|
Name |
Accession |
Description |
Interval |
E-value |
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
19-500 |
0e+00 |
|
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: 642.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 19 DTAVYHYRgQTLSRLQCRTYILSQASQLARLLKPGDRVVLALN-DSPSLACLFLACIAVGAIPAVINPKSREQALADIAA 97
Cdd:cd05919 1 KTAFYAAD-RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMlDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 98 DCQASLVVREADApslsgplapltlraaagrpllddfsldalvgpadldwsafhrqdpaaACFLQYTSGSTGAPKGVMHS 177
Cdd:cd05919 80 DCEARLVVTSADD-----------------------------------------------IAYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 178 LRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAI 257
Cdd:cd05919 113 HRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 258 YASLRPQA---RELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECR 333
Cdd:cd05919 193 YANLLDSCagsPDALRSLRLCVSAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 334 LVDREGHTIeEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQ 413
Cdd:cd05919 273 LVDEEGHTI-PPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHLPeVSEAVLVPTCRLHDGLRPTLFVTLATPLdDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:cd05919 352 VESLIIQHPA-VAEAAVVAVPESTGLSRLTAFVVLKSPA-APQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
....*..
gi 15596193 494 LARAELR 500
Cdd:cd05919 430 LQRFKLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
8-500 |
6.47e-121 |
|
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: 364.38 E-value: 6.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 8 TEVLFRLD-FDPDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP 85
Cdd:cd05959 7 TLVDLNLNeGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALgVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 86 KSREQALADIAADCQASLVVreadapsLSGPLAPLtLRAAAGRPLLDDFSLDaLVGPADLDWSAFHRQD---------PA 156
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVV-------VSGELAPV-LAAALTKSEHTLVVLI-VSGGAGPEAGALLLAElvaaeaeqlKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 157 AA------CFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLD 230
Cdd:cd05959 158 AAthaddpAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 231 DTWPSPERVLENLVAFRPRVLFGVPAIYASL----RPQAReLLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATE 305
Cdd:cd05959 238 PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMlaapNLPSR-DLSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 306 VGHVFLANRPGQARADSTGLPLPGYECRLVDREGHtIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFE 385
Cdd:cd05959 317 MLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGG-DVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 386 RDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTcRLHDGL-RPTLFVTLATPLDDNQIlLAQRID 464
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQH-PAVLEAAVVGV-EDEDGLtKPKAFVVLRPGYEDSEA-LEEELK 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 15596193 465 QHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05959 473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-504 |
2.37e-112 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 344.40 E-value: 2.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 6 NLTEVLF--RLDFDPDTAVYHYRGQTLSRLQcRTY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAV 76
Cdd:COG0365 9 NIAYNCLdrHAEGRGDKVALIWEGEDGEERT-LTYaeLRREVNRFANALRalgvkKGDRVAIYLPNIPEAVIAMLACARI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 77 GAIPAVINPKSREQALADIAADCQASLVVreADAPSLSG----PLAPLTLRAAAGRPLLD-----DFSLDALVGPADLDW 147
Cdd:COG0365 88 GAVHSPVFPGFGAEALADRIEDAEAKVLI--TADGGLRGgkviDLKEKVDEALEELPSLEhvivvGRTGADVPMEGDLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 148 SAFHRQDPAAA----------CFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSL 217
Cdd:COG0365 166 DELLAAASAEFepeptdaddpLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 FFPWFSGASALLDD---TWPSPERVLENLVAFRPRVLFGVPAIYASLRPQAREL-----LSSVRLAFSAGSPLPRGEFEF 289
Cdd:COG0365 246 YGPLLNGATVVLYEgrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkydLSSLRLLGSAGEPLNPEVWEW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 290 WAAH-GLEICDGIGATEVGHVFLANRPGQA-RADSTGLPLPGYECRLVDREGHTIeEAGRQGVLLVRG--PGLSPGYWRA 365
Cdd:COG0365 326 WYEAvGVPIVDGWGQTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVDEDGNPV-PPGEEGELVIKGpwPGMFRGYWND 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 366 SEEQQARFAG---GWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHDGLR- 441
Cdd:COG0365 405 PERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH-PAVAEAAVVG---VPDEIRg 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596193 442 --PTLFVTLA--TPLDDNqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLAD 504
Cdd:COG0365 481 qvVKAFVVLKpgVEPSDE---LAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
18-500 |
1.99e-108 |
|
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: 330.23 E-value: 1.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIA 96
Cdd:COG0318 13 PDRPALVFGGRRLTYAELDARARRLAAALRALgVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLVVreadapslsgplapltlraaagrpllddfsldalvgpadldwsafhrqdpaaACFLQYTSGSTGAPKGVMH 176
Cdd:COG0318 93 EDSGARALV----------------------------------------------------TALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 177 SLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPA 256
Cdd:COG0318 121 THRNLLANAAAIA-AALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF-DPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 257 IYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLAN--RPGQARADSTGLPLPGY 330
Cdd:COG0318 199 MLARLlrHPEFARYdLSSLRLVVSGGAPLPPELLErFEERFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 331 ECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVV 410
Cdd:COG0318 279 EVRIVDEDGRELP-PGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 411 PTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRND 490
Cdd:COG0318 358 PAEVEEVLAAH-PGVAEAAVVGVPDEKWGERVVAFVVLR----PGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTA 432
|
490
....*....|
gi 15596193 491 NGKLARAELR 500
Cdd:COG0318 433 SGKIDRRALR 442
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-500 |
4.52e-94 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 295.21 E-value: 4.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQAS-LVVREADAPSLS---GPL 117
Cdd:TIGR02262 44 AAALRRLgVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARvVFVSGALLPVIKaalGKS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 118 APLTLRAAAGRPLLDDFSLDALVGP-ADLDWSAFHRQDPAaaCFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQ 196
Cdd:TIGR02262 124 PHLEHRVVVGRPEAGEVQLAELLATeSEQFKPAATQADDP--AFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 197 AGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASL-----RPQARELlsS 271
Cdd:TIGR02262 202 EDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMladpnLPSEDQV--R 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 272 VRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDrEGHTIEEAGRQGV 350
Cdd:TIGR02262 280 LRLCTSAGEALPAEVGQRWQARfGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQDVADGEPGE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 351 LLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL 430
Cdd:TIGR02262 359 LLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQH-PAVLEAAV 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 431 VPTCRLHDGLRPTLFVTLATplddNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:TIGR02262 438 VGVADEDGLIKPKAFVVLRP----GQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-500 |
1.96e-90 |
|
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: 283.60 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 39 ILSQASQLARLLK------PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVreadaps 112
Cdd:cd05958 16 LLALANRIANVLVgelgivPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 113 lsgplapltlraaagrpllddfsldalvgpadLDWSAFHRQDpaaACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATEL 192
Cdd:cd05958 89 --------------------------------CAHALTASDD---ICILAFTSGTTGAPKATMHFHRDPLASADRYAVNV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 193 LALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTwPSPERVLENLVAFRPRVLFGVPAIYAS---LRPQARELL 269
Cdd:cd05958 134 LRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-ATPDLLLSAIARYKPTVLFTAPTAYRAmlaHPDAAGPDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 270 SSVRLAFSAGSPLPRGEFEFW-AAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIeEAGRQ 348
Cdd:cd05958 213 SSLRKCVSAGEALPAALHRAWkEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPV-PDGTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 349 GVLLVRGPglsPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE 427
Cdd:cd05958 292 GRLAVRGP---TGCRYLADKrQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQH-PAVAE 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 428 AVLVPTCRLHDGLRPTLFVTLAtPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05958 368 CAVVGHPDESRGVVVKAFVVLR-PGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
159-493 |
6.67e-80 |
|
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: 252.98 E-value: 6.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 159 CFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATeLLALQAGDRLYSIPKMFFGyGMGNSLFFPWFSGASALLDDTWPsPER 238
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAA-SGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFD-PEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 239 VLENLVAFRPRVLFGVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLANR 314
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLErFEEAPGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 315 P--GQARADSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAY 392
Cdd:cd04433 160 PddDARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 393 RHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDdnqiLLAQRIDQHLAEQIP 472
Cdd:cd04433 239 YIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAVVGVPDPEWGERVVAVVVLRPGAD----LDAEELRAHVRERLA 313
|
330 340
....*....|....*....|.
gi 15596193 473 SHMLPSQLHVLPALPRNDNGK 493
Cdd:cd04433 314 PYKVPRRVVFVDALPRTASGK 334
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
18-404 |
1.18e-76 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 247.23 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PD-TAVYHYRGQTLsrlqcrTY--ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSRE 89
Cdd:pfam00501 9 PDkTALEVGEGRRL------TYreLDERANRLAAGLralgvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 90 QALADIAADCQASLVV---------READAPSLSGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAaacF 160
Cdd:pfam00501 83 EELAYILEDSGAKVLItddalkleeLLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLA---Y 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVMHSLRNTLGFCRAFA---TELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWP--S 235
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPalD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 236 PERVLENLVAFRPRVLFGVPAIY---ASLRPQARELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVFL 311
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLnmlLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 312 ANRPG---QARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERD 387
Cdd:pfam00501 320 TPLPLdedLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRD 399
|
410
....*....|....*..
gi 15596193 388 ESGAYRHCGREDDLFKV 404
Cdd:pfam00501 400 EDGYLEIVGRKKDQIKL 416
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-500 |
5.64e-75 |
|
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: 244.39 E-value: 5.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 15 DFDPDTAVYhYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALA 93
Cdd:cd05936 11 RFPDKTALI-FMGRKLTYRELDALAEAFAAGLQNLgVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 94 DIAADCQASLVVreadapslsgplapltlraaAGRPLLDDFSLDALVGPadldWSAFHRQDPAaacFLQYTSGSTGAPKG 173
Cdd:cd05936 90 HILNDSGAKALI--------------------VAVSFTDLLAAGAPLGE----RVALTPEDVA---VLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 174 VMHSLRNTLG---FCRAFATELlaLQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTwPSPERVLENLVAFRPRV 250
Cdd:cd05936 143 AMLTHRNLVAnalQIKAWLEDL--LEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR-FRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LFGVPAIYASL---RPQARELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVFLANRP-GQARADSTGL 325
Cdd:cd05936 220 FPGVPTMYIALlnaPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLdGPRKPGSIGI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVN 405
Cdd:cd05936 300 PLPGTEVKIVDDDGEELPP-GEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 406 GRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPA 485
Cdd:cd05936 379 GFNVYPREVEEVLYEH-PAVAEAAVVGVPDPYSGEAVKAFVVLK----EGASLTEEEIIAFCREQLAGYKVPRQVEFRDE 453
|
490
....*....|....*
gi 15596193 486 LPRNDNGKLARAELR 500
Cdd:cd05936 454 LPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
18-500 |
4.15e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 227.76 E-value: 4.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTlsrlqcRTY--ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:PRK06187 20 PDKEAVYFDGRR------TTYaeLDERVNRLANALralgvKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREAD-APSLSGPLAPLTLR--------AAAGRPLLDDFSLDALVG--PADLDWSAFHRQDPAAAC 159
Cdd:PRK06187 94 EIAYILNDAEDRVVLVDSEfVPLLAAILPQLPTVrtvivegdGPAAPLAPEVGEYEELLAaaSDTFDFPDIDENDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 flqYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYSIPKMF--FGYGMGnslFFPWFSGASALLDDTWPsPE 237
Cdd:PRK06187 174 ---YTSGTTGHPKGVVLSHRNLFLHSLA-VCAWLKLSRDDVYLVIVPMFhvHAWGLP---YLALMAGAKQVIPRRFD-PE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 238 RVLENLVAFRPRVLFGVPAIY----ASLRPQARELlSSVRLAFSAGSPLPRG---EFEfwAAHGLEICDGIGATEVGHVF 310
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWqmllKAPRAYFVDF-SSLRLVIYGGAALPPAllrEFK--EKFGIDLVQGYGMTETSPVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 311 LANRP------GQARADSTGLPLPGYECRLVDREGHTIEEAGRQ-GVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDL 383
Cdd:PRK06187 323 SVLPPedqlpgQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 384 FERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE-AVL-VPtcrlhD---GLRPTLFVTLAtpldDNQIL 458
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGH-PAVAEvAVIgVP-----DekwGERPVAVVVLK----PGATL 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15596193 459 LAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK06187 473 DAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
17-496 |
8.84e-62 |
|
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: 208.62 E-value: 8.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRV-VLALNdSPSLACLFLACIAVGAIPAVINPKSREQALAD 94
Cdd:cd17631 8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALgVAKGDRVaVLSKN-SPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 95 IAADCQASLvvreadapslsgplapltlraaagrpLLDDFsldalvgpadldwsafhrqdpaaaCFLQYTSGSTGAPKGV 174
Cdd:cd17631 87 ILADSGAKV--------------------------LFDDL------------------------ALLMYTSGTTGRPKGA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 175 MHSLRNTLGFCRAFATELlALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTwPSPERVLENLVAFRPRVLFGV 254
Cdd:cd17631 117 MLTHRNLLWNAVNALAAL-DLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK-FDPETVLDLIERHRVTSFFLV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 255 PAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPG--QARADSTGLPLPG 329
Cdd:cd17631 195 PTMIQALlqHPRFATTdLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEdhRRKLGSAGRPVFF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 330 YECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWV 409
Cdd:cd17631 275 VEVRIVDPDGREVP-PGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 410 VPTQVEQAICRHlPEVSE-AVL-VPtcrlHD--GLRPTLFVTlatpLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPA 485
Cdd:cd17631 354 YPAEVEDVLYEH-PAVAEvAVIgVP----DEkwGEAVVAVVV----PRPGAELDEDELIAHCRERLARYKIPKSVEFVDA 424
|
490
....*....|.
gi 15596193 486 LPRNDNGKLAR 496
Cdd:cd17631 425 LPRNATGKILK 435
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
48-500 |
1.09e-58 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 206.42 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 48 RLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVReadapslSGPLApltlraaag 127
Cdd:PRK06060 50 RGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-------SDALR--------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 128 rpllDDFSLDALVGPADLdWSAFHRQDPA--------AACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGD 199
Cdd:PRK06060 114 ----DRFQPSRVAEAAEL-MSEAARVAPGgyepmggdALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 200 RLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQ-ARELLSSVRLAFSA 278
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDScSPDSFRSLRCVVSA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 279 GSPLPRG----EFEFWAahGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTiEEAGRQGVLLVR 354
Cdd:PRK06060 269 GEALELGlaerLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTT-AGPGVEGDLWVR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 355 GPGLSPGYWRASEEQQARfaGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTc 434
Cdd:PRK06060 346 GPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED-EAVAEAAVVAV- 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 435 RLHDG---LRPTLFVTLATPLDDNqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK06060 422 RESTGastLQAFLVATSGATIDGS---VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
43-500 |
1.27e-57 |
|
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: 197.56 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAI--PAVINPKSReqALADIAADCQASLVVREADAPslsgplap 119
Cdd:cd05972 14 ANVLAKLgLRKGDRVAVLLPRVPELWAVILAVIKLGAVyvPLTTLLGPK--DIEYRLEAAGAKAIVTDAEDP-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 120 ltlraaagrpllddfsldalvgpadldwsafhrqdpaaaCFLQYTSGSTGAPKGVMHSLRNTLGFcRAFATELLALQAGD 199
Cdd:cd05972 84 ---------------------------------------ALIYFTSGTTGLPKGVLHTHSYPLGH-IPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 200 RLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWP-SPERVLENLVAFRPRVLFGVPAIYASLRPQ--ARELLSSVRLAF 276
Cdd:cd05972 124 IHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYRMLIKQdlSSYKFSHLRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 277 SAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVfLANRPGQ-ARADSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVR 354
Cdd:cd05972 204 SAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGLT-VGNFPDMpVKPGSMGRPTPGYDVAIIDDDGRELPP-GEEGDIAIK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 355 --GPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVP 432
Cdd:cd05972 282 lpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH-PAVAEAAVVG 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 433 TcrlHDGLR---PTLFVTLA---TPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05972 361 S---PDPVRgevVKAFVVLTsgyEPSEE----LAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-500 |
5.45e-56 |
|
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: 192.89 E-value: 5.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVreadapslsgplapltl 122
Cdd:cd05934 18 AALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 123 raaagrpllddfsldalvgpadldwsafhrQDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLY 202
Cdd:cd05934 81 ------------------------------VDPAS---ILYTSGTTGPPKGVVITHANLTFAGYYSA-RRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 203 SIPKMFFGYGMGNSLFFPWFSGASALLDDT------WPSPER---VLENLVAFRPRVLFGVPaiyaslrPQARELLSSVR 273
Cdd:cd05934 127 TVLPLFHINAQAVSVLAALSVGATLVLLPRfsasrfWSDVRRygaTVTNYLGAMLSYLLAQP-------PSPDDRAHRLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 274 LAFSAGSPlPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLV 353
Cdd:cd05934 200 AAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELP-AGEPGELVI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 354 R---GPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL 430
Cdd:cd05934 278 RglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRH-PAVREAAV 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 431 VPTcrlHDGLRPTLfVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05934 357 VAV---PDEVGEDE-VKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
42-499 |
8.03e-56 |
|
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: 193.13 E-value: 8.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVvreadapslsgp 116
Cdd:cd05930 21 RANRLARYLrergvGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 lapltlraaagrpllddfsldaLVGPADLdwsafhrqdpaaaCFLQYTSGSTGAPKGVM---HSLRNTLgfcrAFATELL 193
Cdd:cd05930 89 ----------------------LTDPDDL-------------AYVIYTSGSTGKPKGVMvehRGLVNLL----LWMQEAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 194 ALQAGDRLYSipKMFFGY-GMGNSLFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQA-RELL 269
Cdd:cd05930 130 PLTPGDRVLQ--FTSFSFdVSVWEIFGALLAGATLVVlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELeLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 270 SSVRLAFSAGSPLPRGEFEFWAA--HGLEICDGIGATE--VGHVFLANRPGQARADST--GLPLPGYECRLVDREGHTIE 343
Cdd:cd05930 208 PSLRLVLVGGEALPPDLVRRWREllPGARLVNLYGPTEatVDATYYRVPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 344 eAGRQGVLLVRGPGLSPGYWRASEEQQARF------AGGW-YRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQ 416
Cdd:cd05930 288 -PGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERmYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 417 AICRHlPEVSEAVLVPtcRLHDGLRPTL--FVTLatplDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKL 494
Cdd:cd05930 367 ALLAH-PGVREAAVVA--REDGDGEKRLvaYVVP----DEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
....*
gi 15596193 495 ARAEL 499
Cdd:cd05930 440 DRKAL 444
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
27-500 |
1.36e-54 |
|
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: 189.81 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCrtyiLSQASQLARLL------KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQ 100
Cdd:cd05941 9 GDSITYADL----VARAARLANRLlalgkdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 101 ASLVVreadapslsgplapltlraaagrpllddfsldalvgpadldwsafhrqDPAAACflqYTSGSTGAPKGVMHSLRN 180
Cdd:cd05941 85 PSLVL------------------------------------------------DPALIL---YTSGTTGRPKGVVLTHAN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 181 TLGFCRAFAtELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDdTWPSPERVLENLVAFRPRVLFGVPAIYAS 260
Cdd:cd05941 114 LAANVRALV-DAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL-PKFDPKEVAISRLMPSITVFMGVPTIYTR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 261 L-----------RPQARELLSSVRLAFSAGSPLPRGEFEFWAA-HGLEICDGIGATEVGhVFLANR-PGQARADSTGLPL 327
Cdd:cd05941 192 LlqyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAiTGHTLLERYGMTEIG-MALSNPlDGERRPGTVGMPL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 328 PGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGRE-DDLFKVN 405
Cdd:cd05941 271 PGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFtDDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 406 GRWVVPTQVEQAICRHlPEVSE-AVL-VPtcrlHD--GLRPTLFVTLAtplDDNQILLAQRIDQHLAEQIPSHMLPSQLH 481
Cdd:cd05941 351 GYKVSALEIERVLLAH-PGVSEcAVIgVP----DPdwGERVVAVVVLR---AGAAALSLEELKEWAKQRLAPYKRPRRLI 422
|
490
....*....|....*....
gi 15596193 482 VLPALPRNDNGKLARAELR 500
Cdd:cd05941 423 LVDELPRNAMGKVNKKELR 441
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
27-494 |
8.01e-54 |
|
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: 188.96 E-value: 8.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVV 105
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLgLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 READapslsgpLAPLTLRAAAGRP------LLDDfSLDALVGPADLDWSAFHRQ-------------DPAAACflqYTSG 166
Cdd:cd05911 88 TDPD-------GLEKVKEAAKELGpkdkiiVLDD-KPDGVLSIEDLLSPTLGEEdedlppplkdgkdDTAAIL---YSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 167 STGAPKGVMHSLRN-TLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFsGASALLDDTwPSPERVLENLVA 245
Cdd:cd05911 157 TTGLPKGVCLSHRNlIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPK-FDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 246 FRPRVLFGVPAIYASL--RPQA-RELLSSVRLAFSAGSPLPRGEFEFWAA--HGLEICDGIGATEVGHVFLANRPGQARA 320
Cdd:cd05911 235 YKITFLYLVPPIAAALakSPLLdKYDLSSLRVILSGGAPLSKELQELLAKrfPNATIKQGYGMTETGGILTVNPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 321 DSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGRED 399
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEAtKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 400 DLFKVNGRWVVPTQVEQAIcRHLPEVSEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHmlpSQ 479
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVL-LEHPGVADAAVIGIPDEVSGELPRAYVVRK----PGEKLTEKEVKDYVAKKVASY---KQ 466
|
490
....*....|....*....
gi 15596193 480 LH----VLPALPRNDNGKL 494
Cdd:cd05911 467 LRggvvFVDEIPKSASGKI 485
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
43-431 |
7.70e-52 |
|
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: 182.80 E-value: 7.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREadapslsgplaplt 121
Cdd:cd05907 19 AKGLIALgVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 122 lraaagrpllddfsldalvGPADLdwsafhrqdpaaaCFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRL 201
Cdd:cd05907 85 -------------------DPDDL-------------ATIIYTSGTTGRPKGVMLSHRNILSNALA-LAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 202 YSipkmF------FGYGMGnsLFFPWFSGASALLddtWPSPERVLENLVAFRPRVLFGVPAI----YASLRPQA------ 265
Cdd:cd05907 132 LS----FlplahvFERRAG--LYVPLLAGARIYF---ASSAETLLDDLSEVRPTVFLAVPRVwekvYAAIKVKAvpglkr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 266 ----RELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDreght 341
Cdd:cd05907 203 klfdLAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 342 ieeagrQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV-NGRWVVPTQVEQAIC 419
Cdd:cd05907 278 ------DGEILVRGPNVMLGYYKNPEAtAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALK 351
|
410
....*....|..
gi 15596193 420 RHlPEVSEAVLV 431
Cdd:cd05907 352 AS-PLISQAVVI 362
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-431 |
5.86e-51 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 183.38 E-value: 5.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 1 MSTLANLTEVLF-RLDFDPDTAVYHYRG----QTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACI 74
Cdd:COG1022 7 VPPADTLPDLLRrRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALgVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 75 AVGAIPAVINPKSREQALADIAADCQASLVVRE------------ADAPSL--------SGPLAPLTLRA-----AAGRP 129
Cdd:COG1022 87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldkllevrDELPSLrhivvldpRGLRDDPRLLSldellALGRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 130 LLDDFSLDALVGPADLDwsafhrqDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYSI-P--- 205
Cdd:COG1022 167 VADPAELEARRAAVKPD-------DLAT---IIYTSGTTGRPKGVMLTHRNLLSNARA-LLERLPLGPGDRTLSFlPlah 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 206 ---KMFFGYGM--GNSLFFPwfsgasallddtwPSPERVLENLVAFRPRVLFGVPAIY---------------------- 258
Cdd:COG1022 236 vfeRTVSYYALaaGATVAFA-------------ESPDTLAEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkrklf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 259 ---------------------ASLRPQA-----------RELL-SSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATE 305
Cdd:COG1022 303 rwalavgrryararlagkspsLLLRLKHaladklvfsklREALgGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 306 VGHVFLANRPGQARADSTGLPLPGYECRLvdreghtieeaGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLF 384
Cdd:COG1022 383 TSPVITVNRPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEAtAEAFDADGWLHTGDIG 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15596193 385 ERDESGAYRHCGREDDLFKV-NGRWVVPTQVEQAICRHlPEVSEAVLV 431
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKAS-PLIEQAVVV 498
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
6-500 |
4.86e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.33 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 6 NLTEVLFRL-DFDPDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVI 83
Cdd:PRK07656 6 TLPELLARAaRRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALgIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 84 NPKSREQALADIAADCQASLVVReadapslSGPLAPLTLRAAAGRPLLD-----DFSLDALVGPADLDWSAF-------- 150
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFV-------LGLFLGVDYSATTRLPALEhvvicETEEDDPHTEKMKTFTDFlaagdpae 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 151 -----HRQDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMF--FGYGMGnsLFFPWFS 223
Cdd:PRK07656 159 rapevDPDDVAD---ILFTSGTTGRPKGAMLTHRQLLSNAADWA-EYLGLTEGDRYLAANPFFhvFGYKAG--VNAPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 224 GASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLP-------RGEFEFWAah 293
Cdd:PRK07656 233 GATILPLPVF-DPDEVFRLIETERITVLPGPPTMYNSLlqHPDRSAEdLSSLRLAVTGAASMPvallerfESELGVDI-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 294 gleICDGIGATEVGHVFLANRPGQARAD---STGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQ 370
Cdd:PRK07656 310 ---VLTGYGLSEASGVTTFNRLDDDRKTvagTIGTAIAGVENKIVNELGEEVP-VGEVGELLVRGPNVMKGYYDDPEATA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 371 ARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL--VPTCRLHDGLRPtlFVT 447
Cdd:PRK07656 386 AAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH-PAVAEAAVigVPDERLGEVGKA--YVV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 448 L--ATPLDDNQILLAQRidQHLAeqipSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07656 463 LkpGAELTEEELIAYCR--EHLA----KYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
43-500 |
1.24e-49 |
|
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: 178.21 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRV-VLALNDSPSLACLFlaciAVGAIPAV---INPK-SREQaLADIAADCQASLVVREADAPSLSGP 116
Cdd:cd12119 39 ANALRRLgVKPGDRVaTLAWNTHRHLELYY----AVPGMGAVlhtINPRlFPEQ-IAYIINHAEDRVVFVDRDFLPLLEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 LAP--------LTLRAAAGRPLLDDFSL---DALVGPAD--LDWSAFHRQDPAAACflqYTSGSTGAPKGVMHSLRNT-L 182
Cdd:cd12119 114 IAPrlptvehvVVMTDDAAMPEPAGVGVlayEELLAAESpeYDWPDFDENTAAAIC---YTSGTTGNPKGVVYSHRSLvL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 183 GFCRAFATELLALQAGDRLYSIPKMFFGYGMGnslfFPW---FSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYA 259
Cdd:cd12119 191 HAMAALLTDGLGLSESDVVLPVVPMFHVNAWG----LPYaaaMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 260 SLRPQAREL---LSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATE------VGHV--FLANRPGQARAD---STGL 325
Cdd:cd12119 267 GLLDHLEANgrdLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTEtsplgtVARPpsEHSNLSEDEQLAlraKQGR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREGHTIEEAGR-QGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV 404
Cdd:cd12119 347 PVPGVELRIVDDDGRELPWDGKaVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 NGRWVVPTQVEQAICRHlPEVSEA--VLVPtcrlHD--GLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHMLPSQL 480
Cdd:cd12119 427 GGEWISSVELENAIMAH-PAVAEAavIGVP----HPkwGERPLAVVVLK----EGATVTAEELLEFLADKVAKWWLPDDV 497
|
490 500
....*....|....*....|
gi 15596193 481 HVLPALPRNDNGKLARAELR 500
Cdd:cd12119 498 VFVDEIPKTSTGKIDKKALR 517
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
42-429 |
2.30e-49 |
|
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: 174.76 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLL------KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSLsg 115
Cdd:TIGR01733 8 RANRLARHLraaggvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 plapltLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLAL 195
Cdd:TIGR01733 86 ------LAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLA-RRYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 196 QAGDRLYsipkMFFGYGMGNS---LFFPWFSGASALLDDtwPSPERVLENLVAF--RPR---VLFGVPAIYASLRPQARE 267
Cdd:TIGR01733 159 DPDDRVL----QFASLSFDASveeIFGALLAGATLVVPP--EDEERDDAALLAAliAEHpvtVLNLTPSLLALLAAALPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 268 LLSSVRLAFSAGSPLPRGEFEFWAA--HGLEICDGIGATE---VGHVFLANRPGQARADST--GLPLPGYECRLVDREGh 340
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDRWRArgPGARLINLYGPTEttvWSTATLVDPDDAPRESPVpiGRPLANTRLYVLDDDL- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 341 TIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFA---------GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVP 411
Cdd:TIGR01733 312 RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVpdpfaggdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 15596193 412 TQVEQAICRHlPEVSEAV 429
Cdd:TIGR01733 392 GEIEAALLRH-PGVREAV 408
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
48-500 |
4.96e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 176.15 E-value: 4.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 48 RLLKPGDRV-VLALNdSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAdapslsgplapltlRAAA 126
Cdd:PRK09088 42 RGCVDGERLaVLARN-SVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDD--------------AVAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 127 GRPllDDFSLDALVGPADLDWSAFHRQ-DPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATeLLALQAGDRLYSIP 205
Cdd:PRK09088 107 GRT--DVEDLAAFIASADALEPADTPSiPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGV-LGRVDAHSSFLCDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 206 KMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLV--AFRPRVLFGVPAIYASLRPQ---ARELLSSVRLAFSAGS 280
Cdd:PRK09088 184 PMFHIIGLITSVRPVLAVGGSILVSNGF-EPKRTLGRLGdpALGITHYFCVPQMAQAFRAQpgfDAAALRHLTALFTGGA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 281 PLPRGEFEFWAAHGLEICDGIGATEVGHVF-LANRPG--QARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPG 357
Cdd:PRK09088 263 PHAAEDILGWLDDGIPMVDGFGMSEAGTVFgMSVDCDviRAKAGAAGIPTPTVQTRVVDDQGNDCP-AGVPGELLLRGPN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 358 LSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRL 436
Cdd:PRK09088 342 LSPGYWRRPQAtARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADH-PGIRECAVVGMADA 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 437 HDGLRPTLFVTLATPLDdnqiLLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK09088 421 QWGEVGYLAIVPADGAP----LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
16-500 |
5.72e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 177.50 E-value: 5.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 16 FDPDTAVYHYrGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALAD 94
Cdd:PRK05605 45 FGDRPALDFF-GATTTYAELGKQVRRAAAGLRALgVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 95 IAADCQASLVV---READ-APSLSGPLAPLTLRAA---AGRPLLDDFSL-----------DALVGPAD--LDWSAF---- 150
Cdd:PRK05605 124 PFEDHGARVAIvwdKVAPtVERLRRTTPLETIVSVnmiAAMPLLQRLALrlpipalrkarAALTGPAPgtVPWETLvdaa 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 151 ----------HRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFC---RAFATELlalqaGD---RLYSIPKMFFGYGMG 214
Cdd:PRK05605 204 iggdgsdvshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgKAWVPGL-----GDgpeRVLAALPMFHAYGLT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 215 NSLFFPWFSGASALLddtWPSPE--RVLENLVAFRPRVLFGVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGEFEF 289
Cdd:PRK05605 279 LCLTLAVSIGGELVL---LPAPDidLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvdLSGVRNAFSGAMALPVSTVEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 290 WAAH-GLEICDGIGATEVGHVFLANRPGQAR-ADSTGLPLPGYECRLVDREGHTIEEA-GRQGVLLVRGPGLSPGYWRAS 366
Cdd:PRK05605 356 WEKLtGGLLVEGYGLTETSPIIVGNPMSDDRrPGYVGVPFPDTEVRIVDPEDPDETMPdGEEGELLVRGPQVFKGYWNRP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 367 EEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRlHDGLRPtlfV 446
Cdd:PRK05605 436 EETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH-PGVEDAAVVGLPR-EDGSEE---V 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15596193 447 TLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK05605 511 VAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
18-496 |
6.06e-49 |
|
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: 174.74 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGA--IPavINPKSREQALAD 94
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLgLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVP--LDASSPAERIRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 95 IAADCQASLVVreadapslsgplapltlraaagrpllddfsldalvgpadldwsafhrQDPAAACFLQYTSGSTGAPKGV 174
Cdd:cd05945 83 ILDAAKPALLI-----------------------------------------------ADGDDNAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 175 MHSLRNTLGFCRAfATELLALQAGDRLYSIPKMFFGYGMGnSLFFPWFSGASallddTWPSPERVLEN---LVAFRPR-- 249
Cdd:cd05945 116 QISHDNLVSFTNW-MLSDFPLGPGDVFLNQAPFSFDLSVM-DLYPALASGAT-----LVPVPRDATADpkqLFRFLAEhg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 250 --VLFGVPAIYASLR---PQARELLSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATE-----VGHVFLANRPGQ 317
Cdd:cd05945 189 itVWVSTPSFAAMCLlspTFTPESLPSLRHFLFCGEVLPHKTARALQQRfpDARIYNTYGPTEatvavTYIEVTPEVLDG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 318 ARADSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF----AGGWYRTGDLFERDESGAYR 393
Cdd:cd05945 269 YDRLPIGYAKPGAKLVILDEDGRPVPP-GEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDnqiLLAQRIDQHLAEQIPS 473
Cdd:cd05945 348 YRGRLDFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA---GLTKAIKAELAERLPP 423
|
490 500
....*....|....*....|...
gi 15596193 474 HMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd05945 424 YMIPRRFVYLDELPLNANGKIDR 446
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
41-500 |
1.07e-48 |
|
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: 173.72 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVreadAPSLSG 115
Cdd:cd05903 9 TRADRLAAGLaalgvGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV----VPERFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 PLAPLtlraaagrpllddfsldalvgpadldwsafhrQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLAL 195
Cdd:cd05903 85 QFDPA--------------------------------AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYA-ERLGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 196 QAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL---RPQARELLSSV 272
Cdd:cd05903 132 GPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW-DPDKALALMREHGVTFMMGATPFLTDLlnaVEEAGEPLSRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLANRPG--QARADSTGLPLPGYECRLVDREGHTIEeAGRQG 349
Cdd:cd05903 211 RTFVCGGATVPRSLARrAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDDTGATLA-PGVEG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 350 VLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAV 429
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH-PGVIEAA 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596193 430 LV--PTCRLhdGLRPTLFVTLATP----LDDnqilLAQRIDQHlaeQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05903 369 VValPDERL--GERACAVVVTKSGalltFDE----LVAYLDRQ---GVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
43-500 |
1.59e-47 |
|
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: 170.76 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVReadAPSLsgplaplt 121
Cdd:cd05969 14 ANVLKSLgVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT---TEEL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 122 lraaagrpllddfsldalvgpadldwsaFHRQDPAAACFLQYTSGSTGAPKGVMHSlRNTLGFCRAFATELLALQAGDRL 201
Cdd:cd05969 83 ----------------------------YERTDPEDPTLLHYTSGTTGTPKGVLHV-HDAMIFYYFTGKYVLDLHPDDIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 202 YSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQAREL-----LSSVRLAF 276
Cdd:cd05969 134 WCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELarkydLSSLRFIH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 277 SAGSPL-PrgEFEFWA--AHGLEICDGIGATEVGHVFLANRPGQ-ARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLL 352
Cdd:cd05969 214 SVGEPLnP--EAIRWGmeVFGVPIHDTWWQTETGSIMIANYPCMpIKPGSMGKPLPGVKAAVVDENGNELP-PGTKGILA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 353 VRG--PGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL 430
Cdd:cd05969 291 LKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH-PAVAEAGV 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 431 VPTCRLHDGLRPTLFVTLA---TPLDDNQILLAQRIDQHLAeqipSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05969 370 IGKPDPLRGEIIKAFISLKegfEPSDELKEEIINFVRQKLG----AHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
41-499 |
5.07e-47 |
|
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: 169.17 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLLKP-----GDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAdapslsg 115
Cdd:TIGR01923 7 CEAAHLAKALKAqgirsGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 plaPLTLRAAagrpLLDDFSLDALVGPADLDWSA-FHRQDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLA 194
Cdd:TIGR01923 80 ---LLEEKDF----QADSLDRIEAAGRYETSLSAsFNMDQIAT---LMFTSGTTGKPKAVPHTFRNHYASAVGSK-ENLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 195 LQAGDR-LYSIPkMFFGYGMgnSLFFPWFSGASALlddTWPSPERVLENLVAfrprvlfGVPAIYASLRPQ-----AREL 268
Cdd:TIGR01923 149 FTEDDNwLLSLP-LYHISGL--SILFRWLIEGATL---RIVDKFNQLLEMIA-------NERVTHISLVPTqlnrlLDEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 269 LS--SVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRP-GQARADSTGLPLPGYECRLV--DREGHtie 343
Cdd:TIGR01923 216 GHneNLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPeMLHARPDVGRPLAGREIKIKvdNKEGH--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 344 eagrqGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlP 423
Cdd:TIGR01923 293 -----GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH-P 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 424 EVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQillaqrIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:TIGR01923 367 GIQEAVVVPKPDAEWGQVPVAYIVSESDISQAK------LIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
18-494 |
8.15e-45 |
|
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: 166.21 E-value: 8.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:cd17634 67 GDRTAIIYEGDDTSQSRTISYreLHREVCRFAGTLLdlgvkKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVrEADAPSLSGPLAPLtlraaagRPLLDDfSLDALVGP-------------------ADLDW---- 147
Cdd:cd17634 147 AVAGRIIDSSSRLLI-TADGGVRAGRSVPL-------KKNVDD-ALNPNVTSvehvivlkrtgsdidwqegRDLWWrdli 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 148 ---SAFHRQDPAAA---CFLQYTSGSTGAPKGVMHSlrnTLGFCRAFATEL---LALQAGDRLYSIPKMffGYGMGNS-- 216
Cdd:cd17634 218 akaSPEHQPEAMNAedpLFILYTSGTTGKPKGVLHT---TGGYLVYAATTMkyvFDYGPGDIYWCTADV--GWVTGHSyl 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 217 LFFPWFSGASALLDD---TWPSPERVLENLVAFRPRVLFGVPAIYASLRPQ-----ARELLSSVRLAFSAGSPLPRGEFE 288
Cdd:cd17634 293 LYGPLACGATTLLYEgvpNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaiEGTDRSSLRILGSVGEPINPEAYE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 289 -FWAAHGLEIC---DGIGATEVGHVFLANRPG--QARADSTGLPLPGYECRLVDREGHTIeEAGRQGVLLVRG--PGLSP 360
Cdd:cd17634 373 wYWKKIGKEKCpvvDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVDNEGHPQ-PGGTEGNLVITDpwPGQTR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 361 GYWRASEEQQ----ARFAGGWYrTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRL 436
Cdd:cd17634 452 TLFGDHERFEqtyfSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAH-PKVAEAAVVGIPHA 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 437 HDGLRPTLFVTL---ATPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKL 494
Cdd:cd17634 530 IKGQAPYAYVVLnhgVEPSPE----LYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
18-502 |
1.75e-44 |
|
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: 164.72 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHY------RGQTLSRLQCRTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPA-VINPKSREQ 90
Cdd:cd05931 7 PDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVpLPPPTPGRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 A--LADIAADCQASLVVreADAPSLSGPLAPLTLRAAAGRPLLddFSLDALVGPADLDWSAFHrQDPAAACFLQYTSGST 168
Cdd:cd05931 87 AerLAAILADAGPRVVL--TTAAALAAVRAFAASRPAAGTPRL--LVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 169 GAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYS-IPkMFFGYGMGNSLFFPWFSGASALLddTWPS-----PERVLEN 242
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQ-IRRAYGLDPGDVVVSwLP-LYHDMGLIGGLLTPLYSGGPSVL--MSPAaflrrPLRWLRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 243 LVAFRPRVLfGVP------AIYASLRPQAREL-LSSVRLAFSAGSP-----LPRGEFEFwAAHGL------------EIC 298
Cdd:cd05931 238 ISRYRATIS-AAPnfaydlCVRRVRDEDLEGLdLSSWRVALNGAEPvrpatLRRFAEAF-APFGFrpeafrpsyglaEAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 ---------DGIGATEVGHVFLANRPGQARAD--------STGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPG 361
Cdd:cd05931 316 lfvsggppgTGPVVLRVDRDALAGRAVAVAADdpaarelvSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 362 YWRASEEQQARF-------AGGWYRTGDL-FERDesGAYRHCGREDDLFKVNGRWVVPTQVEQAIcrhlpEVSEAVLVPT 433
Cdd:cd05931 396 YWGRPEATAETFgalaatdEGGWLRTGDLgFLHD--GELYITGRLKDLIIVRGRNHYPQDIEATA-----EEAHPALRPG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 434 C-----RLHDGLRPTLFV----TLATPLDDNQIllAQRIDQHLAEQipsHML-PSQLHVLP--ALPRNDNGKLARAELRH 501
Cdd:cd05931 469 CvaafsVPDDGEERLVVVaeveRGADPADLAAI--AAAIRAAVARE---HGVaPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
.
gi 15596193 502 L 502
Cdd:cd05931 544 A 544
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-499 |
6.44e-44 |
|
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: 161.69 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQcrtyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:cd12116 1 PDATAVRDDDRSLSYAE----LDERANRLAARLrargvGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVV---READAPSLSGPLAPLTLRAAAGrpllddfSLDALVGPADLDWSAFhrqdpaaacfLQYTSGSTG 169
Cdd:cd12116 77 RYILEDAEPALVLtddALPDRLPAGLPVLLLALAAAAA-------APAAPRTPVSPDDLAY----------VIYTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 170 APKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGYGmGNSLFFPWFSGASALL--DDTWPSPERVLENLVAFR 247
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMR-ERLGLGPGDRLLAVTTYAFDIS-LLELLLPLLAGARVVIapRETQRDPEALARLIEAHS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 248 PRVLFGVPAIYASLRPQARELLSSVRlAFSAGSPLPRGEFEFWAAHGLEICDGIGATE------VGHVFLANRPGQArad 321
Cdd:cd12116 218 ITVMQATPATWRMLLDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVGSLWNLYGPTEttiwstAARVTAAAGPIPI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 322 stGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARF--------AGGWYRTGDLFERDESGAYR 393
Cdd:cd12116 294 --GRPLANTQVYVLDAALRPVP-PGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagpGSRLYRTGDLVRRRADGRLE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVptcRLHDGLRPTL--FVTLATPLddnqILLAQRIDQHLAEQI 471
Cdd:cd12116 371 YLGRADGQVKIRGHRIELGEIEAALAAH-PGVAQAAVV---VREDGGDRRLvaYVVLKAGA----APDAAALRAHLRATL 442
|
490 500
....*....|....*....|....*...
gi 15596193 472 PSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
36-500 |
8.58e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 161.31 E-value: 8.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 36 RTYILSQASQLARLLKPGDRV-VLAlndSPSLACL--FLACIAVGaIPAV-INPKSREQALADIAADCQASLVVREADAP 111
Cdd:PRK07787 28 RSDLAGAATAVAERVAGARRVaVLA---TPTLATVlaVVGALIAG-VPVVpVPPDSGVAERRHILADSGAQAWLGPAPDD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 112 SLSGPLAPLTLRAAAgrpllddfsldalvgpadldWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRntlgfcrAFATE 191
Cdd:PRK07787 104 PAGLPHVPVRLHARS--------------------WHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRR-------AIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 192 LLALQ------AGDRLYSIPKMFFGYGMGNSLFFPWFSGaSALLDDTWPSPERVLENLvAFRPRVLFGVPAIYASL--RP 263
Cdd:PRK07787 157 LDALAeawqwtADDVLVHGLPLFHVHGLVLGVLGPLRIG-NRFVHTGRPTPEAYAQAL-SEGGTLYFGVPTVWSRIaaDP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 264 QARELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTI 342
Cdd:PRK07787 235 EAARALRGARLLVSGSAALPVPVFDRLAALtGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 343 EEAGRQ-GVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGRED-DLFKVNGRWVVPTQVEQAIC 419
Cdd:PRK07787 315 PHDGETvGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 420 RHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQIllaqrIDqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK07787 395 GH-PGVREAAVVGVPDDDLGQRIVAYVVGADDVAADEL-----ID-FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
.
gi 15596193 500 R 500
Cdd:PRK07787 468 L 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-500 |
1.06e-42 |
|
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: 157.68 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAI--P--AVINPKSREQALAdiAADcqASLVVREADap 111
Cdd:cd05973 8 ALSARFANALqelgvGPGDVVAGLLPRTPELVVTILGIWRLGAVyqPlfTAFGPKAIEHRLR--TSG--ARLVVTDAA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 112 slsgplapltlraaaGRPLLDDfslDALVgpadldwsafhrqdpaaacfLQYTSGSTGAPKGVMHSLRNTLGFcRAFATE 191
Cdd:cd05973 82 ---------------NRHKLDS---DPFV--------------------MMFTSGTTGLPKGVPVPLRALAAF-GAYLRD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 192 LLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLR----PQARE 267
Cdd:cd05973 123 AVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMaagaEVPAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 268 LLSSVRLAFSAGSPL-PRGEFEFWAAHGLEICDGIGATEVGhVFLANRPGQA---RADSTGLPLPGYECRLVDREGHTIE 343
Cdd:cd05973 203 PKGRLRRVSSAGEPLtPEVIRWFDAALGVPIHDHYGQTELG-MVLANHHALEhpvHAGSAGRAMPGWRVAVLDDDGDELG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 344 EaGRQGVLLV---RGPGLS-PGYWRAseeQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAIC 419
Cdd:cd05973 282 P-GEPGRLAIdiaNSPLMWfRGYQLP---DTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 420 RHlPEVSEAVLVPTcrlHDGLRPTL---FVTLAtPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd05973 358 EH-PAVAEAAVIGV---PDPERTEVvkaFVVLR-GGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....
gi 15596193 497 AELR 500
Cdd:cd05973 433 FLLR 436
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
43-499 |
1.07e-42 |
|
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: 158.52 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSLSGPL 117
Cdd:cd12117 32 ANRLARRLRaagvgPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 118 APLTLRAAAgrplLDDFSLDALVGPADldwsafhrqdPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAfaTELLALQA 197
Cdd:cd12117 112 EVAVVIDEA----LDAGPAGNPAVPVS----------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN--TNYVTLGP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 198 GDR-LYSIPKMF--FGYgmgnSLFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQARELLSSV 272
Cdd:cd12117 176 DDRvLQTSPLAFdaSTF----EIWGALLNGARLVLapKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATE-----VGHVFlanRPGQARADST--GLPLPGYECRLVDREGHtIE 343
Cdd:cd12117 252 RELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEnttftTSHVV---TELDEVAGSIpiGRPIANTRVYVLDEDGR-PV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 344 EAGRQGVLLVRGPGLSPGYWRASEEQQARFA-------GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQ 416
Cdd:cd12117 328 PPGVPGELYVGGDGLALGYLNRPALTAERFVadpfgpgERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 417 AICRHlPEVSEAVLVPtcRLHDGLRPTL--FVTLATPLDDNQIllaqriDQHLAEQIPSHMLPSQLHVLPALPRNDNGKL 494
Cdd:cd12117 408 ALRAH-PGVREAVVVV--REDAGGDKRLvaYVVAEGALDAAEL------RAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
....*
gi 15596193 495 ARAEL 499
Cdd:cd12117 479 DRRAL 483
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
18-503 |
3.85e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 158.29 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PD-TAVYHYRG-----QTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:PRK13295 38 PDkTAVTAVRLgtgapRRFTYRELAALVDRVAVGLARLgVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRER 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALadiaadcqaSLVVREADAPSLsgpLAPLTLR-------AAAGRPLL------------DDFSLDALV-------GPAD 144
Cdd:PRK13295 118 EL---------SFMLKHAESKVL---VVPKTFRgfdhaamARRLRPELpalrhvvvvggdGADSFEALLitpaweqEPDA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 145 LDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMF----FGYGMgnslFFP 220
Cdd:PRK13295 186 PAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYA-ERLGLGADDVILMASPMAhqtgFMYGL----MMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 221 WFSGASALLDDTWpSPERVLEnLVAfRPRVLF---GVPAIYASLRPQA--RELLSSVRLAFSAGSPLPRGEFE-FWAAHG 294
Cdd:PRK13295 261 VMLGATAVLQDIW-DPARAAE-LIR-TEGVTFtmaSTPFLTDLTRAVKesGRPVSSLRTFLCAGAPIPGALVErARAALG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 295 LEICDGIGATEVGHVFLAnRPGQA--RADST-GLPLPGYECRLVDREGHTIeEAGRQGVLLVRGPGLSPGYWRaSEEQQA 371
Cdd:PRK13295 338 AKIVSAWGMTENGAVTLT-KLDDPdeRASTTdGCPLPGVEVRVVDADGAPL-PAGQIGRLQVRGCSNFGGYLK-RPQLNG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 372 RFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA--VLVPTCRLhdGLRPTLFVTLA 449
Cdd:PRK13295 415 TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRH-PAIAQVaiVAYPDERL--GERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596193 450 TpldDNQILLAQRID----QHLAEQipshMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:PRK13295 492 P---GQSLDFEEMVEflkaQKVAKQ----YIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
41-500 |
5.20e-41 |
|
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: 154.04 E-value: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREA-DAPSLS 114
Cdd:cd17651 28 RRANRLAHRLrargvGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPaLAGELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 115 GPLAPLTLRAAAGRPLLDDFSLDALVGPADLdwsafhrqdpaaaCFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLA 194
Cdd:cd17651 108 VELVAVTLLDQPGAAAGADAEPDPALDADDL-------------AYVIYTSGSTGRPKGVVMPHRSLANLVAWQA-RASS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 195 LQAGDRLYSIpkMFFGYGMGNSLFFPWFSGASALL---DDTWPSPERVLENLVAFRPRVLF----GVPAIYASLRPQARE 267
Cdd:cd17651 174 LGPGARTLQF--AGLGFDVSVQEIFSTLCAGATLVlppEEVRTDPPALAAWLDEQRISRVFlptvALRALAEHGRPLGVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 268 LLSsVRLAFSAGSPLPRGEF--EFWAAH-GLEICDGIGATE----VGHVFLANRPGQARADSTGLPLPGYECRLVDREGH 340
Cdd:cd17651 252 LAA-LRYLLTGGEQLVLTEDlrEFCAGLpGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 341 TIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFA-------GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQ 413
Cdd:cd17651 331 PVP-PGVPGELYIGGAGLARGYLNRPELTAERFVpdpfvpgARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLatplDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:cd17651 410 IEAALARH-PGVREAVVLAREDRPGEKRLVAYVVG----DPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGK 484
|
....*..
gi 15596193 494 LARAELR 500
Cdd:cd17651 485 LDRRALP 491
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-500 |
7.63e-41 |
|
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: 152.98 E-value: 7.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVI----NPKSREQALADIAADCQASLVVreadapsl 113
Cdd:cd05922 3 VSAAASALLeaggvRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvplNPTLKESVLRYLVADAGGRIVL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 114 sgPLAPLTLRAAAGRPLLDD----FSLDALVGPADlDWSAFHRQDPAAACFLqYTSGSTGAPKGVMHSLRNTLGFCRAFA 189
Cdd:cd05922 75 --ADAGAADRLRDALPASPDpgtvLDADGIRAARA-SAPAHEVSHEDLALLL-YTSGSTGSPKLVRLSHQNLLANARSIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 190 tELLALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQAR--E 267
Cdd:cd05922 151 -EYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFdpA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 268 LLSSVRLAFSAGSPLP-------RGEFEFWAAHGLeicdgIGATEVGHVF-------LANRPGqaradSTGLPLPGYECR 333
Cdd:cd05922 229 KLPSLRYLTQAGGRLPqetiarlRELLPGAQVYVM-----YGQTEATRRMtylpperILEKPG-----SIGLAIPGGEFE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 334 LVDREGhTIEEAGRQGVLLVRGPGLSPGYWRA-SEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPT 412
Cdd:cd05922 299 ILDDDG-TPTPPGEPGEIVHRGPNVMKGYWNDpPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 413 QVEQAICRhLPEVSEAVLVptcrlhdGLRPT------LFVTLATPLDDNQILlaqridQHLAEQIPSHMLPSQLHVLPAL 486
Cdd:cd05922 378 EIEAAARS-IGLIIEAAAV-------GLPDPlgeklaLFVTAPDKIDPKDVL------RSLAERLPPYKVPATVRVVDEL 443
|
490
....*....|....
gi 15596193 487 PRNDNGKLARAELR 500
Cdd:cd05922 444 PLTASGKVDYAALR 457
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
18-499 |
1.26e-40 |
|
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: 152.81 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTyilsQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDE----RANRLAHLLrargvGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVVREADapsLSGPLAPLTLRAAAGRPLLDDFsldalvgPADLDWSAFHRQDPAaacFLQYTSGSTGAPK 172
Cdd:cd17646 88 AYMLADAGPAVVLTTAD---LAARLPAGGDVALLGDEALAAP-------PATPPLVPPRPDNLA---YVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVM--HslrntlgfcRAFATELLALQ------AGDRLysIPKMFFGYGM-GNSLFFPWFSGASALLDDtwPSPERVLENL 243
Cdd:cd17646 155 GVMvtH---------AGIVNRLLWMQdeyplgPGDRV--LQKTPLSFDVsVWELFWPLVAGARLVVAR--PGGHRDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 244 VAFRPR----VLFGVPAIYAS-LRPQARELLSSVRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATE----VGHVfLAN 313
Cdd:cd17646 222 AALIREhgvtTCHFVPSMLRVfLAEPAAGSCASLRRVFCSGEALPPELAArFLALPGAELHNLYGPTEaaidVTHW-PVR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 RPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGW-------YRTGDLFER 386
Cdd:cd17646 301 GPAETPSVPIGRPVPNTRLYVLDDALRPVP-VGVPGELYLGGVQLARGYLGRPALTAERFVPDPfgpgsrmYRTGDLARW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 387 DESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtplDDNQILLAQRIDQH 466
Cdd:cd17646 380 RPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH-PAVTHAVVVARAAPAGAARLVGYVVPA---AGAAGPDTAALRAH 455
|
490 500 510
....*....|....*....|....*....|...
gi 15596193 467 LAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17646 456 LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
27-503 |
2.79e-40 |
|
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: 152.10 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLV-- 104
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVlt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 105 ----VREADAPSLSGPLAPLT------LRAAAGRPLLDDFSLDALVGPADLDWSAF-HRQDPAAACFLQYTSGSTGAPKG 173
Cdd:cd05909 85 skqfIEKLKLHHLFDVEYDARivyledLRAKISKADKCKAFLAGKFPPKWLLRIFGvAPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 174 VMHSLRNTLGFCRAfATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLddtWPSP---ERVLENLVAFRPRV 250
Cdd:cd05909 165 VVLSHKNLLANVEQ-ITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF---HPNPldyKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LFGVPAIY-ASLRPQARELLSSVRLAFSAGSPLPRGEFEFWA-AHGLEICDGIGATEVGHVFLANRPGQA-RADSTGLPL 327
Cdd:cd05909 241 LLGTPTFLrGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQeKFGIRILEGYGTTECSPVISVNTPQSPnKEGTVGRPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 328 PGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGR 407
Cdd:cd05909 321 PGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 408 WVVPTQVEQAICRHLPEVSE--AVLVPTCRLHDGLRPTLFVTLATPLDDNQILLAQridqhlaeQIPSHMLPSQLHVLPA 485
Cdd:cd05909 401 MVSLEAIEDILSEILPEDNEvaVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNA--------GISNLAKPSYIHQVEE 472
|
490
....*....|....*...
gi 15596193 486 LPRNDNGKLARAELRHLA 503
Cdd:cd05909 473 IPLLGTGKPDYVTLKALA 490
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
45-503 |
5.88e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 153.19 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 45 QLARLLK-PGDRVVLALNDSPSLACLFLACIAVGAIPAVinpksreqaladiaadcQASLVVREADAPSLSGPLAPLTLR 123
Cdd:PRK07529 120 QIAELLRaAGAKVLVTLGPFPGTDIWQKVAEVLAALPEL-----------------RTVVEVDLARYLPGPKRLAVPLIR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 124 AAAGRPLLD-DFSLDALVGPADLDWSAFHRQDPAAaCFlqYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLY 202
Cdd:PRK07529 183 RKAHARILDfDAELARQPGDRLFSGRPIGPDDVAA-YF--HTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFC 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 203 SIPkMFFGYGMGNSLFFPWFSGASALlddtWPSP-----ERVLEN---LVA-FRPRVLFGVPAIYASL--RPQARELLSS 271
Cdd:PRK07529 260 GLP-LFHVNALLVTGLAPLARGAHVV----LATPqgyrgPGVIANfwkIVErYRINFLSGVPTVYAALlqVPVDGHDISS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 272 VRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLANRP-GQARADSTGLPLPGYECRLV--DREGHTIEEAGR 347
Cdd:PRK07529 335 LRYALCGAAPLPVEVFRrFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 348 Q--GVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEV 425
Cdd:PRK07529 415 DevGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRH-PAV 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 426 SEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSH-MLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:PRK07529 494 ALAAAVGRPDAHAGELPVAYVQLK----PGASATEAELLAFARDHIAERaAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
159-503 |
8.24e-40 |
|
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: 146.71 E-value: 8.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 159 CFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDR-LYSIPKMFFGyGMGNSLFFPWFSGASALLDDTWPspe 237
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAG-LHSRLGFGGGDSwLLSLPLYHVG-GLAILVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 238 rVLENLVAFRPRVLFGVPAIYASL--RPQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRP 315
Cdd:cd17630 78 -LAEDLAPPGVTHVSLVPTQLQRLldSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 316 GQARADSTGLPLPGYECRLVDReghtieeagrqGVLLVRGPGLSPGYWRAsEEQQARFAGGWYRTGDLFERDESGAYRHC 395
Cdd:cd17630 157 DGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRG-QLVPEFNEDGWFTTKDLGELHADGRLTVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 396 GREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDnqillaQRIDQHLAEQIPSHM 475
Cdd:cd17630 225 GRADNMIISGGENIQPEEIEAALAAH-PAVRDAFVVGVPDEELGQRPVAVIVGRGPADP------AELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*...
gi 15596193 476 LPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
43-500 |
1.88e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 150.08 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADapslsgpLAPlT 121
Cdd:PRK08316 50 AAALLDLgLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA-------LAP-T 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 122 LRAAAGRPLLDDFSLDALVGPAD-----LDWSAFHRQDPAAA----------CFLQYTSGSTGAPKGVMHSLRNTLG-FC 185
Cdd:PRK08316 122 AEAALALLPVDTLILSLVLGGREapggwLDFADWAEAGSVAEpdveladddlAQILYTSGTESLPKGAMLTHRALIAeYV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 186 RAFATelLALQAGDR-LYSIPkMFFGYGMGNsLFFPWFS-GASALLDDTwPSPERVLENLVAFRPRVLFGVPAIYASL-- 261
Cdd:PRK08316 202 SCIVA--GDMSADDIpLHALP-LYHCAQLDV-FLGPYLYvGATNVILDA-PDPELILRTIEAERITSFFAPPTVWISLlr 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 262 RPQ-ARELLSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVGHVFLANRPGQ--ARADSTGLPLPGYECRLVD 336
Cdd:PRK08316 277 HPDfDTRDLSSLRKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAPLATVLGPEEhlRRPGSAGRPVLNVETRVVD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 337 REGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQ 416
Cdd:PRK08316 357 DDGNDVA-PGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 417 AICRHlPEVSEAVLVptcrlhdGL---RPTLFVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:PRK08316 436 ALYTH-PAVAEVAVI-------GLpdpKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
....*..
gi 15596193 494 LARAELR 500
Cdd:PRK08316 508 ILKRELR 514
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
53-500 |
4.20e-39 |
|
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: 149.57 E-value: 4.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 53 GDRVVLALNDSPSLACLFLACIAVGA--IPAVINPKSREQALADIAADCQASLVVREADAPSlsgplapltlRAAAGRPL 130
Cdd:cd05970 72 GDTVMLTLKRRYEFWYSLLALHKLGAiaIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPE----------EIEKAAPE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 131 LDDFSLDALVGPADLD-WSAFH------------RQDPAAAC-----FLQYTSGSTGAPKGVMHSLRNTLGFCrAFATEL 192
Cdd:cd05970 142 CPSKPKLVWVGDPVPEgWIDFRkliknaspdferPTANSYPCgedilLVYFSSGTTGMPKMVEHDFTYPLGHI-VTAKYW 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 193 LALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWP-SPERVLENLVAFRPRVLFGVPAIYASLRPQ--ARELL 269
Cdd:cd05970 221 QNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREdlSRYDL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 270 SSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGhVFLANRPG-QARADSTGLPLPGYECRLVDREGHTIEeAGR 347
Cdd:cd05970 301 SSLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTETT-LTIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCE-AGE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 348 QGVLLVRGP-----GLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHl 422
Cdd:cd05970 379 EGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQH- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 423 PEVSEAVL--VPtcrlhDGLRPTL---FVTLATPLDDNQILLAQRIDqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARA 497
Cdd:cd05970 458 PAVLECAVtgVP-----DPIRGQVvkaTIVLAKGYEPSEELKKELQD-HVKKVTAPYKYPRIVEFVDELPKTISGKIRRV 531
|
...
gi 15596193 498 ELR 500
Cdd:cd05970 532 EIR 534
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
18-506 |
8.75e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.04 E-value: 8.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQcrtyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ-- 90
Cdd:PRK06178 47 PQRPAIIFYGHVITYAE----LDELSDRFAALLrqrgvGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHel 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ----------------ALADIAADCQASLVVREA----------DAPSLsgPLAPLTL---RAAAGR----PLLDDFSLD 137
Cdd:PRK06178 123 syelndagaevllaldQLAPVVEQVRAETSLRHVivtsladvlpAEPTL--PLPDSLRaprLAAAGAidllPALRACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 138 ALVGPADLDwsafhrqDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSL 217
Cdd:PRK06178 201 VPLPPPALD-------ALAA---LNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 FFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAG-----SPLPR----- 284
Cdd:PRK06178 271 LFPLFSGATLVLLARW-DAVAFMAAVERYRVTRTVMLVDNAVELmdHPRFAEYdLSSLRQVRVVSfvkklNPDYRqrwra 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 285 --GEFEFWAAHGL---EICDGIGA-TEVGHVFLANRPGqaradSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGL 358
Cdd:PRK06178 350 ltGSVLAEAAWGMtetHTCDTFTAgFQDDDFDLLSQPV-----FVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 359 SPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHD 438
Cdd:PRK06178 425 LKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQH-PAVLGSAVVGRPDPDK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596193 439 GLRPTLFVTLATPLDdnqiLLAQRIDQHLAEQIPSHMLPsQLHVLPALPRNDNGKLARAELRHLADTL 506
Cdd:PRK06178 504 GQVPVAFVQLKPGAD----LTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEEL 566
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
11-499 |
7.28e-38 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 145.70 E-value: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 11 LFRLDFD-----PDTAVYHYRGQTLSRLQCRTYILSQASQL-ARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVIN 84
Cdd:TIGR03098 2 LHHLLEDaaarlPDATALVHHDRTLTYAALSERVLALASGLrGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 85 PKSREQALADIAADCQASLVVREA---DAPSLSGPLAPLTL---------RAAAGRPLLDDFSLDALVGPADLDwSAFHR 152
Cdd:TIGR03098 82 PLLKAEQVAHILADCNVRLLVTSSerlDLLHPALPGCHDLRtliivgdpaHASEGHPGEEPASWPKLLALGDAD-PPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 153 QDPAAACFLqYTSGSTGAPKGVMHSLRNTLGFCRAFATeLLALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLDDt 232
Cdd:TIGR03098 161 IDSDMAAIL-YTSGSTGRPKGVVLSHRNLVAGAQSVAT-YLENRPDDRLLAVLPLSFDYGF-NQLTTAFYVGATVVLHD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 233 WPSPERVLENLVAFRPRVLFGVPAIYASL-----RPQAREllsSVRLAFSAGSPLPRG----------EFEFWAAHGLei 297
Cdd:TIGR03098 237 YLLPRDVLKALEKHGITGLAAVPPLWAQLaqldwPESAAP---SLRYLTNSGGAMPRAtlsrlrsflpNARLFLMYGL-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 298 cdgigaTEV-GHVFLANRPGQARADSTGLPLPGYECrLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF--- 373
Cdd:TIGR03098 312 ------TEAfRSTYLPPEEVDRRPDSIGKAIPNAEV-LVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrpl 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 374 ---AGGWYRT------GDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRhLPEVSEAVL--VPTCRLHDGLrp 442
Cdd:TIGR03098 385 ppfPGELHLPelavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYA-TGLVAEAVAfgVPDPTLGQAI-- 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596193 443 tlfVTLATPLDDNQILLAQrIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:TIGR03098 462 ---VLVVTPPGGEELDRAA-LLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-500 |
3.52e-37 |
|
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: 142.19 E-value: 3.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAI----PAVINPKSREQALADIAADCqasLVVREADAPSL 113
Cdd:cd05971 16 SNRFANVLKeigleKGDRVGVFLSQGPECAIAHIAILRSGAIavplFALFGPEALEYRLSNSGASA---LVTDGSDDPAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 114 sgplapltlraaagrpllddfsldalvgpadldwsafhrqdpaaacfLQYTSGSTGAPKGVMHSLRNTLGFCRA--FATE 191
Cdd:cd05971 93 -----------------------------------------------IIYTSGTTGPPKGALHAHRVLLGHLPGvqFPFN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 192 LLAlQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWP-SPERVLENLVAFRPRVLFGVP-------AIYASLRP 263
Cdd:cd05971 126 LFP-RDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPtalkmmrQQGEQLKH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 264 QARELLSsvrlAFSAGSPLPRgEFEFWA--AHGLEICDGIGATEvGHVFLANRP--GQARADSTGLPLPGYECRLVDREG 339
Cdd:cd05971 205 AQVKLRA----IATGGESLGE-ELLGWAreQFGVEVNEFYGQTE-CNLVIGNCSalFPIKPGSMGKPIPGHRVAIVDDNG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 340 hTIEEAGRQGVLLVRGPglSP----GYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVE 415
Cdd:cd05971 279 -TPLPPGEVGEIAVELP--DPvaflGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 416 QAICRHlPEVSEAVLVPtcrLHDGLRPTL---FVTLATPLDDNQIlLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNG 492
Cdd:cd05971 356 ECLLKH-PAVLMAAVVG---IPDPIRGEIvkaFVVLNPGETPSDA-LAREIQELVKTRLAAHEYPREIEFVNELPRTATG 430
|
....*...
gi 15596193 493 KLARAELR 500
Cdd:cd05971 431 KIRRRELR 438
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
43-496 |
3.64e-37 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 143.22 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAD--------APSL 113
Cdd:cd05926 28 ARQLAALgIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGelgpasraASKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 114 SGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAAACFLqYTSGSTGAPKGVMHSLRNTLGFCRAFATElL 193
Cdd:cd05926 108 GLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALIL-HTSGTTGRPKGVPLTHRNLAASATNITNT-Y 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 194 ALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL--RPQA--RELL 269
Cdd:cd05926 186 KLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRF-SASTFWPDVRDYNATWYTAVPTIHQILlnRPEPnpESPP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 270 SSVRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLANR--PGQARADSTGLPLpGYECRLVDREGHTIeEAG 346
Cdd:cd05926 265 PKLRFIRSCSASLPPAVLEaLEATFGAPVLEAYGMTEAAHQMTSNPlpPGPRKPGSVGKPV-GVEVRILDEDGEIL-PPG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 347 RQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEV 425
Cdd:cd05926 343 VVGEICLRGPNVTRGYLNNPEAnAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAV 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 426 SEAVLVptcrlhdGLRPTLF---VTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd05926 422 LEAVAF-------GVPDEKYgeeVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR 488
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
50-499 |
6.14e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 142.69 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREadaPSLSGPLAPLTLRAAAGRP 129
Cdd:PRK06839 50 VKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE---KTFQNMALSMQKVSYVQRV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 130 LlddfSLDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLgFCRAFATELLALQAGDRLYSIPKMFF 209
Cdd:PRK06839 127 I----SITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMF-WNALNNTFAIDLTMHDRSIVLLPLFH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 210 GYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGE 286
Cdd:PRK06839 202 IGGIGLFAFPTLFAGGVIIVPRKF-EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFEttnLQSVRWFYNGGAPCPEEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 287 FEFWAAHGLEICDGIGATEVG-HVFLANRPGQAR-ADSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWR 364
Cdd:PRK06839 281 MREFIDRGFLFGQGFGMTETSpTVFMLSEEDARRkVGSIGKPVLFCDYELIDENKNKVEV-GEVGELLIRGPNVMKEYWN 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 365 ASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTL 444
Cdd:PRK06839 360 RPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKL-SDVYEVAVVGRQHVKWGEIPIA 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 445 FVTLATplddNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK06839 439 FIVKKS----SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
18-500 |
1.28e-36 |
|
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: 140.97 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRtyilSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:cd17649 1 PDAVALVFGDQSLSYAELD----ARANRLAHRLRalgvgPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVVReadapslsgplapltlraaagrpllddfsldalvgpadldwsafhrQDPAAACFLQYTSGSTGAPK 172
Cdd:cd17649 77 RYMLEDSGAGLLLT----------------------------------------------HHPRQLAYVIYTSGSTGTPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGyGMGNSLFFPWFSGASALLDDT--WPSPERVLENLVAFRPRV 250
Cdd:cd17649 111 GVAVSHGPLAAHCQATA-ERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVLRPDelWASADELAEMVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LfGVPAIYasLRPQARELLS-------SVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATE---VGHVFLAnRPGQARA 320
Cdd:cd17649 189 L-DLPPAY--LQQLAEEADRtgdgrppSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEatvTPLVWKC-EAGAARA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 321 DST---GLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-------AGG-WYRTGDLFERDES 389
Cdd:cd17649 265 GASmpiGRPLGGRSAYILDADLNPVPV-GVTGELYIGGEGLARGYLGRPELTAERFvpdpfgaPGSrLYRTGDLARWRDD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 390 GAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHDGLRPTLFVTLATPLDDNQILLAQRIDQHLAE 469
Cdd:cd17649 344 GVIEYLGRVDHQVKIRGFRIELGEIEAALLEH-PGVREAAVVA---LDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRA 419
|
490 500 510
....*....|....*....|....*....|.
gi 15596193 470 QIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd17649 420 SLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
39-500 |
1.82e-36 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 141.55 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 39 ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAI---------------------PAVI--NPKSREq 90
Cdd:PRK07514 34 LDAASARLANLLvalgvKPGDRVAVQVEKSPEALALYLATLRAGAVflplntaytlaeldyfigdaePALVvcDPANFA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLV-VREADApslSGPLapltLRAAAGRPllDDFSlDALVGPADLdwsafhrqdpaaACFLqYTSGSTG 169
Cdd:PRK07514 113 WLSKIAAAAGAPHVeTLDADG---TGSL----LEAAAAAP--DDFE-TVPRGADDL------------AAIL-YTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 170 APKGVMHSLRNTLGFCRAFAtELLALQAGDRL-YSIPkMFFGYGmgnsLFFP----WFSGASAL----LDdtwpsPERVL 240
Cdd:PRK07514 170 RSKGAMLSHGNLLSNALTLV-DYWRFTPDDVLiHALP-IFHTHG----LFVAtnvaLLAGASMIflpkFD-----PDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 241 ENLvafrPR--VLFGVPAIYASLRPQA---RELLSSVRLaFSAGS-PLPRGEFEFWAAH-GLEICDGIGATEVGhvFLAN 313
Cdd:PRK07514 239 ALM----PRatVMMGVPTFYTRLLQEPrltREAAAHMRL-FISGSaPLLAETHREFQERtGHAILERYGMTETN--MNTS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 RP--GQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESG 390
Cdd:PRK07514 312 NPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 391 aYRH-CGREDDLFKVNGRWVVPTQVEQAICRhLPEVSE----------------AVLVPtcrlhdglRPtlfvtlATPLD 453
Cdd:PRK07514 392 -YVHiVGRGKDLIISGGYNVYPKEVEGEIDE-LPGVVEsavigvphpdfgegvtAVVVP--------KP------GAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15596193 454 DNQILLAqridqhLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07514 456 EAAILAA------LKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
18-499 |
6.44e-36 |
|
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: 138.98 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLS--RLQCRtyilsqASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:cd17643 1 PEAVAVVDEDRRLTygELDAR------ANRLARTLRaegvgPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREADapslsgplapltlraaagrpllddfsldalvgpadldwsafhrqDPAaacFLQYTSGSTGA 170
Cdd:cd17643 75 RIAFILADSGPSLLLTDPD--------------------------------------------DLA---YVIYTSGSTGR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 171 PKGVMHSLRNtlgfcrafATELLAlqAGDRLYSIPK-----MFFGYGMGNS---LFFPWFSGASALLDDTWP--SPERVL 240
Cdd:cd17643 108 PKGVVVSHAN--------VLALFA--ATQRWFGFNEddvwtLFHSYAFDFSvweIWGALLHGGRLVVVPYEVarSPEDFA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 241 ENLVAFRPRVLFGVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGEFEFWAAH----GLEICDGIGATE----VGHV 309
Cdd:cd17643 178 RLLRDEGVTVLNQTPSAFYQLVEAADRDgrdPLALRYVIFGGEALEAAMLRPWAGRfgldRPQLVNMYGITEttvhVTFR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 310 FLANRPGQARADST-GLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARF----AGG----WYRT 380
Cdd:cd17643 258 PLDAADLPAAAASPiGRPLPGLRVYVLDADGRPVP-PGVVGELYVSGAGVARGYLGRPELTAERFvanpFGGpgsrMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 381 GDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTcrlHDGLRPTLFVTLATPlDDNQILLA 460
Cdd:cd17643 337 GDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH-PSVRDAAVIVR---EDEPGDTRLVAYVVA-DDGAAADI 411
|
490 500 510
....*....|....*....|....*....|....*....
gi 15596193 461 QRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17643 412 AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-500 |
2.89e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 138.09 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQL-ARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIA 96
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLhARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLVVREADAPSLSGPLAPLTLRAAAGRpllddfSLDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMH 176
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPKIVIDAAAQ------ADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 177 SLRNtLGFCRAFATELLALQAGDRLYSIPKMffgYGMGnSLFFP-----WFSGASALLDDTwpSPERVLENLVAFRPRVL 251
Cdd:PRK06145 170 SYGN-LHWKSIDHVIALGLTASERLLVVGPL---YHVG-AFDLPgiavlWVGGTLRIHREF--DPEAVLAAIERHRLTCA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 252 FGVPAIYA---SLRPQARELLSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEV--GHVFLANRPGQARADSTG 324
Cdd:PRK06145 243 WMAPVMLSrvlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETcsGDTLMEAGREIEKIGSTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 325 LPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV 404
Cdd:PRK06145 323 RALAHVEIRIADGAGRWLP-PNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 NGRWVVPTQVEQAIcRHLPEVSEAVLVPtcrLHD---GLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHMLPSQLH 481
Cdd:PRK06145 402 GGENIASSEVERVI-YELPEVAEAAVIG---VHDdrwGERITAVVVLN----PGATLTLEALDRHCRQRLASFKVPRQLK 473
|
490
....*....|....*....
gi 15596193 482 VLPALPRNDNGKLARAELR 500
Cdd:PRK06145 474 VRDELPRNPSGKVLKRVLR 492
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
42-513 |
5.16e-35 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 138.10 E-value: 5.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAD------A 110
Cdd:PRK04319 82 LSNKFANVLKelgveKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPAllerkpA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 111 PSLSGpLAPLTLRAAAGRPLLDDFSLDALV--GPADLDWSAFHRQDPAaacFLQYTSGSTGAPKGVMHsLRNTLGFCRAF 188
Cdd:PRK04319 162 DDLPS-LKHVLLVGEDVEEGPGTLDFNALMeqASDEFDIEWTDREDGA---ILHYTSGSTGKPKGVLH-VHNAMLQHYQT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 189 ATELLALQAGDRLYSI--PkmffGYGMGNS--LFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVP-AIY----A 259
Cdd:PRK04319 237 GKYVLDLHEDDVYWCTadP----GWVTGTSygIFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPtAIRmlmgA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 260 SLRPQARELLSSVRLAFSAGSPL-PrgEFEFWA--AHGLEICDGIGATEVGHVFLANRPGQA-RADSTGLPLPGYECRLV 335
Cdd:PRK04319 313 GDDLVKKYDLSSLRHILSVGEPLnP--EVVRWGmkVFGLPIHDNWWMTETGGIMIANYPAMDiKPGSMGKPLPGIEAAIV 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 336 DREGHTIEeAGRQGVLLVRG--PGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQ 413
Cdd:PRK04319 391 DDQGNELP-PNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHlPEVSEA-VL-VPtcrlhDGLRPTL---FVTLA---TPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLPA 485
Cdd:PRK04319 470 VESKLMEH-PAVAEAgVIgKP-----DPVRGEIikaFVALRpgyEPSEE----LKEEIRGFVKKGLGAHAAPREIEFKDK 539
|
490 500
....*....|....*....|....*...
gi 15596193 486 LPRNDNGKLARAELRhlADTLyhdNLPE 513
Cdd:PRK04319 540 LPKTRSGKIMRRVLK--AWEL---GLPE 562
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
50-500 |
8.66e-35 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 137.20 E-value: 8.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREA---------DAPSLSGPL--- 117
Cdd:PRK06155 68 VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAallaaleaaDPGDLPLPAvwl 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 118 --APLTLRAAAGRPLLDDFSLDALVGPADLdwsafHRQDPAAacfLQYTSGSTGAPKGVM--HSLRNTLGfcrAFATELL 193
Cdd:PRK06155 148 ldAPASVSVPAGWSTAPLPPLDAPAPAAAV-----QPGDTAA---ILYTSGTTGPSKGVCcpHAQFYWWG---RNSAEDL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 194 ALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPA---IYASLRPQARELLS 270
Cdd:PRK06155 217 EIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRF-SASGFWPAVRRHGATVTYLLGAmvsILLSQPARESDRAH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 271 SVRLAFSAGSPlPRGEFEFWAAHGLEICDGIGATEVGHVFlANRPGQARADSTGLPLPGYECRLVDREGHTIeEAGRQGV 350
Cdd:PRK06155 295 RVRVALGPGVP-AALHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQEL-PDGEPGE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 351 LLVRG--PG-LSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE 427
Cdd:PRK06155 372 LLLRAdePFaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH-PAVAA 450
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 428 AVLVPtcrlhdgLRPTLF---VTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK06155 451 AAVFP-------VPSELGedeVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-499 |
1.55e-34 |
|
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: 135.48 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PD-TAVyHYRGQTLSRLQCRTYILSQASQL-ARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADI 95
Cdd:cd12114 1 PDaTAV-ICGDGTLTYGELAERARRVAGALkAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 96 AADCQASLVVREADAPSLSGPLA-PLTLRAAAGRPllDDFSLDALVGPadldwsafhrQDPAaacFLQYTSGSTGAPKGV 174
Cdd:cd12114 80 LADAGARLVLTDGPDAQLDVAVFdVLILDLDALAA--PAPPPPVDVAP----------DDLA---YVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 175 MHSLRNTLGFCRAFaTELLALQAGDRLYSIPKMFFG---YgmgnSLFFPWFSGASALLddtwPSPERVLEN-----LVA- 245
Cdd:cd12114 145 MISHRAALNTILDI-NRRFAVGPDDRVLALSSLSFDlsvY----DIFGALSAGATLVL----PDEARRRDPahwaeLIEr 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 246 FRPRVLFGVPAIY---ASLRPQARELLSSVRLAFSAGS----PLPRGEFEFWAahGLEICDGIGATEVGHVFLANRPGQA 318
Cdd:cd12114 216 HGVTLWNSVPALLemlLDVLEAAQALLPSLRLVLLSGDwiplDLPARLRALAP--DARLISLGGATEASIWSIYHPIDEV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 319 RADST----GLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-----AGGWYRTGDLferdes 389
Cdd:cd12114 294 PPDWRsipyGRPLANQRYRVLDPRGRDCPD-WVPGELWIGGRGVALGYLGDPELTAARFvthpdGERLYRTGDL------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 390 GAYRH------CGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVptcRLHDGLRPTLfVTLATPLDDNQILLAQRI 463
Cdd:cd12114 367 GRYRPdgtlefLGRRDGQVKVRGYRIELGEIEAALQAH-PGVARAVVV---VLGDPGGKRL-AAFVVPDNDGTPIAPDAL 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 15596193 464 DQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd12114 442 RAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-503 |
2.14e-34 |
|
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: 132.99 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 DPAAACFlqYTSGSTGAPKGVMHSLRNTLGfcRAFATELLAL-QAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALlddt 232
Cdd:cd05944 2 DDVAAYF--HTGGTTGTPKLAQHTHSNEVY--NAWMLALNSLfDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 233 WPSP-----ERVLEN---LVA-FRPRVLFGVPAIYASL--RPQARELlSSVRLAFSAGSPLP---RGEFEfwAAHGLEIC 298
Cdd:cd05944 74 LAGPagyrnPGLFDNfwkLVErYRITSLSTVPTVYAALlqVPVNADI-SSLRFAMSGAAPLPvelRARFE--DATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 DGIGATEVGHVFLANRP-GQARADSTGLPLPGYECRLV--DREGHTIEEAG--RQGVLLVRGPGLSPGYWRASEEQQARF 373
Cdd:cd05944 151 EGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCApdEVGEICVAGPGVFGGYLYTEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 374 AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATpld 453
Cdd:cd05944 231 ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRH-PAVAFAGAVGQPDAHAGELPVAYVQLKP--- 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15596193 454 dNQILLAQRIDQHLAEQIPSH-MLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:cd05944 307 -GAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
42-516 |
9.96e-34 |
|
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: 136.53 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGA--IPavINPKSREQALADIAADCQASLVV-READAPSL 113
Cdd:COG1020 510 RANRLAHHLralgvGPGDLVGVCLERSLEMVVALLAVLKAGAayVP--LDPAYPAERLAYMLEDAGARLVLtQSALAARL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 114 SGPLAPLtlraaagrPLLDDFSLDAlvGPADLDWSAFHRQDPAaacFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELL 193
Cdd:COG1020 588 PELGVPV--------LALDALALAA--EPATNPPVPVTPDDLA---YVIYTSGSTGRPKGVMVEHRALVNLLAWMQ-RRY 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 194 ALQAGDRLYsipkMFFGYGMGNS---LFFPWFSGAS-ALLDDTW-PSPERVLENLVAFRPRVLFGVPAIYASLRPQAREL 268
Cdd:COG1020 654 GLGPGDRVL----QFASLSFDASvweIFGALLSGATlVLAPPEArRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 269 LSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVgHVF-----LANRPGQARADSTGLPLPGYECRLVDREGHT 341
Cdd:COG1020 730 LPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTET-TVDstyyeVTPPDADGGSVPIGRPIANTRVYVLDAHLQP 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 342 IeEAGRQGVLLVRGPGLSPGYWRASEEQQARF-------AGG-WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQ 413
Cdd:COG1020 809 V-PVGVPGELYIGGAGLARGYLNRPELTAERFvadpfgfPGArLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGE 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHlPEVSEAVLVPtcrLHDGLRPTLFVTLATPlDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:COG1020 888 IEAALLQH-PGVREAVVVA---REDAPGDKRLVAYVVP-EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGK 962
|
490 500
....*....|....*....|...
gi 15596193 494 LARAELRHLADTLYHDNLPEERA 516
Cdd:COG1020 963 LDRLALPAPAAAAAAAAAAPPAE 985
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
37-504 |
1.64e-33 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 134.37 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 37 TY--ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVI----NPKSreqaLADIAADCQASLVV 105
Cdd:cd05967 84 TYaeLLDEVSRLAGVLrklgvVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVfggfAAKE----LASRIDDAKPKLIV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 rEADA---PSLSGPLAPL---TLRAAAGRP---LL---DDFSLDALVGPADLDWSAFHRQDPAAAC---------FLQYT 164
Cdd:cd05967 160 -TASCgiePGKVVPYKPLldkALELSGHKPhhvLVlnrPQVPADLTKPGRDLDWSELLAKAEPVDCvpvaatdplYILYT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 165 SGSTGAPKGVmhsLRNTLGFCRAFATE---LLALQAGDRLYSIPKMffGYGMGNSL--FFPWFSGASALL----DDTWPS 235
Cdd:cd05967 239 SGTTGKPKGV---VRDNGGHAVALNWSmrnIYGIKPGDVWWAASDV--GWVVGHSYivYGPLLHGATTVLyegkPVGTPD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 236 PE---RVLENlvaFRPRVLFGVPAIYASLR---PQAREL----LSSVRLAFSAGSPLPRGEFEfWA--AHGLEICDGIGA 303
Cdd:cd05967 314 PGafwRVIEK---YQVNALFTAPTAIRAIRkedPDGKYIkkydLSSLRTLFLAGERLDPPTLE-WAenTLGVPVIDHWWQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 304 TEVGHVFLANRPGQA----RADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPgLSPGY----WRASEEQQARFAG 375
Cdd:cd05967 390 TETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLDEDGEPVG-PNELGNIVIKLP-LPPGClltlWKNDERFKKLYLS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 376 ---GWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHDGLR---PTLFVTLA 449
Cdd:cd05967 468 kfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSH-PAVAECAVVG---VRDELKgqvPLGLVVLK 543
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 450 TPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLAD 504
Cdd:cd05967 544 EGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
43-500 |
4.65e-33 |
|
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: 132.19 E-value: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVV--------------RE 107
Cdd:COG1021 64 AAGLLALgLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIipdrhrgfdyralaRE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 108 --ADAPSLSGPLApltlraaAGRPllDDF-SLDALV-GPADLDWSafhRQDPAAACFLQYTSGSTGAPKGV-------MH 176
Cdd:COG1021 144 lqAEVPSLRHVLV-------VGDA--GEFtSLDALLaAPADLSEP---RPDPDDVAFFQLSGGTTGLPKLIprthddyLY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 177 SLRNTLGFCRafatellaLQAGDR-LYSIPkMFFGYGMGNSLFF-PWFSGASALLDDTwPSPERVLEnLVAfRPRVLFG- 253
Cdd:COG1021 212 SVRASAEICG--------LDADTVyLAALP-AAHNFPLSSPGVLgVLYAGGTVVLAPD-PSPDTAFP-LIE-RERVTVTa 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 254 -VPAIyASL----RPQARELLSSVRLAFSAGSPLPRGefefwAAHGLEicDGIGATeVGHVF-----LAN--RPG---QA 318
Cdd:COG1021 280 lVPPL-ALLwldaAERSRYDLSSLRVLQVGGAKLSPE-----LARRVR--PALGCT-LQQVFgmaegLVNytRLDdpeEV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 319 RADSTGLPL-PGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCG 396
Cdd:COG1021 351 ILTTQGRPIsPDDEVRIVDEDGNPVPP-GEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 397 REDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHD---GLRPTLFVTLatpldDNQILLAQRIDQHLAEQ-IP 472
Cdd:COG1021 430 RAKDQINRGGEKIAAEEVENLLLAH-PAVHDAAVVA---MPDeylGERSCAFVVP-----RGEPLTLAELRRFLRERgLA 500
|
490 500
....*....|....*....|....*...
gi 15596193 473 SHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:COG1021 501 AFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
37-503 |
5.72e-33 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 132.76 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 37 TY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVrEAD 109
Cdd:TIGR02188 90 TYreLHREVCRFANVLKslgvkKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVI-TAD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 110 APSLSGplAPLTLRAAAGRPLLD--------------DFSLDALVGPADLDW-------SAFHRQDPAAA---CFLQYTS 165
Cdd:TIGR02188 169 EGLRGG--KVIPLKAIVDEALEKcpvsvehvlvvrrtGNPVVPWVEGRDVWWhdlmakaSAYCEPEPMDSedpLFILYTS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 166 GSTGAPKGVMHSlrnTLGF-CRAFATE--LLALQAGDRlysipkmFF-----GYGMGNS--LFFPWFSGASALLDD---T 232
Cdd:TIGR02188 247 GSTGKPKGVLHT---TGGYlLYAAMTMkyVFDIKDGDI-------FWctadvGWITGHSyiVYGPLANGATTVMFEgvpT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 233 WPSPERVLENLVAFRPRVLFGVP-AIYASLR-----PQARElLSSVRLAFSAGSPLPRGEFE-FWAAHGLE---ICDGIG 302
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPtAIRALMRlgdewVKKHD-LSSLRLLGSVGEPINPEAWMwYYKVVGKErcpIVDTWW 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVGHVFLANRPG--QARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRG--PGLSPGYWRASEeqqaRF----- 373
Cdd:TIGR02188 396 QTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQpwPGMLRTIYGDHE----RFvdtyf 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 374 --AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcRLHD--GLRPTLFVTL- 448
Cdd:TIGR02188 472 spFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSH-PAVAEAAVVG--IPDDikGQAIYAFVTLk 548
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 449 -ATPLDDNqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:TIGR02188 549 dGYEPDDE---LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIA 601
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
43-499 |
5.73e-33 |
|
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: 130.29 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADapslsgplaplt 121
Cdd:cd05935 15 ASFLSNKgVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 122 lraaagrplLDDFSLdalvgpadldwsafhrqdpaaacfLQYTSGSTGAPKGVMHS----LRNTLGFCRAFAtellaLQA 197
Cdd:cd05935 83 ---------LDDLAL------------------------IPYTSGTTGLPKGCMHThfsaAANALQSAVWTG-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 198 GDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFGVPA----IYASLRPQARELlSSVR 273
Cdd:cd05935 125 SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW-DRETALELIEKYKVTFWTNIPTmlvdLLATPEFKTRDL-SSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 274 LAFSAGSPLPRGEFE-FWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLL 352
Cdd:cd05935 203 VLTGGGAPMPPAVAEkLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 353 VRGPGLSPGYWRASEEQQARFA--GG--WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA 428
Cdd:cd05935 283 VRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH-PAI*EV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 429 VLVPTCRLHDGLRPTLFVTLaTPLDDNQIlLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd05935 362 CVISVPDERVGEEVKAFIVL-RPEYRGKV-TEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-499 |
9.54e-33 |
|
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: 130.71 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 26 RGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLV 104
Cdd:cd05923 25 RGLRLTYSELRARIEAVAARLHARgLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 105 VREADAPSLSGplapltLRAAAGRPLlddfSLDALVGPADL----DWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRN 180
Cdd:cd05923 105 VIAVDAQVMDA------IFQSGVRVL----ALSDLVGLGEPesagPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 181 tlgfcRAFATELLALQAGDRlysipkmffgYGMGNSL-----------FFPWFSGASAlLDDTWP-----SPERVLENLV 244
Cdd:cd05923 175 -----AESRVLFMSTQAGLR----------HGRHNVVlglmplyhvigFFAVLVAALA-LDGTYVvveefDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 245 AFRPRVLFGVPAIYASL---RPQARELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVgHVFLANRpgQARA 320
Cdd:cd05923 239 QERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHlPGEKVNIYGTTEA-MNSLYMR--DART 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 321 DSTGLPLPGYECRLVDREGHTIE--EAGRQGVLLVRGPGLSP--GYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCG 396
Cdd:cd05923 316 GTEMRPGFFSEVRIVRIGGSPDEalANGEEGELIVAAAADAAftGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 397 REDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLatpldDNQILLAQRIDQH-LAEQIPSHM 475
Cdd:cd05923 396 RVDDMIISGGENIHPSEIERVLSRH-PGVTEVVVIGVADERWGQSVTACVVP-----REGTLSADELDQFcRASELADFK 469
|
490 500
....*....|....*....|....
gi 15596193 476 LPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd05923 470 RPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
17-504 |
1.31e-32 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 132.78 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRgqtlsRLQCRTYILSQAsqLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSreqALADIA 96
Cdd:PRK06814 653 DPVNGPLTYR-----KLLTGAFVLGRK--LKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSA---GIANIL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLV--VREADAPSLSGPLAPLTLRAAAGRPL--LDDFSldALVGPAD-----LDWS----AFHRQDPAAACFLQY 163
Cdd:PRK06814 723 SACKAAQVktVLTSRAFIEKARLGPLIEALEFGIRIiyLEDVR--AQIGLADkikglLAGRfplvYFCNRDPDDPAVILF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHSLRNTLGFCrAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLddtWPSP--ERVLE 241
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANR-AQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFL---YPSPlhYRIIP 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 242 NLV-AFRPRVLFGVPAI---YAslRPQARELLSSVRLAFSAGSPLPRGEFEFWA-AHGLEICDGIGATEVGHVFLANRPG 316
Cdd:PRK06814 877 ELIyDTNATILFGTDTFlngYA--RYAHPYDFRSLRYVFAGAEKVKEETRQTWMeKFGIRILEGYGVTETAPVIALNTPM 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 317 QARADSTGLPLPGYECRLVDREGhtIEEAGRqgvLLVRGPGLSPGYWRAS-----EEQqarfAGGWYRTGDLFERDESGA 391
Cdd:PRK06814 955 HNKAGTVGRLLPGIEYRLEPVPG--IDEGGR---LFVRGPNVMLGYLRAEnpgvlEPP----ADGWYDTGDIVTIDEEGF 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 392 YRHCGREDDLFKVNGRWVVPTQVEQAICRHLPE-VSEAVLVPTCRlhDGLRPTLFVTlatpldDNQILLAQRIDQHLAEQ 470
Cdd:PRK06814 1026 ITIKGRAKRFAKIAGEMISLAAVEELAAELWPDaLHAAVSIPDAR--KGERIILLTT------ASDATRAAFLAHAKAAG 1097
|
490 500 510
....*....|....*....|....*....|....
gi 15596193 471 IPSHMLPSQLHVLPALPRNDNGKLARAELRHLAD 504
Cdd:PRK06814 1098 ASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-500 |
4.82e-32 |
|
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: 129.92 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 28 QTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVr 106
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALgVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 107 EADAPSLSGPLAPLT--LRAAA---------------GRPLL----DDFSLDALVGPADLDWSAFHRQDPaaaCFLQYTS 165
Cdd:cd05968 169 TADGFTRRGREVNLKeeADKACaqcptvekvvvvrhlGNDFTpakgRDLSYDEEKETAGDGAERTESEDP---LMIIYTS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 166 GSTGAPKGVMHSlrnTLGFCRAFATEL---LALQAGDRLYSIPKMffGYGMGnslffPWF------SGASALLDDTWP-- 234
Cdd:cd05968 246 GTTGKPKGTVHV---HAGFPLKAAQDMyfqFDLKPGDLLTWFTDL--GWMMG-----PWLifggliLGATMVLYDGAPdh 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 235 -SPERVLENLVAFRPRVLFGVPAIYASLRPQ-----ARELLSSVRLAFSAGSPL-PRGEFEFWAAHGLE---ICDGIGAT 304
Cdd:cd05968 316 pKADRLWRMVEDHEITHLGLSPTLIRALKPRgdapvNAHDLSSLRVLGSTGEPWnPEPWNWLFETVGKGrnpIINYSGGT 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 305 EVGHVFLAN---RPGQARADSTglPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRAS----EEQQARFAGGW 377
Cdd:cd05968 396 EISGGILGNvliKPIKPSSFNG--PVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEdrylETYWSRFDNVW 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 378 YRtGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE--AVLVPtcrlHD--GLRPTLFVTLATPLD 453
Cdd:cd05968 474 VH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAH-PAVLEsaAIGVP----HPvkGEAIVCFVVLKPGVT 547
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15596193 454 DNQIlLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05968 548 PTEA-LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
41-500 |
1.02e-31 |
|
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: 126.66 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVrEADAPslsg 115
Cdd:cd17653 30 AASNALANRLlqlgvVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL-TTDSP---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 plapltlraaagrpllddfsldalvgpadldwsafhrQDPAAACFlqyTSGSTGAPKGVMHSLRNTLGFCrAFATELLAL 195
Cdd:cd17653 105 -------------------------------------DDLAYIIF---TSGSTGIPKGVMVPHRGVLNYV-SQPPARLDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 196 QAGDRLYSIPKMFFGYGMGnSLFFPWFSGASALL---DDTWPSPERVLEnlvafrprVLFGVPAIYASLRPQArelLSSV 272
Cdd:cd17653 144 GPGSRVAQVLSIAFDACIG-EIFSTLCNGGTLVLadpSDPFAHVARTVD--------ALMSTPSILSTLSPQD---FPNL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFEFWAaHGLEICDGIGATE--VGHVFLANRPGQAraDSTGLPLPGYECRLVDREGHTIEEaGRQGV 350
Cdd:cd17653 212 KTIFLGGEAVPPSLLDRWS-PGRRLYNAYGPTEctISSTMTELLPGQP--VTIGKPIPNSTCYILDADLQPVPE-GVVGE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 351 LLVRGPGLSPGYWRASEEQQARFA-----GGW--YRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLP 423
Cdd:cd17653 288 ICISGVQVARGYLGNPALTASKFVpdpfwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQP 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596193 424 EVSEAVLVptcrLHDGlrptLFVTLATPLDDNQILLAQRIDQHLaeqiPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd17653 368 EVTQAAAI----VVNG----RLVAFVTPETVDVDGLRSELAKHL----PSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
155-500 |
1.39e-31 |
|
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: 124.70 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 155 PAAACFLQYTSGSTGAPKGVMHSLRNTL--GFcraFATELLALQAGDRLYSIPKMF--FGYGMGN--SLFFpwfsGASAL 228
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGY---FIGERLGLTEQDRLCIPVPLFhcFGSVLGVlaCLTH----GATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 229 LDDTWPSPERVLENLVAFRPRVLFGVPAIYASL--RP-QARELLSSVRLAFSAGSPLP----RGEFEFWAAHGLEICdgI 301
Cdd:cd05917 74 FPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAEleHPdFDKFDLSSLRTGIMAGAPCPpelmKRVIEVMNMKDVTIA--Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 302 GATEVGHVFLANRPGQA---RADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWrASEEQQARFAG--G 376
Cdd:cd05917 152 GMTETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYW-NDPEKTAEAIDgdG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 377 WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA--VLVP-------TC---RLHDGLRPTl 444
Cdd:cd05917 231 WLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTH-PKVSDVqvVGVPderygeeVCawiRLKEGAELT- 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 445 fvtlatplddnqillAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05917 309 ---------------EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
154-506 |
2.12e-31 |
|
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: 126.50 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 DPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSipkmFFGYGMGNSL---FFPWFSGASALLd 230
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHG-RALGLTSESRVLQ----FASYTFDVSIleiFTTLAAGGCLCI- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 231 dtwPSPERVLENLVAF----RPRVLFGVPAIYASLRPqarELLSSVRLAFSAGSPLPRGEFEFWAaHGLEICDGIGATEV 306
Cdd:cd05918 178 ---PSEEDRLNDLAGFinrlRVTWAFLTPSVARLLDP---EDVPSLRTLVLGGEALTQSDVDTWA-DRVRLINAYGPAEC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 307 G-HVFLANRPGQARADSTGLPLPGyECRLVDREGHTIEEA-GRQGVLLVRGPGLSPGYWRASEEQQARF--AGGW----- 377
Cdd:cd05918 251 TiAATVSPVVPSTDPRNIGRPLGA-TCWVVDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAAFieDPAWlkqeg 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 378 -------YRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLVPTCRLHDGLRPTL--FVTL 448
Cdd:cd05918 330 sgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLvaFVVL 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 449 AT-------------PLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLADTL 506
Cdd:cd05918 410 DGsssgsgdgdslflEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
17-503 |
2.18e-31 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 128.06 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRGQTLSRLQCRTY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSRE 89
Cdd:cd05966 66 RGDKVAIIWEGDEPDQSRTITYreLLREVCRFANVLKslgvkKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 90 QALADIAADCQASLVVrEADAPSLSG---PLAPLTLRAAAGRPLLDDfsldALV-----GPA------DLDWS-AFHRQD 154
Cdd:cd05966 146 ESLADRINDAQCKLVI-TADGGYRGGkviPLKEIVDEALEKCPSVEK----VLVvkrtgGEVpmtegrDLWWHdLMAKQS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 155 PAAAC---------FLQYTSGSTGAPKGVMHSlrnTLGFCRAFATEL---LALQAGDRlysipkmFF-----GYGMGNS- 216
Cdd:cd05966 221 PECEPewmdsedplFILYTSGSTGKPKGVVHT---TGGYLLYAATTFkyvFDYHPDDI-------YWctadiGWITGHSy 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 217 -LFFPWFSGASALLDD---TWPSPERVLENLVAFRPRVLFGVP-AIYASLR----PQARELLSSVRLAFSAGSPL-PRGE 286
Cdd:cd05966 291 iVYGPLANGATTVMFEgtpTYPDPGRYWDIVEKHKVTIFYTAPtAIRALMKfgdeWVKKHDLSSLRVLGSVGEPInPEAW 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 287 FEFWAAHGLE---ICDGIGATEVGHVFLANRPGQA--RADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRG--PGLS 359
Cdd:cd05966 371 MWYYEVIGKErcpIVDTWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAILDEEGNEVE-GEVEGYLVIKRpwPGMA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 360 PGYWRASEeqqaRFA-------GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVP 432
Cdd:cd05966 450 RTIYGDHE----RYEdtyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAH-PAVAEAAVVG 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 433 tcRLHD--GLRPTLFVTL---ATPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:cd05966 525 --RPHDikGEAIYAFVTLkdgEEPSDE----LRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA 594
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
7-500 |
4.07e-31 |
|
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: 126.63 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 7 LTEVLFRLDFDPDTAVYHYRGQTLSRlQCRTY--ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAI 79
Cdd:cd05906 12 LLELLLRAAERGPTKGITYIDADGSE-EFQSYqdLLEDARRLAAGLrqlglRPGDSVILQFDDNEDFIPAFWACVLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 80 PAVINP-------KSREQALADIAADCQASLVVREadaPSLSGPLAPLTlraaAGRPLLDD---FSLDALVGPADLDWsa 149
Cdd:cd05906 91 PAPLTVpptydepNARLRKLRHIWQLLGSPVVLTD---AELVAEFAGLE----TLSGLPGIrvlSIEELLDTAADHDL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 150 fHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSG----- 224
Cdd:cd05906 162 -PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGcqqvh 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 225 --ASALLDDtwpsPERVLENL------VAFRPRVLFGVPAIYASLRPQARELLSSVRLAFSAGSPL-------------P 283
Cdd:cd05906 240 vpTEEILAD----PLRWLDLIdryrvtITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVvaktirrllrlleP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 284 RG--EFEFWAAHGL-EICDGIgatEVGHVFLANRPGQA-RADSTGLPLPGYECRLVDREGhTIEEAGRQGVLLVRGPGLS 359
Cdd:cd05906 316 YGlpPDAIRPAFGMtETCSGV---IYSRSFPTYDHSQAlEFVSLGRPIPGVSMRIVDDEG-QLLPEGEVGRLQVRGPVVT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 360 PGYWRASEEQQARF-AGGWYRTGDL-FERDesGAYRHCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVsEAVLVPTCRLH 437
Cdd:cd05906 392 KGYYNNPEANAEAFtEDGWFRTGDLgFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAV-EEVPGV-EPSFTAAFAVR 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 438 DGLRPT-----LFVTLATPlDDNQILLAQRIDQHLAEQI---PSHMLPSQLHvlpALPRNDNGKLARAELR 500
Cdd:cd05906 468 DPGAETeelaiFFVPEYDL-QDALSETLRAIRSVVSREVgvsPAYLIPLPKE---EIPKTSLGKIQRSKLK 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
39-500 |
5.75e-31 |
|
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: 126.04 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 39 ILSQASQLarllKPGDRVVLALNDSPSLACLFLACIAVGA--IPAVINPKSRE--------QALADIAADCQASLV-VRE 107
Cdd:cd05928 57 VLSGACGL----QRGDRVAVILPRVPEWWLVNVACIRTGLvfIPGTIQLTAKDilyrlqasKAKCIVTSDELAPEVdSVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 108 ADAPSLSGPLapltLRAAAGRPLLDDFSldALVGPADLDWSAFH--RQDPAAACFlqyTSGSTGAPKGVMHSLRNT-LGF 184
Cdd:cd05928 133 SECPSLKTKL----LVSEKSRDGWLNFK--ELLNEASTEHHCVEtgSQEPMAIYF---TSGTTGSPKMAEHSHSSLgLGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 185 cRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTwP--SPERVLENLVAFRPRVLFGVPAIYASLR 262
Cdd:cd05928 204 -KVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHL-PrfDPLVILKTLSSYPITTFCGAPTVYRMLV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 263 PQ--ARELLSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVGhVFLANRPGQA-RADSTGLPLPGYECRLVDRE 338
Cdd:cd05928 282 QQdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQTETG-LICANFKGMKiKPGSMGKASPPYDVQIIDDN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 339 GHTIEEaGRQGVLLVR-GP----GLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQ 413
Cdd:cd05928 361 GNVLPP-GTEGDIGIRvKPirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHlPEVSEAVLVPTcrlHDGLRPTL---FVTLATP-LDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRN 489
Cdd:cd05928 440 VESALIEH-PAVVESAVVSS---PDPIRGEVvkaFVVLAPQfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKT 515
|
490
....*....|.
gi 15596193 490 DNGKLARAELR 500
Cdd:cd05928 516 VTGKIQRNELR 526
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
18-433 |
7.77e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 125.84 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARLL--KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADI 95
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQECgvRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 96 AADCQASLVVREADapsLSGPLAPL----------------TLRAAAGRPLLDDF----SLDALVGPADLDWS----AFH 151
Cdd:PRK08314 104 VTDSGARVAIVGSE---LAPKVAPAvgnlrlrhvivaqysdYLPAEPEIAVPAWLraepPLQALAPGGVVAWKealaAGL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 152 RQDPAAA-----CFLQYTSGSTGAPKGVMHSLR----NTLGFCRAFatellALQAGDRLYSIPKMFFGYGMGNSLFFPWF 222
Cdd:PRK08314 181 APPPHTAgpddlAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWS-----NSTPESVVLAVLPLFHVTGMVHSMNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 223 SGASALLDDTWpspERVLENLVAFRPRVLF--GVPAI----YASLRPQARElLSSVRLAFSAGSPLPRGEFE-FWAAHGL 295
Cdd:PRK08314 256 AGATVVLMPRW---DREAAARLIERYRVTHwtNIPTMvvdfLASPGLAERD-LSSLRYIGGGGAAMPEAVAErLKELTGL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 296 EICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREghTIEE--AGRQGVLLVRGPGLSPGYWRASEEQQARF 373
Cdd:PRK08314 332 DYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPE--TLEElpPGEVGEIVVHGPQVFKGYWNRPEATAEAF 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 374 A--GG--WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPT 433
Cdd:PRK08314 410 IeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH-PAIQEACVIAT 472
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
43-503 |
9.78e-31 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 126.22 E-value: 9.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVrEADAPSLSG---PLA 118
Cdd:PRK10524 98 AAMLRSLgVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV-SADAGSRGGkvvPYK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 119 PL---TLRAAAGRP---LLDDFSLD--ALVGPADLDWSAFHRQ--DPAAAC---------FLQYTSGSTGAPKGVMhslR 179
Cdd:PRK10524 177 PLldeAIALAQHKPrhvLLVDRGLApmARVAGRDVDYATLRAQhlGARVPVewlesnepsYILYTSGTTGKPKGVQ---R 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 180 NTLGFCRAFATE---LLALQAGDRLYSIPKMffGYGMGNS--LFFPWFSGASALLDD---TWPSPErVLENLV-AFRPRV 250
Cdd:PRK10524 254 DTGGYAVALATSmdtIFGGKAGETFFCASDI--GWVVGHSyiVYAPLLAGMATIMYEglpTRPDAG-IWWRIVeKYKVNR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LFGVPAIYASLRPQAREL-----LSSVRLAFSAGSPL--PRGEfefWAAHGLE--ICDGIGATEVGHVFLANRPG----Q 317
Cdd:PRK10524 331 MFSAPTAIRVLKKQDPALlrkhdLSSLRALFLAGEPLdePTAS---WISEALGvpVIDNYWQTETGWPILAIARGvedrP 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 318 ARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPgLSPG---------------YWRASEEQQarfaggwYRTGD 382
Cdd:PRK10524 408 TRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGP-LPPGcmqtvwgdddrfvktYWSLFGRQV-------YSTFD 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 383 LFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHDGLR---PTLFVTLATPL----DDN 455
Cdd:PRK10524 480 WGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSH-PAVAEVAVVG---VKDALKgqvAVAFVVPKDSDsladREA 555
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15596193 456 QILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:PRK10524 556 RLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
17-516 |
1.01e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 125.24 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADI 95
Cdd:PRK06164 23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQgVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 96 AADCQASLVV-----READAPSLSGPLAPLTLRAAAGRPLLDDFSlDALVGPADLDW-------------SAFHRQDPAA 157
Cdd:PRK06164 103 LGRGRARWLVvwpgfKGIDFAAILAAVPPDALPPLRAIAVVDDAA-DATPAPAPGARvqlfalpdpappaAAGERAADPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 158 ACFLQYT-SGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLDDTWPSP 236
Cdd:PRK06164 182 AGALLFTtSGTTSGPKLVLHRQATLLRHARAIA-RAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 237 eRVLENLVAFRPRVLFGVPAIYASL---RPQARELLSSVRLAFSAGSPlPRGEFEFWA-AHGLEICDGIGATEVGHVFLA 312
Cdd:PRK06164 260 -RTARALRRHRVTHTFGNDEMLRRIldtAGERADFPSARLFGFASFAP-ALGELAALArARGVPLTGLYGSSEVQALVAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 313 NR---PGQARADSTGLPL-PGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASE-EQQARFAGGWYRTGDLFERD 387
Cdd:PRK06164 338 QPatdPVSVRIEGGGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDaTARALTDDGYFRTGDLGYTR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCrlHDG-LRPTLFVTlatpLDDNQILLAQRIDQH 466
Cdd:PRK06164 418 GDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL-PGVAAAQVVGAT--RDGkTVPVAFVI----PTDGASPDEAGLMAA 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15596193 467 LAEQIPSHMLPSQLHVLPALPRNDNG---KLARAELRHLADTLyhdnLPEERA 516
Cdd:PRK06164 491 CREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR----LAAERA 539
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
41-499 |
1.78e-30 |
|
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: 123.58 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSlsg 115
Cdd:cd12115 32 RRANRLAARLraagvGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTDPDDLA--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 plapltlraaagrpllddfsldalvgpadldwsafhrqdpaaacFLQYTSGSTGAPKGVMHSLRNTLGFCR----AFATE 191
Cdd:cd12115 109 --------------------------------------------YVIYTSGSTGRPKGVAIEHRNAAAFLQwaaaAFSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 192 LLA--LQAGDRLY--SIPKMFFGYGMGNSLFFpwFSGASALLDDtwPSPERV-LENLVafrprvlfgvPAIYASLRpQAR 266
Cdd:cd12115 145 ELAgvLASTSICFdlSVFELFGPLATGGKVVL--ADNVLALPDL--PAAAEVtLINTV----------PSAAAELL-RHD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 267 ELLSSVRLAFSAGSPLPRGEFE--FWAAHGLEICDGIGATEVG--HVFLANRPGQARADSTGLPLPGYECRLVDREGhTI 342
Cdd:cd12115 210 ALPASVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLDRAL-QP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 343 EEAGRQGVLLVRGPGLSPGYWRASEEQQARF------AGGW-YRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVE 415
Cdd:cd12115 289 VPLGVPGELYIGGAGVARGYLGRPGLTAERFlpdpfgPGARlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 416 QAIcRHLPEVSEAVLVPTcrlHDGLRPTLFVTLATPLDDNQILLAQrIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLA 495
Cdd:cd12115 369 AAL-RSIPGVREAVVVAI---GDAAGERRLVAYIVAEPGAAGLVED-LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKID 443
|
....
gi 15596193 496 RAEL 499
Cdd:cd12115 444 RSAL 447
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
41-500 |
1.84e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 124.86 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 41 SQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQAS------------- 102
Cdd:PRK06087 57 HAASRLANWLlakgiEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKmffaptlfkqtrp 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 103 ----LVVREaDAPSLSG-----PLAPLTLRAAAGRPLLDDFSLDALVgPADLDwsafhrqdpAAACFLqYTSGSTGAPKG 173
Cdd:PRK06087 137 vdliLPLQN-QLPQLQQivgvdKLAPATSSLSLSQIIADYEPLTTAI-TTHGD---------ELAAVL-FTSGTEGLPKG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 174 VMHSLRNTLGFCRAFATElLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPERVLENLVAFRPRVLFG 253
Cdd:PRK06087 205 VMLTHNNILASERAYCAR-LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF-TPDACLALLEQQRCTCMLG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 254 -VPAIYASLR--PQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATE-VGHVFLA-NRPGQARADSTGLPLP 328
Cdd:PRK06087 283 aTPFIYDLLNllEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTEsSPHAVVNlDDPLSRFMHTDGYAAA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 329 GYECRLVDREGHTIeEAGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGR 407
Cdd:PRK06087 363 GVEIKVVDEARKTL-PPGCEGEEASRGPNVFMGYLDEPELtARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 408 WVVPTQVEQAICRHlPEVSEAVLV--PTCRLhdGLRPTLFVTLATPlddNQILLAQRIDQHLAEQ-IPSHMLPSQLHVLP 484
Cdd:PRK06087 442 NISSREVEDILLQH-PKIHDACVVamPDERL--GERSCAYVVLKAP---HHSLTLEEVVAFFSRKrVAKYKYPEHIVVID 515
|
490
....*....|....*.
gi 15596193 485 ALPRNDNGKLARAELR 500
Cdd:PRK06087 516 KLPRTASGKIQKFLLR 531
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
27-432 |
2.05e-30 |
|
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: 124.27 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLA-RLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVV 105
Cdd:cd05904 30 GRALTYAELERRVRRLAAGLAkRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 READ-APSLSGPLAP-LTLRAAAGRPLLDDfSLDALVGPADLDWSAFHRQDPAAacfLQYTSGSTGAPKGVMHSLRNTLg 183
Cdd:cd05904 110 TTAElAEKLASLALPvVLLDSAEFDSLSFS-DLLFEADEAEPPVVVIKQDDVAA---LLYSSGTTGRSKGVMLTHRNLI- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 184 fcrAFATELLALQAGDR------LYSIPkMFFGYGMGNSLFFPWFSGASALLDDTWPSPErVLENLVAFRPRVLFGVPAI 257
Cdd:cd05904 185 ---AMVAQFVAGEGSNSdsedvfLCVLP-MFHIYGLSSFALGLLRLGATVVVMPRFDLEE-LLAAIERYKVTHLPVVPPI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 258 YASLRPQAREL---LSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATE---VGHVFLANRPGQARADSTGLPLPG 329
Cdd:cd05904 260 VLALVKSPIVDkydLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPN 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 330 YECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAG-GWYRTGDLFERDESGAYRHCGREDDLFKVNGRW 408
Cdd:cd05904 340 VEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQ 419
|
410 420
....*....|....*....|....
gi 15596193 409 VVPTQVEQAICRHlPEVSEAVLVP 432
Cdd:cd05904 420 VAPAELEALLLSH-PEILDAAVIP 442
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-503 |
2.05e-30 |
|
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: 123.06 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIpaVInpksreqaladiaadcqaslvvreaDAPSLSGPlAPLTLRAAAGRp 129
Cdd:cd05974 22 VGRGDRILLMLGNVVELWEAMLAAMKLGAV--VI-------------------------PATTLLTP-DDLRDRVDRGG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 130 llddfsldALVGPADldwSAFHRQDPAaacFLQYTSGSTGAPKGVMHSLRnTLGFCRAFATELLALQAGDRLYSIPKMFF 209
Cdd:cd05974 73 --------AVYAAVD---ENTHADDPM---LLYFTSGTTSKPKLVEHTHR-SYPVGHLSTMYWIGLKPGDVHWNISSPGW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 210 GYGMGNSLFFPWFSGASALL-DDTWPSPERVLENLVAFRPRVLFGVPAIY--------ASLRPQARELLSsvrlafsAGS 280
Cdd:cd05974 138 AKHAWSCFFAPWNAGATVFLfNYARFDAKRVLAALVRYGVTTLCAPPTVWrmliqqdlASFDVKLREVVG-------AGE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 281 PL-PRGEFEFWAAHGLEICDGIGATEVGhVFLANRPGQ-ARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGP-G 357
Cdd:cd05974 211 PLnPEVIEQVRRAWGLTIRDGYGQTETT-ALVGNSPGQpVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPvG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 358 LSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTcrlH 437
Cdd:cd05974 290 LMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEH-PAVAEAAVVPS---P 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 438 DGLR---PTLFVTLATPLDDNQiLLAQRIDQHLAEQIPSHMLPSQLHVLpALPRNDNGKLARAELRHLA 503
Cdd:cd05974 366 DPVRlsvPKAFIVLRAGYEPSP-ETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
29-500 |
2.57e-30 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 122.46 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 29 TLSRLQCRTYILsqASQLARLLKP-GDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLvvre 107
Cdd:cd05912 3 TFAELFEEVSRL--AEHLAALGVRkGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 108 adapslsgplapltlraaagrpllddfsldalvgpadldwsafhrqDPAAAcfLQYTSGSTGAPKGVMHSLRNTlgFCRA 187
Cdd:cd05912 77 ----------------------------------------------DDIAT--IMYTSGTTGKPKGVQQTFGNH--WWSA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 188 FATEL-LALQAGDRLYSIPKMFFGYG---MGNSLFFpwfsGASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASLRP 263
Cdd:cd05912 107 IGSALnLGLTEDDNWLCALPLFHISGlsiLMRSVIY----GMTVYLVDKF-DAEQVLHLINSGKVTIISVVPTMLQRLLE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 264 QARELLS-SVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQA--RADSTGLPLPGYECRLVDREGh 340
Cdd:cd05912 182 ILGEGYPnNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDDGQ- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 341 tieEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICR 420
Cdd:cd05912 261 ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 421 HlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILlaqridQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05912 338 H-PAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELI------AYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
18-500 |
2.32e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 121.42 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIA 96
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRgVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLVVREAdapslsgPLAPLTLRAAAGRPLLD------DFSLDALVGPADLDWSAFHRQDPA-----AACFLQYTS 165
Cdd:PRK07786 111 SDCGAHVVVTEA-------ALAPVATAVRDIVPLLStvvvagGSSDDSVLGYEDLLAEAGPAHAPVdipndSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 166 GSTGAPKGVMHSLRNTLGFcrafATELLALQAGDR-----LYSIPkMFFGYGMGNSLFFPWFSGASALLDDTWPSPERVL 240
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQ----AMTCLRTNGADInsdvgFVGVP-LFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 241 ENLVAFRPRVLFGVP----AIYASLRPQARELlsSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVGHV--FLA 312
Cdd:PRK07786 259 DVLEAEKVTGIFLVPaqwqAVCAEQQARPRDL--ALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVtcMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 313 NRPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAY 392
Cdd:PRK07786 337 GEDAIRKLGSVGKVIPTVAARVVDENMNDVP-VGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 393 RHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcRLHD--GLRPtlfVTLATPLDDNQILLAQRIDQHLAEQ 470
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASH-PDIVEVAVIG--RADEkwGEVP---VAVAAVRNDDAALTLEDLAEFLTDR 489
|
490 500 510
....*....|....*....|....*....|
gi 15596193 471 IPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
161-496 |
5.52e-29 |
|
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: 116.83 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMF--FGYGMGnsLFFPWFSGASALLDDTWpSPER 238
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWA-DCADLTEDDRYLIINPFFhtFGYKAG--IVACLLTGATVVPVAVF-DVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 239 VLENLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLP-------RGEFEFWAahgleICDGIGATEVGH 308
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLldHPGRKKFdLSSLRAAVTGAATVPvelvrrmRSELGFET-----VLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 309 VFLAnRPG---QARADSTGLPLPGYECRLVDreghtieeagrQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLF 384
Cdd:cd17638 156 ATMC-RPGddaETVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 385 ERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA--VLVPTCRLhdGLRPTLFVTLATP--LDDNQILLA 460
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEH-PGVAQVavIGVPDERM--GEVGKAFVVARPGvtLTEEDVIAW 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 15596193 461 QRidqhlaEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd17638 301 CR------ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
161-421 |
6.86e-29 |
|
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: 119.88 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVMHSLrNTLGFCRAFATELLALQAGDRLYS-IP------KMFFGYGM---GNSLFFpwfsgASALld 230
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTF-GSFAWAAQAGIEHIGTEENDRMLSyLPlahvteRVFVEGGSlygGVLVAF-----AESL-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 231 DTWPspervlENLVAFRPRVLFGVP--------AIYASLRPQAREL--------------------LSSVRLAFSAGSPL 282
Cdd:cd05932 214 DTFV------EDVQRARPTLFFSVPrlwtkfqqGVQDKIPQQKLNLllkipvvnslvkrkvlkglgLDQCRLAGCGSAPV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 283 PRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDreghtieeagrQGVLLVRGPGLSPGY 362
Cdd:cd05932 288 PPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGY 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 363 WRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVN-GRWVVPTQVEQAICRH 421
Cdd:cd05932 357 YKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEH 417
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
43-499 |
1.72e-28 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 117.74 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSlsgpl 117
Cdd:cd17652 22 ANRLARLLaargvGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTPDNLA----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 118 apltlraaagrpllddfsldalvgpadldwsafhrqdpaaacFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQA 197
Cdd:cd17652 97 ------------------------------------------YVIYTSGSTGRPKGVVVTHRGLANLAAA-QIAAFDVGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 198 GDRLYSipkmFFGYGMGNS---LFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQArelLSSV 272
Cdd:cd17652 134 GSRVLQ----FASPSFDASvweLLMALLAGATLVLapAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD---LPDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFEFWAAhGLEICDGIGATEVGHVFLANRPGQARADST-GLPLPGYECRLVDREGHTIEeAGRQGVL 351
Cdd:cd17652 207 RTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLPGGGVPPiGRPVPGTRVYVLDARLRPVP-PGVPGEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 352 LVRGPGLSPGYWRASEEQQARF--------AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlP 423
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFvadpfgapGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH-P 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 424 EVSEAVLVPTcrlHDGLRPTLFVTLATPLDDNQiLLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17652 364 GVAEAVVVVR---DDRPGDKRLVAYVVPAPGAA-PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
18-499 |
2.99e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.21 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIA 96
Cdd:PRK06710 38 PEKKALHFLGKDITFSVFHDKVKRFANYLQKLgVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLVV-------READAPSLSGPLAPLTLRAAAGRP----LLDDF------SLDALVGPADLD--WSAFHRQ---- 153
Cdd:PRK06710 118 HDSGAKVILcldlvfpRVTNVQSATKIEHVIVTRIADFLPfpknLLYPFvqkkqsNLVVKVSESETIhlWNSVEKEvntg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 -----DPAA-ACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRL-YSIPKMFFGYGMGNSLFFPWFSGAS 226
Cdd:PRK06710 198 vevpcDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVvLGVLPFFHVYGMTAVMNLSIMQGYK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 227 ALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLP-RGEFEFWAAHGLEICDGIG 302
Cdd:PRK06710 278 MVLIPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALlnSPLLKEYdISSIRACISGSAPLPvEVQEKFETVTGGKLVEGYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVGHVFLANRPGQARA-DSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTG 381
Cdd:PRK06710 357 LTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 382 DLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTlatpLDDNQILLAQ 461
Cdd:PRK06710 437 DVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH-EKVQEVVTIGVPDPYRGETVKAFVV----LKEGTECSEE 511
|
490 500 510
....*....|....*....|....*....|....*...
gi 15596193 462 RIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK06710 512 ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-499 |
4.40e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.50 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADapslsgp 116
Cdd:PRK12467 546 QANRLAHVLIaagvgPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH------- 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 LAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAfhRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQ 196
Cdd:PRK12467 619 LLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEV--ALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA-ERLQLA 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 197 AGDRLYSIPKMFFGYGmGNSLFFPWFSGASALL---DDTWpSPERVLENLVAFRPRVLFGVPAIYASLRPQAR-ELLSSV 272
Cdd:PRK12467 696 ADDSMLMVSTFAFDLG-VTELFGALASGATLHLlppDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRvALPRPQ 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFEFW--AAHGLEICDGIGATE----VGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEeAG 346
Cdd:PRK12467 774 RALVCGGEALQVDLLARVraLGPGARLINHYGPTEttvgVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP-VG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 347 RQGVLLVRGPGLSPGYWRASEEQQARF-------AGG-WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEqAI 418
Cdd:PRK12467 853 VVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE-AR 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 419 CRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAE 498
Cdd:PRK12467 932 LLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKA 1011
|
.
gi 15596193 499 L 499
Cdd:PRK12467 1012 L 1012
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
50-433 |
4.56e-28 |
|
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: 116.77 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVvreadapslsgplapltlraaagrp 129
Cdd:cd05914 29 VGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 130 llddFSLDalvgpadldwsafhRQDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRaFATELLALQAGDRLYSIPKMFF 209
Cdd:cd05914 84 ----FVSD--------------EDDVAL---INYTSGTTGNSKGVMLTYRNIVSNVD-GVKEVVLLGKGDKILSILPLHH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 210 GYGMGNSLFFPWFSGASALLDDTWPSP-------ERVLENLVAFRPRVLF--------------------GVPAIYASLR 262
Cdd:cd05914 142 IYPLTFTLLLPLLNGAHVVFLDKIPSAkiialafAQVTPTLGVPVPLVIEkifkmdiipkltlkkfkfklAKKINNRKIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 263 PQARELLS-----SVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDR 337
Cdd:cd05914 222 KLAFKKVHeafggNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 338 EGHTIEeagrqGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKV-NGRWVVPTQVE 415
Cdd:cd05914 302 DPATGE-----GEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIE 376
|
410
....*....|....*...
gi 15596193 416 qAICRHLPEVSEAVLVPT 433
Cdd:cd05914 377 -AKINNMPFVLESLVVVQ 393
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
14-504 |
1.54e-27 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 116.73 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 14 LDFDPDTavyhYRGQTlsrlqcrTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL- 92
Cdd:PRK08043 227 VNFTPDS----YRKLL-------KKTLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLt 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 -ADIAADCQASLVVREADApslSGPLAPLTLRAAAGRPL-LDDfsLDALVGPADLDWSAFH---------RQDPAAACFL 161
Cdd:PRK08043 296 sAITAAEIKTIFTSRQFLD---KGKLWHLPEQLTQVRWVyLED--LKDDVTTADKLWIFAHllmprlaqvKQQPEDAALI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 162 QYTSGSTGAPKGVMHSLRNTLGFCRAFATeLLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLddtWPSP--ERV 239
Cdd:PRK08043 371 LFTSGSEGHPKGVVHSHKSLLANVEQIKT-IADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL---YPSPlhYRI 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 240 LENLVAFRP-RVLFGV------------PAIYASLR---PQARELLSSVRlafsagsplprgefEFWA-AHGLEICDGIG 302
Cdd:PRK08043 447 VPELVYDRNcTVLFGTstflgnyarfanPYDFARLRyvvAGAEKLQESTK--------------QLWQdKFGLRILEGYG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGhtIEEAGRqgvLLVRGPGLSPGYWR----------ASEEQQAR 372
Cdd:PRK08043 513 VTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG--IEQGGR---LQLKGPNIMNGYLRvekpgvlevpTAENARGE 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 373 FAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLVPTcrlhDGLRPTLFVTLATpl 452
Cdd:PRK08043 588 MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKS----DASKGEALVLFTT-- 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15596193 453 dDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLAD 504
Cdd:PRK08043 662 -DSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVD 712
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
163-431 |
5.20e-27 |
|
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: 113.61 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 163 YTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGYGMGNSLFFpwFS-GASalldDTWPSPERVLE 241
Cdd:cd17640 95 YTSGTTGNPKGVMLTHANLLHQIRSLS-DIVPPQPGDRFLSILPIWHSYERSAEYFI--FAcGCS----QAYTSIRTLKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 242 NLVAFRPRVLFGVPAIYASLR----------PQARELL-------SSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGAT 304
Cdd:cd17640 168 DLKRVKPHYIVSVPRLWESLYsgiqkqvsksSPIKQFLflfflsgGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 305 EVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDL 383
Cdd:cd17640 248 ETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEAtSKVLDSDGWFNTGDL 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15596193 384 FERDESGAYRHCGREDDLFKV-NGRWVVPTQVEQAICRHlPEVSEAVLV 431
Cdd:cd17640 328 GWLTCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMRS-PFIEQIMVV 375
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
17-427 |
5.76e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.48 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRGQTLSRLQcrtyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP--KSRE 89
Cdd:PRK12583 33 DREALVVRHQALRYTWRQ----LADAVDRLARGLlalgvQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPayRASE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 90 QALADIAADCQASLVV---READAPSLSGPLAPLTLRAAAGRPLLDDF-------SLDALVGPADLDW------------ 147
Cdd:PRK12583 109 LEYALGQSGVRWVICAdafKTSDYHAMLQELLPGLAEGQPGALACERLpelrgvvSLAPAPPPGFLAWhelqargetvsr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 148 -------SAFHRQDPAAacfLQYTSGSTGAPKGVMHSLRNTLGFCRaFATELLALQAGDRLYSIPKMFFGYGMGNSLFFP 220
Cdd:PRK12583 189 ealaerqASLDRDDPIN---IQYTSGTTGFPKGATLSHHNILNNGY-FVAESLGLTEHDRLCVPVPLYHCFGMVLANLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 221 WFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIY-ASL-RPQAREL-LSSVRLAFSAGSPLPR-------GEFefw 290
Cdd:PRK12583 265 MTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFiAELdHPQRGNFdLSSLRTGIMAGAPCPIevmrrvmDEM--- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 291 aaHGLEICDGIGATE---VGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASE 367
Cdd:PRK12583 342 --HMAEVQIAYGMTEtspVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPR-GEIGELCTRGYSVMKGYWNNPE 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 368 E-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE 427
Cdd:PRK12583 419 AtAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTH-PAVAD 478
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
27-511 |
6.44e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 114.17 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLARL--LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLV 104
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVmgVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 105 VREADA----PSLSGP--LAPLTLRAAAGRPLLDDF----SLDALVGPADLDwsafhRQDPAAAcfLQYTSGSTGAPKGV 174
Cdd:PLN02574 144 FTSPENveklSPLGVPviGVPENYDFDSKRIEFPKFyeliKEDFDFVPKPVI-----KQDDVAA--IMYSSGTTGASKGV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 175 MHSLRNTLG----FCRaFATELLALQAGDRLY-SIPKMFFGYGMgnSLF-FPWFSGASALLDDTWPSPERVLENLVAFRP 248
Cdd:PLN02574 217 VLTHRNLIAmvelFVR-FEASQYEYPGSDNVYlAALPMFHIYGL--SLFvVGLLSLGSTIVVMRRFDASDMVKVIDRFKV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 249 RVLFGVPAIYASL----RPQARELLSSVRLAFSAGSPLPRG---EFEFWAAHgLEICDGIGATEVGHVFLA--NRPGQAR 319
Cdd:PLN02574 294 THFPVVPPILMALtkkaKGVCGEVLKSLKQVSCGAAPLSGKfiqDFVQTLPH-VDFIQGYGMTESTAVGTRgfNTEKLSK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 320 ADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGRE 398
Cdd:PLN02574 373 YSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 399 DDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTL--ATPLDDNQILlaqridQHLAEQIPSHML 476
Cdd:PLN02574 453 KEIIKYKGFQIAPADLEAVLISH-PEIIDAAVTAVPDKECGEIPVAFVVRrqGSTLSQEAVI------NYVAKQVAPYKK 525
|
490 500 510
....*....|....*....|....*....|....*
gi 15596193 477 PSQLHVLPALPRNDNGKLARAELRHLADTLYHDNL 511
Cdd:PLN02574 526 VRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
53-504 |
6.01e-26 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 111.41 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 53 GDRV-VLALNDSPSLACLFlaciAVGAIPAVINPKSREqaLAD--------------IAADCQAS--LVVREADAPSLSG 115
Cdd:PRK05620 64 DQRVgSMMYNCAEHLEVLF----AVACMGAVFNPLNKQ--LMNdqivhiinhaedevIVADPRLAeqLGEILKECPCVRA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 PL----APLTLRAAAGRPLLDDFSLDALVG--PADLDWSAFHRQDPAAACflqYTSGSTGAPKGVMHSLRNTLGFCRAF- 188
Cdd:PRK05620 138 VVfigpSDADSAAAHMPEGIKVYSYEALLDgrSTVYDWPELDETTAAAIC---YSTGTTGAPKGVVYSHRSLYLQSLSLr 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 189 ATELLALQAGDR-LYSIP-KMFFGYGMGnslFFPWFSGASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASL----- 261
Cdd:PRK05620 215 TTDSLAVTHGESfLCCVPiYHVLSWGVP---LAAFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLmvhyl 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 262 -RPQARellSSVRLAFSAGSPLPRGEFEFWAA-HGLEICDGIGATEVGHVFLANRP-----GQARAD---STGLPLPGYE 331
Cdd:PRK05620 292 kNPPER---MSLQEIYVGGSAVPPILIKAWEErYGVDVVHVWGMTETSPVGTVARPpsgvsGEARWAyrvSQGRFPASLE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 332 CRLVDrEGHTIEEAGR-QGVLLVRGPGLSPGYW----------------RASEEQQARF-AGGWYRTGDLFERDESGAYR 393
Cdd:PRK05620 369 YRIVN-DGQVMESTDRnEGEIQVRGNWVTASYYhspteegggaastfrgEDVEDANDRFtADGWLRTGDVGSVTRDGFLT 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPtLFVTLATPLDDNQILLAQRIDQHLAEQIPS 473
Cdd:PRK05620 448 IHDRARDVIRSGGEWIYSAQLENYIMAA-PEVVECAVIGYPDDKWGERP-LAVTVLAPGIEPTRETAERLRDQLRDRLPN 525
|
490 500 510
....*....|....*....|....*....|..
gi 15596193 474 HMLPSQLHVLPALPRNDNGKLARAELR-HLAD 504
Cdd:PRK05620 526 WMLPEYWTFVDEIDKTSVGKFDKKDLRqHLAD 557
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-499 |
7.65e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.74 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 34 QCRTY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVR 106
Cdd:PRK12316 2027 QHLSYaeLDSRANRLAHRLRargvgPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 107 EadapslSGPLAPLTLRAAAGRPLLDDfsldalvgpaDLDWSAFHRQDPAAA------CFLQYTSGSTGAPKGVMHSLRN 180
Cdd:PRK12316 2107 Q------RHLLERLPLPAGVARLPLDR----------DAEWADYPDTAPAVQlagenlAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 181 TLGFCRAfATELLALQAGDRlySIPKMFFGY-GMGNSLFFPWFSGASALL-DDTWPSPERVLENLVafRPRVLFGV-PAI 257
Cdd:PRK12316 2171 LVAHCQA-AGERYELSPADC--ELQFMSFSFdGAHEQWFHPLLNGARVLIrDDELWDPEQLYDEME--RHGVTILDfPPV 2245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 258 YasLRPQAREL-----LSSVRLAFSAGSPLPRGEFEFWAA--HGLEICDGIGATEVGHVFLANRPGqaRADSTGLPLPGY 330
Cdd:PRK12316 2246 Y--LQQLAEHAerdgrPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVVTPLLWKCR--PQDPCGAAYVPI 2321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 331 ECRLVDREGHTIEEA------GRQGVLLVRGPGLSPGYWRASEEQQARF--------AGGWYRTGDLFERDESGAYRHCG 396
Cdd:PRK12316 2322 GRALGNRRAYILDADlnllapGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsasGERLYRTGDLARYRADGVVEYLG 2401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 397 REDDLFKVNGRWVVPTQVEqAICRHLPEVSEAVLVPtcrlHDGLRPTLFVTLATPlDDNQILLAQRIDQHLAEQIPSHML 476
Cdd:PRK12316 2402 RIDHQVKIRGFRIELGEIE-ARLQAHPAVREAVVVA----QDGASGKQLVAYVVP-DDAAEDLLAELRAWLAARLPAYMV 2475
|
490 500
....*....|....*....|...
gi 15596193 477 PSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK12316 2476 PAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
160-500 |
1.73e-25 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 110.14 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 FLQYTSGSTGAPKGVMHSLRNTLG-FCRAFATELLALQAGDR-------LYSIpkmfFGYGMgNSLFFPWFSGASALLDD 231
Cdd:PRK08974 210 FLQYTGGTTGVAKGAMLTHRNMLAnLEQAKAAYGPLLHPGKElvvtalpLYHI----FALTV-NCLLFIELGGQNLLITN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 232 TWPSPERVLEnLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFWAAH-GLEICDGIGATEVG 307
Cdd:PRK08974 285 PRDIPGFVKE-LKKYPFTAITGVNTLFNALlnNEEFQELdFSSLKLSVGGGMAVQQAVAERWVKLtGQYLLEGYGLTECS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 308 HVFLANRPGQARAD-STGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFER 386
Cdd:PRK08974 364 PLVSVNPYDLDYYSgSIGLPVPSTEIKLVDDDGNEVPP-GEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVM 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 387 DESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE--AVLVPtcrlHD--GLRPTLFVTLATPlddnqILLAQR 462
Cdd:PRK08974 443 DEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLH-PKVLEvaAVGVP----SEvsGEAVKIFVVKKDP-----SLTEEE 512
|
330 340 350
....*....|....*....|....*....|....*...
gi 15596193 463 IDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK08974 513 LITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
161-500 |
2.39e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 109.47 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVMHSLRNTLGF---CRAFATELL-----ALQAGDRLYSIPKMFFgygmgNSLFFPWFSGASALLDDT 232
Cdd:PRK05677 212 LQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLnegceILIAPLPLYHIYAFTF-----HCMAMMLIGNHNILISNP 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 233 WPSPERVLEnLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFW-AAHGLEICDGIGATEVGH 308
Cdd:PRK05677 287 RDLPAMVKE-LGKWKFSGFVGLNTLFVALcnNEAFRKLdFSALKLTLSGGMALQLATAERWkEVTGCAICEGYGMTETSP 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 309 VFLANRPGQARADSTGLPLPGYECRLVDREGHTIeEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERD 387
Cdd:PRK05677 366 VVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNEL-PLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQ 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE--AVLVPTCRLHDGLRptLFVTLATplddNQILLAQRIDQ 465
Cdd:PRK05677 445 EDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL-PGVLQcaAIGVPDEKSGEAIK--VFVVVKP----GETLTKEQVME 517
|
330 340 350
....*....|....*....|....*....|....*
gi 15596193 466 HLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK05677 518 HMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-500 |
2.60e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 109.39 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 1 MSTLANLTEVLFRLDFDPDTAVyHYRGQTLSRlqcRTYILSQASQLARLLKPGDR-----VVLALNDSPSLACLFLACIA 75
Cdd:PRK07867 1 TSSAPTVAELLLPLAEDDDRGL-YFEDSFTSW---REHIRGSAARAAALRARLDPtrpphVGVLLDNTPEFSLLLGAAAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 76 VGAIPAVINPKSREQALA-DIA-ADCQasLVVREADAPSLSGPLAPltlraaaGRPLLDDFSL---DALVGPADLDWSaF 150
Cdd:PRK07867 77 SGIVPVGLNPTRRGAALArDIAhADCQ--LVLTESAHAELLDGLDP-------GVRVINVDSPawaDELAAHRDAEPP-F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 151 HRQDPAAACFLQYTSGSTGAPKGVMHSLRnTLGFCRAFATELLALQAGDRLY-SIPkMFFGygmgNSLFFPW-------- 221
Cdd:PRK07867 147 RVADPDDLFMLIFTSGTSGDPKAVRCTHR-KVASAGVMLAQRFGLGPDDVCYvSMP-LFHS----NAVMAGWavalaaga 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 222 -------FSgASALLDDtwpsperVLENLVAFRPRVlfGVPAIY---ASLRPQAREllSSVRLAF-SAGSPLPRGEFEfw 290
Cdd:PRK07867 221 sialrrkFS-ASGFLPD-------VRRYGATYANYV--GKPLSYvlaTPERPDDAD--NPLRIVYgNEGAPGDIARFA-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 291 AAHGLEICDGIGATEvGHVFLANRPGqARADSTGLPLPGYEcrLVDREGHT------IEEAGRQ------GVLL-VRGPG 357
Cdd:PRK07867 287 RRFGCVVVDGFGSTE-GGVAITRTPD-TPPGALGPLPPGVA--IVDPDTGTecppaeDADGRLLnadeaiGELVnTAGPG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 358 LSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLH 437
Cdd:PRK07867 363 GFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY-PDATEVAVYAVPDPV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 438 DGLRptlfVTLATPLDDNQILLAQRIDQHLAEQ--IPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07867 442 VGDQ----VMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
153-496 |
2.91e-25 |
|
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: 106.58 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 153 QDPAAACFlqyTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDT 232
Cdd:cd17635 1 EDPLAVIF---TSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 233 wPSPERVLENLVAFRPRVLFGVPAIYASLRPQARELLS---SVRLAFSAGSPLPRGEFEFWAAHGL-EICDGIGATEVGH 308
Cdd:cd17635 78 -TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANAtvpSLRLIGYGGSRAIAADVRFIEATGLtNTAQVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 309 V-FLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGrQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERD 387
Cdd:cd17635 157 AlCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSAS-FGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQaICRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQIllaQRIDQHL 467
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVER-IAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAI---RALKHTI 311
|
330 340
....*....|....*....|....*....
gi 15596193 468 AEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd17635 312 RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-499 |
8.29e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.28 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQcrtyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:PRK12316 4565 PDAVAVVFDEEKLTYAE----LNRRANRLAHALiargvGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERL 4640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVVREAdapslsgplapltlRAAAGRPLLDdfSLDALVGPADLDWSAFHRQDPAAA------CFLQYTSG 166
Cdd:PRK12316 4641 AYMMEDSGAALLLTQS--------------HLLQRLPIPD--GLASLALDRDEDWEGFPAHDPAVRlhpdnlAYVIYTSG 4704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 167 STGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLysIPKMFFGY-GMGNSLFFPWFSGASALL-DDTWPSPERVLENLV 244
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVNHLHATG-ERYELTPDDRV--LQFMSFSFdGSHEGLYHPLINGASVVIrDDSLWDPERLYAEIH 4781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 245 AFRPRVLFGVPAIYASLRPQAREL--LSSVRLAFSAGSPLPRGEFEFW--AAHGLEICDGIGATE--VGHVFLANRPGQA 318
Cdd:PRK12316 4782 EHRVTVLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTEttVTVLLWKARDGDA 4861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 319 RADST---GLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARF--------AGGWYRTGDLFERD 387
Cdd:PRK12316 4862 CGAAYmpiGTPLGNRSGYVLDGQLNPLP-VGVAGELYLGGEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYR 4940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrlHDGLRPTLFVTLATPLD-------DNQILLA 460
Cdd:PRK12316 4941 ADGVIDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVREAVVIA----QEGAVGKQLVGYVVPQDpaladadEAQAELR 5015
|
490 500 510
....*....|....*....|....*....|....*....
gi 15596193 461 QRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK12316 5016 DELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-500 |
8.61e-25 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.92 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 29 TLSRLQCRTYILSQAsqLARL-LKPGDRV-VLALNDSPSLACLFlACIAVGAIPAVINPKSREQALADIAADCQASLV-- 104
Cdd:PRK06018 41 TYAQIHDRALKVSQA--LDRDgIKLGDRVaTIAWNTWRHLEAWY-GIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVit 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 105 ------VREADAPSLSGPLAPLTLRAAAGRP---LLDDFSLDALVGPADLD--WSAFhrqDPAAACFLQYTSGSTGAPKG 173
Cdd:PRK06018 118 dltfvpILEKIADKLPSVERYVVLTDAAHMPqttLKNAVAYEEWIAEADGDfaWKTF---DENTAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 174 VMHSLR-NTLGFCRAFATELLALQAGDRLYSIPKMFF---------GYGMGNSLFFPW--FSGASA--LLDDtwpspERV 239
Cdd:PRK06018 195 VLYSHRsNVLHALMANNGDALGTSAADTMLPVVPLFHanswgiafsAPSMGTKLVMPGakLDGASVyeLLDT-----EKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 240 leNLVAfrprvlfGVPAIYASLRPQARE---LLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATE---VGHVF--- 310
Cdd:PRK06018 270 --TFTA-------GVPTVWLMLLQYMEKeglKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEmspLGTLAalk 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 311 --LANRPGQARAD---STGLPLPGYECRLVDREGHTIEEAGRQ-GVLLVRGPGLSPGYWRASEEQQArfAGGWYRTGDLF 384
Cdd:PRK06018 341 ppFSKLPGDARLDvlqKQGYPPFGVEMKITDDAGKELPWDGKTfGRLKVRGPAVAAAYYRVDGEILD--DDGFFDTGDVA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 385 ERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRID 464
Cdd:PRK06018 419 TIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGH-PKVAEAAVIGVYHPKWDERPLLIVQLK----PGETATREEIL 493
|
490 500 510
....*....|....*....|....*....|....*.
gi 15596193 465 QHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
23-516 |
9.20e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 107.78 E-value: 9.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 23 YHYRGQTLSRLQCRTyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVI----NPKSRE---Q 90
Cdd:PRK09192 40 YDRRGQLEEALPYQT-LRARAEAGARRLlalglKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLplpmGFGGREsyiA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREADapslsgpLAPLTLRAAAGRPLLDDFSLDALVGPADLDwSAFHRQDPAAACFLQYTSGSTGA 170
Cdd:PRK09192 119 QLRGMLASAQPAAIITPDE-------LLPWVNEATHGNPLLHVLSHAWFKALPEAD-VALPRPTPDDIAYLQYSSGSTRF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 171 PKGVMHSLRNTLGFCRAFATELLALQAGDRLYS-IPkmfFGYGMGNSLFF--PWFSGASALLDDTWPSPERVLENL---- 243
Cdd:PRK09192 191 PRGVIITHRALMANLRAISHDGLKVRPGDRCVSwLP---FYHDMGLVGFLltPVATQLSVDYLPTRDFARRPLQWLdlis 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 244 -----VAFRPRVLFGVPAIYASLRPQARELLSSVRLAFSAGSPL-------------PRG--EFEFWAAHGL-------- 295
Cdd:PRK09192 268 rnrgtISYSPPFGYELCARRVNSKDLAELDLSCWRVAGIGADMIrpdvlhqfaeafaPAGfdDKAFMPSYGLaeatlavs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 296 --EICDGIGATEV--------GH-VFLANRPGQARA-DSTGLPLPGYECRLVDREGHTIEEagRQ-GVLLVRGPGLSPGY 362
Cdd:PRK09192 348 fsPLGSGIVVEEVdrdrleyqGKaVAPGAETRRVRTfVNCGKALPGHEIEIRNEAGMPLPE--RVvGHICVRGPSLMSGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 363 WRASEEQQARFAGGWYRTGDLFERDESGAYRhCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSE----AVLVPTcrlHD 438
Cdd:PRK09192 426 FRDEESQDVLAADGWLDTGDLGYLLDGYLYI-TGRAKDLIIINGRNIWPQDIEWIA-EQEPELRSgdaaAFSIAQ---EN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 439 GLRPTLFVTLATPLDDNQILLAQRIDQHLAEQipsHMLPSQLHVLP--ALPRNDNGKLARAELR--HLADTLYHDNLPEE 514
Cdd:PRK09192 501 GEKIVLLVQCRISDEERRGQLIHALAALVRSE---FGVEAAVELVPphSLPRTSSGKLSRAKAKkrYLSGAFASLDVAAS 577
|
..
gi 15596193 515 RA 516
Cdd:PRK09192 578 LA 579
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
23-469 |
1.06e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 107.68 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 23 YHYRGQTLSRLqcrtyiLSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP----KSREQALA 93
Cdd:PRK09274 37 LAYDELSFAEL------DARSDAIAHGLnaagiGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPgmgiKNLKQCLA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 94 DIAADcqASLVVREADAPSLSGPLAPLTLRA--AAGRPL------LDDFSLDALVGPADLDWSAfhRQDPAAACFlqyTS 165
Cdd:PRK09274 111 EAQPD--AFIGIPKAHLARRLFGWGKPSVRRlvTVGGRLlwggttLATLLRDGAAAPFPMADLA--PDDMAAILF---TS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 166 GSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDR-LYSIPKMffgygmgnSLFFPWFSGASAL--LDDTWPS---PERV 239
Cdd:PRK09274 184 GSTGTPKGVVYTHGMFEAQIEA-LREDYGIEPGEIdLPTFPLF--------ALFGPALGMTSVIpdMDPTRPAtvdPAKL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 240 LENLVAFRPRVLFGVPAIyasLRPQAREL------LSSVRLAFSAGSPLPRG---EFEFWAAHGLEICDGIGATEV---- 306
Cdd:PRK09274 255 FAAIERYGVTNLFGSPAL---LERLGRYGeangikLPSLRRVISAGAPVPIAvieRFRAMLPPDAEILTPYGATEAlpis 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 307 ----GHVFLANRPGQARADST--GLPLPGYECRLV---DREGHTIEE-----AGRQGVLLVRGPGLSPGY-WRASEEQQA 371
Cdd:PRK09274 332 siesREILFATRAATDNGAGIcvGRPVDGVEVRIIaisDAPIPEWDDalrlaTGEIGEIVVAGPMVTRSYyNRPEATRLA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 372 RFAGG----WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEqAICRHLPEV--SEAVLVPTcrlHDGLRPTLF 445
Cdd:PRK09274 412 KIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVkrSALVGVGV---PGAQRPVLC 487
|
490 500
....*....|....*....|....
gi 15596193 446 VTLATPLDDNQILLAQRIDQHLAE 469
Cdd:PRK09274 488 VELEPGVACSKSALYQELRALAAA 511
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
163-496 |
1.14e-24 |
|
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: 104.66 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 163 YTSGSTGAPKGVMHSLRNTLgfCRAFATEL-LALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDTwpSPERVLE 241
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLI--AANLQLIHaMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKF--DPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 242 NLVAFRPRVLFGVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGEFE------FWAahgleicdGIGATEV-GHVFL 311
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLLDAAEKSgvdLSSLRHVLGLDAPETIQRFEettgatFWS--------LYGQTETsGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 312 A---NRPGqaradSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDE 388
Cdd:cd17637 155 SpyrERPG-----SAGRPGPLVRVRIVDDNDRPVP-AGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 389 SGAYRHCGR--EDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL--VP----------TCRLHDGLRPTlfvtlatpldd 454
Cdd:cd17637 229 DGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEH-PAIAEVCVigVPdpkwgegikaVCVLKPGATLT----------- 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15596193 455 nqillAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd17637 297 -----ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
13-502 |
6.45e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.66 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 13 RLDFDPD-TAVYhYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:PRK03640 11 RAFLTPDrTAIE-FEEKKVTFMELHEAVVSVAGKLAALgVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREADAPSLSGPLAPLTLRAAAGRP-----LLDDFSLDAlvgpadldwsafhrqdpaaACFLQYTS 165
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPkeeaeIQEEFDLDE-------------------VATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 166 GSTGAPKGVMHSLRNTlgFCRAFATEL-LALQAGDR-LYSIPkMFFGYG---MGNSLFFpwfsGASALLDDTWpSPERVL 240
Cdd:PRK03640 151 GTTGKPKGVIQTYGNH--WWSAVGSALnLGLTEDDCwLAAVP-IFHISGlsiLMRSVIY----GMRVVLVEKF-DAEKIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 241 ENLVAFRPRVLFGVPAIYASL--RPQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGH--VFLANRPG 316
Cdd:PRK03640 223 KLLQTGGVTIISVVSTMLQRLleRLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqiVTLSPEDA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 317 QARADSTGLPLPGYECRLVDreGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCG 396
Cdd:PRK03640 303 LTKLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 397 REDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILlaqridQHLAEQIPSHML 476
Cdd:PRK03640 381 RRSDLIISGGENIYPAEIEEVLLSH-PGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELR------HFCEEKLAKYKV 453
|
490 500
....*....|....*....|....*.
gi 15596193 477 PSQLHVLPALPRNDNGKLARAELRHL 502
Cdd:PRK03640 454 PKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
154-500 |
6.93e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 104.96 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 DPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLA----LQAGDR--LYSIPKMFFGYGMGNSLFFPWFSGASA 227
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAgtgkLEEGCEvvITALPLYHIFALTANGLVFMKIGGCNH 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 228 LLDDTWPSPERVLEnLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFWA-AHGLEICDGIGA 303
Cdd:PRK08751 285 LISNPRDMPGFVKE-LKKTRFTAFTGVNTLFNGLlnTPGFDQIdFSSLKMTLGGGMAVQRSVAERWKqVTGLTLVEAYGL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 304 TEVGHVFLANRPG-QARADSTGLPLPGYECRLVDREGhTIEEAGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTG 381
Cdd:PRK08751 364 TETSPAACINPLTlKEYNGSIGLPIPSTDACIKDDAG-TVLAIGEIGELCIKGPQVMKGYWKRPEEtAKVMDADGWLHTG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 382 DLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRhLPEVSE--AVLVPTCRLHDGLRPTLfvtlatpLDDNQILL 459
Cdd:PRK08751 443 DIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAM-MPGVLEvaAVGVPDEKSGEIVKVVI-------VKKDPALT 514
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15596193 460 AQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK08751 515 AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
164-500 |
8.21e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 104.84 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHSLRNTLGFCRAFATELlALQAGDRLYSIPKMFFGYGMGNSLFFpwFSGASALLDDTWPSPERVLENL 243
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKAILDRT-PWRAEEPTVIVAPMFHAWGFSQLVLA--ASLACTIVTRRRFDPEATLDLI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 244 VAFRPRVLFGVPAIYASLRPQARELLS-----SVRLAFSAGSPL-PRGEFEFWAAHGLEICDGIGATEVGHVFLANrPGQ 317
Cdd:PRK13382 281 DRHRATGLAVVPVMFDRIMDLPAEVRNrysgrSLRFAAASGSRMrPDVVIAFMDQFGDVIYNNYNATEAGMIATAT-PAD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 318 ARA--DSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQqarFAGGWYRTGDLFERDESGAYRHC 395
Cdd:PRK13382 360 LRAapDTAGRPAEGTEIRILDQDFREVPT-GEVGTIFVRNDTQFDGYTSGSTKD---FHDGFMASGDVGYLDENGRLFVV 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 396 GREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHM 475
Cdd:PRK13382 436 GRDDEMIVSGGENVYPIEVEKTLATH-PDVAEAAVIGVDDEQYGQRLAAFVVLK----PGASATPETLKQHVRDNLANYK 510
|
330 340
....*....|....*....|....*
gi 15596193 476 LPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK13382 511 VPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-499 |
1.16e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.81 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVRE-ADAPSLsg 115
Cdd:PRK12316 545 RANRLAHALIergvgPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQsHLGRKL-- 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 PLAPLTLRAAAGRPllddfsldALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLAL 195
Cdd:PRK12316 623 PLAAGVQVLDLDRP--------AAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGL 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 196 QAGDRLYSIPKMFFGYGMGnSLFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQAR-ELLSSV 272
Cdd:PRK12316 694 GVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDvASCTSL 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFE--FWAAHGLEICDGIGATE--VGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQ 348
Cdd:PRK12316 773 RRIVCSGEALPADAQEqvFAKLPQAGLYNLYGPTEaaIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVP-VGVL 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 349 GVLLVRGPGLSPGYWR-----ASEEQQARFAGG--WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRH 421
Cdd:PRK12316 852 GELYLAGRGLARGYHGrpgltAERFVPSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596193 422 lPEVSEAVLVPTcrlhDGLRPTLFVTLATPLDDNQILLAQridqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK12316 932 -PWVREAAVLAV----DGKQLVGYVVLESEGGDWREALKA----HLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
43-499 |
1.59e-23 |
|
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: 103.56 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQA-SLVVREADAPSLSGPLAPL 120
Cdd:cd05920 54 AAGLRGLgIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAvAYIVPDRHAGFDHRALARE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 121 TLRAAAgrpllddfsldalvgpadldwsafhrqDPAaacFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDR 200
Cdd:cd05920 134 LAESIP---------------------------EVA---LFLLSGGTTGTPKLIPRTHNDYAYNVRASA-EVCGLDQDTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 201 LYSIPKMFFGY-----GMGNSLffpWFSGASALLDDtwPSPERVLENLVAFRPRVLFGVPAIyASLRPQAREL----LSS 271
Cdd:cd05920 183 YLAVLPAAHNFplacpGVLGTL---LAGGRVVLAPD--PSPDAAFPLIEREGVTVTALVPAL-VSLWLDAAASrradLSS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 272 VRLAFSAGSPLPrgefefwAAHGLEICDGIGATeVGHVF-----LAN-----RPGQARADSTGLPL-PGYECRLVDREGH 340
Cdd:cd05920 257 LRLLQVGGARLS-------PALARRVPPVLGCT-LQQVFgmaegLLNytrldDPDEVIIHTQGRPMsPDDEIRVVDEEGN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 341 TIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAIC 419
Cdd:cd05920 329 PVPP-GEEGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 420 RHlPEVSEAVLV--PTCRLhdGLRPTLFVTLAtplddNQILLAQRIDQHLAEQ-IPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd05920 408 RH-PAVHDAAVVamPDELL--GERSCAFVVLR-----DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
...
gi 15596193 497 AEL 499
Cdd:cd05920 480 KAL 482
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
27-500 |
1.75e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 103.03 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVV 105
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQgVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 READAPSLSGpLAPLTLRAAAGRPllddfsldalvgpaDLDWsafhrqDPAAACFLQYTSGSTGAPKGVMHSLRNTL--- 182
Cdd:PRK09029 106 VLEGENTFSA-LTSLHLQLVEGAH--------------AVAW------QPQRLATMTLTSGSTGLPKAAVHTAQAHLasa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 183 -GFCrafatELLALQAGDR-LYSIPkMFFGYGMGnsLFFPW-FSGASALLDDTWPspervLENLVAfrprvlfGVPaiYA 259
Cdd:PRK09029 165 eGVL-----SLMPFTAQDSwLLSLP-LFHVSGQG--IVWRWlYAGATLVVRDKQP-----LEQALA-------GCT--HA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 260 SLRP-QARELLSSVRLAFS------AGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANrpgqaRADST---GLPLPG 329
Cdd:PRK09029 223 SLVPtQLWRLLDNRSEPLSlkavllGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAK-----RADGLagvGSPLPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 330 YECRLVDREghtieeagrqgvLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDEsGAYRHCGREDDLFKVNGRWV 409
Cdd:PRK09029 298 REVKLVDGE------------IWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 410 VPTQVEQAICRHlPEVSEAVLVPtcrLHD---GLRPTLFVTLATPLDDNQillaqrIDQHLAEQIPSHMLPSQLHVLPAL 486
Cdd:PRK09029 365 QPEEIERVINQH-PLVQQVFVVP---VADaefGQRPVAVVESDSEAAVVN------LAEWLQDKLARFQQPVAYYLLPPE 434
|
490
....*....|....
gi 15596193 487 PRNDNGKLARAELR 500
Cdd:PRK09029 435 LKNGGIKISRQALK 448
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
23-500 |
1.79e-23 |
|
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: 103.53 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 23 YHYRgQTLSRlqCRtyilSQASQLARL-LKPGDRV-VLALNdSPSLACLFLACIAVGAIPAVINPKSREQALADIA--AD 98
Cdd:cd12118 30 YTWR-QTYDR--CR----RLASALAALgISRGDTVaVLAPN-TPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILrhSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 99 CQASLVVREADAPSLsgplapltlrAAAGRPllddfslDALVGPADLDWsafhrqDPAAacfLQYTSGSTGAPKGVMHSL 178
Cdd:cd12118 102 AKVLFVDREFEYEDL----------LAEGDP-------DFEWIPPADEW------DPIA---LNYTSGTTGRPKGVVYHH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 179 R----NTLGfcrafatELLALQAGDR---LYSIPkMFFGYGMGnslfFPW----FSGASALLDDTwpSPERVLENLVAFR 247
Cdd:cd12118 156 RgaylNALA-------NILEWEMKQHpvyLWTLP-MFHCNGWC----FPWtvaaVGGTNVCLRKV--DAKAIYDLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 248 PRVLFGVPAIYASL---RPQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEV-G-HVFLANRPG------ 316
Cdd:cd12118 222 VTHFCGAPTVLNMLanaPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETyGpATVCAWKPEwdelpt 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 317 --QARADS-TGLPLPGYE---------CRLVDREGHTIeeagrqGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLF 384
Cdd:cd12118 302 eeRARLKArQGVRYVGLEevdvldpetMKPVPRDGKTI------GEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 385 ERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTlatpLDDNQILLAQRID 464
Cdd:cd12118 376 VIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKH-PAVLEAAVVARPDEKWGEVPCAFVE----LKEGAKVTEEEII 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 15596193 465 QHLAEQIPSHMLPSQLHVLPaLPRNDNGKLARAELR 500
Cdd:cd12118 451 AFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-499 |
2.08e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.04 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQL-ARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIA 96
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLiERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 97 ADCQASLVVREADapslsgplapLTLRAAAGRPLLDDFSLDALVGPADLDwsafHRQDPAAACFLQYTSGSTGAPKGVMH 176
Cdd:PRK12316 3151 EDSGAQLLLSQSH----------LRLPLAQGVQVLDLDRGDENYAEANPA----IRTMPENLAYVIYTSGSTGKPKGVGI 3216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 177 SLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGyGMGNSLFFPWFSGASALLDDT--WPSPERVLENLVAFRPRVLFGV 254
Cdd:PRK12316 3217 RHSALSNHLCWMQ-QAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAGPedWRDPALLVELINSEGVDVLHAY 3294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 255 PAIYASLRPQAR-ELLSSVRLAFSAGSPLPRGEFEFWAAhGLEICDGIGATEVGHVFLANRPGQARADS--TGLPLPGYE 331
Cdd:PRK12316 3295 PSMLQAFLEEEDaHRCTSLKRIVCGGEALPADLQQQVFA-GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 332 CRLVDrEGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-------AGGWYRTGDLFERDESGAYRHCGREDDLFKV 404
Cdd:PRK12316 3374 CYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvpGERLYRTGDLARYRADGVIEYIGRVDHQVKI 3452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 NGRWVVPTQVEQAICRHlPEVSEAVLVPTcrlhDGLRPTLFVTLATPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLP 484
Cdd:PRK12316 3453 RGFRIELGEIEARLLEH-PWVREAVVLAV----DGRQLVAYVVPEDEAGD----LREALKAHLKASLPEYMVPAHLLFLE 3523
|
490
....*....|....*
gi 15596193 485 ALPRNDNGKLARAEL 499
Cdd:PRK12316 3524 RMPLTPNGKLDRKAL 3538
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-504 |
4.39e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.09 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 33 LQCRTYilsqASQLARLLKPGDRVVLALNDSPS-----LACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVRE 107
Cdd:PRK05691 48 LRARTI----AAALQARASFGDRAVLLFPSGPDyvaafFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 108 ADapsLSGPLAPL-TLRAAAGRPLLDDFSLDAlvGPADlDWSAFHRQDPAAAcFLQYTSGSTGAPKGVMHSLRNTLgfcr 186
Cdd:PRK05691 124 AD---LRDSLLQMeELAAANAPELLCVDTLDP--ALAE-AWQEPALQPDDIA-FLQYTSGSTALPKGVQVSHGNLV---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 187 afATELL-------ALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDDT---WPSPERVLENLVAFRPRVLFGVPA 256
Cdd:PRK05691 193 --ANEQLirhgfgiDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPayfLERPLRWLEAISEYGGTISGGPDF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 257 IY------ASLRPQARELLSSVRLAFSAGSPLPRGEFE---------------FWAAHGLEIC----------DGIGATE 305
Cdd:PRK05691 271 AYrlcserVSESALERLDLSRWRVAYSGSEPIRQDSLErfaekfaacgfdpdsFFASYGLAEAtlfvsggrrgQGIPALE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 306 V-GHVFLANR--PGQARA-DSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF---AG-GW 377
Cdd:PRK05691 351 LdAEALARNRaePGTGSVlMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGrTW 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 378 YRTGDL-FERDesGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLVPTCRLHDGlRPTLFVTLATPLDDNQ 456
Cdd:PRK05691 431 LRTGDLgFLRD--GELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQG-EEGIGIAAEISRSVQK 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 457 ILLAQ----RIDQHLAEQIpsHMLPSQLHVLP--ALPRNDNGKLARAELR-HLAD 504
Cdd:PRK05691 508 ILPPQalikSIRQAVAEAC--QEAPSVVLLLNpgALPKTSSGKLQRSACRlRLAD 560
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
92-502 |
6.55e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 102.00 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 92 LADIAADCQASLVVREADAPSLSGP---LAPLtLRAAAGRPLLddfsLDALVGPADLDWSAFHRQDPAaacFLQYTSGST 168
Cdd:PRK07768 93 LAVWAEDTLRVIGMIGAKAVVVGEPflaAAPV-LEEKGIRVLT----VADLLAADPIDPVETGEDDLA---LMQLTSGST 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 169 GAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALL---DDTWPSPERVLENLVA 245
Cdd:PRK07768 165 GSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKvtpMDFLRDPLLWAELISK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 246 FRPRVLFGVPAIYA----SLRPQAREL---LSSVRLAFSAGSPL-PRGEFEFWAA---HGL------------EICDGIG 302
Cdd:PRK07768 245 YRGTMTAAPNFAYAllarRLRRQAKPGafdLSSLRFALNGAEPIdPADVEDLLDAgarFGLrpeailpaygmaEATLAVS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVG----------------HVFLANRPGQARADST-GLPLPGYECRLVDREGHTIEEAGrQGVLLVRGPGLSPGYWRA 365
Cdd:PRK07768 325 FSPCGaglvvdevdadllaalRRAVPATKGNTRRLATlGPPLPGLEVRVVDEDGQVLPPRG-VGVIELRGESVTPGYLTM 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 366 SEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRhLPEVSE--AVLVptcRLHDGLRPT 443
Cdd:PRK07768 404 DGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAAR-VEGVRPgnAVAV---RLDAGHSRE 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 444 LFVTLATPLDDNQILLAQRIDQHLAEQIPSH--MLPSQLHVLPA--LPRNDNGKLARAELRHL 502
Cdd:PRK07768 480 GFAVAVESNAFEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLGPgsIPKTPSGKLRRANAAEL 542
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
37-503 |
9.41e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 101.90 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 37 TY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVreaD 109
Cdd:PLN02654 122 TYseLLDRVCQLANYLKdvgvkKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI---T 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 110 APSLSGPLAPLTLR----AAAGRPLLDDFSLDALVG-----------------------------PADLDWSAFHRQDPa 156
Cdd:PLN02654 199 CNAVKRGPKTINLKdivdAALDESAKNGVSVGICLTyenqlamkredtkwqegrdvwwqdvvpnyPTKCEVEWVDAEDP- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 157 aaCFLQYTSGSTGAPKGVMHSlrnTLGFCRAFATEL---LALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALLDD-- 231
Cdd:PLN02654 278 --LFLLYTSGSTGKPKGVLHT---TGGYMVYTATTFkyaFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEga 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 232 -TWPSPERVLENLVAFRPRVLFGVPAIYASL-----RPQARELLSSVRLAFSAGSPLP----RGEFEFWAAHGLEICDGI 301
Cdd:PLN02654 353 pNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLmrdgdEYVTRHSRKSLRVLGSVGEPINpsawRWFFNVVGDSRCPISDTW 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 302 GATEVGHVFLANRPGQ--ARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGlsPGYWRASEEQQARFA----- 374
Cdd:PLN02654 433 WQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKEIE-GECSGYLCVKKSW--PGAFRTLYGDHERYEttyfk 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 375 --GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTL--AT 450
Cdd:PLN02654 510 pfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSH-PQCAEAAVVGIEHEVKGQGIYAFVTLveGV 588
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15596193 451 PLDDNqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:PLN02654 589 PYSEE---LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
159-409 |
1.45e-22 |
|
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: 100.75 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 159 CFLQYTSGSTGAPKGVMHSLRN----TLGFCR----------------------AFATELLALQAGDRL-YSIPKmffgy 211
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNlvagIAGLGDrvpellgpddrylaylplahifELAAENVCLYRGGTIgYGSPR----- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 212 gmgnslffpwfsgasALLDDTWPSPErvlENLVAFRPRVLFGVPAI--------------------------YASLRPQA 265
Cdd:cd17639 166 ---------------TLTDKSKRGCK---GDLTEFKPTLMVGVPAIwdtirkgvlaklnpmgglkrtlfwtaYQSKLKAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 266 RELLSS------------------VRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPL 327
Cdd:cd17639 228 KEGPGTplldelvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 328 PGYECRLVDreghtIEEAGR-------QGVLLVRGPGLSPGYWRASEEQQARFAG-GWYRTGDLFERDESGAYRHCGRED 399
Cdd:cd17639 308 PCCEIKLVD-----WEEGGYstdkpppRGEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKK 382
|
330
....*....|.
gi 15596193 400 DLFKV-NGRWV 409
Cdd:cd17639 383 DLVKLqNGEYI 393
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-499 |
2.74e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 101.27 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 3 TLANLTEVlfRLDFDPDTAVYHYRGQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPA 81
Cdd:PRK10252 459 TLSALVAQ--QAAKTPDAPALADARYQFSYREMREQVVALANLLRERgVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 82 VINPKSREQALADIAADCQASLVVREAD-APSLsgplapltlraaAGRPLLDDFSLDALvgPADLDWSAFHRQDPAAACF 160
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADqLPRF------------ADVPDLTSLCYNAP--LAPQGAAPLQLSQPHHTAY 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVM--HslrntlgfcRAFATELLALQ------AGDR-LYSIPKMF------FgygmgnslFFPWFSGA 225
Cdd:PRK10252 603 IIFTSGSTGRPKGVMvgQ---------TAIVNRLLWMQnhypltADDVvLQKTPCSFdvsvweF--------FWPFIAGA 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 226 SALLDDtwPSPER---VLENLVA--------FRPRVLfgvPAIYASLRPQ-ARELLSSVRLAFSAGSPLP---RGEFEFW 290
Cdd:PRK10252 666 KLVMAE--PEAHRdplAMQQFFAeygvttthFVPSML---AAFVASLTPEgARQSCASLRQVFCSGEALPadlCREWQQL 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 291 AA---HGLeicdgIGATEVGhVFLANRP--GQARADSTGLPLP-GYEC-----RLVDREGHTIEeAGRQGVLLVRGPGLS 359
Cdd:PRK10252 741 TGaplHNL-----YGPTEAA-VDVSWYPafGEELAAVRGSSVPiGYPVwntglRILDARMRPVP-PGVAGDLYLTGIQLA 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 360 PGYWRASEEQQARF-------AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSEAVLVP 432
Cdd:PRK10252 814 QGYLGRPDLTASRFiadpfapGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAM-QALPDVEQAVTHA 892
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596193 433 tCRLHDglrptlfvTLATPLDDNQI---LLAQ---RID-----QHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK10252 893 -CVINQ--------AAATGGDARQLvgyLVSQsglPLDtsalqAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
150-506 |
5.97e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 100.00 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 150 FHRQDPAAACFlqyTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALl 229
Cdd:PRK08633 779 FKPDDTATIIF---SSGSEGEPKGVMLSHHNILSNIEQIS-DVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV- 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 230 ddTWPSP--ERVLENLVA-FRPRVLFGVPA---IYASLRPQARELLSSVRLAFSAGSPLP---RGEFE--FwaahGLEIC 298
Cdd:PRK08633 854 --YHPDPtdALGIAKLVAkHRATILLGTPTflrLYLRNKKLHPLMFASLRLVVAGAEKLKpevADAFEekF----GIRIL 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 DGIGATEVGHVFLANRPGQARAD----------STGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYW----R 364
Cdd:PRK08633 928 EGYGATETSPVASVNLPDVLAADfkrqtgskegSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLgdpeK 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 365 ASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHLPEvSEAVLVPTcRLHDGLRPTL 444
Cdd:PRK08633 1008 TAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGG-EEVVFAVT-AVPDEKKGEK 1085
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 445 FVTLATPLDDNqillAQRIDQHLAE-QIPSHMLPSQLHVLPALPRNDNGKLARAELRHLADTL 506
Cdd:PRK08633 1086 LVVLHTCGAED----VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
6-493 |
7.82e-22 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 99.27 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 6 NLTE-VLFRLDFDPDTAVYHYRGQTLSRL---QCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAI- 79
Cdd:cd05943 71 NYAEnLLRHADADDPAAIYAAEDGERTEVtwaELRRRVARLAAALRALgVKPGDRVAGYLPNIPEAVVAMLATASIGAIw 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 80 ---------PAV------INPK-----------SREQALADIAADCQASLvvreadaPSL--------SGPLAPLTLRAA 125
Cdd:cd05943 151 sscspdfgvPGVldrfgqIEPKvlfavdaytynGKRHDVREKVAELVKGL-------PSLlavvvvpyTVAAGQPDLSKI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLLDDFSLDALVGPADldwsaFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLgfcrAFATELLALQA----GDRL 201
Cdd:cd05943 224 AKALTLEDFLATGAAGELE-----FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL----LQHLKEHILHCdlrpGDRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 202 ysipkMFF---GYGMGNSLFFPWFSGASALLDD---TWPSPErVLENLVAfRPRV-LFGVPAIY------ASLRPQAREL 268
Cdd:cd05943 295 -----FYYttcGWMMWNWLVSGLAVGATIVLYDgspFYPDTN-ALWDLAD-EEGItVFGTSAKYldalekAGLKPAETHD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 269 LSSVRLAFSAGSPLPRGEFEF---WAAHGLEICDGIGATEVGHVF------LANRPGQARADSTGLPLPGYecrlvDREG 339
Cdd:cd05943 368 LSSLRTILSTGSPLKPESFDYvydHIKPDVLLASISGGTDIISCFvggnplLPVYRGEIQCRGLGMAVEAF-----DEEG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 340 HTIeeAGRQGVLLVRGPGLS-P-GYWRASEE---QQARFA--GGWYRTGDLFERDESGAYRHCGREDDLFKVNGrwV--- 409
Cdd:cd05943 443 KPV--WGEKGELVCTKPFPSmPvGFWNDPDGsryRAAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGG--Vrig 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 410 ---VPTQVEQaicrhLPEVSEAVLVPTCRLHDGLRPTLFVTLA--TPLDDNqilLAQRIDQHLAEQIPSHMLPSQLHVLP 484
Cdd:cd05943 519 taeIYRVVEK-----IPEVEDSLVVGQEWKDGDERVILFVKLRegVELDDE---LRKRIRSTIRSALSPRHVPAKIIAVP 590
|
....*....
gi 15596193 485 ALPRNDNGK 493
Cdd:cd05943 591 DIPRTLSGK 599
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
251-503 |
8.16e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 98.74 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFWAA-HGLEICDGIGATEVGHVFLANRPGQ-ARADSTGL 325
Cdd:PRK12492 311 LLGLNTLFVALmdHPGFKDLdFSALKLTNSGGTALVKATAERWEQlTGCTIVEGYGLTETSPVASTNPYGElARLGTVGI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV 404
Cdd:PRK12492 391 PVPGTALKVIDDDGNELP-LGERGELCIKGPQVMKGYWQQPEAtAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 NGRWVVPTQVEQAICRHlPEVSE--AVLVPTCRLHDGLRptLFVTLATPlddnqILLAQRIDQHLAEQIPSHMLPSQLHV 482
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAH-PKVANcaAIGVPDERSGEAVK--LFVVARDP-----GLSVEELKAYCKENFTGYKVPKHIVL 541
|
250 260
....*....|....*....|.
gi 15596193 483 LPALPRNDNGKLARAELRHLA 503
Cdd:PRK12492 542 RDSLPMTPVGKILRRELRDIA 562
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
159-496 |
9.07e-22 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 95.94 E-value: 9.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 159 CFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYsIPKMFFGYGMGNSLFFPWFSGASALLDDTWpSPER 238
Cdd:cd17633 3 FYIGFTSGTTGLPKAYYRSERSWIESFVC-NEDLFNISGEDAIL-APGPLSHSLFLYGAISALYLGGTFIGQRKF-NPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 239 VLENLVAFRPRVLFGVPAIYASLrpqARELL--SSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVGHVfLANR 314
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQAL---ARTLEpeSKIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSELSFI-TYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 315 PGQAR-ADSTGLPLPGYECRLVDREGhtieeaGRQGVLLVRGPGLSPGYWRASEEQqarfAGGWYRTGDLFERDESGAYR 393
Cdd:cd17633 156 NQESRpPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATpLDDNQILlaqridQHLAEQIPS 473
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVL-KAIPGIEEAIVVGIPDARFGEIAVALYSGDK-LTYKQLK------RFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 15596193 474 HMLPSQLHVLPALPRNDNGKLAR 496
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
164-499 |
1.41e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 97.76 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHS--LRNTLGFCRAFaTELLALQAGDRLYSIPKMFFGYGMGnSLFFPWFSGASALLDDTWPSpERVLE 241
Cdd:PRK13383 182 TSGTTGKPKGVPRApqLRSAVGVWVTI-LDRTRLRTGSRISVAMPMFHGLGLG-MLMLTIALGGTVLTHRHFDA-EAALA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 242 NLVAFRPRVLFGVPAIYASL-----RPQARELLSSVRLAFSAGSPL-PRGEFEFWAAHGLEICDGIGATEVGHVFLANrP 315
Cdd:PRK13383 259 QASLHRADAFTAVPVVLARIlelppRVRARNPLPQLRVVMSSGDRLdPTLGQRFMDTYGDILYNGYGSTEVGIGALAT-P 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 316 GQAR--ADSTGLPLPGYECRLVDREGHTIeeagrqgvllvrGPGLSPGYWRASEEQQARFAGGWYR--------TGDLFE 385
Cdd:PRK13383 338 ADLRdaPETVGKPVAGCPVRILDRNNRPV------------GPRVTGRIFVGGELAGTRYTDGGGKavvdgmtsTGDMGY 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 386 RDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNqillAQRIDQ 465
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAH-PAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD----AAQLRD 480
|
330 340 350
....*....|....*....|....*....|....
gi 15596193 466 HLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK13383 481 YLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-499 |
1.77e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLA-RLLKPG---DRVV-LALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADApslsgp 116
Cdd:PRK12467 3129 RANRLAhRLIAIGvgpDVLVgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHL------ 3202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 LAPLTLRAAAGRPLLDDFSLDALvgpadLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFAtELLALQ 196
Cdd:PRK12467 3203 LEQLPAPAGDTALTLDRLDLNGY-----SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIA-EAYELD 3276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 197 AGDRLysIPKMFFGY-GMGNSLFFPWFSGASALL--DDTWpSPERVLENLVAFRPRVLFGVPAIYASLRPQA-RELLSSV 272
Cdd:PRK12467 3277 ANDRV--LLFMSFSFdGAQERFLWTLICGGCLVVrdNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAgGADCASL 3353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRGEFEFWAAHGLEIC--DGIGATE-VGHVFLANRPGQARADST----GLPLPGYECRLVDREGHTIEeA 345
Cdd:PRK12467 3354 DIYVFGGEAVPPAAFEQVKRKLKPRGltNGYGPTEaVVTVTLWKCGGDAVCEAPyapiGRPVAGRSIYVLDGQLNPVP-V 3432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 346 GRQGVLLVRGPGLSPGYWRASEEQQARF-------AGG-WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQA 417
Cdd:PRK12467 3433 GVAGELYIGGVGLARGYHQRPSLTAERFvadpfsgSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 3512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 418 ICRHlPEVSEAVLVPTcrlhDGLRPTLFVTLATPLDDNQILLAQRIDqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARA 497
Cdd:PRK12467 3513 LLQH-PSVREAVVLAR----DGAGGKQLVAYVVPADPQGDWRETLRD-HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
..
gi 15596193 498 EL 499
Cdd:PRK12467 3587 AL 3588
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
18-499 |
2.56e-21 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 97.01 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLsrlqcrTY--ILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQ 90
Cdd:cd17655 11 PDHTAVVFEDQTL------TYreLNERANQLARTLrekgvGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREadapslsGPLAPLtlRAAAGRPLLDDfsldalvgpaDLDWSAFHRQDPAAAC------FLQYT 164
Cdd:cd17655 85 RIQYILEDSGADILLTQ-------SHLQPP--IAFIGLIDLLD----------EDTIYHEESENLEPVSksddlaYVIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 165 SGSTGAPKGVM---HSLRNTLgfcrAFATELLALQAGDRLYSIPKMFFGYGMGnSLFFPWFSGASALL---DDTWPSPEr 238
Cdd:cd17655 146 SGSTGKPKGVMiehRGVVNLV----EWANKVIYQGEHLRVALFASISFDASVT-EIFASLLSGNTLYIvrkETVLDGQA- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 239 VLENLVAFRPRVLFGVPAIYASLRPQARELLSSVRLAFSAGSPLPRGEFEFWAAH---GLEICDGIGATE--VGHVFLAN 313
Cdd:cd17655 220 LTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTEttVDASIYQY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 RPGQARADST--GLPLPGYECRLVDREGHtIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF------AGG-WYRTGDLF 384
Cdd:cd17655 300 EPETDQQVSVpiGKPLGNTRIYILDQYGR-PQPVGVAGELYIGGEGVARGYLNRPELTAEKFvddpfvPGErMYRTGDLA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 385 ERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVlVPTCRLHDGlRPTLFVTLATpldDNQILLAQrID 464
Cdd:cd17655 379 RWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQH-PDIKEAV-VIARKDEQG-QNYLCAYIVS---EKELPVAQ-LR 451
|
490 500 510
....*....|....*....|....*....|....*
gi 15596193 465 QHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17655 452 EFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
155-500 |
3.71e-21 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 96.63 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 155 PAAACFLQYTSGSTGAPKGVMHSLRNTL------------GFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLffpwf 222
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawlqpAFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRT----- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 223 sGASALLddtWPSPERV---LENLVAFRPRVLFGVPAIYASL--RPQAREL-LSSVRLAFSAGSPLPRGEFEFW-AAHGL 295
Cdd:PRK07059 278 -GGRNIL---IPNPRDIpgfIKELKKYQVHIFPAVNTLYNALlnNPDFDKLdFSKLIVANGGGMAVQRPVAERWlEMTGC 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 296 EICDGIGATEVGHVFLANRpgqarADST------GLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYW-RASEE 368
Cdd:PRK07059 354 PITEGYGLSETSPVATCNP-----VDATefsgtiGLPLPSTEVSIRDDDGNDLP-LGEPGEICIRGPQVMAGYWnRPDET 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 369 QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTL 448
Cdd:PRK07059 428 AKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASH-PGVLEVAAVGVPDEHSGEAVKLFVVK 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15596193 449 ATPlddnqILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07059 507 KDP-----ALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
17-503 |
5.04e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 96.42 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 17 DPDTAVYHYRG--QTLSRLQCRTYILsqASQLARL-LKPGDRV-VLALNDSPSLACLFlACIAVGAIPAVINP--KSREQ 90
Cdd:PRK08315 31 DREALVYRDQGlrWTYREFNEEVDAL--AKGLLALgIEKGDRVgIWAPNVPEWVLTQF-ATAKIGAILVTINPayRLSEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQAsLVV----READAPSLSGPLAPLTLRAAAGR------PLLDD-FSLDALVGPADLDWSAF-----HRQD 154
Cdd:PRK08315 108 EYALNQSGCKA-LIAadgfKDSDYVAMLYELAPELATCEPGQlqsarlPELRRvIFLGDEKHPGMLNFDELlalgrAVDD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 155 PAAACF-----------LQYTSGSTGAPKGVMHSLRNTL--GFcraFATELLALQAGDRLySIPKMF---FGYGMGN--- 215
Cdd:PRK08315 187 AELAARqatldpddpinIQYTSGTTGFPKGATLTHRNILnnGY---FIGEAMKLTEEDRL-CIPVPLyhcFGMVLGNlac 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 216 -SlffpwfSGASALlddtWPS----PERVLENLVAFRPRVLFGVPAIY-ASL-RPQ-ARELLSSVRLAFSAGSPLPR--- 284
Cdd:PRK08315 263 vT------HGATMV----YPGegfdPLATLAAVEEERCTALYGVPTMFiAELdHPDfARFDLSSLRTGIMAGSPCPIevm 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 285 ----GEFefwaaHGLEICDGIGATEVGHVFLANR---PGQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPG 357
Cdd:PRK08315 333 krviDKM-----HMSEVTIAYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 358 LSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA--VLVPT- 433
Cdd:PRK08315 408 VMKGYWNDPEKtAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTH-PKIQDVqvVGVPDe 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 434 ------C---RLHDGlrptlfvtlatplddnQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:PRK08315 487 kygeevCawiILRPG----------------ATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
154-499 |
1.07e-20 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 94.46 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 DPAAACFLQYTSGSTGAPKGVMHSLRNtlgFCRAFAT-----ELLALQAgdRLYSIPKMFFgygmgnSLFFPWFsgASAL 228
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRN---VAHAAHAwrreyELDSFPV--RLLQMASFSF------DVFAGDF--ARSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 229 L---------DDTWPSPERVLENLVAFRPRVLFGVPAIyasLRPQAREL------LSSVRLaFSAGSPLPRGEFEFWAA- 292
Cdd:cd17650 158 LnggtlvicpDEVKLDPAALYDLILKSRITLMESTPAL---IRPVMAYVyrngldLSAMRL-LIVGSDGCKAQDFKTLAa 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 293 ---HGLEICDGIGATEV---GHVFLANRPGQARADST--GLPLPGYECRLVDrEGHTIEEAGRQGVLLVRGPGLSPGYWR 364
Cdd:cd17650 234 rfgQGMRIINSYGVTEAtidSTYYEEGRDPLGDSANVpiGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 365 ASEEQQARF------AGG-WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLvpTCRLH 437
Cdd:cd17650 313 RPELTAERFvenpfaPGErMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARH-PAIDEAVV--AVRED 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 438 DGLRPTL--FVTLATPLDDNQIllaqriDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17650 390 KGGEARLcaYVVAAATLNTAEL------RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
43-500 |
1.11e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 95.11 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARLLKPGDRV-VLALNDSPSLACLFlACIAVGAIPAVINPKSREQALADIAADCQASLVVREAD-----------A 110
Cdd:PRK07470 47 AALAARGVRKGDRIlVHSRNCNQMFESMF-AAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADfpehaaavraaS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 111 PSLSGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDwsafhRQDPaaaCFLQYTSGSTGAPKGVMHSlRNTLGFcrAFAT 190
Cdd:PRK07470 126 PDLTHVVAIGGARAGLDYEALVARHLGARVANAAVD-----HDDP---CWFFFTSGTTGRPKAAVLT-HGQMAF--VITN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 191 ELLALQAG----DRlySIPKMFFGYGMGNSLFFPWFSGASALLDDTWP-SPERVLEnLVAfRPRV--LFGVPAIYASL-- 261
Cdd:PRK07470 195 HLADLMPGtteqDA--SLVVAPLSHGAGIHQLCQVARGAATVLLPSERfDPAEVWA-LVE-RHRVtnLFTVPTILKMLve 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 262 RPQ-ARELLSSVRLAFSAGSPLPRGEFEfwaaHGLEIcdgIGATEVGHVFLANRPG----------------QARADSTG 324
Cdd:PRK07470 271 HPAvDRYDHSSLRYVIYAGAPMYRADQK----RALAK---LGKVLVQYFGLGEVTGnitvlppalhdaedgpDARIGTCG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 325 LPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV 404
Cdd:PRK07470 344 FERTGMEVQIQDDEGRELP-PGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYIS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 NGRWVVPTQVEQAICRHlPEVSE-AVL-----------VPTCRLHDGLRPTlfvtlatplddnqillAQRIDQHLAEQIP 472
Cdd:PRK07470 423 GGSNVYPREIEEKLLTH-PAVSEvAVLgvpdpvwgevgVAVCVARDGAPVD----------------EAELLAWLDGKVA 485
|
490 500
....*....|....*....|....*...
gi 15596193 473 SHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK07470 486 RYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
37-503 |
1.12e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 95.59 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 37 TY--ILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVI----NPksreQALADIAADCQASLVV 105
Cdd:PRK00174 100 TYreLHREVCRFANALKslgvkKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSA----EALADRIIDAGAKLVI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 rEADApslsgplaplTLRAaaGRPL-LDDFSLDALVGPA-------------DLDWSA-----FHR-QDPAAA-C----- 159
Cdd:PRK00174 176 -TADE----------GVRG--GKPIpLKANVDEALANCPsvekvivvrrtggDVDWVEgrdlwWHElVAGASDeCepepm 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 ------FLQYTSGSTGAPKGVMHSlrnTLGFcrafatELLA---------LQAGDrlysipkMFF-----GYGMGNS--L 217
Cdd:PRK00174 243 daedplFILYTSGSTGKPKGVLHT---TGGY------LVYAamtmkyvfdYKDGD-------VYWctadvGWVTGHSyiV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 FFPWFSGASALLDD---TWPSPERVLEnlVAFRPRV--LFGVP-AIYASLR-----PQARELlSSVRLAFSAGSPL-Prg 285
Cdd:PRK00174 307 YGPLANGATTLMFEgvpNYPDPGRFWE--VIDKHKVtiFYTAPtAIRALMKegdehPKKYDL-SSLRLLGSVGEPInP-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 286 EFEFWAAH--GLEIC---DGIGATEVGHVFLANRPG--QARADSTGLPLPGYECRLVDREGHTIEEAGRqGVLLVRGPGl 358
Cdd:PRK00174 382 EAWEWYYKvvGGERCpivDTWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPAVVDEEGNPLEGGEG-GNLVIKDPW- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 359 sPG---------------YWraseeqqARFAGGwYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlP 423
Cdd:PRK00174 460 -PGmmrtiygdherfvktYF-------STFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH-P 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 424 EVSEAVLVPtcRLHD--GLRPTLFVTL---ATPLDDnqilLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAE 498
Cdd:PRK00174 530 KVAEAAVVG--RPDDikGQGIYAFVTLkggEEPSDE----LRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRI 603
|
....*
gi 15596193 499 LRHLA 503
Cdd:PRK00174 604 LRKIA 608
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
53-499 |
2.06e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 94.30 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 53 GDRVVLALNDSPSLACLFLACIAVGAIPAVIN---PKSREQALADIAaDCQASLVVREA--DAPSLSGPLA--PLTLRAA 125
Cdd:PRK05857 66 GSRVLVISDNGPETYLSVLACAKLGAIAVMADgnlPIAAIERFCQIT-DPAAALVAPGSkmASSAVPEALHsiPVIAVDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLLDDFSLDALVGPADLDWSAfhrQDPAAACFlqyTSGSTGAPKGVMhsLRNTLGFC-----RAFATELLALQAGDR 200
Cdd:PRK05857 145 AAVTRESEHSLDAASLAGNADQGS---EDPLAMIF---TSGTTGEPKAVL--LANRTFFAvpdilQKEGLNWVTWVVGET 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 201 LYS-IPKMFFG--YGMGNSLFfpwfSGASALLDDTWPSPERVLENLVAFRPRVLfgVPAIYASLRPQ---ARELLSSVRL 274
Cdd:PRK05857 217 TYSpLPATHIGglWWILTCLM----HGGLCVTGGENTTSLLEILTTNAVATTCL--VPTLLSKLVSElksANATVPSLRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 275 AFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFL-----ANRPGQARADSTGLPLPGYECRLVDREGH--TIEEAGR 347
Cdd:PRK05857 291 VGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALclptdDGSIVKIEAGAVGRPYPGVDVYLAATDGIgpTAPGAGP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 348 Q---GVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQaICRHLPE 424
Cdd:PRK05857 371 SasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDR-IAEGVSG 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 425 VSEAVLVPTCRLHDGLRPTLFVTLATPLDDN-QILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK05857 450 VREAACYEIPDEEFGALVGLAVVASAELDESaARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
18-499 |
3.65e-20 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 93.00 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRtyilSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLN----EKANQLARHLrgkgvKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVVREADapslsgplapltlraaagrpllddfsldalvgpaDLdwsafhrqdpaaaCFLQYTSGSTGAPK 172
Cdd:cd17645 88 AYMLADSSAKILLTNPD----------------------------------DL-------------AYVIYTSGSTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVMHSLRNTLGFCrAFATELLALQAGDRlysiPKMFFGYGMGNS---LFFPWFSGASALLddtwpSPERVLENLVAFRPr 249
Cdd:cd17645 121 GVMIEHHNLVNLC-EWHRPYFGVTPADK----SLVYASFSFDASaweIFPHLTAGAALHV-----VPSERRLDLDALND- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 250 vLFGVPAIYASLRP-QARELL-----SSVRLAFSAGSPLPRGEfefwaAHGLEICDGIGATE---VGHVFLANRPGQARa 320
Cdd:cd17645 190 -YFNQEGITISFLPtGAAEQFmqldnQSLRVLLTGGDKLKKIE-----RKGYKLVNNYGPTEntvVATSFEIDKPYANI- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 321 dSTGLPLPGYECRLVDrEGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG-------WYRTGDLFERDESGAYR 393
Cdd:cd17645 263 -PIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLvpTCRLHDGLRPTL--FVTLATPLDdnqillAQRIDQHLAEQI 471
Cdd:cd17645 341 FLGRLDQQVKIRGYRIEPGEIEPFLMNH-PLIELAAV--LAKEDADGRKYLvaYVTAPEEIP------HEELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 15596193 472 PSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
14-500 |
1.08e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 91.97 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 14 LDFDPDTAVYHYRGQTLSRLQCRTYIlSQASQL--ARLLKPGDRV-VLALNDSPSLACLFLACIAvGAIPAVINPKSREQ 90
Cdd:PRK06188 22 LKRYPDRPALVLGDTRLTYGQLADRI-SRYIQAfeALGLGTGDAVaLLSLNRPEVLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 91 ALADIAADCQASLVVREAdapslsGPLAPLTLRAAAGRP-LLDDFSLDALVGPADLdWSAFHRQDPA----AAC-----F 160
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDP------APFVERALALLARVPsLKHVLTLGPVPDGVDL-LAAAAKFGPAplvaAALppdiaG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 LQYTSGSTGAPKGVMHSLRNTLGFCRAFATELlALQAGDRLYSIPKMFFGygmGNSLFFP-WFSGASALLDDTWpSPERV 239
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEW-EWPADPRFLMCTPLSHA---GGAFFLPtLLRGGTVIVLAKF-DPAEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 240 LENLVAFRPRVLFGVPA-IYASL---RPQARELlSSVRLAFSAGSPLPRGEFefwaAHGLEICDGI-----GATEVGHVF 310
Cdd:PRK06188 248 LRAIEEQRITATFLVPTmIYALLdhpDLRTRDL-SSLETVYYGASPMSPVRL----AEAIERFGPIfaqyyGQTEAPMVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 311 LANRPGQ------ARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLF 384
Cdd:PRK06188 323 TYLRKRDhdpddpKRLTSCGRPTPGLRVALLDEDGREVA-QGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 385 ERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA--VLVPtcrlHD--GLRPTLFVTLATPLDDNqillA 460
Cdd:PRK06188 402 REDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEH-PAVAQVavIGVP----DEkwGEAVTAVVVLRPGAAVD----A 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15596193 461 QRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
42-499 |
1.13e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.31 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADAPSlsgp 116
Cdd:PRK05691 1165 QANRLAHYLRdkgvgPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLE---- 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 laplTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAaacFLQYTSGSTGAPKGVMHSlRNTLGFCRAFATELLALQ 196
Cdd:PRK05691 1241 ----RLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLA---YVIYTSGSTGQPKGVGNT-HAALAERLQWMQATYALD 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 197 AGDRLYSIPKMFFGYGMGNSlFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAIYASL--RPQARELlSSV 272
Cdd:PRK05691 1313 DSDVLMQKAPISFDVSVWEC-FWPLITGCRLVLagPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFidEPLAAAC-TSL 1390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 273 RLAFSAGSPLPRgefefwaahglEICDGIGAtEVGHVFLANRPG-----------QARADST-----GLPLPGYECRLVD 336
Cdd:PRK05691 1391 RRLFSGGEALPA-----------ELRNRVLQ-RLPQVQLHNRYGptetainvthwQCQAEDGerspiGRPLGNVLCRVLD 1458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 337 REGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG--------WYRTGDLFERDESGAYRHCGREDDLFKVNGRW 408
Cdd:PRK05691 1459 AELNLLP-PGVAGELCIGGAGLARGYLGRPALTAERFVPDplgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFR 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 409 VVPTQVEQAICRhLPEVSEAVLVptcrLHDGLRPTLFVTLATpLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPR 488
Cdd:PRK05691 1538 VEPEEIQARLLA-QPGVAQAAVL----VREGAAGAQLVGYYT-GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPL 1611
|
490
....*....|.
gi 15596193 489 NDNGKLARAEL 499
Cdd:PRK05691 1612 GPSGKLDRRAL 1622
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
50-474 |
2.49e-19 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 90.95 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP----KSREQA-LADIAADCQASLVVREaDAPSLSGPLAPL---- 120
Cdd:cd05921 47 LSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslMSQDLAkLKHLFELLKPGLVFAQ-DAAPFARALAAIfplg 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 121 -----TLRAAAGRPLLDDFSLDALVGPADLDwSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNtLGFCRAFATELLAL 195
Cdd:cd05921 126 tplvvSRNAVAGRGAISFAELAATPPTAAVD-AAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRM-LCANQAMLEQTYPF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 196 QAGDRLYSIPKMFFGYGMGNSLFFP--WFSGASALLDDTWPSP---ERVLENLVAFRPRVLFGVPAIYASLRPQ------ 264
Cdd:cd05921 204 FGEEPPVLVDWLPWNHTFGGNHNFNlvLYNGGTLYIDDGKPMPggfEETLRNLREISPTVYFNVPAGWEMLVAAlekdea 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 265 -ARELLSSVRLAFSAGSPLPRGEFEFWAA-------HGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVd 336
Cdd:cd05921 284 lRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavatvgERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 337 reghtieEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLF-----ERDESGAYRHcGREDDLFKVN-GRWV 409
Cdd:cd05921 363 -------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAkladpDDPAKGLVFD-GRVAEDFKLAsGTWV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 410 -VPTQVEQAICRHLPEVSEAVL---------------VPTCRLHDGLRptlfvtlatPLDDNQILLAQRIDQHLAEQIPS 473
Cdd:cd05921 435 sVGPLRARAVAACAPLVHDAVVagedraevgalvfpdLLACRRLVGLQ---------EASDAEVLRHAKVRAAFRDRLAA 505
|
.
gi 15596193 474 H 474
Cdd:cd05921 506 L 506
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
36-500 |
2.61e-19 |
|
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: 90.57 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 36 RTYILSQASQLA----------RLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPksreqaladiaadcqaslvv 105
Cdd:cd05937 4 KTWTYSETYDLVlryahwlhddLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINY-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 readapSLSGplapltlraaagrpllddfslDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFC 185
Cdd:cd05937 64 ------NLSG---------------------DPLIHCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 186 RAFATELlALQAGDRLYSIPKMFFG----YGMGNSL-------FFPWFSgASALLDDTWPSPERVLEnLVAFRPRVLFGV 254
Cdd:cd05937 117 NLLSHDL-NLKNGDRTYTCMPLYHGtaafLGACNCLmsggtlaLSRKFS-ASQFWKDVRDSGATIIQ-YVGELCRYLLST 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 255 PaiyaslrPQARELLSSVRLAFSAG-SPLPRGEF----------EFWAAhgleiCDGIGAT-----------EVGH---- 308
Cdd:cd05937 194 P-------PSPYDRDHKVRVAWGNGlRPDIWERFrerfnvpeigEFYAA-----TEGVFALtnhnvgdfgagAIGHhgli 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 309 --VFLANRPGQARAD-STGLPLpgyecrLVDREGHTIEEA-GRQGVLLVRGP----GLSPGYWRASEEQQAR-----FAG 375
Cdd:cd05937 262 rrWKFENQVVLVKMDpETDDPI------RDPKTGFCVRAPvGEPGEMLGRVPfknrEAFQGYLHNEDATESKlvrdvFRK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 376 G--WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA----VLVPTcrlHDGLRPTLFVTLA 449
Cdd:cd05937 336 GdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAH-PDIAEAnvygVKVPG---HDGRAGCAAITLE 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15596193 450 TPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05937 412 ESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
152-431 |
2.77e-19 |
|
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: 90.95 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 152 RQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFaTELLALQAGDRLYS------IPKMFFGYGM----GNSLFFPw 221
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAY-LAADPLGPGDEYVSvlplpwIGEQMYSVGQalvcGFIVNFP- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 222 fSGASALLDD---TWP----SPERVLENLVAF----------------------------------------RPRVLFGV 254
Cdd:cd17641 232 -EEPETMMEDlreIGPtfvlLPPRVWEGIAADvrarmmdatpfkrfmfelgmklglraldrgkrgrpvslwlRLASWLAD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 255 PAIYASLRpqARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRl 334
Cdd:cd17641 311 ALLFRPLR--DRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 335 vdreghtIEEAGRqgvLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKV-NGRWVVPT 412
Cdd:cd17641 388 -------IDEVGE---ILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQ 457
|
330
....*....|....*....
gi 15596193 413 QVEQAIcRHLPEVSEAVLV 431
Cdd:cd17641 458 FIENKL-KFSPYIAEAVVL 475
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
50-500 |
4.43e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 90.13 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPS-LACLF-LACIavGAIPAVINPKSREQALADIAADCQASLVVREAdapslsgPLAPL--TLRAA 125
Cdd:PRK08008 59 IRKGDKVALHLDNCPEfIFCWFgLAKI--GAIMVPINARLLREESAWILQNSQASLLVTSA-------QFYPMyrQIQQE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLLDDFSLDAlVGPADLDWSAFHRQDPAAACFLQY--------------TSGSTGAPKGVMHSLRNTL--GFCRAFA 189
Cdd:PRK08008 130 DATPLRHICLTRV-ALPADDGVSSFTQLKAQQPATLCYapplstddtaeilfTSGTTSRPKGVVITHYNLRfaGYYSAWQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 190 TellALQAGDRLYSIPKMFFGYGMGNSLFfPWFS-GASALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASL--RPQA- 265
Cdd:PRK08008 209 C---ALRDDDVYLTVMPAFHIDCQCTAAM-AAFSaGATFVLLEKY-SARAFWGQVCKYRATITECIPMMIRTLmvQPPSa 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 266 -------RELLSSVRLafsagSPLPRGEFEfwAAHGLEICDGIGATE--VGhvFLANRPGQARA-DSTGLPLPGYECRLV 335
Cdd:PRK08008 284 ndrqhclREVMFYLNL-----SDQEKDAFE--ERFGVRLLTSYGMTEtiVG--IIGDRPGDKRRwPSIGRPGFCYEAEIR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 336 DREGHTIEeAGRQGVLLVRG-PG--LSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVP 411
Cdd:PRK08008 355 DDHNRPLP-AGEIGEICIKGvPGktIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 412 TQVEQAICRHlPEVSEAVLVPtcrLHDGLRP---TLFVTLAtpldDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPR 488
Cdd:PRK08008 434 VELENIIATH-PKIQDIVVVG---IKDSIRDeaiKAFVVLN----EGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPR 505
|
490
....*....|..
gi 15596193 489 NDNGKLARAELR 500
Cdd:PRK08008 506 NCSGKIIKKNLK 517
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-499 |
5.93e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.99 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVvreadapslsgp 116
Cdd:PRK12467 1608 RANRLAHRLialgvGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL------------ 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 117 lapLTLRAAAGR-PLLDdfSLDALVGPADLDWSAFH-------RQDPAAACFLQYTSGSTGAPKGVM---HSLRNTLGFC 185
Cdd:PRK12467 1676 ---LTQSHLQARlPLPD--GLRSLVLDQEDDWLEGYsdsnpavNLAPQNLAYVIYTSGSTGRPKGAGnrhGALVNRLCAT 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 186 RafatELLALQAGDRLysIPKMFFGYGMGN-SLFFPWFSGASALL--DDTWPSPERVLENLVAFRPRVLFGVPAI---YA 259
Cdd:PRK12467 1751 Q----EAYQLSAADVV--LQFTSFAFDVSVwELFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMlqqLL 1824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 260 SLRPQARELLSSVRLAFSaGSPLP----RGEFEFWAAHGLeiCDGIGATEVG-HV--FLANRPGQARADST--GLPLPGY 330
Cdd:PRK12467 1825 QMDEQVEHPLSLRRVVCG-GEALEvealRPWLERLPDTGL--FNLYGPTETAvDVthWTCRRKDLEGRDSVpiGQPIANL 1901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 331 ECRLVDREGHTIeEAGRQGVLLVRGPGLSPGYWRASEEQQARF--------AGGWYRTGDLFERDESGAYRHCGREDDLF 402
Cdd:PRK12467 1902 STYILDASLNPV-PIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 403 KVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrlHDGLRPTLFVTLATPLD-------DNQILLAQRIDQHLAEQIPSHM 475
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQ-GGVREAVVIA----QDGANGKQLVAYVVPTDpglvdddEAQVALRAILKNHLKASLPEYM 2055
|
490 500
....*....|....*....|....
gi 15596193 476 LPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK12467 2056 VPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
27-517 |
8.14e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 89.55 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCrtyiLSQAsQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP----KSREQA-LADIAADCQA 101
Cdd:PRK08180 73 AEALERVRA----IAQA-LLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslVSQDFGkLRHVLELLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 102 SLVV--------READAPSLSGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDwSAFHRQDP-AAACFLqYTSGSTGAPK 172
Cdd:PRK08180 148 GLVFaddgaafaRALAAVVPADVEVVAVRGAVPGRAATPFAALLATPPTAAVD-AAHAAVGPdTIAKFL-FTSGSTGLPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVMHSLRNtlgfcrafatelLALQAGDRLYSIPkmFFGYG---MGNSLffPW--------------FSGASALLDDTWPS 235
Cdd:PRK08180 226 AVINTHRM------------LCANQQMLAQTFP--FLAEEppvLVDWL--PWnhtfggnhnlgivlYNGGTLYIDDGKPT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 236 PERV---LENLVAFRPRVLFGVPAIYASLRPQ-------ARELLSSVRLAFSAGSPLPRGEFEFWAAHGLE-------IC 298
Cdd:PRK08180 290 PGGFdetLRNLREISPTVYFNVPKGWEMLVPAlerdaalRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEAtcgerirMM 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 DGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTieEAgrqgvlLVRGPGLSPGYWRASEEQQARF-AGGW 377
Cdd:PRK08180 370 TGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGGKL--EV------RVKGPNVTPGYWRAPELTAEAFdEEGY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 378 YRTGDLF----ERDESGAYRHCGR--EDdlFKV-NGRWV-VPTQVEQAICRHLPEVSEAVL---------------VPTC 434
Cdd:PRK08180 442 YRSGDAVrfvdPADPERGLMFDGRiaED--FKLsSGTWVsVGPLRARAVSAGAPLVQDVVItghdrdeigllvfpnLDAC 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 435 RLHDGLRPTLfvTLATPLDDNQIL--LAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLA-------RAELRH---L 502
Cdd:PRK08180 520 RRLAGLLADA--SLAEVLAHPAVRaaFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEITdkgyinqRAVLARraaL 597
|
570
....*....|....*
gi 15596193 503 ADTLYHDNLPEERAC 517
Cdd:PRK08180 598 VEALYADEPDDPVII 612
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
23-428 |
8.40e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 89.38 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 23 YHYRGqtlsrLQCRTYILSQAsqLARL-LKPGDRV-VLALNDSPSLAcLFLACIAVGAIPAVINPKSREQALADIA--AD 98
Cdd:PRK07008 40 YTYRD-----CERRAKQLAQA--LAALgVEPGDRVgTLAWNGYRHLE-AYYGVSGSGAVCHTINPRLFPEQIAYIVnhAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 99 CQ--------ASLVVREADA-PSLSGPLApLTLRA---AAGRPLLddfSLDALVG--PADLDWSAFhrqDPAAACFLQYT 164
Cdd:PRK07008 112 DRyvlfdltfLPLVDALAPQcPNVKGWVA-MTDAAhlpAGSTPLL---CYETLVGaqDGDYDWPRF---DENQASSLCYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 165 SGSTGAPKGVMHSLRNTLgfCRAFATEL---LALQAGDRLYSIPKMFF--GYGM-------GNSLFFPW--FSGASalld 230
Cdd:PRK07008 185 SGTTGNPKGALYSHRSTV--LHAYGAALpdaMGLSARDAVLPVVPMFHvnAWGLpysapltGAKLVLPGpdLDGKS---- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 231 dtwpspervLENLVAfRPRVLF--GVPAIYASLRPQAREL---LSSVRLAFSAGSPLPRGEFE-FWAAHGLEICDGIGAT 304
Cdd:PRK07008 259 ---------LYELIE-AERVTFsaGVPTVWLGLLNHMREAglrFSTLRRTVIGGSACPPAMIRtFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 305 EVG-----------HVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGR-QGVLLVRGPGLSPGYWRASEEQQAR 372
Cdd:PRK07008 329 EMSplgtlcklkwkHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKaFGDLQVRGPWVIDRYFRGDASPLVD 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 373 fagGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA 428
Cdd:PRK07008 409 ---GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAH-PAVAEA 460
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
18-499 |
1.39e-18 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 88.30 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQcrtyiLSQAS-QLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQA 91
Cdd:cd17656 2 PDAVAVVFENQKLTYRE-----LNERSnQLARFLrekgvKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 92 LADIAADCQASLVVREADAPSlsgplapltlraaagrPLLDDFSLDALVGPADLDWSAFHRQDPAAA---CFLQYTSGST 168
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRHLKS----------------KLSFNKSTILLEDPSISQEDTSNIDYINNSddlLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 169 GAPKGVMHSLRNTLGFCrAFATELLALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLDDTwpSPERVLENLVAF-- 246
Cdd:cd17656 141 GKPKGVQLEHKNMVNLL-HFEREKTNINFSDKVLQFATCSFDVCY-QEIFSTLLSGGTLYIIRE--ETKRDVEQLFDLvk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 247 --RPRVLFgVPAIY----ASLRPQARELLSSVRLAFSAGSPLP-RGEF-EFWAAHGLEICDGIGATEVgHVFLANR---- 314
Cdd:cd17656 217 rhNIEVVF-LPVAFlkfiFSEREFINRFPTCVKHIITAGEQLViTNEFkEMLHEHNVHLHNHYGPSET-HVVTTYTinpe 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 315 PGQARADSTGLPLPGYECRLVDREGhTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG-------WYRTGDLFERD 387
Cdd:cd17656 295 AEIPELPPIGKPISNTWIYILDQEQ-QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQIllaqriDQHL 467
Cdd:cd17656 374 PDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNH-PGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQL------REYL 446
|
490 500 510
....*....|....*....|....*....|..
gi 15596193 468 AEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17656 447 AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-493 |
7.17e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 85.13 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 FLQYTSGSTGAPKGVM---HSLRNTLGFCRAFATE-----LLALQA-----GDRLYSIPKMFFGYGMgNSLFFPWFSGAS 226
Cdd:cd05924 7 YILYTGGTTGMPKGVMwrqEDIFRMLMGGADFGTGeftpsEDAHKAaaaaaGTVMFPAPPLMHGTGS-WTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 227 ALLDDTWPSPERVLENLVAFRPRVLFGVPAIYAslRPQAREL-------LSSVRLAFSAGSPL-PRGEFEFWAA-HGLEI 297
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMA--RPLIDALrdagpydLSSLFAISSGGALLsPEVKQGLLELvPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 298 CDGIGATEVGhvFLANRPGQARADSTG-LPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSP-GYWRASEEQQARF-- 373
Cdd:cd05924 164 VDAFGSSETG--FTGSGHSAGSGPETGpFTRANPDTVVLDDDGRVVPP-GSGGVGWIARRGHIPlGYYGDEAKTAETFpe 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 374 AGG--WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLV--PTCRLhdGLRptlfVTLA 449
Cdd:cd05924 241 VDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSH-PAVYDVLVVgrPDERW--GQE----VVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15596193 450 TPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
43-500 |
9.40e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 85.91 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLAL-NDSPSLACLfLACIAVGAIPAVINPKSREQALADIAADCQASLVVREADapsLSGPLAP- 119
Cdd:PRK12406 25 AGGLAALgVRPGDCVALLMrNDFAFFEAA-YAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD---LLHGLASa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 120 ----LTLRAAAGRP-LLDDFSLDA---LVGPADLDWSAFHRQDP-------AAACFLQYTSGSTGAPKGVMhslrntlgf 184
Cdd:PRK12406 101 lpagVTVLSVPTPPeIAAAYRISPallTPPAGAIDWEGWLAQQEpydgppvPQPQSMIYTSGTTGHPKGVR--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 185 cRAFATELLALQAGDR------------------LY-SIPKmffGYGM------GNSLFFPWFSgasallddtwpsPERV 239
Cdd:PRK12406 172 -RAAPTPEQAAAAEQMraliyglkpgiralltgpLYhSAPN---AYGLragrlgGVLVLQPRFD------------PEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 240 LENLVAFRPRVLFGVPAIYASL-----RPQARELLSSVRLAFSAGSPLP----RGEFEFWaahGLEICDGIGATEVGHVF 310
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLlklpeEVRAKYDVSSLRHVIHAAAPCPadvkRAMIEWW---GPVIYEYYGSTESGAVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 311 LA------NRPGqaradSTGLPLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSP-GYWRASEEQQARFAGGWYRTGDL 383
Cdd:PRK12406 313 FAtsedalSHPG-----TVGKAAPGAELRFVDEDGRPLPQ-GEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 384 FERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRhLPEVSE-AVL-VPTCRLHDGLRPTLFVTLATPLDdnqillAQ 461
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHA-VPGVHDcAVFgIPDAEFGEALMAVVEPQPGATLD------EA 459
|
490 500 510
....*....|....*....|....*....|....*....
gi 15596193 462 RIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
46-500 |
1.55e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 85.36 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 46 LARLLKPGDRV-VLALNDSPSLACLfLACIAVGAIPAVINPK-SREQaLADIAADCQASLVVR--------EADAPSLSG 115
Cdd:PRK07788 92 LALGVRAGDGVaVLARNHRGFVLAL-YAAGKVGARIILLNTGfSGPQ-LAEVAAREGVKALVYddeftdllSALPPDLGR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 PLAPLTLRAAAGRPLLDDFSLDALVGPADldwsafHRQDPAA---ACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATEL 192
Cdd:PRK07788 170 LRAWGGNPDDDEPSGSTDETLDDLIAGSS------TAPLPKPpkpGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 193 lALQAGDRLYSIPKMFFGYGMGNsLFFPWFSGASALL----DdtwpsPERVLENLVAFRPRVLFGVPAIYA---SLRPQA 265
Cdd:PRK07788 244 -PFRAGETTLLPAPMFHATGWAH-LTLAMALGSTVVLrrrfD-----PEATLEDIAKHKATALVVVPVMLSrilDLGPEV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 266 REL--LSSVRLAFSAGSPLPrGEF--EFWAAHGLEICDGIGATEVGHVFLANRPGQARADST-GLPLPGYECRLVDREGH 340
Cdd:PRK07788 317 LAKydTSSLKIIFVSGSALS-PELatRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTvGRPPKGVTVKILDENGN 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 341 TIEEaGRQGVLLVRGPGLSPGYWRASEEQQArfaGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICR 420
Cdd:PRK07788 396 EVPR-GVVGRIFVGNGFPFEGYTDGRDKQII---DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 421 HlPEVSEAVLVPTCRLHDGLRPTLFVTLA--TPLDDNQIllAQRIDQHLAEqipsHMLPSQLHVLPALPRNDNGKLARAE 498
Cdd:PRK07788 472 H-PDVVEAAVIGVDDEEFGQRLRAFVVKApgAALDEDAI--KDYVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKRE 544
|
..
gi 15596193 499 LR 500
Cdd:PRK07788 545 LR 546
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
157-488 |
2.08e-17 |
|
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: 83.51 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 157 AACFLQYTSGSTGAPKGVMHSLRNTLgfcrAFATELLALQAGDR---------LYSIPKMFFGYGM----GNSLFFPWFS 223
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALL----AQALVLAVLQAIDEgtvflnsgpLFHIGTLMFTLATfhagGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 224 gasallddtwpsPERVLENLVAFRPRVLFGVPAIYAslrpQAREL-------LSSVRlaFSAGSPLPRGEFEFWAAHGLE 296
Cdd:cd17636 77 ------------AEEVLELIEAERCTHAFLLPPTID----QIVELnadglydLSSLR--SSPAAPEWNDMATVDTSPWGR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 297 ICDGIGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG 376
Cdd:cd17636 139 KPGGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVP-DGEVGEIVARGPTVMAGYWNRPEVNARRTRGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 377 WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSEAVL--VPTCRLHDGLRpTLFVtlatpLDD 454
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCL-RQHPAVADAAVigVPDPRWAQSVK-AIVV-----LKP 290
|
330 340 350
....*....|....*....|....*....|....
gi 15596193 455 NQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPR 488
Cdd:cd17636 291 GASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-431 |
2.11e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 84.43 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP----KSREQALADIAADcqaslvvreadapslsgplapltlrAA 125
Cdd:cd05910 24 IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgmgrKNLKQCLQEAEPD-------------------------AF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLLDDfsldalvgpadldwsafhrqdPAAACFlqyTSGSTGAPKGVMHSLRNTLGFCRAFATeLLALQAGDRLYSIP 205
Cdd:cd05910 79 IGIPKADE---------------------PAAILF---TSGSTGTPKGVVYRHGTFAAQIDALRQ-LYGIRPGEVDLATF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 206 KMFfgygmgnSLFFPWFSGASAL--LDDTWP---SPERVLENLVAFRPRVLFGVPAIYASLR---PQARELLSSVRLAFS 277
Cdd:cd05910 134 PLF-------ALFGPALGLTSVIpdMDPTRParaDPQKLVGAIRQYGVSIVFGSPALLERVArycAQHGITLPSLRRVLS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 278 AGSPLPRG---EFEFWAAHGLEICDGIGATEV-------GHVFLANR---PGQARADSTGLPLPGYECRLVDREGHTIEE 344
Cdd:cd05910 207 AGAPVPIAlaaRLRKMLSDEAEILTPYGATEAlpvssigSRELLATTtaaTSGGAGTCVGRPIPGVRVRIIEIDDEPIAE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 345 --------AGRQGVLLVRGPGLSPGYWraSEEQQARFA-------GGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWV 409
Cdd:cd05910 287 wddtlelpRGEIGEITVTGPTVTPTYV--NRPVATALAkiddnseGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTL 364
|
410 420
....*....|....*....|..
gi 15596193 410 VPTQVEQAICRHlPEVSEAVLV 431
Cdd:cd05910 365 YTEPVERVFNTH-PGVRRSALV 385
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
46-409 |
5.71e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.94 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 46 LARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINP-----KSREQALADIAADCQASLVVREaDAPSLSGPLAPL 120
Cdd:PRK12582 98 LDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPayslmSHDHAKLKHLFDLVKPRVVFAQ-SGAPFARALAAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 121 TL---------RAAAGRPLLddfSLDALVG--PADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMhslrNTLGFCRAFA 189
Cdd:PRK12582 177 DLldvtvvhvtGPGEGIASI---AFADLAAtpPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVI----NTQRMMCANI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 190 TELLALQAGDRLYSIPKMF--------FGygmGNSLFFP-WFSGASALLDDTWPSP---ERVLENLVAFRPRVLFGVPAI 257
Cdd:PRK12582 250 AMQEQLRPREPDPPPPVSLdwmpwnhtMG---GNANFNGlLWGGGTLYIDDGKPLPgmfEETIRNLREISPTVYGNVPAG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 258 YASLRPQ-------ARELLSSVRLAFSAGSPLPRGEFEFWAA-------HGLEICDGIGATE-----VGHVFLANRPGQA 318
Cdd:PRK12582 327 YAMLAEAmekddalRRSFFKNLRLMAYGGATLSDDLYERMQAlavrttgHRIPFYTGYGATEtapttTGTHWDTERVGLI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 319 radstGLPLPGYECRLVDrEGHTIEeagrqgvLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGD----LFERDESGAYR 393
Cdd:PRK12582 407 -----GLPLPGVELKLAP-VGDKYE-------VRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDaarfVDPDDPEKGLI 473
|
410
....*....|....*..
gi 15596193 394 HCGREDDLFKV-NGRWV 409
Cdd:PRK12582 474 FDGRVAEDFKLsTGTWV 490
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
36-500 |
6.25e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 83.41 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 36 RTY--ILSQASQLARL-----LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREA 108
Cdd:PRK08276 12 VTYgeLEARSNRLAHGlralgLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 109 DapslsgpLAPLTLRAAAGRPL-LDDFSLDALVGPADLDWSAFHRQDPA-------AACFLQYTSGSTGAPKGVmhslrn 180
Cdd:PRK08276 92 A-------LADTAAELAAELPAgVPLLLVVAGPVPGFRSYEEALAAQPDtpiadetAGADMLYSSGTTGRPKGI------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 181 tlgfcRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFP----------WFSGASAL-----LDDTWpSPERVLENLVA 245
Cdd:PRK08276 159 -----KRPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPaplyhtaplrFGMSALALggtvvVMEKF-DAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 246 FRPRVLFGVPAIYA---SLRPQAREL--LSSVRLAFSAGSPLP----RGEFEFWaahGLEICDGIGATEVGHVFLAN--- 313
Cdd:PRK08276 233 YRVTHSQLVPTMFVrmlKLPEEVRARydVSSLRVAIHAAAPCPvevkRAMIDWW---GPIIHEYYASSEGGGVTVITsed 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 ---RPGqaradSTGLPLPGyECRLVDREGhtiEE--AGRQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERD 387
Cdd:PRK08276 310 wlaHPG-----SVGKAVLG-EVRILDEDG---NElpPGEIGTVYFEMDGYPFEYHNDPEKtAAARNPHGWVTVGDVGYLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL--VPtcrlHD--GLRPTLFVTLATPLDDNQiLLAQRI 463
Cdd:PRK08276 381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTH-PKVADVAVfgVP----DEemGERVKAVVQPADGADAGD-ALAAEL 454
|
490 500 510
....*....|....*....|....*....|....*..
gi 15596193 464 DQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
160-504 |
6.88e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 83.29 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 FLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELlALQAGDRLySIPKMF----FGYGMGNSLFFpwfsGASALLDDTWpS 235
Cdd:PRK07638 147 YMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDF-HMKREDSV-LIAGTLvhslFLYGAISTLYV----GQTVHLMRKF-I 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 236 PERVLENLVAFRPRVLFGVPAIYASLRpQARELLSSVRLAFSAGSPLPRGE-------------FEFWaahgleicdgiG 302
Cdd:PRK07638 220 PNQVLDKLETENISVMYTVPTMLESLY-KENRVIENKMKIISSGAKWEAEAkekiknifpyaklYEFY-----------G 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVGHV-FLANRPGQARADSTGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTG 381
Cdd:PRK07638 288 ASELSFVtALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQ-KGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 382 DLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVtlatplDDNQIllAQ 461
Cdd:PRK07638 367 DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEH-PAVDEIVVIGVPDSYWGEKPVAII------KGSAT--KQ 437
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15596193 462 RIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLAD 504
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
160-409 |
1.42e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 82.72 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 FLQYTSGSTGAPKGVMHslrnTLGfcrAFATELLALqaGDRLYS-IPKM--------------FFGYGMGNSLFFP---- 220
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMH----THG---SLTAGILAL--EDRLNDlIGPPeedetycsylplahIMEFGVTNIFLARgali 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 221 WFSGASALLDDTwpspERVLENLVAFRPRVLFGVPAIY--------ASLRP----------------------------- 263
Cdd:PTZ00216 339 GFGSPRTLTDTF----ARPHGDLTEFRPVFLIGVPRIFdtikkaveAKLPPvgslkrrvfdhayqsrlralkegkdtpyw 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 264 ------QARELLSS-VRLAFSAGSPLPRGEFEFwaahgLEICDGI-----GATE---VGHVflaNRPGQARADSTGLPLP 328
Cdd:PTZ00216 415 nekvfsAPRAVLGGrVRAMLSGGGPLSAATQEF-----VNVVFGMviqgwGLTEtvcCGGI---QRTGDLEPNAVGQLLK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 329 GYECRLVDREG--HTIEEAGRqGVLLVRGPGLSPGYWRaSEEQ--QARFAGGWYRTGDLFERDESGAYRHCGREDDLFK- 403
Cdd:PTZ00216 487 GVEMKLLDTEEykHTDTPEPR-GEILLRGPFLFKGYYK-QEELtrEVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKn 564
|
....*.
gi 15596193 404 VNGRWV 409
Cdd:PTZ00216 565 CLGEYI 570
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
46-493 |
1.87e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.86 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 46 LARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAdapSLSGPLAPLTLRAA 125
Cdd:PRK07798 46 IAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYER---EFAPRVAEVLPRLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLL---DDFSLDALVGPADLDwSAFHRQDPAAA--------CFLQYTSGSTGAPKGVM---HSLRNTLGFCRAFAT- 190
Cdd:PRK07798 123 KLRTLVvveDGSGNDLLPGAVDYE-DALAAGSPERDfgerspddLYLLYTGGTTGMPKGVMwrqEDIFRVLLGGRDFATg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 191 ------ELLALQA----GDRLYSIPKMFFGYGMgNSLFFPWFSGASA-LLDDTWPSPERVLENLVAFRPRVLFGVPAIYA 259
Cdd:PRK07798 202 epiedeEELAKRAaagpGMRRFPAPPLMHGAGQ-WAAFAALFSGQTVvLLPDVRFDADEVWRTIEREKVNVITIVGDAMA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 260 slRPQAREL-------LSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVGhvFLANRPGQARADSTGLPL--P 328
Cdd:PRK07798 281 --RPLLDALeargpydLSSLFAIASGGALFSPSVKEALLELlpNVVLTDSIGSSETG--FGGSGTVAKGAVHTGGPRftI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 329 GYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF--AGG--WYRTGDLFERDESGAYRHCGRedDLFKV 404
Cdd:PRK07798 357 GPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTITLLGR--GSVCI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 405 N--GRWVVPTQVEQAICRHlPEVSEAVLV--PTCRLhdGLRPTLFVTLAtplDDNQILLAQrIDQHLAEQIPSHMLPSQL 480
Cdd:PRK07798 435 NtgGEKVFPEEVEEALKAH-PDVADALVVgvPDERW--GQEVVAVVQLR---EGARPDLAE-LRAHCRSSLAGYKVPRAI 507
|
490
....*....|...
gi 15596193 481 HVLPALPRNDNGK 493
Cdd:PRK07798 508 WFVDEVQRSPAGK 520
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
154-416 |
2.07e-16 |
|
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: 81.88 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 154 DPAAACFLQYTSGSTGAPKGVMHSLRN---TLGFCRAFATELLALQAGDRLYS---IPKMF----------FGYGMGnsl 217
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNivsNVAGVFKILEILNKINPTDVYISylpLAHIFervvealflyHGAKIG--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 ffpWFSGASALLddtwpspervLENLVAFRPRVLFGVPAIY-----------------------ASLRPQARELLSS--- 271
Cdd:cd05927 189 ---FYSGDIRLL----------LDDIKALKPTVFPGVPRVLnriydkifnkvqakgplkrklfnFALNYKLAELRSGvvr 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 272 --------------------VRLAFSAGSPLPRGEFEFW-AAHGLEICDGIGATE-VGHVFLaNRPGQARADSTGLPLPG 329
Cdd:cd05927 256 aspfwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLrVALGCPVLEGYGQTEcTAGATL-TLPGDTSVGHVGGPLPC 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 330 YECRLVDreghtIEEAG-------RQGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGREDDL 401
Cdd:cd05927 335 AEVKLVD-----VPEMNydakdpnPRGEVCIRGPNVFSGYYKDPEKtAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNI 409
|
330
....*....|....*.
gi 15596193 402 FK-VNGRWVVPTQVEQ 416
Cdd:cd05927 410 FKlSQGEYVAPEKIEN 425
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
18-499 |
2.99e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.52 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQcrtyILSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQAL 92
Cdd:PRK05691 2202 PQAPALTFAGQTLSYAE----LDARANRLARALRergvgPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQASLVVREADAPSLSGPLApltlrAAAGR-PLLDDFSLDALVGPADLDWSAFhrqdPAAACFLQYTSGSTGAP 171
Cdd:PRK05691 2278 HYMIEDSGIGLLLSDRALFEALGELP-----AGVARwCLEDDAAALAAYSDAPLPFLSL----PQHQAYLIYTSGSTGKP 2348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 172 KGVMHSLRNTLGFCRAfATELLALQAGD---RLYSIPkmfFGyGMGNSLFFPWFSGASALL--DDTWPSPErvLENLVAF 246
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQA-VIERFGMRADDcelHFYSIN---FD-AASERLLVPLLCGARVVLraQGQWGAEE--ICQLIRE 2421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 247 RPRVLFGVPAIYASLRPQ---ARELLSSVRLAFSAGSPLP-------RGEFE---FWAAHGleicdgigATEVGHVFLAN 313
Cdd:PRK05691 2422 QQVSILGFTPSYGSQLAQwlaGQGEQLPVRMCITGGEALTgehlqriRQAFApqlFFNAYG--------PTETVVMPLAC 2493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 R-PGQARADSTGLPLPgyecRLV-DREGHTIEE------AGRQGVLLVRGPGLSPGYWRASEEQQARF--------AGGW 377
Cdd:PRK05691 2494 LaPEQLEEGAASVPIG----RVVgARVAYILDAdlalvpQGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaadGGRL 2569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 378 YRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA-VLVPTCRLHDGLRPTLFVTLATPLDDNQ 456
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEH-PAVREAvVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15596193 457 ILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
149-502 |
5.69e-16 |
|
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: 80.65 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 149 AFHRQDPAAacFLQYTSGSTGAPKGVMHSLRN---TLGFCRAfATELLALQAGDRLYSIPKMFFGYGMGNSLFFpWFSGA 225
Cdd:cd17642 179 SFDRDEQVA--LIMNSSGSTGLPKGVQLTHKNivaRFSHARD-PIFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LICGF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 226 SALLDDTWpSPERVLENLVAFRPRVLFGVPAIYASLRPQA---RELLSSVRLAFSAGSPLPRGEFEFWAAH-GLE-ICDG 300
Cdd:cd17642 255 RVVLMYKF-EEELFLRSLQDYKVQSALLVPTLFAFFAKSTlvdKYDLSNLHEIASGGAPLSKEVGEAVAKRfKLPgIRQG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 301 IGATEVGHVFLANRPGQARADSTGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYR 379
Cdd:cd17642 334 YGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLH 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 380 TGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATplddNQILL 459
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH-PKIFDAGVAGIPDEDAGELPAAVVVLEA----GKTMT 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15596193 460 AQRIDQHLAEQI-PSHMLPSQLHVLPALPRNDNGKLARAELRHL 502
Cdd:cd17642 489 EKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
27-500 |
6.63e-16 |
|
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: 80.09 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQCRTYILSQASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVV 105
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLgLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 106 readapslsgplapltlraaagrpllddfsldalvgpadldwsafhrqdpAAACFLQYTSGSTGAPKGVMHSLRNTLGFC 185
Cdd:cd05940 81 --------------------------------------------------VDAALYIYTSGTTGLPKAAIISHRRAWRGG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 186 RAFATELLALQAgDRLYSIPKMFFG----YGMGNSLFfpwfSGASALLDDTWPS----PERVLENLVAFR-----PRVLF 252
Cdd:cd05940 111 AFFAGSGGALPS-DVLYTCLPLYHStaliVGWSACLA----SGATLVIRKKFSAsnfwDDIRKYQATIFQyigelCRYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 253 GVPAiyaslRPQAREllSSVRLAFSAGSplpRGEF--EFWAAHGL-EICDGIGATEvGHVFLANRPGQARA--DSTGLPL 327
Cdd:cd05940 186 NQPP-----KPTERK--HKVRMIFGNGL---RPDIweEFKERFGVpRIAEFYAATE-GNSGFINFFGKPGAigRNPSLLR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 328 PGYECRLV-----------DREGHTIEEA-GRQGVLLVRGPGLSP--GYW--RASEEQQAR--FAGG--WYRTGDLFERD 387
Cdd:cd05940 255 KVAPLALVkydlesgepirDAEGRCIKVPrGEPGLLISRINPLEPfdGYTdpAATEKKILRdvFKKGdaWFNTGDLMRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 388 ESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA----VLVPTcrlHDGLRPTLFVTLATPLDDNQILLAQRI 463
Cdd:cd05940 335 GEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAF-PGVEEAnvygVQVPG---TDGRAGMAAIVLQPNEEFDLSALAAHL 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 15596193 464 DQHLaeqiPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05940 411 EKNL----PGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
145-508 |
6.93e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 80.25 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 145 LDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAfATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSG 224
Cdd:PRK06334 172 MRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 225 ASALLDDTWPSPERVLENLVAFRPRVLFGVPAIYASLRPQARE---LLSSVRLAFSAGSPLP---RGEFEFWAAHgLEIC 298
Cdd:PRK06334 251 VPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKqesCLPSLRFVVIGGDAFKdslYQEALKTFPH-IQLR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 DGIGATEVGHVFLANRPGQARADS-TGLPLPGYECRLVDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG- 376
Cdd:PRK06334 330 QGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGe 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 377 -WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRH--LPEVSEAVLVPTCRL-HDGLRPTLFVTLATPL 452
Cdd:PRK06334 410 tWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgQNAADHAGPLVVCGLpGEKVRLCLFTTFPTSI 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596193 453 DD-NQILLAQRIDqhlaeqipSHMLPSQLHVLPALPRNDNGKLARAELRHLADTLYH 508
Cdd:PRK06334 490 SEvNDILKNSKTS--------SILKISYHHQVESIPMLGTGKPDYCSLNALAKSLFG 538
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
160-494 |
1.49e-15 |
|
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: 78.98 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 160 FLQYTSGSTGAPKGVMHSLRNTLGFCRafatellalqagdrlySIPKMFFGYGMGNS--LFFpwfsgASALLDdtwPSPE 237
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGSVVNLRT----------------SLSERYFGRDNGDEavLFF-----SNYVFD---FFVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 238 RVL------ENLVAFRPRVLFGVPAIYASLRPQARELLS---SV--RLAFSAGSPLPR----GEfEFWAAH--------- 293
Cdd:cd17648 154 QMTlallngQKLVVPPDEMRFDPDRFYAYINREKVTYLSgtpSVlqQYDLARLPHLKRvdaaGE-EFTAPVfeklrsrfa 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 294 GLeICDGIGATEVGhVFLANR--PGQARAD-STGLPLPGYECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWR------ 364
Cdd:cd17648 233 GL-IINAYGPTETT-VTNHKRffPGDQRFDkSLGRPVRNTKCYVLNDAMKRVP-VGAVGELYLGGDGVARGYLNrpelta 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 365 --------ASEEQQARFAGG-WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCR 435
Cdd:cd17648 310 erflpnpfQTEQERARGRNArLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASY-PGVRECAVVAKED 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 436 LHDGLRPTLFVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKL 494
Cdd:cd17648 389 ASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
164-505 |
4.77e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 76.62 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHSLRNTLGfcRAFATE---------LLALQAgdrlYSIPKM-------FFGY-----GMGNSLFFPWF 222
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTA--SADATHdrlggpgqwLLALPA----HHIAGLqvlvrsvIAGSepvelDVSAGFDPTAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 223 SGASALLddtwpSPERVLENLVAFRPRVLFGVPAIYASLRpqareLLSSVRLAfsaGSPLPRGEFEFWAAHGLEICDGIG 302
Cdd:PRK07824 117 PRAVAEL-----GGGRRYTSLVPMQLAKALDDPAATAALA-----ELDAVLVG---GGPAPAPVLDAAAAAGINVVRTYG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEV--GHVFlanrpgqaradsTGLPLPGYECRLVDreghtieeagrqGVLLVRGPGLSPGYwRASEEQQARFAGGWYRT 380
Cdd:PRK07824 184 MSETsgGCVY------------DGVPLDGVRVRVED------------GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 381 GDLFERDeSGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL--VPTCRLhdGLRPT-LFVTLATPLDDNQI 457
Cdd:PRK07824 239 DDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATH-PAVADCAVfgLPDDRL--GQRVVaAVVGDGGPAPTLEA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15596193 458 LLAqridqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLADT 505
Cdd:PRK07824 315 LRA-----HVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
43-500 |
4.84e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 77.71 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAdapSLSGPLAPLT 121
Cdd:PLN02246 64 AAGLHKLgIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS---CYVDKLKGLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 122 LRAAAGRPLLDD-------FSLDALVGPADLDWSAFHRQDPAAacfLQYTSGSTGAPKGVMHSLRntlGFCRAFATEL-- 192
Cdd:PLN02246 141 EDDGVTVVTIDDppegclhFSELTQADENELPEVEISPDDVVA---LPYSSGTTGLPKGVMLTHK---GLVTSVAQQVdg 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 193 ----LALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLddTWPSPE--RVLENLVAFRPRVLFGVPAIYASL--RPQ 264
Cdd:PLN02246 215 enpnLYFHSDDVILCVLPMFHIYSL-NSVLLCGLRVGAAIL--IMPKFEigALLELIQRHKVTIAPFVPPIVLAIakSPV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 265 -ARELLSSVRLAFSAGSPLprgefefwaahGLEICD-------------GIGATEVGHVF-----LANRPGQARADSTGL 325
Cdd:PLN02246 292 vEKYDLSSIRMVLSGAAPL-----------GKELEDafraklpnavlgqGYGMTEAGPVLamclaFAKEPFPVKSGSCGT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREghTIEEAGRQ--GVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLF 402
Cdd:PLN02246 361 VVRNAELKIVDPE--TGASLPRNqpGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELI 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 403 KVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLAtplDDNQIlLAQRIDQHLAEQIPSHMLPSQLHV 482
Cdd:PLN02246 439 KYKGFQVAPAELEALLISH-PSIADAAVVPMKDEVAGEVPVAFVVRS---NGSEI-TEDEIKQFVAKQVVFYKRIHKVFF 513
|
490
....*....|....*...
gi 15596193 483 LPALPRNDNGKLARAELR 500
Cdd:PLN02246 514 VDSIPKAPSGKILRKDLR 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1-500 |
5.30e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 77.37 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 1 MSTLANLteVLFRLDfDPDTAVyHYRGQTLSRLQCRTYILSQASQLARLLKPGDR--VVLALNDSPSLACLFLACIAVGA 78
Cdd:PRK13388 2 RDTIAQL--LRDRAG-DDTIAV-RYGDRTWTWREVLAEAAARAAALIALADPDRPlhVGVLLGNTPEMLFWLAAAALGGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 79 IPAVINPKSREQALA-DIA-ADCQaslvvreadapslsgplapLTLRAAAGRPLLDDFSLDALV-----GPADLDWSAFH 151
Cdd:PRK13388 78 VLVGLNTTRRGAALAaDIRrADCQ-------------------LLVTDAEHRPLLDGLDLPGVRvldvdTPAYAELVAAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 152 RQ-------DPAAACFLQYTSGSTGAPKGVMHSlRNTLGFCRAFATELLALQAGDRLYSIPKMFFGygmgNSLFFPW--- 221
Cdd:PRK13388 139 GAltphrevDAMDPFMLIFTSGTTGAPKAVRCS-HGRLAFAGRALTERFGLTRDDVCYVSMPLFHS----NAVMAGWapa 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 222 -FSGASALLDDTWpSPERVLENLVAFRPRVL--FGVPAIYASLRP-QARELLSSVRLAF--SAGsplPRGEFEFWAAHGL 295
Cdd:PRK13388 214 vASGAAVALPAKF-SASGFLDDVRRYGATYFnyVGKPLAYILATPeRPDDADNPLRVAFgnEAS---PRDIAEFSRRFGC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 296 EICDGIGATEvGHVFLANRPGQARAdSTGLPLPGYEcrLVDreGHTIEEAGR-----QGVLL-----------VRGPGLS 359
Cdd:PRK13388 290 QVEDGYGSSE-GAVIVVREPGTPPG-SIGRGAPGVA--IYN--PETLTECAVarfdaHGALLnadeaigelvnTAGAGFF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 360 PGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVL--VPTCRLH 437
Cdd:PRK13388 364 EGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRH-PAINRVAVyaVPDERVG 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 438 DGlrptlfVTLATPLDDNQILLAQRIDQHLAEQ--IPSHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK13388 443 DQ------VMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
150-499 |
5.37e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 77.13 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 150 FHRQDPAAACFLQYTSGSTGAPKGVM--HS--LRNTLGFCrafatELLALQAGDRLYSIPKMFFGYGMGNsLFFPWFSGA 225
Cdd:cd17654 112 FNIRTDECLAYVIHTSGTTGTPKIVAvpHKciLPNIQHFR-----SLFNITSEDILFLTSPLTFDPSVVE-IFLSLSSGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 226 SALlddTWPSPERVLENLVA------FRPRVLFGVPAIY-----ASLRPQARELLSSVRLAFSAGSPLPRG-EFEFWAAH 293
Cdd:cd17654 186 TLL---IVPTSVKVLPSKLAdilfkrHRITVLQATPTLFrrfgsQSIKSTVLSATSSLRVLALGGEPFPSLvILSSWRGK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 294 G--LEICDGIGATEVGHVFLANR-PGQARADSTGLPLPGYECRLVDREGHTIeeagrQGVLLVRgpGLSPGYWRASEEQQ 370
Cdd:cd17654 263 GnrTRIFNIYGITEVSCWALAYKvPEEDSPVQLGSPLLGTVIEVRDQNGSEG-----TGQVFLG--GLNRVCILDDEVTV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 371 ARfaGGWYRTGDLFERDESGAYrHCGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLvptcrLHDGLRPTLFVTLaT 450
Cdd:cd17654 336 PK--GTMRATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-----LSDQQRLIAFIVG-E 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15596193 451 PLDDnqillaqRIDQHL-AEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17654 407 SSSS-------RIHKELqLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
6-494 |
1.45e-14 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 76.37 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 6 NLTEVLFRLDFDPDTAVYHYR----GQTLSRLQCRtyilSQASQLARLLK-----PGDRVVLALNDSPSLACLFLACIAV 76
Cdd:PRK03584 87 NYAENLLRHRRDDRPAIIFRGedgpRRELSWAELR----RQVAALAAALRalgvgPGDRVAAYLPNIPETVVAMLATASL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 77 GAIPAVINPKSREQALAD----------IAA----------DCQAslVVRE--ADAPSLsgplapltlRAAAGRPLLDDf 134
Cdd:PRK03584 163 GAIWSSCSPDFGVQGVLDrfgqiepkvlIAVdgyryggkafDRRA--KVAElrAALPSL---------EHVVVVPYLGP- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 135 SLDALVGPADLDWSAFHRQDPAAAC-FLQ----------YTSGSTGAPKGVMHS----LRNTLgfcrafatELLALQ--- 196
Cdd:PRK03584 231 AAAAAALPGALLWEDFLAPAEAAELeFEPvpfdhplwilYSSGTTGLPKCIVHGhggiLLEHL--------KELGLHcdl 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 197 -AGDRLysipkMFF---GYGMGNSLFFPWFSGASALLDD---TWPSPErVLENLVAfRPRV-LFGVPAIY------ASLR 262
Cdd:PRK03584 303 gPGDRF-----FWYttcGWMMWNWLVSGLLVGATLVLYDgspFYPDPN-VLWDLAA-EEGVtVFGTSAKYldacekAGLV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 263 PQARELLSSVRLAFSAGSPLPRGEFEFWAAH---GLEICDGIGATEV------GHVFLANRPG--QARadstGLplpGYE 331
Cdd:PRK03584 376 PGETHDLSALRTIGSTGSPLPPEGFDWVYEHvkaDVWLASISGGTDIcscfvgGNPLLPVYRGeiQCR----GL---GMA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 332 CRLVDREGHTIeeAGRQGVLLVRGPGLS-P-GYWRASEEQQ------ARFAGGWyRTGDLFERDESGAYRHCGREDDLFK 403
Cdd:PRK03584 449 VEAWDEDGRPV--VGEVGELVCTKPFPSmPlGFWNDPDGSRyrdayfDTFPGVW-RHGDWIEITEHGGVVIYGRSDATLN 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 404 VNG---------RwvvptQVEQaicrhLPEVSEAVLVPTCRLHDGLRPTLFVTLA--TPLDDNqilLAQRIDQHLAEQI- 471
Cdd:PRK03584 526 RGGvrigtaeiyR-----QVEA-----LPEVLDSLVIGQEWPDGDVRMPLFVVLAegVTLDDA---LRARIRTTIRTNLs 592
|
570 580
....*....|....*....|...
gi 15596193 472 PSHmLPSQLHVLPALPRNDNGKL 494
Cdd:PRK03584 593 PRH-VPDKIIAVPDIPRTLSGKK 614
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
27-500 |
1.53e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.82 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 27 GQTLSRLQcrtyILSQASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQA 101
Cdd:PRK13390 22 GEQVSYRQ----LDDDSAALARVLydaglRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 102 SLVVREADAPSLSGPL-APLTLRAAAGRPLlDDF-SLDALVGPADLDWSafhrQDPAAACFLqYTSGSTGAPKGVMHSLr 179
Cdd:PRK13390 98 RVLVASAALDGLAAKVgADLPLRLSFGGEI-DGFgSFEAALAGAGPRLT----EQPCGAVML-YSSGTTGFPKGIQPDL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 180 ntlgfcrafaTELLALQAGDRLYSIPKMFFGYGMGNSLF----------FPWFS-----GASALLDDTWPSPErVLENLV 244
Cdd:PRK13390 171 ----------PGRDVDAPGDPIVAIARAFYDISESDIYYssapiyhaapLRWCSmvhalGGTVVLAKRFDAQA-TLGHVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 245 AFRPRVLFGVPAIYASL-----RPQARELLSSVRLAFSAGSPLP---RGEFEFWAahGLEICDGIGATEV-GHVFLANRP 315
Cdd:PRK13390 240 RYRITVTQMVPTMFVRLlkldaDVRTRYDVSSLRAVIHAAAPCPvdvKHAMIDWL--GPIVYEYYSSTEAhGMTFIDSPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 316 GQARADSTGLPLPGyECRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASE---EQQARFAGGWYRTGDLFERDESGAY 392
Cdd:PRK13390 318 WLAHPGSVGRSVLG-DLHICDDDGNELP-AGRIGTVYFERDRLPFRYLNDPEktaAAQHPAHPFWTTVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 393 RHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILLAQRIDqHLAEQIP 472
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMH-PAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELID-YTRSRIA 473
|
490 500
....*....|....*....|....*...
gi 15596193 473 SHMLPSQLHVLPALPRNDNGKLARAELR 500
Cdd:PRK13390 474 HYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
43-503 |
8.78e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 73.83 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLaclFLACIAVGAIPAV---INPKSREQALADIAADCQASLVV--RE-----ADAP 111
Cdd:PRK08162 57 ASALARRgIGRGDTVAVLLPNIPAM---VEAHFGVPMAGAVlntLNTRLDAASIAFMLRHGEAKVLIvdTEfaevaREAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 112 SLSGPLAPLT----LRAAAGRPLLDDFSLDALV--GPADLDWSAfhRQDPAAACFLQYTSGSTGAPKGVMHSLRntlGFC 185
Cdd:PRK08162 134 ALLPGPKPLVidvdDPEYPGGRFIGALDYEAFLasGDPDFAWTL--PADEWDAIALNYTSGTTGNPKGVVYHHR---GAY 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 186 RAFATELLALQAGDR---LYSIPkMFFGYGMGnslfFPWFSGASA----LLddTWPSPERVLENLVAFRPRVLFGVPAIY 258
Cdd:PRK08162 209 LNALSNILAWGMPKHpvyLWTLP-MFHCNGWC----FPWTVAARAgtnvCL--RKVDPKLIFDLIREHGVTHYCGAPIVL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 259 ASL---RPQARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEV-GHVFL-------ANRPGQARADST---G 324
Cdd:PRK08162 282 SALinaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETyGPATVcawqpewDALPLDERAQLKarqG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 325 LPLPGYE-CRLVDREghTIEEAGR----QGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGRED 399
Cdd:PRK08162 362 VRYPLQEgVTVLDPD--TMQPVPAdgetIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 400 DLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPtcrLHD---GLRPTLFVTLAtpldDNQILLAQRIDQHLAEQIPSHML 476
Cdd:PRK08162 440 DIIISGGENISSIEVEDVLYRH-PAVLVAAVVA---KPDpkwGEVPCAFVELK----DGASATEEEIIAHCREHLAGFKV 511
|
490 500
....*....|....*....|....*..
gi 15596193 477 PSQLhVLPALPRNDNGKLARAELRHLA 503
Cdd:PRK08162 512 PKAV-VFGELPKTSTGKIQKFVLREQA 537
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
39-436 |
1.49e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.91 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 39 ILSQASQLARL-LKPGDRV-VLALNDSPSLAClFLACIAVGAIPAVINPK-SREQALADIAAdCQASLVVREADAPSLSG 115
Cdd:PLN02860 42 VLSLAAGLLRLgLRNGDVVaIAALNSDLYLEW-LLAVACAGGIVAPLNYRwSFEEAKSAMLL-VRPVMLVTDETCSSWYE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 116 PLAPLTLRAAAGRPLLDDFSLDALV----------------GPADLDWsAFHRQDPAAACFlqyTSGSTGAPKGVMHSLR 179
Cdd:PLN02860 120 ELQNDRLPSLMWQVFLESPSSSVFIflnsflttemlkqralGTTELDY-AWAPDDAVLICF---TSGTTGRPKGVTISHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 180 ntlgfcrAFATELLALQAgdrlysipkmFFGYG------------------------M--GNSLFFPWFSGASALlddtw 233
Cdd:PLN02860 196 -------ALIVQSLAKIA----------IVGYGeddvylhtaplchigglssalamlMvgACHVLLPKFDAKAAL----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 234 pspERVLENLVAfrprVLFGVPAIYASL------------RPQARELLS-----SVRLAFSAGSPLPRGEFefWAAHGL- 295
Cdd:PLN02860 254 ---QAIKQHNVT----SMITVPAMMADLisltrksmtwkvFPSVRKILNgggslSSRLLPDAKKLFPNAKL--FSAYGMt 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 296 EICDGIGATEVgHVFLANRPGQA-----RADSTGLPLPGYECrlVDREGHTIE------EAGRQGVLLVRGPGLSPGYW- 363
Cdd:PLN02860 325 EACSSLTFMTL-HDPTLESPKQTlqtvnQTKSSSVHQPQGVC--VGKPAPHVElkigldESSRVGRILTRGPHVMLGYWg 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596193 364 RASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLV--PTCRL 436
Cdd:PLN02860 402 QNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQH-PGVASVVVVgvPDSRL 475
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
50-500 |
1.60e-13 |
|
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: 72.91 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAAdcqaslVVREADAPSLsgplapltlraaagrp 129
Cdd:cd05908 37 IKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLKLNK------VWNTLKNPYL---------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 130 LLDDFSLDalvgpadldwsafhrQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELlALQAGDRLYSIPKMFF 209
Cdd:cd05908 95 ITEEEVLC---------------ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRILSWMPLTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 210 GYGMGNSLFFPWFSGASALLDDT---------WPspERVLENLVAFRPRVLFGVPAIYASLRPQAREL--LSSVRLAFSA 278
Cdd:cd05908 159 DMGLIAFHLAPLIAGMNQYLMPTrlfirrpilWL--KKASEHKATIVSSPNFGYKYFLKTLKPEKANDwdLSSIRMILNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 279 GSPLPRG---EF-EFWAAHGLE-----ICDGIGATEVG------------------HVFLANR-PGQARADSTGL----- 325
Cdd:cd05908 237 AEPIDYElchEFlDHMSKYGLKrnailPVYGLAEASVGaslpkaqspfktitlgrrHVTHGEPePEVDKKDSECLtfvev 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 --PLPGYECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDL-FERDesGAYRHCGREDDL 401
Cdd:cd05908 317 gkPIDETDIRICDEDNKILPD-GYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLgFIRN--GRLVITGREKDI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 402 FKVNGRWVVPTQVEQAICRHLPEVSEAVLVptCRLHD----GLRPTLFVTLATPLDDnQILLAQRIDQHLAE----QIpS 473
Cdd:cd05908 394 IFVNGQNVYPHDIERIAEELEGVELGRVVA--CGVNNsntrNEEIFCFIEHRKSEDD-FYPLGKKIKKHLNKrggwQI-N 469
|
490 500
....*....|....*....|....*..
gi 15596193 474 HMLPSQlhvlpALPRNDNGKLARAELR 500
Cdd:cd05908 470 EVLPIR-----RIPKTTSGKVKRYELA 491
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
50-500 |
1.72e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 72.70 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 50 LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREA----DAPSLSGPLAPLTLRAA 125
Cdd:PLN02330 77 LRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygKVKGLGLPVIVLGEEKI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 126 AGRPLLDDFsLDALVGPAD-LDWSAFHRQDpaaACFLQYTSGSTGAPKGVMHSLRNTLG-FCRAfatellalqagdrLYS 203
Cdd:PLN02330 157 EGAVNWKEL-LEAADRAGDtSDNEEILQTD---LCALPFSSGTTGISKGVMLTHRNLVAnLCSS-------------LFS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 204 I-PKMFfgyGMGNSL-FFPWFS--GASALLDDTWPSPERV---------------LENLVAFRPRVlfgvPAIYASL--R 262
Cdd:PLN02330 220 VgPEMI---GQVVTLgLIPFFHiyGITGICCATLRNKGKVvvmsrfelrtflnalITQEVSFAPIV----PPIILNLvkN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 263 PQAREL-LSSVRL--AFSAGSPL-PRGEFEFWAAH-GLEICDGIGATEVGHVFLAN-RP----GQARADSTGLPLPGYEC 332
Cdd:PLN02330 293 PIVEEFdLSKLKLqaIMTAAAPLaPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHgDPekghGIAKKNSVGFILPNLEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 333 RLVDRE-GHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVV 410
Cdd:PLN02330 373 KFIDPDtGRSLPK-NTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 411 PTQVEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQillaQRIDQHLAEQIPSHMLPSQLHVLPALPRND 490
Cdd:PLN02330 452 PAELEAILLTH-PSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE----EDILNFVAANVAHYKKVRVVQFVDSIPKSL 526
|
490
....*....|
gi 15596193 491 NGKLARAELR 500
Cdd:PLN02330 527 SGKIMRRLLK 536
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
18-499 |
2.37e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 72.24 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 18 PDTAVYHYRGQTLSRLQCRTYILSQASQLARLLKPGDR--VVLALNDSPSLAClFLACIAVGA--IP-AVINPKSREQAL 92
Cdd:PRK04813 16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSpiIVFGHMSPEMLAT-FLGAVKAGHayIPvDVSSPAERIEMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAadcQASLVVREADAPSLSGPLAPLTLraaagrpllDDFSlDALVGPADLDWSAFHRQDPAAacFLQYTSGSTGAPK 172
Cdd:PRK04813 95 IEVA---KPSLIIATEELPLEILGIPVITL---------DELK-DIFATGNPYDFDHAVKGDDNY--YIIFTSGTTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVMHSLRNTLGF----CRAFAT----ELLA----------------LQAGDRLYSIPKmffgyGMGNS---LF--FP--- 220
Cdd:PRK04813 160 GVQISHDNLVSFtnwmLEDFALpegpQFLNqapysfdlsvmdlyptLASGGTLVALPK-----DMTANfkqLFetLPqlp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 221 ---WFSGAS----ALLDDTWPspERVLENLVAFrprvLFGVPAIYASlrpQARELLSsvrlafsagsplprgefEFWAAH 293
Cdd:PRK04813 235 invWVSTPSfadmCLLDPSFN--EEHLPNLTHF----LFCGEELPHK---TAKKLLE-----------------RFPSAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 294 gleICDGIGATE----VGHV-----FLANRP----GQARADSTglplpgyecRLVDREGHTIEEAGRQGVLLVRGPGLSP 360
Cdd:PRK04813 289 ---IYNTYGPTEatvaVTSIeitdeMLDQYKrlpiGYAKPDSP---------LLIIDEEGTKLPDGEQGEIVISGPSVSK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 361 GYWRASEEQQARF---AGGW-YRTGDLFERDEsGAYRHCGREDDLFKVNGRWVVPTQVEQAIcRHLPEVSEAVLVPTCRL 436
Cdd:PRK04813 357 GYLNNPEKTAEAFftfDGQPaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNL-RQSSYVESAVVVPYNKD 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 437 HDGLRPTLFVTLATPLDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK04813 435 HKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
42-507 |
3.44e-13 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 71.83 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 42 QASQLARLL-----KPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALA---DIAadcQASLVVREAD---- 109
Cdd:PRK08279 71 RANRYAHWAaargvGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAhslNLV---DAKHLIVGEElvea 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 110 ----APSLSGPLAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAA-ACFLQYTSGSTGAPKGVMHSLRNTLGF 184
Cdd:PRK08279 148 feeaRADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKdTAFYIYTSGTTGLPKAAVMSHMRWLKA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 185 CRAFAtELLALQAGDRLYSIPKMFFGYGM----------GNSLFF-PWFSgASALLDDTwpsperVLENLVAFR-----P 248
Cdd:PRK08279 228 MGGFG-GLLRLTPDDVLYCCLPLYHNTGGtvawssvlaaGATLALrRKFS-ASRFWDDV------RRYRATAFQyigelC 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 249 RVLFGVPAiyaslRPQAREllSSVRLAFSAGSplpRGEF--EFWAAHGLE-ICDGIGATE--VGHVFLANRPGqaradST 323
Cdd:PRK08279 300 RYLLNQPP-----KPTDRD--HRLRLMIGNGL---RPDIwdEFQQRFGIPrILEFYAASEgnVGFINVFNFDG-----TV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 324 GLpLPGYEC---RLV-----------DREGHTIE-EAGRQGVLLVRGPGLSP--GYWR--ASEEQQAR--FAGG--WYRT 380
Cdd:PRK08279 365 GR-VPLWLAhpyAIVkydvdtgepvrDADGRCIKvKPGEVGLLIGRITDRGPfdGYTDpeASEKKILRdvFKKGdaWFNT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 381 GDLFERDESGAYRHCGREDDLFkvngRW----VVPTQVEQAICRHlPEVSEAVL----VPTcrlHDG------LRPTLFV 446
Cdd:PRK08279 444 GDLMRDDGFGHAQFVDRLGDTF----RWkgenVATTEVENALSGF-PGVEEAVVygveVPG---TDGragmaaIVLADGA 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596193 447 TLatpldDNQILLAqridqHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA-------DTLY 507
Cdd:PRK08279 516 EF-----DLAALAA-----HLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGfdpskvdDPLY 573
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
148-506 |
5.84e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.20 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 148 SAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRntlGFCRAFATELLALQAGD---RLYSIPkMFFGygmgNSLFFPWFS- 223
Cdd:PLN03102 178 RMFRIQDEHDPISLNYTSGTTADPKGVVISHR---GAYLSTLSAIIGWEMGTcpvYLWTLP-MFHC----NGWTFTWGTa 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 224 --GASALLDDTWPSPErVLENLVAFRPRVLFGVPAIYASLRPQARELLS---SVRLAFSAGSPLPRGEFEFWAAHGLEIC 298
Cdd:PLN03102 250 arGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSprsGPVHVLTGGSPPPAALVKKVQRLGFQVM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 299 DGIGATE-VGHVFLA------NR-PG------QARADSTGLPLPGYECR------LVDREGHTIeeagrqGVLLVRGPGL 358
Cdd:PLN03102 329 HAYGLTEaTGPVLFCewqdewNRlPEnqqmelKARQGVSILGLADVDVKnketqeSVPRDGKTM------GEIVIKGSSI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 359 SPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTCRLHD 438
Cdd:PLN03102 403 MKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY-PKVLETAVVAMPHPTW 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596193 439 GLRPTLFVTL----ATPLDDNQILLAQRID--QHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLADTL 506
Cdd:PLN03102 482 GETPCAFVVLekgeTTKEDRVDKLVTRERDliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGL 555
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
163-499 |
8.69e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 70.16 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 163 YTSGSTGAPKGVM---HSLRN-TLGFCRAFatellALQAGDRLYSIPKMFFGYGMgNSLFFPWFSGASALLddtwpSPER 238
Cdd:cd17644 113 YTSGSTGKPKGVMiehQSLVNlSHGLIKEY-----GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATLVL-----RPEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 239 VLENLVAFRPRV------LFGVPAIY-----ASLRPQARELLSSVRLAFSAGSPLPRGEFEFWA---AHGLEICDGIGAT 304
Cdd:cd17644 182 MRSSLEDFVQYIqqwqltVLSLPPAYwhllvLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQknvGNFIQLINVYGPT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 305 EVG-----HVFLANRPGQARADSTGLPLPGYECRLVDREGHTIeEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGG--- 376
Cdd:cd17644 262 EATiaatvCRLTQLTERNITSVPIGRPIANTQVYILDENLQPV-PVGVPGELHIGGVGLARGYLNRPELTAEKFISHpfn 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 377 ------WYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVPTcrlHDGLRPTLFVTLAT 450
Cdd:cd17644 341 sseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQH-NDVKTAVVIVR---EDQPGNKRLVAYIV 416
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15596193 451 PLDDNQILLAQrIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:cd17644 417 PHYEESPSTVE-LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
22-383 |
1.89e-12 |
|
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: 69.79 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 22 VYHYRGQTLSRLQCRTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQA 101
Cdd:cd17632 62 LPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 102 SLVVREAD------APSLSGPlAPLTLRAAAGRPLLDDF--SLDALVGPA---------DLDWSAFHRQDPAAACF---- 160
Cdd:cd17632 142 RLLAVSAEhldlavEAVLEGG-TPPRLVVFDHRPEVDAHraALESARERLaavgipvttLTLIAVRGRDLPPAPLFrpep 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 161 -------LQYTSGSTGAPKGVMHSLRNTlgfcRAFATELLALQAGDRLYSIPKMFF-------------GYGMGNSLFFP 220
Cdd:cd17632 221 dddplalLIYTSGSTGTPKGAMYTERLV----ATFWLKVSSIQDIRPPASITLNFMpmshiagrislygTLARGGTAYFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 221 WFSGASALLDDtwpspervlenLVAFRPRVLFGVPAIY-------------------------ASLRPQARELLSSVRL- 274
Cdd:cd17632 297 AASDMSTLFDD-----------LALVRPTELFLVPRVCdmlfqryqaeldrrsvagadaetlaERVKAELRERVLGGRLl 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 275 -AFSAGSPLPrGEFEFWAAH--GLEICDGIGATEVGHVFLAN---RPgqaradstglplPGYECRLVDreghtIEEAGR- 347
Cdd:cd17632 366 aAVCGSAPLS-AEMKAFMESllDLDLHDGYGSTEAGAVILDGvivRP------------PVLDYKLVD-----VPELGYf 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15596193 348 -------QGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDL 383
Cdd:cd17632 428 rtdrphpRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDV 471
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
163-499 |
4.57e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 163 YTSGSTGAPKGVMHSLRNTLGfCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWFSGASALL-DDTWPSPERVLE 241
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLN-NQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVpNAIAHDPQGLLA 3954
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 242 NLVAFRPRVLFGVPAIYASLRPQARELLSSVRLAFSAGSPLPRGEFEFWAAH--GLEICDGIGATEVGHVFLANRPGQAR 319
Cdd:PRK05691 3955 HVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRypQIGLVNAYGPAECSDDVAFFRVDLAS 4034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 320 ADSTGLPL--PGYECRL-VDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARF------AGG--WYRTGDLFERDE 388
Cdd:PRK05691 4035 TRGSYLPIgsPTDNNRLyLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgAPGerLYRTGDLARRRS 4114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 389 SGAYRHCGREDDLFKVNGRWVVPTQVEqAICRHLPEVSEAVLVPTCRLHDGLRPTLFVTLATPLDDNQILlaQRIDQHLA 468
Cdd:PRK05691 4115 DGVLEYVGRIDHQVKIRGYRIELGEIE-ARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALL--ERIKQRLR 4191
|
330 340 350
....*....|....*....|....*....|.
gi 15596193 469 EQIPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK05691 4192 AELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
349-506 |
8.00e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.56 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 349 GVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEA 428
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTH-PAVLEA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 429 VLVptCRLHD--GLRPTLFVTLATPLD-DNQILLAQRIDQHLAEQIPSHMLPSQLhVLPALPRNDNGKLARAELRHLADT 505
Cdd:PLN02479 482 SVV--ARPDErwGESPCAFVTLKPGVDkSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLRAKAKE 558
|
.
gi 15596193 506 L 506
Cdd:PLN02479 559 M 559
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
43-430 |
2.18e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 66.06 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPK--SREQALADIAADCQASLVVREA--DAPSLSGPL 117
Cdd:PRK05852 57 AGQLTRSgLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPAlpIAEQRVRSQAAGARVVLIDADGphDRAEPTTRW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 118 APLTLRAAAGRPLLD---DFSLDALVGP-ADLDWSAFHRQDPAaacFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATell 193
Cdd:PRK05852 137 WPLTVNVGGDSGPSGgtlSVHLDAATEPtPATSTPEGLRPDDA---MIMFTGGTTGLPKMVPWTHANIASSVRAIIT--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 194 ALQAGDRLYSIPKM--FFGYGMGNSLFFPWFSGASALLddtwP-----SPERVLENLVAFRPRVLFGVPAIYASLRPQAR 266
Cdd:PRK05852 211 GYRLSPRDATVAVMplYHGHGLIAALLATLASGGAVLL----PargrfSAHTFWDDIKAVGATWYTAVPTIHQILLERAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 267 ELLS-----SVRLAFSAGSPLPRGEFEfwAAH---GLEICDGIGATEVGH-VFLANRPGQARAD----STGL--PLPGYE 331
Cdd:PRK05852 287 TEPSgrkpaALRFIRSCSAPLTAETAQ--ALQtefAAPVVCAFGMTEATHqVTTTQIEGIGQTEnpvvSTGLvgRSTGAQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 332 CRLVDREGHTIEeAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVP 411
Cdd:PRK05852 365 IRIVGSDGLPLP-AGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISP 443
|
410
....*....|....*....
gi 15596193 412 TQVEQAICRHlPEVSEAVL 430
Cdd:PRK05852 444 ERVEGVLASH-PNVMEAAV 461
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
331-503 |
2.62e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.78 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 331 ECRLVDREGHTIEEaGRQGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFKVNGRWV 409
Cdd:PRK10946 364 EVWVADADGNPLPQ-GEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKI 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 410 VPTQVEQAICRHlPEVSEAVLV--PTCRLhdGLRPTLFVTLATPLDdnqillAQRIDQHLAEQ-IPSHMLPSQLHVLPAL 486
Cdd:PRK10946 443 AAEEIENLLLRH-PAVIHAALVsmEDELM--GEKSCAFLVVKEPLK------AVQLRRFLREQgIAEFKLPDRVECVDSL 513
|
170
....*....|....*..
gi 15596193 487 PRNDNGKLARAELRHLA 503
Cdd:PRK10946 514 PLTAVGKVDKKQLRQWL 530
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
164-496 |
8.34e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 64.01 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHS---LRNTLG-FCRAFATelLALQAGDRLYsipkMFFGYGMGNSlFFPWFSGASAL--------LDD 231
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdLDRWAElFARSLRA--AGVRPGDRVQ----NAFGYGLFTG-GLGLHYGAERLgatvipagGGN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 232 TwpspERVLENLVAFRPRVLFGVPAiYA-SLRPQAREL-----LSSVRLAFSAGSPLP---RGEFEfwAAHGLEICDGIG 302
Cdd:COG1541 164 T----ERQLRLMQDFGPTVLVGTPS-YLlYLAEVAEEEgidprDLSLKKGIFGGEPWSeemRKEIE--ERWGIKAYDIYG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 303 ATEVGhvflanrpgqaradsTGLplpGYECR----LVDREGHTIEEA----------------------GRQGVLLVRgp 356
Cdd:COG1541 237 LTEVG---------------PGV---AYECEaqdgLHIWEDHFLVEIidpetgepvpegeegelvvttlTKEAMPLIR-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 357 glspgywraseeqqarfaggwYRTGDL--FERDESGayrhC-----------GREDDLFKVNGRWVVPTQVEQAICRHlP 423
Cdd:COG1541 297 ---------------------YRTGDLtrLLPEPCP----CgrthprigrilGRADDMLIIRGVNVFPSQIEEVLLRI-P 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596193 424 EVS-EAVLVPTcrlHDGLRPTLFVTLATPLDDNQILLAQRIDQHLAEQIpshMLPSQLHVLPA--LPRNDnGKLAR 496
Cdd:COG1541 351 EVGpEYQIVVD---REGGLDELTVRVELAPGASLEALAEAIAAALKAVL---GLRAEVELVEPgsLPRSE-GKAKR 419
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
93-499 |
8.90e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.90 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 93 ADIAADCQAslvVREADAPSLsgPLAPLTLRAAAGRPLLDDFSLDALVGPADLDWSAFHRQDPAAACFLQYTSGSTGAPK 172
Cdd:PRK08308 43 FDIITLVFF---LKEKGASVL--PIHPDTPKEAAIRMAKRAGCHGLLYGESDFTKLEAVNYLAEEPSLLQYSSGTTGEPK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 173 GVMhslrntlgfcRAFA---TELLA----LQAGDRLYSI---PkMFFGYGMgnslffpwFSGA-SALLDDTWPS------ 235
Cdd:PRK08308 118 LIR----------RSWTeidREIEAyneaLNCEQDETPIvacP-VTHSYGL--------ICGVlAALTRGSKPViitnkn 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 236 PERVLENLVAFRPRVLFGVPAIYASLrpqARELLSSVRL--AFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLAn 313
Cdd:PRK08308 179 PKFALNILRNTPQHILYAVPLMLHIL---GRLLPGTFQFhaVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSIC- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 314 rPGQARADSTGLPLPgyecrlvdregHTIEEAGRqgvllvrGPGlspgywrASEEQQARFAGGWYRTGDLFERDESGAYR 393
Cdd:PRK08308 255 -PDMKSHLDLGNPLP-----------HVSVSAGS-------DEN-------APEEIVVKMGDKEIFTKDLGYKSERGTLH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 394 HCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSEAVLVptcRLHD---GLRPTLFVTLATPLDDNQillaqrIDQHLAEQ 470
Cdd:PRK08308 309 FMGRMDDVINVSGLNVYPIEVEDVMLRL-PGVQEAVVY---RGKDpvaGERVKAKVISHEEIDPVQ------LREWCIQH 378
|
410 420
....*....|....*....|....*....
gi 15596193 471 IPSHMLPSQLHVLPALPRNDNGKLARAEL 499
Cdd:PRK08308 379 LAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
152-431 |
8.90e-11 |
|
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: 64.30 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 152 RQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSI----P---------KMFFGYGMGNSLf 218
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVvsylPlshiaaqilDIWLPIKVGGQV- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 219 fpWFSGASAL---LDDTwpspervlenLVAFRPRVLFGVPAIY-----------ASLRPQARELLS-------------- 270
Cdd:cd05933 225 --YFAQPDALkgtLVKT----------LREVRPTAFMGVPRVWekiqekmkavgAKSGTLKRKIASwakgvgletnlklm 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 271 --------SVRLA--------------------FSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQARADS 322
Cdd:cd05933 293 ggespsplFYRLAkklvfkkvrkalgldrcqkfFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 323 TGLPLPGYECRLV--DREGHtieeagrqGVLLVRGPGLSPGYWRASEE-QQARFAGGWYRTGDLFERDESGAYRHCGRED 399
Cdd:cd05933 373 CGKALPGCKTKIHnpDADGI--------GEICFWGRHVFMGYLNMEDKtEEAIDEDGWLHSGDLGKLDEDGFLYITGRIK 444
|
330 340 350
....*....|....*....|....*....|...
gi 15596193 400 DLFKV-NGRWVVPTQVEQAICRHLPEVSEAVLV 431
Cdd:cd05933 445 ELIITaGGENVPPVPIEDAVKKELPIISNAMLI 477
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
138-420 |
9.26e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 64.48 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 138 ALVGPADLDWSAFHRQDpaaACFLQYTSGSTGAPKGVMhsLRNTLGFCRAFATELLaLQAGDRLYSIPKMFFGYGMGNSL 217
Cdd:PLN02861 205 SLMGSLDCELPPKQKTD---ICTIMYTSGTTGEPKGVI--LTNRAIIAEVLSTDHL-LKVTDRVATEEDSYFSYLPLAHV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 F------FPWFSGASAlldDTWPSPERVL-ENLVAFRPRVLFGVPAIYASLRPQARELLSS------------------- 271
Cdd:PLN02861 279 YdqvietYCISKGASI---GFWQGDIRYLmEDVQALKPTIFCGVPRVYDRIYTGIMQKISSggmlrkklfdfaynyklgn 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 272 -----------------------------VRLAFSAGSPLPRGEFEFW---------AAHGL-EICDGIgATEVGHVFla 312
Cdd:PLN02861 356 lrkglkqeeasprldrlvfdkikeglggrVRLLLSGAAPLPRHVEEFLrvtscsvlsQGYGLtESCGGC-FTSIANVF-- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 313 nrpgqARADSTGLPLPGYECRL--VDREGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESG 390
Cdd:PLN02861 433 -----SMVGTVGVPMTTIEARLesVPEMGYDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNG 507
|
330 340 350
....*....|....*....|....*....|.
gi 15596193 391 AYRHCGREDDLFKVN-GRWVVPTQVEQAICR 420
Cdd:PLN02861 508 AMKIIDRKKNIFKLSqGEYVAVENLENTYSR 538
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
108-500 |
1.75e-10 |
|
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: 63.17 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 108 ADAPSLSGPLAPLTLRAAA----GRPLLDDFSL--DALVGPADLDWSAFHRQDP-----AAACFLQYTSGSTGAPKGVM- 175
Cdd:cd05929 66 GACPAYKSSRAPRAEACAIieikAAALVCGLFTggGALDGLEDYEAAEGGSPETpiedeAAGWKMLYSGGTTGRPKGIKr 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 176 -HSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSlFFPWFSGASALLDDTWpSPERVLeNLVAfRPRVLFG- 253
Cdd:cd05929 146 gLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWS-MTALFMGGTLVLMEKF-DPEEFL-RLIE-RYRVTFAq 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 254 -VPAIYASLRP-----QARELLSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGI-GATEvghvflanRPGQARADSTG-L 325
Cdd:cd05929 222 fVPTMFVRLLKlpeavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYyGGTE--------GQGLTIINGEEwL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREGHTIEEAGRQ------GVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGRED 399
Cdd:cd05929 294 THPGSVGRAVLGKVHILDEDGNEvppgeiGEVYFANGPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRS 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 400 DLFKVNGRWVVPTQVEQAICRHlPEVSEAVLV--PTCRLhdGLRPTLFVTLATPLDDNQILLAQRIDqHLAEQIPSHMLP 477
Cdd:cd05929 374 DMIISGGVNIYPQEIENALIAH-PKVLDAAVVgvPDEEL--GQRVHAVVQPAPGADAGTALAEELIA-FLRDRLSRYKCP 449
|
410 420
....*....|....*....|...
gi 15596193 478 SQLHVLPALPRNDNGKLARAELR 500
Cdd:cd05929 450 RSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
153-460 |
2.90e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 62.81 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 153 QDPAAACflqYTSGSTGAPKGVMHSLRNTLGFCrAFATELLALQAGD-------------RLYSIPKMFFGYGMGnslff 219
Cdd:PLN02736 221 EDVATIC---YTSGTTGTPKGVVLTHGNLIANV-AGSSLSTKFYPSDvhisylplahiyeRVNQIVMLHYGVAVG----- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 220 pWFSGAS-ALLDDtwpspervlenLVAFRPRVLFGVP----AIYASL---------------------RPQARE------ 267
Cdd:PLN02736 292 -FYQGDNlKLMDD-----------LAALRPTIFCSVPrlynRIYDGItnavkesgglkerlfnaaynaKKQALEngknps 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 268 --------------LLSSVRLAFSAGSPLPRGEFEFwaahgLEIC------DGIGATEVGHVFLANRPGQARADSTGLPL 327
Cdd:PLN02736 360 pmwdrlvfnkikakLGGRVRFMSSGASPLSPDVMEF-----LRICfggrvlEGYGMTETSCVISGMDEGDNLSGHVGSPN 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 328 PGYECRLVD--REGHTIEEAGR-QGVLLVRGPGLSPGYWRASEEQQARF-AGGWYRTGDLFERDESGAYRHCGREDDLFK 403
Cdd:PLN02736 435 PACEVKLVDvpEMNYTSEDQPYpRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFK 514
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596193 404 V-NGRWVVPTQVEQ--AICRhlpevseavLVPTCRLH-DGLRPTLfVTLATPldDNQILLA 460
Cdd:PLN02736 515 LaQGEYIAPEKIENvyAKCK---------FVAQCFVYgDSLNSSL-VAVVVV--DPEVLKA 563
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
414-493 |
5.61e-10 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 55.63 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 414 VEQAICRHlPEVSEAVLVPTCRLHDGLRPTLFVTLatplDDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGK 493
Cdd:pfam13193 2 VESALVSH-PAVAEAAVVGVPDELKGEAPVAFVVL----KPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
148-501 |
2.05e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.78 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 148 SAFHRQDPAAACFLQYTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGDRLYSIPKMFFGYGMGNSLFFPWfSGASA 227
Cdd:PRK05851 144 ASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAAL-AGAPL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 228 LLDDTWP---SPERVLENLVAFR------PRVLFGVPAIYASLRPQARelLSSVRLAFSAGSPLPRGEFEFWAAH----G 294
Cdd:PRK05851 223 WLAPTTAfsaSPFRWLSWLSDSRatltaaPNFAYNLIGKYARRVSDVD--LGALRVALNGGEPVDCDGFERFATAmapfG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 295 LE---ICDGIGATEVGHVFLANRPGQ-ARADST--------------GLPLPGYECRLVDREGhTIEEAGRQ-GVLLVRG 355
Cdd:PRK05851 301 FDagaAAPSYGLAESTCAVTVPVPGIgLRVDEVttddgsgarrhavlGNPIPGMEVRISPGDG-AAGVAGREiGEIEIRG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 356 PGLSPGYWraseEQQARFAGGWYRTGDL-FERDesGAYRHCGREDDLFKVNGRWVVPTQVEQAICRhLPEVSEAVLVPTC 434
Cdd:PRK05851 380 ASMMSGYL----GQAPIDPDDWFPTGDLgYLVD--GGLVVCGRAKELITVAGRNIFPTEIERVAAQ-VRGVREGAVVAVG 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 435 RLHDGLRPTLFVTLATPLDDNQILLAQRIdQHLAEQipSHMLPSQLHVLP--ALPRNDNGKLARAELRH 501
Cdd:PRK05851 453 TGEGSARPGLVIAAEFRGPDEAGARSEVV-QRVASE--CGVVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
29-407 |
3.75e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 59.19 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 29 TLSRLQCRTYILsqASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIP---AVINPKSREQALADIAADCQASLV- 104
Cdd:PRK05850 37 TWSQLYRRTLNV--AEELRRHGSTGDRAVILAPQGLEYIVAFLGALQAGLIAvplSVPQGGAHDERVSAVLRDTSPSVVl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 105 --------VREADAPSlSGPLAPLTLRaaagrplLDDFSLDALVGPAdldwsaFHRQDPAAACFLQYTSGSTGAPKGVMH 176
Cdd:PRK05850 115 ttsavvddVTEYVAPQ-PGQSAPPVIE-------VDLLDLDSPRGSD------ARPRDLPSTAYLQYTSGSTRTPAGVMV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 177 SLRNTLGFCRAFATELLAlqAGDRLYSIPKMF-----FGYGMGNSL--FFPWFSGasallddtWPSperVLENLVAFrpr 249
Cdd:PRK05850 181 SHRNVIANFEQLMSDYFG--DTGGVPPPDTTVvswlpFYHDMGLVLgvCAPILGG--------CPA---VLTSPVAF--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 250 vlfgvpaiyasLRPQAR--ELLSSVRLAFSAGsplPRGEFEFWAAH-------GLEICD--GI--GATEV---------- 306
Cdd:PRK05850 245 -----------LQRPARwmQLLASNPHAFSAA---PNFAFELAVRKtsdddmaGLDLGGvlGIisGSERVhpatlkrfad 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 307 --------------------GHVFLANRP-----------------GQAR--ADSTGLPLPGY------ECRLVDREGHT 341
Cdd:PRK05850 311 rfapfnlretairpsyglaeATVYVATREpgqppesvrfdyeklsaGHAKrcETGGGTPLVSYgsprspTVRIVDPDTCI 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596193 342 IEEAGRQGVLLVRGPGLSPGYWRASEEQQARF------------AGGWYRTGDL-FERDesGAYRHCGREDDLFKVNGR 407
Cdd:PRK05850 391 ECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLgFISE--GELFIVGRIKDLLIVDGR 467
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
26-246 |
2.03e-08 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 56.59 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 26 RGQTLSRLQCRTyILSQASQLARL------LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADC 99
Cdd:cd05905 8 KGKEATTLTWGK-LLSRAEKIAAVlqkkvgLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 100 QASLVVR-EADAPSLsgPLAPLTLRAAA------GRPLLDDFSLDALVGPADL-DWSAFHRQDPAAACFLQYTSGSTGAP 171
Cdd:cd05905 87 KVRVALTvEACLKGL--PKKLLKSKTAAeiakkkGWPKILDFVKIPKSKRSKLkKWGPHPPTRDGDTAYIEYSFSSDGSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 172 KGVMHSLRNTLGFCRAFaTELLALQAGDRLYSI--PKMffgyGMGnslFFPW-----FSGASALlddtWPSPERVLENLV 244
Cdd:cd05905 165 SGVAVSHSSLLAHCRAL-KEACELYESRPLVTVldFKS----GLG---LWHGcllsvYSGHHTI----LIPPELMKTNPL 232
|
..
gi 15596193 245 AF 246
Cdd:cd05905 233 LW 234
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
376-496 |
3.94e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 52.82 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 376 GWYRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAICRHlPEVSE----AVLVPTCRlhdgLRPTLFVTLATP 451
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKH-PLVLEccsiGIYDPDCY----NVPIGLLVLKQD 566
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15596193 452 LDDNQILLAQ---RIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLAR 496
Cdd:PTZ00237 567 QSNQSIDLNKlknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
269-503 |
6.00e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.92 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 269 LSSVRLAFSAGSPLPRGEFEFWAAHGLEICDGIGATEVGHVFLANRPGQ--ARADSTGLPLPGYECRLvdREGHTieeag 346
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDflAGNNSSGQVLPHAQITI--PANQT----- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 347 rqGVLLVRGPGLSPGYWRASEEQQARFaggwyRTGDLFERDESGAYRHCGREDDLFKVNGRWVVPTQVEQAI-------- 418
Cdd:PRK07445 302 --GNITIQAQSLALGYYPQILDSQGIF-----ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIlatglvqd 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 419 -C------RHLPEVSEAVLVPtcrlhdglrptlfvtlatpldDNQILLAQRIDQHLAEQIPSHMLPSQLHVLPALPRNDN 491
Cdd:PRK07445 375 vCvlglpdPHWGEVVTAIYVP---------------------KDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQ 433
|
250
....*....|..
gi 15596193 492 GKLARAELRHLA 503
Cdd:PRK07445 434 GKINRQQLQQIA 445
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
164-471 |
1.15e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 51.09 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 164 TSGSTGAPKGVMHSlRNTLG-----FCRAFATellalqAGDRLYSIPKMFFGYG--MGnslFFPWFSGASALLDDTWP-- 234
Cdd:cd05913 86 SSGTTGKPTVVGYT-KNDLDvwaelVARCLDA------AGVTPGDRVQNAYGYGlfTG---GLGFHYGAERLGALVIPag 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 235 --SPERVLENLVAFRPRVLFGVP---------AIYASLRPQArellSSVRLAFSAGSPL---PRGEFEfwAAHGLEICDG 300
Cdd:cd05913 156 ggNTERQLQLIKDFGPTVLCCTPsyalylaeeAEEEGIDPRE----LSLKVGIFGAEPWteeMRKRIE--RRLGIKAYDI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 301 IGATEVGHVFLANRPGQARA--------------DSTGLPLP-GYECRLVdreghtIEEAGRQGVLLVRgpglspgywra 365
Cdd:cd05913 230 YGLTEIIGPGVAFECEEKDGlhiwedhfipeiidPETGEPVPpGEVGELV------FTTLTKEAMPLIR----------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 366 seeqqarfaggwYRTGDL--FERDESGAYRH-------CGREDDLFKVNGRWVVPTQVEQAICRHLPEVSEAVLVPTcRL 436
Cdd:cd05913 293 ------------YRTRDItrLLPGPCPCGRThrridriTGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILT-RQ 359
|
330 340 350
....*....|....*....|....*....|....*..
gi 15596193 437 HDGLRPTLFVTLATPLDDNQIL--LAQRIDQHLAEQI 471
Cdd:cd05913 360 EHLDELTIKVEVRPEADDDEKLeaLKQRLERHIKSVL 396
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-503 |
4.20e-06 |
|
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: 49.35 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 46 LARLLKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALAD--IAADCQAsLVVREadapslsgpLAPLTLR 123
Cdd:cd05939 21 QAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHciTVSKAKA-LIFNL---------LDPLLTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 124 AAAGRPLLDDFSLDALVgpadldwsafhrqdpaaaCFLqYTSGSTGAPK-GVMHSLRNTlgFCRAFATELLALQAGDRLY 202
Cdd:cd05939 91 SSTEPPSQDDVNFRDKL------------------FYI-YTSGTTGLPKaAVIVHSRYY--RIAAGAYYAFGMRPEDVVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 203 SIPKMFFG----YGMGNSLFF-------PWFSgASALLDD---------------------TWPSPERVLENLvafrpRV 250
Cdd:cd05939 150 DCLPLYHSaggiMGVGQALLHgstvvirKKFS-ASNFWDDcvkynctivqyigeicryllaQPPSEEEQKHNV-----RL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 251 LFGvpaiyASLRPQAREllssvrlAFSAGSPLPR-GEFefwaahgleicdgIGATEvGHVFLANRPGQARAdsTG----L 325
Cdd:cd05939 224 AVG-----NGLRPQIWE-------QFVRRFGIPQiGEF-------------YGATE-GNSSLVNIDNHVGA--CGfnsrI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 326 PLPGYECRLVDREGHTIE-EAGRQGVLLVRGPGLS----------------PGYW--RASEEQQAR--FAGG--WYRTGD 382
Cdd:cd05939 276 LPSVYPIRLIKVDEDTGElIRDSDGLCIPCQPGEPgllvgkiiqndplrrfDGYVneGATNKKIARdvFKKGdsAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 383 LFERDESGAYRHCGREDDLFKVNGRWVVPTQVEqAICRHLPEVSEAVL----VPTCRLHDGLRPTLFVTLATPLDdnqil 458
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVE-GILSNVLGLEDVVVygveVPGVEGRAGMAAIVDPERKVDLD----- 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15596193 459 laqRIDQHLAEQIPSHMLPSQLHVLPALPRNDNGKLARAELRHLA 503
Cdd:cd05939 430 ---RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
153-415 |
1.97e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 47.32 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 153 QDPAAACFLQYTSGSTGAPKGVMHSLRN----TLGFCRAFATELLALQAGDRLYS-----------IPKMFFGYGmgNSL 217
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESivtlIAGVIRLLKSANAALTVKDVYLSylplahifdrvIEECFIQHG--AAI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 218 FFpWFSGASALLDD-------TWPSPERVLENLVA----------FRPRVLFGVPAIY-----------ASLRPQARELL 269
Cdd:PLN02614 298 GF-WRGDVKLLIEDlgelkptIFCAVPRVLDRVYSglqkklsdggFLKKFVFDSAFSYkfgnmkkgqshVEASPLCDKLV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 270 SS---------VRLAFSAGSPLPRGEFEFW-AAHGLEICDGIGATEVGHVFLANRPGQARADST-GLPLPGYECRL--VD 336
Cdd:PLN02614 377 FNkvkqglggnVRIILSGAAPLASHVESFLrVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTvGPPVPNVDIRLesVP 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 337 REGHTIEEAGRQGVLLVRGPGLSPGYWRASEEQQARFAGGWYRTGDLFERDESGAYRHCGREDDLFKV-NGRWVVPTQVE 415
Cdd:PLN02614 457 EMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIE 536
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
43-500 |
1.52e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 44.30 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 43 ASQLARL-----LKPGDRVVLALNDSPSLACLFLACIAVGAIPAVINPKSREQALADIAADCQASLVVREAD----APSL 113
Cdd:PRK13391 34 SNRLAHLfrslgLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAkldvARAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 114 SGPLAPLTLRAAAGRPllDDfsLDALVG--PADLDWSAFHRQDPAAACFLQYTSGSTGAPKGVMHSL--------RNTLG 183
Cdd:PRK13391 114 LKQCPGVRHRLVLDGD--GE--LEGFVGyaEAVAGLPATPIADESLGTDMLYSSGTTGRPKGIKRPLpeqppdtpLPLTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 184 FCR---AFATELLALQAGDRLYSIPKMFfgYGMGNSLffpwfsGASALLDDTWpSPERVLEnLVAfRPRVLFG--VPAIY 258
Cdd:PRK13391 190 FLQrlwGFRSDMVYLSPAPLYHSAPQRA--VMLVIRL------GGTVIVMEHF-DAEQYLA-LIE-EYGVTHTqlVPTMF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 259 ASLRPQAREL-----LSSVRLAFSAGSPLP----RGEFEFWaahGLEICDGIGATE-VGHVFLANRPGQARADSTGLPLP 328
Cdd:PRK13391 259 SRMLKLPEEVrdkydLSSLEVAIHAAAPCPpqvkEQMIDWW---GPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 329 GyECRLVDREGHTIeEAGRQGVLLVRGpGLSPGYWRASEE-QQARFA-GGWYRTGDLFERDESGAYRHCGREDDLFKVNG 406
Cdd:PRK13391 336 G-DLHILDDDGAEL-PPGEPGTIWFEG-GRPFEYLNDPAKtAEARHPdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 407 RWVVPTQVEQAICRHlPEVSEAVL--VPTCRLHDGLRPTlfVTLATPLDDNQIlLAQRIDQHLAEQIPSHMLPSQLHVLP 484
Cdd:PRK13391 413 VNIYPQEAENLLITH-PKVADAAVfgVPNEDLGEEVKAV--VQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDFED 488
|
490
....*....|....*.
gi 15596193 485 ALPRNDNGKLARAELR 500
Cdd:PRK13391 489 ELPRLPTGKLYKRLLR 504
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
14-174 |
3.91e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.19 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 14 LDFDPDTAVyhyRGQTLSRLQCRTYILSQASQLARLLKPGDRVVLALNDSPSLACLFLACIAVGAIpAV--INPKSREQA 91
Cdd:PRK12476 56 LDHSHSAAG---CAVELTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTI-AVplFAPELPGHA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 92 --LADIAADCQASLVV-READAPSLSGPLAPLtlrAAAGRPLLddFSLDALVGPADLDWSAFHRQDPAAAcFLQYTSGST 168
Cdd:PRK12476 132 erLDTALRDAEPTVVLtTTAAAEAVEGFLRNL---PRLRRPRV--IAIDAIPDSAGESFVPVELDTDDVS-HLQYTSGST 205
|
....*.
gi 15596193 169 GAPKGV 174
Cdd:PRK12476 206 RPPVGV 211
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
279-490 |
5.78e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.78 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 279 GSPLPRGEFE-----FWAAHGLEICdgigATEVGHVFLANRPGqARADSTGLPLPGY-ECRLVD---REGHTIE------ 343
Cdd:PRK07868 727 GSGMPTGLWErvveaFAPAHVVEFF----ATTDGQAVLANVSG-AKIGSKGRPLPGAgRVELAAydpEHDLILEddrgfv 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596193 344 ---EAGRQGVLLVRGPGlsPGYWRASEEQQArFAGG--WYRTGDLFERDESGAYRHCGREDDLFKvNGRWVVPTQ-VEQA 417
Cdd:PRK07868 802 rraEVNEVGVLLARARG--PIDPTASVKRGV-FAPAdtWISTEYLFRRDDDGDYWLVDRRGSVIR-TARGPVYTEpVTDA 877
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596193 418 ICRhLPEVSEAVlvpTCRLHDGLRpTLFVTLATPLDDNQILLAQrIDQHLAEqIPSHMLPSQLHVLPALPRND 490
Cdd:PRK07868 878 LGR-IGGVDLAV---TYGVEVGGR-QLAVAAVTLRPGAAITAAD-LTEALAS-LPVGLGPDIVHVVPEIPLSA 943
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
163-199 |
5.81e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 39.33 E-value: 5.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 15596193 163 YTSGSTGAPKGVMHSLRNTLGFCRAFATELLALQAGD 199
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKND 293
|
|
| |
