|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
308-798 |
0e+00 |
|
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: 542.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 308 CLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 387
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 388 PLtrkdaGSQQVGFLLGSCGVFLALTTDACQKGLPKA-----QTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDT 462
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 463 GTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALM 542
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 543 KANPLSWIQKVCFYKARAALVKSRDMHWSL------LAQRGQRDVSLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 616
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 617 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEgTP 694
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPE-TK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 695 YLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGP----------DNLVFIVGK 764
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510
....*....|....*....|....*....|....
gi 225735627 765 LDGLMVTGVRRHNADDVVATALAVEPmkfvYRGR 798
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGR 490
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
298-790 |
7.39e-53 |
|
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: 192.84 E-value: 7.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 298 RWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLnkltsknePLLKPGDRVALVFPNSdpVMFMVAFYGCLL 377
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 378 AELVPVPIEVPLTRKDAgsQQVGFLLGSCGVFLALTTDACQKGLPKAqtgeVAAFKGWPPLSWLVIDGKHLAkPPKDWHP 457
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 458 LAQDTGTgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHV 534
Cdd:cd05931 144 PSPDPDD-IAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 535 VsvpyaLMK-----ANPLSWIQKVCFYKAR--AAlvksRDMHWSLLAQRGQR----DVSLSSLRMLIVadGANPWSISSC 603
Cdd:cd05931 220 V-----LMSpaaflRRPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 604 DAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPG 682
Cdd:cd05931 289 RRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 683 ANVCVVKLEGTPyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGapifdrPFTRTGLLGFIGPDNLvFIV 762
Cdd:cd05931 364 QEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YIT 435
|
490 500
....*....|....*....|....*...
gi 225735627 763 GKLDGLMVTGVRRHNADDVVATALAVEP 790
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-123 |
3.45e-28 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 109.05 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 10 AAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIpliqgidpsLQAENripgPSQTTAAAPKQQKSRPTASRD 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------LHPET----PTKLSAEAQNQLASLETKLRD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 225735627 90 ERFRSDVHTEAVQAALAKYKERKM--PMPSKRRSVL 123
Cdd:pfam06464 69 EELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
296-772 |
2.08e-27 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 115.87 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 296 LQRWGTTQPKSPCLTALDTTgkavyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 375
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 376 LLAELVPVPIEVpltrkDAGSQQVGFLLGSCGVFLALTTD--------ACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKH 447
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 448 LAKPPKDWHPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQAC----GYSEAETLTNVLDFKRDAGL 520
Cdd:pfam00501 142 ADVPPPPPPPPDPDD---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 521 WHGVLTSVMNRMHVVSVP--YALMKANPLSWIQKvcfYKARAALVKSRDMHWsLLAQRGQRDVSLSSLRMLIVadGANPW 598
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPPgfPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 599 SISSCDAFLNVFqsrglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQ 678
Cdd:pfam00501 290 PPELARRFRELF------GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 679 VMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvttggapiFDRPFTRTGLLGFIGPDNL 758
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAF------------DEDGWYRTGDLGRRDEDGY 403
|
490
....*....|....
gi 225735627 759 VFIVGKLDGLMVTG 772
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
292-781 |
2.74e-27 |
|
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: 116.06 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 292 LLATLQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSDPvmFMVA 371
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 372 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGvflalttdacqkglPKAqtgevaafkgwpplswlVIdgkhlakp 451
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSG--------------ARA-----------------LV-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 452 pkdwhplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSV 528
Cdd:COG0318 102 --------------TALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 529 MNRMHVVSVPyalmKANPLSWIQKVCFYKA-RAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFL 607
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 608 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGANVC 686
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 687 VVKLEGTPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttGGapifdrpFTRTGLLGFIGPDNLVFIVGKLD 766
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVGRKK 346
|
490
....*....|....*
gi 225735627 767 GLMVTGVRRHNADDV 781
Cdd:COG0318 347 DMIISGGENVYPAEV 361
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
280-773 |
1.32e-24 |
|
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: 108.91 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 280 EPLTAGVPRppSLLATLQRWGTTQPKSPClTALDTTGkAVYTLTYGKLWSRSLKLAyTLLNKLTskneplLKPGDRVALV 359
Cdd:cd05906 2 LHRPEGAPR--TLLELLLRAAERGPTKGI-TYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 360 FP-NSDpvmFMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVflaLTTDACQkglpkAQTGEVAAFK 433
Cdd:cd05906 71 FDdNED---FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 434 GWPPLSWLVIDGKHLAKPPKDWHPLAQDtgtgTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTN 510
Cdd:cd05906 140 GLPGIRVLSIEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 511 VLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKA------RAALVKSRDmhwsLLAQRGQRDVSLS 584
Cdd:cd05906 214 WVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 585 SLRMLIVADGANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RV 662
Cdd:cd05906 290 SLRYLVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 663 DTEEKLS-VLTVQDVGQVMPGANVCVVKLEGTpyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifd 741
Cdd:cd05906 342 FPTYDHSqALEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDG----- 409
|
490 500 510
....*....|....*....|....*....|..
gi 225735627 742 rpFTRTGLLGFIGPDNLVFIVGKLDGLMVTGV 773
Cdd:cd05906 410 --WFRTGDLGFLDNGNLTITGRTKDTIIVNGV 439
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
291-784 |
2.55e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 95.78 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 291 SLLATLQRWGTTQPKSPCLT----ALDTTGKAvYTLTYGKLWSRSLKLAYTLlNKLTSknepllkPGDRVALVFPNSdpV 366
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVA-ETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 367 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVFLALTTDACqkglpkaqTGEVAAF----KGWPPLSWLV 442
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 443 IDGKHLAKPPKDwhPLAQDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQA----CGYSEAETLTNV--LD 513
Cdd:PRK05850 141 VDLLDLDSPRGS--DARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFEQLMSDyfgdTGGVPPPDTTVVswLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 514 FKRDAGLWHGVLTSVMNRMHVV-SVPYALMkANPLSWIQkvcfykaraaLVKSRDMHWSL-------LAQRGQRDVSLSS 585
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPAVlTSPVAFL-QRPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 586 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 661
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 662 VDTEeKLSVltvqdvGQVMPGANVcvvklEGTPYL--------------------CKTDEVGEICVSSSATGTAYYGLLG 721
Cdd:PRK05850 349 FDYE-KLSA------GHAKRCETG-----GGTPLVsygsprsptvrivdpdtcieCPAGTVGEIWVHGDNVAAGYWQKPE 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735627 722 ITKNVFEAVPVT-TGGAPifDRPFTRTGLLGFIGPDNLvFIVGKL-DGLMVTGvRRHNADDVVAT 784
Cdd:PRK05850 417 ETERTFGATLVDpSPGTP--EGPWLRTGDLGFISEGEL-FIVGRIkDLLIVDG-RNHYPDDIEAT 477
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
313-718 |
3.92e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 313 DTTGKAVYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LT 390
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 391 RKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEvaafkgwpPLSWlVIDGKHLAKPPKDWHPLAQDTGTGTAYIE 470
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 471 YkTSkeGST---VGVTVSHASLLAQCRALTQ-ACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANP 546
Cdd:PRK09192 183 Y-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 547 LSWIQKVCfyKARAALVKSRDMHWSLLAQRGQ----RDVSLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICP 622
Cdd:PRK09192 260 LQWLDLIS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 623 CASSPEAlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGANVCVVKLEGTPYlcKTDE 701
Cdd:PRK09192 336 SYGLAEA-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERV 410
|
410
....*....|....*..
gi 225735627 702 VGEICVSSSATGTAYYG 718
Cdd:PRK09192 411 VGHICVRGPSLMSGYFR 427
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
288-777 |
1.00e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.14 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 288 RPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLlnkltsknEPLLKPGDRVALVFPnSDPvM 367
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 368 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLpkAQTGEVAAfKGWPPlsWLVIDGKh 447
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL--LQMEELAA-ANAPE--LLCVDTL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 448 LAKPPKDWHPLAQDtGTGTAYIEYkTSkeGSTV---GVTVSHASLLAQCRALTQACG--YSEAETLTNVLDFKRDAGLWH 522
Cdd:PRK05691 151 DPALAEAWQEPALQ-PDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 523 GVLTSVMNrmhvvSVPYALMK-----ANPLSWIQKVCFYkaRAALVKSRDMHWSLLAQRgqrdVSLSSLRML------IV 591
Cdd:PRK05691 227 GLLQPIFS-----GVPCVLMSpayflERPLRWLEAISEY--GGTISGGPDFAYRLCSER----VSESALERLdlsrwrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 592 ADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSV 670
Cdd:PRK05691 296 YSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 671 LTVQDVGQVM-------PGANVCVV---KLEGTPylckTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGapif 740
Cdd:PRK05691 360 RAEPGTGSVLmscgrsqPGHAVLIVdpqSLEVLG----DNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDG---- 427
|
490 500 510
....*....|....*....|....*....|....*..
gi 225735627 741 dRPFTRTGLLGFIgPDNLVFIVGKLDGLMVtgVRRHN 777
Cdd:PRK05691 428 -RTWLRTGDLGFL-RDGELFVTGRLKDMLI--VRGHN 460
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
323-790 |
2.98e-15 |
|
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: 79.45 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 323 TYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRValVFPNSDPVMFMVAFYGCLLAELVPVPIEVpltrkdaGSQQvgfl 402
Cdd:cd05908 17 SYRHLREEALGYLGAL-------QELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSI-------GSNE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 403 lgscgvflalttDACQKglpkaqtgevaAFKGWPPLS--WLVIDGKHLAKPPKDwhplaqdtgtgTAYIEYKTSKEGSTV 480
Cdd:cd05908 77 ------------EHKLK-----------LNKVWNTLKnpYLITEEEVLCELADE-----------LAFIQFSSGSTGDPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 481 GVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKarA 560
Cdd:cd05908 123 GVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHK--A 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 561 ALVKSRDMHWSLLAQRGQ----RDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlTVAIRR 636
Cdd:cd05908 201 TIVSSPNFGYKYFLKTLKpekaNDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 637 PPdlGGPPPRKAVLSMNGLSYG--VIRVDTEEKlSVLTVQDVGQVMPGANV--CVVKLEGTPylckTDEVGEICVSSSAT 712
Cdd:cd05908 278 PK--AQSPFKTITLGRRHVTHGepEPEVDKKDS-ECLTFVEVGKPIDETDIriCDEDNKILP----DGYIGHIQIRGKNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 713 GTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTGvrrHNA--DDVVATALAVEP 790
Cdd:cd05908 351 TPGYYNNPEATAKVF-----TDDG-------WLKTGDLGFIRNGRLVITGREKDIIFVNG---QNVypHDIERIAEELEG 415
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
351-785 |
1.87e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 74.00 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 351 KPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVFLALTTDACQKG----- 420
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGvrkff 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 421 --LPKAQTGEVAAFKGWPP---LSWlvidgkhlaKPPkdwhPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQ 492
Cdd:PRK07769 148 raRPAKERPRVIAVDAVPDevgATW---------VPP----EANEDT---IAYLQY-TS--GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 493 CRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKaNPLSWIqkvcfykaRAALVKSRDMH--- 569
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWI--------RELARKPGGTGgtf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 570 -------WSLLAQRG-----QRDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRR 636
Cdd:PRK07769 280 saapnfaFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 637 PPDlggpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTA 715
Cdd:PRK07769 358 MDE----EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225735627 716 YYGLLGITKNVFEAV------PVTTGGAPIfDRPFTRTGLLGFIGPDNLvFIVGKLDGLMVTGVRRHNADDVVATA 785
Cdd:PRK07769 432 YWGKPEETAATFQNIlksrlsESHAEGAPD-DALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTA 505
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
466-772 |
3.18e-11 |
|
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: 65.38 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 466 TAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPyalm 542
Cdd:cd04433 2 PALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 543 KANPLSWIQKVCFYKARAALVkSRDMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVICP 622
Cdd:cd04433 74 KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 623 CASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPylCKTDEV 702
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGEI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 703 GEICVSSsatgtaYYGLLGITKNVFEAVPVTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTG 772
Cdd:cd04433 195 GELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
323-766 |
3.63e-11 |
|
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: 65.75 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 323 TYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 400
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 401 FLLGSCGVFLALTTdacqkglpkAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYkTSkeGST- 479
Cdd:TIGR01733 66 FILEDAGARLLLTD---------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 480 --VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVVSVPYALMKANPLSWiqkvcfyk 557
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 558 arAALVKSRDM-HWSLLAqrgqrdvslSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 635
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 636 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIC 706
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 707 VSSSATGTAYYGLLGITKNVFEAVPVTTGGapifDRPFTRTGLLGFIGPDNLVFIVGKLD 766
Cdd:TIGR01733 324 IGGPGVARGYLNRPELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRID 379
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
313-770 |
9.19e-11 |
|
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: 64.93 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 313 DTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIevpltrk 392
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 393 DAGSQQ--VGFLLGSCGVFLALTTdacQKGLPKAQtgevAAFKGWPPLSWLVIDGKHLAK---PPKDWHPLA-------- 459
Cdd:cd05911 66 NPIYTAdeLAHQLKISKPKVIFTD---PDGLEKVK----EAAKELGPKDKIIVLDDKPDGvlsIEDLLSPTLgeededlp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 460 ---QDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCralTQACGYSEA-----ETLTNVLDFKRDAGLWhGVLTSV 528
Cdd:cd05911 139 pplKDGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANL---SQVQTFLYGndgsnDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 529 MNRMHVVSVPyalmKANPLSWIQKVCFYKARAALVKSRDMHWslLAQRGQRDV-SLSSLRMLIVadGANPWSISSCDAFL 607
Cdd:cd05911 212 LNGATVIIMP----KFDSELFLDLIEKYKITFLYLVPPIAAA--LAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 608 NVFQSRGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPG 682
Cdd:cd05911 284 KRFPNATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 683 ANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIV 762
Cdd:cd05911 324 VEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIV 390
|
490
....*....|....
gi 225735627 763 G------KLDGLMV 770
Cdd:cd05911 391 DrkkeliKYKGFQV 404
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
350-787 |
3.41e-10 |
|
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: 63.23 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 350 LKPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVFLALttdaCQKGL-PKAQ 425
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVL----ADAGAaDRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 426 TGEVAAFKgwpPLSWLVIDGKHLAKPPKDWHPLAQDTgtgTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEA 505
Cdd:cd05922 85 DALPASPD---PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 506 ETLTNVLDFKRDAGLwhGVLTS--------VMNRMHVVsvPYALMKAnplswiqkvcFYKARAALVKSRDMHWSLLAQRG 577
Cdd:cd05922 159 DRALTVLPLSYDYGL--SVLNThllrgatlVLTNDGVL--DDAFWED----------LREHGATGLAGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 578 QRDVSLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavls 651
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 652 mnglsygvirvdteeklsvltvQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIcVSSSATGTAYYGllgiTKNVFEAVP 731
Cdd:cd05922 286 ----------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKE 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 225735627 732 VTTGGApifdrpfTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALA 787
Cdd:cd05922 337 GRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
321-521 |
6.66e-10 |
|
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: 62.95 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 398
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 399 VGFLLGSCGVFLALTTDACQKGLPKAQtgevaafkgwppLSWLVIDGKHLAKPPKDWhPLAQDTGTGTAYIEYkTSkeGS 478
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 225735627 479 T---VGVTVSHASLLAQCRALTQACGYSEAETLTNV--LDFkrDAGLW 521
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
225-766 |
6.82e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 225 RVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSV-LRGEPLTAGVPRPPSLLATLQRwgttq 303
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVFGDQH----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 304 pkspcltaldttgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELV 381
Cdd:PRK12316 2029 ------------------LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYV 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 382 PVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKgwPPLSWlvidgkhlakppKDW---HPL 458
Cdd:PRK12316 2082 PLDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLD--RDAEW------------ADYpdtAPA 2140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 459 AQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVvsvp 538
Cdd:PRK12316 2141 VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARV---- 2215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 539 yaLMKANPLsWIQKVCFYKARAALVKSRDM---HWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAflnvfQSRGL 615
Cdd:PRK12316 2216 --LIRDDEL-WDPEQLYDEMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEAL 2285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 616 RPEVIcpcasspealtvairrppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGANVCVvkLEGTPY 695
Cdd:PRK12316 2286 RPVYL-------------------FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLN 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225735627 696 LCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 766
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY-----RTGDLARYRADGVVEYLGRID 2404
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
310-495 |
1.87e-09 |
|
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: 60.65 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 310 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 389
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 390 TrkdagSQQVGFLLGSCGVFLALTtdacqkglpkaqtgeVAAFkgwpplswlvidgKHLAKPPKDWHPLAQDTGTGTAYI 469
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190
....*....|....*....|....*....|..
gi 225735627 470 EYkTSkeGST---VGVTVSHASLLA---QCRA 495
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKA 159
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
321-508 |
4.62e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 56.15 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 400
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 401 FLLGSCGVFLALTTDACQKGLPkaqtgevaafkGWPPLSWLVIDGKHLAKPPkdwhPLAQDTGTGTAYIEYkTSkeGST- 479
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-----------AGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GSTg 139
|
170 180 190
....*....|....*....|....*....|.
gi 225735627 480 --VGVTVSHASLLAQCRALTQACGYSEAETL 508
Cdd:cd12116 140 rpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
313-797 |
8.42e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.90 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 313 DTTGKAVyTLTYGKLWSRslklaytlLNKLTSKNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 388
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 389 -LTRKDAgsqqvgfLLGSCGVFLALTTDACQ-------KGLPKAQTGEVAAFKGWPplswlvidgkhlAKPPKDWHPLAQ 460
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIP------------DSAGESFVPVEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 461 DTgTGTAYIEYkTSkeGST---VGVTVSHasllaqcRAltqACgyseaetlTNVLDFKRDAGLW----HGV--------- 524
Cdd:PRK12476 191 DT-DDVSHLQY-TS--GSTrppVGVEITH-------RA---VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 525 -LTSVM------NRMHVVSvPYALMKaNPLSWIQKVCFYKARAALVKSR-DMHWSLLAQRG----QRDVSLSSLRMLIva 592
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKALSEGSRTGRVVTAApNFAYEWAAQRGlpaeGDDIDLSNVVLII-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 593 dGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSVL 671
Cdd:PRK12476 325 -GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAVA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 672 TVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTT-------GGAPIfDRPF 744
Cdd:PRK12476 401 HVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRlaegshaDGAAD-DGTW 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 225735627 745 TRTGLLGFIgPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRG 797
Cdd:PRK12476 478 LRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRG 527
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
350-504 |
2.43e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 54.17 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 350 LKPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEV 429
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 430 AAFKGWPPL--------SWLVIDgkHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACG 501
Cdd:PRK08316 131 VDTLILSLVlggreapgGWLDFA--DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
...
gi 225735627 502 YSE 504
Cdd:PRK08316 209 MSA 211
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
321-587 |
4.27e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 321 TLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 398
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 399 VGFLLGSCGVFLALTTDACQKGLPKAqtgevaafKGwppLSWLVIDgkhlakPPKDW------HPLAQDTGTGTAYIEYK 472
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIP--------DG---LASLALD------RDEDWegfpahDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 473 TSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPYALmkANPLSWIQK 552
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDSL--WDPERLYAE 4779
|
250 260 270
....*....|....*....|....*....|....*
gi 225735627 553 VcfYKARAALVKSRDMHWSLLAQRGQRDVSLSSLR 587
Cdd:PRK12316 4780 I--HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
284-416 |
2.32e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 51.20 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 284 AGVPRPP-------SLLATLQRWGTTQPKSPcltALDTTGkavYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRV 356
Cdd:PRK06178 20 AGIPREPeyphgerPLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFAALLRQRG-------VGAGDRV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 357 ALVFPNSdPvMFMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVFLALTTDA 416
Cdd:PRK06178 87 AVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
321-460 |
3.06e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 400
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735627 401 FLLGSCGVFLALTT-DACQKGLPKAQTGE-----VAAFKGW-------PPLSWLVIDGKHLAKPPKDWHPLAQ 460
Cdd:PRK08314 102 HYVTDSGARVAIVGsELAPKVAPAVGNLRlrhviVAQYSDYlpaepeiAVPAWLRAEPPLQALAPGGVVAWKE 174
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
287-762 |
4.16e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 50.19 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 287 PRPPSLLATLQRWGTTQPKSpclTALDTTGKAVytlTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDpv 366
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 367 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVFLALTTDacqKGLPkaqtgEVAAFKGWPPL--SWLVID 444
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDS---EFVP-----LLAAILPQLPTvrTVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 445 GKHLAKPPKDWH------------PLAQDTGTGTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEaetlt 509
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 510 nvldfkRDAGLwhgVLTSvMNRMHVVSVPY-ALMKANPLSWIQKVCFYKARAALVKSR--------DMHWSLLAQRGQRD 580
Cdd:PRK06187 208 ------DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDPENLLDLIETERvtfffavpTIWQMLLKAPRAYF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 581 VSLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAVLSmngl 655
Cdd:PRK06187 278 VDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTKRR---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 656 sygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttG 735
Cdd:PRK06187 340 -------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------G 394
|
490 500
....*....|....*....|....*..
gi 225735627 736 GapifdrpFTRTGLLGFIGPDNLVFIV 762
Cdd:PRK06187 395 G-------WLHTGDVGYIDEDGYLYIT 414
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
296-772 |
9.33e-06 |
|
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: 48.76 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 296 LQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPvmFMVAFYGC 375
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 376 LLAELVPVPIEVPLTRKDagsqqVGFLLGSCGvflalttdacqkglpkaqtgevaafkgwpplSWLVIDgkhlakppkDw 455
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSG-------------------------------AKVLFD---------D- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 456 hplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETL--------TNVLDFKRDAGLWHGV 524
Cdd:cd17631 100 ----------LALLMY-TS--GTTgrpKGAMLTHRNLLWNAVNALAALDLGPDDVLlvvaplfhIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 525 LTSVMNRMHVVSVpyalmkanpLSWIQ--KVCFykarAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVADGANPwsiss 602
Cdd:cd17631 167 TVVILRKFDPETV---------LDLIErhRVTS----FFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMP----- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 603 cDAFLNVFQSRGLRpevICPCASSPEALTVAIRRPPDlggppprkavlsmnglsygvirvDTEEKLSvltvqDVGQVMPG 682
Cdd:cd17631 227 -ERLLRALQARGVK---FVQGYGMTETSPGVTFLSPE-----------------------DHRRKLG-----SAGRPVFF 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 683 ANVCVVKLEGTPylCKTDEVGEICVSSSATGTAYYGLlgitknvfeavPVTTGGApIFDRPFtRTGLLGFIGPDNLVFIV 762
Cdd:cd17631 275 VEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWNR-----------PEATAAA-FRDGWF-HTGDLGRLDEDGYLYIV 339
|
490
....*....|
gi 225735627 763 GKLDGLMVTG 772
Cdd:cd17631 340 DRKKDMIISG 349
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
320-498 |
5.38e-05 |
|
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: 46.50 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 320 YTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsq 397
Cdd:cd12114 11 GTLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 398 qvgfLLGSCGVFLALTTDACQKGLPKAqtgevaafkgwPPLSWLVIDGKHLAKPPKDWHPLAQDTgtgtAYIEYkTSkeG 477
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVAPDDL----AYVIF-TS--G 136
|
170 180
....*....|....*....|....
gi 225735627 478 ST---VGVTVSHASLLAQCRALTQ 498
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINR 160
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
307-766 |
5.84e-05 |
|
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: 46.47 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 307 PCLTALDTTGKavyTLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVPIe 386
Cdd:cd05945 5 PDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVPL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 387 vpltrkDAGSqqvgfllgscgvflalttdacqkglPKAQTGEVAAfkgwpplswlvidgkhLAKPpkdwhPLAQDTGTGT 466
Cdd:cd05945 72 ------DASS-------------------------PAERIREILD----------------AAKP-----ALLIADGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 467 AYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLwHGVLTSVMNRMHVVSVPYAlMK 543
Cdd:cd05945 100 AYIIF-TS--GSTgrpKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRD-AT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 544 ANPLSWIqkvcfykarAALVKSRDMHWsllaqrgqrdVSL-SSLRMLIVADGANPWSISSCDAFLnvFqsrglrpevicp 622
Cdd:cd05945 175 ADPKQLF---------RFLAEHGITVW----------VSTpSFAAMCLLSPTFTPESLPSLRHFL--F------------ 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 623 CAsspEALTVA-----IRRPPD-----LGGPPPrkavlSMNGLSYGVIrvdTEEKLSVLTVQDVGQVMPGANVCVVKLEG 692
Cdd:cd05945 222 CG---EVLPHKtaralQQRFPDariynTYGPTE-----ATVAVTYIEV---TPEVLDGYDRLPIGYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225735627 693 TPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 766
Cdd:cd05945 291 RP--VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAY-----RTGDLVRLEADGLLFYRGRLD 353
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
676-779 |
1.03e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.72 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 676 VGQVMPGANVCVVKLEGT-PYL--CKTDEVGEICVSssatgtayygllgiTKNVFEA-VPVTTGGAPIFDRPFTRTGLLG 751
Cdd:PRK07529 388 VGLRLPYQRVRVVILDDAgRYLrdCAVDEVGVLCIA--------------GPNVFSGyLEAAHNKGLWLEDGWLNTGDLG 453
|
90 100
....*....|....*....|....*...
gi 225735627 752 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 779
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIRG--GHNID 479
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
316-495 |
1.21e-04 |
|
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: 45.44 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 316 GKAVY-----TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLT 390
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 391 rkdagSQQVGFLLGSCGVFLALTTDACqkgLPKAQTgevAAFKGWPPLSWLVIDGKHLAKPPKDWhpLAQDTGTGT---- 466
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGEL---APVLAA---ALTKSEHTLVVLIVSGGAGPEAGALL--LAELVAAEAeqlk 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 225735627 467 ---------AYIEYKTSKEGSTVGVTVSHASLLAQCRA 495
Cdd:cd05959 157 paathaddpAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
275-613 |
1.30e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.72 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 275 SVLRGEPLTAGVPRppSLLATLQRwgttQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGD 354
Cdd:PRK12316 502 ATAAEYPLQRGVHR--LFEEQVER----TPEAPALAFGEET------LDYAELNRRANRLAHALI-------ERGVGPDV 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 355 RVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAF 432
Cdd:PRK12316 563 LVGVAMERSIEMV--VALLAILKAggAYVPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 433 KgwPPLSWLviDGKHLAKPPKDWHPLaqdtgtGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVL 512
Cdd:PRK12316 634 D--RPAAWL--EGYSEENPGTELNPE------NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 513 DFKRDAGLWHGVLTsVMNRMHVVSVPYALMKaNPLSWIQkvcfYKARAAlVKSRDMHWSLLA--QRGQRDVSLSSLRMLI 590
Cdd:PRK12316 704 PFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVE----LINREG-VDTLHFVPSMLQafLQDEDVASCTSLRRIV 776
|
330 340
....*....|....*....|...
gi 225735627 591 VADGANPWsisscDAFLNVFQSR 613
Cdd:PRK12316 777 CSGEALPA-----DAQEQVFAKL 794
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
485-774 |
1.60e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 485 SHASLLAQCRALTQACGyseaetltnvLDFKRDAG-----LWHG-----VLTSVMNRMHVVSVPYALMKANPLSWIQKVC 554
Cdd:PRK05851 173 SPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 555 fyKARAALVKSRDMHWSLLAQRGQR--DVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPC---ASSPEA 629
Cdd:PRK05851 243 --DSRATLTAAPNFAYNLIGKYARRvsDVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSyglAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 630 LTVairrppdlggPPPrkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSS 709
Cdd:PRK05851 319 VTV----------PVP--------GIGLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIRG 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735627 710 SATGTAYygllgitknvfeavpvtTGGAPIFDRPFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVR 774
Cdd:PRK05851 380 ASMMSGY-----------------LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGR 426
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
311-393 |
1.81e-04 |
|
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: 45.00 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 311 ALDTTGKAVyTLTYGKLwsrsLKLAYTLLNKLTSKNeplLKPGDRVALVFPNSDPvmFMVAFYGCLLAELVPVPIEvPLT 390
Cdd:cd05926 5 ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVAPLN-PAY 73
|
...
gi 225735627 391 RKD 393
Cdd:cd05926 74 KKA 76
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
322-399 |
2.50e-04 |
|
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: 44.39 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 322 LTYGKLWSRSLKLAYTLLNKLTSKnepllkpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI-------EVPLTRKDA 394
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPInpmlkerELEYILNDS 72
|
....*
gi 225735627 395 GSQQV 399
Cdd:cd05935 73 GAKVA 77
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
310-538 |
2.80e-04 |
|
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: 44.20 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 310 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLTSKnepllkPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI---- 385
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKDL------RGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLnpsy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 386 ---EVPLTRKDAGSQqvgfllgscgvflalttdacqkglpkaqtgevaafkgwpplswLVIDGkhlakppkdwhplaqdt 462
Cdd:cd05941 72 plaELEYVITDSEPS-------------------------------------------LVLDP----------------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225735627 463 gtgtAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVP 538
Cdd:cd05941 92 ----ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-496 |
2.85e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 44.37 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 280 EPLTAGVPRP------PSLLATL----QRWGTtqpkSPCLTALdttGKavyTLTYGKLWSRSLKLAYTLlnkltsKNEPL 349
Cdd:PRK05677 8 DKYPAGIAAEinpdeyPNIQAVLkqscQRFAD----KPAFSNL---GK---TLTYGELYKLSGAFAAWL------QQHTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 350 LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV-------PIEVPLTRKDAGSQQVgfllgscgVFLALTTDACQKGLP 422
Cdd:PRK05677 72 LKPGDRIAVQLPNV--LQYPVAVFGAMRAGLIVVntnplytAREMEHQFNDSGAKAL--------VCLANMAHLAEKVLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 423 KAQ-----TGEVAAFKgwPPLSWLVIDG--KHLAKPPKDWH-------PLAQDTGTG------------TAYIEYKTSKE 476
Cdd:PRK05677 142 KTGvkhviVTEVADML--PPLKRLLINAvvKHVKKMVPAYHlpqavkfNDALAKGAGqpvteanpqaddVAVLQYTGGTT 219
|
250 260
....*....|....*....|...
gi 225735627 477 GSTVGVTVSHASLLA---QCRAL 496
Cdd:PRK05677 220 GVAKGAMLTHRNLVAnmlQCRAL 242
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
320-383 |
4.21e-04 |
|
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: 43.60 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735627 320 YTLTYGKLWSRSLKLAYTLLNkltsknepL-LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 383
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
321-383 |
1.40e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.96 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 383
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
296-385 |
1.97e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 41.64 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 296 LQRWGTTQPKSPCLTALDTTGKAVyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 375
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA----NALRALG---VKKGDRVAIYLPNI--PEAVIAMLAC 84
|
90
....*....|
gi 225735627 376 LLAELVPVPI 385
Cdd:COG0365 85 ARIGAVHSPV 94
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
321-385 |
2.36e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 41.43 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI 385
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPL 85
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
285-489 |
2.52e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 285 GVPRPPSLLATL---QRWGTtqPKSPCLTAldttgkAVYTLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFP 361
Cdd:PRK10252 452 AVEIPETTLSALvaqQAAKT--PDAPALAD------ARYQFSYREMREQVVALANLL-------RERGVKPGDSVAVALP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 362 NSdpVMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPls 439
Cdd:PRK10252 517 RS--VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA-- 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 225735627 440 wlvidgkhlakpPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASL 489
Cdd:PRK10252 586 ------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
321-499 |
2.62e-03 |
|
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: 41.18 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 321 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQQVG 400
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARGV-------GPGDLVALCARRS--AELVVALLAILKAGAAYVPLDP-----AYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 401 FLLGSCGVFLALTTDACQKGLPkaqtgeVAAFKGWPplswlvIDGKHLAKPPKDWHPLAQDTGTgTAYIEYkTSkeGST- 479
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGELA------VELVAVTL------LDQPGAAAGADAEPDPALDADD-LAYVIY-TS--GSTg 149
|
170 180
....*....|....*....|..
gi 225735627 480 --VGVTVSHASLLAQCRALTQA 499
Cdd:cd17651 150 rpKGVVMPHRSLANLVAWQARA 171
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
676-779 |
4.13e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 40.16 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 676 VGQVMPGANVCVVKLEGTPYL---CKTDEVGEICVSSsatgtayygllgitKNVFEAVPVTTGGAPIFDRP-FTRTGLLG 751
Cdd:cd05944 176 VGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAG--------------PGVFGGYLYTEGNKNAFVADgWLNTGDLG 241
|
90 100
....*....|....*....|....*...
gi 225735627 752 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 779
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRG--GHNID 267
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
314-498 |
7.95e-03 |
|
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: 39.53 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 314 TTGKAvytLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKD 393
Cdd:cd05904 28 ATGRA---LTYAELERRVRRLAAGL-------AKRGGRKGDVVLLLSPNS--IEFPVAFLAVLSLGAVVTTAN-PLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735627 394 AGSQQVgfllGSCGVFLALTTDACQKGLPKAQTgEVAAFKGWPPLSWLVIDGKHLAKPPKdwHPLAQDTGTGTAYIEYKT 473
Cdd:cd05904 95 EIAKQV----KDSGAKLAFTTAELAEKLASLAL-PVVLLDSAEFDSLSFSDLLFEADEAE--PPVVVIKQDDVAALLYSS 167
|
170 180
....*....|....*....|....*
gi 225735627 474 SKEGSTVGVTVSHASLLAQCRALTQ 498
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVA 192
|
|
| |
