|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
351-880 |
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: 582.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 351 CLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 430
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 431 PLtrkdaGSQQVGFLLGSCGVFLALTTDACQKGLPKA-----QTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDT 505
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 506 GTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALM 585
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 586 KANPLSWIQKVCFYKARAALVKSRDMHWSL------LAQRGQRDVSLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 659
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 660 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEgTP 737
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPE-TK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 738 YLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGP----------DNLVFIVGK 807
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45827694 808 LDGLMVTGVRRHNADDVVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQV 880
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNA 524
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
341-869 |
6.65e-58 |
|
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: 208.25 E-value: 6.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 341 RWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLnkltsknePLLKPGDRVALVFPNSdpVMFMVAFYGCLL 420
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 421 AELVPVPIEVPLTRKDAgsQQVGFLLGSCGVFLALTTDACQKGLPKAqtgeVAAFKGWPPLSWLVIDGKHLAkPPKDWHP 500
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 501 LAQDTGTgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHV 577
Cdd:cd05931 144 PSPDPDD-IAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 578 VsvpyaLMK-----ANPLSWIQKVCFYKAR--AAlvksRDMHWSLLAQRGQR----DVSLSSLRMLIVadGANPWSISSC 646
Cdd:cd05931 220 V-----LMSpaaflRRPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 647 DAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPG 725
Cdd:cd05931 289 RRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 726 ANVCVVKLEGTPyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGapifdrPFTRTGLLGFIGPDNLvFIV 805
Cdd:cd05931 364 QEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YIT 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45827694 806 GKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEED 869
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPAD 497
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-123 |
3.55e-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: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 10 AAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIpliqgidpsLQAENripgPSQTTAAAPKQQKSRPTASRD 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------LHPET----PTKLSAEAQNQLASLETKLRD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 45827694 90 ERFRSDVHTEAVQAALAKYKERKM--PMPSKRRSVL 123
Cdd:pfam06464 69 EELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
339-815 |
3.82e-27 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 115.10 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 339 LQRWGTTQPKSPCLTALDTTgkavyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 418
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 419 LLAELVPVPIEVpltrkDAGSQQVGFLLGSCGVFLALTTD--------ACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKH 490
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 491 LAKPPKDWHPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQAC----GYSEAETLTNVLDFKRDAGL 563
Cdd:pfam00501 142 ADVPPPPPPPPDPDD---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 564 WHGVLTSVMNRMHVVSVP--YALMKANPLSWIQKvcfYKARAALVKSRDMHWsLLAQRGQRDVSLSSLRMLIVadGANPW 641
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPPgfPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 642 SISSCDAFLNVFqsrglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQ 721
Cdd:pfam00501 290 PPELARRFRELF------GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 722 VMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvttggapiFDRPFTRTGLLGFIGPDNL 801
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAF------------DEDGWYRTGDLGRRDEDGY 403
|
490
....*....|....
gi 45827694 802 VFIVGKLDGLMVTG 815
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
335-824 |
7.24e-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: 114.91 E-value: 7.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 335 LLATLQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSDPvmFMVA 414
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 415 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGvflalttdacqkglPKAqtgevaafkgwpplswlVIdgkhlakp 494
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSG--------------ARA-----------------LV-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 495 pkdwhplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSV 571
Cdd:COG0318 102 --------------TALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 572 MNRMHVVSVPyalmKANPLSWIQKVCFYKA-RAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFL 650
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 651 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGANVC 729
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 730 VVKLEGTPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttGGapifdrpFTRTGLLGFIGPDNLVFIVGKLD 809
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVGRKK 346
|
490
....*....|....*
gi 45827694 810 GLMVTGVRRHNADDV 824
Cdd:COG0318 347 DMIISGGENVYPAEV 361
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
332-816 |
3.13e-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: 107.75 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 332 PPSLLATLQRWGTTQPKSPClTALDTTGkAVYTLTYGKLWSRSLKLAyTLLNKLTskneplLKPGDRVALVFP-NSDpvm 410
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 411 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVflaLTTDACQkglpkAQTGEVAAFKGWPPLSWLV 485
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 486 IDGKHLAKPPKDWHPLAQDtgtgTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAG 562
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 563 LWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKA------RAALVKSRDmhwsLLAQRGQRDVSLSSLRMLIVAD 636
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 637 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 713
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 714 LTVQDVGQVMPGANVCVVKLEGTpyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLL 793
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDG-------WFRTGDL 416
|
490 500
....*....|....*....|...
gi 45827694 794 GFIGPDNLVFIVGKLDGLMVTGV 816
Cdd:cd05906 417 GFLDNGNLTITGRTKDTIIVNGV 439
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
334-877 |
4.06e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 107.72 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 334 SLLATLQRWGTTQPKSPCLT----ALDTTGKAvYTLTYGKLWSRSLKLAYTLlNKLTSknepllkPGDRVALVFPNSdpV 409
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVA-ETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 410 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVFLALTTDACqkglpkaqTGEVAAF----KGWPPLSWLV 485
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 486 IDGKHLAKPPKDwhPLAQDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQA----CGYSEAETLTNV--LD 556
Cdd:PRK05850 141 VDLLDLDSPRGS--DARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFEQLMSDyfgdTGGVPPPDTTVVswLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 557 FKRDAGLWHGVLTSVMNRMHVV-SVPYALMkANPLSWIQkvcfykaraaLVKSRDMHWSL-------LAQRGQRDVSLSS 628
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPAVlTSPVAFL-QRPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 629 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 704
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 705 VDTEeKLSVltvqdvGQVMPGANVcvvklEGTPYL--------------------CKTDEVGEICVSSSATGTAYYGLLG 764
Cdd:PRK05850 349 FDYE-KLSA------GHAKRCETG-----GGTPLVsygsprsptvrivdpdtcieCPAGTVGEIWVHGDNVAAGYWQKPE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 765 ITKNVFEAVPVT-TGGAPifDRPFTRTGLLGFIGPDNLvFIVGKL-DGLMVTGvRRHNADDVVATalavepMKFVYRGRI 842
Cdd:PRK05850 417 ETERTFGATLVDpSPGTP--EGPWLRTGDLGFISEGEL-FIVGRIkDLLIVDG-RNHYPDDIEAT------IQEITGGRV 486
|
570 580 590
....*....|....*....|....*....|....*.
gi 45827694 843 AVFSVTVLHDDRIVLVAE-QRPDASEEDSFQWMSRV 877
Cdd:PRK05850 487 AAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLRTV 522
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
356-868 |
7.91e-19 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 91.22 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 356 DTTGKAVYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LT 433
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 434 RKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEvaafkgwpPLSWlVIDGKHLAKPPKDWHPLAQDTGTGTAYIE 513
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 514 YkTSkeGST---VGVTVSHASLLAQCRALTQ-ACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANP 589
Cdd:PRK09192 183 Y-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 590 LSWIQKVCfyKARAALVKSRDMHWSLLAQRGQ----RDVSLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICP 665
Cdd:PRK09192 260 LQWLDLIS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 666 CASSPEAlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGANVCVVKLEGTPYlcKTDE 744
Cdd:PRK09192 336 SYGLAEA-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 745 VGEICVSSSATGTAYYGllgitKNVFEAVPVTTGgapifdrpFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDV 824
Cdd:PRK09192 411 VGHICVRGPSLMSGYFR-----DEESQDVLAADG--------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 45827694 825 VATAlavEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEE 868
Cdd:PRK09192 477 EWIA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRISDEER 517
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
331-860 |
6.93e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 331 RPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLlnkltsknEPLLKPGDRVALVFPnSDPvM 410
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 411 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLpkAQTGEVAAfKGWPPlsWLVIDGKh 490
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL--LQMEELAA-ANAPE--LLCVDTL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 491 LAKPPKDWHPLAQDtGTGTAYIEYkTSkeGSTV---GVTVSHASLLAQCRALTQACG--YSEAETLTNVLDFKRDAGLWH 565
Cdd:PRK05691 151 DPALAEAWQEPALQ-PDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 566 GVLTSVMNrmhvvSVPYALMK-----ANPLSWIQKVCFYkaRAALVKSRDMHWSLLAQRgqrdVSLSSLRML------IV 634
Cdd:PRK05691 227 GLLQPIFS-----GVPCVLMSpayflERPLRWLEAISEY--GGTISGGPDFAYRLCSER----VSESALERLdlsrwrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 635 ADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSV 713
Cdd:PRK05691 296 YSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 714 LTVQDVGQVM-------PGANVCVV---KLEGTPylckTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGapif 783
Cdd:PRK05691 360 RAEPGTGSVLmscgrsqPGHAVLIVdpqSLEVLG----DNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDG---- 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45827694 784 dRPFTRTGLLGFIgPDNLVFIVGKLDGLMVtgVRRHN--ADDVVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE 860
Cdd:PRK05691 428 -RTWLRTGDLGFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAE 500
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
366-867 |
3.07e-17 |
|
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: 85.62 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 366 TYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRValVFPNSDPVMFMVAFYGCLLAELVPVPIEVpltrkdaGSQQvgfl 445
Cdd:cd05908 17 SYRHLREEALGYLGAL-------QELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSI-------GSNE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 446 lgscgvflalttDACQKglpkaqtgevaAFKGWPPLS--WLVIDGKHLAKPPKDwhplaqdtgtgTAYIEYKTSKEGSTV 523
Cdd:cd05908 77 ------------EHKLK-----------LNKVWNTLKnpYLITEEEVLCELADE-----------LAFIQFSSGSTGDPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 524 GVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKarA 603
Cdd:cd05908 123 GVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHK--A 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 604 ALVKSRDMHWSLLAQRGQ----RDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlTVAIRR 679
Cdd:cd05908 201 TIVSSPNFGYKYFLKTLKpekaNDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 680 PPdlGGPPPRKAVLSMNGLSYG--VIRVDTEEKlSVLTVQDVGQVMPGANV--CVVKLEGTPylckTDEVGEICVSSSAT 755
Cdd:cd05908 278 PK--AQSPFKTITLGRRHVTHGepEPEVDKKDS-ECLTFVEVGKPIDETDIriCDEDNKILP----DGYIGHIQIRGKNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 756 GTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTGvrrHNA--DDVVATALAVEP 833
Cdd:cd05908 351 TPGYYNNPEATAKVF-----TDDG-------WLKTGDLGFIRNGRLVITGREKDIIFVNG---QNVypHDIERIAEELEG 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 45827694 834 mkfVYRGRIAVFSV--TVLHDDRIVLVAEQRPDASE 867
Cdd:cd05908 416 ---VELGRVVACGVnnSNTRNEEIFCFIEHRKSEDD 448
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
394-870 |
8.97e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 81.70 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 394 KPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVFLALTTDACQKG----- 463
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGvrkff 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 464 --LPKAQTGEVAAFKGWPP---LSWlvidgkhlaKPPkdwhPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQ 535
Cdd:PRK07769 148 raRPAKERPRVIAVDAVPDevgATW---------VPP----EANEDT---IAYLQY-TS--GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 536 CRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKaNPLSWIqkvcfykaRAALVKSRDMH--- 612
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWI--------RELARKPGGTGgtf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 613 -------WSLLAQRG-----QRDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRR 679
Cdd:PRK07769 280 saapnfaFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 680 PPDlggpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTA 758
Cdd:PRK07769 358 MDE----EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 759 YYGLLGITKNVFEAV------PVTTGGAPIfDRPFTRTGLLGFIGPDNLvFIVGKLDGLMVTGVRRHNADDVVATALavE 832
Cdd:PRK07769 432 YWGKPEETAATFQNIlksrlsESHAEGAPD-DALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--E 507
|
490 500 510
....*....|....*....|....*....|....*...
gi 45827694 833 PMKFVYRGRIAVFSVTvlhddrivlvAEQRPDASEEDS 870
Cdd:PRK07769 508 ATKALRTGYVAAFSVP----------ANQLPQVVFDDS 535
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
356-869 |
7.23e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 75.55 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 356 DTTGKAVyTLTYGKLWSRslklaytlLNKLTSKNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 431
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 432 -LTRKDAgsqqvgfLLGSCGVFLALTTDACQ-------KGLPKAQTGEVAAFKGWPplswlvidgkhlAKPPKDWHPLAQ 503
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIP------------DSAGESFVPVEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 504 DTgTGTAYIEYkTSkeGST---VGVTVSHasllaqcRAltqACgyseaetlTNVLDFKRDAGLW----HGV--------- 567
Cdd:PRK12476 191 DT-DDVSHLQY-TS--GSTrppVGVEITH-------RA---VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 568 -LTSVM------NRMHVVSvPYALMKaNPLSWIQKVCFYKARAALVKSR-DMHWSLLAQRG----QRDVSLSSLRMLIva 635
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKALSEGSRTGRVVTAApNFAYEWAAQRGlpaeGDDIDLSNVVLII-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 636 dGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSVL 714
Cdd:PRK12476 325 -GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAVA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 715 TVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTT-------GGAPIfDRPF 787
Cdd:PRK12476 401 HVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRlaegshaDGAAD-DGTW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 788 TRTGLLGFIgPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASE 867
Cdd:PRK12476 478 LRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSR 554
|
..
gi 45827694 868 ED 869
Cdd:PRK12476 555 AD 556
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
509-815 |
5.32e-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: 65.00 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 509 TAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPyalm 585
Cdd:cd04433 2 PALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 586 KANPLSWIQKVCFYKARAALVkSRDMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVICP 665
Cdd:cd04433 74 KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 666 CASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPylCKTDEV 745
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGEI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 746 GEICVSSsatgtaYYGLLGITKNVFEAVPVTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTG 815
Cdd:cd04433 195 GELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
366-809 |
8.09e-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: 64.98 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 366 TYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 443
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 444 FLLGSCGVFLALTTdacqkglpkAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYkTSkeGST- 522
Cdd:TIGR01733 66 FILEDAGARLLLTD---------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 523 --VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVVSVPYALMKANPLSWiqkvcfyk 600
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 601 arAALVKSRDM-HWSLLAqrgqrdvslSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 678
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 679 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIC 749
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 750 VSSSATGTAYYGLLGITKNVFEAVPVTTGGapifDRPFTRTGLLGFIGPDNLVFIVGKLD 809
Cdd:TIGR01733 324 IGGPGVARGYLNRPELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRID 379
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
393-878 |
1.04e-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: 64.77 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 393 LKPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVFLALttdaCQKGL-PKAQ 468
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVL----ADAGAaDRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 469 TGEVAAFKgwpPLSWLVIDGKHLAKPPKDWHPLAQDTgtgTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEA 548
Cdd:cd05922 85 DALPASPD---PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 549 ETLTNVLDFKRDAGLwhGVLTS--------VMNRMHVVsvPYALMKAnplswiqkvcFYKARAALVKSRDMHWSLLAQRG 620
Cdd:cd05922 159 DRALTVLPLSYDYGL--SVLNThllrgatlVLTNDGVL--DDAFWED----------LREHGATGLAGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 621 QRDVSLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavls 694
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 695 mnglsygvirvdteeklsvltvQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIcVSSSATGTAYYGllgiTKNVFEAVP 774
Cdd:cd05922 286 ----------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 775 VTTGGApifdrpfTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfvyrGRIAVFSVTVLHDDR 854
Cdd:cd05922 337 GRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEK 404
|
490 500
....*....|....*....|....
gi 45827694 855 IVLVAEQRPDASEEDSFQWMSRVL 878
Cdd:cd05922 405 LALFVTAPDKIDPKDVLRSLAERL 428
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
356-813 |
1.09e-10 |
|
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: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 356 DTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIevpltrk 435
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 436 DAGSQQ--VGFLLGSCGVFLALTTdacQKGLPKAQtgevAAFKGWPPLSWLVIDGKHLAK---PPKDWHPLA-------- 502
Cdd:cd05911 66 NPIYTAdeLAHQLKISKPKVIFTD---PDGLEKVK----EAAKELGPKDKIIVLDDKPDGvlsIEDLLSPTLgeededlp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 503 ---QDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCralTQACGYSEA-----ETLTNVLDFKRDAGLWhGVLTSV 571
Cdd:cd05911 139 pplKDGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANL---SQVQTFLYGndgsnDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 572 MNRMHVVSVPyalmKANPLSWIQKVCFYKARAALVKSRDMHWslLAQRGQRDV-SLSSLRMLIVadGANPWSISSCDAFL 650
Cdd:cd05911 212 LNGATVIIMP----KFDSELFLDLIEKYKITFLYLVPPIAAA--LAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 651 NVFQSRGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPG 725
Cdd:cd05911 284 KRFPNATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 726 ANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIV 805
Cdd:cd05911 324 VEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIV 390
|
490
....*....|....
gi 45827694 806 G------KLDGLMV 813
Cdd:cd05911 391 DrkkeliKYKGFQV 404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
268-809 |
1.41e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.28 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 268 RVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSV-LRGEPLTAGVPRPPSLLATLQRwgttq 346
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVFGDQH----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 347 pkspcltaldttgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELV 424
Cdd:PRK12316 2029 ------------------LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYV 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 425 PVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKgwPPLSWlvidgkhlakppKDW---HPL 501
Cdd:PRK12316 2082 PLDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLD--RDAEW------------ADYpdtAPA 2140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 502 AQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVvsvp 581
Cdd:PRK12316 2141 VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARV---- 2215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 582 yaLMKANPLsWIQKVCFYKARAALVKSRDM---HWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAflnvfQSRGL 658
Cdd:PRK12316 2216 --LIRDDEL-WDPEQLYDEMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEAL 2285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 659 RPEVIcpcasspealtvairrppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGANVCVvkLEGTPY 738
Cdd:PRK12316 2286 RPVYL-------------------FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLN 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45827694 739 LCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 809
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY-----RTGDLARYRADGVVEYLGRID 2404
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
364-564 |
1.96e-09 |
|
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: 61.80 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 441
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 442 VGFLLGSCGVFLALTTDACQKGLPKAQtgevaafkgwppLSWLVIDGKHLAKPPKDWhPLAQDTGTGTAYIEYkTSkeGS 521
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45827694 522 T---VGVTVSHASLLAQCRALTQACGYSEAETLTNV--LDFkrDAGLW 564
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
353-538 |
2.36e-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: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 353 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 432
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 433 TrkdagSQQVGFLLGSCGVFLALTtdacqkglpkaqtgeVAAFkgwpplswlvidgKHLAKPPKDWHPLAQDTGTGTAYI 512
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190
....*....|....*....|....*....|..
gi 45827694 513 EYkTSkeGST---VGVTVSHASLLA---QCRA 538
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKA 159
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
364-551 |
6.24e-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: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 443
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 444 FLLGSCGVFLALTTDACQKGLPkaqtgevaafkGWPPLSWLVIDGKHLAKPPkdwhPLAQDTGTGTAYIEYkTSkeGST- 522
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-----------AGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GSTg 139
|
170 180 190
....*....|....*....|....*....|.
gi 45827694 523 --VGVTVSHASLLAQCRALTQACGYSEAETL 551
Cdd:cd12116 140 rpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
393-547 |
3.66e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.78 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 393 LKPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEV 472
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 473 AAFKGWPPL--------SWLVIDgkHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACG 544
Cdd:PRK08316 131 VDTLILSLVlggreapgGWLDFA--DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
...
gi 45827694 545 YSE 547
Cdd:PRK08316 209 MSA 211
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
364-630 |
7.16e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 364 TLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 441
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 442 VGFLLGSCGVFLALTTDACQKGLPKAqtgevaafKGwppLSWLVIDgkhlakPPKDW------HPLAQDTGTGTAYIEYK 515
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIP--------DG---LASLALD------RDEDWegfpahDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 516 TSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPYALmkANPLSWIQK 595
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDSL--WDPERLYAE 4779
|
250 260 270
....*....|....*....|....*....|....*
gi 45827694 596 VcfYKARAALVKSRDMHWSLLAQRGQRDVSLSSLR 630
Cdd:PRK12316 4780 I--HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
327-459 |
3.12e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 50.81 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 327 AGVPRPP-------SLLATLQRWGTTQPKSPcltALDTTGkavYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRV 399
Cdd:PRK06178 20 AGIPREPeyphgerPLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFAALLRQRG-------VGAGDRV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 400 ALVFPNSdPvMFMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVFLALTTDA 459
Cdd:PRK06178 87 AVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
364-503 |
4.18e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.34 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 443
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45827694 444 FLLGSCGVFLALTT-DACQKGLPKAQTGE-----VAAFKGW-------PPLSWLVIDGKHLAKPPKDWHPLAQ 503
Cdd:PRK08314 102 HYVTDSGARVAIVGsELAPKVAPAVGNLRlrhviVAQYSDYlpaepeiAVPAWLRAEPPLQALAPGGVVAWKE 174
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
330-805 |
7.48e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 49.41 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 330 PRPPSLLATLQRWGTTQPKSpclTALDTTGKAVytlTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDpv 409
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 410 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVFLALTTDacqKGLPkaqtgEVAAFKGWPPL--SWLVID 487
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDS---EFVP-----LLAAILPQLPTvrTVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 488 GKHLAKPPKDWH------------PLAQDTGTGTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEaetlt 552
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 553 nvldfkRDAGLwhgVLTSvMNRMHVVSVPY-ALMKANPLSWIQKVCFYKARAALVKSR--------DMHWSLLAQRGQRD 623
Cdd:PRK06187 208 ------DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDPENLLDLIETERvtfffavpTIWQMLLKAPRAYF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 624 VSLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAVLSmngl 698
Cdd:PRK06187 278 VDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTKRR---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 699 sygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttG 778
Cdd:PRK06187 340 -------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------G 394
|
490 500
....*....|....*....|....*..
gi 45827694 779 GapifdrpFTRTGLLGFIGPDNLVFIV 805
Cdd:PRK06187 395 G-------WLHTGDVGYIDEDGYLYIT 414
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
339-815 |
1.94e-05 |
|
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: 47.99 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 339 LQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPvmFMVAFYGC 418
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 419 LLAELVPVPIEVPLTRKDagsqqVGFLLGSCGvflalttdacqkglpkaqtgevaafkgwpplSWLVIDgkhlakppkDw 498
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSG-------------------------------AKVLFD---------D- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 499 hplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETL--------TNVLDFKRDAGLWHGV 567
Cdd:cd17631 100 ----------LALLMY-TS--GTTgrpKGAMLTHRNLLWNAVNALAALDLGPDDVLlvvaplfhIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 568 LTSVMNRMHVVSVpyalmkanpLSWIQ--KVCFykarAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVADGANPwsiss 645
Cdd:cd17631 167 TVVILRKFDPETV---------LDLIErhRVTS----FFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMP----- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 646 cDAFLNVFQSRGLRpevICPCASSPEALTVAIRRPPDlggppprkavlsmnglsygvirvDTEEKLSvltvqDVGQVMPG 725
Cdd:cd17631 227 -ERLLRALQARGVK---FVQGYGMTETSPGVTFLSPE-----------------------DHRRKLG-----SAGRPVFF 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 726 ANVCVVKLEGTPylCKTDEVGEICVSSSATGTAYYGLlgitknvfeavPVTTGGApIFDRPFtRTGLLGFIGPDNLVFIV 805
Cdd:cd17631 275 VEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWNR-----------PEATAAA-FRDGWF-HTGDLGRLDEDGYLYIV 339
|
490
....*....|
gi 45827694 806 GKLDGLMVTG 815
Cdd:cd17631 340 DRKKDMIISG 349
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
363-541 |
8.54e-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: 46.11 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 363 YTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsq 440
Cdd:cd12114 11 GTLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 441 qvgfLLGSCGVFLALTTDACQKGLPKAqtgevaafkgwPPLSWLVIDGKHLAKPPKDWHPLAQDTgtgtAYIEYkTSkeG 520
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVAPDDL----AYVIF-TS--G 136
|
170 180
....*....|....*....|....
gi 45827694 521 ST---VGVTVSHASLLAQCRALTQ 541
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINR 160
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
350-809 |
9.86e-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: 45.70 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 350 PCLTALDTTGKavyTLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVPIe 429
Cdd:cd05945 5 PDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVPL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 430 vpltrkDAGSqqvgfllgscgvflalttdacqkglPKAQTGEVAAfkgwpplswlvidgkhLAKPpkdwhPLAQDTGTGT 509
Cdd:cd05945 72 ------DASS-------------------------PAERIREILD----------------AAKP-----ALLIADGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 510 AYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLwHGVLTSVMNRMHVVSVPYAlMK 586
Cdd:cd05945 100 AYIIF-TS--GSTgrpKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRD-AT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 587 ANPLSWIqkvcfykarAALVKSRDMHWsllaqrgqrdVSL-SSLRMLIVADGANPWSISSCDAFLnvFqsrglrpevicp 665
Cdd:cd05945 175 ADPKQLF---------RFLAEHGITVW----------VSTpSFAAMCLLSPTFTPESLPSLRHFL--F------------ 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 666 CAsspEALTVA-----IRRPPD-----LGGPPPrkavlSMNGLSYGVIrvdTEEKLSVLTVQDVGQVMPGANVCVVKLEG 735
Cdd:cd05945 222 CG---EVLPHKtaralQQRFPDariynTYGPTE-----ATVAVTYIEV---TPEVLDGYDRLPIGYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45827694 736 TPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 809
Cdd:cd05945 291 RP--VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAY-----RTGDLVRLEADGLLFYRGRLD 353
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
719-822 |
1.50e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.33 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 719 VGQVMPGANVCVVKLEGT-PYL--CKTDEVGEICVSssatgtayygllgiTKNVFEA-VPVTTGGAPIFDRPFTRTGLLG 794
Cdd:PRK07529 388 VGLRLPYQRVRVVILDDAgRYLrdCAVDEVGVLCIA--------------GPNVFSGyLEAAHNKGLWLEDGWLNTGDLG 453
|
90 100
....*....|....*....|....*...
gi 45827694 795 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 822
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIRG--GHNID 479
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
359-538 |
1.72e-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: 45.05 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 359 GKAVY-----TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLT 433
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 434 rkdagSQQVGFLLGSCGVFLALTTDACqkgLPKAQTgevAAFKGWPPLSWLVIDGKHLAKPPKDWhpLAQDTGTGT---- 509
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGEL---APVLAA---ALTKSEHTLVVLIVSGGAGPEAGALL--LAELVAAEAeqlk 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 45827694 510 ---------AYIEYKTSKEGSTVGVTVSHASLLAQCRA 538
Cdd:cd05959 157 paathaddpAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
354-436 |
2.12e-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: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 354 ALDTTGKAVyTLTYGKLwsrsLKLAYTLLNKLTSKNeplLKPGDRVALVFPNSDPvmFMVAFYGCLLAELVPVPIEvPLT 433
Cdd:cd05926 5 ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVAPLN-PAY 73
|
...
gi 45827694 434 RKD 436
Cdd:cd05926 74 KKA 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
318-656 |
2.15e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.33 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 318 SVLRGEPLTAGVPRppSLLATLQRwgttQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGD 397
Cdd:PRK12316 502 ATAAEYPLQRGVHR--LFEEQVER----TPEAPALAFGEET------LDYAELNRRANRLAHALI-------ERGVGPDV 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 398 RVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAF 475
Cdd:PRK12316 563 LVGVAMERSIEMV--VALLAILKAggAYVPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 476 KgwPPLSWLviDGKHLAKPPKDWHPLaqdtgtGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVL 555
Cdd:PRK12316 634 D--RPAAWL--EGYSEENPGTELNPE------NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 556 DFKRDAGLWHGVLTsVMNRMHVVSVPYALMKaNPLSWIQkvcfYKARAAlVKSRDMHWSLLA--QRGQRDVSLSSLRMLI 633
Cdd:PRK12316 704 PFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVE----LINREG-VDTLHFVPSMLQafLQDEDVASCTSLRRIV 776
|
330 340
....*....|....*....|...
gi 45827694 634 VADGANPWsisscDAFLNVFQSR 656
Cdd:PRK12316 777 CSGEALPA-----DAQEQVFAKL 794
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
528-817 |
2.72e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 44.37 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 528 SHASLLAQCRALTQACGyseaetltnvLDFKRDAG-----LWHG-----VLTSVMNRMHVVSVPYALMKANPLSWIQKVC 597
Cdd:PRK05851 173 SPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 598 fyKARAALVKSRDMHWSLLAQRGQR--DVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPC---ASSPEA 672
Cdd:PRK05851 243 --DSRATLTAAPNFAYNLIGKYARRvsDVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSyglAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 673 LTVairrppdlggPPPrkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSS 752
Cdd:PRK05851 319 VTV----------PVP--------GIGLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIRG 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827694 753 SATGTAYygllgitknvfeavpvtTGGAPIFDRPFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVR 817
Cdd:PRK05851 380 ASMMSGY-----------------LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGR 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
365-442 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 365 LTYGKLWSRSLKLAYTLLNKLTSKnepllkpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI-------EVPLTRKDA 437
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPInpmlkerELEYILNDS 72
|
....*
gi 45827694 438 GSQQV 442
Cdd:cd05935 73 GAKVA 77
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
323-539 |
3.01e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 44.37 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 323 EPLTAGVPRP------PSLLATL----QRWGTtqpkSPCLTALdttGKavyTLTYGKLWSRSLKLAYTLlnkltsKNEPL 392
Cdd:PRK05677 8 DKYPAGIAAEinpdeyPNIQAVLkqscQRFAD----KPAFSNL---GK---TLTYGELYKLSGAFAAWL------QQHTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 393 LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV-------PIEVPLTRKDAGSQQVgfllgscgVFLALTTDACQKGLP 465
Cdd:PRK05677 72 LKPGDRIAVQLPNV--LQYPVAVFGAMRAGLIVVntnplytAREMEHQFNDSGAKAL--------VCLANMAHLAEKVLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 466 KAQ-----TGEVAAFKgwPPLSWLVIDG--KHLAKPPKDWH-------PLAQDTGTG------------TAYIEYKTSKE 519
Cdd:PRK05677 142 KTGvkhviVTEVADML--PPLKRLLINAvvKHVKKMVPAYHlpqavkfNDALAKGAGqpvteanpqaddVAVLQYTGGTT 219
|
250 260
....*....|....*....|...
gi 45827694 520 GSTVGVTVSHASLLA---QCRAL 539
Cdd:PRK05677 220 GVAKGAMLTHRNLVAnmlQCRAL 242
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
353-581 |
3.71e-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: 43.82 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 353 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLTSKnepllkPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI---- 428
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKDL------RGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLnpsy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 429 ---EVPLTRKDAGSQqvgfllgscgvflalttdacqkglpkaqtgevaafkgwpplswLVIDGkhlakppkdwhplaqdt 505
Cdd:cd05941 72 plaELEYVITDSEPS-------------------------------------------LVLDP----------------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45827694 506 gtgtAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVP 581
Cdd:cd05941 92 ----ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
363-426 |
5.62e-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: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827694 363 YTLTYGKLWSRSLKLAYTLLNkltsknepL-LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 426
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
364-426 |
1.59e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.96 E-value: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 426
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
339-428 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 339 LQRWGTTQPKSPCLTALDTTGKAVyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 418
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA----NALRALG---VKKGDRVAIYLPNI--PEAVIAMLAC 84
|
90
....*....|
gi 45827694 419 LLAELVPVPI 428
Cdd:COG0365 85 ARIGAVHSPV 94
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
364-428 |
2.86e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 41.04 E-value: 2.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI 428
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPL 85
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
328-532 |
3.83e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.18 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 328 GVPRPPSLLATL---QRWGTtqPKSPCLTAldttgkAVYTLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFP 404
Cdd:PRK10252 452 AVEIPETTLSALvaqQAAKT--PDAPALAD------ARYQFSYREMREQVVALANLL-------RERGVKPGDSVAVALP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 405 NSdpVMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPls 482
Cdd:PRK10252 517 RS--VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA-- 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45827694 483 wlvidgkhlakpPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASL 532
Cdd:PRK10252 586 ------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
364-542 |
4.39e-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: 40.40 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 364 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQQVG 443
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARGV-------GPGDLVALCARRS--AELVVALLAILKAGAAYVPLDP-----AYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 444 FLLGSCGVFLALTTDACQKGLPkaqtgeVAAFKGWPplswlvIDGKHLAKPPKDWHPLAQDTGTgTAYIEYkTSkeGST- 522
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGELA------VELVAVTL------LDQPGAAAGADAEPDPALDADD-LAYVIY-TS--GSTg 149
|
170 180
....*....|....*....|..
gi 45827694 523 --VGVTVSHASLLAQCRALTQA 542
Cdd:cd17651 150 rpKGVVMPHRSLANLVAWQARA 171
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
719-822 |
4.86e-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: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827694 719 VGQVMPGANVCVVKLEGTPYL---CKTDEVGEICVSSsatgtayygllgitKNVFEAVPVTTGGAPIFDRP-FTRTGLLG 794
Cdd:cd05944 176 VGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAG--------------PGVFGGYLYTEGNKNAFVADgWLNTGDLG 241
|
90 100
....*....|....*....|....*...
gi 45827694 795 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 822
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRG--GHNID 267
|
|
| |
