNPEVIEWWRAATGlPIR--DGYGQTETGLTV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 442 VNYVG---RCGALGK-MSCllrmlspfelvqFDMEaaepVRDNQGfcIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSER 517
Cdd:cd05972 239 GNFPDmpvKPGSMGRpTPG------------YDVA----IIDDDG--RELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEA 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 768006055 518 KLVrnvrqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQ 573
Cdd:cd05972 301 SIR------GD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
118-582 |
6.94e-18 |
|
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: 86.87 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKA---ELGDPASLCAgEPTALLVLASQAVpalcMWLGL 194
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY---GDRSLTYAELNERANRLARRLRAagvGPGDVVGVLA-ERSPELVVALLAV----LKAGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 195 AKLGCPTAWinPHGRgmpLAHSVLSSGARVLVVDPDLRESLEEIlpklqaeniRCFYLSHTSPTPGvgalgaaldaaPSH 274
Cdd:cd12117 73 AYVPLDPEL--PAER---LAFMLADAGAKVLLTDRSLAGRAGGL---------EVAVVIDEALDAG-----------PAG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 PVPADLRAGitwrSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPL-YHVMGLvvGILGCLDLG 353
Cdd:cd12117 128 NPAVPVSPD----DLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLGPDDRVLQTSPLaFDASTF--EIWGALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 354 ATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHTVRLAMGNGLRADV--WETFQQRFGPIRI 428
Cdd:cd12117 202 ARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLA---DEDPECFAGLRELLTGGEVVSPphVRRVLAACPGLRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 429 WEVYGSTEgNMGLVNYvgrcgalgkmscllrmlspFELVQFDMEAAEP------------VRDNQGfcIPVGLGEPGLL- 495
Cdd:cd12117 279 VNGYGPTE-NTTFTTS-------------------HVVTELDEVAGSIpigrpiantrvyVLDEDG--RPVPPGVPGELy 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 496 -----LTKvvsqqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:cd12117 337 vggdgLAL--------GYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAA 408
|
490
....*....|..
gi 768006055 571 LSQVDFLQQVNV 582
Cdd:cd12117 409 LRAHPGVREAVV 420
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
280-574 |
9.66e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.67 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 LRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISdVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 APkfstscfwdD----------CRQHGVTVILYVGELLR-YLCNIPQQPEDRThTVRLAMGNG--LRADVWETFQQRFGp 425
Cdd:PRK08633 855 HP---------DptdalgiaklVAKHRATILLGTPTFLRlYLRNKKLHPLMFA-SLRLVVAGAekLKPEVADAFEEKFG- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 426 IRIWEVYGSTEgnmglvnyvgrcgalgkmscllrmLSPFELVQF-DMEAAEPVRdnQGFCIP--VGL------------- 489
Cdd:PRK08633 924 IRILEGYGATE------------------------TSPVASVNLpDVLAADFKR--QTGSKEgsVGMplpgvavrivdpe 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 490 -------GEPGLLLTKvvSQQPFVGYRGPRELSErKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENV 562
Cdd:PRK08633 978 tfeelppGEDGLILIG--GPQVMKGYLGDPEKTA-EVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMV 1052
|
330
....*....|..
gi 768006055 563 STHEVEGVLSQV 574
Cdd:PRK08633 1053 PLGAVEEELAKA 1064
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-568 |
1.32e-17 |
|
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: 85.57 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFST-SC 366
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLaNARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLdDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVT---VILYVGELLRYLCNIPQQ-PEDRTHTvrlAMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnmglv 442
Cdd:cd05922 198 FWEDLREHGATglaGVPSTYAMLTRLGFDPAKlPSLRYLT---QAGGRLPQETIARLRELLPGAQVYVMYGQTE------ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 443 nyvgrcgALGKMSCLlrmlsPFELVQFDMEAAEP--------VRDNQGFciPVGLGEPGllltKVVSQQPFVGYRGPREL 514
Cdd:cd05922 269 -------ATRRMTYL-----PPERILEKPGSIGLaipggefeILDDDGT--PTPPGEPG----EIVHRGPNVMKGYWNDP 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 515 SERklvRNVRQSGDVYYnTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVE 568
Cdd:cd05922 331 PYR---RKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
122-363 |
1.59e-17 |
|
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: 86.14 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 122 RRARAQPGRALLVWT---GPGAGSVTFGELDARACQAAWAL--KAELGDPASLcAGEPTALLVLASQAvpalCMWLGLak 196
Cdd:cd05931 1 RRAAARPDRPAYTFLddeGGREETLTYAELDRRARAIAARLqaVGKPGDRVLL-LAPPGLDFVAAFLG----CLYAGA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 197 LGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAenircfylshtSPTPGVGALGAALDAAPSHPV 276
Cdd:cd05931 74 IAVPLPPPTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPA-----------AGTPRLLVVDLLPDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 277 PADLRAGitwrSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGAT 355
Cdd:cd05931 143 PPSPDPD----DIAYLQYTSGSTGTPKGVVVTHRNLLaNVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
....*...
gi 768006055 356 CVLAPKFS 363
Cdd:cd05931 219 SVLMSPAA 226
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
124-585 |
2.51e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 85.09 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAElgdpaSLCAGEPtaLLVLASQAVPAL-CMWLGLaKLGCptA 202
Cdd:PRK07470 17 ARRFPDRIALVW---GDRSWTWREIDARVDALAAALAAR-----GVRKGDR--ILVHSRNCNQMFeSMFAAF-RLGA--V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 203 WINPHGRGMP--LAHSVLSSGARVLVVDPDLRESLEEIlpklqaenircfylshTSPTPGVGALGAALDAAPSHPVPADL 280
Cdd:PRK07470 84 WVPTNFRQTPdeVAYLAEASGARAMICHADFPEHAAAV----------------RAASPDLTHVVAIGGARAGLDYEALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 281 RAGITWRS---------PALFIYTSGTTGLPKPAILTHErvlQMSKMLS------LSGATADDVVYTVLPLYHVMGlvVG 345
Cdd:PRK07470 148 ARHLGARVanaavdhddPCWFFFTSGTTGRPKAAVLTHG---QMAFVITnhladlMPGTTEQDASLVVAPLSHGAG--IH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 346 ILGCLDLGATCVLAP--KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG---LRADvwetfQ 420
Cdd:PRK07470 223 QLCQVARGAATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGapmYRAD-----Q 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 421 QR----FGPIrIWEVYGSTE--GNM------------GLVNYVGRCGalgkmscllrmlspFElvQFDMEAAepVRDNQG 482
Cdd:PRK07470 298 KRalakLGKV-LVQYFGLGEvtGNItvlppalhdaedGPDARIGTCG--------------FE--RTGMEVQ--IQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 483 fcIPVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENV 562
Cdd:PRK07470 359 --RELPPGETGEIC--VIGPAVFAGYYNNPEANAKAFR-------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNV 427
|
490 500
....*....|....*....|...
gi 768006055 563 STHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK07470 428 YPREIEEKLLTHPAVSEVAVLGV 450
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
124-585 |
2.53e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.94 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVWTGPgagSVTFGELDARACQAAWALKAElgdpaSLCAGEPTALLVLASQAVpaLCMWLGLAKLGCPTAW 203
Cdd:PRK06145 12 ARRTPDRAALVYRDQ---EISYAEFHQRILQAAGMLHAR-----GIGQGDVVALLMKNSAAF--LELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 204 INPHGRGMPLAHSVLSSGARVLVVDPDLresleEILPKLQAENIRCFYLSHTSPTpgvGALGAALDAAPSHPV-PADLra 282
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEEF-----DAIVALETPKIVIDAAAQADSR---RLAQGGLEIPPQAAVaPTDL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 283 gitwrspALFIYTSGTTGLPKPAILTHERVLQMS--KMLSLsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 360
Cdd:PRK06145 152 -------VRLMYTSGTTDRPKGVMHSYGNLHWKSidHVIAL-GLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWE--TFQQRFGPIRIWEVYGSTEGN 438
Cdd:PRK06145 224 EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRirDFTRVFTRARYIDAYGLTETC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 439 MG-LVNYVGRcgALGKMSCLLRMLSPFELvqfdmeaaePVRDNQGFCIPVGL-GEPGLLLTKVVSqqpfvGYRGPRELSE 516
Cdd:PRK06145 304 SGdTLMEAGR--EIEKIGSTGRALAHVEI---------RIADGAGRWLPPNMkGEICMRGPKVTK-----GYWKDPEKTA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 517 RKLVRNVRQSGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK06145 368 EAFYGDWFRSGDVGY-------LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGV 429
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
124-585 |
4.71e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 84.59 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVwtgPGAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLVLASQAVpALCMwLGLAKLGCPTAW 203
Cdd:PRK07788 59 ARRAPDRAALI---DERGTLTYAELDEQSNALARGLLA-----LGVRAGDGVAVLARNHRGF-VLAL-YAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 204 INPHGRGMPLAHSVLSSGARVLVVDP---DLRESLEEILPKLQAenIRCFYLSHTSPTPGVGALGAALDAAPSHPVPadl 280
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKALVYDDeftDLLSALPPDLGRLRA--WGGNPDDDEPSGSTDETLDDLIAGSSTAPLP--- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 281 ragiTWRSPA-LFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGcLDLGATCVL 358
Cdd:PRK07788 204 ----KPPKPGgIVILTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 APKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM----GNGLRADVWETFQQRFGPIrIWEVYGS 434
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIifvsGSALSPELATRALEAFGPV-LYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 435 TEgnmglVNYVGrcgalgkmscllrMLSPFELVQFDMEAAEPVR-------DNQGFCIPVglGEPGLLLtkVVSQQPFVG 507
Cdd:PRK07788 358 TE-----VAFAT-------------IATPEDLAEAPGTVGRPPKgvtvkilDENGNEVPR--GVVGRIF--VGNGFPFEG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 508 YRGPRelsERKLVRNVRQSGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK07788 416 YTDGR---DKQIIDGLLSSGDVGY-------FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
137-571 |
7.94e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 83.41 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 137 GPGAGSVTFGELDARACQAAWALKAeLGdpasLCAGEPTALLV---LASQAVPALCMWLGLakLGCPtawINPHGRGMPL 213
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGLRA-LG----LREGDVVAILLennPEFFEVYWAARRSGL--YYTP---INWHLTAAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 214 AHSVLSSGARVLVVDPDLRESLEEILPKLQAEnIRCFYLShTSPTPGVGALGAALDAAPSHPvPADLRAGitwrspALFI 293
Cdd:PRK08276 76 AYIVDDSGAKVLIVSAALADTAAELAAELPAG-VPLLLVV-AGPVPGFRSYEEALAAQPDTP-IADETAG------ADML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPK------PAILTHERVLQMSKMLSLSGATADDVVYTV-LPLYHVMGLVVGiLGCLDLGATCVLAPKFSTSC 366
Cdd:PRK08276 147 YSSGTTGRPKgikrplPGLDPDEAPGMMLALLGFGMYGGPDSVYLSpAPLYHTAPLRFG-MSALALGGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVTVILYVGELLRYLCNIPqqPEDRT-----------HT-------VRLAMgnglrADVWetfqqrfGPIrI 428
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLP--EEVRArydvsslrvaiHAaapcpveVKRAM-----IDWW-------GPI-I 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 429 WEVYGSTEGNMGLV----NYVGRCGALGK-MSCLLRMLspfelvqfdmeaaepvrDNQGfcIPVGLGEPGLLLTKvVSQQ 503
Cdd:PRK08276 291 HEYYASSEGGGVTVitseDWLAHPGSVGKaVLGEVRIL-----------------DEDG--NELPPGEIGTVYFE-MDGY 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 504 PFvGYRGPRElserKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PRK08276 351 PF-EYHNDPE----KTAAARNPHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLL 411
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
117-571 |
1.76e-16 |
|
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: 82.32 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 117 VDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKAE---LGDPASLCAgEPTALLVLASQAVpalcMWLG 193
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEG---RTLTYRELDERANRLAHLLRARgvgPEDRVAVLL-PRSADLVVALLAV----LKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 194 LAKLGCPTAWinPHGRgmpLAHSVLSSGARVLVVDPDLRESLeeilpklqaenircfylshtsptPGVGALGAALDAAPS 273
Cdd:cd17646 73 AAYLPLDPGY--PADR---LAYMLADAGPAVVLTTADLAARL-----------------------PAGGDVALLGDEALA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 274 HPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLsgaTADDVVYTVLPL-YHVMglVVGILG 348
Cdd:cd17646 125 APPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHagivNRLLWMQDEYPL---GPGDRVLQKTPLsFDVS--VWELFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 349 CLDLGATCVLA-------PKFSTSCFwddcRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQ 421
Cdd:cd17646 200 PLVAGARLVVArpgghrdPAYLAALI----REHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 422 RFGpIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDmEAAEPVrdnqgfciPVGL-GE---PGLLLT 497
Cdd:cd17646 276 LPG-AELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPV--------PVGVpGElylGGVQLA 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 498 KvvsqqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd17646 346 R--------GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-585 |
1.91e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 82.32 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 123 RARAQPGRALLVWtgpGAGSVTFGELDARAcqAAWALKAelgdpASLCA--GEPTALLVLASQAVPALCMwlGLAKLGCP 200
Cdd:PRK03640 11 RAFLTPDRTAIEF---EEKKVTFMELHEAV--VSVAGKL-----AALGVkkGDRVALLMKNGMEMILVIH--ALQQLGAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 201 TAWIN----PHGRGMPLAHSvlssGARVLVVDPDLRESLEEI-------LPKLQAENIrcfylshtsptpgvgalgaald 269
Cdd:PRK03640 79 AVLLNtrlsREELLWQLDDA----EVKCLITDDDFEAKLIPGisvkfaeLMNGPKEEA---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 270 aAPSHPVPADLRAGItwrspalfIYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVgIL 347
Cdd:PRK03640 133 -EIQEEFDLDEVATI--------MYTSGTTGKPKGVIQTYGNHWwsAVGSALNL-GLTEDDCWLAAVPIFHISGLSI-LM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 348 GCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLcnIPQQPEDRTH-TVRLAMGNGLRAD--VWETFQQRfg 424
Cdd:PRK03640 202 RSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRL--LERLGEGTYPsSFRCMLLGGGPAPkpLLEQCKEK-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 425 PIRIWEVYGSTEGNMGLV-----NYVGRCGALGKmscllrmlsPFelvqFDMEAAepVRDNQGFCIPVGLGEpgllltkV 499
Cdd:PRK03640 278 GIPVYQSYGMTETASQIVtlspeDALTKLGSAGK---------PL----FPCELK--IEKDGVVVPPFEEGE-------I 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 500 VSQQPFV--GYrgpreLSERKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFL 577
Cdd:PRK03640 336 VVKGPNVtkGY-----LNREDATRETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGV 408
|
....*...
gi 768006055 578 QQVNVYGV 585
Cdd:PRK03640 409 AEAGVVGV 416
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
139-550 |
2.08e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 81.81 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 139 GAGSVTFGELDARACQAAWALKAELGDPaslcaGEPTALLVLAS-QAVPALcmwLGLAKLGC---PTAWINPHGRgmpLA 214
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGP-----GDLVAVLLERSlEMVVAI---LAVLKAGAayvPLDPSYPAER---LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 215 HSVLSSGARVLVVDPDlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragitwrSPALFIY 294
Cdd:cd05930 78 YILEDSGAKLVLTDPD---------------------------------------------------------DLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 295 TSGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPK---FSTSCF 367
Cdd:cd05930 101 TSGSTGKPKGVMVEHRglvnLLLWMQEAYPL---TPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEevrKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 368 WDDCRQHGVTVILYVGELLRYLcnIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYV 445
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLLRLL--LQELELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 446 grcgalgkmscllrmlspfelVQFDMEAAEPV-----RDNQGFCI------PVGLGEPGLLLtkVVSQQPFVGYRGPREL 514
Cdd:cd05930 255 ---------------------VPPDDEEDGRVpigrpIPNTRVYVldenlrPVPPGVPGELY--IGGAGLARGYLNRPEL 311
|
410 420 430
....*....|....*....|....*....|....*.
gi 768006055 515 SERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDR 550
Cdd:cd05930 312 TAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGR 347
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
120-592 |
2.83e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAELGDPASLCAgeptallVLASQAVPALCMWLGLAKLGC 199
Cdd:PRK12467 518 IEAQARQHPERPALVF---GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVG-------IAVERSIEMVVGLLAVLKAGG 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 200 PTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLE-----EILPKLQAENIRCFYLSHTSPTPgvgalgaaldaapsh 274
Cdd:PRK12467 588 AYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpaglRSLCLDEPADLLCGYSGHNPEVA--------------- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 pvpadlragITWRSPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCL 350
Cdd:PRK12467 653 ---------LDPDNLAYVIYTSGSTGQPKGVAISHgalaNYVCVIAERLQL---AADDSMLMVSTFAFDLG-VTELFGAL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 351 DLGATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIR 427
Cdd:PRK12467 720 ASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 428 IWEVYGSTEGNMGLVnyVGRCGALGKMSCLLRMLSPFElvqfdmEAAEPVRDNQGFCIPVGLgePGLLLtkVVSQQPFVG 507
Cdd:PRK12467 800 LINHYGPTETTVGVS--TYELSDEERDFGNVPIGQPLA------NLGLYILDHYLNPVPVGV--VGELY--IGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 508 YRGPRELS-ERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVC 586
Cdd:PRK12467 868 YHRRPALTaERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV--LA 945
|
....*.
gi 768006055 587 VPGRHG 592
Cdd:PRK12467 946 QPGDAG 951
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
289-584 |
4.84e-16 |
|
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: 80.72 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVlqMSKMLSLS---GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPkfSTS 365
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNI--LSNALALAerlPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 366 CFWDDCRQHGVTVILYVGELLRYLCNIPQQ---PEDRTHTVRLAMGNGLR----------ADVWETFQQrFGpIRIWEVY 432
Cdd:cd05907 165 TLLDDLSEVRPTVFLAVPRVWEKVYAAIKVkavPGLKRKLFDLAVGGRLRfaasggaplpAELLHFFRA-LG-IPVYEGY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 433 GSTE------GNMGLVNYVGRCGalgkmscllrmlspfelvqfdmeaaEPVRDNQgfcipVGLGEPGLLLTK--VVsqqp 504
Cdd:cd05907 243 GLTEtsavvtLNPPGDNRIGTVG-------------------------KPLPGVE-----VRIADDGEILVRgpNV---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 505 FVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVLSQVDFLQQVNVY 583
Cdd:cd05907 289 MLGYYKNPEATAEALDA------DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVI 362
|
.
gi 768006055 584 G 584
Cdd:cd05907 363 G 363
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
139-585 |
6.68e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 80.90 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 139 GAGSVTFGELDARACQAAWALkAELGdpasLCAGEPTALLVlaSQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVL 218
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGL-AALG----VRPGDCVALLM--RNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDLRESLEEILPK--------LQAENIRCFYLS--HTSPTPGVGALGAALDAAPSHPVPADlragitwRS 288
Cdd:PRK12406 81 DSGARVLIAHADLLHGLASALPAgvtvlsvpTPPEIAAAYRISpaLLTPPAGAIDWEGWLAQQEPYDGPPV-------PQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPK---PAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYH----VMGLVVGilgclDLGATCVLAP 360
Cdd:PRK12406 154 PQSMIYTSGTTGHPKgvrRAAPTPEQAAAAEQMRALIyGLKPGIRALLTGPLYHsapnAYGLRAG-----RLGGVLVLQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR---------THT-------VRLAMgnglrADVWetfqqrfG 424
Cdd:PRK12406 229 RFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKydvsslrhvIHAaapcpadVKRAM-----IEWW-------G 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 425 PIrIWEVYGSTEgnMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAepvrdnqgfciPVGLGEPGLLLTKVVSQQP 504
Cdd:PRK12406 297 PV-IYEYYGSTE--SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGR-----------PLPQGEIGEIYSRIAGNPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 505 FVGYRGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:PRK12406 363 FTYHNKPEKRAE------IDRGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG 434
|
.
gi 768006055 585 V 585
Cdd:PRK12406 435 I 435
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-585 |
9.09e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.39 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 112 PPDTFVDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKAELGDpaslcagEPTALLVLASQAVPALCM- 190
Cdd:PRK08314 8 PETSLFHNLEVSARRYPDKTAIVFYG---RAISYRELLEEAERLAGYLQQECGV-------RKGDRVLLYMQNSPQFVIa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 191 WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLresLEEILPKLQAENIRCF----YLSHTSPTPGVGALGA 266
Cdd:PRK08314 78 YYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSEL---APKVAPAVGNLRLRHVivaqYSDYLPAEPEIAVPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 267 ALDaapSHPVPADLRAG-ITWRSP-----------------ALFIYTSGTTGLPKPAILTHERVlqMSKMLS---LSGAT 325
Cdd:PRK08314 155 LRA---EPPLQALAPGGvVAWKEAlaaglappphtagpddlAVLPYTSGTTGVPKGCMHTHRTV--MANAVGsvlWSNST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 326 ADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKfstscfWDdcRQhgvtvilYVGELL-RYLC----NIPQQPEDRT 400
Cdd:PRK08314 230 PESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------WD--RE-------AAARLIeRYRVthwtNIPTMVVDFL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 401 HTVRLA---------MGNG---LRADVWETFQQRFGpIRIWEVYGSTEgNMG--LVNYVGRcgalGKMSCLlrmLSPFel 466
Cdd:PRK08314 295 ASPGLAerdlsslryIGGGgaaMPEAVAERLKELTG-LDYVEGYGLTE-TMAqtHSNPPDR----PKLQCL---GIPT-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 467 vqFDMEAAepVRDNQGFcIPVGLGEPGLLltkVVS-QQPFVGY-RGPRELSERKLVRNvrqsGDVYYNTGDVLAMDREGF 544
Cdd:PRK08314 364 --FGVDAR--VIDPETL-EELPPGEVGEI---VVHgPQVFKGYwNRPEATAEAFIEID----GKRFFRTGDLGRMDEEGY 431
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 768006055 545 LYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK08314 432 FFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-584 |
9.49e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 80.21 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 121 ERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKAE---LGDpaslcageptALLVLASQAVPALCMWLGLAKL 197
Cdd:PRK07786 24 ARHALMQPDAPALRFLG---NTTTWRELDDRVAALAGALSRRgvgFGD----------RVLILMLNRTEFVESVLAANML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 198 GCPTAWINPHGRGMPLAHSVLSSGARVLVVDP---DLRESLEEILPKLQAenirCFYLSHTSPTPGVGALGAALDAAPSH 274
Cdd:PRK07786 91 GAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAalaPVATAVRDIVPLLST----VVVAGGSSDDSVLGYEDLLAEAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 PvPADlragITWRSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGA-TADDVVYTVLPLYHVMGLvVGILGCLDL 352
Cdd:PRK07786 167 A-PVD----IPNDSPALIMYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGAdINSDVGFVGVPLFHIAGI-GSMLPGLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 353 GATCVLAP--KFSTSCFWDDCRQHGVTVILYVGELLRYLCNiPQQPEDRTHTVR-LAMGNGLRAD-VWETFQQRFGPIRI 428
Cdd:PRK07786 241 GAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCA-EQQARPRDLALRvLSWGAAPASDtLLRQMAATFPEAQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 429 WEVYGSTEgnMGLVNyvgrCGALGKMSclLRMLSPFELVqFDMEAAEPVRDNQGfciPVGLGEPGLLLtkvvsqqpfvgY 508
Cdd:PRK07786 320 LAAFGQTE--MSPVT----CMLLGEDA--IRKLGSVGKV-IPTVAARVVDENMN---DVPVGEVGEIV-----------Y 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 509 RGPRELSErkLVRNVRQSGDVY----YNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:PRK07786 377 RAPTLMSG--YWNNPEATAEAFaggwFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
113-585 |
9.67e-16 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 80.06 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 113 PDTFVDAFERRARAQPGRALLVwtgPGAGSVTFGELDARACQAAWALkAELGdpasLCAGEpTALLVLASQAVPALCmWL 192
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVV---DGDRRLTYRELDRRADRLAAGL-RGLG----IRPGD-RVVVQLPNVAEFVVL-FF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 193 GLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVD---------PDLRESLEEIlpklqaenircfylshtsptpgvga 263
Cdd:cd05920 84 ALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPdrhagfdhrALARELAESI------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 264 lgaaldaapshpvpadlragitwRSPALFIYTSGTTGLPKPAILTHERVLQMSKM-LSLSGATADDVVYTVLPLYHVMGL 342
Cdd:cd05920 139 -----------------------PEVALFLLSGGTTGTPKLIPRTHNDYAYNVRAsAEVCGLDQDTVYLAVLPAAHNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 343 VV-GILGCLDLGATCVLAPKFS-TSCFwDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADvwETFQ 420
Cdd:cd05920 196 ACpGVLGTLLAGGRVVLAPDPSpDAAF-PLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLS--PALA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 421 QRFGPI---RIWEVYGSTEGnmgLVNYVgrcgalgkmscllRMLSPFELVQFD----MEAAEPVR--DNQGfcIPVGLGE 491
Cdd:cd05920 273 RRVPPVlgcTLQQVFGMAEG---LLNYT-------------RLDDPDEVIIHTqgrpMSPDDEIRvvDEEG--NPVPPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 492 PGLLLTkvvsqqpfvgyRGPRELSE--RKLVRNVRQ-SGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVE 568
Cdd:cd05920 335 EGELLT-----------RGPYTIRGyyRAPEHNARAfTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVE 403
|
490
....*....|....*..
gi 768006055 569 GVLSQVDFLQQVNVYGV 585
Cdd:cd05920 404 NLLLRHPAVHDAAVVAM 420
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
287-585 |
1.48e-15 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 78.46 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 287 RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSG--ATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFST 364
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlnWVVGDVTYLPLPATHIGGLW-WILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 365 -SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA---DVweTFQQRFGPIRIWEVYGSTEGNMG 440
Cdd:cd17635 80 yKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiaaDV--RFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 441 LVNYVGR----CGALGKmscllrmlsPFELVQFDmeaaepVRDNQGFCIPVGlgEPGLLLTKvvSQQPFVGYRGPRELSE 516
Cdd:cd17635 158 LCLPTDDdsieINAVGR---------PYPGVDVY------LAATDGIAGPSA--SFGTIWIK--SPANMLGYWNNPERTA 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 517 RKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17635 219 EVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEI 280
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-571 |
2.17e-15 |
|
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: 79.03 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 114 DTFVDAFERRARAQPGRALLVwtgPGAGSVTFGELDARACQAAWALkAELGdpasLCAGEpTALLVLASQA--VPAlcmW 191
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV---DGERRLSYAELDRRADRLAAGL-LALG----LRPGD-RVVVQLPNVAefVIV---F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 192 LGLAKLGC-PTAWINPHgRGMPLAHSVLSSGARVLVVDP-----DLRESLEEilpkLQAEnirCFYLSHT--SPTPGVGA 263
Cdd:COG1021 93 FALFRAGAiPVFALPAH-RRAEISHFAEQSEAVAYIIPDrhrgfDYRALARE----LQAE---VPSLRHVlvVGDAGEFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 264 LGAALDAAPSHPVPADLRAGitwrSPALFIYTSGTTGLPKPAILTH-ERVLQMSKMLSLSGATADDVVYTVLPLYHVMGL 342
Cdd:COG1021 165 SLDALLAAPADLSEPRPDPD----DVAFFQLSGGTTGLPKLIPRTHdDYLYSVRASAEICGLDADTVYLAALPAAHNFPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 343 VV-GILGCLDLGATCVLAPKFSTscfwDDC----RQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLaMGNG---LRAD 414
Cdd:COG1021 241 SSpGVLGVLYAGGTVVLAPDPSP----DTAfpliERERVTVTALVPPLALLWLDAAERSRYDLSSLRV-LQVGgakLSPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 415 VWETFQQRFGpIRIWEVYGSTEgnmGLVNY----------VGRCGalgkmscllRMLSPFELVQfdmeaaepVRDNQGfc 484
Cdd:COG1021 316 LARRVRPALG-CTLQQVFGMAE---GLVNYtrlddpeeviLTTQG---------RPISPDDEVR--------IVDEDG-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 485 IPVGLGEPGLLLTKvvsqQP--FVGY-RGPRElserklvrNVRQ-SGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGE 560
Cdd:COG1021 373 NPVPPGEVGELLTR----GPytIRGYyRAPEH--------NARAfTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGE 440
|
490
....*....|.
gi 768006055 561 NVSTHEVEGVL 571
Cdd:COG1021 441 KIAAEEVENLL 451
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
113-589 |
9.73e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 77.09 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 113 PDTFVDAFERRARAQPGRALLVwtgPGAGSVTFGELDARaCQAAWALKAELGdpasLCAGEPTALLVlaSQAVPALCMWL 192
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALI---DEDRPLSRAELRAL-VDRLAAWLAAQG----VRRGDRVAVWL--PNCIEWVVLFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 193 GLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDP-----DLRESLEEI----LPKLQAENIRCFYLSHT-SPTPGVG 262
Cdd:PRK06164 79 ACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVppdaLPPLRAIAVVDDAADATpAPAPGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 263 ALGAALDAAPSHPVPADLRAGITwrSPALFIYTSGTTGLPK------PAILTHERvlQMSKMLSLSgatADDVVYTVLPL 336
Cdd:PRK06164 159 VQLFALPDPAPPAAAGERAADPD--AGALLFTTSGTTSGPKlvlhrqATLLRHAR--AIARAYGYD---PGAVLLAALPF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 337 YHVMGLvVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA--D 414
Cdd:PRK06164 232 CGVFGF-STLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPAlgE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 415 VWETFQQRFGPIRiwEVYGSTEgnmglvnyvgrcgaLGKMSCLLRMLSPFEL------VQFDMEAAEPVRDNQ--GFCIP 486
Cdd:PRK06164 311 LAALARARGVPLT--GLYGSSE--------------VQALVALQPATDPVSVriegggRPASPEARVRARDPQdgALLPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 487 vglGEPGLLltKVVSQQPFVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHE 566
Cdd:PRK06164 375 ---GESGEI--EIRAPSLMRGYLDNPDATARALTD------DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAE 443
|
490 500
....*....|....*....|...
gi 768006055 567 VEGVLSQVDFLQQVNVYGVCVPG 589
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDG 466
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
293-585 |
1.39e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 75.23 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 293 IYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDC 371
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWAdCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 372 RQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGlvnyvgrcg 449
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtgAATVPVELVRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 450 algkmsCLLRMLSPFELVQFDMEAAEPvrdnqGFciPVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKLvrnvrqSGDV 529
Cdd:cd17638 157 ------TMCRPGDDAETVATTCGRACP-----GF--EVRIADDGEVL--VRGYNVMQGYLDDPEATAEAI------DADG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 768006055 530 YYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV 271
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
294-593 |
1.59e-14 |
|
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: 74.75 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKpAILTHERVLQMS-----KMLSLSGataDDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFW 368
Cdd:cd17633 7 FTSGTTGLPK-AYYRSERSWIESfvcneDLFNISG---EDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 369 DDCRQHGVTVILYVGELLRYLCNIpQQPEDRTHTVrLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVG-- 446
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQes 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 447 -RCGALGKmscllrmlsPFELVQFDMEAAEPvrdnqgfcipvglGEPGLLltKVVSQQPFVGYRGPRELSErklvrnvrq 525
Cdd:cd17633 160 rPPNSVGR---------PFPNVEIEIRNADG-------------GEIGKI--FVKSEMVFSGYVRGGFSNP--------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 526 sgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGRHGG 593
Cdd:cd17633 207 --DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG--IPDARFG 270
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
114-585 |
2.25e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 75.79 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 114 DTFVDAFERRaraqPGRALLVWTGpgaGSVTFGELDARACQAAWALkaelgdpASLCAGEPTALLVLASQAVPALCMwLG 193
Cdd:PRK06188 16 HLLVSALKRY----PDRPALVLGD---TRLTYGQLADRISRYIQAF-------EALGLGTGDAVALLSLNRPEVLMA-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 194 LAKL-GCPTAWINPHGRGMPLAHSVLSSGARVLVVDP----DLRESLEEILPKLQAenircfYLSHTSPTPGVGALGAAL 268
Cdd:PRK06188 81 AAQLaGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPapfvERALALLARVPSLKH------VLTLGPVPDGVDLLAAAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 269 DAAPSHPVPADLRAGITWrspalFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVMGLVVgiL 347
Cdd:PRK06188 155 KFGPAPLVAAALPPDIAG-----LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFlMCTPLSHAGGAFF--L 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 348 GCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNipqQPEDRTHT----------------VRLAMGngl 411
Cdd:PRK06188 228 PTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLD---HPDLRTRDlssletvyygaspmspVRLAEA--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 412 radvwetfQQRFGPIrIWEVYGSTEGNMgLVNYVGRCGALGKMSCLLR---MLSPFELVQfdmeaaepVRDNQGfcIPVG 488
Cdd:PRK06188 302 --------IERFGPI-FAQYYGQTEAPM-VITYLRKRDHDPDDPKRLTscgRPTPGLRVA--------LLDEDG--REVA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 489 LGEPGLLLTKvvsqQPFV--GYRGPRELSERKLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHE 566
Cdd:PRK06188 362 QGEVGEICVR----GPLVmdGYWNRPEETAEAF-------RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPRE 430
|
490
....*....|....*....
gi 768006055 567 VEGVLSQVDFLQQVNVYGV 585
Cdd:PRK06188 431 VEDVLAEHPAVAQVAVIGV 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
124-587 |
2.48e-14 |
|
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: 75.36 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALkaelgdpASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAW 203
Cdd:cd05945 1 AAANPDRPAVVEGG---RTLTYRELKERADALAAAL-------ASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 204 INPHgrgMP---LAHSVLSSGARVLVVDPDlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpadl 280
Cdd:cd05945 71 LDAS---SPaerIREILDAAKPALLIADGD-------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 281 ragitwrSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVyTVLPLYHVMGLVVGILGCLDLGATCVLA 359
Cdd:cd05945 98 -------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNwMLSDFPLGPGDVF-LNQAPFSFDLSVMDLYPALASGATLVPV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 360 PKFSTscfwDDCRQ-------HGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWE 430
Cdd:cd05945 170 PRDAT----ADPKQlfrflaeHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLfcGEVLPHKTARALQQRFPDARIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 431 VYGSTEGNMGLVNYVGRCGALGKMSCLlrmlsPFELVQFDMEAAepVRDNQGfcIPVGLGEPGLLLtkVVSQQPFVGYRG 510
Cdd:cd05945 246 TYGPTEATVAVTYIEVTPEVLDGYDRL-----PIGYAKPGAKLV--ILDEDG--RPVPPGEKGELV--ISGPSVSKGYLN 314
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 511 PRELSERKLVRNvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCV 587
Cdd:cd05945 315 NPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK 388
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
115-585 |
3.23e-14 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 75.47 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPGRALLVWTGPGAGS---VTFGELDARACQAAWALkAELGdpasLCAGEptallVLASQ-----AVP 186
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTGAprrFTYRELAALVDRVAVGL-ARLG----VGRGD-----VVSCQlpnwwEFT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 187 ALcmWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLR-----ESLEEILPKLQAenircfyLSHTSPTPGV 261
Cdd:PRK13295 95 VL--YLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaAMARRLRPELPA-------LRHVVVVGGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 262 GALG-AALDAAPSHPVPADLRAGITWRSP-----ALFIYTSGTTGLPKPAILTHERVlqMSKMLSLS---GATADDVVYT 332
Cdd:PRK13295 166 GADSfEALLITPAWEQEPDAPAILARLRPgpddvTQLIYTSGTTGEPKGVMHTANTL--MANIVPYAerlGLGADDVILM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 333 VLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNG 410
Cdd:PRK13295 244 ASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRtfLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 411 LRADVWETFQQRFGpIRIWEVYGSTEGnmGLVNYVGRCGALGKMS----CLLrmlsPFELVQfdmeaaepVRDNQGFCIP 486
Cdd:PRK13295 324 IPGALVERARAALG-AKIVSAWGMTEN--GAVTLTKLDDPDERASttdgCPL----PGVEVR--------VVDADGAPLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 487 VglGEPGLLLTKVVSQqpFVGYRGPRELSerklvrnvRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHE 566
Cdd:PRK13295 389 A--GQIGRLQVRGCSN--FGGYLKRPQLN--------GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVE 456
|
490
....*....|....*....
gi 768006055 567 VEGVLSQVDFLQQVNVYGV 585
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAY 475
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
123-585 |
4.61e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 74.91 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 123 RARAQPGRALLVWTGPGAgSVTFGELDARACQAAWALKAeLGdpasLCAGEPTALLVLASqaVPALCMWLGLAKLGC--- 199
Cdd:PRK07514 10 RAAFADRDAPFIETPDGL-RYTYGDLDAASARLANLLVA-LG----VKPGDRVAVQVEKS--PEALALYLATLRAGAvfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 200 P--TAWinphgRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRcfylshTSPTPGVGALGAALDAAPSHPVP 277
Cdd:PRK07514 82 PlnTAY-----TLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVE------TLDADGTGSLLEAAAAAPDDFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 278 ADLRAGitwrSPALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATC 356
Cdd:PRK07514 151 VPRGAD----DLAAILYTSGTTGRSKGAMLSHGNLLSNALTLvDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 357 VLAPKFSTSCFWDDCRQhgVTVI-----LYVgellRYLcnipQQPE-DRTHT--VRLAM-GNG-LRADVWETFQQRFGPi 426
Cdd:PRK07514 227 IFLPKFDPDAVLALMPR--ATVMmgvptFYT----RLL----QEPRlTREAAahMRLFIsGSApLLAETHREFQERTGH- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 427 RIWEVYGSTEGNMGLVN-YVG--RCGALGkmscllRMLSPFELVQFDMEAAEpvrdnqgfciPVGLGEPGLLltKVVSQQ 503
Cdd:PRK07514 296 AILERYGMTETNMNTSNpYDGerRAGTVG------FPLPGVSLRVTDPETGA----------ELPPGEIGMI--EVKGPN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 504 PFVGY-RGPR----ELSErklvrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQ 578
Cdd:PRK07514 358 VFKGYwRMPEktaeEFRA-----------DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVV 426
|
....*..
gi 768006055 579 QVNVYGV 585
Cdd:PRK07514 427 ESAVIGV 433
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
121-585 |
9.75e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 73.96 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 121 ERRARAQPGRALLVWTGPGAgSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLVLASQAVPALCmWLGLaKLGCP 200
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGE-VVTYRELDERSNRLAHLFRS-----LGLKRGDHVAIFMENNLRYLEVC-WAAE-RSGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 201 TAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEiLPKlQAENIR-CFYLSHTSPTPGVGALGAALDAAPSHPVPaD 279
Cdd:PRK13391 76 YTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARA-LLK-QCPGVRhRLVLDGDGELEGFVGYAEAVAGLPATPIA-D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 LRAGitwrspALFIYTSGTTG--------LPKPAILTHERVLQMSKMLSlsGATADDVVYTVLPLYHVMGLVVGILGcLD 351
Cdd:PRK13391 153 ESLG------TDMLYSSGTTGrpkgikrpLPEQPPDTPLPLTAFLQRLW--GFRSDMVYLSPAPLYHSAPQRAVMLV-IR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 352 LGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVRLAMGNG--LRADVWETFQQRFGPIr 427
Cdd:PRK13391 224 LGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKydLSSLEVAIHAAapCPPQVKEQMIDWWGPI- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 428 IWEVYGSTEGNMGLV----NYVGRCGALGK-MSCLLRMLspfelvqfdmeaaepvrDNQGFCIPVglGEPGLLLTKvvSQ 502
Cdd:PRK13391 303 IHEYYAATEGLGFTAcdseEWLAHPGTVGRaMFGDLHIL-----------------DDDGAELPP--GEPGTIWFE--GG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 503 QPFVGYRGPRELSErklvrnvRQSGDVYYNT-GDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVN 581
Cdd:PRK13391 362 RPFEYLNDPAKTAE-------ARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAA 434
|
....
gi 768006055 582 VYGV 585
Cdd:PRK13391 435 VFGV 438
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-358 |
3.40e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 72.50 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPGRALLVwtgpgagsvtFGELDARAcqaAWAlkaELGDPASLCAgepTALLVLASQAVPALCMW--- 191
Cdd:PRK12583 19 TIGDAFDATVARFPDREALV----------VRHQALRY---TWR---QLADAVDRLA---RGLLALGVQPGDRVGIWapn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 192 --------LGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRES-----LEEILPKL---QAENIRCFYLSH- 254
Cdd:PRK12583 80 caewlltqFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhamLQELLPGLaegQPGALACERLPEl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 255 -------TSPTPGVGALGAALDAaPSHPVPADL---RAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-G 323
Cdd:PRK12583 160 rgvvslaPAPPPGFLAWHELQAR-GETVSREALaerQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESlG 238
|
250 260 270
....*....|....*....|....*....|....*
gi 768006055 324 ATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK12583 239 LTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY 273
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
290-585 |
3.52e-13 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 72.17 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLqmskmLSLSGA---------TADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAP 360
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIV-----ARFSHArdpifgnqiIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIP-QQPEDRTHTVRLAMGNG-LRADVWETFQQRFGPIRIWEVYGSTEGN 438
Cdd:cd17642 261 KFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 439 MG-LVNYVGRC--GALGKmscllrmLSPFELVQ-FDMEAAEPVRDNQgfcipvgLGE---PGLLLTKvvsqqpfvGYRGP 511
Cdd:cd17642 341 SAiLITPEGDDkpGAVGK-------VVPFFYAKvVDLDTGKTLGPNE-------RGElcvKGPMIMK--------GYVNN 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 512 RELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17642 399 PEATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
139-590 |
6.67e-13 |
|
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: 70.97 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 139 GAGSVTFGELDARACQAAWALKAELGDPASLCAgeptaLLVLASQAVPALCmWLGLAKLGCPTAWINPHGRGMPLAHsVL 218
Cdd:cd05958 7 PEREWTYRDLLALANRIANVLVGELGIVPGNRV-----LLRGSNSPELVAC-WFGIQKAGAIAVATMPLLRPKELAY-IL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDLRESLEEIlpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragitwrspALFIYTSGT 298
Cdd:cd05958 80 DKARITVALCAHALTASDDI---------------------------------------------------CILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 299 TGLPKPAILTHERVLQMSKMLSLS--GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGV 376
Cdd:cd05958 109 TGAPKATMHFHRDPLASADRYAVNvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 377 TVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEG-NMGLVNYVG--RCGAL 451
Cdd:cd05958 189 TVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATG-IPIIDGIGSTEMfHIFISARPGdaRPGAT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 452 GKMscllrmLSPFELVQFDmEAAEPVRDnqgfcipvglGEPGLLLTkvvsQQPfVGYRGPRELSERKLVRnvrqsgDVYY 531
Cdd:cd05958 268 GKP------VPGYEAKVVD-DEGNPVPD----------GTIGRLAV----RGP-TGCRYLADKRQRTYVQ------GGWN 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 532 NTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:cd05958 320 ITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESR 378
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
118-585 |
6.71e-13 |
|
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: 71.45 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGRALLVWTG---PGAGSVTFGELDARACQAAWALKAeLGdpasLCAGEPTAL-LVLASQAVPALcmwLG 193
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGddtSQSRTISYRELHREVCRFAGTLLD-LG----VKKGDRVAIyMPMIPEAAVAM---LA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 194 LAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVV-DPDLRESLEEILPKLQAENIRcfyLSHTSP--------------- 257
Cdd:cd17634 129 CARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITaDGGVRAGRSVPLKKNVDDALN---PNVTSVehvivlkrtgsdidw 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 258 TPGVGALGAALDAAPShpvPADLRAGITWRSPALFIYTSGTTGLPKPAILTH--ERVLQMSKMLSLSGATADDVVYTVLP 335
Cdd:cd17634 206 QEGRDLWWRDLIAKAS---PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTAD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 336 LYHVMGLVVGILGCLDLGATCVL---APKFST-SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL----AM 407
Cdd:cd17634 283 VGWVTGHSYLLYGPLACGATTLLyegVPNWPTpARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLrilgSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 408 GNGLRADVWETFqqrfgpiriWEVYGSteGNMGLVNYVGRCGALGKMSCLLRML------SPFELVqFDMEAAepVRDNQ 481
Cdd:cd17634 363 GEPINPEAYEWY---------WKKIGK--EKCPVVDTWWQTETGGFMITPLPGAielkagSATRPV-FGVQPA--VVDNE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 482 GFCIPVGlGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGEN 561
Cdd:cd17634 429 GHPQPGG-TEGNLVITDPWPGQTRTLFGDHERFEQTYFSTF-----KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
|
490 500
....*....|....*....|....
gi 768006055 562 VSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd17634 503 LGTAEIESVLVAHPKVAEAAVVGI 526
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
290-571 |
1.40e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 70.26 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSKML-----SLSGATADDVVY-TVLPLYHVMGLVVGILGCLDLGATCVLAPKFS 363
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYlAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 364 TSCFWDDCRQHGVTVILYVGELLRYLcnipqqpedrTHTVRLAMGNGLRADVW-------------ETFQQRFGPIRIWE 430
Cdd:PLN02574 281 ASDMVKVIDRFKVTHFPVVPPILMAL----------TKKAKGVCGEVLKSLKQvscgaaplsgkfiQDFVQTLPHVDFIQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 431 VYGSTEGNMglvnyvgrCGALGKMSCLLRMLSPFELVQFDMEaAEPVRDNQGFCIPVG-LGEPGLlltkvvsQQPFV--G 507
Cdd:PLN02574 351 GYGMTESTA--------VGTRGFNTEKLSKYSSVGLLAPNMQ-AKVVDWSTGCLLPPGnCGELWI-------QGPGVmkG 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 508 YRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PLN02574 415 YLNNPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVL 472
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
221-585 |
1.64e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 69.92 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 221 GARVLVVDPDlrESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSH--PVPADLRAgitwrSPALFIYTSGT 298
Cdd:PRK05852 115 GARVVLIDAD--GPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPatSTPEGLRP-----DDAMIMFTGGT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 299 TGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATcVLAP---KFSTSCFWDDCRQH 374
Cdd:PRK05852 188 TGLPKMVPWTHANIAsSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 375 GVTVILYVGELLRYLCNIPQ-QPEDRTHT----VRlAMGNGLRADVWETFQQRFGPIRIwEVYGSTEGNMGL----VNYV 445
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAAtEPSGRKPAalrfIR-SCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVtttqIEGI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 446 GrCGALGKMSCLLRMLSPFELVQFdmeaaepVRDNQGFCIPVGLGEPGLLLTKVVSqqpfvGYRGPRELSERKLVrnvrq 525
Cdd:PRK05852 345 G-QTENPVVSTGLVGRSTGAQIRI-------VGSDGLPLPAGAVGEVWLRGTTVVR-----GYLGDPTITAANFT----- 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 526 sgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK05852 407 --DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
272-364 |
2.13e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.63 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 272 PSHPVPADLRAGITW-----RSPALFIYTSGTTGLPKPAILTHERVlqMSKMLSLSGA---TADDVVYTVLPLYHVMGLV 343
Cdd:PRK07787 108 PHVPVRLHARSWHRYpepdpDAPALIVYTSGTTGPPKGVVLSRRAI--AADLDALAEAwqwTADDVLVHGLPLFHVHGLV 185
|
90 100
....*....|....*....|.
gi 768006055 344 VGILGCLDLGATCVLAPKFST 364
Cdd:PRK07787 186 LGVLGPLRIGNRFVHTGRPTP 206
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-571 |
3.93e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 67.89 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP------KF 362
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLAlNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyrnPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 363 STSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDR-THTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNM 439
Cdd:cd05944 85 LFDNFWKLVERYRITSLSTVPTVYAALL---QVPVNAdISSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 440 GL-VNYVGRCGALGkmSCLLRMlsPFELVQFdmeaaePVRDNQGFCI-PVGLGEPGLLLtkVVSQQPFVGYRGprelSER 517
Cdd:cd05944 161 LVaVNPPDGPKRPG--SVGLRL--PYARVRI------KVLDGVGRLLrDCAPDEVGEIC--VAGPGVFGGYLY----TEG 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 518 KLVRNVrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd05944 225 NKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEAL 275
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
113-590 |
5.55e-12 |
|
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: 68.29 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 113 PDTF---VDAFERRARAQPGRALLVWTGPGAGS--VTFGELDARACQAAWALKAE---LGDpaslcagepTALLVLASQA 184
Cdd:cd05970 13 PENFnfaYDVVDAMAKEYPDKLALVWCDDAGEEriFTFAELADYSDKTANFFKAMgigKGD---------TVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 185 VPALCMwLGLAKLGC----PTAWINPHGrgmpLAHSVLSSGARVLVVD--PDLRESLEEILPKLQAENIRCfyLSHTSPT 258
Cdd:cd05970 84 EFWYSL-LALHKLGAiaipATHQLTAKD----IVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLV--WVGDPVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 259 PG-VGALGAALDAAPSHPVPADlRAGITWRSPALFIYTSGTTGLPKpaILTHERVLQMSKMLSLS---GATADDVVYTVL 334
Cdd:cd05970 157 EGwIDFRKLIKNASPDFERPTA-NSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKywqNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 335 PL---YHVMGLVVG--ILGC----LDLGatcvlapKFSTSCFWDDCRQHGVTVILYVGELLRYLCNipqqpEDRTH---- 401
Cdd:cd05970 234 DTgwgKAVWGKIYGqwIAGAavfvYDYD-------KFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-----EDLSRydls 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 402 TVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVG---RCGALGKMScllrmlsPfelvQFDMEaaep 476
Cdd:cd05970 302 SLRYCTtaGEALNPEVFNTFKEKTG-IKLMEGFGQTETTLTIATFPWmepKPGSMGKPA-------P----GYEID---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 477 VRDNQGFCIPVGlgEPGLLLTKVVSQQP---FVGY-RGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLG 552
Cdd:cd05970 366 LIDREGRSCEAG--EEGEIVIRTSKGKPvglFGGYyKDAEKTAE------VWHDG--YYHTGDAAWMDEDGYLWFVGRTD 435
|
490 500 510
....*....|....*....|....*....|....*...
gi 768006055 553 DTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:cd05970 436 DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
140-585 |
5.88e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.25 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 140 AGSVTFGELDARACQAAWALKAelgdpasLCAGEPTALLVLASQA---VPALCmwlGLAKLGCPTAWINPHGRGMPLAHS 216
Cdd:PRK13382 66 LGTLTWRELDERSDALAAALQA-------LPIGEPRVVGIMCRNHrgfVEALL---AANRIGADILLLNTSFAGPALAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 217 VLSSGARVLVVDPDLRESLEEILPKL-QAENIrcfyLSHTSPTPGVGALGAALDAAPSHPVPADlragitwRSPALFIYT 295
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCpQATRI----VAWTDEDHDLTVEVLIAAHAGQRPEPTG-------RKGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 296 SGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLvVGILGCLDLGATCVLAPKFSTSCFWDDCRQH 374
Cdd:PRK13382 205 SGTTGTPKGARRSGPGgIGTLKAILDRTPWRAEEPTVIVAPMFHAWGF-SQLVLAASLACTIVTRRRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 375 GVTVILYVGELLRYLCNIPQQPEDR--THTVRLAMGNG--LRADVWETFQQRFGPIrIWEVYGSTEGNMglvnyvgrcga 450
Cdd:PRK13382 284 RATGLAVVPVMFDRIMDLPAEVRNRysGRSLRFAAASGsrMRPDVVIAFMDQFGDV-IYNNYNATEAGM----------- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 451 lgkmsclLRMLSPFELVQFDMEAAEP-------VRDNQGFCIPVglGEPGLLLTKVVSQqpFVGYRGPRElserklvrnv 523
Cdd:PRK13382 352 -------IATATPADLRAAPDTAGRPaegteirILDQDFREVPT--GEVGTIFVRNDTQ--FDGYTSGST---------- 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006055 524 RQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK13382 411 KDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGV 472
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
288-573 |
8.42e-12 |
|
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: 67.41 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 366
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERlGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIrIWEVYGSTEgnmglvny 444
Cdd:cd05903 174 ALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRtfVCGGATVPRSLARRAAELLGAK-VCSAYGSTE-------- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 445 vgRCGALGKMS---CLLRMLS---PFELVQFDmeaaepVRDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELserk 518
Cdd:cd05903 245 --CPGAVTSITpapEDRRLYTdgrPLPGVEIK------VVDDTGATLAP--GVEGELLSR--GPSVFLGYLDRPDL---- 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 519 lvrNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQ 573
Cdd:cd05903 309 ---TADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
120-574 |
1.80e-11 |
|
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: 66.60 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKA---ELGDPASLCAgEPTALLVLASqavpalcmwLGLAK 196
Cdd:cd17651 1 FERQAARTPDAPALVAEG---RRLTYAELDRRANRLAHRLRArgvGPGDLVALCA-RRSAELVVAL---------LAILK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 197 LGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPklqaenircfylshtsptPGVGALGAALDAAPSHPV 276
Cdd:cd17651 68 AGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV------------------AVTLLDQPGAAAGADAEP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 277 PADLRAGitwrSPALFIYTSGTTGLPKPAILTH----------ERVLQM---SKMLSLSGATADDVVYTVLPlyhvmglv 343
Cdd:cd17651 130 DPALDAD----DLAYVIYTSGSTGRPKGVVMPHrslanlvawqARASSLgpgARTLQFAGLGFDVSVQEIFS-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 344 vgilgCLDLGATCVLAP---KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ 420
Cdd:cd17651 198 -----TLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 421 Q---RFGPIRIWEVYGSTEgnmglvNYVGRCGALGKMSC-------LLRMLSPFELVQFDmEAAEPVrdnqgfciPVglG 490
Cdd:cd17651 273 EfcaGLPGLRLHNHYGPTE------THVVTALSLPGDPAawpapppIGRPIDNTRVYVLD-AALRPV--------PP--G 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 491 EPGLLLTKVVSQQPfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:cd17651 336 VPGELYIGGAGLAR--GYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAA 413
|
....
gi 768006055 571 LSQV 574
Cdd:cd17651 414 LARH 417
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
124-573 |
2.65e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 66.22 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVWTGPgagSVTFGELDARACQAAwALKAELGdpasLCAGEPTA-LLVLASQAVPALcmwLGLAKLGCPTA 202
Cdd:PRK06178 43 ARERPQRPAIIFYGH---VITYAELDELSDRFA-ALLRQRG----VGAGDRVAvFLPNCPQFHIVF---FGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 203 WINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSP-TPGVGALGAALDAAPSHPVPADL- 280
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPaEPTLPLPDSLRAPRLAAAGAIDLl 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 281 ------RAGITWRSPAL-----FIYTSGTTGLPKPAILTHERVLQMSKMLSLSGAT--ADDVVYTVLPLYHVMGLVVGIL 347
Cdd:PRK06178 192 palracTAPVPLPPPALdalaaLNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVggEDSVFLSFLPEFWIAGENFGLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 348 GCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG----LRADVWETFQQRF 423
Cdd:PRK06178 272 FPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfvkkLNPDYRQRWRALT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 424 GPIRIWEVYGSTE-------------GNMGLVNYVGRCGalgkmscLLRMLSPFELVQFDMEAaepvrdnqgfciPVGLG 490
Cdd:PRK06178 352 GSVLAEAAWGMTEthtcdtftagfqdDDFDLLSQPVFVG-------LPVPGTEFKICDFETGE------------LLPLG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 491 EPGLLLtkVVSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:PRK06178 413 AEGEIV--VRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEAL 483
|
...
gi 768006055 571 LSQ 573
Cdd:PRK06178 484 LGQ 486
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
288-597 |
3.18e-11 |
|
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: 65.04 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHeRVLQMSKMLSLS--GATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKfsTS 365
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA-ANLLASAAGLHSrlGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLER--NQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 366 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG-LRADVWETFQQRfgPIRIWEVYGSTEgnMGLVNY 444
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGApIPPELLERAADR--GIPLYTTYGMTE--TASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 445 VGRCGALGKMSCllrmlspfelvqfdmeaAEPVRDNQgfcipVGLGEPGLLLTKVVSQqpFVGYRGPRELSERklvrnvr 524
Cdd:cd17630 153 TKRPDGFGRGGV-----------------GVLLPGRE-----LRIVEDGEIWVGGASL--AMGYLRGQLVPEF------- 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006055 525 qSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGRHGGHQHV 597
Cdd:cd17630 202 -NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDEELGQRPV 271
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
144-590 |
3.40e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 65.62 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 144 TFGELDARACQAAWALKAELGDPASLCAGeptaLLVLASQAVPALcmwLGLAKLGC---P--TAWINPhgrgmPLAHSVL 218
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAG----LLPRTPELVVTI---LGIWRLGAvyqPlfTAFGPK-----AIEHRLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDLRESLEEilpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragitwrSPALFIYTSGT 298
Cdd:cd05973 70 TSGARLVVTDAANRHKLDS--------------------------------------------------DPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 299 TGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLG-ATCVLAPKFSTSCFWDDCRQHGV 376
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAYLRDAvDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 377 TVILYVGELLRYL----CNIPQQPEDRTHTVRLAmGNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVG-----R 447
Cdd:cd05973 180 TNLAGSPTAYRLLmaagAEVPARPKGRLRRVSSA-GEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHHAlehpvH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 448 CGALGkmscllRMLSPFELVQFDMEAAEPvrdnqgfcipvGLGEPGLLLTKVvSQQP---FVGYRGPRELSerklvrnvr 524
Cdd:cd05973 258 AGSAG------RAMPGWRVAVLDDDGDEL-----------GPGEPGRLAIDI-ANSPlmwFRGYQLPDTPA--------- 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006055 525 QSGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:cd05973 311 IDGG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPER 375
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
289-590 |
6.41e-11 |
|
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: 64.83 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVLQ--MSKMLSLsGATADDVVY-TVLPLYhVMGLVVGILGCLDLGATCVL-APKFST 364
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLHPDDIYWcTADPGW-VTGTVYGIWAPWLNGVTNVVyEGRFDA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 365 SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPE---DRTHT-VRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTE-GNM 439
Cdd:cd05969 169 ESWYGIIERVKVTVWYTAPTAIRMLMKEGDELArkyDLSSLrFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 440 GLVNYVG---RCGALGKmscllrmlsPFELVqfdmEAAepVRDNQGFCIPVGlgEPGLLLTKVVSQQPFVGYRGPRELSE 516
Cdd:cd05969 248 MIANYPCmpiKPGSMGK---------PLPGV----KAA--VVDENGNELPPG--TKGILALKPGWPSMFRGIWNDEERYK 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 517 RKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:cd05969 311 NSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLR 377
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
294-378 |
6.69e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.00 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKPAILTHervlqmsKMLSLSGA------------TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK 361
Cdd:PLN02246 186 YSSGTTGLPKGVMLTH-------KGLVTSVAqqvdgenpnlyfHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK 258
|
90
....*....|....*..
gi 768006055 362 FSTSCFWDDCRQHGVTV 378
Cdd:PLN02246 259 FEIGALLELIQRHKVTI 275
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
119-571 |
8.66e-11 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 64.82 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 119 AFERRARAQPGRALLVWTGP-GAG-SVTFGELDARACQAAWALKA---ELGDPASLcageptaLLVLASQAVPALcmwLG 193
Cdd:cd05968 66 LLDKWLADTRTRPALRWEGEdGTSrTLTYGELLYEVKRLANGLRAlgvGKGDRVGI-------YLPMIPEIVPAF---LA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 194 LAKLGcptAWINPHGRGM---PLAHSVLSSGARVLVV-DPDLRESLE-EILPKLQAENIRCFYLSHTSPTPGVGALGAAL 268
Cdd:cd05968 136 VARIG---GIVVPIFSGFgkeAAATRLQDAEAKALITaDGFTRRGREvNLKEEADKACAQCPTVEKVVVVRHLGNDFTPA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 269 DAAPSHP-----VPADLRAGITWRSPALFIYTSGTTGLPKPAILTH-----ERVLQMSKMLSLSgatADDVVYTVLPLYH 338
Cdd:cd05968 213 KGRDLSYdeekeTAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQDMYFQFDLK---PGDLLTWFTDLGW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 339 VMGLVVgILGCLDLGATCVL---APKFSTSC-FWDDCRQHGVTVILYVGELLRYL---CNIPQQPEDRThTVRLAMGNG- 410
Cdd:cd05968 290 MMGPWL-IFGGLILGATMVLydgAPDHPKADrLWRMVEDHEITHLGLSPTLIRALkprGDAPVNAHDLS-SLRVLGSTGe 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 411 -LRADVWETFQQRFGpiriwevygstEGNMGLVNYVGRCGALGKMSC--LLRMLSP--FELVQFDMEAAepVRDNQGFCI 485
Cdd:cd05968 368 pWNPEPWNWLFETVG-----------KGRNPIINYSGGTEISGGILGnvLIKPIKPssFNGPVPGMKAD--VLDESGKPA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 486 PVGLGEpgLLLTKvvsqqPFVGY-RGPRELSERKLVRNVRQSGDVYYNtGDVLAMDREGFLYFRDRLGDTFRWKGENVST 564
Cdd:cd05968 435 RPEVGE--LVLLA-----PWPGMtRGFWRDEDRYLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGP 506
|
....*..
gi 768006055 565 HEVEGVL 571
Cdd:cd05968 507 AEIESVL 513
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
124-588 |
1.18e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.26 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 124 ARAQPGRALLVWTGPGAgSVTFGELDARACqaawALKAELGDpASLCAGEPTALLvlASQAVPALCMWLGLAKLGCPTAW 203
Cdd:PRK13390 7 AQIAPDRPAVIVAETGE-QVSYRQLDDDSA----ALARVLYD-AGLRTGDVVALL--SDNSPEALVVLWAALRSGLYITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 204 INPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAEnircfyLSHTSPTPGVgalgaaldaapshpvpADLRAG 283
Cdd:PRK13390 79 INHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLR------LSFGGEIDGF----------------GSFEAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 284 ITWRSP--------ALFIYTSGTTGLPK---PAILTHERVLQMSKMLSLSGA----TADDVVYTVLPLYHVMGLV-VGIL 347
Cdd:PRK13390 137 LAGAGPrlteqpcgAVMLYSSGTTGFPKgiqPDLPGRDVDAPGDPIVAIARAfydiSESDIYYSSAPIYHAAPLRwCSMV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 348 GCldLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTvrlamgNGLRA----------DVWE 417
Cdd:PRK13390 217 HA--LGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDV------SSLRAvihaaapcpvDVKH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 418 TFQQRFGPIrIWEVYGSTEGN-MGLVN---YVGRCGALGKmscllRMLSPFELVqfdmeaaepvrDNQGFCIPVglGEPG 493
Cdd:PRK13390 289 AMIDWLGPI-VYEYYSSTEAHgMTFIDspdWLAHPGSVGR-----SVLGDLHIC-----------DDDGNELPA--GRIG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 494 LLLTKvVSQQPFVGYRGPRELSErklvrnVRQSGDVYYNT-GDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLS 572
Cdd:PRK13390 350 TVYFE-RDRLPFRYLNDPEKTAA------AQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT 422
|
490
....*....|....*.
gi 768006055 573 QVDFLQQVNVYGVCVP 588
Cdd:PRK13390 423 MHPAVHDVAVIGVPDP 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
113-358 |
2.69e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 113 PDTFVDAFERRARAQPGR-ALLVWTGPGAGSV--TFGELD--ARACQAAWALKAELGDPASLcageptaLLVLASQAVPA 187
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRlALRFLADDPGEGVvlSYRDLDlrARTIAAALQARASFGDRAVL-------LFPSGPDYVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 188 L--CMWLG-LAKLGCPTAWINPHGRGMpLAHSVLSSGARVLVVDPDLRESLEEiLPKLQAENircfylshtspTPGVGAL 264
Cdd:PRK05691 81 FfgCLYAGvIAVPAYPPESARRHHQER-LLSIIADAEPRLLLTVADLRDSLLQ-MEELAAAN-----------APELLCV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 265 GAALdaapshPVPADlragiTWRSPAL------FI-YTSGTTGLPKPAILTHERVLQMSKMLSLS---GATADDVVYTVL 334
Cdd:PRK05691 148 DTLD------PALAE-----AWQEPALqpddiaFLqYTSGSTALPKGVQVSHGNLVANEQLIRHGfgiDLNPDDVIVSWL 216
|
250 260
....*....|....*....|....
gi 768006055 335 PLYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK05691 217 PLYHDMGLIGGLLQPIFSGVPCVL 240
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
118-575 |
3.07e-10 |
|
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: 62.71 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPgrALLVWTGPGaGSVTFGELDARACQAAWALKaelgdPASLCAGEPTALLVLASQAvpalcmWLglakl 197
Cdd:cd17653 1 DAFERIAAAHP--DAVAVESLG-GSLTYGELDAASNALANRLL-----QLGVVPGDVVPLLSDRSLE------ML----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 198 gcptAWInphgrgmpLAhsVLSSGARVLVVDPDL-RESLEEILPKLQAenirCFYLSHTSPtpgvgalgaaldaapshpv 276
Cdd:cd17653 62 ----VAI--------LA--ILKAGAAYVPLDAKLpSARIQAILRTSGA----TLLLTTDSP------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 277 padlragitwRSPALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVL-PLYHVMGLVvgILGCLDLGA 354
Cdd:cd17653 105 ----------DDLAYIIFTSGSTGIPKGVMVPHRGVLNyVSQPPARLDVGPGSRVAQVLsIAFDACIGE--IFSTLCNGG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 355 TCVLAPKFSTscFWDDCRQhgVTVILYVGELLRYLcniPQQPEDRTHTVRLAmGNGLRADVWETFqqRFGPiRIWEVYGS 434
Cdd:cd17653 173 TLVLADPSDP--FAHVART--VDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRW--SPGR-RLYNAYGP 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 435 TEgnmglvnyvgrCgalgKMSCLLRMLSPFELVQFdmeaAEPVRdNQGFCI------PVGLGEPGLLLtkVVSQQPFVGY 508
Cdd:cd17653 242 TE-----------C----TISSTMTELLPGQPVTI----GKPIP-NSTCYIldadlqPVPEGVVGEIC--ISGVQVARGY 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 509 RGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVD 575
Cdd:cd17653 300 LGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ 366
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
139-437 |
3.16e-10 |
|
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: 62.67 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 139 GAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTAllVLASQAVPALcmwlgLAKLGcptawinphgrgmplahsVL 218
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKA-----AGVRPGDLVA--VTLPKGPEQV-----VAVLG------------------IL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDL-RESLEEILPKLQAenirCFYLSHTSPTPGVGAL--GAALDAAPSHPVPADLRAGITWRSPALFIYT 295
Cdd:cd12114 59 AAGAAYVPVDIDQpAARREAILADAGA----RLVLTDGPDAQLDVAVfdVLILDLDALAAPAPPPPVDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 296 SGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAP--KFSTSCFW- 368
Cdd:cd12114 135 SGSTGTPKGVMISHRaalnTILDINRRFAV---GPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDeaRRRDPAHWa 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006055 369 DDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEG 437
Cdd:cd12114 211 ELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLlsGDWIPLDLPARLRALAPDARLISLGGATEA 281
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
289-571 |
3.74e-10 |
|
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: 62.45 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHeRVL-------QMSKMLSlsgATADDVVYTVLPLYHVMGLVVGILGCLDLGATcVLA-- 359
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAH-RVLlghlpgvQFPFNLF---PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVP-VLAhr 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 360 -PKFSTSCFWDDCRQHGVTVILYVGELLRYlcnIPQQPEDRTHTVR--LAMGNG---LRADVWETFQQRFGpIRIWEVYG 433
Cdd:cd05971 165 mTKFDPKAALDLMSRYGVTTAFLPPTALKM---MRQQGEQLKHAQVklRAIATGgesLGEELLGWAREQFG-VEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 434 STEGNMglvnYVGRCGALgkmscllrmlspFELVQFDMEAAEP-----VRDNQGFCIPVG-LGEPGLLLTKVVSqqpFVG 507
Cdd:cd05971 241 QTECNL----VIGNCSAL------------FPIKPGSMGKPIPghrvaIVDDNGTPLPPGeVGEIAVELPDPVA---FLG 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 508 YRGPRELSERKLVrnvrqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd05971 302 YWNNPSATEKKMA------GD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
120-585 |
4.65e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 62.26 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWTGPGAGSV-TFGELDARACQAAWALKaELGdpasLCAGEPTAllVLASQAVPALCMWLGLAKLG 198
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGEVHRyTYAEVAERARRLANALR-RLG----VKPGDRVA--TLAWNTHRHLELYYAVPGMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 199 CPTAWINPhgRGMP--LAHSVLSSGARVLVVDPDLRESLEEILPKLqaenircfylshtsPT-PGVGALGAALDAAPSHP 275
Cdd:cd12119 75 AVLHTINP--RLFPeqIAYIINHAEDRVVFVDRDFLPLLEAIAPRL--------------PTvEHVVVMTDDAAMPEPAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 276 VPA----DLRAG----ITW-----RSPALFIYTSGTTGLPKPAILTHER-VLQmskmlSLSGATAD-------DVVYTVL 334
Cdd:cd12119 139 VGVlayeELLAAespeYDWpdfdeNTAAAICYTSGTTGNPKGVVYSHRSlVLH-----AMAALLTDglglsesDVVLPVV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 335 PLYHVMGLVVGILGCLdLGATCVL-APKFSTSCFWDDCRQHGVTVILYVGE----LLRYLCNIPQqpeDRTHTVRLAMGN 409
Cdd:cd12119 214 PMFHVNAWGLPYAAAM-VGAKLVLpGPYLDPASLAELIEREGVTFAAGVPTvwqgLLDHLEANGR---DLSSLRRVVIGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 410 G-LRADVWETFQQRFgpIRIWEVYGSTEgnmglvnyvgrCGALGKMSCLlrmlsPFELVQFDMEAAEPVRDNQGFCIP-V 487
Cdd:cd12119 290 SaVPRSLIEAFEERG--VRVIHAWGMTE-----------TSPLGTVARP-----PSEHSNLSEDEQLALRAKQGRPVPgV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 488 GL---GEPGLLLTK-------VVSQQPFV--GYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTF 555
Cdd:cd12119 352 ELrivDDDGRELPWdgkavgeLQVRGPWVtkSYYKNDEESEALTE-------DGWLRTGDVATIDEDGYLTITDRSKDVI 424
|
490 500 510
....*....|....*....|....*....|
gi 768006055 556 RWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:cd12119 425 KSGGEWISSVELENAIMAHPAVAEAAVIGV 454
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
278-585 |
3.20e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 59.44 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 278 ADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSG-ATADDVVYTVLPLYHVMGLVVGILGCLDLGATC 356
Cdd:PRK09088 126 PADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 357 VLAPKF--STSCFWDDCRQHGVTVILYVGELLRYLCNIPQ-QPEDRTHTVRLAMGNG--LRADVWETFQQrfgPIRIWEV 431
Cdd:PRK09088 206 LVSNGFepKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGfDAAALRHLTALFTGGAphAAEDILGWLDD---GIPMVDG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 432 YGSTEG--------NMGLVNyvGRCGALGkmscllrmlSPFELVQFDmeaaepVRDNQGFCIPVglGEPGLLLTKVVSQQ 503
Cdd:PRK09088 283 FGMSEAgtvfgmsvDCDVIR--AKAGAAG---------IPTPTVQTR------VVDDQGNDCPA--GVPGELLLRGPNLS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 504 PfvGY-RGPRELSERKlvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 582
Cdd:PRK09088 344 P--GYwRRPQATARAF-------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAV 414
|
...
gi 768006055 583 YGV 585
Cdd:PRK09088 415 VGM 417
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
290-593 |
3.35e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 59.65 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHE----RVLQMSKML--SLSGATADDVVYTV--LPLYHVMGLVVGILGCLDLGATCVLAPK 361
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRnivaNVLQMEAWLqpAFEKKPRPDQLNFVcaLPLYHIFALTVCGLLGMRTGGRNILIPN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 362 -FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGL---RAdVWETFQQRFG-PIRiwEVYGSTE 436
Cdd:PRK07059 287 pRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMavqRP-VAERWLEMTGcPIT--EGYGLSE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 gnmglVNYVGRCgalgkmscllrmlSPFELVQFDMEAAEP-------VRDNQGFCIPvgLGEPGLLLTKvvSQQPFVGYR 509
Cdd:PRK07059 364 -----TSPVATC-------------NPVDATEFSGTIGLPlpstevsIRDDDGNDLP--LGEPGEICIR--GPQVMAGYW 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 510 GPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPG 589
Cdd:PRK07059 422 NRPDETAKVM------TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG--VPD 493
|
....
gi 768006055 590 RHGG 593
Cdd:PRK07059 494 EHSG 497
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
290-365 |
3.65e-09 |
|
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: 59.38 E-value: 3.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 365
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSA 168
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
205-585 |
4.71e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 59.01 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 205 NPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENI----------------------------RCFYLSHTS 256
Cdd:PRK05677 106 NPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVivtevadmlpplkrllinavvkhvkkmvPAYHLPQAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 257 PTPGVGALGAALDAAPSHPVPADLragitwrspALFIYTSGTTGLPKPAILTHE----RVLQMSKMLSLSGATADDVVYT 332
Cdd:PRK05677 186 KFNDALAKGAGQPVTEANPQADDV---------AVLQYTGGTTGVAKGAMLTHRnlvaNMLQCRALMGSNLNEGCEILIA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 333 VLPLYHVMGLVVGILGCLDLGATCVLAPK-FSTSCFWDDCRQHGVTVILYVGELLRYLCNIP--QQPEDRTHTVRLAMGN 409
Cdd:PRK05677 257 PLPLYHIYAFTFHCMAMMLIGNHNILISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEafRKLDFSALKLTLSGGM 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 410 GLRADVWETFQQRFGpIRIWEVYGSTEGN-MGLVNYVG--RCGALGkmscllrMLSPFELVQfdmeaaepVRDNQGFCIP 486
Cdd:PRK05677 337 ALQLATAERWKEVTG-CAICEGYGMTETSpVVSVNPSQaiQVGTIG-------IPVPSTLCK--------VIDDDGNELP 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 487 vgLGEPGLLLTKvvSQQPFVGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHE 566
Cdd:PRK05677 401 --LGEVGELCVK--GPQVMKGYWQRPEATDEIL------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNE 470
|
410
....*....|....*....
gi 768006055 567 VEGVLSQVDFLQQVNVYGV 585
Cdd:PRK05677 471 LEDVLAALPGVLQCAAIGV 489
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
143-585 |
4.78e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 59.02 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 143 VTFGELDARACQAAWALKAElgdpaslcAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGA 222
Cdd:PRK07638 27 LTYKDWFESVCKVANWLNEK--------ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 223 RVLVVDpdlreslEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHpvpadlragitwrSPALFIYTSGTTGLP 302
Cdd:PRK07638 99 DMIVTE-------RYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQN-------------APFYMGFTSGSTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 303 KPAILTHErvlqmSKMLSLS------GATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFWDDCRQHGV 376
Cdd:PRK07638 159 KAFLRAQQ-----SWLHSFDcnvhdfHMKREDSVLIAGTLVHSLFLY-GAISTLYVGQTVHLMRKFIPNQVLDKLETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 377 TVILYVGELLRYLCNIPQQPEdrtHTVR-LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnMGLVNYVGRCGALGKMS 455
Cdd:PRK07638 233 SVMYTVPTMLESLYKENRVIE---NKMKiISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE--LSFVTALVDEESERRPN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 456 CLLRmlsPFELVQFDMEAAEPVRdnqgfCIPvglGEPGLLLTKvvSQQPFVGY----RGPRELSErklvrnvrqsgDVYY 531
Cdd:PRK07638 308 SVGR---PFHNVQVRICNEAGEE-----VQK---GEIGTVYVK--SPQFFMGYiiggVLARELNA-----------DGWM 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 532 NTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 585
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGV 417
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
290-571 |
4.94e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 59.06 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSKM-LSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLA-----PKFS 363
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRAcLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAynplyPKKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 364 TScFWDDCRqhgVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEGNMgl 441
Cdd:PRK06334 266 VE-MIDEAK---VTFLGSTPVFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQLRQGYGTTECSP-- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 442 VNYVGRCGALGKMSCllrmlspfelVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQqpFVGYrgpreLSERKLVR 521
Cdd:PRK06334 340 VITINTVNSPKHESC----------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL--FSGY-----LGEDFGQG 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 768006055 522 NVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PRK06334 403 FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
114-584 |
5.88e-09 |
|
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: 59.01 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 114 DTFVDAF-ERRARAQpgRALLVWTGPGAGSVTFGELDAR--ACQAAW-----ALKAELGDPASLCAGEPTALLVLASQ-- 183
Cdd:cd17632 29 ATVMTGYaDRPALGQ--RATELVTDPATGRTTLRLLPRFetITYAELwervgAVAAAHDPEQPVRPGDFVAVLGFTSPdy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 184 -AVPALCMWLGLAKL----GCPTAWINP------------HGRGMPLA-HSVLSSGA--RVLVVD--PDL---RESLEEI 238
Cdd:cd17632 107 aTVDLALTRLGAVSVplqaGASAAQLAPilaeteprllavSAEHLDLAvEAVLEGGTppRLVVFDhrPEVdahRAALESA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 239 LPKLQAENIrcfylshtsptpGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKM 318
Cdd:cd17632 187 RERLAAVGI------------PVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 319 LSLSGATADDVVYTV--LPLYHVMGLVVgILGCLDLGATCVLAPKFSTSCFWDD---CRQHGVTVILYVGELL--RYlcn 391
Cdd:cd17632 255 VSSIQDIRPPASITLnfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLFDDlalVRPTELFLVPRVCDMLfqRY--- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 392 ipQQPEDR---THTVRLAMGNGLRADVWE----------------------TFQQRFGPIRIWEVYGSTEGNMGLVN-YV 445
Cdd:cd17632 331 --QAELDRrsvAGADAETLAERVKAELRErvlggrllaavcgsaplsaemkAFMESLLDLDLHDGYGSTEAGAVILDgVI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 446 GRCGALGkmsclLRMLSPFELVQFDMEAAEPvrdnqgfcipvglgePGLLLTKvvSQQPFVGY-RGPRELSErklVRNvr 524
Cdd:cd17632 409 VRPPVLD-----YKLVDVPELGYFRTDRPHP---------------RGELLVK--TDTLFPGYyKRPEVTAE---VFD-- 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 525 qsGDVYYNTGDVLAM---DRegfLYFRDRLGDTFRW-KGENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:cd17632 462 --EDGFYRTGDVMAElgpDR---LVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYG 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
120-573 |
5.93e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAelgdpaslCAGEPTALLVLASQAVPALCMWLgLAKLGC 199
Cdd:PRK12316 517 FEEQVERTPEAPALAF---GEETLDYAELNRRANRLAHALIE--------RGVGPDVLVGVAMERSIEMVVAL-LAILKA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 200 PTAWInPHGRGMP---LAHSVLSSGARVLVVDPDLRE--SLEEILPKLQAENIRCFYLSHTSPTPGVGalgaaldaapsh 274
Cdd:PRK12316 585 GGAYV-PLDPEYPaerLAYMLEDSGVQLLLSQSHLGRklPLAAGVQVLDLDRPAAWLEGYSEENPGTE------------ 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 pvpadlragITWRSPALFIYTSGTTGLPKPAILTHeRVLQ--MSKMLSLSGATADDVVYTVLPLYHVMGlVVGILGCLDL 352
Cdd:PRK12316 652 ---------LNPENLAYVIYTSGSTGKPKGAGNRH-RALSnrLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMS 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 353 GATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIW 429
Cdd:PRK12316 721 GARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 430 EVYGSTEGNMGL-----VNYVGRCGALGKMSCLLRMLspfelvqfdmeaaepVRDNQGFCIPVG-LGEpgLLLTKVVSQQ 503
Cdd:PRK12316 801 NLYGPTEAAIDVthwtcVEEGGDSVPIGRPIANLACY---------------ILDANLEPVPVGvLGE--LYLAGRGLAR 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 504 pfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQ 573
Cdd:PRK12316 864 ---GYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 930
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
275-572 |
1.01e-08 |
|
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: 57.77 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 275 PVPADLRAGitwrspALFIYTSGTTGLPK------PAILTHErVLQMSKMLsLSGATADDVVYTVLPLYHVMGLVVGILG 348
Cdd:cd05929 119 TPIEDEAAG------WKMLYSGGTTGRPKgikrglPGGPPDN-DTLMAAAL-GFGPGADSVYLSPAPLYHAAPFRWSMTA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 349 cLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVRLAMGNGLRADVWetFQQR---F 423
Cdd:cd05929 191 -LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydLSSLKRVIHAAAPCPPW--VKEQwidW 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 424 GPIRIWEVYGSTEGN-MGLVN---------YVGRCGaLGKMSCL---LRMLSPFELVQFDMEAAEPVrdnqgfcipvglg 490
Cdd:cd05929 268 GGPIIWEYYGGTEGQgLTIINgeewlthpgSVGRAV-LGKVHILdedGNEVPPGEIGEVYFANGPGF------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 491 epgllltkvvsqQPFVGYRGPRELSERKLVRNVrqsGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:cd05929 334 ------------EYTNDPEKTAAARNEGGWSTL---GDVGY-------LDEDGYLYLTDRRSDMIISGGVNIYPQEIENA 391
|
..
gi 768006055 571 LS 572
Cdd:cd05929 392 LI 393
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
109-355 |
1.10e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 58.13 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 109 SRQPPD----TFVDAFERRARAQPGRALLVWTGPGAGS---VTFGELDARA---CQAAWALKAELGDPaslcageptaLL 178
Cdd:PRK12582 40 SRHPLGpyprSIPHLLAKWAAEAPDRPWLAQREPGHGQwrkVTYGEAKRAVdalAQALLDLGLDPGRP----------VM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 179 VLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVL---VVDPDLRESLEEILPKLQAENIRCfyLSHT 255
Cdd:PRK12582 110 ILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAKLKHLFDLVkprVVFAQSGAPFARALAALDLLDVTV--VHVT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 256 SPTPGVGALGAALDAapSHPVPADL---RAGITWRSPALFIYTSGTTGLPKPAILTHER---VLQMSKMLSLSGATAD-D 328
Cdd:PRK12582 188 GPGEGIASIAFADLA--ATPPTAAVaaaIAAITPDTVAKYLFTSGSTGMPKAVINTQRMmcaNIAMQEQLRPREPDPPpP 265
|
250 260
....*....|....*....|....*..
gi 768006055 329 VVYTVLPLYHVMGLVVGILGCLDLGAT 355
Cdd:PRK12582 266 VSLDWMPWNHTMGGNANFNGLLWGGGT 292
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
139-582 |
1.69e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 57.30 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 139 GAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLVLASQAVPAlcMWLGLAKLGCPTAWINPHGRGMPLAHSVL 218
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRA-----RGVGPGDRVAVYLPRSARLVA--AMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 219 SSGARVLVVDPDLRESLeeilpklqaenircfylSHTSPTPGVGALGAALDAAPSHPVPADlragitwRSPALFIYTSGT 298
Cdd:cd12116 82 DAEPALVLTDDALPDRL-----------------PAGLPVLLLALAAAAAAPAAPRTPVSP-------DDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 299 TGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPKFSTS---CFWDDCRQH 374
Cdd:cd12116 138 TGRPKGVVVSHRNLVnFLHSMRERLGLGPGDRLLAVTTYAFDIS-LLELLLPLLAGARVVIAPRETQRdpeALARLIEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 375 GVTVILYVGELLRYLCNIPQQPEDRTHTvrLAMGNGLRADVWETFQQRFGpiRIWEVYGSTE----GNMGLVNYVGRCGA 450
Cdd:cd12116 217 SITVMQATPATWRMLLDAGWQGRAGLTA--LCGGEALPPDLAARLLSRVG--SLWNLYGPTEttiwSTAARVTAAAGPIP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 451 LGKmscllrmlsPFELVQFdmeaaePVRDNQGfcIPVGLGEPGLLLT--KVVSQqpfvGYRGPRELSERKLVRN-VRQSG 527
Cdd:cd12116 293 IGR---------PLANTQV------YVLDAAL--RPVPPGVPGELYIggDGVAQ----GYLGRPALTAERFVPDpFAGPG 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768006055 528 DVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 582
Cdd:cd12116 352 SRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAV 406
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
294-571 |
1.80e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 57.30 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKPAILTHERVLQ--MSKMLSLSGATADDVV-YTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDD 370
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEMIGQVVtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 371 CRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL----AMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnmglvnyvg 446
Cdd:PLN02330 271 LITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTE---------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 447 rcgalgkMSCLlrmlspfELVQFDMEAAEPV--RDNQGFCIP---VGLGEP--GLLLTK-------VVSQQPFVGYRGPR 512
Cdd:PLN02330 341 -------HSCI-------TLTHGDPEKGHGIakKNSVGFILPnleVKFIDPdtGRSLPKntpgelcVRSQCVMQGYYNNK 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 513 ELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PLN02330 407 EETDRTI------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAIL 459
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
287-571 |
2.70e-08 |
|
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: 56.71 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 287 RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPlyhvMGLVVGILGCL----DLGAtCVLA- 359
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGryWLDLTASDIMWNTSD----TGWIKSAWSSLfepwIQGA-CVFVh 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 360 --PKFSTSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHTVRL----AMGNGLRADVWETFQQRFGpIRIWEVYG 433
Cdd:cd05928 249 hlPRFDPLVILKTLSSYPITTFCGAPTVYRMLV---QQDLSSYKFPSLqhcvTGGEPLNPEVLEKWKAQTG-LDIYEGYG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 434 STEGNMGLVNYVG---RCGALGKMScllrmlSPFElVQfdmeaaepVRDNQGFCIPVGlgEPGLLLTKVVSQQP---FVG 507
Cdd:cd05928 325 QTETGLICANFKGmkiKPGSMGKAS------PPYD-VQ--------IIDDNGNVLPPG--TEGDIGIRVKPIRPfglFSG 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 508 YRGPRElserKLVRNVRqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd05928 388 YVDNPE----KTAATIR--GD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESAL 444
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
294-357 |
7.01e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 55.20 E-value: 7.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006055 294 YTSGTTGLPKPAILTHERVL--------QMskmlslsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCV 357
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnngyfigeAM-------KLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMV 270
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
218-347 |
1.16e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.49 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 218 LSSGARVLVVDPDLRESL-EEILPKLqaeNIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAgitwrsPALFIYTS 296
Cdd:PRK09029 74 LQCGARVLPLNPQLPQPLlEELLPSL---TLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR------LATMTLTS 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 768006055 297 GTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLvvGIL 347
Cdd:PRK09029 145 GSTGLPKAAVHTAQAHLASAEgVLSLMPFTAQDSWLLSLPLFHVSGQ--GIV 194
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
135-571 |
1.21e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.79 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 135 WTGPGAGSVTFGELDARACQAAWALKAELGdpasLCAGEPTA-LLVLASQAVPALcmwLGLAKLGCPTAWINPHGRGMPL 213
Cdd:PRK05620 31 WGGAEQEQTTFAAIGARAAALAHALHDELG----ITGDQRVGsMMYNCAEHLEVL---FAVACMGAVFNPLNKQLMNDQI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 214 AHSVLSSGARVLVVDPDLRESLEEILPklQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGI-TW-----R 287
Cdd:PRK05620 104 VHIINHAEDEVIVADPRLAEQLGEILK--ECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVyDWpeldeT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHeRVLQMSkmlSLSGATADDVVYT-------VLPLYHVMGLVVGILGCLDlGATCVL-- 358
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVYSH-RSLYLQ---SLSLRTTDSLAVThgesflcCVPIYHVLSWGVPLAAFMS-GTPLVFpg 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 ----APKFSTSCFWDDCRQ-HGVTViLYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWEtfqQRFGpIRIWEVYG 433
Cdd:PRK05620 257 pdlsAPTLAKIIATAMPRVaHGVPT-LWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWE---ERYG-VDVVHVWG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 434 STEgnMGLVNYVGR--CGALGKMSCLLRMLS---PFEL---VQFDMEAAEPVRDNQGfcipvGLGEPGLLLTKVVSQQPF 505
Cdd:PRK05620 332 MTE--TSPVGTVARppSGVSGEARWAYRVSQgrfPASLeyrIVNDGQVMESTDRNEG-----EIQVRGNWVTASYYHSPT 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 506 VGYRGPRELSERKLVRNVRQS--GDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PRK05620 405 EEGGGAASTFRGEDVEDANDRftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYI 472
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
288-360 |
1.69e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 54.21 E-value: 1.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 360
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIqHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVP 241
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
294-571 |
2.95e-07 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 53.07 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFWDDCR 372
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYlWTLPMFHCNGWC-FPWTVAAVGGTNVCLRKVDAKAIYDLIE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 373 QHGVTVILYVGELLRYLCNIPqqPEDR---THTVRLAMGNGL-RADVWETFQQrfGPIRIWEVYGSTEG-NMGLVNY--- 444
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANAP--PSDArplPHRVHVMTAGAPpPAAVLAKMEE--LGFDVTHVYGLTETyGPATVCAwkp 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 445 -------------VGRCGalgkmsclLRMLSPFELVQFDMEAAEPV-RDNQGfcipvgLGEpgllltkVVsqqpFVG--- 507
Cdd:cd12118 295 ewdelpteerarlKARQG--------VRYVGLEEVDVLDPETMKPVpRDGKT------IGE-------IV----FRGniv 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 508 ----YRGPRelSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd12118 350 mkgyLKNPE--ATAEAFR------GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
224-354 |
3.81e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 52.99 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 224 VLVVDPDLR-ESLEEILpKLQAENIRcfylshtSPTPgvgalgaaldaapshPVPADLragitwrspALFIYTSGTTGLP 302
Cdd:cd05927 82 IVFCDAGVKvYSLEEFE-KLGKKNKV-------PPPP---------------PKPEDL---------ATICYTSGTTGNP 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 303 KPAILTHERVLQ----MSKML-SLSGATADDVVYTVLPLYHVMGLVVgILGCLDLGA 354
Cdd:cd05927 130 KGVMLTHGNIVSnvagVFKILeILNKINPTDVYISYLPLAHIFERVV-EALFLYHGA 185
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
115-383 |
4.12e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 52.97 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAelgdpASLCAGEPTALLvlASQAVPALCMWLGL 194
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVC---GDRRLTYAELEERANRLAHYLIA-----QGLGPGDHVGIY--ARNRIEYVEAMLGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 195 AKLGcpTAWINPHGRGMP--LAHSVLSSGARVLVVDPDLRESLEEILPKLqaENIRCFYL-----SHTSPTPGVGALGAA 267
Cdd:PRK07798 74 FKAR--AVPVNVNYRYVEdeLRYLLDDSDAVALVYEREFAPRVAEVLPRL--PKLRTLVVvedgsGNDLLPGAVDYEDAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 268 LDAAPSHPVPAdlragitwRSP--ALFIYTSGTTGLPKPAILTHE--RVLQMSKMLSLSGATADD--------------V 329
Cdd:PRK07798 150 AAGSPERDFGE--------RSPddLYLLYTGGTTGMPKGVMWRQEdiFRVLLGGRDFATGEPIEDeeelakraaagpgmR 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 768006055 330 VYTVLPLYHVMGLvVGILGCLDLGATCVLAP--KFSTSCFWDDCRQHGVTVILYVG 383
Cdd:PRK07798 222 RFPAPPLMHGAGQ-WAAFAALFSGQTVVLLPdvRFDADEVWRTIEREKVNVITIVG 276
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
115-343 |
4.22e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 52.69 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 115 TFVDAFERRARAQPgRALLvwTG-PGAGS-VTFGELDARACQAAWALKAE---LGDPASLCAGEPTALLVLAsQAVpalc 189
Cdd:PRK07768 3 RFTEKMYANARTSP-RGMV--TGePDAPVrHTWGEVHERARRIAGGLAAAgvgPGDAVAVLAGAPVEIAPTA-QGL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 190 mWLGLAKLGC---PTA------WINPHGRgmplAHSVLSSGArVLVVDPdlresLEEILPKLQAENIRcfylshtsptpg 260
Cdd:PRK07768 75 -WMRGASLTMlhqPTPrtdlavWAEDTLR----VIGMIGAKA-VVVGEP-----FLAAAPVLEEKGIR------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 261 VGALGAALDAAPSHPVPADLRAgitwrsPALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATAD-DVVYTVLPLYH 338
Cdd:PRK07768 132 VLTVADLLAADPIDPVETGEDD------LALMQLTSGSTGSPKAVQITHGNlYANAEAMFVAAEFDVEtDVMVSWLPLFH 205
|
....*
gi 768006055 339 VMGLV 343
Cdd:PRK07768 206 DMGMV 210
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
290-574 |
4.54e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK------- 361
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLaNVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyriv 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 362 ------------FSTSCFWDDCRQHGVTvilYVGELLRYLCNIPQQPEDRTHTvrlamgnglradVWetfQQRFGpIRIW 429
Cdd:PRK08043 448 pelvydrnctvlFGTSTFLGNYARFANP---YDFARLRYVVAGAEKLQESTKQ------------LW---QDKFG-LRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 430 EVYGSTEG------NMGLVNYVGRCGalgkmscllRMLSpfelvqfDMEAAepvrdnqgfCIPV-GLGEPGLLLTKvvsq 502
Cdd:PRK08043 509 EGYGVTECapvvsiNVPMAAKPGTVG---------RILP-------GMDAR---------LLSVpGIEQGGRLQLK---- 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 503 QPFV--GY-----RGPRELSERKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQV 574
Cdd:PRK08043 560 GPNImnGYlrvekPGVLEVPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGV 636
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
279-575 |
7.24e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 52.66 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 279 DLRAGITW----------------------RSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLP 335
Cdd:PRK06814 763 DVRAQIGLadkikgllagrfplvyfcnrdpDDPAVILFTSGSEGTPKGVVLSHRNLLaNRAQVAARIDFSPEDKVFNALP 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 336 LYHVMGLVVGILGCL-----------------------DLGATCVlapkFSTSCFWD---------DCRQhgvtvilyvg 383
Cdd:PRK06814 843 VFHSFGLTGGLVLPLlsgvkvflypsplhyriipeliyDTNATIL----FGTDTFLNgyaryahpyDFRS---------- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 384 elLRYLcnipqqpedrthtvrLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEG------NMGLVNyvgRCGALGKmscl 457
Cdd:PRK06814 909 --LRYV---------------FAGAEKVKEETRQTWMEKFG-IRILEGYGVTETapvialNTPMHN---KAGTVGR---- 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 458 lrmLSPfelvqfDMEAA-EPVRdnqgfcipvGLGEPGLLLTKvvsqQPFV--GY---RGPRELSERKlvrnvrqsgDVYY 531
Cdd:PRK06814 964 ---LLP------GIEYRlEPVP---------GIDEGGRLFVR----GPNVmlGYlraENPGVLEPPA---------DGWY 1012
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 768006055 532 NTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVD 575
Cdd:PRK06814 1013 DTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW 1056
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
120-436 |
8.48e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 120 FERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAELGDPASLCAgeptallVLASQAVPALCMWLGLAKLGC 199
Cdd:PRK12316 4557 VAERARMTPDAVAVVF---DEEKLTYAELNRRANRLAHALIARGVGPEVLVG-------IAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 200 PTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEeilpklQAENIRCFYLSHTSPTPGvgalgaALDAAPSHPVPAD 279
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLP------IPDGLASLALDRDEDWEG------FPAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 280 lragitwrSPALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPlYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK12316 4695 --------NLAYVIYTSGSTGRPKGVAVSHGSLVNhLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVI 4765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 359 APkfstSCFWDDCR------QHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL-----AMGNGLRADVWETFQqrfgPIR 427
Cdd:PRK12316 4766 RD----DSLWDPERlyaeihEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYcfggeAVAQASYDLAWRALK----PVY 4837
|
....*....
gi 768006055 428 IWEVYGSTE 436
Cdd:PRK12316 4838 LFNGYGPTE 4846
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
289-593 |
9.16e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.93 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGA-----TADDVVYTVLPLYHVMGLvVGILGCLDLGATCVLAPKfS 363
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLnwvtwVVGETTYSPLPATHIGGL-WWILTCLMHGGLCVTGGE-N 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 364 TSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLR---ADVweTFQQRFGpIRIWEVYGSTE---- 436
Cdd:PRK05857 249 TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRaiaADV--RFIEATG-VRTAQVYGLSEtgct 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 -----GNMGLVNYVgRCGALGKmscllrmlsPFELVQFDMEAAepvrDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGP 511
Cdd:PRK05857 326 alclpTDDGSIVKI-EAGAVGR---------PYPGVDVYLAAT----DGIGPTAPGAGPSASFGTLWIKSPANMLGYWNN 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 512 RELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGRH 591
Cdd:PRK05857 392 PERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYE--IPDEE 462
|
..
gi 768006055 592 GG 593
Cdd:PRK05857 463 FG 464
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
128-582 |
1.69e-06 |
|
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: 50.77 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 128 PGRALLVWtgpGAGSVTFGELDARACQAAWALKAE---LGDPASLCAgEPTALLVLASqavpalcmwLGLAKLGCPTAWI 204
Cdd:cd17643 1 PEAVAVVD---EDRRLTYGELDARANRLARTLRAEgvgPGDRVALAL-PRSAELIVAL---------LAILKAGGAYVPI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 205 NPHGRGMPLAHSVLSSGARVLVVDPDlresleeilpklqaenircfylshtsptpgvgalgaaldaapshpvpadlragi 284
Cdd:cd17643 68 DPAYPVERIAFILADSGPSLLLTDPD------------------------------------------------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 285 twrSPALFIYTSGTTGLPKPAILTHERVLQM-SKMLSLSGATADDVVYtvlpLYHVMGL---VVGILGCLDLGATCVLAP 360
Cdd:cd17643 94 ---DLAYVIYTSGSTGRPKGVVVSHANVLALfAATQRWFGFNEDDVWT----LFHSYAFdfsVWEIWGALLHGGRLVVVP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KF---STSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEV--YG 433
Cdd:cd17643 167 YEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDRPQLVnmYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 434 STEGNMgLVNYvgrcgalgkmscllRMLSPFELVQFDMEA-AEP-------VRDNQGfcIPVGLGEPGLLLtkVVSQQPF 505
Cdd:cd17643 247 ITETTV-HVTF--------------RPLDAADLPAAAASPiGRPlpglrvyVLDADG--RPVPPGVVGELY--VSGAGVA 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 506 VGYRGPRELSERKLVRN-VRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 582
Cdd:cd17643 308 RGYLGRPELTAERFVANpFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-571 |
2.28e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 112 PPDTFVDAFERRARAQPGRALLVWTGpgaGSVTFGELDARACQAAWALKaELGDPASLCAGeptallVLASQAVPALCMW 191
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVWDG---GSLDYAELHAQANRLAHYLR-DKGVGPDVCVA------IAAERSPQLLVGL 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 192 LGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEI-------LPKLQAENircfylshtsptpgvgal 264
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAegvsaiaLDSLHLDS------------------ 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 265 gaaldaAPSHPVPADLRAGitwrSPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLsgaTADDVVYTVLPLyhvm 340
Cdd:PRK05691 1261 ------WPSQAPGLHLHGD----NLAYVIYTSGSTGQPKGVGNTHaalaERLQWMQATYAL---DDSDVLMQKAPI---- 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 341 GLVVGILGC---LDLGATCVLA-------PKFSTSCfwddCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG 410
Cdd:PRK05691 1324 SFDVSVWECfwpLITGCRLVLAgpgehrdPQRIAEL----VQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEA 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 411 LRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYvgRCGAL-GKMSCLLRMLSPFELVQFDMEAAepvrdnqgfciPVGL 489
Cdd:PRK05691 1400 LPAELRNRVLQRLPQVQLHNRYGPTETAINVTHW--QCQAEdGERSPIGRPLGNVLCRVLDAELN-----------LLPP 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 490 GEPGLLLTKVVSQQPfvGYRG-PRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVE 568
Cdd:PRK05691 1467 GVAGELCIGGAGLAR--GYLGrPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ 1544
|
...
gi 768006055 569 GVL 571
Cdd:PRK05691 1545 ARL 1547
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
290-584 |
2.44e-06 |
|
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: 50.44 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVG--ILGCldlGATCVLApkfSTSC 366
Cdd:cd17640 91 ATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEyfIFAC---GCSQAYT---SIRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 367 FWDDCRQHGVTVILYVGELLRYLCN-----IPQQPEDRTHTVRLAM----------GNGLRADVWETFQQRFGpIRIWEV 431
Cdd:cd17640 165 LKDDLKRVKPHYIVSVPRLWESLYSgiqkqVSKSSPIKQFLFLFFLsggifkfgisGGGALPPHVDTFFEAIG-IEVLNG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 432 YGSTEGNMGLV------NYVGRCGAlgkmscllrmlsPFELVQFDmeaaepVRDNQGfCIPVGLGEPGLLLTKvvSQQPF 505
Cdd:cd17640 244 YGLTETSPVVSarrlkcNVRGSVGR------------PLPGTEIK------IVDPEG-NVVLPPGEKGIVWVR--GPQVM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 506 VGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWK-GENVSTHEVEGVLSQVDFLQQVNVYG 584
Cdd:cd17640 303 KGYYKNPEATSKVL------DSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
290-355 |
2.91e-06 |
|
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: 50.29 E-value: 2.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQ----MSKMLSlSGATADDVVYTVLPLYHVMGLVVGILgCLDLGAT 355
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVP-ELLGPDDRYLAYLPLAHIFELAAENV-CLYRGGT 158
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
290-592 |
3.09e-06 |
|
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: 50.16 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERV-LQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTscFW 368
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFaWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT--FV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 369 DDCRQHGVTVILYVGEL-----LRYLCNIPQQPEDRTHTV---------RLAMGNGLRA-------------DVWETFqQ 421
Cdd:cd05932 218 EDVQRARPTLFFSVPRLwtkfqQGVQDKIPQQKLNLLLKIpvvnslvkrKVLKGLGLDQcrlagcgsapvppALLEWY-R 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 422 RFGpIRIWEVYGSTEgNMGL--VNYVGR--CGALGKMScllrmlspfelvqfdmeaaepvrdnQGfcIPVGLGEPGLLLT 497
Cdd:cd05932 297 SLG-LNILEAYGMTE-NFAYshLNYPGRdkIGTVGNAG-------------------------PG--VEVRISEDGEILV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 498 KvvSQQPFVGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVLSQVDF 576
Cdd:cd05932 348 R--SPALMMGYYKDPEATAEAF------TADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDR 419
|
330
....*....|....*.
gi 768006055 577 LQQVNVYGVCVPGRHG 592
Cdd:cd05932 420 VEMVCVIGSGLPAPLA 435
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
290-572 |
4.33e-06 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 49.32 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLY----HVMGLVVGILGcldlGATCVLAP--- 360
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSerYFGRDNGDEAVLFFSNYvfdfFVEQMTLALLN----GQKLVVPPdem 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 361 KFSTSCFWDDCRQHGVTvilyvgellrYLCNIP---QQPE--DRTHTVR-LAMGNGLRADVWETFQQRFgPIRIWEVYGS 434
Cdd:cd17648 173 RFDPDRFYAYINREKVT----------YLSGTPsvlQQYDlaRLPHLKRvDAAGEEFTAPVFEKLRSRF-AGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 435 TEgnmglvnyvgrcgalgkmSCLLRMLSPFELVQ-FDMEAAEPVRDNQGFC-------IPVG-LGE---------PGLLL 496
Cdd:cd17648 242 TE------------------TTVTNHKRFFPGDQrFDKSLGRPVRNTKCYVlndamkrVPVGaVGElylggdgvaRGYLN 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 497 TKVVSQQPFVgyRGP-RELSERKLVRNVRqsgdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLS 572
Cdd:cd17648 304 RPELTAERFL--PNPfQTEQERARGRNAR-----LYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALA 373
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
287-590 |
1.09e-05 |
|
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: 47.76 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 287 RSP--ALFIYTSGTTGLPKPAILTHERVLQMSK---------------MLSLSGATADDVVYTVLPLYHVMGLVVGILGC 349
Cdd:cd05924 1 RSAddLYILYTGGTTGMPKGVMWRQEDIFRMLMggadfgtgeftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 350 LDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGE-LLRYLCNIPQQPEDRTHTVRLAMGNG---LRADVWETFQQRFGP 425
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 426 IRIWEVYGSTEGNMGLVNYVGRCGALGkmscllrmlSPFELVQFDMEaaepVRDNQGFCIPVGLGEPGLLLTK-VVSqqp 504
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGHSAGSGPET---------GPFTRANPDTV----VLDDDGRVVPPGSGGVGWIARRgHIP--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 505 fVGYRGprelSERKLVRNVRQSGDVYYN-TGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSqvdflQQVNVY 583
Cdd:cd05924 225 -LGYYG----DEAKTAETFPEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK-----SHPAVY 294
|
....*..
gi 768006055 584 GVCVPGR 590
Cdd:cd05924 295 DVLVVGR 301
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-436 |
2.26e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.03 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 108 LSRQPPDTFV-DAFERRARAQPGRALLVWtgpGAGSVTFGELDARACQAAWALKAelgdpasLCAGePTALLVLASQAVP 186
Cdd:PRK12316 1996 PEAYPRGPGVhQRIAEQAARAPEAIAVVF---GDQHLSYAELDSRANRLAHRLRA-------RGVG-PEVRVAIAAERSF 2064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 187 ALCM-WLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLeeilpkLQAENIRCFYLSHTSPTPGvgalg 265
Cdd:PRK12316 2065 ELVVaLLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL------PLPAGVARLPLDRDAEWAD----- 2133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 266 aaldaAPSHPvPADLRAGITWrspALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPlYHVMGLVV 344
Cdd:PRK12316 2134 -----YPDTA-PAVQLAGENL---AYVIYTSGSTGLPKGVAVSHGALVAhCQAAGERYELSPADCELQFMS-FSFDGAHE 2203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 345 GILGCLDLGATCVLAPK--FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQpEDRTHTVRLAM--GNGLRADVWETFQ 420
Cdd:PRK12316 2204 QWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAER-DGRPPAVRVYCfgGEAVPAASLRLAW 2282
|
330
....*....|....*.
gi 768006055 421 QRFGPIRIWEVYGSTE 436
Cdd:PRK12316 2283 EALRPVYLFNGYGPTE 2298
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
289-367 |
2.44e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.07 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHERVLQ----MSKMLSLSGATadDVVYTVLPLYHVMGLVVGILGCLDlGATCVLAPK--F 362
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPGAVLSnlrgLNARVGLDAAT--DVGCSWLPLYHDMGLAFLLTAALA-GAPLWLAPTtaF 230
|
....*
gi 768006055 363 STSCF 367
Cdd:PRK05851 231 SASPF 235
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
288-358 |
2.44e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHERVLQ-----MSKMLSLSG--ATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 358
Cdd:PRK05850 161 STAYLQYTSGSTRTPAGVMVSHRNVIAnfeqlMSDYFGDTGgvPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVL 238
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
272-342 |
3.09e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 3.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006055 272 PSHPVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQM--SKMLSLSGATADDVVYTVLPLYHVMGL 342
Cdd:PLN02387 244 PDLPSPNDI---------AVIMYTSGSTGLPKGVMMTHGNIVATvaGVMTVVPKLGKNDVYLAYLPLAHILEL 307
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
293-355 |
3.77e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.76 E-value: 3.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006055 293 IYTSGTTGLPKPAILTHE----RVLQMSKMLSLSG--ATADDVVYTVLPLYHVMGLVVGILgCLDLGAT 355
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRaiiaEVLSTDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETY-CISKGAS 293
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
288-363 |
8.87e-05 |
|
long-chain fatty acid CoA ligase (FadD); 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. 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: 341291 [Multi-domain] Cd Length: 331 Bit Score: 44.99 E-value: 8.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 288 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVmGLVVGILGCLDLGATCVLAPKFS 363
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFlNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVD 76
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
290-340 |
9.08e-05 |
|
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: 45.49 E-value: 9.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVM 340
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAaYLAADPLGPGDEYVSVLPLPWIG 212
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
118-309 |
9.64e-05 |
|
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: 45.23 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGR-ALLVWtgpgAGSVTFGELDARACQAAWALkAELGdpaslcageptallVLASQAVPaLCM----WL 192
Cdd:cd05918 3 DLIEERARSQPDApAVCAW----DGSLTYAELDRLSSRLAHHL-RSLG--------------VGPGVFVP-LCFekskWA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 193 GLAKLGcptawinphgrgmplahsVLSSGARVLVVDPDLRES-LEEILPKLQAENIrcfyLSHTsptpgvgalgaaldaa 271
Cdd:cd05918 63 VVAMLA------------------VLKAGGAFVPLDPSHPLQrLQEILQDTGAKVV----LTSS---------------- 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 768006055 272 PSHPvpadlragitwrspALFIYTSGTTGLPKPAILTH 309
Cdd:cd05918 105 PSDA--------------AYVIFTSGSTGKPKGVVIEH 128
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
109-309 |
1.16e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 45.25 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 109 SRQP----PDTFVDAFERRARAQPGRALLVWTGPGAG--SVTFGELDARACQAAWALkAELGdpasLCAGEPtaLLVLAS 182
Cdd:PRK08180 30 SAEPlgdyPRRLTDRLVHWAQEAPDRVFLAERGADGGwrRLTYAEALERVRAIAQAL-LDRG----LSAERP--LMILSG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 183 ----QAVPAL-CMWLGLaklgcPTAWINP--------HGRgmpLAH--SVLSSGArVLVVDPDL-RESLEEILPklqaEN 246
Cdd:PRK08180 103 nsieHALLALaAMYAGV-----PYAPVSPayslvsqdFGK---LRHvlELLTPGL-VFADDGAAfARALAAVVP----AD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006055 247 IRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAgITWRSPALFIYTSGTTGLPKPAILTH 309
Cdd:PRK08180 170 VEVVAVRGAVPGRAATPFAALLATPPTAAVDAAHAA-VGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
118-596 |
1.52e-04 |
|
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: 44.62 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 118 DAFERRARAQPGRALLVwtgPGAGSVTFGELDARACQAAWALKAELGDPASLCAgeptALLVLASQAVPALcmwlgLAKL 197
Cdd:cd12115 3 DLVEAQAARTPDAIALV---CGDESLTYAELNRRANRLAARLRAAGVGPESRVG----VCLERTPDLVVAL-----LAVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 198 GCPTAWI-----NPHGRgmpLAHSVLSSGARVLVVDPDlresleeilpklqaenircfylshtsptpgvgalgaaldaap 272
Cdd:cd12115 71 KAGAAYVpldpaYPPER---LRFILEDAQARLVLTDPD------------------------------------------ 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 273 shpvpadlragitwrSPALFIYTSGTTGLPKPAILTHERVL-------------QMSKMLSLSGATADDVVYTV-LPLYH 338
Cdd:cd12115 106 ---------------DLAYVIYTSGSTGRPKGVAIEHRNAAaflqwaaaafsaeELAGVLASTSICFDLSVFELfGPLAT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 339 --VMGLVVGILGCLDLGATCvlapkfstscfwddcrqhGVTVILYVGELLRYLCNIPQQPEDrTHTVRLAmGNGLRADVW 416
Cdd:cd12115 171 ggKVVLADNVLALPDLPAAA------------------EVTLINTVPSAAAELLRHDALPAS-VRVVNLA-GEPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 417 ETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMScLLRMLSPFELVQFDmeaaepvrdnqGFCIPVGLGEPGLLL 496
Cdd:cd12115 231 QRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVS-IGRPLANTQAYVLD-----------RALQPVPLGVPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 497 T--KVVSQqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQV 574
Cdd:cd12115 299 IggAGVAR----GYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
490 500
....*....|....*....|..
gi 768006055 575 DflqQVNVYGVCVPGRHGGHQH 596
Cdd:cd12115 375 P---GVREAVVVAIGDAAGERR 393
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
290-350 |
1.84e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.58 E-value: 1.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006055 290 ALFIYTSGTTGLPKPAILTH----ERVLQMS-KMLSLSGATADDVVYTV-LPLYHVMGL-VVGIL---GCL 350
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHgsltAGILALEdRLNDLIGPPEEDETYCSyLPLAHIMEFgVTNIFlarGAL 337
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-360 |
2.09e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that 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: 341234 [Multi-domain] Cd Length: 499 Bit Score: 44.02 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006055 292 FI-YTSGTTGLPKPAILTHERVLqmSKMLSLSGATA---DDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 360
Cdd:cd05908 110 FIqFSSGSTGDPKGVMLTHENLV--HNMFAILNSTEwktKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP 180
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
114-350 |
2.85e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 43.84 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 114 DTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAA---WALKAELGDPASLCAgEPTALLVLASQAvpalCM 190
Cdd:PRK09192 21 PTLVEALDYAALGEAGMNFYDRRGQLEEALPYQTLRARAEAGArrlLALGLKPGDRVALIA-ETDGDFVEAFFA----CQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 191 WLGL--AKLGCPT------AWINpHGRGMplahsVLSSGARVLVVDPDLRESLEEILPKLQAenirCFYLSHTS----PT 258
Cdd:PRK09192 96 YAGLvpVPLPLPMgfggreSYIA-QLRGM-----LASAQPAAIITPDELLPWVNEATHGNPL----LHVLSHAWfkalPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 259 PGVGAlgaaldaapSHPVPADlragitwrsPALFIYTSGTTGLPKPAILTHERVlqmskMLSLSGATAD-------DVVY 331
Cdd:PRK09192 166 ADVAL---------PRPTPDD---------IAYLQYSSGSTRFPRGVIITHRAL-----MANLRAISHDglkvrpgDRCV 222
|
250
....*....|....*....
gi 768006055 332 TVLPLYHVMGLVvgilGCL 350
Cdd:PRK09192 223 SWLPFYHDMGLV----GFL 237
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
293-340 |
2.99e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.65 E-value: 2.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 768006055 293 IYTSGTTGLPKPAILTHERVLQMSKMLSL------SGATADDVVYTVLPLYHVM 340
Cdd:PLN02430 226 MYTSGTSGDPKGVVLTHEAVATFVRGVDLfmeqfeDKMTHDDVYLSFLPLAHIL 279
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
289-571 |
3.22e-04 |
|
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: 43.33 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHER--VLQMSKMLSLsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL--APKFST 364
Cdd:cd05974 87 PMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLfnYARFDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 365 SCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHT-VRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNMGL 441
Cdd:cd05974 166 KRVLAALVRYGVTTLCAPPTVWRMLI---QQDLASFDVkLREVVGAGepLNPEVIEQVRRAWG-LTIRDGYGQTETTALV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 442 VNYVGRCGALGKMScllRMLSPFELVQFDMEAAePVRDNQgFCIPVGLGEPGLLLTkvvsqqpfvGYRG-PRELSErklv 520
Cdd:cd05974 242 GNSPGQPVKAGSMG---RPLPGYRVALLDPDGA-PATEGE-VALDLGDTRPVGLMK---------GYAGdPDKTAH---- 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 768006055 521 rnvrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:cd05974 304 ----AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
272-450 |
5.40e-04 |
|
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: 42.74 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 272 PSHPvPADLR-----AGITW------RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSL-SGATADDVVYTVLPLyHV 339
Cdd:cd17649 69 PEYP-AERLRymledSGAGLllthhpRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAErYGLTPGDRELQFASF-NF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 340 MGLVVGILGCLDLGATCVLAPK---FSTSCFWDDCRQHGVTVI----LYVGELLRYLCNIPQqpeDRTHTVRL--AMGNG 410
Cdd:cd17649 147 DGAHEQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVLdlppAYLQQLAEEADRTGD---GRPPSLRLyiFGGEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768006055 411 LRADVWEtfQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGA 450
Cdd:cd17649 224 LSPELLR--RWLKAPVRLFNAYGPTEATVTPLVWKCEAGA 261
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
276-347 |
7.65e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.41 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 276 VPADLraGITWRSP-------ALFIYTSGTTGLPKPAILTHE----RVLQMskMLSLSGATADDVVyTVLPLYHVMGLVV 344
Cdd:PRK07769 164 VPDEV--GATWVPPeanedtiAYLQYTSGSTRIPAGVQITHLnlptNVLQV--IDALEGQEGDRGV-SWLPFFHDMGLIT 238
|
...
gi 768006055 345 GIL 347
Cdd:PRK07769 239 VLL 241
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
493-584 |
1.04e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 42.01 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 493 GLLLTKvvSQQPFVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVL 571
Cdd:PTZ00342 542 GELLIK--SDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETDMLNNLY 613
|
90
....*....|...
gi 768006055 572 SQVDFLQQVNVYG 584
Cdd:PTZ00342 614 SQISFINFCVVYG 626
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
294-570 |
1.40e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 41.62 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 294 YTSGTTGLPKPAILTHErvlqmSKMLSLSGA--------TADDVVYTVLPLYHVMGLvvGI-LGCLDLGATCVL-APKFS 363
Cdd:PRK07008 183 YTSGTTGNPKGALYSHR-----STVLHAYGAalpdamglSARDAVLPVVPMFHVNAW--GLpYSAPLTGAKLVLpGPDLD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 364 TSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGpIRIWEVYGSTEgnmgl 441
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRrtVIGGSACPPAMIRTFEDEYG-VEVIHAWGMTE----- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 442 vnyvgrCGALGKMSCLLrmlspFELVQFDMEAAEPVRDNQGFCIpVGLGepglllTKVV----SQQPFVG-------YRG 510
Cdd:PRK07008 330 ------MSPLGTLCKLK-----WKHSQLPLDEQRKLLEKQGRVI-YGVD------MKIVgddgRELPWDGkafgdlqVRG 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006055 511 PRELSerklvRNVRQSG----DVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 570
Cdd:PRK07008 392 PWVID-----RYFRGDAsplvDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENV 450
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
291-378 |
1.52e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.70 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 291 LFI-YTSGTTGLPKPAILTHERV-LQMSKMLSL-SGATADDVV--YT----VLPLYHVMGLVVgilgcldlGATCVL--- 358
Cdd:PRK03584 266 LWIlYSSGTTGLPKCIVHGHGGIlLEHLKELGLhCDLGPGDRFfwYTtcgwMMWNWLVSGLLV--------GATLVLydg 337
|
90 100
....*....|....*....|...
gi 768006055 359 ---APKFSTscFWDDCRQHGVTV 378
Cdd:PRK03584 338 spfYPDPNV--LWDLAAEEGVTV 358
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
275-339 |
1.62e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 41.62 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006055 275 PVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQmskmlSLSGATAD------DVVYTVLPLYHV 339
Cdd:PLN02736 218 PKPEDV---------ATICYTSGTTGTPKGVVLTHGNLIA-----NVAGSSLStkfypsDVHISYLPLAHI 274
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
294-338 |
2.09e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 40.89 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 768006055 294 YTSGTTGLPKPAILTHE-RVLQ--MSKMLSLSGATADDVVYTVLPLYH 338
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRsNVLHalMANNGDALGTSAADTMLPVVPLFH 231
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
290-361 |
3.00e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 40.42 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 290 ALFIYTSGTTGLPKPAILTHERVL----QMSKMLSLSGAT-ADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK 361
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATvGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQP 229
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
284-378 |
3.12e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 40.65 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 284 ITW---RSPALFIYTSGTTGLPKPAILTHERVLQMskmlSLSGATA----DDVVY--TVLPLYhVMGLVVGILGCLDLGA 354
Cdd:PRK04319 199 IEWtdrEDGAILHYTSGSTGKPKGVLHVHNAMLQH----YQTGKYVldlhEDDVYwcTADPGW-VTGTSYGIFAPWLNGA 273
|
90 100
....*....|....*....|....*
gi 768006055 355 T-CVLAPKFSTSCFWDDCRQHGVTV 378
Cdd:PRK04319 274 TnVIDGGRFSPERWYRILEDYKVTV 298
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-590 |
3.26e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 40.14 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 289 PALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCL-DLGATC--VLAPKFst 364
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTfAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIpDMDPTRpaRADPQK-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 365 scFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGP-IRIWEVYGSTE----- 436
Cdd:cd05910 165 --LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvs 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006055 437 --GNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVG-LGEpglllTKVVSQQPFVGYRGpRE 513
Cdd:cd05910 243 siGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPIAEWDDTLELPRGeIGE-----ITVTGPTVTPTYVN-RP 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006055 514 LSERkLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGR 590
Cdd:cd05910 317 VATA-LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGC 392
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
530-571 |
9.49e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 38.77 E-value: 9.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 768006055 530 YYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 571
Cdd:PRK08162 417 WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
|
| |
