|
Name |
Accession |
Description |
Interval |
E-value |
| carboxyl_red |
NF041592 |
carboxylic acid reductase; |
9-1168 |
0e+00 |
|
carboxylic acid reductase;
Pssm-ID: 469476 [Multi-domain] Cd Length: 1161 Bit Score: 2286.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 9 TRRVEDLYASDAQFAAASPNEAITQAIDQPGVALPQLIRMVMEGYADRPALGQRALRFVTDPDSGRTMVELLPRFETITY 88
Cdd:NF041592 1 ARRIAELYATDPQFAAARPDPAVTAAIDQPGLRLPQIVRTVLEGYADRPALGQRAVEFVTDPATGRTSARLLPRFETITY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 89 RELWARAGTLATALSAEPaIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDN 168
Cdd:NF041592 81 RELWDRVGAVAAALAGDP-VRPGDRVAVLGFTSVDYTTIDLALIRLGAVAVPLQTSAPVAQLRPIVAETEPRVLAASVDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 169 LGDAVE-VLAGHAPARLVVFDYHGKVDTHREAVEAARARLA--GSVTIDTLAELIERGRALPATPIADSAD-DALALLIY 244
Cdd:NF041592 160 LDDAVElVLTGPAPRRLVVFDYHPEVDDHREALEAARARLAdaGPVVVETLAEVLERGRALPAAPPPASDDdDPLALLIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSFWRKSSG-WFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLA 323
Cdd:NF041592 240 TSGSTGAPKGAMYTERLVANMWRGSARaGWGPRAVPSITLNFMPMSHVMGRGTLYGTLARGGTAYFAARSDLSTLLEDLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 324 LVRPTELCFVPRIWDMVFAEFHSEVDRRLVDGADRAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVESLLaDV 403
Cdd:NF041592 320 LVRPTELNFVPRVWDMLFQEYQSELDRRAADGADRAAAEAAVKAELREDLLGGRFVSAMTGSAPISAEMKAFVESLL-DL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 404 HLVEGYGSTEAGMVLNDGMVRRPAVIDYKLVDVPELGYFGTDQPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRT 483
Cdd:NF041592 399 HLHDGYGSTEAGGVFIDGRVRRPPVLDYKLVDVPELGYFGTDRPHPRGELLVKTTTMFPGYYKRPEVTAEVFDEDGFYRT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 484 GDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSRHG-IENLK 562
Cdd:NF041592 479 GDIVAELGPDQLVYVDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYVYGNSARAYLLAVVVPTEEALARHGdAAELK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 563 PVISESLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTELADSQSNELRELRQSG 642
Cdd:NF041592 559 ALIAESLQRVAREAGLQSYEIPRDFLIETTPFTLENGLLTGIRKLARPKLKERYGERLEQLYTELAAGQADELRALRRSG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 643 PDAPVLPTLCRAAAALLGSTAADVRPDAHFADLGGDSLSALSLANLLHEIFGVDVPVGVIVSPASDLRALADHIEAAR-T 721
Cdd:NF041592 639 ADRPVLETVGRAAAALLGAAAADLRPDAHFTDLGGDSLSALTFSNLLHEIFGVEVPVGVIVSPATDLRALADYIEAERaS 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 722 GVRRPSFASIHGRSATEVHASDLTLDKFIDAATLAAAPNLPAPSAQVRTVLLTGATGFLGRYLALEWLDRMDLVNGKLIC 801
Cdd:NF041592 719 GAKRPTFASVHGRDATEVRAADLTLDKFIDAATLAAAPSLPGPSGEVRTVLLTGATGFLGRYLALEWLERLALVGGTLIC 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 802 LVRARSDEEAQARLDATFDSGDPYLVRHYRELGAGRLEVLAGDKGEADLGLDRVTWQRLADTVDLIVDPAALVNHVLPYS 881
Cdd:NF041592 799 LVRAKDDAAARARLDATFDSGDPELLAHYRELAADHLEVLAGDKGEPDLGLDRATWQRLADTVDLIVDPAALVNHVLPYS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 882 QLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFTEDADIRAISPTRRIDDSYANGYANSKWAGEVLLREAH 961
Cdd:NF041592 879 QLFGPNVVGTAELIRLALTTRLKPFTYLSTIGVGAQIEPGAFTEDADIREISPVRAIDDSYANGYGNSKWAGEVLLREAH 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 962 EQCGLPVTVFRCDMILADTSYTGQLNLPDMFTRLMLSLAATGIAPGSFYELDAHGNRQRAHYDGLPVEFVAEAICTLGTH 1041
Cdd:NF041592 959 DLCGLPVAVFRCDMILADTRYAGQLNLPDMFTRLMLSLVATGIAPGSFYELDADGNRQRAHYDGLPVDFIAEAIATLGAR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 1042 SPDRFVTYHVMNPYDDGIGLDEFVDWLNSptsgSGCTIQRIADYGEWLQRFETSLRALPDRQRHASLLPLLHNYREPAKP 1121
Cdd:NF041592 1039 VTDGFETYHVMNPHDDGIGLDEFVDWLIE----AGHPIQRIDDYADWLQRFETALRALPERQRQASLLPLLHNYRRPAPP 1114
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 489508543 1122 ICGSIAPTDQFRAAVQEAKIGPDKDIPHLTAAIIAKYISNLRLLGLL 1168
Cdd:NF041592 1115 IRGSIAPTDRFRAAVQEAKIGPDKDIPHLTPALIVKYVTDLRLLGLL 1161
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
19-603 |
0e+00 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 929.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 19 DAQFAAASPNEAITQAIDQPGVALPQLIRMVMEGYADRPALGQRALRFVTDPDSGRTMVELLPRFETITYRELWARAGTL 98
Cdd:cd17632 1 DPQFAAAAPLEAVTEAIRRPGLRLAQIIATVMTGYADRPALGQRATELVTDPATGRTTLRLLPRFETITYAELWERVGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 99 ATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVE-VLA 177
Cdd:cd17632 81 AAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEaVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 178 GHAPARLVVFDYHGKVDTHREAVEAARARLAGS---VTIDTLAELIERGRALPATPIADSADDALALLIYTSGSTGAPKG 254
Cdd:cd17632 161 GGTPPRLVVFDHRPEVDAHRAALESARERLAAVgipVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 255 AMYRESQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVP 334
Cdd:cd17632 241 AMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 335 RIWDMVFAEFHSEVDRRLVDGADRAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVESLLaDVHLVEGYGSTEA 414
Cdd:cd17632 321 RVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFMESLL-DLDLHDGYGSTEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 415 GMVLNDGMVRRPAVIDYKLVDVPELGYFGTDQPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQ 494
Cdd:cd17632 400 GAVILDGVIVRPPVLDYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 495 FVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSRHGIENLKPVISESLQEVAR 574
Cdd:cd17632 480 LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTARLRAALAESLQRIAR 559
|
570 580
....*....|....*....|....*....
gi 489508543 575 AAGLQSYEIPRDFIIETTPFTLENGLLTG 603
Cdd:cd17632 560 EAGLQSYEIPRDFLIETEPFTIANGLLSG 588
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
82-624 |
3.31e-102 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 333.80 E-value: 3.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RFETITYRELWARAGTLATALSAEPA-IRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapvtglrpivtetept 160
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGkPAPASFVGIYSINRPEWIISELACYAYSLVTVPL------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 miatsIDNLG-DAVEVLAGHAPARLVVFDyhgkvdthreaveaararlaGSVTIDTLAELIERGRALPATPIADSADDaL 239
Cdd:cd05927 63 -----YDTLGpEAIEYILNHAEISIVFCD--------------------AGVKVYSLEEFEKLGKKNKVPPPPPKPED-L 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 240 ALLIYTSGSTGAPKGAMYRESQVMSFwrkSSGWFE-PSGYPSITLN-----FMPMSHVGGRQVLYGTLSNGGT-AYFvaK 312
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTHGNIVSN---VAGVFKiLEILNKINPTdvyisYLPLAHIFERVVEALFLYHGAKiGFY--S 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 313 SDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVD------RRLVDgadrAALEAQVkAELRENV------------- 373
Cdd:cd05927 192 GDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQakgplkRKLFN----FALNYKL-AELRSGVvraspfwdklvfn 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 374 -----LGGRFVMALTGSAPISAEmtawVESLL---ADVHLVEGYGSTE--AGMVLND------GMVRRPAV-IDYKLVDV 436
Cdd:cd05927 267 kikqaLGGNVRLMLTGSAPLSPE----VLEFLrvaLGCPVLEGYGQTEctAGATLTLpgdtsvGHVGGPLPcAEVKLVDV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 437 PELGYFGTDqPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPD-QFVYLDRRNNVLKLSQGEFIAV 515
Cdd:cd05927 343 PEMNYDAKD-PNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDI-GEWLPNgTLKIIDRKKNIFKLSQGEYVAP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 516 SKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGD-----ALSRHGIE----------NLKPVISESLQEVARAAGLQS 580
Cdd:cd05927 421 EKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDvlkewAASKGGGTgsfeelcknpEVKKAILEDLVRLGKENGLKG 500
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 489508543 581 YEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLY 624
Cdd:cd05927 501 FEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
769-1054 |
4.18e-98 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 312.53 E-value: 4.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLALEWLDRmdlVNGKLICLVRARSDEEAQARLDATFDSGdpylvRHYRELGAGRLEVLAGDKGEA 848
Cdd:COG3320 1 RTVLLTGATGFLGAHLLRELLRR---TDARVYCLVRASDEAAARERLEALLERY-----GLWLELDASRVVVVAGDLTQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 849 DLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFTEDAD 928
Cdd:COG3320 73 RLGLSEAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFEEDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 929 IraisptrRIDDSYANGYANSKWAGEVLLREAHEQcGLPVTVFRCDMILADTSyTGQLNLPDMFTRLMLSLAATGIAPGs 1008
Cdd:COG3320 153 L-------DEGQGFANGYEQSKWVAEKLVREARER-GLPVTIYRPGIVVGDSR-TGETNKDDGFYRLLKGLLRLGAAPG- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489508543 1009 fyeldahgnRQRAHYDGLPVEFVAEAICTLGTHSPDRFVTYHVMNP 1054
Cdd:COG3320 223 ---------LGDARLNLVPVDYVARAIVHLSRQPEAAGRTFHLTNP 259
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
770-1167 |
9.92e-88 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 288.16 E-value: 9.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRmdLVNGKLICLVRARSDEEAQARLDATFDSgdpYLVRHYrELGAGRLEVLAGDKGEAD 849
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRR--STRAKVICLVRADSEEHAMERLREALRS---YRLWHE-NLAMERIEVVAGDLSKPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 LGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGeqippEAFTEDADI 929
Cdd:TIGR01746 75 LGLSDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVG-----AAIDLSTGV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 930 RAISPTRRIDDSYANGYANSKWAGEVLLREAHEQcGLPVTVFRCDMILADtSYTGQLNLPDMFTRLMLSLAATGIAPGSf 1009
Cdd:TIGR01746 150 TEDDATVTPYPGLAGGYTQSKWVAELLVREASDR-GLPVTIVRPGRILGD-SYTGAWNSSDILWRMVKGCLALGAYPQS- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 1010 yeldahgnrQRAHYDGLPVEFVAEAICTLGTH--SPDRFVTYHVMNPydDGIGLDEFVDWLNS---PTsgsgctiqRIAD 1084
Cdd:TIGR01746 227 ---------PELTEDLTPVDFVARAIVALSSRpaASAGGIVFHVVNP--NPVPLDEFLEWLERagyNL--------RLVS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 1085 YGEWLQRFETSLRALPDRQRHaSLLPLLHNYREPAKPicgsiAPTDQFRAAVQEAKIGPDKD---IPHLTAAIIAKYISN 1161
Cdd:TIGR01746 288 FDEWLQRLEDSDTAKRDSRRY-PLLPLLHFTGDAFES-----DETDTRNLDSRSTAEALEGDgirEPSITAPLLHLYLQY 361
|
....*.
gi 489508543 1162 LRLLGL 1167
Cdd:TIGR01746 362 LKEIGF 367
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
42-626 |
1.59e-86 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 292.77 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALGQralrfvtdPDSGRtmvellprFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNS 121
Cdd:COG1022 13 LPDLLRRRAARFPDRVALRE--------KEDGI--------WQSLTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 122 VDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVLAGHAPA--RLVVFDyhgkvdthrea 199
Cdd:COG1022 76 PEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSlrHIVVLD----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 200 veaaRARLAGSVTIDTLAELIERGRALP-----ATPIADSADDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFE 274
Cdd:COG1022 145 ----PRGLRDDPRLLSLDELLALGREVAdpaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 275 PSGyPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVakSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVD----- 349
Cdd:COG1022 221 LGP-GDRTLSFLPLAHVFERTVSYYALAAGATVAFA--ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaggl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 350 -RRLVDGADRAALEAQVKAE-----------------------LREnVLGGRFVMALTGSAPISAEMTAWVESLlaDVHL 405
Cdd:COG1022 298 kRKLFRWALAVGRRYARARLagkspslllrlkhaladklvfskLRE-ALGGRLRFAVSGGAALGPELARFFRAL--GIPV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 406 VEGYGSTEAGMVLNdgmVRRPAviDYKlvdvpelgyFGT-DQPYP--------RGELLVKTQTMFPGYYQRPDVTAEVFD 476
Cdd:COG1022 375 LEGYGLTETSPVIT---VNRPG--DNR---------IGTvGPPLPgvevkiaeDGEILVRGPNVMKGYYKNPEATAEAFD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 477 PDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNsARAYPLAVVVPSGDAL-- 553
Cdd:COG1022 441 ADGWLHTGDI-GELDEDGFLRItGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGD-GRPFLAALIVPDFEALge 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 554 --SRHGIENLKP--------VISESLQEVARA-AGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLER 622
Cdd:COG1022 519 waEENGLPYTSYaelaqdpeVRALIQEEVDRAnAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEA 598
|
....
gi 489508543 623 LYTE 626
Cdd:COG1022 599 LYAG 602
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
24-628 |
2.67e-79 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 274.28 E-value: 2.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 24 AASPNEAITQAIDQPGVA-LPQLIRMVMEGYADRPALGQRalrfvTDPDSgrTMVEllprFETITYRElwarAGTLATAL 102
Cdd:PLN02736 27 ARSPLKLVSRFPDHPEIGtLHDNFVYAVETFRDYKYLGTR-----IRVDG--TVGE----YKWMTYGE----AGTARTAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 103 SA---EPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVLAGH 179
Cdd:PLN02736 92 GSglvQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 180 APARLVVFdyHGKVDTHREAVEAArarlaGSVTIDTLAELIERGRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRE 259
Cdd:PLN02736 172 PSVRLIVV--VGGADEPLPSLPSG-----TGVEIVTYSKLLAQGRSSPQPFRPPKPED-VATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 260 SQVMSFWRKSSgwFEPSGYPS-ITLNFMPMSHVGGRQVLYGTLSNGGTAYFVaKSDLSTLFEDLALVRPTELCFVPRIWD 338
Cdd:PLN02736 244 GNLIANVAGSS--LSTKFYPSdVHISYLPLAHIYERVNQIVMLHYGVAVGFY-QGDNLKLMDDLAALRPTIFCSVPRLYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 339 MVFAEFHSEVD------RRLVDGA---DRAALE--------------AQVKAELrenvlGGRFVMALTGSAPISAEMTAW 395
Cdd:PLN02736 321 RIYDGITNAVKesgglkERLFNAAynaKKQALEngknpspmwdrlvfNKIKAKL-----GGRVRFMSSGASPLSPDVMEF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLLADVhLVEGYGSTE-----AGMVLND---GMVRRP-AVIDYKLVDVPELGYFGTDQPYPRGELLVKTQTMFPGYYQ 466
Cdd:PLN02736 396 LRICFGGR-VLEGYGMTEtscviSGMDEGDnlsGHVGSPnPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 467 RPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVV 546
Cdd:PLN02736 475 DEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 547 VPSGDAL----SRHGI--ENLK-----PVISE----SLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQ 611
Cdd:PLN02736 555 VVDPEVLkawaASEGIkyEDLKqlcndPRVRAavlaDMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQ 634
|
650
....*....|....*..
gi 489508543 612 LKKFYGERLERLYTELA 628
Cdd:PLN02736 635 AKAYFAKAISDMYAELA 651
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
770-1088 |
3.33e-76 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 253.34 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRMDlvNGKLICLVRARSDEEAQARLDATFDSgdpYLVRHYRELGAGRLEVLAGDKGEAD 849
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKN--VSKIYCLVRAKDEEAALERLIDNLKE---YGLNLWDELELSRIKVVVGDLSKPN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 LGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFTEDADI 929
Cdd:cd05235 76 LGLSDDDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEESD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 930 RAISPtrriDDSYANGYANSKWAGEVLLREAHEQcGLPVTVFRCDMILADtSYTGQLNLPDMFTRLMLSLAATGIAPGSf 1009
Cdd:cd05235 156 DMLES----QNGLPNGYIQSKWVAEKLLREAANR-GLPVAIIRPGNIFGD-SETGIGNTDDFFWRLLKGCLQLGIYPIS- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 1010 yeldahgnrqRAHYDGLPVEFVAEAICTLGTHSPDRFVTYHVMNPydDGIGLDEFVDWLNSPtsgsGCTIQRIaDYGEW 1088
Cdd:cd05235 229 ----------GAPLDLSPVDWVARAIVKLALNESNEFSIYHLLNP--PLISLNDLLDALEEK----GYSIKEV-SYEEW 290
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
773-1035 |
4.38e-73 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 243.29 E-value: 4.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 773 LTGATGFLGRYLALEWLDRMDLVnGKLICLVRARSDEEAQARLDATFDSGDPYLVRhyRELGAGRLEVLAGDKGEADLGL 852
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTPDV-KKIYLLVRAKDGESALERLRQELEKYPLFDAL--LKEALERIVPVAGDLSEPNLGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 853 DRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRK-PYIYTSTiAVGEQIPPEAFTEDA---- 927
Cdd:pfam07993 78 SEEDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLkPFHHVST-AYVNGERGGLVEEKPypeg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 928 --DIRAISPTRRIDDSYANGYANSKWAGEVLLREAHEqCGLPVTVFRCDMILADtSYTGQLNLPDMFTRLMLSLAATGIA 1005
Cdd:pfam07993 157 edDMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAAR-RGLPVVIYRPSIITGE-PKTGWINNFDFGPRGLLGGIGKGVL 234
|
250 260 270
....*....|....*....|....*....|
gi 489508543 1006 PGSFYELDahgnrqrAHYDGLPVEFVAEAI 1035
Cdd:pfam07993 235 PSILGDPD-------AVLDLVPVDYVANAI 257
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
231-609 |
1.64e-70 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 245.20 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 231 IADSADDALALLIYTSGSTGAPKGAMYRESQVMS----FWRKSSGWFEPSGYpsiTLNFMPMSHV------------GGR 294
Cdd:cd17639 82 FTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVPELLGPDDR---YLAYLPLAHIfelaaenvclyrGGT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 295 qVLYG---TLSNggTAYFVAKSDLSTLfedlalvRPTELCFVPRIWDMVFAEFHSEVD------------------RRLV 353
Cdd:cd17639 159 -IGYGsprTLTD--KSKRGCKGDLTEF-------KPTLMVGVPAIWDTIRKGVLAKLNpmgglkrtlfwtayqsklKALK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 354 DGADRAALEAQVKAELREnVLGGRFVMALTGSAPISAEMTAWVESLLADVhlVEGYGSTE---AGMV-----LNDGMVRR 425
Cdd:cd17639 229 EGPGTPLLDELVFKKVRA-ALGGRLRYMLSGGAPLSADTQEFLNIVLCPV--IQGYGLTEtcaGGTVqdpgdLETGRVGP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 426 P-AVIDYKLVDVPELGYFgTDQPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPD-QFVYLDRRNN 503
Cdd:cd17639 306 PlPCCEIKLVDWEEGGYS-TDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDI-GEFHPDgTLKIIDRKKD 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 504 VLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSR----HGIEN-----------LKPVISES 568
Cdd:cd17639 384 LVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKlaekHGVINseweelcedkkLQKAVLKS 463
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489508543 569 LQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLAR 609
Cdd:cd17639 464 LAETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
85-612 |
6.29e-70 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 241.73 E-value: 6.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPL-QTSAPvtglrpivteteptmia 163
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIAL-GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSA----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgDAVEVLAGHAPARLVvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpIADSADDaLALLI 243
Cdd:cd05907 67 -------EQIAYILNDSEAKAL---------------------------------------------FVEDPDD-LATII 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAM--YResqvmSFWRKSSGWFE--PSGYPSITLNFMPMSHV-GGRQVLYGTLSNGGTAYFVakSDLSTL 318
Cdd:cd05907 94 YTSGTTGRPKGVMlsHR-----NILSNALALAErlPATEGDRHLSFLPLAHVfERRAGLYVPLLAGARIYFA--SSAETL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVFAefhsevdrrlvdgADRAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVES 398
Cdd:cd05907 167 LDDLSEVRPTVFLAVPRVWEKVYA-------------AIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LlaDVHLVEGYGSTEAGMVLNdgmVRRPAVIDYKLVDVPELGyfGTDQPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPD 478
Cdd:cd05907 234 L--GIPVYEGYGLTETSAVVT---LNPPGDNRIGTVGKPLPG--VEVRIADDGEILVRGPNVMLGYYKNPEATAEALDAD 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 479 GFYRTGDImAKVGPDQFVYL-DRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNsARAYPLAVVVPSGDAL---- 553
Cdd:cd05907 307 GWLHTGDL-GEIDEDGFLHItGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGD-GRPFLVALIVPDPEALeawa 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 554 SRHGIENLKP--------VISESLQEVARA-AGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQL 612
Cdd:cd05907 385 EEHGIAYTDVaelaanpaVRAEIEAAVEAAnARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-508 |
7.88e-61 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.48 E-value: 7.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTM 161
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 162 IatsidnLGDAVEVLAGHAPARLVVFDYHGKVDTHREAVEAArarlagsvtiDTLAELIERGRALPATPIADSADDaLAL 241
Cdd:pfam00501 97 L------ITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKE----------EPLPEEAKPADVPPPPPPPPDPDD-LAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LIYTSGSTGAPKGAMYR----ESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQV-LYGTLSNGGTAYFVAKS--- 313
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRV-LSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFpal 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 DLSTLFEDLALVRPTELCFVPRIWDMVFAEfhsevdrrlvdgadrAALEAQVKAELRenvlggrfvMALTGSAPISAEMT 393
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLEA---------------GAPKRALLSSLR---------LVLSGGAPLPPELA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 394 AWVESLLADvHLVEGYGSTEAGMV------LNDGMVRRPAV------IDYKLVDVPELGYFGTDQPyprGELLVKTQTMF 461
Cdd:pfam00501 295 RRFRELFGG-ALVNGYGLTETTGVvttplpLDEDLRSLGSVgrplpgTEVKIVDDETGEPVPPGEP---GELCVRGPGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489508543 462 PGYYQRPDVTAEVFDPDGFYRTGDImAKVGPD-QFVYLDRRNNVLKLS 508
Cdd:pfam00501 371 KGYLNDPELTAEAFDEDGWYRTGDL-GRRDEDgYLEIVGRKKDQIKLG 417
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
45-630 |
7.38e-55 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 203.71 E-value: 7.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 45 LIRMVMEGYADRPALGQRAlrfVTDPDSGRTMVEllprfetiTYRELWARAGTLATALSAePAIRPGDRVCVLGFNSVDY 124
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRRE---IVDGKPGKYVWQ--------TYQEVYDIVIKLGNSLRS-VGVKDEAKCGIYGANSPEW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 125 TTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVLAGHAPARLVVFDYHGKVDTHREAVEAAr 204
Cdd:PLN02614 118 IISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 205 arlagSVTIDTLAELIERGRALP-ATPIADSADdaLALLIYTSGSTGAPKGAMYRESQ-------VMSFWRKSSgwfEPS 276
Cdd:PLN02614 197 -----GLVIYAWDEFLKLGEGKQyDLPIKKKSD--ICTIMYTSGTTGDPKGVMISNESivtliagVIRLLKSAN---AAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 277 GYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFvAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVD------R 350
Cdd:PLN02614 267 TVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGF-WRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSdggflkK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 351 RLVDGA----------DRAALEAQ------VKAELRENvLGGRFVMALTGSAPISAEMTAWVEsLLADVHLVEGYGSTEA 414
Cdd:PLN02614 346 FVFDSAfsykfgnmkkGQSHVEASplcdklVFNKVKQG-LGGNVRIILSGAAPLASHVESFLR-VVACCHVLQGYGLTES 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 415 ------------GMVlndGMVRRPAV-IDYKLVDVPELGYFGTDQPyPRGELLVKTQTMFPGYYQRPDVTAEVFdPDGFY 481
Cdd:PLN02614 424 cagtfvslpdelDML---GTVGPPVPnVDIRLESVPEMEYDALAST-PRGEICIRGKTLFSGYYKREDLTKEVL-IDGWL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 482 RTGDImAKVGPD-QFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSRHGIEN 560
Cdd:PLN02614 499 HTGDV-GEWQPNgSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAEN 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 561 --------------LKPVISESLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTE 626
Cdd:PLN02614 578 gvsgdynalcqnekAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKT 657
|
....
gi 489508543 627 LADS 630
Cdd:PLN02614 658 TNEK 661
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
53-626 |
1.50e-53 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 199.68 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 53 YADRPALGQRAlrfVTDPDSGRtmvellprFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALI 132
Cdd:PLN02861 56 YPNNQMLGRRQ---VTDSKVGP--------YVWLTYKEVYDAAIRIGSAIRSR-GVNPGDRCGIYGSNCPEWIIAMEACN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 133 RLGAVSVPLqtsapvtglrpivteteptmiatsIDNLG-DAVEVLAGHAPARLVvFDYHGKVDTHREAVEAARARLAGSV 211
Cdd:PLN02861 124 SQGITYVPL------------------------YDTLGaNAVEFIINHAEVSIA-FVQESKISSILSCLPKCSSNLKTIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 212 TI-DTLAELIERGRALPAT-------PIADSAD--------DALALLIYTSGSTGAPKGAMYRE----SQVMS----FWR 267
Cdd:PLN02861 179 SFgDVSSEQKEEAEELGVScfsweefSLMGSLDcelppkqkTDICTIMYTSGTTGEPKGVILTNraiiAEVLStdhlLKV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 268 KSSGWFEPSGYPSitlnFMPMSHVGGRQVLYGTLSNGGTAYFvAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSE 347
Cdd:PLN02861 259 TDRVATEEDSYFS----YLPLAHVYDQVIETYCISKGASIGF-WQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 348 VD------RRLVDGA--------------DRAA--LEAQVKAELRENvLGGRFVMALTGSAPISAEMTAWVESLLADVhL 405
Cdd:PLN02861 334 ISsggmlrKKLFDFAynyklgnlrkglkqEEASprLDRLVFDKIKEG-LGGRVRLLLSGAAPLPRHVEEFLRVTSCSV-L 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 406 VEGYGSTE---------AGMVLNDGMVRRP-AVIDYKLVDVPELGYFGTDQpYPRGELLVKTQTMFPGYYQRPDVTAEVF 475
Cdd:PLN02861 412 SQGYGLTEscggcftsiANVFSMVGTVGVPmTTIEARLESVPEMGYDALSD-VPRGEICLRGNTLFSGYHKRQDLTEEVL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 476 DpDGFYRTGDImAKVGPD-QFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDAL- 553
Cdd:PLN02861 491 I-DGWFHTGDI-GEWQPNgAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALe 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 554 ---SRHGI--------ENLKP--VISESLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERL 620
Cdd:PLN02861 569 dwaANNNKtgdfkslcKNLKArkYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCI 648
|
....*.
gi 489508543 621 ERLYTE 626
Cdd:PLN02861 649 DQLYSE 654
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
87-632 |
4.26e-53 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 198.12 E-value: 4.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEPAiRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapvtglrpivteteptmiatsI 166
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGA-EPGSRVGIYGSNCPQWIVAMEACAAHSLICVPL------------------------Y 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 DNLG-DAVEVLAGHAPARlVVFDYHGKVDTHREAVEAARARLAGSVTIDTLAE------------------LIERGRALP 227
Cdd:PLN02430 133 DTLGpGAVDYIVDHAEID-FVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEeesdkasqigvktyswidFLHMGKENP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 228 ATPIADSADDaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFE----PSGYPSITLNFMPMSHVGGRQVlygtlsn 303
Cdd:PLN02430 212 SETNPPKPLD-ICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedKMTHDDVYLSFLPLAHILDRMI------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 304 ggTAYFVAKS--------DLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVD-----RRLVDG--------------- 355
Cdd:PLN02430 284 --EEYFFRKGasvgyyhgDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQelnprRRLIFNalykyklawmnrgys 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 356 -------ADRAALEaQVKAELrenvlGGRFVMALTGSAPISAEmtawVESLL---ADVHLVEGYGSTE----AGMVLNDG 421
Cdd:PLN02430 362 hkkaspmADFLAFR-KVKAKL-----GGRLRLLISGGAPLSTE----IEEFLrvtSCAFVVQGYGLTEtlgpTTLGFPDE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 422 M-----VRRPAVI-DYKLVDVPELGYFGTDQPyPRGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQF 495
Cdd:PLN02430 432 McmlgtVGAPAVYnELRLEEVPEMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDI-GEILPNGV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 496 V-YLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSRHGIEN-------------- 560
Cdd:PLN02430 509 LkIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNgftgsfeelcslpe 588
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 561 LKPVISESLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTELADSQS 632
Cdd:PLN02430 589 LKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKLAEKRI 660
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
42-622 |
1.16e-48 |
|
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: 180.01 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALgqralrfvTDPDsgrtmvellprfETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNS 121
Cdd:COG0318 1 LADLLRRAAARHPDRPAL--------VFGG------------RRLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 122 VDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEptmiatsidnlgdavevlaghapARLVVFdyhgkvdthreave 201
Cdd:COG0318 60 PEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG-----------------------ARALVT-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 202 aararlagsvtidtlaeliergralpatpiadsaddalALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGyPSI 281
Cdd:COG0318 103 --------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDV 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 282 TLNFMPMSHVGG-RQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVfaefhseVDRRLVDGADRAA 360
Cdd:COG0318 144 VLVALPLFHVFGlTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARL-------LRHPEFARYDLSS 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 361 LEaqvkaelrenvlggrfvMALTGSAPISAE-MTAWVEslLADVHLVEGYGSTEAGMV----LNDGMVRRPAVI------ 429
Cdd:COG0318 217 LR-----------------LVVSGGAPLPPElLERFEE--RFGVRIVEGYGLTETSPVvtvnPEDPGERRPGSVgrplpg 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 430 -DYKLVDVpelgyfgTDQPYPR---GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNV 504
Cdd:COG0318 278 vEVRIVDE-------DGRELPPgevGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDL-GRLDEDGYLYIvGRKKDM 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 505 LKLSqGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAY---PLAVVVPSGDAlsrhgienlkPVISESLQEVARAAgLQSY 581
Cdd:COG0318 349 IISG-GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgerVVAFVVLRPGA----------ELDAEELRAFLRER-LARY 416
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 489508543 582 EIPRDF-IIETTPftlenglLTGIRKLARPQLKKFYGERLER 622
Cdd:COG0318 417 KVPRRVeFVDELP-------RTASGKIDRRALRERYAAGALE 451
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
42-625 |
8.37e-48 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 183.01 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALGQRAL---RFVTDPDsGRTMVEL-LPRFETITYRELWARAGTLATALsAEPAIRPGDRVCVL 117
Cdd:PLN02387 60 LAALFEQSCKKYSDKRLLGTRKLisrEFETSSD-GRKFEKLhLGEYEWITYGQVFERVCNFASGL-VALGHNKEERVAIF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 118 GFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETE-PTMIATS-----IDNLGDAVEVLAghapaRLVVFDYHG 191
Cdd:PLN02387 138 ADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEvTTVICDSkqlkkLIDISSQLETVK-----RVIYMDDEG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 192 KVDThreaveaARARLAGSVTIDTLAELIERGRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSG 271
Cdd:PLN02387 213 VDSD-------SSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPND-IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 272 WFEPSGYPSITLNFMPMSHV-----------GGRQVLYG---TL---SNG---GTayfvaKSDLSTLfedlalvRPTELC 331
Cdd:PLN02387 285 VVPKLGKNDVYLAYLPLAHIlelaaesvmaaVGAAIGYGsplTLtdtSNKikkGT-----KGDASAL-------KPTLMT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 332 FVPRIWDMVFAEFHSEVD---------------RRL--VDGA-------DRAALEAQVKAELREnVLGGRFVMALTGSAP 387
Cdd:PLN02387 353 AVPAILDRVRDGVRKKVDakgglakklfdiaykRRLaaIEGSwfgawglEKLLWDALVFKKIRA-VLGGRIRFMLSGGAP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 388 ISAEMTAWVESLLAdVHLVEGYGSTE--AGMVLND------GMVRRPAVIDY-KLVDVPELGYFGTDQPYPRGELLVKTQ 458
Cdd:PLN02387 432 LSGDTQRFINICLG-APIGQGYGLTEtcAGATFSEwddtsvGRVGPPLPCCYvKLVSWEEGGYLISDKPMPRGEIVIGGP 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 459 TMFPGYYQRPDVTAEVFDPDG-----FYrTGDImAKVGPDQFV-YLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIF 532
Cdd:PLN02387 511 SVTLGYFKNQEKTDEVYKVDErgmrwFY-TGDI-GQFHPDGCLeIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 533 IYGNSARAYPLAVVVPSGDAL----SRHGI------------ENLKPVISeSLQEVARAAGLQSYEIPRDFIIETTPFTL 596
Cdd:PLN02387 589 VHADPFHSYCVALVVPSQQALekwaKKAGIdysnfaelcekeEAVKEVQQ-SLSKAAKAARLEKFEIPAKIKLLPEPWTP 667
|
650 660
....*....|....*....|....*....
gi 489508543 597 ENGLLTGIRKLARPQLKKFYGERLERLYT 625
Cdd:PLN02387 668 ESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
39-626 |
6.42e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 177.09 E-value: 6.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 39 GVALPQLIRMVMEGYADRPALGQRALRFV-----TDPD-SGRTM-VELLPRFETITYRELWARAGTLATALsAEPAIRPG 111
Cdd:PTZ00216 68 GPNFLQRLERICKERGDRRALAYRPVERVekevvKDADgKERTMeVTHFNETRYITYAELWERIVNFGRGL-AELGLTKG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 112 DRVCVLGFNSVDY--TTIDIALIRLGAVSV--PLQTSAPVTGLRpivtETEPTMIATSIDNLGDAVEVL-AGHAPARLVV 186
Cdd:PTZ00216 147 SNVAIYEETRWEWlaSIYGIWSQSMVAATVyaNLGEDALAYALR----ETECKAIVCNGKNVPNLLRLMkSGGMPNTTII 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 187 FdyhgkVDTHREAVEAararlaGSVTIDTLAELIERGRALPAT---PIADSADDaLALLIYTSGSTGAPKGAMYRESQVM 263
Cdd:PTZ00216 223 Y-----LDSLPASVDT------EGCRLVAWTDVVAKGHSAGSHhplNIPENNDD-LALIMYTSGTTGDPKGVMHTHGSLT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 264 SFWRKSSGWF-EPSGYPSIT---LNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFE----DLALVRPTELCFVPR 335
Cdd:PTZ00216 291 AGILALEDRLnDLIGPPEEDetyCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFArphgDLTEFRPVFLIGVPR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 336 IWD------------------MVF-AEFHSEVdRRLVDGADRAALEAQVKAELREnVLGGRFVMALTGSAPISAEMTAWV 396
Cdd:PTZ00216 371 IFDtikkaveaklppvgslkrRVFdHAYQSRL-RALKEGKDTPYWNEKVFSAPRA-VLGGRVRAMLSGGGPLSAATQEFV 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 ESLLADVhlVEGYGSTEAgmVLNdGMVRRPAVIDY------------KLVDVPElgYFGTDQPYPRGELLVKTQTMFPGY 464
Cdd:PTZ00216 449 NVVFGMV--IQGWGLTET--VCC-GGIQRTGDLEPnavgqllkgvemKLLDTEE--YKHTDTPEPRGEILLRGPFLFKGY 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 465 YQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVL-KLSQGEFIAVSKLEAVFGDSPLVRQ--IFIYGNSARAY 541
Cdd:PTZ00216 522 YKQEELTREVLDEDGWFHTGDV-GSIAANGTLRIIGRVKALaKNCLGEYIALEALEALYGQNELVVPngVCVLVHPARSY 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 542 PLAVVV---PSGDALSR-HGIENLKPVI----------SESLQEVARAAGLQSYEIPRDFII---ETTPftlENGLLTGI 604
Cdd:PTZ00216 601 ICALVLtdeAKAMAFAKeHGIEGEYPAIlkdpefqkkaTESLQETARAAGRKSFEIVRHVRVlsdEWTP---ENGVLTAA 677
|
650 660
....*....|....*....|..
gi 489508543 605 RKLARPQLKKFYGERLERLYTE 626
Cdd:PTZ00216 678 MKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
83-610 |
9.55e-45 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 169.08 E-value: 9.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 83 FETITYRELWARAGTLATALSAePAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMI 162
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 163 atsidnlgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpIADSADDALALL 242
Cdd:cd17640 82 --------------------------------------------------------------------VVENDSDDLATI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 243 IYTSGSTGAPKGAMYRE----SQVMSFWRkssgwFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFvakSDLSTL 318
Cdd:cd17640 94 IYTSGTTGNPKGVMLTHanllHQIRSLSD-----IVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY---TSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVFAEFHSEVdrrlvdgadrAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVES 398
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQV----------SKSSPIKQFLFLFFLSGGIFKFGISGGGALPPHVDTFFEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LlaDVHLVEGYGSTEAGMVLNDGMVRRPAV---------IDYKLVDvpELGyfGTDQPYP-RGELLVKTQTMFPGYYQRP 468
Cdd:cd17640 236 I--GIEVLNGYGLTETSPVVSARRLKCNVRgsvgrplpgTEIKIVD--PEG--NVVLPPGeKGIVWVRGPQVMKGYYKNP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 469 DVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPlAVVVP 548
Cdd:cd17640 310 EATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG-ALIVP 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 549 SGDAL-------------SRHGIENLKPVIS----ESLQEVARAAGLQSYEIPRDFIIETTPFTlENGLLTGIRKLARP 610
Cdd:cd17640 389 NFEELekwakesgvklanDRSQLLASKKVLKlyknEIKDEISNRPGFKSFEQIAPFALLEEPFI-ENGEMTQTMKIKRN 466
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
658-1113 |
3.93e-43 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 172.17 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 658 LLGSTAADVRPDAHFADLGGDSLSALSLANLLHEIFGVDVPVGVIVSPASdLRALADHIEAARTGvrrpSFASIHGRSAT 737
Cdd:TIGR03443 860 LLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT-IKGFAKEVDRLKKG----EELADEGDSEI 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 738 EVHASDLTLDKFIDAATLAaaPNLP--------APSAQVRTVLLTGATGFLGRYLALEWLDRMDLVNGKLICLVRARSDE 809
Cdd:TIGR03443 935 EEEETVLELDYAKDAKTLV--DSLPksypsrkeLDASTPITVFLTGATGFLGSFILRDLLTRRSNSNFKVFAHVRAKSEE 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 810 EAQARLDatfDSGDPYLVrhYRELGAGRLEVLAGDKGEADLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAA 889
Cdd:TIGR03443 1013 AGLERLR---KTGTTYGI--WDEEWASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVI 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 890 GTAELLRLALTGKRKPYIYTSTIAVgeqIPPEAFTEDAD--IRA----ISPTRRIDDS---YANGYANSKWAGEVLLREA 960
Cdd:TIGR03443 1088 GTINVLNLCAEGKAKQFSFVSSTSA---LDTEYYVNLSDelVQAggagIPESDDLMGSskgLGTGYGQSKWVAEYIIREA 1164
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 961 HEQcGLPVTVFRCDMILADtSYTGQLNLPDMFTRLMLSLAATGIAPgsfyelDAHGNrqrahYDGLPVEFVAEAICTLGT 1040
Cdd:TIGR03443 1165 GKR-GLRGCIVRPGYVTGD-SKTGATNTDDFLLRMLKGCIQLGLIP------NINNT-----VNMVPVDHVARVVVAAAL 1231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 1041 HSP--DRFVTYHVMN-PyddGIgldEFVDWLNsptsgsgcTIQR------IADYGEWLQRFEtslRALPDRQRHASLLPL 1111
Cdd:TIGR03443 1232 NPPkeSELAVAHVTGhP---RI---RFNDFLG--------TLKTygydveIVDYVHWRKSLE---RFVIERSEDNALFPL 1294
|
..
gi 489508543 1112 LH 1113
Cdd:TIGR03443 1295 LH 1296
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
82-616 |
1.62e-42 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 163.41 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETE-PT 160
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRAL-GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEsKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATSIDNLGDAVEVLAGHAPARLVVfdYHGKVDTHREaveaararlagsvtidtLAELIERGRALPATPIADsaDDALA 240
Cdd:cd05932 82 LFVGKLDDWKAMAPGVPEGLISISLP--PPSAANCQYQ-----------------WDDLIAQHPPLEERPTRF--PEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 241 LLIYTSGSTGAPKGAMyresqvMSFwrKSSGWFEPSGYPSI-------TLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKS 313
Cdd:cd05932 141 TLIYTSGTTGQPKGVM------LTF--GSFAWAAQAGIEHIgteendrMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 dLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRLVDGADRAALeaqVKAELRENVLGG----RFVMALTGSAPIS 389
Cdd:cd05932 213 -LDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKIPV---VNSLVKRKVLKGlgldQCRLAGCGSAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 390 AEMTAWVESLLADVhlVEGYGSTEAgmvlndgmvrrpavIDYKLVDVP---ELGYFGtdQPYP--------RGELLVKTQ 458
Cdd:cd05932 289 PALLEWYRSLGLNI--LEAYGMTEN--------------FAYSHLNYPgrdKIGTVG--NAGPgvevriseDGEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 459 TMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGnSA 538
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG-SG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 539 RAYPLAVVVPSGDAlSRHGIENLKPVISESLQEVARA--AGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFY 616
Cdd:cd05932 430 LPAPLALVVLSEEA-RLRADAFARAELEASLRAHLARvnSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
239-589 |
2.65e-42 |
|
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: 158.22 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 LALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTL 318
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG-GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVfaefhseVDRRLVDGADRAALeaqvkaelrenvlggrfVMALTGSAPISAEMTAWVES 398
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARL-------LKAPESAGYDLSSL-----------------RALVSGGAPLPPELLERFEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLaDVHLVEGYGSTEAGMVLN----DGMVRRP-------AVIDYKLVDVPElgyfGTDQPYPRGELLVKTQTMFPGYYQR 467
Cdd:cd04433 137 AP-GIKLVNGYGLTETGGTVAtgppDDDARKPgsvgrpvPGVEVRIVDPDG----GELPPGEIGELVVRGPSVMKGYWNN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 468 PDVTAEvFDPDGFYRTGDImAKVGPDQFVY-LDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFIYG---NSARAYPL 543
Cdd:cd04433 212 PEATAA-VDEDGWYRTGDL-GRLDEDGYLYiVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVGvpdPEWGERVV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489508543 544 AVVVPsgdalsrhgiENLKPVISESLQEVARAAgLQSYEIPRDFII 589
Cdd:cd04433 289 AVVVL----------RPGADLDAEELRAHVRER-LAPYKVPRRVVF 323
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
83-552 |
1.69e-40 |
|
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: 156.99 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 83 FETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMI 162
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 163 ATSIDNLGDAVEVLAGHAP-ARLVVFDyhgkvdTHREAVeaararlaGSVTIDTLAELIERGRALPATPIaDSADDALAL 241
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPkDKIIVLD------DKPDGV--------LSIEDLLSPTLGEEDEDLPPPLK-DGKDDTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LiYTSGSTGAPKGAMY-RESQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFE 320
Cdd:cd05911 152 L-YSSGTTGLPKGVCLsHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPRIwdMVFAEFHSEVDRrlvdgADRAALEaqvkaelrenvlggrfvMALTGSAPISAEMTAWVESLL 400
Cdd:cd05911 231 LIEKYKITFLYLVPPI--AAALAKSPLLDK-----YDLSSLR-----------------VILSGGAPLSKELQELLAKRF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEAGMVLN---DGMVRRPAV------IDYKLVDVPELGYFGTDQPyprGELLVKTQTMFPGYYQRPDVT 471
Cdd:cd05911 287 PNATIKQGYGMTETGGILTvnpDGDDKPGSVgrllpnVEAKIVDDDGKDSLGPNEP---GEICVRGPQVMKGYYNNPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 472 AEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ---IFIYGNSARAYPLAVVV 547
Cdd:cd05911 364 KETFDEDGWLHTGDI-GYFDEDGYLYIvDRKKELIKY-KGFQVAPAELEAVLLEHPGVADaavIGIPDEVSGELPRAYVV 441
|
....*
gi 489508543 548 PSGDA 552
Cdd:cd05911 442 RKPGE 446
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
84-504 |
2.69e-35 |
|
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: 141.16 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQtsapvtglrPIVTETEptmia 163
Cdd:cd05936 23 RKLTYRELDALAEAFAAGL-QNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN---------PLYTPRE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdaVEVLAGHAPARLVVfdyhgkvdthreaveaararlagsvTIDTLAELIERGRALPATPiADSADDaLALLI 243
Cdd:cd05936 88 ---------LEHILNDSGAKALI-------------------------VAVSFTDLLAAGAPLGERV-ALTPED-VAVLQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPS-ITLNFMPMSHVGGRQV--LYGTLsNGGTAYFVAKSDLSTLFE 320
Cdd:cd05936 132 YTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDdVVLAALPLFHVFGLTValLLPLA-LGATIVLIPRFRPIGVLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPRIWDMVFAefHSEVDRRlvdgaDRAALeaqvkaelrenvlggRFvmALTGSAPISAEM-TAWVEsl 399
Cdd:cd05936 211 EIRKHRVTIFPGVPTMYIALLN--APEFKKR-----DFSSL---------------RL--CISGGAPLPVEVaERFEE-- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LADVHLVEGYGSTEAGMV--LN--DGmVRRPAVI-------DYKLVDVP--ELGyfgtdqPYPRGELLVKTQTMFPGYYQ 466
Cdd:cd05936 265 LTGVPIVEGYGLTETSPVvaVNplDG-PRKPGSIgiplpgtEVKIVDDDgeELP------PGEVGELWVRGPQVMKGYWN 337
|
410 420 430
....*....|....*....|....*....|....*....
gi 489508543 467 RPDVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNV 504
Cdd:cd05936 338 RPEETAEAFV-DGWLRTGDI-GYMDEDGYFFIvDRKKDM 374
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
53-500 |
4.29e-35 |
|
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: 141.22 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 53 YADRPALgqralrfvTDPDSGRTmvellprfetITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALI 132
Cdd:cd05904 18 HPSRPAL--------IDAATGRA----------LTYAELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 133 RLGAVsvplqtsapVTGLRPIVTETEptmIATSIDNLG--------DAVEVLAGHApARLVVFDyhgkvdthreaveAAR 204
Cdd:cd05904 79 SLGAV---------VTTANPLSTPAE---IAKQVKDSGaklafttaELAEKLASLA-LPVVLLD-------------SAE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 205 ARLAGSVTIDTLAElierGRALPATPIadSADDALALLiYTSGSTGAPKGAM--YRE-----SQVMSFWRKSSGwfepsg 277
Cdd:cd05904 133 FDSLSFSDLLFEAD----EAEPPVVVI--KQDDVAALL-YSSGTTGRSKGVMltHRNliamvAQFVAGEGSNSD------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 278 YPSITLNFMPMSHVGG-RQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIwdMVfaefhSEVDRRLVDGA 356
Cdd:cd05904 200 SEDVFLCVLPMFHIYGlSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPI--VL-----ALVKSPIVDKY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 357 DRAALeaqvkaelrenvlggRFVMalTGSAPISAEMTAWVESLLADVHLVEGYGSTEAG----MVLNDGMVRRPAV---- 428
Cdd:cd05904 273 DLSSL---------------RQIM--SGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTgvvaMCFAPEKDRAKYGsvgr 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 429 ----IDYKLVDvPElgyfgTDQPYP---RGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DR 500
Cdd:cd05904 336 lvpnVEAKIVD-PE-----TGESLPpnqTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDL-CYIDEDGYLFIvDR 408
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-530 |
5.63e-34 |
|
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: 135.86 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVD-YTTIdIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATS 165
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAElVVAI-LAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 IDNLGDAVEVLAGHaparlvvfdyhgkvdthreaveaararlagsVTIDTLAELIERGRALPATPIADSADDALALLIYT 245
Cdd:TIGR01733 80 SALASRLAGLVLPV-------------------------------ILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 246 SGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGyPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALV 325
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP-DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 326 R----PTELCFVPRIWDMVFAEFHSEVD--RRLVDGADraALEAQVKAELRENVLGGRfvmaltgsapisaemtawvesl 399
Cdd:TIGR01733 208 IaehpVTVLNLTPSLLALLAAALPPALAslRLVILGGE--ALTPALVDRWRARGPGAR---------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 ladvhLVEGYGSTEA-----GMVLNDGMVRRPAVIDYKlVDVPELGYFGTD---QPYPR---GELLVKTQTMFPGYYQRP 468
Cdd:TIGR01733 264 -----LINLYGPTETtvwstATLVDPDDAPRESPVPIG-RPLANTRLYVLDddlRPVPVgvvGELYIGGPGVARGYLNRP 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 469 DVTAEVFDPDGF--------YRTGDiMAKVGPD-QFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:TIGR01733 338 ELTAERFVPDPFaggdgarlYRTGD-LVRYLPDgNLEFLGRIDDQVKIR-GYRIELGEIEAALLRHPGVRE 406
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
84-521 |
1.25e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 137.24 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapvtgLRPivteteptmia 163
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR-----LKP----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgDAVEVLAGHAPARLVVFDyhgkvDTHREAVEAARARLAGS---VTIDTLAELIERGRALPATPIADSADDA-- 238
Cdd:PRK06187 93 -------EEIAYILNDAEDRVVLVD-----SEFVPLLAAILPQLPTVrtvIVEGDGPAAPLAPEVGEYEELLAAASDTfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 --------LALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFepsgypSIT-----LNFMPMSHVGGRQVLYGTLSNGG 305
Cdd:PRK06187 161 fpdidendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWL------KLSrddvyLVIVPMFHVHAWGLPYLALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 306 TAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVfaefhsevdrrlvdgaDRAALEAQVK-AELRENVLGGrfvmaltg 384
Cdd:PRK06187 235 KQVIPRRFDPENLLDLIETERVTFFFAVPTIWQML----------------LKAPRAYFVDfSSLRLVIYGG-------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 385 sAPISAE-MTAWVESLLADvhLVEGYGSTEAGMV-----LNDGM-----VRRPAVIDYKLVDVPELGYFGTDQP---YPR 450
Cdd:PRK06187 291 -AALPPAlLREFKEKFGID--LVQGYGMTETSPVvsvlpPEDQLpgqwtKRRSAGRPLPGVEARIVDDDGDELPpdgGEV 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 451 GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNVLKlSQGEFI-------AVSKLEAV 521
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDV-GYIDEDGYLYItDRIKDVII-SGGENIypreledALYGHPAV 443
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
87-535 |
3.20e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 129.16 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIatsi 166
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 dnLGDAvevlaGHAPARLVVFDyhgkvdthreaveaararlagsvtidtLAELIERGRALPATPIADSADDALALLIYTS 246
Cdd:PRK09088 99 --LGDD-----AVAAGRTDVED---------------------------LAAFIASADALEPADTPSIPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 247 GSTGAPKGAMYREsQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGG-----RQVLY--GTL--SNGgtayFVAKSDLST 317
Cdd:PRK09088 145 GTSGQPKGVMLSE-RNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGlitsvRPVLAvgGSIlvSNG----FEPKRTLGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LfEDLALVRPTELCfVPRIWDMVfaefhsevdrRLVDGADRAALeaqvkaelrenvlgGRFVMALTGSAP-ISAEMTAWV 396
Cdd:PRK09088 220 L-GDPALGITHYFC-VPQMAQAF----------RAQPGFDAAAL--------------RHLTALFTGGAPhAAEDILGWL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 EsllADVHLVEGYGSTEAGMVLndGMVRRPAVIDYKL----VDVPELGYFGTDQ------PYPRGELLVKTQTMFPGYYQ 466
Cdd:PRK09088 274 D---DGIPMVDGFGMSEAGTVF--GMSVDCDVIRAKAgaagIPTPTVQTRVVDDqgndcpAGVPGELLLRGPNLSPGYWR 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 467 RPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLkLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK09088 349 RPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
84-589 |
8.99e-31 |
|
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: 127.02 E-value: 8.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaddALALLI 243
Cdd:cd05941 90 --------------------------------------------------------------------------DPALIL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYR----ESQVMSF---WRKSSGwfepsgypSITLNFMPMSHVGGR-QVLYGTLSNGGTAYFVAKSDL 315
Cdd:cd05941 96 YTSGTTGRPKGVVLThanlAANVRALvdaWRWTED--------DVLLHVLPLHHVHGLvNALLCPLFAGASVEFLPKFDP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 316 STLFEDLALVRPTELCFVPRIWDmvfaefhsevdrRLVDGADRAALEAQVK-AELRENVlggRFVMalTGSAPISAE-MT 393
Cdd:cd05941 168 KEVAISRLMPSITVFMGVPTIYT------------RLLQYYEAHFTDPQFArAAAAERL---RLMV--SGSAALPVPtLE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 394 AWVEslLADVHLVEGYGSTEAGMVLNDGM--VRRP-AV------IDYKLVDVpelgyfGTDQPYPR---GELLVKTQTMF 461
Cdd:cd05941 231 EWEA--ITGHTLLERYGMTEIGMALSNPLdgERRPgTVgmplpgVQARIVDE------ETGEPLPRgevGEIQVRGPSVF 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 462 PGYYQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEF-IAVSKLEAVFGDSPLVRQIFIYGNSARA 540
Cdd:cd05941 303 KEYWNKPEATKEEFTDDGWFKTGD-LGVVDEDGYYWILGRSSVDIIKSGGYkVSALEIERVLLAHPGVSECAVIGVPDPD 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489508543 541 Y---PLAVVVPSGDAlsrhgienlKPVISESLQEVARAAgLQSYEIPRDFII 589
Cdd:cd05941 382 WgerVVAVVVLRAGA---------AALSLEELKEWAKQR-LAPYKRPRRLIL 423
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
84-589 |
1.46e-29 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 124.35 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQtsapvtglrPIVTETEptmia 163
Cdd:cd05926 13 PALTYADLAELVDDLARQL-AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLN---------PAYKKAE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdaVEVLAGHAPARLVVFDYhgkvDTHREAVEAA---RARLAGSVTIDTLAELIERGRALPATPIADSAD---- 236
Cdd:cd05926 78 ---------FEFYLADLGSKLVLTPK----GELGPASRAAsklGLAILELALDVGVLIRAPSAESLSNLLADKKNAkseg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 237 ----DALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSgyPS-ITLNFMPMSHVGGR-QVLYGTLSNGGTAYFV 310
Cdd:cd05926 145 vplpDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLT--PDdRTLVVMPLFHVHGLvASLLSTLAAGGSVVLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 311 AKSDLSTLFEDLALVRPTELCFVPRIwdmvfaefHSEVDRRlvdgadRAALEAQVKAELrenvlggRFVMalTGSAPISA 390
Cdd:cd05926 223 PRFSASTFWPDVRDYNATWYTAVPTI--------HQILLNR------PEPNPESPPPKL-------RFIR--SCSASLPP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 391 EMTAWVESLLAdVHLVEGYGSTEAG--MVLND--------GMVRRPAVIdyKLVDVPELGyfGTDQPYPRGELLVKTQTM 460
Cdd:cd05926 280 AVLEALEATFG-APVLEAYGMTEAAhqMTSNPlppgprkpGSVGKPVGV--EVRILDEDG--EILPPGVVGEICLRGPNV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 461 FPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARA 540
Cdd:cd05926 355 TRGYLNNPEANAEAAFKDGWFRTGDL-GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEK 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489508543 541 YP---LAVVVPSGDAlsrhgienlkPVISESLQEVARaAGLQSYEIPRDFII 589
Cdd:cd05926 434 YGeevAAAVVLREGA----------SVTEEELRAFCR-KHLAAFKVPKKVYF 474
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
84-530 |
5.17e-28 |
|
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: 118.48 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSApvtglrpivTETEptmia 163
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL---------TPPE----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdaVEVLAGHAPARLVVfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsadDALALLI 243
Cdd:cd17631 84 ---------VAYILADSGAKVLF--------------------------------------------------DDLALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAM--YREsqvMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQV-LYGTLSNGGTAYFVAKSDLSTLFE 320
Cdd:cd17631 105 YTSGTTGRPKGAMltHRN---LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVfTLPTLLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPRIWDMVFAefHSEVDRRlvdgaDRAALEAqvkaelrenVLGGrfvmaltGSAPISAEMTAWVEsll 400
Cdd:cd17631 182 LIERHRVTSFFLVPTMIQALLQ--HPRFATT-----DLSSLRA---------VIYG-------GAPMPERLLRALQA--- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEAGMV----LNDGMVRRP------------AVIDYKLVDVPelgyfgtdqPYPRGELLVKTQTMFPGY 464
Cdd:cd17631 236 RGVKFVQGYGMTETSPGvtflSPEDHRRKLgsagrpvffvevRIVDPDGREVP---------PGEVGEIVVRGPHVMAGY 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489508543 465 YQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:cd17631 307 WNRPEATAAAFR-DGWFHTGDL-GRLDEDGYLYIvDRKKDMII-SGGENVYPAEVEDVLYEHPAVAE 370
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
83-624 |
8.35e-28 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 120.15 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 83 FETITYRELWARAGTLATALsaepaIRPG-DR---VCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapvtglrpivtete 158
Cdd:cd05933 6 WHTLTYKEYYEACRQAAKAF-----LKLGlERfhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTT-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 159 ptmiatsidNLGDAVEVLAGHAPARLVVFDYHGKVD----------------THREAVEAARARLAgsvtidTLAELIER 222
Cdd:cd05933 67 ---------NSPEACQYVAETSEANILVVENQKQLQkilqiqdklphlkaiiQYKEPLKEKEPNLY------SWDEFMEL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 223 GRAlpatpIADSADDAL---------ALLIYTSGSTGAPKGAMYRESQVMsfWR-----KSSGWFEPSGYPSITLNFMPM 288
Cdd:cd05933 132 GRS-----IPDEQLDAIissqkpnqcCTLIYTSGTTGMPKGVMLSHDNIT--WTakaasQHMDLRPATVGQESVVSYLPL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 289 SHVGGRQV-LYGTLSNGGTAYFVAKSDLS-TLFEDLALVRPTELCFVPRIWD-----MVFAEFHSEVDRRLVDG-ADRAA 360
Cdd:cd05933 205 SHIAAQILdIWLPIKVGGQVYFAQPDALKgTLVKTLREVRPTAFMGVPRVWEkiqekMKAVGAKSGTLKRKIASwAKGVG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 361 LEAQVKAELRE------NVLGGRFVMA--------------LTGSAPISAEMTAWVESLlaDVHLVEGYGSTE-AG--MV 417
Cdd:cd05933 285 LETNLKLMGGEspsplfYRLAKKLVFKkvrkalgldrcqkfFTGAAPISRETLEFFLSL--NIPIMELYGMSEtSGphTI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 418 LNDGMVRRPAV------IDYKLVDVPELGYfgtdqpyprGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVG 491
Cdd:cd05933 363 SNPQAYRLLSCgkalpgCKTKIHNPDADGI---------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDL-GKLD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 492 PDQFVYLDRRNN-VLKLSQGEFIA-VSKLEAVFGDSPLVRQIFIYGNSaRAYpLAVVVP--------SG---DALSRHGI 558
Cdd:cd05933 433 EDGFLYITGRIKeLIITAGGENVPpVPIEDAVKKELPIISNAMLIGDK-RKF-LSMLLTlkcevnpeTGeplDELTEEAI 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 559 ENLK-----------------PVISESLQE---------VARAAGLQSYEI-PRDFIIETtpftlenGLLTGIRKLARPQ 611
Cdd:cd05933 511 EFCRklgsqatrvseiaggkdPKVYEAIEEgikrvnkkaISNAQKIQKWVIlEKDFSVPG-------GELGPTMKLKRPV 583
|
650
....*....|...
gi 489508543 612 LKKFYGERLERLY 624
Cdd:cd05933 584 VAKKYKDEIDKLY 596
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
55-602 |
9.42e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 120.15 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 55 DRPALGQRalrfvtDPDSGRtmvellprFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYttidiALIRL 134
Cdd:PRK12582 64 DRPWLAQR------EPGHGQ--------WRKVTYGEAKRAVDALAQALLDL-GLDPGRPVMILSGNSIEH-----ALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 135 GAVSVPLQTsAPVTglrpivteteP--TMIATSIDNLGDAVEVLAghaPArlVVFDYHGkvDTHREAVEAARARLAGSVT 212
Cdd:PRK12582 124 AAMQAGVPA-APVS----------PaySLMSHDHAKLKHLFDLVK---PR--VVFAQSG--APFARALAALDLLDVTVVH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 213 IDTLAELIE--RGRALPATPIADSAD--------DALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGW--FEPSGYPS 280
Cdd:PRK12582 186 VTGPGEGIAsiAFADLAATPPTAAVAaaiaaitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLrpREPDPPPP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 281 ITLNFMPMSHV-GGRQVLYGTLSNGGTAYFVAKSDLSTLFE----DLALVRPTELCFVPRIWDMVFaefhsevdrrlvdg 355
Cdd:PRK12582 266 VSLDWMPWNHTmGGNANFNGLLWGGGTLYIDDGKPLPGMFEetirNLREISPTVYGNVPAGYAMLA-------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 356 adrAALEAQvkAELRENVLGGRFVMALtGSAPISAEMTAWVESLLAD-----VHLVEGYGSTEAG--MVLNDGMVRRPAV 428
Cdd:PRK12582 332 ---EAMEKD--DALRRSFFKNLRLMAY-GGATLSDDLYERMQALAVRttghrIPFYTGYGATETAptTTGTHWDTERVGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 429 IDYKLVDVpELGYFGTDQPYprgELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQ----FVYLDRRNNV 504
Cdd:PRK12582 406 IGLPLPGV-ELKLAPVGDKY---EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDpekgLIFDGRVAED 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 505 LKLSQGEFIAVSKL--EAVFGDSPLVRQIFIYGNSaRAYPLAVVVPSGDALSRHG---------IENLKPVIS---ESLQ 570
Cdd:PRK12582 482 FKLSTGTWVSVGTLrpDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAgdpdaapedVVKHPAVLAilrEGLS 560
|
570 580 590
....*....|....*....|....*....|..
gi 489508543 571 EVARAAGLQSYEIPRdFIIETTPFTLENGLLT 602
Cdd:PRK12582 561 AHNAEAGGSSSRIAR-ALLMTEPPSIDAGEIT 591
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
82-626 |
9.94e-28 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 119.46 E-value: 9.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQ-----TSAPVTGLRPIVTE 156
Cdd:cd05921 22 GWRRVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpayslMSQDLAKLKHLFEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 157 TEPTMI-ATSIDNLGDAV-EVLAGHAPARLVVFDYHGKVDTHREAVEAARARLAgsvtidtLAELIERgralpATPiads 234
Cdd:cd05921 101 LKPGLVfAQDAAPFARALaAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAA-------VDAAFAA-----VGP---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 235 adDALALLIYTSGSTGAPKG-----AMYRESQVMsfwrKSSGWFEPSGYPSITLNFMPMSHV-GGRQVLYGTLSNGGTAY 308
Cdd:cd05921 165 --DTVAKFLFTSGSTGLPKAvintqRMLCANQAM----LEQTYPFFGEEPPVLVDWLPWNHTfGGNHNFNLVLYNGGTLY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 309 FVAKSDLSTLFE----DLALVRPTELCFVPRIWDMVFAEFHSevdrrlvDGADRAALEAQVK------AELRENVLGG-- 376
Cdd:cd05921 239 IDDGKPMPGGFEetlrNLREISPTVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKlmfyagAGLSQDVWDRlq 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 377 RFVMALTGSApisaemtawveslladVHLVEGYGSTEAGMVLND--------GMVRRPAV-IDYKLvdVPELGYFgtdqp 447
Cdd:cd05921 312 ALAVATVGER----------------IPMMAGLGATETAPTATFthwptersGLIGLPAPgTELKL--VPSGGKY----- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 448 yprgELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQ----FVYLDRRNNVLKLSQGEFIAVSKL--EAV 521
Cdd:cd05921 369 ----EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPDDpakgLVFDGRVAEDFKLASGTWVSVGPLraRAV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 522 FGDSPLVRQIFIYGNSaRAYPLAVVVPSGDALSRH-GIENLKP-----------VISESLQEVARAAGLQSYEIPRdFII 589
Cdd:cd05921 445 AACAPLVHDAVVAGED-RAEVGALVFPDLLACRRLvGLQEASDaevlrhakvraAFRDRLAALNGEATGSSSRIAR-ALL 522
|
570 580 590
....*....|....*....|....*....|....*..
gi 489508543 590 ETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTE 626
Cdd:cd05921 523 LDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
85-555 |
1.02e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 119.98 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEPaIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPL-----QTSAPVTGLRPIVTETEP 159
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRG-LSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaysLVSQDFGKLRHVLELLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 160 TMI-ATSIDNLGDAVEVLaghaparlvvfdyhgkVDTHREAVeAARARLAGSVTIdTLAELIergrALPATPIADSADDA 238
Cdd:PRK08180 148 GLVfADDGAAFARALAAV----------------VPADVEVV-AVRGAVPGRAAT-PFAALL----ATPPTAAVDAAHAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 L-----ALLIYTSGSTGAPKG------------AMYResQVMSFWRKSsgwfepsgyPSITLNFMPMSHV-GGRQVLYGT 300
Cdd:PRK08180 206 VgpdtiAKFLFTSGSTGLPKAvinthrmlcanqQMLA--QTFPFLAEE---------PPVLVDWLPWNHTfGGNHNLGIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 301 LSNGGTAYFVAKSDLSTLFE----DLALVRPTELCFVPRIWDMvfaefhsevdrrLVDgadraALEAQvkAELRENVLGg 376
Cdd:PRK08180 275 LYNGGTLYIDDGKPTPGGFDetlrNLREISPTVYFNVPKGWEM------------LVP-----ALERD--AALRRRFFS- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 377 RFVMALTGSAPISAemTAW-------VESLLADVHLVEGYGSTE-AGMVLN-------DGMVRRPAV-IDYKLVDVPElg 440
Cdd:PRK08180 335 RLKLLFYAGAALSQ--DVWdrldrvaEATCGERIRMMTGLGMTEtAPSATFttgplsrAGNIGLPAPgCEVKLVPVGG-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 441 yfgtdqpypRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQ----FVYLDRRNNVLKLSQGEFIAVS 516
Cdd:PRK08180 411 ---------KLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADpergLMFDGRIAEDFKLSSGTWVSVG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489508543 517 --KLEAVFGDSPLVRQIFIYGnSARAYPLAVVVPSGDALSR 555
Cdd:PRK08180 482 plRARAVSAGAPLVQDVVITG-HDRDEIGLLVFPNLDACRR 521
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-554 |
1.03e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 117.39 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSApvtglrpivteteptmiats 165
Cdd:cd05934 4 WTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 idnLGDAVEVLAGHAPARLVVFDyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaddaLALLIYT 245
Cdd:cd05934 63 ---RGDELAYIIDHSGAQLVVVD--------------------------------------------------PASILYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 246 SGSTGAPKGAMYRESQvMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQV-LYGTLSNGGTAYFVAKSDLSTLFEDLAL 324
Cdd:cd05934 90 SGTTGPPKGVVITHAN-LTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVsVLAALSVGATLVLLPRFSASRFWSDVRR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 325 VRPTELCFVPRIWDMVFAEFHSEVDR----RLVDGAdraALEAQVKAELREnvlggRFvmaltgsapisaemtawvesll 400
Cdd:cd05934 169 YGATVTNYLGAMLSYLLAQPPSPDDRahrlRAAYGA---PNPPELHEEFEE-----RF---------------------- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 aDVHLVEGYGSTEAG-MVLND-GMVRRPAVI-------DYKLVDvpelgyfGTDQPYPR---GELLVKTQ---TMFPGYY 465
Cdd:cd05934 219 -GVRLLEGYGMTETIvGVIGPrDEPRRPGSIgrpapgyEVRIVD-------DDGQELPAgepGELVIRGLrgwGFFKGYY 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 466 QRPDVTAEVFdPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG----NSARA 540
Cdd:cd05934 291 NMPEATAEAM-RNGWFHTGDL-GYRDADGFFYFvDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVAvpdeVGEDE 367
|
490
....*....|....
gi 489508543 541 YPLAVVVPSGDALS 554
Cdd:cd05934 368 VKAVVVLRPGETLD 381
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
70-510 |
2.07e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 118.05 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 70 PDSGRTMVELlPRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapvtg 149
Cdd:PRK07514 14 ADRDAPFIET-PDGLRYTYGDLDAASARLANLLVAL-GVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 150 lrpiVTETEptmiatsidnlgdaVEVLAGHAPARLVVfdyhgkVDTHREAVEAARARLAGSVTIDTLAE-----LIERGR 224
Cdd:PRK07514 87 ----YTLAE--------------LDYFIGDAEPALVV------CDPANFAWLSKIAAAAGAPHVETLDAdgtgsLLEAAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 225 ALPAT--PIADSADDaLALLIYTSGSTGAPKGAM------YRESQVM-SFWRKSSGwfepsgypSITLNFMPMSHVGGRQ 295
Cdd:PRK07514 143 AAPDDfeTVPRGADD-LAAILYTSGTTGRSKGAMlshgnlLSNALTLvDYWRFTPD--------DVLIHALPIFHTHGLF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 296 V-LYGTLSNGGTAYFVAKSDLSTLFEDLAlvRPTELCFVPriwdmvfaEFHSevdrRLVdgaDRAALEAQVKAELRenvl 374
Cdd:PRK07514 214 VaTNVALLAGASMIFLPKFDPDAVLALMP--RATVMMGVP--------TFYT----RLL---QEPRLTREAAAHMR---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 375 ggRFVmalTGSAPisaemtawvesLLADVH----------LVEGYGSTEAGMVLN---DGmVRRPAVIDYKLVDV----- 436
Cdd:PRK07514 273 --LFI---SGSAP-----------LLAETHrefqertghaILERYGMTETNMNTSnpyDG-ERRAGTVGFPLPGVslrvt 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 437 -PElgyfgTDQPYPRGE---LLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQG 510
Cdd:PRK07514 336 dPE-----TGAELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDL-GKIDERGYVHIVGRGKDLIISGG 407
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-609 |
2.58e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 114.08 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPaIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKING-VGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSiDNlgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsadDALALLI 243
Cdd:cd05914 85 VS-DE--------------------------------------------------------------------DDVALIN 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAM--YResqvmSFWRKSSGWFE--PSGYPSITLNFMPMSHVGG--RQVLYGTLsNGGTAYFVAKSDlST 317
Cdd:cd05914 96 YTSGTTGNSKGVMltYR-----NIVSNVDGVKEvvLLGKGDKILSILPLHHIYPltFTLLLPLL-NGAHVVFLDKIP-SA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LFEDLALVRPTELCFVPRIWDM-----------------VFAEFHSEVDRRLVDGADRAALEAqvkaelrenvLGGRFVM 380
Cdd:cd05914 169 KIIALAFAQVTPTLGVPVPLVIekifkmdiipkltlkkfKFKLAKKINNRKIRKLAFKKVHEA----------FGGNIKE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 381 ALTGSAPISAEMTAWVESLlaDVHLVEGYGSTEAGMVLNdgmVRRPAVIDY----KLVDVPELGYFGTDQPYPRGELLVK 456
Cdd:cd05914 239 FVIGGAKINPDVEEFLRTI--GFPYTIGYGMTETAPIIS---YSPPNRIRLgsagKVIDGVEVRIDSPDPATGEGEIIVR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 457 TQTMFPGYYQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYL-DRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFDKDGWFHTGD-LGKIDAEGYLYIrGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVV 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 536 NSARAYPLAVVVPSGDALSRHGIENLKPVIS-ESLQEVARAagLQSYEIPRDFIIETTPFTlenglLTGIRKLAR 609
Cdd:cd05914 393 QEKKLVALAYIDPDFLDVKALKQRNIIDAIKwEVRDKVNQK--VPNYKKISKVKIVKEEFE-----KTPKGKIKR 460
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
237-546 |
3.77e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 115.97 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 237 DALALLIYTSGSTGAPKGAMYRE----SQVMSFWRKSsgwFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAK 312
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNknlyNTVVPLCKHS---IFKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTINIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 313 sDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVD------RRLV-----------DGADRAALEA--QVKAELRENV 373
Cdd:PTZ00342 381 -DINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlpplkRFLVkkilslrksnnNGGFSKFLEGitHISSKIKDKV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 374 lGGRFVMALTGSAPISAEMtAWVESLLADVHLVEGYGSTEAG--MVLNDGMVRRPAVI--------DYKLVDVPElgYFG 443
Cdd:PTZ00342 460 -NPNLEVILNGGGKLSPKI-AEELSVLLNVNYYQGYGLTETTgpIFVQHADDNNTESIggpispntKYKVRTWET--YKA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 444 TDQPyPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFG 523
Cdd:PTZ00342 536 TDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYS 614
|
330 340
....*....|....*....|...
gi 489508543 524 DSPLVRQIFIYGNSARAYPLAVV 546
Cdd:PTZ00342 615 QISFINFCVVYGDDSMDGPLAII 637
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
75-589 |
1.20e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 112.26 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 75 TMVELLPRFETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQ---TSAPV---- 147
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNirlTENELifql 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 148 --TGLRPIVTETEPTMIATSIdnlgdavevlaghaparlvvfdyhgkvdthreaveAARARLAGSVTIDTLAELIERGRa 225
Cdd:PRK06839 97 kdSGTTVLFVEKTFQNMALSM-----------------------------------QKVSYVQRVISITSLKEIEDRKI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 226 lpaTPIADSADDALALLIYTSGSTGAPKGAMYreSQVMSFWRKSSGWFE---PSGYPSITLnfMPMSHVGGRQVL-YGTL 301
Cdd:PRK06839 141 ---DNFVEKNESASFIICYTSGTTGKPKGAVL--TQENMFWNALNNTFAidlTMHDRSIVL--LPLFHIGGIGLFaFPTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 302 SNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIwdmvfaefhsevDRRLVDGADRAALEAQvkaELRenvlggrfvMA 381
Cdd:PRK06839 214 FAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTI------------HQALINCSKFETTNLQ---SVR---------WF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 382 LTGSAPISAE-MTAWVESLLAdvhLVEGYGSTEAG----MVLNDGMVRRPAVI-------DYKLVDvPELGYFGtdqPYP 449
Cdd:PRK06839 270 YNGGAPCPEElMREFIDRGFL---FGQGFGMTETSptvfMLSEEDARRKVGSIgkpvlfcDYELID-ENKNKVE---VGE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 450 RGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVR 529
Cdd:PRK06839 343 VGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGD-LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVY 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 530 QIFIYGNSARAY---PLAVVVPSGDALsrhgienlkpVISESLQEVARAAgLQSYEIPRDFII 589
Cdd:PRK06839 421 EVAVVGRQHVKWgeiPIAFIVKKSSSV----------LIEKDVIEHCRLF-LAKYKIPKEIVF 472
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
35-589 |
1.56e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 112.79 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 35 IDQPGVALPQLIRMVMEGYADRPALgqralRFVtdpdsGRTMvellprfetiTYRELWARAGTLATALSAEpAIRPGDRV 114
Cdd:PRK05605 27 LDYGDTTLVDLYDNAVARFGDRPAL-----DFF-----GATT----------TYAELGKQVRRAAAGLRAL-GVRPGDRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 115 CVLGFNSVDYTTIDIALIRLGAVSV---PLQTSAPVTGLrpivTETEPTMIATSIDNLGDAVEVLAGHAPARLVVfdyhg 191
Cdd:PRK05605 86 AIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAHELEHP----FEDHGARVAIVWDKVAPTVERLRRTTPLETIV----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 192 KVDTHRE--------------AVEAARARLAGSVTiDTLA-ELIERGRALPATPIAD----SADDaLALLIYTSGSTGAP 252
Cdd:PRK05605 157 SVNMIAAmpllqrlalrlpipALRKARAALTGPAP-GTVPwETLVDAAIGGDGSDVShprpTPDD-VALILYTSGTTGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 253 KGAMYRESQVMSFWRKSSGWFEPSG-YPSITLNFMPMSHVGGrQVLYGTL--SNGGTAYFVAKSDLSTLFEDLALVRPTE 329
Cdd:PRK05605 235 KGAQLTHRNLFANAAQGKAWVPGLGdGPERVLAALPMFHAYG-LTLCLTLavSIGGELVLLPAPDIDLILDAMKKHPPTW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 330 LCFVPRIWDmvfaefhsevdrRLVDGAdraaleaqvkAELRENVLGGRFvmALTGSAPISAEMTAWVESLLADvHLVEGY 409
Cdd:PRK05605 314 LPGVPPLYE------------KIAEAA----------EERGVDLSGVRN--AFSGAMALPVSTVELWEKLTGG-LLVEGY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 410 GSTE-----AGMVLNDGmvRRPAVI-------DYKLVDvPElgYFGTDQPY-PRGELLVKTQTMFPGYYQRPDVTAEVFD 476
Cdd:PRK05605 369 GLTEtspiiVGNPMSDD--RRPGYVgvpfpdtEVRIVD-PE--DPDETMPDgEEGELLVRGPQVFKGYWNRPEETAKSFL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 477 pDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG----NSARAYPLAVVVPSGDA 552
Cdd:PRK05605 444 -DGWFRTGD-VVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGlpreDGSEEVVAAVVLEPGAA 521
|
570 580 590
....*....|....*....|....*....|....*..
gi 489508543 553 LSRHGienlkpvisesLQEVARaAGLQSYEIPRDFII 589
Cdd:PRK05605 522 LDPEG-----------LRAYCR-EHLTRYKVPRRFYH 546
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
771-1076 |
1.77e-25 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 107.84 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 771 VLLTGATGFLGRYLaLEWLdrmdLVNG-KLICLVRARSDEEAQARLDatfdsgdpylvrhYRELGAGRLEVLAGDKGEAD 849
Cdd:cd05263 1 VFVTGGTGFLGRHL-VKRL----LENGfKVLVLVRSESLGEAHERIE-------------EAGLEADRVRVLEGDLTQPN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 LGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAV-GEQipPEAFTEDAD 928
Cdd:cd05263 63 LGLSAAASRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVaGNR--EGNIRETEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 929 iraiSPTRRIddsyANGYANSKWAGEVLLREAHEQcgLPVTVFRCDMILADtSYTGQLNLPDMFTRLMLSLAATGIAPGs 1008
Cdd:cd05263 141 ----NPGQNF----KNPYEQSKAEAEQLVRAAATQ--IPLTVYRPSIVVGD-SKTGRIEKIDGLYELLNLLAKLGRWLP- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 1009 fyeldAHGNRQrAHYDGLPVEFVAEAICTLGTHSPDRFVTYHVMNPydDGIGLDEFVDWLNSPTSGSG 1076
Cdd:cd05263 209 -----MPGNKG-ARLNLVPVDYVADAIVYLSKKPEANGQIFHLTDP--TPQTLREIADLFKSAFLSPG 268
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
85-595 |
2.86e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 112.06 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLAtALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:PRK06178 58 VITYAELDELSDRFA-ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sIDNLGDAVEVLAGHAPARLVVFDYHGKVDTHR------EAVEAARARLAGsvTIDTLAELiergRALPATPIADSAD-D 237
Cdd:PRK06178 137 -LDQLAPVVEQVRAETSLRHVIVTSLADVLPAEptlplpDSLRAPRLAAAG--AIDLLPAL----RACTAPVPLPPPAlD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 238 ALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGrqvlygtlsnggtayfvaksdlst 317
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG------------------------ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 lfEDLALVRPT----ELCFVPRiWDMVfaEFHSEVDRR-------LVDGADRAALEAQVKA-ELR--ENVLGGRFVMALT 383
Cdd:PRK06178 266 --ENFGLLFPLfsgaTLVLLAR-WDAV--AFMAAVERYrvtrtvmLVDNAVELMDHPRFAEyDLSslRQVRVVSFVKKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 384 gsapiSAEMTAWVEslLADVHLVEG-YGSTE--------AGMVLND-GMVRRPAVI-------DYKLVDvpelgyFGTDQ 446
Cdd:PRK06178 341 -----PDYRQRWRA--LTGSVLAEAaWGMTEthtcdtftAGFQDDDfDLLSQPVFVglpvpgtEFKICD------FETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 447 PYP---RGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFV-YLDRRNNVLKLSqGEFIAVSKLEAVF 522
Cdd:PRK06178 408 LLPlgaEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDI-GKIDEQGFLhYLGRRKEMLKVN-GMSVFPSEVEALL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 523 GDSPLVRQIFIYGNSAR---AYPLAVVVPSGDAlsrhgienlkPVISESLQEVARAAgLQSYEIPRDFIIETTPFT 595
Cdd:PRK06178 485 GQHPAVLGSAVVGRPDPdkgQVPVAFVQLKPGA----------DLTAAALQAWCREN-MAVYKVPEIRIVDALPMT 549
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
769-1042 |
4.49e-25 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 107.38 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLaLEWLDRMDLVNGKLICLVRARSDEEAQARL-----DATFDSGdpylvRHYRELGAGRLEVLAG 843
Cdd:cd05236 1 KSVLITGATGFLGKVL-LEKLLRSCPDIGKIYLLIRGKSGQSAEERLrellkDKLFDRG-----RNLNPLFESKIVPIEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 844 DKGEADLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKR-KPYIYTST-------IAVG 915
Cdd:cd05236 75 DLSEPNLGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKlKAFVHVSTayvngdrQLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 916 EQIPPEAFTEDA---------DIRAISPTRRIDDSYANGYANSKWAGEVLLREahEQCGLPVTVFRCDMILADT-----S 981
Cdd:cd05236 155 EKVYPPPADPEKlidilelmdDLELERATPKLLGGHPNTYTFTKALAERLVLK--ERGNLPLVIVRPSIVGATLkepfpG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 982 YTGQLNLPDMftrlMLSLAATGIapgsFYELDAhgnRQRAHYDGLPVEFVAEAICTLGTHS 1042
Cdd:cd05236 233 WIDNFNGPDG----LFLAYGKGI----LRTMNA---DPNAVADIIPVDVVANALLAAAAYS 282
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-485 |
6.48e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 110.97 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 51 EGYADRPALgqralRFVTDPDSGRTmvellprfetITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIA 130
Cdd:COG0365 20 EGRGDKVAL-----IWEGEDGEERT----------LTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEAVIAMLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 131 LIRLGAVSVPLqtsapVTGLRPivteteptmiatsidnlgDAVEVLAGHAPARLVVFD----YHGKVDTHREAVEAARA- 205
Cdd:COG0365 84 CARIGAVHSPV-----FPGFGA------------------EALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDEALEe 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 206 -----------RLAGSVTID---TLAELIERGRAlPATPIADSADDALaLLIYTSGSTGAPKGAMYRESQVMSFWRKSSG 271
Cdd:COG0365 141 lpslehvivvgRTGADVPMEgdlDWDELLAAASA-EFEPEPTDADDPL-FILYTSGTTGKPKGVVHTHGGYLVHAATTAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 272 W---FEPSG---YPSiTLNFMpMSHVGgrqVLYGTLSNGGTAYFVAKS----DLSTLFEDLALVRPTELCFVPRIWDMVF 341
Cdd:COG0365 219 YvldLKPGDvfwCTA-DIGWA-TGHSY---IVYGPLLNGATVVLYEGRpdfpDPGRLWELIEKYGVTVFFTAPTAIRALM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 342 AEfhsevDRRLVDGADRAALEAqvkaelrenvlggrfvMALTGSaPISAEMTAWVESLLaDVHLVEGYGSTEAGMVL--- 418
Cdd:COG0365 294 KA-----GDEPLKKYDLSSLRL----------------LGSAGE-PLNPEVWEWWYEAV-GVPIVDGWGQTETGGIFisn 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 419 NDGMVRRP-----AV--IDYKLVDvpELGyfgtdQPYPR---GELLVKTQ--TMFPGYYQRPDVTAEVF--DPDGFYRTG 484
Cdd:COG0365 351 LPGLPVKPgsmgkPVpgYDVAVVD--EDG-----NPVPPgeeGELVIKGPwpGMFRGYWNDPERYRETYfgRFPGWYRTG 423
|
.
gi 489508543 485 D 485
Cdd:COG0365 424 D 424
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
42-486 |
9.86e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 109.61 E-value: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALgqralrfVTDPdsgrtmvellprfETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNS 121
Cdd:PRK07656 7 LPELLARAARRFGDKEAY-------VFGD-------------QRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 122 VDYTTIDIALIRLGAVSVPLQtsapvtglrPIVTETEPT-MIATSIDNLGDAVEVLAGH---APARLVVFDyhgkvdtHR 197
Cdd:PRK07656 66 PHWVIAALGALKAGAVVVPLN---------TRYTADEAAyILARGDAKALFVLGLFLGVdysATTRLPALE-------HV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 198 EAVEAARARLAGSVTIdTLAELIERGrALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQVMSfwrKSSGWfepSG 277
Cdd:PRK07656 130 VICETEEDDPHTEKMK-TFTDFLAAG-DPAERAPEVDPDD-VADILFTSGTTGRPKGAMLTHRQLLS---NAADW---AE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 278 YPSIT-----LNFMPMSHVGGRQV-LYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAefhsevdrr 351
Cdd:PRK07656 201 YLGLTegdryLAANPFFHVFGYKAgVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQ--------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 352 lVDGADRAALeaqvkAELRenvlggrfvMALTGSAPISAEMTAWVESLLADVHLVEGYGSTEAGMV-----LNDGMVRRP 426
Cdd:PRK07656 272 -HPDRSAEDL-----SSLR---------LAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVttfnrLDDDRKTVA 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 427 AVI-----DYKLVDVPELGYF-GTDQPyprGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDI 486
Cdd:PRK07656 337 GTIgtaiaGVENKIVNELGEEvPVGEV---GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDL 399
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
82-589 |
1.01e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 110.25 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RF--ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQ---TSAPV------TGL 150
Cdd:PRK07786 37 RFlgNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNfrlTPPEIaflvsdCGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 151 RPIVTETEPTMIATSIDNLGDAVE-VLAGHAPARLVVFDYHgkvdthreaveaararlagsvtiDTLAEliergrALPAT 229
Cdd:PRK07786 116 HVVVTEAALAPVATAVRDIVPLLStVVVAGGSSDDSVLGYE-----------------------DLLAE------AGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 230 PIADSADDALALLIYTSGSTGAPKGAMYRES----QVMSFWRkSSGWFEPSgypSITLNFMPMSHVGGRQVLYGTLSNGG 305
Cdd:PRK07786 167 APVDIPNDSPALIMYTSGTTGRPKGAVLTHAnltgQAMTCLR-TNGADINS---DVGFVGVPLFHIAGIGSMLPGLLLGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 306 TA--YFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEfhSEVDRRlvdgadraaleaqvkaELRENVLGgrfvmalT 383
Cdd:PRK07786 243 PTviYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE--QQARPR----------------DLALRVLS-------W 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 384 GSAPISAEMTAWVESLLADVHLVEGYGSTEAG----MVLND------GMVRRPA------VIDYKLVDVPelgyfgtdqP 447
Cdd:PRK07786 298 GAAPASDTLLRQMAATFPEAQILAAFGQTEMSpvtcMLLGEdairklGSVGKVIptvaarVVDENMNDVP---------V 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 448 YPRGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDIMaKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPL 527
Cdd:PRK07786 369 GEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLV-RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPD 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 528 VRQIFIYGNSARAY---PLAVVVPSGDAlSRHGIENLKPVISESLqevARaaglqsYEIPRDFII 589
Cdd:PRK07786 447 IVEVAVIGRADEKWgevPVAVAAVRNDD-AALTLEDLAEFLTDRL---AR------YKHPKALEI 501
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
84-612 |
1.56e-24 |
|
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: 108.49 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIa 163
Cdd:cd05945 15 RTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpIADsaDDALALLI 243
Cdd:cd05945 93 -------------------------------------------------------------------IAD--GDDNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSF--WRKSSGWFEP----SGYPSITLNFMPMShvggrqvLYGTLSNGGTAYFVAK---SD 314
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNLVSFtnWMLSDFPLGPgdvfLNQAPFSFDLSVMD-------LYPALASGATLVPVPRdatAD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 LSTLFEDLALVRPTELCFVPRIWDMVFAEfhsevdrrlvdgadrAALEAQVKAELRENVLGGRfvmALTgsapiSAEMTA 394
Cdd:cd05945 177 PKQLFRFLAEHGITVWVSTPSFAAMCLLS---------------PTFTPESLPSLRHFLFCGE---VLP-----HKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 395 WVEsLLADVHLVEGYGSTEAGMVLNDGMVRRPAVIDYKLVDV----PELGYFGTDQ------PYPRGELLVKTQTMFPGY 464
Cdd:cd05945 234 LQQ-RFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIgyakPGAKLVILDEdgrpvpPGEKGELVISGPSVSKGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 465 YQRPDVTAEVFDPD---GFYRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ---IFIYGNSA 538
Cdd:cd05945 313 LNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEavvVPKYKGEK 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 539 RAYPLAVVVPsgdalsRHGIENLKPV-ISESLQEVaraagLQSYEIPRDFI-IETTPFTlENGlltgirKLARPQL 612
Cdd:cd05945 392 VTELIAFVVP------KPGAEAGLTKaIKAELAER-----LPPYMIPRRFVyLDELPLN-ANG------KIDRKAL 449
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
84-536 |
3.51e-24 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 108.66 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTsapvtglrpivteteptmia 163
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLAL-GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQ-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsiDNLGDAVEVLAGHAPARLVVFDYHGKVD---THREAVEAAR---------------ARLAgsvtidTLAELIERGRA 225
Cdd:cd17641 69 ---DSMAEEVAYLLNYTGARVVIAEDEEQVDkllEIADRIPSVRyviycdprgmrkyddPRLI------SFEDVVALGRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 226 LPAT-------PIADSADDALALLIYTSGSTGAPKGAMYRESQVMSFwRKSSGWFEPSGYPSITLNFMPMSHVGGRQVLY 298
Cdd:cd17641 140 LDRRdpglyerEVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPLGPGDEYVSVLPLPWIGEQMYSV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 299 G-TLSNGGTAYFVakSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSE------VDRRLVDGADRAALEA-------- 363
Cdd:cd17641 219 GqALVCGFIVNFP--EEPETMMEDLREIGPTFVLLPPRVWEGIAADVRARmmdatpFKRFMFELGMKLGLRAldrgkrgr 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 364 QVKAELR--------------ENVLGGRFV-MALTGSAPISAEMTAWVESLlaDVHLVEGYGSTE-AGMVlndgMVRRPA 427
Cdd:cd17641 297 PVSLWLRlaswladallfrplRDRLGFSRLrSAATGGAALGPDTFRFFHAI--GVPLKQLYGQTElAGAY----TVHRDG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 428 VIDYKLVDVPelgYFGTD-QPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLK 506
Cdd:cd17641 371 DVDPDTVGVP---FPGTEvRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510
....*....|....*....|....*....|
gi 489508543 507 LSQGEFIAVSKLEAVFGDSPLVRQIFIYGN 536
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
85-486 |
4.13e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.12 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 SIDNLGDAVEVLAGHAPARLVVFDYHGKVDTHRE-------AVEAARARLAGSVTIdTLAELIERGRALPatPIADSADD 237
Cdd:PRK08314 115 GSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEiavpawlRAEPPLQALAPGGVV-AWKEALAAGLAPP--PHTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 238 aLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEpSGYPSITLNFMPMSHVGGRQ-VLYGTLSNGGTAYFVAKSDLS 316
Cdd:PRK08314 192 -LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN-STPESVVLAVLPLFHVTGMVhSMNAPIYAGATVVLMPRWDRE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTelcFVPRIWDMVfaefhsevdrrlVDGADRAALEAQVKAELRenVLGGrfvmaltGSAPISaemTAWV 396
Cdd:PRK08314 270 AAARLIERYRVT---HWTNIPTMV------------VDFLASPGLAERDLSSLR--YIGG-------GGAAMP---EAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 ESLLADVHL--VEGYGSTEAGMVLNDGMVRRPavidyKL--VDVPelgYFGTD---------QPYPR---GELLVKTQTM 460
Cdd:PRK08314 323 ERLKELTGLdyVEGYGLTETMAQTHSNPPDRP-----KLqcLGIP---TFGVDarvidpetlEELPPgevGEIVVHGPQV 394
|
410 420
....*....|....*....|....*....
gi 489508543 461 FPGYYQRPDVTAEVF-DPDG--FYRTGDI 486
Cdd:PRK08314 395 FKGYWNRPEATAEAFiEIDGkrFFRTGDL 423
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
770-1068 |
2.54e-21 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 95.82 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRmdlvNGKLICLVRARSDEEAQARLDatfdsgdpylvrhyrelgagRLEVLAGDkgead 849
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLAR----GHEVVGLDRSPPGAANLAALP--------------------GVEFVRGD----- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 lGLDRVTWQRLADTVDLIVDPAALVNHVL-PYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAV-GEqiPPEAFTEDA 927
Cdd:COG0451 52 -LRDPEALAAALAGVDAVVHLAAPAGVGEeDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVyGD--GEGPIDEDT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 928 DIRAISPtrriddsyangYANSKWAGEVLLREAHEQCGLPVTVFRCDMILadtSYTGQLNLPDMFTRLMLSLAATGIAPG 1007
Cdd:COG0451 129 PLRPVSP-----------YGASKLAAELLARAYARRYGLPVTILRPGNVY---GPGDRGVLPRLIRRALAGEPVPVFGDG 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 1008 SFYeldahgnRQRAHydglpVEFVAEAICTLGTHSPDRFVTYHVMNpyDDGIGLDEFVDWL 1068
Cdd:COG0451 195 DQR-------RDFIH-----VDDVARAIVLALEAPAAPGGVYNVGG--GEPVTLRELAEAI 241
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
84-599 |
4.50e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 97.60 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPaIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivteteptmia 163
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYP----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlaghaPARLvvfdyhgkvdthREAVEAARARLAgsvtidtlaeliergralpatpIADSADdaLALLI 243
Cdd:cd05930 73 -----------------AERL------------AYILEDSGAKLV----------------------LTDPDD--LAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSF--WRKSSGWFEPSGypsITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKS---DLSTL 318
Cdd:cd05930 100 YTSGSTGKPKGVMVEHRGLVNLllWMQEAYPLTPGD---RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEvrkDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWdmvfaefhsevdRRLVDGADRAALEAqvkaeLRenvlggrfvMALTGSAPISAEMTAWVES 398
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLL------------RLLLQELELAALPS-----LR---------LVLVGGEALPPDLVRRWRE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVHLVEGYGSTEAGM------VLNDGMVRRPAVI-------DYKLVDvpelgyfGTDQPYPR---GELLVKTQTMFP 462
Cdd:cd05930 231 LLPGARLVNLYGPTEATVdatyyrVPPDDEEDGRVPIgrpipntRVYVLD-------ENLRPVPPgvpGELYIGGAGLAR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 463 GYYQRPDVTAEVFDPDGF------YRTGDiMAKVGPD-QFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQifiyg 535
Cdd:cd05930 304 GYLNRPELTAERFVPNPFgpgermYRTGD-LVRWLPDgNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVRE----- 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 536 nsarayplAVVVPSGDALsrhGIENL---------KPVISESLQEVARAAgLQSYEIPRDFI-IETTPFTlENG 599
Cdd:cd05930 377 --------AAVVAREDGD---GEKRLvayvvpdegGELDEEELRAHLAER-LPDYMVPSAFVvLDALPLT-PNG 437
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
238-616 |
7.96e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 95.09 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 238 ALALLIYTSGSTGAPKGAMYRESQ-VMSFwrKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTayFVAKSDLS 316
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANlLASA--AGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAE--LVLLERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTELCFVPRiwdmvfaefhsEVDRRLVDGADRAALeaqvkAELRENVLGGrfvmaltgsAPISAEMTAwv 396
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPT-----------QLQRLLDSGQGPAAL-----KSLRAVLLGG---------APIPPELLE-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 ESLLADVHLVEGYGSTEAGmvlndgmvrrpAVIDYKLVDVPELGYFGTDQPY------PRGELLVKTQTMFPGYYQRPDV 470
Cdd:cd17630 130 RAADRGIPLYTTYGMTETA-----------SQVATKRPDGFGRGGVGVLLPGrelrivEDGEIWVGGASLAMGYLRGQLV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 471 taEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLkLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAY---PLAVVV 547
Cdd:cd17630 199 --PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELgqrPVAVIV 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 548 PSGDALSRHGIENLKpviseslqevaraAGLQSYEIPRDFIIettpftLENGLLTGIRKLARPQLKKFY 616
Cdd:cd17630 276 GRGPADPAELRAWLK-------------DKLARFKLPKRIYP------VPELPRTGGGKVDRRALRAWL 325
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-548 |
1.08e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.43 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 55 DRPAlgqralrfVTDPDSGRTMVEllprfeTITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRL 134
Cdd:PRK13295 39 DKTA--------VTAVRLGTGAPR------RFTYRELAALVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 135 GAVSVPLQtsapvtglrPIVTETEptmiatsidnlgdaVEVLAGHAPARLVV-------FDYHGKVDTHREAVEAARARL 207
Cdd:PRK13295 104 GAVLNPLM---------PIFRERE--------------LSFMLKHAESKVLVvpktfrgFDHAAMARRLRPELPALRHVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 208 ----AGSVTIDTLAELIERGRALPATPIADS----ADDaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEpSGYP 279
Cdd:PRK13295 161 vvggDGADSFEALLITPAWEQEPDAPAILARlrpgPDD-VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG-LGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 280 SITLNFMPMSHVGGrqVLYGT---LSNGGTAYFvakSDLSTLFEDLALVRPTELCFVpriwdMVFAEFhsevdrrLVDGA 356
Cdd:PRK13295 239 DVILMASPMAHQTG--FMYGLmmpVMLGATAVL---QDIWDPARAAELIRTEGVTFT-----MASTPF-------LTDLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 357 DRAALEAQVKAELRenvlggRFvmaLTGSAPISAEMTAWVESLLAdVHLVEGYGSTEAGMV----LNDGMVRRPAV---- 428
Cdd:PRK13295 302 RAVKESGRPVSSLR------TF---LCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVtltkLDDPDERASTTdgcp 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 429 ---IDYKLVDvpelgyfGTDQPYPRGE---LLVKTQTMFPGYYQRPDVTAEvfDPDGFYRTGDImAKVGPDQFVYLDRRN 502
Cdd:PRK13295 372 lpgVEVRVVD-------ADGAPLPAGQigrLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDL-ARIDADGYIRISGRS 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489508543 503 NVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYgnsarAYP--------LAVVVP 548
Cdd:PRK13295 442 KDVIIRGGENIPVVEIEALLYRHPAIAQVAIV-----AYPderlgeraCAFVVP 490
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
86-589 |
1.29e-20 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 96.81 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQtsapvtglrpivtetePTMIATS 165
Cdd:cd05923 29 LTYSELRARIEAVAARL-HARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN----------------PRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 IDNLGDAVEVLAG-HAPARLVVfdyhgkvdthrEAVEAARARLAGSVTIDTLAELIERGRALPATPIADSADdalALLIY 244
Cdd:cd05923 92 LAELIERGEMTAAvIAVDAQVM-----------DAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQP---AFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAM----YRESQVMSFWRKSSGWFepsGYPSITLNFMPMSHV-GGRQVLYGTLSNGGTAYFVAKSDLSTLF 319
Cdd:cd05923 158 TSGTTGLPKGAVipqrAAESRVLFMSTQAGLRH---GRHNVVLGLMPLYHViGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 EDLALVRPTELCFVPRIWDMVFAefHSEVDRRLVDgadraaleaqvkaELRENVLGGrfvmaltgsapisAEMTawvESL 399
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAA--AAEFAGLKLS-------------SLRHVTFAG-------------ATMP---DAV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LADVH------LVEGYGSTEAGMVLND-----GMVRRPAVidYKLVDVPELGYfGTDQPYP---RGELLVKTQT--MFPG 463
Cdd:cd05923 284 LERVNqhlpgeKVNIYGTTEAMNSLYMrdartGTEMRPGF--FSEVRIVRIGG-SPDEALAngeEGELIVAAAAdaAFTG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 464 YYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYP- 542
Cdd:cd05923 361 YLNQPEATAKKLQ-DGWYRTGDV-GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGq 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489508543 543 --LAVVVPsgdalsrhgieNLKPVISESLQEVARAAGLQSYEIPRDFII 589
Cdd:cd05923 439 svTACVVP-----------REGTLSADELDQFCRASELADFKRPRRYFF 476
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
86-548 |
5.16e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 95.20 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATS 165
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 IDNLG-DAVEVLAGHAPARLVVFDYHGKVDTHREAVeAARARLAGSVTIDTlaeliERGRALPATPIADSADDALALLIY 244
Cdd:PRK06164 115 PGFKGiDFAAILAAVPPDALPPLRAIAVVDDAADAT-PAPAPGARVQLFAL-----PDPAPPAAAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSFWRKSSGWFepsGYP--SITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDL 322
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAY---GYDpgAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 323 ALVRPTElcfvpriwdmVFAefHSEVDRRLVDGADRAALEAQVKaelrenvlggrfVMALTGSAPISAEMTAWVESllAD 402
Cdd:PRK06164 266 RRHRVTH----------TFG--NDEMLRRILDTAGERADFPSAR------------LFGFASFAPALGELAALARA--RG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 403 VHLVEGYGSTE--AGMVLND------------GMVRRPAvIDYKLVDVPELGYFGTDQPyprGELLVKTQTMFPGYYQRP 468
Cdd:PRK06164 320 VPLTGLYGSSEvqALVALQPatdpvsvrieggGRPASPE-ARVRARDPQDGALLPDGES---GEIEIRAPSLMRGYLDNP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 469 DVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAV--V 546
Cdd:PRK06164 396 DATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVafV 474
|
..
gi 489508543 547 VP 548
Cdd:PRK06164 475 IP 476
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
82-533 |
1.07e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 93.80 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 82 RFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTM 161
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 162 IATSidnlgdavevlaghaparlvvfdyhgkvdthreavEAARARLAGSVTIDTLAELIERGRALPATPIADSadDALAL 241
Cdd:cd12117 98 LLTD-----------------------------------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSP--DDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LIYTSGSTGAPKGAMYRESQVMSFwRKSSGWFEPSGYPSItLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSdlstlfed 321
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRL-VKNTNYVTLGPDDRV-LQTSPLAFDASTFEIWGALLNGARLVLAPKG-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 322 lALVRPTELcfvpriwdmvfaefhsevdRRLVD--GADRAALEA---QVKAELRENVLGG-RFVmaLTGSAPISAemtAW 395
Cdd:cd12117 211 -TLLDPDAL-------------------GALIAeeGVTVLWLTAalfNQLADEDPECFAGlREL--LTGGEVVSP---PH 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLLA---DVHLVEGYGSTE-----AGMVLNDGMVRRPAV-----IDYKLVDVpeLGYFGTDQPYPR-GELLVKTQTMF 461
Cdd:cd12117 266 VRRVLAacpGLRLVNGYGPTEnttftTSHVVTELDEVAGSIpigrpIANTRVYV--LDEDGRPVPPGVpGELYVGGDGLA 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 462 PGYYQRPDVTAEVFDPDGF------YRTGDImAKVGPD-QFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFI 533
Cdd:cd12117 344 LGYLNRPALTAERFVADPFgpgerlYRTGDL-ARWLPDgRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVV 420
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
85-585 |
1.69e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 93.67 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSV---PLQTSAPV------TGLRPIVT 155
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYTAREMehqfndSGAKALVC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 156 eteptmiatsIDNLGDAVEVLAGHAPARLV----VFDYHGKVdtHREAVEAA---------RARLAGSVTidtLAELIER 222
Cdd:PRK05677 129 ----------LANMAHLAEKVLPKTGVKHVivteVADMLPPL--KRLLINAVvkhvkkmvpAYHLPQAVK---FNDALAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 223 GRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQV---MSFWRKSSGWFEPSGYPSI------------TLNFMP 287
Cdd:PRK05677 194 GAGQPVTEANPQADD-VAVLQYTGGTTGVAKGAMLTHRNLvanMLQCRALMGSNLNEGCEILiaplplyhiyafTFHCMA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 288 MSHVGGRQVLY-------GTLSNGGTAYFVAKSDLSTLFedlalvrpTELCfvpriwdmvfaefHSEVDRRLvdgaDRAA 360
Cdd:PRK05677 273 MMLIGNHNILIsnprdlpAMVKELGKWKFSGFVGLNTLF--------VALC-------------NNEAFRKL----DFSA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 361 LEAQVKaelrenvlGGrfvMALTGSApisAEMtaWVEslLADVHLVEGYGSTEAGMVLNdgmVRRPAVIDYKLVDVP--- 437
Cdd:PRK05677 328 LKLTLS--------GG---MALQLAT---AER--WKE--VTGCAICEGYGMTETSPVVS---VNPSQAIQVGTIGIPvps 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 438 ----ELGYFGTDQPY-PRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSqGE 511
Cdd:PRK05677 387 tlckVIDDDGNELPLgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDI-ALIQEDGYMRIvDRKKDMILVS-GF 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 512 FIAVSKLEAVFGDSPLVRQIFIYG----NSARAYPLAVVVPSGDALSRhgienlkpvisESLQEVARaAGLQSYEIPR 585
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAIGvpdeKSGEAIKVFVVVKPGETLTK-----------EQVMEHMR-ANLTGYKVPK 530
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
84-560 |
2.42e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.37 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAvevlaghAPARLVVFDYHGKVDTHREAVEAARARlagsvtidtlAELIERGRALPATPIadSADDALALLi 243
Cdd:PLN02574 145 TSPENVEKL-------SPLGVPVIGVPENYDFDSKRIEFPKFY----------ELIKEDFDFVPKPVI--KQDDVAAIM- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRE----SQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQVL-YGTLSNGGTAYFVAKSDLSTL 318
Cdd:PLN02574 205 YSSGTTGASKGVVLTHrnliAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFvVGLLSLGSTIVVMRRFDASDM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWdmvfaefhsevdrrlvdgadrAALEAQVKAELRENVlgGRFVMALTGSAPISAEMTAWVES 398
Cdd:PLN02574 285 VKVIDRFKVTHFPVVPPIL---------------------MALTKKAKGVCGEVL--KSLKQVSCGAAPLSGKFIQDFVQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVHLVEGYGSTEAGMV----LNDGMVRRPAVI-------DYKLVDVPELGYFgtdQPYPRGELLVKTQTMFPGYYQR 467
Cdd:PLN02574 342 TLPHVDFIQGYGMTESTAVgtrgFNTEKLSKYSSVgllapnmQAKVVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 468 PDVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIYG---NSARAYPL 543
Cdd:PLN02574 419 PKATQSTIDKDGWLRTGDI-AYFDEDGYLYIvDRLKEIIKY-KGFQIAPADLEAVLISHPEIIDAAVTAvpdKECGEIPV 496
|
490
....*....|....*...
gi 489508543 544 AVVVP-SGDALSRHGIEN 560
Cdd:PLN02574 497 AFVVRrQGSTLSQEAVIN 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
84-715 |
2.61e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.84 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLrpivteteptmiA 163
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL------------A 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGdavevlaghapARLVVFDYHGkvdthreaveAARARLAGSVT---IDTLAELIERGRAL-PATPIADsadDAL 239
Cdd:PRK12467 603 YMLDDSG-----------VRLLLTQSHL----------LAQLPVPAGLRslcLDEPADLLCGYSGHnPEVALDP---DNL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 240 ALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKS---DLS 316
Cdd:PRK12467 659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERL-QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDcarDAE 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRlvdgadraaleaqvkaeLRENVLGGRfVMALTGSAPISAemtawv 396
Cdd:PRK12467 738 AFAALMADQGVTVLKIVPSHLQALLQASRVALPRP-----------------QRALVCGGE-ALQVDLLARVRA------ 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 esLLADVHLVEGYGSTEAGMVLNDGMVRR-PAVIDYKLVDVP--ELGYFGTD---QPYP---RGELLVKTQTMFPGYYQR 467
Cdd:PRK12467 794 --LGPGARLINHYGPTETTVGVSTYELSDeERDFGNVPIGQPlaNLGLYILDhylNPVPvgvVGELYIGGAGLARGYHRR 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 468 PDVTAEVFDPDGF-------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFI--YGNSA 538
Cdd:PRK12467 872 PALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDA 950
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 539 RAYPLAVVVPSGDALS-RHGIENLKpvISESLQEVaraagLQSYEIPRDFI-IETTPFTlENGlltgirKLARPQLKKFY 616
Cdd:PRK12467 951 GLQLVAYLVPAAVADGaEHQATRDE--LKAQLRQV-----LPDYMVPAHLLlLDSLPLT-PNG------KLDRKALPKPD 1016
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 617 GERLERLYteladsqsnelrelrqsgpDAPVLPtLCRAAAALLGST--AADVRPDAHFADLGGDSLSALSLANLLHEIFG 694
Cdd:PRK12467 1017 ASAVQATF-------------------VAPQTE-LEKRLAAIWADVlkVERVGLTDNFFELGGHSLLATQVISRVRQRLG 1076
|
650 660
....*....|....*....|.
gi 489508543 695 VDVPvgvivspasdLRALADH 715
Cdd:PRK12467 1077 IQVP----------LRTLFEH 1087
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-508 |
7.67e-19 |
|
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: 91.25 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSidnlgdavevlaghaparlvvfdyhgkvdthreavEAARARLAGSVTIDTLAELIERGRALPATPIADSADDALALLI 243
Cdd:cd17651 98 TH-----------------------------------PALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFV---AKSDLSTLFE 320
Cdd:cd17651 143 YTSGSTGRPKGVVMPHRSLANLVAWQARAS-SLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPpeeVRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLAlVRPTELCFVPriwdMVFAEFHSEVDRRLVDGAdraaleaqvkAELRENVLGGRfvmALTGSAPIsAEMTAWVESLL 400
Cdd:cd17651 222 WLD-EQRISRVFLP----TVALRALAEHGRPLGVRL----------AALRYLLTGGE---QLVLTEDL-REFCAGLPGLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 advhLVEGYGSTEA----GMVLNDGMVRRPAV------IDYKLVDVPElgyfGTDQPYPR---GELLVKTQTMFPGYYQR 467
Cdd:cd17651 283 ----LHNHYGPTEThvvtALSLPGDPAAWPAPppigrpIDNTRVYVLD----AALRPVPPgvpGELYIGGAGLARGYLNR 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489508543 468 PDVTAEVFDPDGF------YRTGDiMAKVGPD-QFVYLDRRNNVLKLS 508
Cdd:cd17651 355 PELTAERFVPDPFvpgarmYRTGD-LARWLPDgELEFLGRADDQVKIR 401
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-624 |
9.20e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 52 GYADRPALGQR-ALRFVTDPDSgrtmVELLPRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIA 130
Cdd:PRK12316 4546 GYPATRCVHQLvAERARMTPDA----VAVVFDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 131 LIRLGAVSVPLQTSAPVTGLrpivteteptmiATSIDNLGDAVEVLAGHAPARLVVfdyhgkvdthreaveaarARLAGS 210
Cdd:PRK12316 4621 VLKAGGAYVPLDPEYPRERL------------AYMMEDSGAALLLTQSHLLQRLPI------------------PDGLAS 4670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 211 VTIDTLAELIERGRALPATPIADsadDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSH 290
Cdd:PRK12316 4671 LALDRDEDWEGFPAHDPAVRLHP---DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRV-LQFMSFSF 4746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 291 VGGRQVLYGTLSNGGTAYFVAKS--DLSTLFEDLALVRPTELCFVPRIWDMvFAEfHSEVDRRLvdgadraaleaqvkAE 368
Cdd:PRK12316 4747 DGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQ-LAE-HAERDGEP--------------PS 4810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 369 LRENVLGGRFVmaltgsAPISAEMtAWveSLLADVHLVEGYGSTEAGMVLN-----DGMVRRPAVIDYKLVDVPELGYFG 443
Cdd:PRK12316 4811 LRVYCFGGEAV------AQASYDL-AW--RALKPVYLFNGYGPTETTVTVLlwkarDGDACGAAYMPIGTPLGNRSGYVL 4881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 444 TDQPYPR-----GELLVKTQTMFPGYYQRPDVTAEVFDPDGF-------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQG 510
Cdd:PRK12316 4882 DGQLNPLpvgvaGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGD-LARYRADGVIdYLGRVDHQVKI-RG 4959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 511 EFIAVSKLEAVFGDSPLVRQIFIYG--NSARAYPLAVVVPSGDALSrhgieNLKPVISESLQEVARAAG--LQSYEIPRD 586
Cdd:PRK12316 4960 FRIELGEIEARLREHPAVREAVVIAqeGAVGKQLVGYVVPQDPALA-----DADEAQAELRDELKAALRerLPEYMVPAH 5034
|
570 580 590
....*....|....*....|....*....|....*....
gi 489508543 587 FI-IETTPFTlENGlltgirKLARPQLKKFYGERLERLY 624
Cdd:PRK12316 5035 LVfLARMPLT-PNG------KLDRKALPQPDASLLQQAY 5066
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-552 |
1.29e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 90.77 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsapvtgLRPIVTETEPTMIATSI 166
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV------------LHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 DNLGDAV-----------EVLAGHAPARLVVFDYHGKVDTHREAVEAARArlagsvtidtLAELIERGRALPATPIADsa 235
Cdd:cd12119 94 NHAEDRVvfvdrdflpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLA----------YEELLAAESPEYDWPDFD-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDALALLIYTSGSTGAPKGAMY-RESQV---MSFWRKSSGWFEPSgypSITLNFMPMSHV------------GGRQVLYG 299
Cdd:cd12119 162 ENTAAAICYTSGTTGNPKGVVYsHRSLVlhaMAALLTDGLGLSES---DVVLPVVPMFHVnawglpyaaamvGAKLVLPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 300 tlsnggtayfvAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEvdrrlvdGADRAAleaqvkaeLRENVLGgrfv 379
Cdd:cd12119 239 -----------PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEAN-------GRDLSS--------LRRVVIG---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 380 maltGSAPISAEMTAWVEsllADVHLVEGYGSTEA---GMV--LNDGMV---------------RRPAVIDYKLVDvPEl 439
Cdd:cd12119 289 ----GSAVPRSLIEAFEE---RGVRVIHAWGMTETsplGTVarPPSEHSnlsedeqlalrakqgRPVPGVELRIVD-DD- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 440 gyfGTDQPY---PRGELLVKTQTMFPGYYqRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKlSQGEFIAV 515
Cdd:cd12119 360 ---GRELPWdgkAVGELQVRGPWVTKSYY-KNDEESEALTEDGWLRTGDV-ATIDEDGYLTItDRSKDVIK-SGGEWISS 433
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489508543 516 SKLEAVFGDSPLVRQIFIYGN-----SARayPLAVVVPSGDA 552
Cdd:cd12119 434 VELENAIMAHPAVAEAAVIGVphpkwGER--PLAVVVLKEGA 473
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-595 |
1.60e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 90.65 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 53 YADRPALGQRALrfvtdpdsgrtmvellprfeTITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALI 132
Cdd:PRK12492 37 FADRPAFSNLGV--------------------TLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 133 RLGAVSV---PLQTSAPV------TGLRPIV------TETEPTMIATSIDNLgdaVEVLAGHAPARLVVFDYHGKVDTHR 197
Cdd:PRK12492 97 RAGLIVVntnPLYTAREMrhqfkdSGARALVylnmfgKLVQEVLPDTGIEYL---IEAKMGDLLPAAKGWLVNTVVDKVK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 198 EAVEAARARLAGSvtidtLAELIERGRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQV---MSFWRKSSGWFE 274
Cdd:PRK12492 174 KMVPAYHLPQAVP-----FKQALRQGRGLSLKPVPVGLDD-IAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 275 PSGYPSI-------------------TLNFMPMSHVGGRQVLY-------GTLSNGGTAYFVAKSDLSTLFedLALvrpt 328
Cdd:PRK12492 248 PDGQPLMkegqevmiaplplyhiyafTANCMCMMVSGNHNVLItnprdipGFIKELGKWRFSALLGLNTLF--VAL---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 329 elcfvpriwdMVFAEFHSevdrrlvdgADRAALEaqvkaelrenvlggrfVMALTGSAPISAEMTAWVEslLADVHLVEG 408
Cdd:PRK12492 322 ----------MDHPGFKD---------LDFSALK----------------LTNSGGTALVKATAERWEQ--LTGCTIVEG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 409 YGSTEAGMVLND---------GMVRRPA------VIDYKLVDVPelgyFGTdqpypRGELLVKTQTMFPGYYQRPDVTAE 473
Cdd:PRK12492 365 YGLTETSPVASTnpygelarlGTVGIPVpgtalkVIDDDGNELP----LGE-----RGELCIKGPQVMKGYWQQPEATAE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 474 VFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG----NSARAYPLaVVVP 548
Cdd:PRK12492 436 ALDAEGWFKTGDI-AVIDPDGFVRIvDRKKDLIIVS-GFNVYPNEIEDVVMAHPKVANCAAIGvpdeRSGEAVKL-FVVA 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 489508543 549 SGDALSrhgIENLKPVISESlqevaraagLQSYEIPRDFII-ETTPFT 595
Cdd:PRK12492 513 RDPGLS---VEELKAYCKEN---------FTGYKVPKHIVLrDSLPMT 548
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
84-614 |
1.68e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 90.02 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTsapvtglRPIVTEteptmIA 163
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT-------RLSREE-----LL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNlgdavevlaghAPARLVVFD--YHGKVDTHreaveaararlaGSVTIDTLAELIERgralPATPIADSADDALAL 241
Cdd:PRK03640 93 WQLDD-----------AEVKCLITDddFEAKLIPG------------ISVKFAELMNGPKE----EAEIQEEFDLDEVAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LIYTSGSTGAPKGAMYR-----ESQVMSFW----RKSSGWfepsgypsitLNFMPMSHVGG-----RQVLYGTlsnggTA 307
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTygnhwWSAVGSALnlglTEDDCW----------LAAVPIFHISGlsilmRSVIYGM-----RV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 308 YFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHsevdrrlvdgadraalEAQVKAELRENVLGGrfvmaltGSAP 387
Cdd:PRK03640 211 VLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLG----------------EGTYPSSFRCMLLGG-------GPAP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 388 isaemtawvESLLA-----DVHLVEGYGSTEAG----------MVLNDGMVRRP---AVIdyKLVDVPELGyfgtdQPYP 449
Cdd:PRK03640 268 ---------KPLLEqckekGIPVYQSYGMTETAsqivtlspedALTKLGSAGKPlfpCEL--KIEKDGVVV-----PPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 450 RGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVY-LDRRNNvLKLSQGEFIAVSKLEAVFGDSPLV 528
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDI-GYLDEEGFLYvLDRRSD-LIISGGENIYPAEIEEVLLSHPGV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 529 RQIFIYGNSAR---AYPLAVVVPSGdalsrhgienlkPVISESLQEVARAAgLQSYEIPRDF-IIETTPFTLENglltgi 604
Cdd:PRK03640 409 AEAGVVGVPDDkwgQVPVAFVVKSG------------EVTEEELRHFCEEK-LAKYKVPKRFyFVEELPRNASG------ 469
|
570
....*....|
gi 489508543 605 rKLARPQLKK 614
Cdd:PRK03640 470 -KLLRHELKQ 478
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
84-547 |
2.64e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 90.23 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAVEVLAGHAPARLVVFdyhgkvdTHREAVEAARARLAGSVTIDTLAELIERGRALPATPIADsaDDALALLI 243
Cdd:PRK05620 117 ADPRLAEQLGEILKECPCVRAVVF-------IGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELD--ETTAAAIC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESqvmSFWRKSSGWFEPSGYpSIT-----LNFMPMSHVggrqvlygtLSNG--------GTAYFV 310
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHR---SLYLQSLSLRTTDSL-AVThgesfLCCVPIYHV---------LSWGvplaafmsGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 311 AKSDLS--TLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRLvdgadraaleaqvkaELRENVLGgrfvmaltGSAPI 388
Cdd:PRK05620 255 PGPDLSapTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERM---------------SLQEIYVG--------GSAVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 389 SAEMTAWVESLLADVhlVEGYGSTEAGMVlndGMVRRP--------------------AVIDYKLVDVPELgYFGTDQpy 448
Cdd:PRK05620 312 PILIKAWEERYGVDV--VHVWGMTETSPV---GTVARPpsgvsgearwayrvsqgrfpASLEYRIVNDGQV-MESTDR-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 449 PRGELLVKTQTMFPGYYQRP----------------DVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKlSQGE 511
Cdd:PRK05620 384 NEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDV-GSVTRDGFLTIhDRARDVIR-SGGE 461
|
490 500 510
....*....|....*....|....*....|....*....
gi 489508543 512 FIAVSKLEAVFGDSPLVRQIFIYGNSARAY---PLAVVV 547
Cdd:PRK05620 462 WIYSAQLENYIMAAPEVVECAVIGYPDDKWgerPLAVTV 500
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
84-514 |
2.78e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 89.61 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAVEVLAGHAPARLVVfdyhgkvdthrEAVEAARARLAGSVTIDTLAEliergRALPATPIADSADDALALLI 243
Cdd:PRK08316 114 VDPALAPTAEAALALLPVDTLIL-----------SLVLGGREAPGGWLDFADWAE-----AGSVAEPDVELADDDLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMsfWRKSS----GWFEPSGYPsitLNFMPMSHVGGRQVLYGT-LSNGGTAYFVAKSDLSTL 318
Cdd:PRK08316 178 YTSGTESLPKGAMLTHRALI--AEYVScivaGDMSADDIP---LHALPLYHCAQLDVFLGPyLYVGATNVILDAPDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWdmVFAEFHSEVDRRlvdgaDRAALEaqvKAELrenvlgGRFVMaltgSAPISAEMTAwves 398
Cdd:PRK08316 253 LRTIEAERITSFFAPPTVW--ISLLRHPDFDTR-----DLSSLR---KGYY------GASIM----PVEVLKELRE---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVHLVEGYGSTEAG---MVLN-DGMVRRPA------------VIDYKLVDVPElgyfGTdqpypRGELLVKTQTMFP 462
Cdd:PRK08316 309 RLPGLRFYNCYGQTEIAplaTVLGpEEHLRRPGsagrpvlnvetrVVDDDGNDVAP----GE-----VGEIVHRSPQLML 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 463 GYYQRPDVTAEVFDpDGFYRTGDIMAKvgpDQFVYL---DRRNNVLKlSQGEFIA 514
Cdd:PRK08316 380 GYWDDPEKTAEAFR-GGWFHSGDLGVM---DEEGYItvvDRKKDMIK-TGGENVA 429
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
86-535 |
5.37e-18 |
|
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: 87.92 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQtsapvtglrPIVTETEPTMIATS 165
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNK-GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPIN---------PMLKERELEYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 idnlgdavevlaghaparlvvfdyhgkvdthreaveaararlAGSVTIDTLAELiergralpatpiadsadDALALLIYT 245
Cdd:cd05935 72 ------------------------------------------SGAKVAVVGSEL-----------------DDLALIPYT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 246 SGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGyPSITLNFMPMSHVGGRQVLYGT-LSNGGTAYFVAKSDLSTLFEDLAL 324
Cdd:cd05935 93 SGTTGLPKGCMHTHFSAAANALQSAVWTGLTP-SDVILACLPLFHVTGFVGSLNTaVYVGGTYVLMARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 325 VRPTelcfvpriwdmvfaeFHSEVDRRLVDGADRAALEAQVKAELRenVLGGrfvmaltGSAPISaemTAWVESL--LAD 402
Cdd:cd05935 172 YKVT---------------FWTNIPTMLVDLLATPEFKTRDLSSLK--VLTG-------GGAPMP---PAVAEKLlkLTG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 403 VHLVEGYGSTEAGMVLNDGMVRRPAV---------IDYKLVDVPELGYFGTDQpypRGELLVKTQTMFPGYYQRPDVTAE 473
Cdd:cd05935 225 LRFVEGYGLTETMSQTHTNPPLRPKLqclgip*fgVDARVIDIETGRELPPNE---VGEIVVRGPQIFKGYWNRPEETEE 301
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 474 VFDPDG---FYRTGDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:cd05935 302 SFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
84-556 |
1.08e-17 |
|
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: 87.35 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd12116 11 RSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSidnlgdavevlaghaparlvvfdyhgkvdthreavEAARARLAGSVtiDTLAELIERGRALPATPIADSADDALALLI 243
Cdd:cd12116 90 TD-----------------------------------DALPDRLPAGL--PVLLLALAAAAAAPAAPRTPVSPDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRkssgwfepsgypSI--TLNFMPmshvGGRQV-------------LYGTLSNGGTAY 308
Cdd:cd12116 133 YTSGSTGRPKGVVVSHRNLVNFLH------------SMreRLGLGP----GDRLLavttyafdislleLLLPLLAGARVV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 309 FV---AKSDLSTLFEDLALVRPTELCFVPRIWDMVFAefhsevdrrlVDGADRAALEAQVKAELRENVLGGRFVmALTGS 385
Cdd:cd12116 197 IApreTQRDPEALARLIEAHSITVMQATPATWRMLLD----------AGWQGRAGLTALCGGEALPPDLAARLL-SRVGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 386 A-----PisAEMTAW-----VESLLADVHLVEGYGSTEAgMVLNDGMvrrpavidyklvdvpelgyfgtdQPYPRG---E 452
Cdd:cd12116 266 LwnlygP--TETTIWstaarVTAAAGPIPIGRPLANTQV-YVLDAAL-----------------------RPVPPGvpgE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 453 LLVKTQTMFPGYYQRPDVTAEVFDPDGF-------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDS 525
Cdd:cd12116 320 LYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAH 398
|
490 500 510
....*....|....*....|....*....|....*....
gi 489508543 526 PLVRQ----IFIYGNSAR--AY--PLAVVVPSGDALSRH 556
Cdd:cd12116 399 PGVAQaavvVREDGGDRRlvAYvvLKAGAAPDAAALRAH 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
45-589 |
1.26e-17 |
|
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: 87.42 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 45 LIRMVMEGYADRPALgqralrfvTDPDSgrtmvellprfeTITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDY 124
Cdd:cd05959 9 VDLNLNEGRGDKTAF--------IDDAG------------SLTYAELEAEARRVAGAL-RALGVKREERVLLIMLDTVDF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 125 TTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATS---IDNLGDAVEvLAGHAPARLVVFDYHGKVDTHreave 201
Cdd:cd05959 68 PTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSgelAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 202 aararlagsvtiDTLAELIeRGRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESqvmsfwrkssgwfepsgypsi 281
Cdd:cd05959 142 ------------LLLAELV-AAEAEQLKPAATHADD-PAFWLYSSGSTGRPKGVVHLHA--------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 282 tlNFMPMSHVGGRQVLYGT------------------------LSNGGTAYFVA-KSDLSTLFEDLALVRPTELCFVPRI 336
Cdd:cd05959 187 --DIYWTAELYARNVLGIReddvcfsaaklffayglgnsltfpLSVGATTVLMPeRPTPAAVFKRIRRYRPTVFFGVPTL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 337 WDMVFAefhSEVDRRLVDGADRAALEAqvkAELRENVLGGRFvMALTGsapisaemtawveslladVHLVEGYGSTEAGM 416
Cdd:cd05959 265 YAAMLA---APNLPSRDLSSLRLCVSA---GEALPAEVGERW-KARFG------------------LDILDGIGSTEMLH 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 417 VLndgMVRRPAVIDYKLVDVPELGY-----------FGTDQPyprGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGD 485
Cdd:cd05959 320 IF---LSNRPGRVRYGTTGKPVPGYevelrdedggdVADGEP---GELYVRGPSSATMYWNNRDKTRDTFQ-GEWTRTGD 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 486 IMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG---NSARAYPLAVVVP-----SGDALSRHG 557
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQHPAVLEAAVVGvedEDGLTKPKAFVVLrpgyeDSEALEEEL 471
|
570 580 590
....*....|....*....|....*....|..
gi 489508543 558 IENLKpviseslqevaraAGLQSYEIPRDFII 589
Cdd:cd05959 472 KEFVK-------------DRLAPYKYPRWIVF 490
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
85-614 |
1.45e-17 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 86.63 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTsapvtglrpivteteptmiat 164
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAL-GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNT--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sidnlgdavevlaghaparlvvfdyhgkvdthreaveaaraRLagsvtidTLAELIERGRAlpatpiADSADDALALLIY 244
Cdd:cd05912 59 -----------------------------------------RL-------TPNELAFQLKD------SDVKLDDIATIMY 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMyrESQVMSFWR-KSS----GWFEPSGYpsitLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLF 319
Cdd:cd05912 85 TSGTTGKPKGVQ--QTFGNHWWSaIGSalnlGLTEDDNW----LCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 EDLALVRPTELCFVPRIWDMVFAEFHSevdrrlvdgadraaleaQVKAELRENVLGGrfvmaltgsAPISAEMTAwvESL 399
Cdd:cd05912 159 HLINSGKVTIISVVPTMLQRLLEILGE-----------------GYPNNLRCILLGG---------GPAPKPLLE--QCK 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LADVHLVEGYGSTEAG----------MVLNDGMVRRP-AVIDYKLVDvpelgyfGTDQPYPRGELLVKTQTMFPGYYQRP 468
Cdd:cd05912 211 EKGIPVYQSYGMTETCsqivtlspedALNKIGSAGKPlFPVELKIED-------DGQPPYEVGEILLKGPNVTKGYLNRP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 469 DVTAEVFDpDGFYRTGDImAKVGPDQFVY-LDRRNNvLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAY---PLA 544
Cdd:cd05912 284 DATEESFE-NGWFKTGDI-GYLDEEGFLYvLDRRSD-LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvPVA 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 545 VVVPSgdalsrhgienlKPVISESLQEVARAAgLQSYEIPRDFII-ETTPFTLENglltgirKLARPQLKK 614
Cdd:cd05912 361 FVVSE------------RPISEEELIAYCSEK-LAKYKVPKKIYFvDELPRTASG-------KLLRHELKQ 411
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
86-600 |
1.55e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 87.63 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRpivteteptmiats 165
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQR-------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 idnlgdaveVLAGHAPARLVVFDYHGKVDThreAVEAARA-RLAGSVTIDTLAE----LIERGRALPATPIAdSADDAL- 239
Cdd:PRK05852 109 ---------VRSQAAGARVVLIDADGPHDR---AEPTTRWwPLTVNVGGDSGPSggtlSVHLDAATEPTPAT-STPEGLr 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 240 ---ALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEpSGYPSITLNFMPMSHVGGR-QVLYGTLSNGGTAYFVAKSDL 315
Cdd:PRK05852 176 pddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR-LSPRDATVAVMPLYHGHGLiAALLATLASGGAVLLPARGRF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 316 S--TLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRlvdgaDRAALeaqvkaelrenvlggRFVMALtgSAPISAEMT 393
Cdd:PRK05852 255 SahTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGR-----KPAAL---------------RFIRSC--SAPLTAETA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 394 -AWVESLLADVhlVEGYGSTEAGM----------------VLNDGMVRRPAVIDYKLVdvpelgyfGTD-QPYPR---GE 452
Cdd:PRK05852 313 qALQTEFAAPV--VCAFGMTEATHqvtttqiegigqtenpVVSTGLVGRSTGAQIRIV--------GSDgLPLPAgavGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 453 LLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIF 532
Cdd:PRK05852 383 VWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAA 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 533 IYGNSARAYP---LAVVVPSGDAlsrhgienlkPVISESLQEVARaAGLQSYEIPRDF-IIETTPFTLENGL 600
Cdd:PRK05852 461 VFGVPDQLYGeavAAVIVPRESA----------PPTAEELVQFCR-ERLAAFEIPASFqEASGLPHTAKGSL 521
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
85-588 |
2.93e-17 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 86.18 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivteteptmiat 164
Cdd:cd17646 23 TLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sidnlGDAVEVLAGHAPARLVVfdyhgkvdTHREAVEAARARLAGSVTIDTLAelierGRALPATPIADSADDALALLIY 244
Cdd:cd17646 84 -----ADRLAYMLADAGPAVVL--------TTADLAARLPAGGDVALLGDEAL-----AAPPATPPLVPPRPDNLAYVIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSFWRkssgWFE---------------PSGY-PSITLNFMPMShVGGRQVLygtLSNGGtay 308
Cdd:cd17646 146 TSGSTGRPKGVMVTHAGIVNRLL----WMQdeyplgpgdrvlqktPLSFdVSVWELFWPLV-AGARLVV---ARPGG--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 309 fvaKSDLSTLFEDLALVRPTELCFVPRIWDmVFAEfhsevdrrlVDGADRAaleaqvkAELRENVLGGRfvmALTGSApi 388
Cdd:cd17646 215 ---HRDPAYLAALIREHGVTTCHFVPSMLR-VFLA---------EPAAGSC-------ASLRRVFCSGE---ALPPEL-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 389 saeMTAWVEslLADVHLVEGYGSTEAGMVLNDGMVRRPAVIDYKLVDVPELG---YFGTD--QPYPR---GELLVKTQTM 460
Cdd:cd17646 270 ---AARFLA--LPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNtrlYVLDDalRPVPVgvpGELYLGGVQL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 461 FPGYYQRPDVTAEVFDPDGF------YRTGDImAKVGPD-QFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFI 533
Cdd:cd17646 345 ARGYLGRPALTAERFVPDPFgpgsrmYRTGDL-ARWRPDgALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 534 Y---GNSARAYPLAVVVPSGDALsrhgienlkPVISESLQEVARAAgLQSYEIPRDFI 588
Cdd:cd17646 423 VaraAPAGAARLVGYVVPAAGAA---------GPDTAALRAHLAER-LPEYMVPAAFV 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-741 |
2.99e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 51 EGYADRPALGQR-ALRFVTDPDSgrtmVELLPRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDI 129
Cdd:PRK12316 1997 EAYPRGPGVHQRiAEQAARAPEA----IAVVFGDQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALL 2071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 130 ALIRLGAVSVPLQTSAPvtglrpivTETEPTMIATSidnlGDAVEVLAGHAPARLvvfdyhgkvdthreAVEAARARLAg 209
Cdd:PRK12316 2072 AVLKAGGAYVPLDPNYP--------AERLAYMLEDS----GAALLLTQRHLLERL--------------PLPAGVARLP- 2124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 210 svtIDTLAELIERGRALPATpiaDSADDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSgyPSIT-LNFMPM 288
Cdd:PRK12316 2125 ---LDRDAEWADYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELS--PADCeLQFMSF 2196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 289 SHVGGRQVLYGTLSNGgtAYFVAKSDLSTLFEDLA--LVRP--TELCFVPRIWDMvFAEfHSEVDRRlvdgadraaleaq 364
Cdd:PRK12316 2197 SFDGAHEQWFHPLLNG--ARVLIRDDELWDPEQLYdeMERHgvTILDFPPVYLQQ-LAE-HAERDGR------------- 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 365 vKAELRENVLGGrfvmaltgSAPISAEMTAWVESLLAdVHLVEGYGSTEA----------------------GMVLNDgm 422
Cdd:PRK12316 2260 -PPAVRVYCFGG--------EAVPAASLRLAWEALRP-VYLFNGYGPTEAvvtpllwkcrpqdpcgaayvpiGRALGN-- 2327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 423 vRRPAVIDYKLVDVPelgyfgtdqPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGF-------YRTGDIMAKVGPDQF 495
Cdd:PRK12316 2328 -RRAYILDADLNLLA---------PGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVV 2397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 496 VYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQifiygnsarayplAVVV----PSGDALSRHGI-ENLKPVISESLQ 570
Cdd:PRK12316 2398 EYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVRE-------------AVVVaqdgASGKQLVAYVVpDDAAEDLLAELR 2463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 571 EVARAAgLQSYEIPRDFIIettpftLENGLLTGIRKLARPQLKKFYGERLERLYTeladsqsnelrelrqsGPDAPVLPT 650
Cdd:PRK12316 2464 AWLAAR-LPAYMVPAHWVV------LERLPLNPNGKLDRKALPKPDVSQLRQAYV----------------APQEGLEQR 2520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 651 LCRAAAALLGstAADVRPDAHFADLGGDSLSALSLANLLHEIFGVDVPVGvIVSPASDLRALADHIEAARTGVRRPSFAS 730
Cdd:PRK12316 2521 LAAIWQAVLK--VEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLR-ILFERPTLAAFAASLESGQTSRAPVLQKV 2597
|
730
....*....|.
gi 489508543 731 IHGRSATEVHA 741
Cdd:PRK12316 2598 TRVQPLPLSHA 2608
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
84-531 |
3.64e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.82 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaddalALLI 243
Cdd:cd17643 90 TDPDDL----------------------------------------------------------------------AYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSITLnFMPMSHVGGRQVLYGTLSNGGTAYFVAKsDLSTLFEDLA 323
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTL-FHSYAFDFSVWEIWGALLHGGRLVVVPY-EVARSPEDFA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 324 LV----RPTELCFVPriwdmvfAEFhsevdRRLVDgADRAALEAQvkAELRENVLGGRfvmALTGSApisaeMTAWVESL 399
Cdd:cd17643 178 RLlrdeGVTVLNQTP-------SAF-----YQLVE-AADRDGRDP--LALRYVIFGGE---ALEAAM-----LRPWAGRF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LAD-VHLVEGYGSTEAgMVLNDGMVRRPAVIDYKLVDV-----PELGYFGTD---QPYPR---GELLVKTQTMFPGYYQR 467
Cdd:cd17643 235 GLDrPQLVNMYGITET-TVHVTFRPLDAADLPAAAASPigrplPGLRVYVLDadgRPVPPgvvGELYVSGAGVARGYLGR 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 468 PDVTAEVFDPDGF-------YRTGDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQI 531
Cdd:cd17643 314 PELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIR-GFRIELGEIEAALATHPSVRDA 383
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
97-627 |
3.88e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.39 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 97 TLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVL 176
Cdd:PLN02860 44 SLAAGLL-RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 177 AGHAPA-RLVVFdyhGKVDTHREAVEAARArlagsVTIDTLaelieRGRAL-PATPIADSADDALALLIYTSGSTGAPKG 254
Cdd:PLN02860 123 NDRLPSlMWQVF---LESPSSSVFIFLNSF-----LTTEML-----KQRALgTTELDYAWAPDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 255 AMYRESqvmSFWRKSSGWFEPSGYPS--ITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCF 332
Cdd:PLN02860 190 VTISHS---ALIVQSLAKIAIVGYGEddVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 333 VPRIWdmvfaefhsevdrrlvdgADRAALeaqvkAELRENVLGGRFVMA-LTGSAPISAEMTAWVESLLADVHLVEGYGS 411
Cdd:PLN02860 267 VPAMM------------------ADLISL-----TRKSMTWKVFPSVRKiLNGGGSLSSRLLPDAKKLFPNAKLFSAYGM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 412 TEAG-----MVLNDGMVRRPAVIDYKLVDVP-------------------ELGyFGTDQPYPRGELLVKTQTMFPGYYQR 467
Cdd:PLN02860 324 TEACssltfMTLHDPTLESPKQTLQTVNQTKsssvhqpqgvcvgkpaphvELK-IGLDESSRVGRILTRGPHVMLGYWGQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 468 PDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFIYG-NSARAYPLAVV 546
Cdd:PLN02860 403 NSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVGvPDSRLTEMVVA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 547 VPS-------GDALSRHGIENLKpVISESLQEVARAAGLQSYEIPRDFIIETTPFTLENgllTGirKLARPQLKKFYGER 619
Cdd:PLN02860 482 CVRlrdgwiwSDNEKENAKKNLT-LSSETLRHHCREKNLSRFKIPKLFVQWRKPFPLTT---TG--KIRRDEVRREVLSH 555
|
....*...
gi 489508543 620 LERLYTEL 627
Cdd:PLN02860 556 LQSLPSNL 563
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
75-571 |
8.96e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.55 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 75 TMVELLPRFETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpiv 154
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRL-IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYP-------- 3142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 155 teteptmiatsidnlGDAVEVLAGHAPARLVVFDYHgkvdthreaveaarARLAGSVTIDTLAELIERGRALPATPIADS 234
Cdd:PRK12316 3143 ---------------EERLAYMLEDSGAQLLLSQSH--------------LRLPLAQGVQVLDLDRGDENYAEANPAIRT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 235 ADDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEpSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSD 314
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG-LGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPED 3272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 LSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRLVDGADRAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTA 394
Cdd:PRK12316 3273 WRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 395 WVESLLADVHLVEGYGSTEAGMVLNDGMVrrpavidyklvdvpelgyfgtdQPYPRG---ELLVKTQTMFPGYYQRPDVT 471
Cdd:PRK12316 3353 WQCVEEGKDAVPIGRPIANRACYILDGSL----------------------EPVPVGalgELYLGGEGLARGYHNRPGLT 3410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 472 AEVFDPDGF------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAV 545
Cdd:PRK12316 3411 AERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYV 3489
|
490 500
....*....|....*....|....*.
gi 489508543 546 VVPSGDALSRhgiENLKPVISESLQE 571
Cdd:PRK12316 3490 VPEDEAGDLR---EALKAHLKASLPE 3512
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
84-530 |
1.14e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAirpGDRVCVlGF---NSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivTETEPT 160
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGV---GPDVLV-GVaveRSVEMIVALLAVLKAGGAYVPLDPEYP--------RERLAY 3186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATSidnlgdAVEVLAGHAparlvvfdyhgKVDTHREAVEAARArlagsVTIDTLAELIErgraLPATPIADSADDALA 240
Cdd:PRK12467 3187 MIEDS------GVKLLLTQA-----------HLLEQLPAPAGDTA-----LTLDRLDLNGY----SENNPSTRVMGENLA 3240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 241 LLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQVLYGTLSNGGtAYFVAKSDL---ST 317
Cdd:PRK12467 3241 YVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRV-LLFMSFSFDGAQERFLWTLICGG-CLVVRDNDLwdpEE 3318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LFEDLALVRPTELCFVPRIWDMvFAEFHsevdrrlvDGADRAALEaqvkaelrenvlggrfVMALTGSApISAEMTAWVE 397
Cdd:PRK12467 3319 LWQAIHAHRISIACFPPAYLQQ-FAEDA--------GGADCASLD----------------IYVFGGEA-VPPAAFEQVK 3372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 SLLADVHLVEGYGSTEAGMVL------NDGMVRRPAV-IDyklVDVPELGYFGTD---QPYPR---GELLVKTQTMFPGY 464
Cdd:PRK12467 3373 RKLKPRGLTNGYGPTEAVVTVtlwkcgGDAVCEAPYApIG---RPVAGRSIYVLDgqlNPVPVgvaGELYIGGVGLARGY 3449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 465 YQRPDVTAEVFDPDGF-------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:PRK12467 3450 HQRPSLTAERFVADPFsgsggrlYRTGD-LARYRADGVIeYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVRE 3521
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
85-535 |
1.75e-16 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 83.58 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:cd05903 1 RLTYSELDTRADRLAAGL-AALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 SidnlgdavEVLAGHAPArlvvfdyhgkvdthreaveaararlagsvtidtlaeliergrALPatpiadsadDALALLIY 244
Cdd:cd05903 80 P--------ERFRQFDPA------------------------------------------AMP---------DAVALLLF 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGrqVLYGTlsnggTAYFV--AKSDLSTLFED- 321
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAHQTG--FVYGF-----TLPLLlgAPVVLQDIWDPd 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 322 --LALVRPTELCFV----PRIWDMVfaefhsevdrRLVDGADRAAleaqvkAELRENVLGGrfvmaltgsAPISAEMTAW 395
Cdd:cd05903 173 kaLALMREHGVTFMmgatPFLTDLL----------NAVEEAGEPL------SRLRTFVCGG---------ATVPRSLARR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLLADVhLVEGYGSTEAGMVL-------------NDGMVRrpAVIDYKLVDvpelGYFGTDQPYPRGELLVKTQTMFP 462
Cdd:cd05903 228 AAELLGAK-VCSAYGSTECPGAVtsitpapedrrlyTDGRPL--PGVEIKVVD----DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 463 GYYQRPDVTAEvFDPDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:cd05903 301 GYLDRPDLTAD-AAPEGWFRTGD-LARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
84-590 |
1.97e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 84.16 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSV---PLQTSAPvtgLRPIVTETEPT 160
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVnvnPLYTPRE---LKHQLIDSGAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATsIDNLGDAVEVLAGHAPARLVVFDYHG------KVDTHREAVEAARA-----RLAGSVTI-DTLAelIERGRALPA 228
Cdd:PRK08751 126 VLVV-IDNFGTTVQQVIADTPVKQVITTGLGdmlgfpKAALVNFVVKYVKKlvpeyRINGAIRFrEALA--LGRKHSMPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 229 TPIADsadDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGY----PSITLNFMPMSHVggrqvlYGTLSN- 303
Cdd:PRK08751 203 LQIEP---DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHI------FALTANg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 304 ------GGTAYFVAK-SDLSTLFEDLALVRPTELCFVPRIwdmvfaeFHSEVDRRLVDGADRAALEAqvkaelrenVLGG 376
Cdd:PRK08751 274 lvfmkiGGCNHLISNpRDMPGFVKELKKTRFTAFTGVNTL-------FNGLLNTPGFDQIDFSSLKM---------TLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 377 rfvmaltGSAPISAEMTAWVEslLADVHLVEGYGSTEAG-------MVLND--GMVRRP-----AVIDYKLVDVPELGYF 442
Cdd:PRK08751 338 -------GMAVQRSVAERWKQ--VTGLTLVEAYGLTETSpaacinpLTLKEynGSIGLPipstdACIKDDAGTVLAIGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 443 GtdqpyprgELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVF 522
Cdd:PRK08751 409 G--------ELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDI-ARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 523 GDSPLVRQIfiygnsaraypLAVVVP---SGDALSRHGIENLKPVISESLQEVARaAGLQSYEIPRdfIIE 590
Cdd:PRK08751 480 AMMPGVLEV-----------AAVGVPdekSGEIVKVVIVKKDPALTAEDVKAHAR-ANLTGYKQPR--IIE 536
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
85-535 |
2.78e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.12 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALsaepaiRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIat 164
Cdd:PRK07787 25 VLSRSDLAGAATAVAERV------AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sidnLGDAVEVLAG--HAParlvvfdyhgkVDTHreaveaararlagsvtidtlaeliERGRALPATPiadsADDALALL 242
Cdd:PRK07787 97 ----LGPAPDDPAGlpHVP-----------VRLH------------------------ARSWHRYPEP----DPDAPALI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 243 IYTSGSTGAPKGAMYRESQVMS-------FWrkssGWfepsgYPSITL-NFMPMSHVGGRQV-LYGTLSNGGTAYFVAKS 313
Cdd:PRK07787 134 VYTSGTTGPPKGVVLSRRAIAAdldalaeAW----QW-----TADDVLvHGLPLFHVHGLVLgVLGPLRIGNRFVHTGRP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 DLSTLFEdlALVRPTELCF-VPRIWDMVFAEFHS----EVDRRLVDGAdrAALEAQVKAELRenvlggrfvmALTGSAPi 388
Cdd:PRK07787 205 TPEAYAQ--ALSEGGTLYFgVPTVWSRIAADPEAaralRGARLLVSGS--AALPVPVFDRLA----------ALTGHRP- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 389 saemtawveslladvhlVEGYGSTEAGMVLN---DGMvRRP-------AVIDYKLVDVPelgyfGTDQPYPR---GELLV 455
Cdd:PRK07787 270 -----------------VERYGMTETLITLStraDGE-RRPgwvglplAGVETRLVDED-----GGPVPHDGetvGELQV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 456 KTQTMFPGYYQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYL-DRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIY 534
Cdd:PRK07787 327 RGPTLFDGYLNRPDATAAAFTADGWFRTGD-VAVVDPDGMHRIvGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVV 405
|
.
gi 489508543 535 G 535
Cdd:PRK07787 406 G 406
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
85-593 |
3.21e-16 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 83.15 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELwaRAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:cd05909 7 SLTYRKL--LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 S---IDnLGDAVEVLAGHAPARLV-VFDYHGKVDThreaVEAARARLAGsvTIDTLAELIERGRAlpatpiADSADDaLA 240
Cdd:cd05909 85 SkqfIE-KLKLHHLFDVEYDARIVyLEDLRAKISK----ADKCKAFLAG--KFPPKWLLRIFGVA------PVQPDD-PA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 241 LLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQV-LYGTLSNGGTAYFVAKS-DLSTL 318
Cdd:cd05909 151 VILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVV-FGALPFFHSFGLTGcLWLPLLSGIKVVFHPNPlDYKKI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRL---VDGADRaaleaqVKAELREnvlggrfvmaltgsapisaemtAW 395
Cdd:cd05909 230 PELIYDKKATILLGTPTFLRGYARAAHPEDFSSLrlvVAGAEK------LKDTLRQ----------------------EF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLlaDVHLVEGYGSTEAGMVLN---------DGMVRRPAV-IDYKLVDVPelgyfgTDQPYPRGE---LLVKTQTMFP 462
Cdd:cd05909 282 QEKF--GIRILEGYGTTECSPVISvntpqspnkEGTVGRPLPgMEVKIVSVE------THEEVPIGEgglLLVRGPNVML 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 463 GYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSqGEFIAVSKLEAVFGDsplvrqifIYGNSARAy 541
Cdd:cd05909 354 GYLNEPELTSFAFG-DGWYDTGDI-GKIDGEGFLTItGRLSRFAKIA-GEMVSLEAIEDILSE--------ILPEDNEV- 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 542 pLAVVVPSGdalsRHG--------IENLKPvisESLQEVARAAGLQSYEIPR-DFIIETTP 593
Cdd:cd05909 422 -AVVSVPDG----RKGekivllttTTDTDP---SSLNDILKNAGISNLAKPSyIHQVEEIP 474
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
84-899 |
3.26e-16 |
|
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: 84.52 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTtidIALI---RLGAVSVPLQTSAPVTGLRpivtetepT 160
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMV---VALLavlKAGAAYVPLDPAYPAERLA--------Y 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIAtsidnlgdavevlagHAPARLVVfdyhgkvdTHREAVEAARARLAGSVTIDTLaeliERGRALPATPIADSADDALA 240
Cdd:COG1020 568 MLE---------------DAGARLVL--------TQSALAARLPELGVPVLALDAL----ALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 241 LLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGyPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFE 320
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAA 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALV---RPTELCFVPRIWDMvfaefhsevdrrLVDGADRAALeaqvkaELRENVLGGRfvmALTGSAPisaemTAWVE 397
Cdd:COG1020 700 LAELLarhRVTVLNLTPSLLRA------------LLDAAPEALP------SLRLVLVGGE---ALPPELV-----RRWRA 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 sLLADVHLVEGYGSTEA-----GMVLNDGMVRRPA-------------VIDYKLVDVPelgyfgtdqPYPRGELLVKTQT 459
Cdd:COG1020 754 -RLPGARLVNLYGPTETtvdstYYEVTPPDADGGSvpigrpiantrvyVLDAHLQPVP---------VGVPGELYIGGAG 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 460 MFPGYYQRPDVTAEVF--DPDGF-----YRTGDiMAKVGPD-QFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQ- 530
Cdd:COG1020 824 LARGYLNRPELTAERFvaDPFGFpgarlYRTGD-LARWLPDgNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREa 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 531 -IFIYGNSARAYPLAVVVPSGDALSrhgienlkpviSESLQEVARAAGLQSYEIPRDFIIETTPFTlenglLTGIRKLAR 609
Cdd:COG1020 902 vVVAREDAPGDKRLVAYVVPEAGAA-----------AAAALLRLALALLLPPYMVPAAVVLLLPLP-----LTGNGKLDR 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 610 PQLKKfygerlerlyteladsqsnELRELRQSGPDAPVLPTLCRAAAALLGSTAADVRPDAHFADLGGDSLSALSLANLL 689
Cdd:COG1020 966 LALPA-------------------PAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 690 HEIFGVDVPVGVIVSPASDLRALADHIEAARTGVRRPSFASIHGRSATEVHAS-DLTLDKFIDAATLAAAPNLPAPSAQV 768
Cdd:COG1020 1027 ARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLlALLLALLLLLALLALLALLLLLLLLL 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLALEWLDRMDLVNGKLICLVRARSDEEAQARLDATFDSGDPYLVRHYRELGAGRLEVLAGDKGEA 848
Cdd:COG1020 1107 LLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLL 1186
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 489508543 849 DLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLAL 899
Cdd:COG1020 1187 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALL 1237
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
239-595 |
3.67e-16 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 82.87 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 LALLIYTSGSTGAPKGAMYRESQVMSF-WRKSSGWFEPSgyPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLST 317
Cdd:cd17644 108 LAYVIYTSGSTGKPKGVMIEHQSLVNLsHGLIKEYGITS--SDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LFEDLALVRPTELcfvpRIWDMVFAEFHSEVDRRLVDGADraaleaqVKAELRENVLGGRFVMaltgsaPISAEMtaWVE 397
Cdd:cd17644 186 LEDFVQYIQQWQL----TVLSLPPAYWHLLVLELLLSTID-------LPSSLRLVIVGGEAVQ------PELVRQ--WQK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 SLLADVHLVEGYGSTEAGMvlnDGMVRRPAVIDYKLVDVPELG--------YF--GTDQPYP---RGELLVKTQTMFPGY 464
Cdd:cd17644 247 NVGNFIQLINVYGPTEATI---AATVCRLTQLTERNITSVPIGrpiantqvYIldENLQPVPvgvPGELHIGGVGLARGY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 465 YQRPDVTAEVFDPDGF--------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ---IF 532
Cdd:cd17644 324 LNRPELTAEKFISHPFnsseserlYKTGD-LARYLPDGNIeYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTavvIV 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 533 IYGNSARAYPLAVVVPSgdalsrhgiENLKPVISEsLQEVARAAgLQSYEIPRDFII-ETTPFT 595
Cdd:cd17644 402 REDQPGNKRLVAYIVPH---------YEESPSTVE-LRQFLKAK-LPDYMIPSAFVVlEELPLT 454
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
79-589 |
4.90e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 82.63 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 79 LLPRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapvtgLRPivtete 158
Cdd:PRK06145 21 LVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR-----LAA------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 159 ptmiatsidnlgDAVEVLAGHAPARLVVFDyhgkvdthrEAVEAARARLAGSVTIDTLAELIERGRA---LPATPIADSA 235
Cdd:PRK06145 89 ------------DEVAYILGDAGAKLLLVD---------EEFDAIVALETPKIVIDAAAQADSRRLAqggLEIPPQAAVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDALALLIYTSGSTGAPKGAMYRESQVmsFWrKSSGWFEPSGYPSIT--LNFMPMSHVGGRQVL-YGTLSNGGTAYFVAK 312
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNL--HW-KSIDHVIALGLTASErlLVVGPLYHVGAFDLPgIAVLWVGGTLRIHRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 313 SDLSTLFEDLALVRPTELCFVPRIWDMVFA-----EFHSEVDRRLVDGADRAAlEAQVKaELRENVLGGRFVMA--LTGS 385
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTvpdrdRFDLDSLAWCIGGGEKTP-ESRIR-DFTRVFTRARYIDAygLTET 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 386 APISAEMTAWVEslladvhlVEGYGSTEagmvlndgmvRRPAVIDYKLVDvpelGYFGTDQPYPRGELLVKTQTMFPGYY 465
Cdd:PRK06145 303 CSGDTLMEAGRE--------IEKIGSTG----------RALAHVEIRIAD----GAGRWLPPNMKGEICMRGPKVTKGYW 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 466 QRPDVTAEVFdPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG-NSAR--AYP 542
Cdd:PRK06145 361 KDPEKTAEAF-YGDWFRSGDV-GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGvHDDRwgERI 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489508543 543 LAVVVpsgdalsrhgienLKPVISESLQEVAR--AAGLQSYEIPRDFII 589
Cdd:PRK06145 439 TAVVV-------------LNPGATLTLEALDRhcRQRLASFKVPRQLKV 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
84-486 |
5.76e-16 |
|
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: 82.33 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPaIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSApvtglrpivTETEPtmiA 163
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPP---------TYDEP---N 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAVEVLagHAPARLvvfdyhgkvdTHREAVEAARARLAGSVT-IDTLAELIERGRALPATPIADSADDALALL 242
Cdd:cd05906 105 ARLRKLRHIWQLL--GSPVVL----------TDAELVAEFAGLETLSGLpGIRVLSIEELLDTAADHDLPQSRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 243 IYTSGSTGAPKGAMYRESQVMSFWRkSSGWFEPSGYPSITLNFMPMSHVGG------RQVLYGTLS-NGGTAYFVAKsdl 315
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRNILARSA-GKIQHNGLTPQDVFLNWVPLDHVGGlvelhlRAVYLGCQQvHVPTEEILAD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 316 STLFEDLALVRPTELCFVPRiwdmvFAefHSEVDRRLVDGADRAAleaqvkaelreNVLGGRFVMalTGSAPISAEMTAW 395
Cdd:cd05906 249 PLRWLDLIDRYRVTITWAPN-----FA--FALLNDLLEEIEDGTW-----------DLSSLRYLV--NAGEAVVAKTIRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLL------ADVhLVEGYGSTE--AGMVLNDGMVRRPAVIDYKLVDVpelgyfgtDQPYP------------------ 449
Cdd:cd05906 309 LLRLLepyglpPDA-IRPAFGMTEtcSGVIYSRSFPTYDHSQALEFVSL--------GRPIPgvsmrivddegqllpege 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 489508543 450 RGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDI 486
Cdd:cd05906 380 VGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDL 416
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
87-620 |
7.61e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 82.13 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATsI 166
Cdd:PRK12583 47 TWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC-A 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 DNL--GDAVEVLAGHAParlvvfdyhGKVDTHREAVEAAR-ARLAGSVTID--------TLAELIERGRALPATPIAD-- 233
Cdd:PRK12583 125 DAFktSDYHAMLQELLP---------GLAEGQPGALACERlPELRGVVSLApapppgflAWHELQARGETVSREALAErq 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 234 ---SADDALALLiYTSGSTGAPKGAMYRESQVMSfwrksSGWFEpsgypSITLNF---------MPMSHVGGrQVL--YG 299
Cdd:PRK12583 196 aslDRDDPINIQ-YTSGTTGFPKGATLSHHNILN-----NGYFV-----AESLGLtehdrlcvpVPLYHCFG-MVLanLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 300 TLSNGGTAYF--VAKSDLSTLfEDLALVRPTELCFVPriwDMVFAEfhsevdrrlVDGADRAALEAqvkAELRENVLGGr 377
Cdd:PRK12583 264 CMTVGACLVYpnEAFDPLATL-QAVEEERCTALYGVP---TMFIAE---------LDHPQRGNFDL---SSLRTGIMAG- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 378 fvmaltgsAPISAEMtawVESLLADVHLVE---GYGSTEAGMVL-----NDGMVRRPAVI-------DYKLVDvPELGYF 442
Cdd:PRK12583 327 --------APCPIEV---MRRVMDEMHMAEvqiAYGMTETSPVSlqttaADDLERRVETVgrtqphlEVKVVD-PDGATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 443 GTDQpypRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVF 522
Cdd:PRK12583 395 PRGE---IGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGD-LATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 523 GDSPLVRQIFIYGnsarayplavvVPSgdalSRHGIE-----NLKP---VISESLQEVARaAGLQSYEIPRDF-IIETTP 593
Cdd:PRK12583 471 FTHPAVADVQVFG-----------VPD----EKYGEEivawvRLHPghaASEEELREFCK-ARIAHFKVPRYFrFVDEFP 534
|
570 580
....*....|....*....|....*..
gi 489508543 594 FTlenglLTGirKLARPQLKKFYGERL 620
Cdd:PRK12583 535 MT-----VTG--KVQKFRMREISIEEL 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
84-624 |
1.90e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivtetePTMIA 163
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRL-IALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP------------RERLA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAVEVLAGHAPARLVVFDYHGKVdthreAVEAARARLAGSVtidtlaeliergralPATPIADSADDALALLI 243
Cdd:PRK12467 1665 YMIEDSGIELLLTQSHLQARLPLPDGLRSL-----VLDQEDDWLEGYS---------------DSNPAVNLAPQNLAYVI 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSITLnFMPMSHVGGRQVLYGTLSNGGTAYFVAKS---DLSTLFE 320
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQ-FTSFAFDVSVWELFWPLINGARLVIAPPGahrDPEQLIQ 1803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPriwdMVFAEFHSevdrrlVDGADRAALeaqvkaELRENVLGGRfvmALtgsaPISAEMTAWVEslL 400
Cdd:PRK12467 1804 LIERQQVTTLHFVP----SMLQQLLQ------MDEQVEHPL------SLRRVVCGGE---AL----EVEALRPWLER--L 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEAGMVLNDGMVRR--PAVIDYKLVDVP--ELGYFGTDQ---PYPR---GELLVKTQTMFPGYYQRPDV 470
Cdd:PRK12467 1859 PDTGLFNLYGPTETAVDVTHWTCRRkdLEGRDSVPIGQPiaNLSTYILDAslnPVPIgvaGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 471 TAEVFDPDGF-------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIY---GNSAR 539
Cdd:PRK12467 1939 TAERFVADPFgtvgsrlYRTGD-LARYRADGVIeYLGRIDHQVKI-RGFRIELGEIEARLREQGGVREAVVIaqdGANGK 2016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 540 AYpLAVVVPSGDALSRhgiENLKPVISESLQEVARAAGLQSYEIPRDFI-IETTPFTlENGlltgirKLARPQLKKFYGE 618
Cdd:PRK12467 2017 QL-VAYVVPTDPGLVD---DDEAQVALRAILKNHLKASLPEYMVPAHLVfLARMPLT-PNG------KLDRKALPAPDAS 2085
|
....*.
gi 489508543 619 RLERLY 624
Cdd:PRK12467 2086 ELQQAY 2091
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
39-501 |
2.11e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 80.80 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 39 GVALPQLIRMVMEGYADRPALgqralrfvTDPDSgrtmvellprfeTITYRELWARAGTLATALSAEpAIRPGDRVCVLG 118
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPAL--------VLGDT------------RLTYGQLADRISRYIQAFEAL-GLGTGDAVALLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 119 FNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVLAGHAPARLVVFDyHGKVDTHRE 198
Cdd:PRK06188 70 LNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVLT-LGPVPDGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 199 AVEAARArlagsvtidtlaeliergrALPATPIADSADDALALLIYTSGSTGAPKGAM--YRESQVMSFWRKSS-GWFEP 275
Cdd:PRK06188 149 LLAAAAK-------------------FGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMgtHRSIATMAQIQLAEwEWPAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 276 SGYPSITlnfmPMSHVGGRQVLyGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPriwDMVFAEF-HSEVDRRlvd 354
Cdd:PRK06188 210 PRFLMCT----PLSHAGGAFFL-PTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVP---TMIYALLdHPDLRTR--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 355 gaDRAALEaqvkaelrenvlggrfvMALTGSAPISAemtawveslladVHLVEG-----------YGSTEAGMVLN---- 419
Cdd:PRK06188 279 --DLSSLE-----------------TVYYGASPMSP------------VRLAEAierfgpifaqyYGQTEAPMVITylrk 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 420 -DGMVRRPAVID-----YKLVDVPELGyfGTDQPYPR---GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKV 490
Cdd:PRK06188 328 rDHDPDDPKRLTscgrpTPGLRVALLD--EDGREVAQgevGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGD-VARE 403
|
490
....*....|..
gi 489508543 491 GPDQFVY-LDRR 501
Cdd:PRK06188 404 DEDGFYYiVDRK 415
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
84-521 |
2.33e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 80.41 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSV---PLQTSAPV------TGLRPIV 154
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKL-GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTtanPFYTPAEIakqakaSGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 155 TETEptmiatsidnlgdAVEVLAGHAPARLVVFDyhgKVDTHREaveaararlaGSVTIDTLAELIERgrALPATPIadS 234
Cdd:PLN02246 128 TQSC-------------YVDKLKGLAEDDGVTVV---TIDDPPE----------GCLHFSELTQADEN--ELPEVEI--S 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 235 ADDALALlIYTSGSTGAPKGAMY-RESQVMSFWRKSSG-----WFEPSgypSITLNFMPMSHVGG-RQVLYGTLSNGGTA 307
Cdd:PLN02246 178 PDDVVAL-PYSSGTTGLPKGVMLtHKGLVTSVAQQVDGenpnlYFHSD---DVILCVLPMFHIYSlNSVLLCGLRVGAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 308 YFVAKSDLSTLFEDLALVRPTELCFVPRIwdmVFAEFHSEVdrrlVDGADRAALeaqvkaelrenvlggRFVMalTGSAP 387
Cdd:PLN02246 254 LIMPKFEIGALLELIQRHKVTIAPFVPPI---VLAIAKSPV----VEKYDLSSI---------------RMVL--SGAAP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 388 ISAEMTAWVESLLADVHLVEGYGSTEAGMVLND----------------GMVRRPAviDYKLVDvPELGY-FGTDQPypr 450
Cdd:PLN02246 310 LGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafakepfpvksgscGTVVRNA--ELKIVD-PETGAsLPRNQP--- 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 451 GELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAV 521
Cdd:PLN02246 384 GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEAL 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
235-599 |
2.67e-15 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 80.21 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 235 ADDALALLIYTSGSTGAPKGAMYRE---SQVMSFWRKSSGWFEPSGypsiTLNFMPMSHVGGRQVLYGTLSNGGTAYFV- 310
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHknmVNLLHFEREKTNINFSDK----VLQFATCSFDVCYQEIFSTLLSGGTLYIIr 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 311 --AKSDLSTLFEDLAlVRPTELCFVP-RIWDMVFAEFhsEVDRRLVDGADRAaleaqvkaelrenVLGGRFVMaltgsap 387
Cdd:cd17656 202 eeTKRDVEQLFDLVK-RHNIEVVFLPvAFLKFIFSER--EFINRFPTCVKHI-------------ITAGEQLV------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 388 ISAEMTAWVESllADVHLVEGYGSTEAGMVLNDGMVRRPAVIDYKLVDVPE-------LGYFGTDQPYPR-GELLVKTQT 459
Cdd:cd17656 259 ITNEFKEMLHE--HNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPIsntwiyiLDQEQQLQPQGIvGELYISGAS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 460 MFPGYYQRPDVTAEVFDPDGF------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ-- 530
Cdd:cd17656 337 VARGYLNRQELTAEKFFPDPFdpnermYRTGD-LARYLPDGNIeFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEav 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 531 IFIYGNSARAYPLAVVVPSGDALSrhgIENLKPVISESLQEvaraaglqsYEIPRDFI-IETTPFTlENG 599
Cdd:cd17656 415 VLDKADDKGEKYLCAYFVMEQELN---ISQLREYLAKQLPE---------YMIPSFFVpLDQLPLT-PNG 471
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
229-547 |
3.45e-15 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 79.88 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 229 TPIADSADDALALLIYTSGSTGAPKGAMY-RESQVMSFWRKSSGWFEPSGYPSIT-LNFMPMSHVGGRQVLYGTLSNGGT 306
Cdd:cd17642 176 KPPSFDRDEQVALIMNSSGSTGLPKGVQLtHKNIVARFSHARDPIFGNQIIPDTAiLTVIPFHHGFGMFTTLGYLICGFR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 307 AYFVAKSDLSTLFEDLALVRPTELCFVPRIwdMVFAEFHSevdrrLVDGADRAALeaqvkaelrenvlggrfVMALTGSA 386
Cdd:cd17642 256 VVLMYKFEEELFLRSLQDYKVQSALLVPTL--FAFFAKST-----LVDKYDLSNL-----------------HEIASGGA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 387 PISAEMTAWVESLLADVHLVEGYGSTE---AGMVLNDGMVRRPAV------IDYKLVDVPELGYFGTDQpypRGELLVKT 457
Cdd:cd17642 312 PLSKEVGEAVAKRFKLPGIRQGYGLTEttsAILITPEGDDKPGAVgkvvpfFYAKVVDLDTGKTLGPNE---RGELCVKG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 458 QTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIYG-- 535
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAGip 467
|
330
....*....|...
gi 489508543 536 -NSARAYPLAVVV 547
Cdd:cd17642 468 dEDAGELPAAVVV 480
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
40-552 |
3.46e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 80.02 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 40 VALPQLIRMVMEGYADRPALGQRAlrfvtdpdSGRTmvellprfetITYRELWARAGTLATALSAePAIRPGDRVCVLGF 119
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAV--------TGKA----------VTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 120 NSVDYTTIDIALIRLGAVsvplqtsapVTGLRPIVTETEptmiatsidnlgdaVEVLAGHAPARLVVFDyhgkvDTHREA 199
Cdd:PLN02330 89 NVAEYGIVALGIMAAGGV---------FSGANPTALESE--------------IKKQAEAAGAKLIVTN-----DTNYGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 200 VEA--------ARARLAGSVTIDTLAELIERGRALPATPIADSADdaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSG 271
Cdd:PLN02330 141 VKGlglpvivlGEEKIEGAVNWKELLEAADRAGDTSDNEEILQTD--LCALPFSSGTTGISKGVMLTHRNLVANLCSSLF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 272 WFEPSGYPSI-TLNFMPMSHVGG-RQVLYGTLSNGGTAYFVAKSDLSTLFEdlALVrPTELCFVPRIWDMVFAEfhseVD 349
Cdd:PLN02330 219 SVGPEMIGQVvTLGLIPFFHIYGiTGICCATLRNKGKVVVMSRFELRTFLN--ALI-TQEVSFAPIVPPIILNL----VK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 350 RRLVDGADRAALEAQVkaelrenvlggrfvmALTGSAPISAEMTAWVESLLADVHLVEGYGSTEAGMVL--------NDG 421
Cdd:PLN02330 292 NPIVEEFDLSKLKLQA---------------IMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITlthgdpekGHG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 422 MVRRPAV------IDYKLVDvPELGyfgtdQPYPR---GELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGP 492
Cdd:PLN02330 357 IAKKNSVgfilpnLEVKFID-PDTG-----RSLPKntpGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDI-GYIDD 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 493 DQFVYL-DRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIY---GNSARAYPLAVVVPSGDA 552
Cdd:PLN02330 430 DGDIFIvDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVVplpDEEAGEIPAACVVINPKA 492
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
67-258 |
2.90e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 67 VTDPDSGRTMVELlpRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAP 146
Cdd:PRK09274 25 VAVPGGRGADGKL--AYDELSFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 147 VTGLRPIVTETEPtmiatsidnlgdavEVLAGHAPARLVVFDYHGKVDTHREAVEAARARLAGSVTIDTlaelIERGRAL 226
Cdd:PRK09274 102 IKNLKQCLAEAQP--------------DAFIGIPKAHLARRLFGWGKPSVRRLVTVGGRLLWGGTTLAT----LLRDGAA 163
|
170 180 190
....*....|....*....|....*....|..
gi 489508543 227 PATPIADSADDALALLIYTSGSTGAPKGAMYR 258
Cdd:PRK09274 164 APFPMADLAPDDMAAILFTSGSTGTPKGVVYT 195
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
84-599 |
2.91e-14 |
|
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: 76.93 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTEteptmia 163
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAA-GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAD------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlGDAVEVLAGHAPARLVVFdyhgkvdthreaveaararlagsvTIDTLAELIERGRALPATPIADSADDALALLI 243
Cdd:cd12114 83 ------AGARLVLTDGPDAQLDVA------------------------VFDVLILDLDALAAPAPPPPVDVAPDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSI----TLNFmPMShvggrqV--LYGTLSNGGTAYFVA---KSD 314
Cdd:cd12114 133 FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVlalsSLSF-DLS------VydIFGALSAGATLVLPDearRRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 LSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDR----RLV-DGADRAALeaQVKAELRENVLGGRFVmALTGsapiS 389
Cdd:cd12114 206 PAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALlpslRLVlLSGDWIPL--DLPARLRALAPDARLI-SLGG----A 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 390 AEMTAWveSLLADVHLV-EGYGSTEAGMVLNDGMVRrpaVIDYKLVDVPELGyfgtdqpypRGELLVKTQTMFPGYYQRP 468
Cdd:cd12114 279 TEASIW--SIYHPIDEVpPDWRSIPYGRPLANQRYR---VLDPRGRDCPDWV---------PGELWIGGRGVALGYLGDP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 469 DVTAEVF--DPDG--FYRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ--IFIYGNSARAY 541
Cdd:cd12114 345 ELTAARFvtHPDGerLYRTGD-LGRYRPDGTLeFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKR 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 542 PLAVVVPSGDAlsrhgienlKPVISESLQEVArAAGLQSYEIPRDFI-IETTPFTLeNG 599
Cdd:cd12114 423 LAAFVVPDNDG---------TPIAPDALRAFL-AQTLPAYMIPSRVIaLEALPLTA-NG 470
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
87-486 |
3.36e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 77.10 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETE------PT 160
Cdd:PRK06087 51 TYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQakmffaPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATSidNLGDAVEVLAGHAPA--RLVVFDyhgkvdthreaveaaraRLAGSVTIDTLAELIERGRALPATPIADSadDA 238
Cdd:PRK06087 130 LFKQT--RPVDLILPLQNQLPQlqQIVGVD-----------------KLAPATSSLSLSQIIADYEPLTTAITTHG--DE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 LALLIYTSGSTGAPKGAMYRESQVMsfwrkssgwFEPSGYPSiTLN-------FM--PMSHVGGrqVLYGTLSN---GGT 306
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNIL---------ASERAYCA-RLNltwqdvfMMpaPLGHATG--FLHGVTAPfliGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 307 AYFVAKSDLSTLFEDLALVRPT-ELCFVPRIWDMVfaefhSEVDRrlvDGADRAALeaqvkaelrenvlggRFVmaLTGS 385
Cdd:PRK06087 257 SVLLDIFTPDACLALLEQQRCTcMLGATPFIYDLL-----NLLEK---QPADLSAL---------------RFF--LCGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 386 APISAEMTAwvESLLADVHLVEGYGSTEA---GMV-LNDGMVRRPAV-------IDYKLVDvpelgyfGTDQPYPRGEL- 453
Cdd:PRK06087 312 TTIPKKVAR--ECQQRGIKLLSVYGSTESsphAVVnLDDPLSRFMHTdgyaaagVEIKVVD-------EARKTLPPGCEg 382
|
410 420 430
....*....|....*....|....*....|....*
gi 489508543 454 --LVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDI 486
Cdd:PRK06087 383 eeASRGPNVFMGYLDEPELTARALDEEGWYYSGDL 417
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
63-486 |
3.39e-14 |
|
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: 76.89 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 63 ALRFVTDPDSGRtmvellprfETITYRELWARAGTLATALSAepAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLq 142
Cdd:cd05931 11 AYTFLDDEGGRE---------ETLTYAELDRRARAIAARLQA--VGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 143 tsAPVTGLRPIVTeteptmIATSIDNLGDAVeVLAGHAPARLVvfdyhgkvdtHREAVEAARARLAGSVTIDTLAElieR 222
Cdd:cd05931 79 --PPPTPGRHAER------LAAILADAGPRV-VLTTAAALAAV----------RAFAASRPAAGTPRLLVVDLLPD---T 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 223 GRALPATPIADSadDALALLIYTSGSTGAPKGAMYRESQVMS-FWRKSSGWFEPSGypSITLNFMPMSH----VGGrqvL 297
Cdd:cd05931 137 SAADWPPPSPDP--DDIAYLQYTSGSTGTPKGVVVTHRNLLAnVRQIRRAYGLDPG--DVVVSWLPLYHdmglIGG---L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 298 YGTLSNGGTAYFVAKSDlstlfedlalvrptelcFV--PRIW-----------------------DMVFAEFHSEVD--- 349
Cdd:cd05931 210 LTPLYSGGPSVLMSPAA-----------------FLrrPLRWlrlisryratisaapnfaydlcvRRVRDEDLEGLDlss 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 350 -RRLVDGADR---AALEAQVKA---------------ELRENVLggrFV-MALTGSAPISAEMTAWVESLLADVHLVEGY 409
Cdd:cd05931 273 wRVALNGAEPvrpATLRRFAEAfapfgfrpeafrpsyGLAEATL---FVsGGPPGTGPVVLRVDRDALAGRAVAVAADDP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 410 GSTE---AGMVLNDGMVRrpavidykLVDvPElgyfgTDQPYPR---GELLVKTQTMFPGYYQRPDVTAEVF------DP 477
Cdd:cd05931 350 AARElvsCGRPLPDQEVR--------IVD-PE-----TGRELPDgevGEIWVRGPSVASGYWGRPEATAETFgalaatDE 415
|
....*....
gi 489508543 478 DGFYRTGDI 486
Cdd:cd05931 416 GGWLRTGDL 424
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
35-487 |
3.80e-14 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 76.72 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 35 IDQPgvaLPQLIRMVMEGYADRPAlgqralrfVTDPDSgrtmvellprfeTITYRELWARAGTLATALSAEpAIRPGDRV 114
Cdd:COG1021 23 RGET---LGDLLRRRAERHPDRIA--------VVDGER------------RLSYAELDRRADRLAAGLLAL-GLRPGDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 115 CV-LGfNSVDYTTIDIALIRLGAVsvplqtsaPVTGL---RpivtETEPTMIATSIdnlgDAVEVLaghAPARLVVFDYH 190
Cdd:COG1021 79 VVqLP-NVAEFVIVFFALFRAGAI--------PVFALpahR----RAEISHFAEQS----EAVAYI---IPDRHRGFDYR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 191 GKVDTHREAVEAARARL----AGSVTidTLAELIERGRALPAtpiADSADDALALLIYTSGSTGAPKG-----AMYRESq 261
Cdd:COG1021 139 ALARELQAEVPSLRHVLvvgdAGEFT--SLDALLAAPADLSE---PRPDPDDVAFFQLSGGTTGLPKLiprthDDYLYS- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 262 vmsfWRKSS---GWFEPSGY----PsITLNFmPMSHVGgrqVLyGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVP 334
Cdd:COG1021 213 ----VRASAeicGLDADTVYlaalP-AAHNF-PLSSPG---VL-GVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 335 ---RIWdmvfaefhseVDRRLVDGADRAALEA-QVkaelrenvlGGrfvmaltgsAPISAEMTAWVESLLaDVHLVEGYG 410
Cdd:COG1021 283 plaLLW----------LDAAERSRYDLSSLRVlQV---------GG---------AKLSPELARRVRPAL-GCTLQQVFG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 411 STEaGMV----LND------GMVRRPAVID--YKLVDvpelgyfGTDQPYPRGE---LLVKTQTMFPGYYQRPDVTAEVF 475
Cdd:COG1021 334 MAE-GLVnytrLDDpeevilTTQGRPISPDdeVRIVD-------EDGNPVPPGEvgeLLTRGPYTIRGYYRAPEHNARAF 405
|
490
....*....|..
gi 489508543 476 DPDGFYRTGDIM 487
Cdd:COG1021 406 TPDGFYRTGDLV 417
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
220-585 |
4.13e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 76.61 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 220 IERGRALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGW-FEPSGYPSITLNFMPMSHV-GGRQVL 297
Cdd:PRK06710 190 VEKEVNTGVEVPCDPEND-LALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWlYNCKEGEEVVLGVLPFFHVyGMTAVM 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 298 YGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIW-----DMVFAEFHSEVDRRLVDGADRAALEAQVKAelrEN 372
Cdd:PRK06710 269 NLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYiallnSPLLKEYDISSIRACISGSAPLPVEVQEKF---ET 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 373 VLGGRFV--MALTGSAPISAEMTAWVESLLADVHLveGYGSTEAGMV-LNDGMVRRPAVIdyklvdvpelgyfgtdqpyp 449
Cdd:PRK06710 346 VTGGKLVegYGLTESSPVTHSNFLWEKRVPGSIGV--PWPDTEAMIMsLETGEALPPGEI-------------------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 450 rGELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVR 529
Cdd:PRK06710 404 -GEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDV-GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 530 QIFIY-------GNSARAYplaVVVPSGDALSRhgienlkpvisESLQEVARAAgLQSYEIPR 585
Cdd:PRK06710 481 EVVTIgvpdpyrGETVKAF---VVLKEGTECSE-----------EELNQFARKY-LAAYKVPK 528
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
84-507 |
5.49e-14 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 75.81 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEptmia 163
Cdd:cd17653 21 GSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSG----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlaghapARLVVFdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiADSADDaLALLI 243
Cdd:cd17653 95 ------------------ATLLLT--------------------------------------------TDSPDD-LAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWrkssgWFEP----SGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDlsTLF 319
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRGVLNYV-----SQPParldVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSD--PFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 EDLALVrpTELCFVPRIWDMVFAEFHSEVDRRLVDGadraalEAqVKAELRENVLGGRFVmaLTGSAPISAEMTAWVESL 399
Cdd:cd17653 185 HVARTV--DALMSTPSILSTLSPQDFPNLKTIFLGG------EA-VPPSLLDRWSPGRRL--YNAYGPTECTISSTMTEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LADVHLVEGYGSTEAGMVLNDGMvRRPAVIDYKlvdvpelgyfgtdqpyprGELLVKTQTMFPGYYQRPDVTAEVFDPDG 479
Cdd:cd17653 254 LPGQPVTIGKPIPNSTCYILDAD-LQPVPEGVV------------------GEICISGVQVARGYLGNPALTASKFVPDP 314
|
410 420 430
....*....|....*....|....*....|....*
gi 489508543 480 F------YRTGDiMAKVGPD-QFVYLDRRNNVLKL 507
Cdd:cd17653 315 FwpgsrmYRTGD-YGRWTEDgGLEFLGREDNQVKV 348
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
85-535 |
6.63e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.87 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWA---RAGTLATALsaepAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTM 161
Cdd:PRK08008 37 RYSYLELNEeinRTANLFYSL----GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 162 IATSIDNLG--DAVEVLAGHAPARLVVFDYHGKVDTHREAVEAARARLAgsvtidtlAELIErgralpATPIadSADDAl 239
Cdd:PRK08008 113 LVTSAQFYPmyRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQP--------ATLCY------APPL--STDDT- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 240 ALLIYTSGSTGAPKGAMYRESQVMsFWRKSSGWFEPSGYPSITLNFMPMSHVGGR-QVLYGTLSNGGTAYFVAKSDLSTL 318
Cdd:PRK08008 176 AEILFTSGTTSRPKGVVITHYNLR-FAGYYSAWQCALRDDDVYLTVMPAFHIDCQcTAAMAAFSAGATFVLLEKYSARAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVFAEFHSEVDRrlvdgadraaleaqvKAELREnVLggrFVMALTgsapiSAEMTAWVES 398
Cdd:PRK08008 255 WGQVCKYRATITECIPMMIRTLMVQPPSANDR---------------QHCLRE-VM---FYLNLS-----DQEKDAFEER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LlaDVHLVEGYGSTEA-GMVLND--GMVRRpavidYKLVDVPELGYFG-----TDQPYPR---GELLVKT---QTMFPGY 464
Cdd:PRK08008 311 F--GVRLLTSYGMTETiVGIIGDrpGDKRR-----WPSIGRPGFCYEAeirddHNRPLPAgeiGEICIKGvpgKTIFKEY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 465 YQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVY-LDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK08008 384 YLDPKATAKVLEADGWLHTGD-TGYVDEEGFFYfVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
84-585 |
7.50e-14 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 75.55 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsapvtglrpivtetePTMIA 163
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------------------PAFIN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TsidNLGDavevlaghaparlvvfdyhgkvDTHREAVEAARARLagsVTIDtlaeliergralpatpiadsaDDALALLI 243
Cdd:cd05937 63 Y---NLSG----------------------DPLIHCLKLSGSRF---VIVD---------------------PDDPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYResqvmsfWRKS--SGWFEPSGY----PSITLNFMPMSH-VGGRQVLYGTLSNGGTAYFVAKSDLS 316
Cdd:cd05937 94 YTSGTTGLPKAAAIS-------WRRTlvTSNLLSHDLnlknGDRTYTCMPLYHgTAAFLGACNCLMSGGTLALSRKFSAS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDR----RLVDGadrAALEAQVKAELREnvlggRFvmaltgSAPISAEM 392
Cdd:cd05937 167 QFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRdhkvRVAWG---NGLRPDIWERFRE-----RF------NVPEIGEF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 393 TAWVESLLA-DVHLVEGYGsteAGMVLNDGMVRR--------PAVIDYKLVDV---PELGyFGTDQPYPR-GELLV---- 455
Cdd:cd05937 233 YAATEGVFAlTNHNVGDFG---AGAIGHHGLIRRwkfenqvvLVKMDPETDDPirdPKTG-FCVRAPVGEpGEMLGrvpf 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 456 KTQTMFPGYYQRPDVTA-----EVFDP-DGFYRTGDiMAKVGPDQFVY-LDRRNNVLKLsQGEFIAVSKLEAVFGDSPLV 528
Cdd:cd05937 309 KNREAFQGYLHNEDATEsklvrDVFRKgDIYFRTGD-LLRQDADGRWYfLDRLGDTFRW-KSENVSTTEVADVLGAHPDI 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 529 RQIFIYGnsarayplaVVVPSGD----ALSRHGIENLKPVISESLQEVARAA--GLQSYEIPR 585
Cdd:cd05937 387 AEANVYG---------VKVPGHDgragCAAITLEESSAVPTEFTKSLLASLArkNLPSYAVPL 440
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-722 |
8.21e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 76.62 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 6 QRLTRRVEDLYASDAQFAA----ASPNE-AITQAIDQPGVALPQ-----LIRMVMEGYADRPALGqralrfvtdpDSGRT 75
Cdd:PRK10252 414 ERLKALIAQFAADPALLCGdvdiLLPGEyAQLAQVNATAVEIPEttlsaLVAQQAAKTPDAPALA----------DARYQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 76 MvellprfetiTYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVT 155
Cdd:PRK10252 484 F----------SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 156 ETEPTMIATSidnlgdavevlaghaparlvvfdyhgkvdthreAVEAARARLAGSVTIDTLAELIERGRAlpaTPIADSA 235
Cdd:PRK10252 553 DARPSLLITT---------------------------------ADQLPRFADVPDLTSLCYNAPLAPQGA---APLQLSQ 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDALALLIYTSGSTGAPKGAMYRESQVMS--FWRKSSgwfepsgYP-----------------SITLNFMPMShVGGRQV 296
Cdd:PRK10252 597 PHHTAYIIFTSGSTGRPKGVMVGQTAIVNrlLWMQNH-------YPltaddvvlqktpcsfdvSVWEFFWPFI-AGAKLV 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 297 LYGTLSNGGTAYfvaksdLSTLFEDLALvrpTELCFVPRIWDMVFAEFHSEvdrrlvdGADRAAleaqvkAELRENVLGG 376
Cdd:PRK10252 669 MAEPEAHRDPLA------MQQFFAEYGV---TTTHFVPSMLAAFVASLTPE-------GARQSC------ASLRQVFCSG 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 377 RfvmALTgsAPISAEMTAWVESLLADVhlvegYGSTEAGM-------------------------VLNDGMvrrpAVIDY 431
Cdd:PRK10252 727 E---ALP--ADLCREWQQLTGAPLHNL-----YGPTEAAVdvswypafgeelaavrgssvpigypVWNTGL----RILDA 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 432 KLVDVPelgyfgtdqPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGF------YRTGDiMAKVGPDQFV-YLDRRNNV 504
Cdd:PRK10252 793 RMRPVP---------PGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGD-VARWLDDGAVeYLGRSDDQ 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 505 LKLsQGEFIAVSKLEAVFGDSPLVrqifiygnsARAYPLAVVVPSGDALSRHGIENLKPVISES--------LQEvARAA 576
Cdd:PRK10252 863 LKI-RGQRIELGEIDRAMQALPDV---------EQAVTHACVINQAAATGGDARQLVGYLVSQSglpldtsaLQA-QLRE 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 577 GLQSYEIPRDFI-IETTPFTlENGLLTgiRK-LARPQLKKFYGERlerlyteladsqsnelrelrqsGPDAPVLPTLCRA 654
Cdd:PRK10252 932 RLPPHMVPVVLLqLDQLPLS-ANGKLD--RKaLPLPELKAQVPGR----------------------APKTGTETIIAAA 986
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 655 AAALLGSTAADVrpDAHFADLGGDSLSALSLANLLHEIFGVDVPVG-VIVSPA-SDLRAL--ADHIEAARTG 722
Cdd:PRK10252 987 FSSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVTPGqVMVASTvAKLATLldAEEDESRRLG 1056
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
85-508 |
1.27e-13 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 74.42 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapvtgLRPivteteptmiat 164
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPL-----LHP------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sidnlgDAVEVLAGHAPARLVVFDyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaDDALALLIY 244
Cdd:cd05919 72 ------DDYAYIARDCEARLVVTS-----------------------------------------------ADDIAYLLY 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSF---WRKSSGWFEPS--GYPSITLNFMpmshVGGRQVLYGTLSNGGTA-YFVAKSDLSTL 318
Cdd:cd05919 99 SSGTTGPPKGVMHAHRDPLLFadaMAREALGLTPGdrVFSSAKMFFG----YGLGNSLWFPLAVGASAvLNPGWPTAERV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVFAEfhsevdrrlvdgadrAALEAQVKAELRenvlggRFVMAltGSAPISAEMTAWVES 398
Cdd:cd05919 175 LATLARFRPTVLYGVPTFYANLLDS---------------CAGSPDALRSLR------LCVSA--GEALPRGLGERWMEH 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVhlVEGYGSTEAGMVLndgMVRRPAVIDY------------KLVDvpELGYfgTDQPYPRGELLVKTQTMFPGYYQ 466
Cdd:cd05919 232 FGGPI--LDGIGATEVGHIF---LSNRPGAWRLgstgrpvpgyeiRLVD--EEGH--TIPPGEEGDLLVRGPSAAVGYWN 302
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489508543 467 RPDVTAEVFDpDGFYRTGDiMAKVGPDQFV-YLDRRNNVLKLS 508
Cdd:cd05919 303 NPEKSRATFN-GGWYRTGD-KFCRDADGWYtHAGRADDMLKVG 343
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
84-589 |
1.58e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPlqtsapvtglrpivteteptmia 163
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP----------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLGDAVEVLAGHAPARLVVFdyHGKVDTHREAVEAARARLAGSVTIDT------LAELIERGRALPATPIADSADD 237
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMIC--HADFPEHAAAVRAASPDLTHVVAIGGaragldYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 238 ALaLLIYTSGSTGAPKGAMYRESQvMSF--WRKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTlSNGGTAYFVA--KS 313
Cdd:PRK07470 165 PC-WFFFTSGTTGRPKAAVLTHGQ-MAFviTNHLADLMPGTTEQDASLVVAPLSHGAGIHQLCQV-ARGAATVLLPseRF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 DLSTLFEDLALVRPTELCFVPRIWDMVFAefHSEVDR------RLVDGADRAALEAQVKAELRE--NVLGGRFVMaltgs 385
Cdd:PRK07470 242 DPAEVWALVERHRVTNLFTVPTILKMLVE--HPAVDRydhsslRYVIYAGAPMYRADQKRALAKlgKVLVQYFGL----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 386 apisAEMTAWVESLLADVHLVE----------GYGSTeaGMVLndgmvrrpAVIDYKLVDVPelgyfgtdqPYPRGELLV 455
Cdd:PRK07470 315 ----GEVTGNITVLPPALHDAEdgpdarigtcGFERT--GMEV--------QIQDDEGRELP---------PGETGEICV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 456 KTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK07470 372 IGPAVFAGYYNNPEANAKAFR-DGWFRTGDL-GHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 536 NSARAY---PLAVVVPSGDAlsrhgienlkPVISESLQE-----VARaaglqsYEIPRDFII 589
Cdd:PRK07470 450 VPDPVWgevGVAVCVARDGA----------PVDEAELLAwldgkVAR------YKLPKRFFF 495
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-505 |
1.85e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 74.34 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLgDAVEVLAGHAPARLVVFDYHGKVDTHReaveaararlagsvtIDTLAELIErgrALPATPIADSADDALalLI 243
Cdd:PRK13391 102 TSAAKL-DVARALLKQCPGVRHRLVLDGDGELEG---------------FVGYAEAVA---GLPATPIADESLGTD--ML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGaMYRE-------------SQVMSFWRKSSGwfepsgypSITLNFMPMSHVGGRQVLYGTLSNGGTAYFV 310
Cdd:PRK13391 161 YSSGTTGRPKG-IKRPlpeqppdtplpltAFLQRLWGFRSD--------MVYLSPAPLYHSAPQRAVMLVIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 311 AKSDLSTLfedLALV---RPTELCFVPRIWDMVFaEFHSEVDRRLvdgaDRAALEAQVKAelrenvlggrfvmaltgSAP 387
Cdd:PRK13391 232 EHFDAEQY---LALIeeyGVTHTQLVPTMFSRML-KLPEEVRDKY----DLSSLEVAIHA-----------------AAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 388 ----ISAEMTAWVESLladVHlvEGYGSTEAGMVL---------NDGMVRRPAVIDYKLVDvpELGyfgtdQPYPRGE-- 452
Cdd:PRK13391 287 cppqVKEQMIDWWGPI---IH--EYYAATEGLGFTacdseewlaHPGTVGRAMFGDLHILD--DDG-----AELPPGEpg 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 453 -LLVKTQTMFPgYYQRPDVTAEVFDPDGFYRT-GDImAKVGPDQFVYL-DRRNNVL 505
Cdd:PRK13391 355 tIWFEGGRPFE-YLNDPAKTAEARHPDGTWSTvGDI-GYVDEDGYLYLtDRAAFMI 408
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
84-529 |
2.48e-13 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 73.56 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapvtglrpivtetEPTmia 163
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRAL-GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL----------------DPE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlagHAPARLvvfdyhgkvdthREAVEAARARLAgsvtidtlaeLIERGRALpatpiadsaddalALLI 243
Cdd:cd17649 71 ---------------YPAERL------------RYMLEDSGAGLL----------LTHHPRQL-------------AYVI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLA 323
Cdd:cd17649 101 YTSGSTGTPKGVAVSHGPLAAHCQATAERY-GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 324 LVRP---TELCFVPRIWDMVFAEFHSEVDRRlvdgadraaleaqvKAELRENVLGGRfvmALTGSApisaemtaWVESLL 400
Cdd:cd17649 180 MVRElgvTVLDLPPAYLQQLAEEADRTGDGR--------------PPSLRLYIFGGE---ALSPEL--------LRRWLK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEA----------------GMVLNDGMV---RRPAVIDYKLVDVPelgyfgtdqPYPRGELLVKTQTMF 461
Cdd:cd17649 235 APVRLFNAYGPTEAtvtplvwkceagaaraGASMPIGRPlggRSAYILDADLNPVP---------VGVTGELYIGGEGLA 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 462 PGYYQRPDVTAEVFDPDGF-------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVR 529
Cdd:cd17649 306 RGYLGRPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALLEHPGVR 379
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
69-508 |
4.66e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 69 DPDSGRTMVELL----------PRF----ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTtidIAL--- 131
Cdd:PRK08974 18 NPDRYQSLVDMFeqavaryadqPAFinmgEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYP---IALfgi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 132 IRLGAVSV---PLQT-------------SAPV------TGLRPIVTETE-PTMIATSidnLGDAVEvlaghAPAR-LV-- 185
Cdd:PRK08974 95 LRAGMIVVnvnPLYTprelehqlndsgaKAIVivsnfaHTLEKVVFKTPvKHVILTR---MGDQLS-----TAKGtLVnf 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 186 VFDYHGKVdthreaveAARARLAGSVTidtLAELIERGRAL----PatpiaDSADDALALLIYTSGSTGAPKGAMYRESQ 261
Cdd:PRK08974 167 VVKYIKRL--------VPKYHLPDAIS---FRSALHKGRRMqyvkP-----ELVPEDLAFLQYTGGTTGVAKGAMLTHRN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 262 VMSFWRKSSGWFEP----------SGYP-----SITLNFMPMSHVGGRQVLY-------GTLSNGGTAYFVAKSDLSTLF 319
Cdd:PRK08974 231 MLANLEQAKAAYGPllhpgkelvvTALPlyhifALTVNCLLFIELGGQNLLItnprdipGFVKELKKYPFTAITGVNTLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 EdlALVRPTElcfvpriwdmvfaeFHsEVDRrlvdgadraaleaqvkAELRENVLGGrfvMALTgsapiSAEMTAWVEsl 399
Cdd:PRK08974 311 N--ALLNNEE--------------FQ-ELDF----------------SSLKLSVGGG---MAVQ-----QAVAERWVK-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 400 LADVHLVEGYGSTEAG---------MVLNDGMVRRP-AVIDYKLVDVPelgyfGTDQPY-PRGELLVKTQTMFPGYYQRP 468
Cdd:PRK08974 348 LTGQYLLEGYGLTECSplvsvnpydLDYYSGSIGLPvPSTEIKLVDDD-----GNEVPPgEPGELWVKGPQVMLGYWQRP 422
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489508543 469 DVTAEVFDpDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLS 508
Cdd:PRK08974 423 EATDEVIK-DGWLATGDI-AVMDEEGFLRIvDRKKDMILVS 461
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
219-528 |
6.22e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.13 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 219 LIERGRALPATP-----IADSADDALalLIYTSGSTGAPKGAMY-RESQVMSFWRKSSGWfEPSGYPsITLNFMPMSHVG 292
Cdd:PLN03102 165 LIQRGEPTPSLVarmfrIQDEHDPIS--LNYTSGTTADPKGVVIsHRGAYLSTLSAIIGW-EMGTCP-VYLWTLPMFHCN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 293 GRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWdmvfaefhsevdRRLVDGaDRAALEAQVKAelren 372
Cdd:PLN03102 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVF------------NILLKG-NSLDLSPRSGP----- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 373 vlggrfVMALTGSAPISAEMTAWVESLlaDVHLVEGYGSTEA-GMVL-------------NDGM--VRRPAVIDYKLVDV 436
Cdd:PLN03102 303 ------VHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEAtGPVLfcewqdewnrlpeNQQMelKARQGVSILGLADV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 437 pELGYFGTDQPYPR-----GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGE 511
Cdd:PLN03102 375 -DVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDV-GVIHPDGHVEIKDRSKDIIISGGE 451
|
330
....*....|....*..
gi 489508543 512 FIAVSKLEAVFGDSPLV 528
Cdd:PLN03102 452 NISSVEVENVLYKYPKV 468
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
87-590 |
6.86e-13 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 71.98 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapVTGLRPivteteptmiatsi 166
Cdd:cd05972 2 SFRELKRESAKAANVL-AKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL-----TTLLGP-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 dnlgDAVEVLAGHAPARLVVFDyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsADDaLALLIYTS 246
Cdd:cd05972 62 ----KDIEYRLEAAGAKAIVTD----------------------------------------------AED-PALIYFTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 247 GSTGAPKGAMYRESQVMSFWRKSSGW--FEPSGypsitlnfmpmshvggrqvLYGTLSNGGTAYFVaksdLSTLFEDLAL 324
Cdd:cd05972 91 GTTGLPKGVLHTHSYPLGHIPTAAYWlgLRPDD-------------------IHWNIADPGWAKGA----WSSFFGPWLL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 325 VRPTELC----FVPRIWDMVFAEFHSEV-------DRRLVdgadRAALEAQVKAELRENVLGGRfvmaltgsaPISAE-M 392
Cdd:cd05972 148 GATVFVYegprFDAERILELLERYGVTSfcgpptaYRMLI----KQDLSSYKFSHLRLVVSAGE---------PLNPEvI 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 393 TAWVESLLADVHlvEGYGSTEAGMVLND--GMVRRPAVIDYklvdvPELGY--FGTDQ------PYPRGELLVKTQT--M 460
Cdd:cd05972 215 EWWRAATGLPIR--DGYGQTETGLTVGNfpDMPVKPGSMGR-----PTPGYdvAIIDDdgrelpPGEEGDIAIKLPPpgL 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 461 FPGYYQRPDVTAEVFDpDGFYRTGDIMAKVGPDQFVYLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFI------- 533
Cdd:cd05972 288 FLGYVGDPEKTEASIR-GDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpv 365
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489508543 534 YGNSARAYplaVVVPSGDALSrhgienlkPVISESLQEVARAAgLQSYEIPRdfIIE 590
Cdd:cd05972 366 RGEVVKAF---VVLTSGYEPS--------EELAEELQGHVKKV-LAPYKYPR--EIE 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
84-601 |
1.16e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivTETEPTMIA 163
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP--------AERLAYMLE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSidnlgDAVEVLAGHAPARLVVFDyhgkVDTHREAVEAARARLAGSVTidtlaeliergralpATPIADSADDALALLI 243
Cdd:PRK12316 606 DS-----GVQLLLSQSHLGRKLPLA----AGVQVLDLDRPAAWLEGYSE---------------ENPGTELNPENLAYVI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKS---DLSTLFE 320
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdhrDPAKLVE 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPriwdmvfaefhSEVDRRLVDGADRAAleaqvkAELRENVLGGRfvmaltgsaPISAEMTAWVESLL 400
Cdd:PRK12316 741 LINREGVDTLHFVP-----------SMLQAFLQDEDVASC------TSLRRIVCSGE---------ALPADAQEQVFAKL 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEAGMVLNDgMVRRPAVIDYKLVDVP--ELGYFGTD---QPYP---RGELLVKTQTMFPGYYQRPDVTA 472
Cdd:PRK12316 795 PQAGLYNLYGPTEAAIDVTH-WTCVEEGGDSVPIGRPiaNLACYILDanlEPVPvgvLGELYLAGRGLARGYHGRPGLTA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 473 EVFDPDGF------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYpLAV 545
Cdd:PRK12316 874 ERFVPSPFvagermYRTGD-LARYRADGVIeYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQL-VGY 950
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489508543 546 VVPsgdalsrhgiENLKPVISESLQEvARAAGLQSYEIPRDFI-IETTPFTlENGLL 601
Cdd:PRK12316 951 VVL----------ESEGGDWREALKA-HLAASLPEYMVPAQWLaLERLPLT-PNGKL 995
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
87-595 |
1.36e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 71.66 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvpLQTSAPvtGLRPivteteptmiatsi 166
Cdd:PRK07008 41 TYRDCERRAKQLAQALAAL-GVEPGDRVGTLAWNGYRHLEAYYGVSGSGAV---CHTINP--RLFP-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 dnlgDAVEVLAGHAPARLVVFD---------YHGKVDTHREAVEAA-RARL-AGSVTIDTLAELIERGRALPATPIADsa 235
Cdd:PRK07008 101 ----EQIAYIVNHAEDRYVLFDltflplvdaLAPQCPNVKGWVAMTdAAHLpAGSTPLLCYETLVGAQDGDYDWPRFD-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDALALLIYTSGSTGAPKGAMY--RESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKS 313
Cdd:PRK07008 175 ENQASSLCYTSGTTGNPKGALYshRSTVLHAYGAALPDAMGLSARDAV-LPVVPMFHVNAWGLPYSAPLTGAKLVLPGPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 -DLSTLFEDLALVRPTELCFVPRIWDMVFAEFHsevdrrlvdgadraalEAQVK-AELRENVLGgrfvmaltGSAPISAE 391
Cdd:PRK07008 254 lDGKSLYELIEAERVTFSAGVPTVWLGLLNHMR----------------EAGLRfSTLRRTVIG--------GSACPPAM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 392 MTAWVESLlaDVHLVEGYGSTEA---GMV--LNDGMVRRPAVIDYKL----------VDVPELGYFGTDQPY---PRGEL 453
Cdd:PRK07008 310 IRTFEDEY--GVEVIHAWGMTEMsplGTLckLKWKHSQLPLDEQRKLlekqgrviygVDMKIVGDDGRELPWdgkAFGDL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 454 LVKTQTMFPGYYQRPDvtaevfDP--DGFYRTGDImAKVGPDQFVYL-DRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:PRK07008 388 QVRGPWVIDRYFRGDA------SPlvDGWFPTGDV-ATIDADGFMQItDRSKDVIK-SGGEWISSIDIENVAVAHPAVAE 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 531 ---IFIYGNSARAYPLAVVVPSGDAlsrhgienlkpviseslqEVARAAGLQSYE-------IPRDFI-IETTPFT 595
Cdd:PRK07008 460 aacIACAHPKWDERPLLVVVKRPGA------------------EVTREELLAFYEgkvakwwIPDDVVfVDAIPHT 517
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-595 |
1.38e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 71.31 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapvtglrpivtetePTMIA 163
Cdd:cd05971 5 EKVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL-----------------FALFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlGDAVEVLAGHAPARLVVfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiADSADDaLALLI 243
Cdd:cd05971 67 ------PEALEYRLSNSGASALV---------------------------------------------TDGSDD-PALII 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSfwrkssgwfepsgypsitlnfmpmsHVGGRQVLYGTLSNGGTAYFvAKSD--------- 314
Cdd:cd05971 95 YTSGTTGPPKGALHAHRVLLG-------------------------HLPGVQFPFNLFPRDGDLYW-TPADwawigglld 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 --LSTLFEDLALV--RPTElcFVP-RIWDMVfaEFHSEVDRRLVDGADRaaLEAQVKAELRENVLGGRFVMalTGSAPIS 389
Cdd:cd05971 149 vlLPSLYFGVPVLahRMTK--FDPkAALDLM--SRYGVTTAFLPPTALK--MMRQQGEQLKHAQVKLRAIA--TGGESLG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 390 AEMTAWV-ESLLADVHlvEGYGSTEAGMVLND---------GMVRRP------AVIDYKLVDVP--ELGYFGTDQPYPrg 451
Cdd:cd05971 221 EELLGWArEQFGVEVN--EFYGQTECNLVIGNcsalfpikpGSMGKPipghrvAIVDDNGTPLPpgEVGEIAVELPDP-- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 452 ellvktqTMFPGYYQRPDVTAEVFDPDgFYRTGDIMAKVGPDQFVYLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQI 531
Cdd:cd05971 297 -------VAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMA 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 532 F-------IYGNSARAYplaVVVPSGDALSRhgienlkpVISESLQEVARAAgLQSYEIPRDFI-IETTPFT 595
Cdd:cd05971 368 AvvgipdpIRGEIVKAF---VVLNPGETPSD--------ALAREIQELVKTR-LAAHEYPREIEfVNELPRT 427
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
42-534 |
3.24e-12 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 70.56 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALGQRALRFvtdpdsgrtmvellprfetiTYRELWARAGTLATALSAEpAIRPGDRVCVLGFNS 121
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVFGGTRW--------------------TYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 122 VDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLgDAVEvlagHAPARlvvfdyhgkvDTHREAVE 201
Cdd:PRK06155 82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALL-AALE----AADPG----------DLPLPAVW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 202 AARARLAGSVTID-TLAELIERGRALPATPIADSadDALALLiYTSGSTGAPKGAMYRESQvMSFWRKSSGWFEPSGYPS 280
Cdd:PRK06155 147 LLDAPASVSVPAGwSTAPLPPLDAPAPAAAVQPG--DTAAIL-YTSGTTGPSKGVCCPHAQ-FYWWGRNSAEDLEIGADD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 281 ITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRrlvDGADRAA 360
Cdd:PRK06155 223 VLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDR---AHRVRVA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 361 L----EAQVKAELREnvlggRFvmaltgsapisaemtawvesllaDVHLVEGYGSTEAGMV---------------LNDG 421
Cdd:PRK06155 300 LgpgvPAALHAAFRE-----RF-----------------------GVDLLDGYGSTETNFViavthgsqrpgsmgrLAPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 422 MVRRpaVIDYKLVDVPElgyfgtDQPyprGELLVKTQTMFP---GYYQRPDVTAEVFDpDGFYRTGDIMAKVGPDQFVYL 498
Cdd:PRK06155 352 FEAR--VVDEHDQELPD------GEP---GELLLRADEPFAfatGYFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFV 419
|
490 500 510
....*....|....*....|....*....|....*.
gi 489508543 499 DRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFIY 534
Cdd:PRK06155 420 DRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVF 454
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
771-973 |
3.26e-12 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 67.71 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 771 VLLTGATGFLGRYLALEWLDRmdlvNGKLICLVRARSDEEAQARLDATFDsgdpylvrhyrelgagrlevlagdkgEADL 850
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEK----GYEVIGLDRLTSASNTARLADLRFV--------------------------EGDL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 851 gLDRVTWQRLADTV--DLIVDPAAL----VNHVLPySQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAV---GEQIPPE 921
Cdd:pfam01370 51 -TDRDALEKLLADVrpDAVIHLAAVggvgASIEDP-EDFIEANVLGTLNLLEAARKAGVKRFLFASSSEVygdGAEIPQE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489508543 922 AFTEDADIRAISPtrriddsyangYANSKWAGEVLLREAHEQCGLPVTVFRC 973
Cdd:pfam01370 129 ETTLTGPLAPNSP-----------YAAAKLAGEWLVLAYAAAYGLRAVILRL 169
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
240-592 |
4.67e-12 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 68.83 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 240 ALLIYTSGSTGAPKGAMY-RESQVMSFWRKSSGWFEPSGyPSITLNFMPMSHVGGR-QVLYGTLSNGGTAYFVAKSDLST 317
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLaNKTFFAVPDILQKEGLNWVV-GDVTYLPLPATHIGGLwWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LFEDLALVRPTELCFVPRIWDMVFAEFHSEVdrrlvdgadraaleaQVKAELRENVLGGRFvmaltgsaPISAEMTawVE 397
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSAN---------------ATVPSLRLIGYGGSR--------AIAADVR--FI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 SLLADVHLVEGYGSTEAGMVL---------NDGMVRRP------AVIDYKLVDVPELGYfgtdqpyprGELLVKTQTMFP 462
Cdd:cd17635 138 EATGLTNTAQVYGLSETGTALclptdddsiEINAVGRPypgvdvYLAATDGIAGPSASF---------GTIWIKSPANML 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 463 GYYQRPDVTAEVFdPDGFYRTGDIMAKVgPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIY----GNSA 538
Cdd:cd17635 209 GYWNNPERTAEVL-IDGWVNTGDLGERR-EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYeisdEEFG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489508543 539 RAYPLAVVVPSGDALSRhgIENLKPVISESLQEVARAaglQSYEIPRDfiIETT 592
Cdd:cd17635 287 ELVGLAVVASAELDENA--IRALKHTIRRELEPYARP---STIVIVTD--IPRT 333
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
85-558 |
5.90e-12 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 69.81 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:TIGR03098 25 TLTYAALSERVLALASGLRGL-GLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 SIDNLGDAVEVLAG-HAPARLVVFDyhgkvdthreAVEAARARLAGSVTIDtLAELIERGRALPATPIADsadDALALLI 243
Cdd:TIGR03098 104 SSERLDLLHPALPGcHDLRTLIIVG----------DPAHASEGHPGEEPAS-WPKLLALGDADPPHPVID---SDMAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQVLYGTLSNGGTAY---FVAKSDLSTLfe 320
Cdd:TIGR03098 170 YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRL-LAVLPLSFDYGFNQLTTAFYVGATVVlhdYLLPRDVLKA-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 dLALVRPTELCFVPRIWDMVFaefhsEVDRRLVDGadraaleaqvkAELRenvlggrfVMALTGSApISAEMTAWVESLL 400
Cdd:TIGR03098 247 -LEKHGITGLAAVPPLWAQLA-----QLDWPESAA-----------PSLR--------YLTNSGGA-MPRATLSRLRSFL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEA--GMVLNDGMV-RRP-----AVIDYKLVDVPELGyfGTDQPYPRGELLVKTQTMFPGYYQRPDVTA 472
Cdd:TIGR03098 301 PNARLFLMYGLTEAfrSTYLPPEEVdRRPdsigkAIPNAEVLVLREDG--SECAPGEEGELVHRGALVAMGYWNDPEKTA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 473 EVFDP-----DGFYRT------GDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG----NS 537
Cdd:TIGR03098 379 ERFRPlppfpGELHLPelavwsGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAFGvpdpTL 457
|
490 500
....*....|....*....|.
gi 489508543 538 ARAYPLAVVVPSGDALSRHGI 558
Cdd:TIGR03098 458 GQAIVLVVTPPGGEELDRAAL 478
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
84-599 |
7.37e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.15 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATAL--SAEPAIRPgdrVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTM 161
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIdsLKLPDKSP---IIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 162 -IATSIDNLGDavevlaghaparlvvfdyhgkvdthreaveaararlaGSVTIDTLAELiERGRALPATPIADSA--DDA 238
Cdd:PRK04813 103 iIATEELPLEI-------------------------------------LGIPVITLDEL-KDIFATGNPYDFDHAvkGDD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 LALLIYTSGSTGAPKGAMYRESQVMSFwrksSGW----FEPSGYPSItLNFMP-------MShvggrqvLYGTLSNGGTA 307
Cdd:PRK04813 145 NYYIIFTSGTTGKPKGVQISHDNLVSF----TNWmledFALPEGPQF-LNQAPysfdlsvMD-------LYPTLASGGTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 308 YFVAK---SDLSTLFEDLALVR-------PT--ELCFVPRIWDmvfAEFHSEVDRRLVDGAdraALEAQVKAELREnvlg 375
Cdd:PRK04813 213 VALPKdmtANFKQLFETLPQLPinvwvstPSfaDMCLLDPSFN---EEHLPNLTHFLFCGE---ELPHKTAKKLLE---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 376 gRFvmaltgsaPisaemtawvesllaDVHLVEGYGSTEAGM----------VLND------GMVR---RPAVIDYKLVDV 436
Cdd:PRK04813 283 -RF--------P--------------SATIYNTYGPTEATVavtsieitdeMLDQykrlpiGYAKpdsPLLIIDEEGTKL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 437 PElgyfgTDQpyprGELLVKTQTMFPGYYQRPDVTAEVF-DPDG--FYRTGDImAKVGPDQFVYLDRRNNVLKLSqGEFI 513
Cdd:PRK04813 340 PD-----GEQ----GEIVISGPSVSKGYLNNPEKTAEAFfTFDGqpAYHTGDA-GYLEDGLLFYQGRIDFQIKLN-GYRI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 514 AVSKLEAVFGDSPLVRQ---IFIYGNSARAYPLAVVVPSGDALSRHGieNLKPVISESLQEVaraagLQSYEIPRDFI-I 589
Cdd:PRK04813 409 ELEEIEQNLRQSSYVESavvVPYNKDHKVQYLIAYVVPKEEDFEREF--ELTKAIKKELKER-----LMEYMIPRKFIyR 481
|
570
....*....|
gi 489508543 590 ETTPFTLeNG 599
Cdd:PRK04813 482 DSLPLTP-NG 490
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
41-273 |
7.94e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 69.52 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 41 ALPQLIRMVMEGYADRP--------ALGQRALRFvtdPDsgRTMVellpRFE--TITYRELWARAGTLATALSAEpAIRP 110
Cdd:PRK08279 17 DLPGILRGLKRTALITPdskrslgdVFEEAAARH---PD--RPAL----LFEdqSISYAELNARANRYAHWAAAR-GVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 111 GDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSapVTGLRpivteteptmIATSIdNLGDAVEVLAGHAPArlvvfdyh 190
Cdd:PRK08279 87 GDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ--QRGAV----------LAHSL-NLVDAKHLIVGEELV-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 191 gkvdthrEAVEAARARLAGSVTI-----------DTLAELIERGRALPATPIADSAD---DALALLIYTSGSTGAPKGAm 256
Cdd:PRK08279 146 -------EAFEEARADLARPPRLwvaggdtlddpEGYEDLAAAAAGAPTTNPASRSGvtaKDTAFYIYTSGTTGLPKAA- 217
|
250
....*....|....*....
gi 489508543 257 yresqVMSF--WRKSSGWF 273
Cdd:PRK08279 218 -----VMSHmrWLKAMGGF 231
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
84-507 |
1.19e-11 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 68.51 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd17655 21 QTLTYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TsidnlgdavevlaghaparlvvfdyHGKVDthreaveaarARLAGSVTIDTLAEliERGRALPATPIA-DSADDALALL 242
Cdd:cd17655 100 T-------------------------QSHLQ----------PPIAFIGLIDLLDE--DTIYHEESENLEpVSKSDDLAYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 243 IYTSGSTGAPKGAMYRESQVMSF-WrkssgWFEPSGYPSITLNFmpmshvggrqVLYGTLSnggtayFvaksDLST--LF 319
Cdd:cd17655 143 IYTSGSTGKPKGVMIEHRGVVNLvE-----WANKVIYQGEHLRV----------ALFASIS------F----DASVteIF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 EDLALvrPTELCFVPRIWDMVFAEFHSEVDRRLVDGAD--RAALEAQVKAELRENVLGGRFVMAltGSAPISAEMTAWVE 397
Cdd:cd17655 198 ASLLS--GNTLYIVRKETVLDGQALTQYIRQNRITIIDltPAHLKLLDAADDSEGLSLKHLIVG--GEALSTELAKKIIE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 SLLADVHLVEGYGSTEA---GMVLN-DGMVRRPAVI-------DYKLVDVPELGyfgtdQPYP---RGELLVKTQTMFPG 463
Cdd:cd17655 274 LFGTNPTITNAYGPTETtvdASIYQyEPETDQQVSVpigkplgNTRIYILDQYG-----RPQPvgvAGELYIGGEGVARG 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489508543 464 YYQRPDVTAEVFDPDGF------YRTGDiMAKVGPD-QFVYLDRRNNVLKL 507
Cdd:cd17655 349 YLNRPELTAEKFVDDPFvpgermYRTGD-LARWLPDgNIEFLGRIDHQVKI 398
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
85-617 |
2.54e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 67.57 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALsAEPAIRPGDRVCVLgFNSVDYTTIDI-ALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd05918 24 SLTYAELDRLSSRLAHHL-RSLGVGPGVFVPLC-FEKSKWAVVAMlAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSidnlgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpaTPiadsadDALALLI 243
Cdd:cd05918 102 TS---------------------------------------------------------------SP------SDAAYVI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAM-------------------YRESQVMSFwrkSSGWFEPSgypsItlnfmpmshvggrQVLYGTLSNG 304
Cdd:cd05918 113 FTSGSTGKPKGVViehralstsalahgralglTSESRVLQF---ASYTFDVS----I-------------LEIFTTLAAG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 305 GTAyFVAkSDlSTLFEDLALV----RPTELCFVPRiwdmvFAefhsevdrRLVDGADRAALEaqvkaelrenvlggrfVM 380
Cdd:cd05918 173 GCL-CIP-SE-EDRLNDLAGFinrlRVTWAFLTPS-----VA--------RLLDPEDVPSLR----------------TL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 381 ALTGSAPISAEMTAWVEsllaDVHLVEGYGSTEAGMvlndGMVRRPAVIDyklVDVPELGY-FGT----------DQPYP 449
Cdd:cd05918 221 VLGGEALTQSDVDTWAD----RVRLINAYGPAECTI----AATVSPVVPS---TDPRNIGRpLGAtcwvvdpdnhDRLVP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 450 R---GELLVKTQTMFPGYYQRPDVTAEVFDPDG-------------FYRTGDiMAKVGPDQ-FVYLDRRNNVLKLsQGEF 512
Cdd:cd05918 290 IgavGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsgrgrrLYRTGD-LVRYNPDGsLEYVGRKDTQVKI-RGQR 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 513 IAVSKLEAVFGDS-PLVRQ-----IFIYGNSARAYPLAVVVPSGDALSRHGIENLKPVISESLQEVARAA--GLQ----S 580
Cdd:cd05918 368 VELGEIEHHLRQSlPGAKEvvvevVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELrsKLRqrlpS 447
|
570 580 590
....*....|....*....|....*....|....*...
gi 489508543 581 YEIPRDFI-IETTPFTlenglLTGirKLARPQLKKFYG 617
Cdd:cd05918 448 YMVPSVFLpLSHLPLT-----ASG--KIDRRALRELAE 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
86-528 |
3.56e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 66.77 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTS-APvtglrpivteteptmiat 164
Cdd:cd05973 1 LTFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAfGP------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sidnlgDAVEVLAGHAPARLVVFDyhgkvdthreavEAARARLagsvtidtlaeliergralpatpiadsaDDALALLIY 244
Cdd:cd05973 62 ------KAIEHRLRTSGARLVVTD------------AANRHKL----------------------------DSDPFVMMF 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMSFwrkssgwfepSGYPSITLNFMPMShvggrqvLYGTLSNGGTAYFVAKSDLSTLfedlAL 324
Cdd:cd05973 96 TSGTTGLPKGVPVPLRALAAF----------GAYLRDAVDLRPED-------SFWNAADPGWAYGLYYAITGPL----AL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 325 VRPTELC----FVPRIWDMVfaEFHSEVDRRLVDGADRAALEAQVKAELRenvLGGRFVMALTGSAPISAEMTAWVESLL 400
Cdd:cd05973 155 GHPTILLeggfSVESTWRVI--ERLGVTNLAGSPTAYRLLMAAGAEVPAR---PKGRLRRVSSAGEPLTPEVIRWFDAAL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 -ADVHlvEGYGSTEAGMVLND-------------GMV---RRPAVIDYKLVDVP--ELGYFGTDQpyPRGELLvktqtMF 461
Cdd:cd05973 230 gVPIH--DHYGQTELGMVLANhhalehpvhagsaGRAmpgWRVAVLDDDGDELGpgEPGRLAIDI--ANSPLM-----WF 300
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 462 PGYYQRPDVTAEvfdpDGFYRTGDImAKVGPD-QFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSPLV 528
Cdd:cd05973 301 RGYQLPDTPAID----GGYYLTGDT-VEFDPDgSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAV 362
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
84-535 |
5.21e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 66.55 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAV---------SVPLQTSAPVTGLRPIV 154
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPvaflntnirSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 155 TETEptmiatsidnLGDAV-EVLAGHAPARLVVFdYHGKvDTHREAVEAARARLAGSVtidtlaelierGRALPATPIAD 233
Cdd:cd05938 84 VAPE----------LQEAVeEVLPALRADGVSVW-YLSH-TSNTEGVISLLDKVDAAS-----------DEPVPASLRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 234 SADDALALLIYTSGSTGAPKGAMYRESQVMSfwrkSSGWFEPSGYPS-----ITLnfmPMSHVGGRQV-LYGTLSNGGTa 307
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHLRVLQ----CSGFLSLCGVTAddviyITL---PLYHSSGFLLgIGGCIELGAT- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 308 yFVAKSDLSTlfedlalvrptelcfvPRIWD-------MVFaEFHSEVDRRLVDgadraalEAQVKAELRENVLggrfvM 380
Cdd:cd05938 213 -CVLKPKFSA----------------SQFWDdcrkhnvTVI-QYIGELLRYLCN-------QPQSPNDRDHKVR-----L 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 381 ALtGSApISAEMtaWVESL--LADVHLVEGYGSTEAGMVLND-----GMVRRPAVIdYKLVDVPELGYFGTDQ------- 446
Cdd:cd05938 263 AI-GNG-LRADV--WREFLrrFGPIRIREFYGSTEGNIGFFNytgkiGAVGRVSYL-YKLLFPFELIKFDVEKeepvrda 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 447 -----PYPRGE--LLV---KTQTMFPGYYQRPDVT-----AEVFDP-DGFYRTGDIMAkVGPDQFVYL-DRRNNVLKLsQ 509
Cdd:cd05938 338 qgfciPVAKGEpgLLVakiTQQSPFLGYAGDKEQTekkllRDVFKKgDVYFNTGDLLV-QDQQNFLYFhDRVGDTFRW-K 415
|
490 500
....*....|....*....|....*.
gi 489508543 510 GEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:cd05938 416 GENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
87-612 |
6.77e-11 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 66.20 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsaPVTGLrpivtetePTMIATSI 166
Cdd:cd05920 42 TYRELDRRADRLAAGL-RGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--------PVLAL--------PSHRRSEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 DNLGDAVEvlaghaPARLVVFDYHGKVDTHREAVEAARarlagsvtidtlaeliergralpatpiaDSADDALALLiyTS 246
Cdd:cd05920 105 SAFCAHAE------AVAYIVPDRHAGFDHRALARELAE----------------------------SIPEVALFLL--SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 247 GSTGAPKgAMYRESQVMSFWRKSSG---WFEPSgypSITLNFMPMSH---VGGRQVLyGTLSNGGTAYFVAKSDLSTLFE 320
Cdd:cd05920 149 GTTGTPK-LIPRTHNDYAYNVRASAevcGLDQD---TVYLAVLPAAHnfpLACPGVL-GTLLAGGRVVLAPDPSPDAAFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVP---RIWdmvfaefhseVDRRLVDGADRAALEA-QVkaelrenvlggrfvmaltGSAPISAEMTAWV 396
Cdd:cd05920 224 LIEREGVTVTALVPalvSLW----------LDAAASRRADLSSLRLlQV------------------GGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 397 ESLLaDVHLVEGYGSTEaGMV----LND------GMVRRPA-------VIDYKLVDVPelgyfgtdqPYPRGELLVKTQT 459
Cdd:cd05920 276 PPVL-GCTLQQVFGMAE-GLLnytrLDDpdeviiHTQGRPMspddeirVVDEEGNPVP---------PGEEGELLTRGPY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 460 MFPGYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIfiygnSAR 539
Cdd:cd05920 345 TIRGYYRAPEHNARAFTPDGFYRTGDL-VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDA-----AVV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 540 AYP--------LAVVVPSGDALSrhgienlkpviSESLQEVARAAGLQSYEIPRDFI-IETTPftlenglLTGIRKLARP 610
Cdd:cd05920 419 AMPdellgersCAFVVLRDPPPS-----------AAQLRRFLRERGLAAYKLPDRIEfVDSLP-------LTAVGKIDKK 480
|
..
gi 489508543 611 QL 612
Cdd:cd05920 481 AL 482
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
84-502 |
9.19e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.70 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDnLGDAVEVLAGHAPArlvvfdyhgkvdthreaveAARARLAGSVTIDTLAELIERGRALPATPIADSAddALALLI 243
Cdd:PRK08276 89 VSAA-LADTAAELAAELPA-------------------GVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET--AGADML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKG----AMYRESQVMSFWRKSSGWFEPSGYP-SITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLStl 318
Cdd:PRK08276 147 YSSGTTGRPKGikrpLPGLDPDEAPGMMLALLGFGMYGGPdSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAE-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 fEDLALV---RPTELCFVPriwdmvfAEFHsevdrRLVdgadraALEAQVKAelRENVLGGRFVMalTGSAP----ISAE 391
Cdd:PRK08276 225 -EALALIeryRVTHSQLVP-------TMFV-----RML------KLPEEVRA--RYDVSSLRVAI--HAAAPcpveVKRA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 392 MTAWveslLADVhLVEGYGSTEAGMVL---------NDGMVRRPAVIDYKLVDvpelgyfGTDQPYPRGEL-LVKTQTMF 461
Cdd:PRK08276 282 MIDW----WGPI-IHEYYASSEGGGVTvitsedwlaHPGSVGKAVLGEVRILD-------EDGNELPPGEIgTVYFEMDG 349
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489508543 462 PG--YYQRPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYL-DRRN 502
Cdd:PRK08276 350 YPfeYHNDPEKTAAARNPHGWVTVGD-VGYLDEDGYLYLtDRKS 392
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
81-577 |
1.07e-10 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 65.68 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 81 PRFETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsapvtgLRPIVTETEPT 160
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAV------------HSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATSIDNLGDAVEVLA--GHAPARLVvfDYHGKVDthrEAVEAARARLAGSVTIDTLA--------------ELIErgR 224
Cdd:cd17634 147 AVAGRIIDSSSRLLITAdgGVRAGRSV--PLKKNVD---DALNPNVTSVEHVIVLKRTGsdidwqegrdlwwrDLIA--K 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 225 ALPA-TPIADSADDALaLLIYTSGSTGAPKGAMY-------RESQVMS-----------FWRKSSGWFepsgypsitlnf 285
Cdd:cd17634 220 ASPEhQPEAMNAEDPL-FILYTSGTTGKPKGVLHttggylvYAATTMKyvfdygpgdiyWCTADVGWV------------ 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 286 mpmshVGGRQVLYGTLSNGGTayfvaksdlSTLFEDlALVRPTElcfvPRIWDMV-----FAEFHSEVDRRLVDGADRAA 360
Cdd:cd17634 287 -----TGHSYLLYGPLACGAT---------TLLYEG-VPNWPTP----ARMWQVVdkhgvNILYTAPTAIRALMAAGDDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 361 LEAQVKAELRenVLGGrfvmalTGSaPISAEMTAWVESLLADVH--LVEGYGSTEAG--MVLNdgmvrRPAVIDYKL--V 434
Cdd:cd17634 348 IEGTDRSSLR--ILGS------VGE-PINPEAYEWYWKKIGKEKcpVVDTWWQTETGgfMITP-----LPGAIELKAgsA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 435 DVPELGYFGT-----DQPYPRGEL--LVKTQTMFP---GYYQRPDVTAEVF--DPDGFYRTGDiMAKVGPDQFVY-LDRR 501
Cdd:cd17634 414 TRPVFGVQPAvvdneGHPQPGGTEgnLVITDPWPGqtrTLFGDHERFEQTYfsTFKGMYFSGD-GARRDEDGYYWiTGRS 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 502 NNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYGnsaRAYPLAVVVPSGDALSRHGIENLKPVISESLQEVARAAG 577
Cdd:cd17634 493 DDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG---IPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIG 564
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
84-530 |
1.18e-10 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 65.18 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVtglrpivteteptmia 163
Cdd:cd17650 11 RQLTYRELNERANQLARTL-RGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA---------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgDAVEVLAGHAPARLVVFDyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaDDALALLI 243
Cdd:cd17650 74 -------ERLQYMLEDSGAKLLLTQ-----------------------------------------------PEDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAM--YRESQVMSF-WRKSsgwFEPSGYPSITLNFMPMSHvggrQVLYG----TLSNGGTAYFV---AKS 313
Cdd:cd17650 100 YTSGTTGKPKGVMveHRNVAHAAHaWRRE---YELDSFPVRLLQMASFSF----DVFAGdfarSLLNGGTLVICpdeVKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 DLSTLFEDLALVRPTELCFVPRIWDMVFAefhsEVDRRLVDGADRAALeaqvkaelrenvlggrfvmaLTGSAPISAEMT 393
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMA----YVYRNGLDLSAMRLL--------------------IVGSDGCKAQDF 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 394 AW-VESLLADVHLVEGYGSTEAGM---VLNDGMVRRPAV----IDYKLVDVPELGYFGTDQPYP---RGELLVKTQTMFP 462
Cdd:cd17650 229 KTlAARFGQGMRIINSYGVTEATIdstYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPvgvAGELYIGGAGVAR 308
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 463 GYYQRPDVTAEVFDPDGF------YRTGDiMAKVGPD-QFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:cd17650 309 GYLNRPELTAERFVENPFapgermYRTGD-LARWRADgNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDE 381
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
86-534 |
1.24e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.41 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEPAIRpGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivtetePTMIAtS 165
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSR-GSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP------------IAAIE-R 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 IDNLGDAVEVLaghaPARlvvfdyHGKVDTHR-EAVEAARARLAGSVTIDTLAELIERGRALPATPIADSADDALALlIY 244
Cdd:PRK05857 108 FCQITDPAAAL----VAP------GSKMASSAvPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAM-IF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 245 TSGSTGAPKGAMYRESQVMS----FWRKSSGWFEPSGYPSiTLNFMPMSHVGGRQVLYGTLSNGGTAyFVAKSDLSTLFE 320
Cdd:PRK05857 177 TSGTTGEPKAVLLANRTFFAvpdiLQKEGLNWVTWVVGET-TYSPLPATHIGGLWWILTCLMHGGLC-VTGGENTTSLLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPRIWDMVFAEFHSEvdrrlvdGADRAALeaqvkaelrenvlggRFVmALTGSAPISAEMTaWVESll 400
Cdd:PRK05857 255 ILTTNAVATTCLVPTLLSKLVSELKSA-------NATVPSL---------------RLV-GYGGSRAIAADVR-FIEA-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEAGMV-------------LNDGMVRRPavidYKLVDV---PELG----YFGTDQPYPRGELLVKTQTM 460
Cdd:PRK05857 309 TGVRTAQVYGLSETGCTalclptddgsivkIEAGAVGRP----YPGVDVylaATDGigptAPGAGPSASFGTLWIKSPAN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 461 FPGYYQRPDVTAEVFdPDGFYRTGDIMAKvGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIY 534
Cdd:PRK05857 385 MLGYWNNPERTAEVL-IDGWVNTGDLLER-REDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY 456
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
86-486 |
2.53e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 64.66 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSV---PLQTSAPV------TGLRPIVTe 156
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTPRELehqlkdSGAEAIVV- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 157 teptmiatsIDNLGDAVEVLAGHAPARLVVF----DYHG--------KVDTHREAVEAARarLAGSVTI-DTLAElierG 223
Cdd:PRK07059 127 ---------LENFATTVQQVLAKTAVKHVVVasmgDLLGfkghivnfVVRRVKKMVPAWS--LPGHVRFnDALAE----G 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 224 RALPATPIADSADDaLALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEP--SGYPSI-TLNFM---PMSHVGGRQVL 297
Cdd:PRK07059 192 ARQTFKPVKLGPDD-VAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPafEKKPRPdQLNFVcalPLYHIFALTVC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 298 Y-GTLSNGGTAYFVAKS-DLSTLFEDLALVRPTelCFvPRIWDMVFAEFHSEvDRRLVDgadraaleaqvKAELRENVLG 375
Cdd:PRK07059 271 GlLGMRTGGRNILIPNPrDIPGFIKELKKYQVH--IF-PAVNTLYNALLNNP-DFDKLD-----------FSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 376 GrfvMALtgSAPIsAEmtAWVEslLADVHLVEGYGSTEAGMVLN---------DGMVRRP------AVIDYKLVDVPeLG 440
Cdd:PRK07059 336 G---MAV--QRPV-AE--RWLE--MTGCPITEGYGLSETSPVATcnpvdatefSGTIGLPlpstevSIRDDDGNDLP-LG 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489508543 441 yfgtdQPyprGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDI 486
Cdd:PRK07059 405 -----EP---GEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDV 442
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
86-535 |
6.55e-10 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 63.28 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPlqtsAPVT-GLRPIVTETEPT---- 160
Cdd:cd05970 48 FTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP----ATHQlTAKDIVYRIESAdikm 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 161 MIATSIDNLGDAVEVLAGHAPARLVVFDYHGKVdthREAVEAARArlagsvTIDTLAELIERgralPATPIADSADDaLA 240
Cdd:cd05970 123 IVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPV---PEGWIDFRK------LIKNASPDFER----PTANSYPCGED-IL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 241 LLIYTSGSTGAPKGA----MYRESQVM--SFWRKssgwFEPSGYpsitlnFMPMSHVGGRQVLYGTLSN---GGTAYFV- 310
Cdd:cd05970 189 LVYFSSGTTGMPKMVehdfTYPLGHIVtaKYWQN----VREGGL------HLTVADTGWGKAVWGKIYGqwiAGAAVFVy 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 311 --AKSDLSTLFEDLALVRPTELCFVPRIWdmvfaefhsevdRRLVdgadRAALEAQVKAELRENVLGGRfvmaltgsaPI 388
Cdd:cd05970 259 dyDKFDPKALLEKLSKYGVTTFCAPPTIY------------RFLI----REDLSRYDLSSLRYCTTAGE---------AL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 389 SAEM-TAWVEslLADVHLVEGYGSTE--------AGMVLNDGMVRRPA------VIDY--KLVDVPELG--YFGTDQPYP 449
Cdd:cd05970 314 NPEVfNTFKE--KTGIKLMEGFGQTEttltiatfPWMEPKPGSMGKPApgyeidLIDRegRSCEAGEEGeiVIRTSKGKP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 450 RGellvktqtMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFV-YLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLV 528
Cdd:cd05970 392 VG--------LFGGYYKDAEKTAEVWH-DGYYHTGD-AAWMDEDGYLwFVGRTDDLIK-SSGYRIGPFEVESALIQHPAV 460
|
....*..
gi 489508543 529 RQIFIYG 535
Cdd:cd05970 461 LECAVTG 467
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-553 |
8.76e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 62.33 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPvtglrpivteteptmia 163
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdavevlaghaPARLvvfdyhgkvdthREAVEAARARLAgsvtidtlaeliergralpatpIADSadDALALLI 243
Cdd:cd12115 85 -----------------PERL------------RFILEDAQARLV----------------------LTDP--DDLAYVI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFePSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVakSDLSTLFEDLA 323
Cdd:cd12115 112 YTSGSTGRPKGVAIEHRNAAAFLQWAAAAF-SAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 324 LVRPTELCFVPriwdmvfaefhsevdrrlvdGADRAALEAQ-VKAELRenvlggrfVMALTGSaPISAEMTAWVESLLAD 402
Cdd:cd12115 189 AAEVTLINTVP--------------------SAAAELLRHDaLPASVR--------VVNLAGE-PLPRDLVQRLYARLQV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 403 VHLVEGYGSTEA-----GMVLNDGMVRRPAV---IDYKLVDVpeLGYFGtdQPYP---RGELLVKTQTMFPGYYQRPDVT 471
Cdd:cd12115 240 ERVVNLYGPSEDttystVAPVPPGASGEVSIgrpLANTQAYV--LDRAL--QPVPlgvPGELYIGGAGVARGYLGRPGLT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 472 AEVFDPDGF------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQifiygnsarayplAV 545
Cdd:cd12115 316 AERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVRE-------------AV 381
|
....*...
gi 489508543 546 VVPSGDAL 553
Cdd:cd12115 382 VVAIGDAA 389
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
87-613 |
1.32e-09 |
|
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme family (pfam00501). Members activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate; many are involved in synthesis of siderophores such as enterobactin, vibriobactin, vulnibactin, etc. The most closely related proteine believed to differ in function activates salicylate rather than DHB. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 274063 [Multi-domain] Cd Length: 526 Bit Score: 62.12 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATS- 165
Cdd:TIGR02275 50 SYRELDQRADNLAAGL-TKLGIKQGDTAVVQLPNIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDr 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 ----IDNLGDAVEVLAGHAPARLVVFDyhGKVDTHREAVEaararlagsvtIDTLAEliergrALPATPiadSADDALAL 241
Cdd:TIGR02275 129 ahslFDYDDFARQLQSKLPTLRNIIVA--GQTGEAELFLW-----------LESPAE------PVKFPP---TKSDEVAF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LIYTSGSTGAPKGAMYRESQVMSFWRKSSG--WFEPSGYPSITL----NFmPMSHVGGRQVLYGtlsnGGTAyfVAKSDL 315
Cdd:TIGR02275 187 FQLSGGSTGTPKLIPRTHNDYYYSVRRSVEicWLTQQTRYLCALpaahNY-PLSSPGALGVFYA----GGCV--VLAPDP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 316 StlfedlalvrPTeLCFvPRIwdmvfaEFHSEVDRRLVDGAdrAALEAQVKAELRENVLGGRFVMalTGSAPISAEMTAW 395
Cdd:TIGR02275 260 S----------PT-DCF-PLI------ERHKVTVTALVPPA--VALWMQAASKSRADLSSLKLLQ--VGGAKFSAAAARR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESLLAdVHLVEGYGSTEaGMV----LNDGMVR------RPAVIDYKLVDVPELGyfgtdQPYPRGE---LLVKTQTMFP 462
Cdd:TIGR02275 318 VPAVFG-CQLQQVFGMAE-GLVnytrLDDPAEIifttqgRPMSPDDEVRVVDDHG-----NPVAPGEtgmLLTRGPYTFR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 463 GYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQ---IFIYGNSAR 539
Cdd:TIGR02275 391 GYYKAPEHNAAAFDAEGFYYTGDL-VRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDaalVSMPDELLG 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 540 AYPLAVVVPSGdalsrhgiENLKPViseSLQEVARAAGLQSYEIPRDF-IIETTPftlenglLTGIRKLARPQLK 613
Cdd:TIGR02275 470 EKSCAFIVVRD--------PALKAA---QLRRFLRERGLAEYKLPDRVeFVDSLP-------LTAVGKVDKKALR 526
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
16-498 |
1.33e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 62.28 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 16 YASDAQFAAAspnEAITQAIDQPGVALPQLIRMVMEGYADRPALgqralRFVTDPDSGRtmvellpRFETITYRELWARA 95
Cdd:PRK07529 4 FATLADIEAI---EAVPLAARDLPASTYELLSRAAARHPDAPAL-----SFLLDADPLD-------RPETWTYAELLADV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 96 GTLATALSAEpAIRPGDRVCVLGFNsvdytTIDIALIRLGAvsvplQTSAPVTGLRPIVtetEPTMIATSIDNLG----- 170
Cdd:PRK07529 69 TRTANLLHSL-GVGPGDVVAFLLPN-----LPETHFALWGG-----EAAGIANPINPLL---EPEQIAELLRAAGakvlv 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 171 -----------DAVEVLAGHAPA--RLVVFDYHGKVDTHREAVEAARARLAGSVTIDTLAELIERG--RALPATPIadSA 235
Cdd:PRK07529 135 tlgpfpgtdiwQKVAEVLAALPElrTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPgdRLFSGRPI--GP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDaLALLIYTSGSTGAPKGAMYRES-QVMSFWRKSSGWFEPSGypSITLNFMPMSHVGGrqvLYGTLsnggtayfvaksd 314
Cdd:PRK07529 213 DD-VAAYFHTGGTTGMPKLAQHTHGnEVANAWLGALLLGLGPG--DTVFCGLPLFHVNA---LLVTG------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 LSTLFEDLALVRPTELCF-----VPRIWDMVFA---EFHSEVD-------RRLVDGADRAALEAqvkaelrenvlggrfv 379
Cdd:PRK07529 274 LAPLARGAHVVLATPQGYrgpgvIANFWKIVERyriNFLSGVPtvyaallQVPVDGHDISSLRY---------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 380 mALTGSAPISAEMTAWVESLLAdVHLVEGYGSTEAGMV--LN--DGmVRRPAVI-------DYKLVDVPELGYFGTDQPY 448
Cdd:PRK07529 338 -ALCGAAPLPVEVFRRFEAATG-VRIVEGYGLTEATCVssVNppDG-ERRIGSVglrlpyqRVRVVILDDAGRYLRDCAV 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489508543 449 PR-GELLVKTQTMFPGYYQrPDVTAEVFDPDGFYRTGDiMAKVGPDQFVYL 498
Cdd:PRK07529 415 DEvGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGD-LGRIDADGYFWL 463
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
87-535 |
1.75e-09 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 61.36 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtsapvtglrpivteteptmiatsi 166
Cdd:cd05969 2 TFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 dnlgdavevlaghaparlvvFDYHGKvDTHREAVEAARARLAgsVTIDTLAEliergRALPATPiadsaddalALLIYTS 246
Cdd:cd05969 56 --------------------FSAFGP-EAIRDRLENSEAKVL--ITTEELYE-----RTDPEDP---------TLLHYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 247 GSTGAPKGAMYRESQVMSFWRKSS-----------------GWFEPSGYPSIT--LNFMPMSHVGGR---QVLYGTL-SN 303
Cdd:cd05969 99 GTTGTPKGVLHVHDAMIFYYFTGKyvldlhpddiywctadpGWVTGTVYGIWApwLNGVTNVVYEGRfdaESWYGIIeRV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 304 GGTAYFVAksdlstlfedlalvrPTELcfvpriwdmvfaefhsevdrRLVDGADRAALEAQVKAELRenvlggrfvMALT 383
Cdd:cd05969 179 KVTVWYTA---------------PTAI--------------------RMLMKEGDELARKYDLSSLR---------FIHS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 384 GSAPISAEMTAWVESLLaDVHLVEGYGSTEAG--MVLN-------DGMVRRP------AVIDYKLVDVPelgyfgtdqPY 448
Cdd:cd05969 215 VGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGsiMIANypcmpikPGSMGKPlpgvkaAVVDENGNELP---------PG 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 449 PRGELLVKTQ--TMFPGYYQRPDVTAEVFdPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSqGEFIAVSKLEAVFGDSP 526
Cdd:cd05969 285 TKGILALKPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHP 362
|
....*....
gi 489508543 527 LVRQIFIYG 535
Cdd:cd05969 363 AVAEAGVIG 371
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
90-535 |
1.95e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 61.64 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 90 ELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNL 169
Cdd:PRK12406 16 ELAQRAARAAGGLAAL-GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 170 gdavEVLAGHAPARLVVFdyhgKVDTHREAVEAAR----ARLAGSVTIDtLAELIERGRALPATPIADSADdalalLIYT 245
Cdd:PRK12406 95 ----HGLASALPAGVTVL----SVPTPPEIAAAYRispaLLTPPAGAID-WEGWLAQQEPYDGPPVPQPQS-----MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 246 SGSTGAPKGAMYR-----ESQVMSFWRKSSGWFEPsgyPSITLNFMPMSHVGGRQvlYGTLSN--GGTAYFVAKSDLSTL 318
Cdd:PRK12406 161 SGTTGHPKGVRRAaptpeQAAAAEQMRALIYGLKP---GIRALLTGPLYHSAPNA--YGLRAGrlGGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIwdmvfaeFHsevdrRLVDgadraaLEAQVKAelRENVLGGRFVmaLTGSAPISAE----MTA 394
Cdd:PRK12406 236 LQLIERHRITHMHMVPTM-------FI-----RLLK------LPEEVRA--KYDVSSLRHV--IHAAAPCPADvkraMIE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 395 WVESLladvhLVEGYGSTEAGMVL---NDGMVRRPAVIDyKLVDVPELGYFGTD-QPYPR---GELLVKTQTM--FPgYY 465
Cdd:PRK12406 294 WWGPV-----IYEYYGSTESGAVTfatSEDALSHPGTVG-KAAPGAELRFVDEDgRPLPQgeiGEIYSRIAGNpdFT-YH 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 466 QRPDVTAEVfDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLkLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK12406 367 NKPEKRAEI-DRGGFITSGDV-GYLDADGYLFLcDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFG 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
72-253 |
4.13e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.39 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 72 SGRTMVELLPRFET-ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGL 150
Cdd:PRK07768 15 SPRGMVTGEPDAPVrHTWGEVHERARRIAGGLAAA-GVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 151 RPIVTETE--PTMIATSIDNLGD----AVEVLAGHAparlvvfdyhgkvdthreaveaararlagsVTIDTLAELIErgr 224
Cdd:PRK07768 94 AVWAEDTLrvIGMIGAKAVVVGEpflaAAPVLEEKG------------------------------IRVLTVADLLA--- 140
|
170 180
....*....|....*....|....*....
gi 489508543 225 ALPATPIaDSADDALALLIYTSGSTGAPK 253
Cdd:PRK07768 141 ADPIDPV-ETGEDDLALMQLTSGSTGSPK 168
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
242-486 |
9.29e-09 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 58.67 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 242 LIYTSGSTGAPKGAMYRESQVMSF---WRKSSGWFEPSGYPSITlnfmPMSHVGGRQV-LYGTLSNGGTAYFVAKSDLST 317
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAaaaWADCADLTEDDRYLIIN----PFFHTFGYKAgIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 318 LFEDLALVRPTELCFVPRIwdmvfaeFHSEVDRRLVDGADRAALEAqvkaelrenvlggrfvmALTGSAPISAEMTAWVE 397
Cdd:cd17638 81 ILEAIERERITVLPGPPTL-------FQSLLDHPGRKKFDLSSLRA-----------------AVTGAATVPVELVRRMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 398 SLLADVHLVEGYGSTEAGMVlndgMVRRPAvidyklvDVPELGYFGTDQPYP--------RGELLVKTQTMFPGYYQRPD 469
Cdd:cd17638 137 SELGFETVLTAYGLTEAGVA----TMCRPG-------DDAETVATTCGRACPgfevriadDGEVLVRGYNVMQGYLDDPE 205
|
250
....*....|....*..
gi 489508543 470 VTAEVFDPDGFYRTGDI 486
Cdd:cd17638 206 ATAEAIDADGWLHTGDV 222
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
84-262 |
1.17e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 59.13 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQtsapvtgLRpiVTETEptmia 163
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN-------YR--YVEDE----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnlgdaVEVLAGHAPARLVVFDyhgkvDTHREAVEAARARLAGsvtIDTLAElIERGRALPATPIADSADDALA--- 240
Cdd:PRK07798 92 ---------LRYLLDDSDAVALVYE-----REFAPRVAEVLPRLPK---LRTLVV-VEDGSGNDLLPGAVDYEDALAags 153
|
170 180 190
....*....|....*....|....*....|....*
gi 489508543 241 -------------LLIYTSGSTGAPKGAMYRESQV 262
Cdd:PRK07798 154 perdfgerspddlYLLYTGGTTGMPKGVMWRQEDI 188
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
770-1054 |
1.58e-08 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 58.81 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRMDlvNGKLICLVRARSdeeaQARLDAtfdsgdpylvrHYRELGAGRLEVLAGDKGEAD 849
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDRRR--EATVHVLVRRQS----LSRLEA-----------LAAYWGADRVVPLVGDLTEPG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 LGLDRVTWQRLADtVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEaFTEDADI 929
Cdd:PRK07201 65 LGLSEADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVAGDYEGV-FREDDFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 930 RAisptrridDSYANGYANSKWAGEVLLReahEQCGLPVTVFRCDMILADtSYTGQLN-----------------LPDMF 992
Cdd:PRK07201 143 EG--------QGLPTPYHRTKFEAEKLVR---EECGLPWRVYRPAVVVGD-SRTGEMDkidgpyyffkvlaklakLPSWL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 993 TRLMLSLAATGIapgsfyeldahgnrqrahydgLPVEFVAEAICTLgTHSPDR-FVTYHVMNP 1054
Cdd:PRK07201 211 PMVGPDGGRTNI---------------------VPVDYVADALDHL-MHKDGRdGQTFHLTDP 251
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-563 |
2.20e-08 |
|
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: 57.84 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 109 RPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsapvtgLRPIVTETEPTMIATsidnlgdAVEVLAGHAPARLVVFD 188
Cdd:cd05922 16 VRGERVVLILPNRFTYIELSFAVAYAGGR------------LGLVFVPLNPTLKES-------VLRYLVADAGGRIVLAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 189 yHGKVDTHREAVEAARArlaGSVTIDTlAELIERGRALPATPiadSADDALALLIYTSGSTGAPKGAMYRESQVMSFWRK 268
Cdd:cd05922 77 -AGAADRLRDALPASPD---PGTVLDA-DGIRAARASAPAHE---VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 269 SSGWFEPSGYpSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDL-STLFEDLALVRPTELCFVPRIWDMvfaefhse 347
Cdd:cd05922 149 IAEYLGITAD-DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLdDAFWEDLREHGATGLAGVPSTYAM-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 348 VDRRLVDGADRAALeaqvkaelrenvlggRFVMALTGSAPisAEMTAWVESLLADVHLVEGYGSTEAgmvlndgmVRRPA 427
Cdd:cd05922 220 LTRLGFDPAKLPSL---------------RYLTQAGGRLP--QETIARLRELLPGAQVYVMYGQTEA--------TRRMT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 428 VIDYKLVDvPELGYFGtdQPYPRGELLVKTQ------------------TMFPGYYQRPDVTAEVFDPDGFYRTGDImAK 489
Cdd:cd05922 275 YLPPERIL-EKPGSIG--LAIPGGEFEILDDdgtptppgepgeivhrgpNVMKGYWNDPPYRRKEGRGGGVLHTGDL-AR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 490 VGPDQFVYL-DRRNNVLKLSqGEFIAVSKLEAVFGDSPLVRQIFIYG---NSARAYPLAVVVPSG---DALSRHGIENLK 562
Cdd:cd05922 351 RDEDGFLFIvGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEAAAVGlpdPLGEKLALFVTAPDKidpKDVLRSLAERLP 429
|
.
gi 489508543 563 P 563
Cdd:cd05922 430 P 430
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
42-256 |
2.49e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 57.90 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 42 LPQLIRMVMEGYADRPALgqralrfvTDPDSGRtmvellpRFetiTYRELWARAGTLATALSAEpAIRPGDRVCVLGFNS 121
Cdd:PRK08315 18 IGQLLDRTAARYPDREAL--------VYRDQGL-------RW---TYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 122 VDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATsIDNLGDAvevlaghaparlvvfDYHGKVDTHR-EAV 200
Cdd:PRK08315 79 PEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIA-ADGFKDS---------------DYVAMLYELApELA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 201 EAARARLAGS--------VTID--------TLAELIERGRALPATPIAD-----SADDAlallI---YTSGSTGAPKGAM 256
Cdd:PRK08315 143 TCEPGQLQSArlpelrrvIFLGdekhpgmlNFDELLALGRAVDDAELAArqatlDPDDP----IniqYTSGTTGFPKGAT 218
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
55-264 |
2.75e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.09 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 55 DRPALGQRALRFVtdpdSGR-TMVELLPrfetitYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIR 133
Cdd:PRK09192 28 DYAALGEAGMNFY----DRRgQLEEALP------YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 134 LGAVSVPLQTSAPVTGLrpivteteptmiATSIDNLGdaveVLAGHAPARLVVFDyHGKVDTHREAVEAARARLAGSVTi 213
Cdd:PRK09192 97 AGLVPVPLPLPMGFGGR------------ESYIAQLR----GMLASAQPAAIITP-DELLPWVNEATHGNPLLHVLSHA- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489508543 214 dTLAELIERGRALP-ATPiadsadDALALLIYTSGSTGAPKGAMYRESQVMS 264
Cdd:PRK09192 159 -WFKALPEADVALPrPTP------DDIAYLQYSSGSTRFPRGVIITHRALMA 203
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
84-585 |
2.98e-08 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 57.49 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVplqtsapvtGLRPIVTETEPTMIa 163
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAV---------ATMPLLRPKELAYI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsidnLGDAVEvlaghaparlvvfdyhgkvdthreaveaARARLAGSVTidtlaeliergralpatpiadsADDALALLI 243
Cdd:cd05958 79 -----LDKARI----------------------------TVALCAHALT----------------------ASDDICILA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYresqvmsFWRKSSGWFEpsGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYF----------VAKS 313
Cdd:cd05958 104 FTSGTTGAPKATMH-------FHRDPLASAD--RYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFpfgvgasgvlLEEA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 314 DLSTLFEDLALVRPTELCFVPRIWdmvfaefhsevdrrlvdgadRAALEAQVKAElrenVLGGRFVMALTGSAPISAEM- 392
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAY--------------------RAMLAHPDAAG----PDLSSLRKCVSAGEALPAALh 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 393 TAWVESLlaDVHLVEGYGSTEAGMVL--NDGMVRRPA-----VIDYKLVDVPELGyfgtdQPYPRGE---LLVKTQTmfp 462
Cdd:cd05958 231 RAWKEAT--GIPIIDGIGSTEMFHIFisARPGDARPGatgkpVPGYEAKVVDDEG-----NPVPDGTigrLAVRGPT--- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 463 GYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFIYG---NSAR 539
Cdd:cd05958 301 GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVVGhpdESRG 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489508543 540 AYPLAVVVPSGDALSrhgienlKPVISESLQEVARAAgLQSYEIPR 585
Cdd:cd05958 380 VVVKAFVVLRPGVIP-------GPVLARELQDHAKAH-IAPYKYPR 417
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
244-486 |
3.13e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 56.90 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSfwrksSGWF--EPSGYPS---ITLNfMPMSHVGGRQV-LYGTLSNGGTAYFVAKS-DLS 316
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVN-----NGYFigERLGLTEqdrLCIP-VPLFHCFGSVLgVLACLTHGATMVFPSPSfDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTELCFVPriwDMVFAEFHSEvDRRLVDgadraaleaqvKAELRENVLGGrfvmaltgsAPISAE-MTAW 395
Cdd:cd05917 83 AVLEAIEKEKCTALHGVP---TMFIAELEHP-DFDKFD-----------LSSLRTGIMAG---------APCPPElMKRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 VESL-LADVHLVegYGSTEAGMV-----LNDGMVRRPAV-------IDYKLVD-----VPELGYfgtdqpypRGELLVKT 457
Cdd:cd05917 139 IEVMnMKDVTIA--YGMTETSPVstqtrTDDSIEKRVNTvgrimphTEAKIVDpeggiVPPVGV--------PGELCIRG 208
|
250 260
....*....|....*....|....*....
gi 489508543 458 QTMFPGYYQRPDVTAEVFDPDGFYRTGDI 486
Cdd:cd05917 209 YSVMKGYWNDPEKTAEAIDGDGWLHTGDL 237
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
86-530 |
3.49e-08 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 57.41 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEptmiats 165
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTG------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 idnlgdavevlaghapARLVvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpIADSADdaLALLIYT 245
Cdd:cd17648 86 ----------------ARVV---------------------------------------------ITNSTD--LAYAIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 246 SGSTGAPKGAMYRESQVMSFWRKSSGWF--EPSGYPSITL--NFMPMSHVggRQVLYgTLSNGGTAYFV---AKSDLSTL 318
Cdd:cd17648 103 SGTTGKPKGVLVEHGSVVNLRTSLSERYfgRDNGDEAVLFfsNYVFDFFV--EQMTL-ALLNGQKLVVPpdeMRFDPDRF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPRIWDMVfaEFHSEVDRRLVDGADRaALEAQVKAELRENvLGGRFvmaLTGSAPISAEMTAWVES 398
Cdd:cd17648 180 YAYINREKVTYLSGTPSVLQQY--DLARLPHLKRVDAAGE-EFTAPVFEKLRSR-FAGLI---INAYGPTETTVTNHKRF 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVHLVEGYGSTEAGM---VLNDGMVRRP--AVidyklvdvpelgyfgtdqpyprGELLVKTQTMFPGYYQRPDVTAE 473
Cdd:cd17648 253 FPGDQRFDKSLGRPVRNTkcyVLNDAMKRVPvgAV----------------------GELYLGGDGVARGYLNRPELTAE 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 474 VFDPDGF--------------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:cd17648 311 RFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALASYPGVRE 380
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
244-596 |
3.72e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 56.64 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKgAMYR--ESQVMSFWRKSSGwFEPSGYPSITLNfMPMSHVGGrqvLYG---TLSNGGTAYFVAKSDLSTL 318
Cdd:cd17633 7 FTSGTTGLPK-AYYRseRSWIESFVCNEDL-FNISGEDAILAP-GPLSHSLF---LYGaisALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 FEDLALVRPTELCFVPriwdmvfaefhsevdrrlvdgadraaleAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVES 398
Cdd:cd17633 81 IRKINQYNATVIYLVP----------------------------TMLQALARTLEPESKIKSIFSSGQKLFESTKKKLKN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 399 LLADVHLVEGYGSTEAGMV---LNDGMVRRPAV------IDYKLVDvPELGYFGTdqpyprgeLLVKTQTMFPGYyqrpd 469
Cdd:cd17633 133 IFPKANLIEFYGTSELSFItynFNQESRPPNSVgrpfpnVEIEIRN-ADGGEIGK--------IFVKSEMVFSGY----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 470 VTAEVFDPDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNS-ARAYPLAVVVP 548
Cdd:cd17633 199 VRGGFSNPDGWMSVGD-IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPdARFGEIAVALY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489508543 549 SGDALSRhgienlKPVISESLQEVARaaglqsYEIPRDFI-IETTPFTL 596
Cdd:cd17633 278 SGDKLTY------KQLKRFLKQKLSR------YEIPKKIIfVDSLPYTS 314
|
|
| PLN02503 |
PLN02503 |
fatty acyl-CoA reductase 2 |
718-917 |
3.93e-08 |
|
fatty acyl-CoA reductase 2
Pssm-ID: 215279 [Multi-domain] Cd Length: 605 Bit Score: 57.56 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 718 AARTGVRRPSFASI-HGRSAteVHASDLTLDKFIDAATLAAAPN-----------LPAPSA----------------QVR 769
Cdd:PLN02503 43 GGGDGIRSSGLSSVlAERSR--VGSSQQHVAACRDAGSLVLSPNgkgqpeiavkdLVPYGSssavemadgigiaeflRGK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLaLEWLDRMDLVNGKLICLVRARSDEEAQARL-----DAT-FDSGDPYLVRHYRELGAGRLEVLAG 843
Cdd:PLN02503 121 NFLITGATGFLAKVL-IEKILRTNPDVGKIYLLIKAKDKEAAIERLkneviDAElFKCLQETHGKSYQSFMLSKLVPVVG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489508543 844 DKGEADLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKR-KPYIYTSTIAVGEQ 917
Cdd:PLN02503 200 NVCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKlKLFLQVSTAYVNGQ 274
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
771-970 |
4.03e-08 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 56.52 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 771 VLLTGATGFLGRYLALEWLDRMDLVNGklicLVRARSDEEAQARLDATFDSGDpylVRHYRELGAGrlevLAGdkgeadl 850
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGYRVRA----LVRSGSDAVLLDGLPVEVVEGD---LTDAASLAAA----MKG------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 851 gldrvtwqrladtVDLIVDPAALVNHVLPY-SQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFTEDADI 929
Cdd:cd05228 63 -------------CDRVFHLAAFTSLWAKDrKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPW 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489508543 930 RAISPtrriddsyANGYANSKWAGEVLLREAHEQcGLPVTV 970
Cdd:cd05228 130 NERPF--------PNDYYRSKLLAELEVLEAAAE-GLDVVI 161
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
84-612 |
5.16e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRpivtetepTMIA 163
Cdd:PRK05691 2212 QTLSYAELDARANRLARALR-ERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH--------YMIE 2282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSidnlgdAVEVLAGHAparlVVFDYHGKVdthreAVEAARARLAgsvtiDTLAELiergRALPATPIAD-SADDALALL 242
Cdd:PRK05691 2283 DS------GIGLLLSDR----ALFEALGEL-----PAGVARWCLE-----DDAAAL----AAYSDAPLPFlSLPQHQAYL 2338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 243 IYTSGSTGAPKG--------AMYRESQVMSFWRKSSgwfepsgypSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSD 314
Cdd:PRK05691 2339 IYTSGSTGKPKGvvvshgeiAMHCQAVIERFGMRAD---------DCELHFYSINFDAASERLLVPLLCGARVVLRAQGQ 2409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 LSTlfEDLA-LVRPTE---LCFVPRiWDMVFAEFHSEVDRRL-----------VDGADRAALEAQVKAELRENVLG--GR 377
Cdd:PRK05691 2410 WGA--EEICqLIREQQvsiLGFTPS-YGSQLAQWLAGQGEQLpvrmcitggeaLTGEHLQRIRQAFAPQLFFNAYGptET 2486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 378 FVMALTGSAPISAEmtawveslladvhlvEGYGSTEAGMVLNDgmvRRPAVIDYKLVDVPELGyfgtdqpypRGELLVKT 457
Cdd:PRK05691 2487 VVMPLACLAPEQLE---------------EGAASVPIGRVVGA---RVAYILDADLALVPQGA---------TGELYVGG 2539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 458 QTMFPGYYQRPDVTAEVFDPDGF-------YRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:PRK05691 2540 AGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDHQVKI-RGFRIELGEIESRLLEHPAVRE 2618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 531 ifiygnsarAYPLAVVVPSGDALSRH-------GIENLKPVISESLQEVARAAgLQSYEIPRDFIIettpftLENGLLTG 603
Cdd:PRK05691 2619 ---------AVVLALDTPSGKQLAGYlvsavagQDDEAQAALREALKAHLKQQ-LPDYMVPAHLIL------LDSLPLTA 2682
|
....*....
gi 489508543 604 IRKLARPQL 612
Cdd:PRK05691 2683 NGKLDRRAL 2691
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-521 |
5.21e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 56.88 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 86 ITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVsvplqtsapvtgLRPIVTETEPTMIATS 165
Cdd:PRK08162 44 RTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAV------------LNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 166 IDnlgdavevlagHAPARLVVfdyhgkVDTH-REAVEAARARLAGS--VTIDTLAELIERGRAL-------------PAT 229
Cdd:PRK08162 111 LR-----------HGEAKVLI------VDTEfAEVAREALALLPGPkpLVIDVDDPEYPGGRFIgaldyeaflasgdPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 230 PIADSAD--DALALlIYTSGSTGAPKGAMYRE--------SQVMSFwrkssgwfepsGYP--SITLNFMPMSHVGGRQVL 297
Cdd:PRK08162 174 AWTLPADewDAIAL-NYTSGTTGNPKGVVYHHrgaylnalSNILAW-----------GMPkhPVYLWTLPMFHCNGWCFP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 298 YGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMvfaefhsevdrrLVD--GADRAALEAQVKAelrenvlg 375
Cdd:PRK08162 242 WTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSA------------LINapAEWRAGIDHPVHA-------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 376 grfvmaLTGSAPISAEMTAWVESLLADV-HLvegYGSTE----------------------AGMVLNDGmVRRPAVIDYK 432
Cdd:PRK08162 302 ------MVAGAAPPAAVIAKMEEIGFDLtHV---YGLTEtygpatvcawqpewdalplderAQLKARQG-VRYPLQEGVT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 433 LVDvPElgyfgTDQPYPR-----GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFVYL-DRRNNVLk 506
Cdd:PRK08162 372 VLD-PD-----TMQPVPAdgetiGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGD-LAVLHPDGYIKIkDRSKDII- 442
|
490
....*....|....*
gi 489508543 507 LSQGEFIAVSKLEAV 521
Cdd:PRK08162 443 ISGGENISSIEVEDV 457
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
234-589 |
1.19e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 55.47 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 234 SADDALalLIYTSGSTGAPKGAMYRESQvmsFWRKSSGwfepsGYPSITLNFMPMSHVGGRQVlygtlSNGGTAYFVAK- 312
Cdd:cd05924 2 SADDLY--ILYTGGTTGMPKGVMWRQED---IFRMLMG-----GADFGTGEFTPSEDAHKAAA-----AAAGTVMFPAPp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 313 ----SDLSTLFEDL----ALVRPtELCFVPR-IWDMVfaEFHSEVDRRLV-DGADRAALEAQVKAELREnvLGGRFVMAl 382
Cdd:cd05924 67 lmhgTGSWTAFGGLlggqTVVLP-DDRFDPEeVWRTI--EKHKVTSMTIVgDAMARPLIDALRDAGPYD--LSSLFAIS- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 383 TGSAPISAEMTAWVESLLADVHLVEGYGSTEAGM---VLNDGMVRRPAVIDYKLVDVPELGYFGTDQPYPRGEL-LVKTQ 458
Cdd:cd05924 141 SGGALLSPEVKQGLLELVPNITLVDAFGSSETGFtgsGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVgWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 459 TMFP-GYYQRPDVTAEVFDPDGFYR---TGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIY 534
Cdd:cd05924 221 GHIPlGYYGDEAKTAETFPEVDGVRyavPGD-RATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489508543 535 GNSARAYPLAVVV---------PSGDALSRHgienlkpviseSLQEVARaaglqsYEIPRDFII 589
Cdd:cd05924 300 GRPDERWGQEVVAvvqlregagVDLEELREH-----------CRTRIAR------YKLPKQVVF 346
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
38-254 |
1.65e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.52 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 38 PGVALPQLIRMVMEGYADRPALgqRALRFVTDPDsGRTmVELlprfetiTYRELWARAGTLATALsaEPAIRPGDRVCVL 117
Cdd:PRK12476 32 PGTTLISLIERNIANVGDTVAY--RYLDHSHSAA-GCA-VEL-------TWTQLGVRLRAVGARL--QQVAGPGDRVAIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 118 GFNSVDYTTIDIALIRLGAVSVPLqtSAP-----VTGLRPIVTETEPTMIATSidnlgdavevlaghaparlvvfdyhgk 192
Cdd:PRK12476 99 APQGIDYVAGFFAAIKAGTIAVPL--FAPelpghAERLDTALRDAEPTVVLTT--------------------------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 193 vDTHREAVEAARARLAGSvtidtlaeliERGRALPATPIADSA----------DDALALLIYTSGSTGAPKG 254
Cdd:PRK12476 150 -TAAAEAVEGFLRNLPRL----------RRPRVIAIDAIPDSAgesfvpveldTDDVSHLQYTSGSTRPPVG 210
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
85-259 |
2.19e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 54.93 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAt 164
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLAL-GVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 sIDnlgDAVEVLAGHAPARLVvfDYHGKVDtHREAVEAARArlagsvTIDTLAELIERGRALPATPIADSAddalALLIY 244
Cdd:PRK07788 152 -YD---DEFTDLLSALPPDLG--RLRAWGG-NPDDDEPSGS------TDETLDDLIAGSSTAPLPKPPKPG----GIVIL 214
|
170
....*....|....*
gi 489508543 245 TSGSTGAPKGAMYRE 259
Cdd:PRK07788 215 TSGTTGTPKGAPRPE 229
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-254 |
2.34e-07 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 55.01 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 47 RMVMEGYADRPALGQralrfvtdpDSGRTMVEllprfETITYRELWARAGTLATALSAEpAIRPGDRVcVLGFNSVDYTT 126
Cdd:cd05967 58 RHVEAGRGDQIALIY---------DSPVTGTE-----RTYTYAELLDEVSRLAGVLRKL-GVVKGDRV-IIYMPMIPEAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 127 ID-IALIRLGAV-SV------PLQTSAPVTGLRPIVTET-----EPTMIATSIDNLGDAVEvLAGHAPARLVVFDyhgkv 193
Cdd:cd05967 122 IAmLACARIGAIhSVvfggfaAKELASRIDDAKPKLIVTascgiEPGKVVPYKPLLDKALE-LSGHKPHHVLVLN----- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489508543 194 dthREAVEAARARLAGSVTIDTLaelieRGRALPATPIADSADDALALLiYTSGSTGAPKG 254
Cdd:cd05967 196 ---RPQVPADLTKPGRDLDWSEL-----LAKAEPVDCVPVAATDPLYIL-YTSGTTGKPKG 247
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
63-254 |
4.09e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 63 ALRFVTD-PDSGRTMvellprfetiTYRELWARAGTLATALSAEPAirPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPl 141
Cdd:PRK05691 27 ALRFLADdPGEGVVL----------SYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 142 qtSAPVTGLRP--------IVTETEPTMIATS---IDNLGDAVEVLAGHAPARLVVfdyhgkvdthreaveaararlags 210
Cdd:PRK05691 94 --AYPPESARRhhqerllsIIADAEPRLLLTVadlRDSLLQMEELAAANAPELLCV------------------------ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489508543 211 vtiDTL-AELIERGRAlPATPiadsaDDALALLIYTSGSTGAPKG 254
Cdd:PRK05691 148 ---DTLdPALAEAWQE-PALQ-----PDDIAFLQYTSGSTALPKG 183
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
204-772 |
4.70e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 204 RARLAGSVTIDTLAELIERGRALPA--TPIADsadDALALLIYTSGSTGAPKGAMYRESQVMSFWR---KSSGWFEPS-- 276
Cdd:PRK06060 113 RDRFQPSRVAEAAELMSEAARVAPGgyEPMGG---DALAYATYTSGTTGPPKAAIHRHADPLTFVDamcRKALRLTPEdt 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 277 GYPSITLNFmpmSHVGGRQVLYgTLSNGGTAYFV-------AKSDLSTLFEdlalvrPTELCFVPRIWDMVFAEFHSEVD 349
Cdd:PRK06060 190 GLCSARMYF---AYGLGNSVWF-PLATGGSAVINsapvtpeAAAILSARFG------PSVLYGVPNFFARVIDSCSPDSF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 350 RRLvdgadRAALEAqvkAELRENVLGGRFVmALTGSAPIsaemtawveslladvhlVEGYGSTEAGMVLNDGMVR--RPA 427
Cdd:PRK06060 260 RSL-----RCVVSA---GEALELGLAERLM-EFFGGIPI-----------------LDGIGSTEVGQTFVSNRVDewRLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 428 VID-----YKLVDVPELGyfGTDQPYPRGELLVKTQTMFPGYYQRPDvtaEVFDPDGFYRTGDiMAKVGPDQFVYLDRRN 502
Cdd:PRK06060 314 TLGrvlppYEIRVVAPDG--TTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRD-RVCIDSDGWVTYRCRA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 503 NVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG--NSARAYPL-AVVVPSGDALsrhgienlkpvISES-LQEVARA--A 576
Cdd:PRK06060 388 DDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAvrESTGASTLqAFLVATSGAT-----------IDGSvMRDLHRGllN 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 577 GLQSYEIPRDF-IIETTPFTLENGLLTGI------------------RKLARPQLKkfyGERLERLYTELADSQSNELRE 637
Cdd:PRK06060 457 RLSAFKVPHRFaVVDRLPRTPNGKLVRGAlrkqsptkpiwelsltepGSGVRAQRD---DLSASNMTIAGGNDGGATLRE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 638 ---LRQSGPDAPVLPTLCRAAAALLG-STAADVRPDAHFADLGGDSLSALSLANLLHEIFGVDVPVGVIVSPASdLRALA 713
Cdd:PRK06060 534 rlvALRQERQRLVVDAVCAEAAKMLGePDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGS-ISGLA 612
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 714 DHIEAARTGVRRPSFASIHGRS-ATEVHASDLTLDKFIDAATLAAAPNLPAPSAQVRTVL 772
Cdd:PRK06060 613 QYLEAELAGGHGRLKSAGPVNSgATGLWAIEEQLNKVEELVAVIADGEKQRVADRLRALL 672
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-605 |
5.16e-07 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 53.54 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 225 ALPATPIADSAddALALLIYTSGSTGAPKG--------AMYRESQVMsfWRKSSGWfepsGYPSITLNFMPMSHVGGRQV 296
Cdd:cd05929 115 GSPETPIEDEA--AGWKMLYSGGTTGRPKGikrglpggPPDNDTLMA--AALGFGP----GADSVYLSPAPLYHAAPFRW 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 297 LYGTLSNGGTAYFVAKSDLStlfEDLALV---RPTELCFVP----RIWDMVFAEFHSEvdrrlvdgaDRAALEAQVKAel 369
Cdd:cd05929 187 SMTALFMGGTLVLMEKFDPE---EFLRLIeryRVTFAQFVPtmfvRLLKLPEAVRNAY---------DLSSLKRVIHA-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 370 renvlggrfvmALTGSAPISAEMTAWVESLladvhLVEGYGSTEA-GMVLND--------GMVRRPAVIDYKLVDVPelg 440
Cdd:cd05929 253 -----------AAPCPPWVKEQWIDWGGPI-----IWEYYGGTEGqGLTIINgeewlthpGSVGRAVLGKVHILDED--- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 441 yfGTDQPyPR--GELLVKTQTMFPgYYQRPDVTAEVFDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLkLSQGEFIAVSK 517
Cdd:cd05929 314 --GNEVP-PGeiGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDV-GYLDEDGYLYLtDRRSDMI-ISGGVNIYPQE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 518 LEAVFGDSPLVRQIFIYG----NSARAyPLAVV--VPSGDAlsrhgienlKPVISESLQEVARAAgLQSYEIPRDFIIET 591
Cdd:cd05929 388 IENALIAHPKVLDAAVVGvpdeELGQR-VHAVVqpAPGADA---------GTALAEELIAFLRDR-LSRYKCPRSIEFVA 456
|
410
....*....|....*.
gi 489508543 592 TPFTLENGLL--TGIR 605
Cdd:cd05929 457 ELPRDDTGKLyrRLLR 472
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
84-530 |
8.57e-07 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 53.03 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd17652 11 ETLTYAELNARANRLARLL-AARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaddalALLI 243
Cdd:cd17652 90 TTPDNL----------------------------------------------------------------------AYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPsGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLST---LFE 320
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDV-GPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgepLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 321 DLALVRPTELCFVPriwdmvfaefhsevdrrlvdgADRAALEAqvkaelrENVLGGRFVMaLTGSAPiSAEMtawVESLL 400
Cdd:cd17652 179 LLREHRITHVTLPP---------------------AALAALPP-------DDLPDLRTLV-VAGEAC-PAEL---VDRWA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 401 ADVHLVEGYGSTEA-------GMVLNDGMVR--RPA------VIDYKLVDVPelgyfgtdqPYPRGELLVKTQTMFPGYY 465
Cdd:cd17652 226 PGRRMINAYGPTETtvcatmaGPLPGGGVPPigRPVpgtrvyVLDARLRPVP---------PGVPGELYIAGAGLARGYL 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 466 QRPDVTAEVFDPDGF-------YRTGDImAKVGPD-QFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQ 530
Cdd:cd17652 297 NRPGLTAERFVADPFgapgsrmYRTGDL-ARWRADgQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAE 367
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
237-619 |
9.02e-07 |
|
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: 52.48 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 237 DALALLIYTSGSTGAPKGAMYRES-QVMSFWrkSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGT-LSNGGTAYFVAKSD 314
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSnEVYNAW--MLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 315 L--STLFEDL-ALV---RPTELCFVPRIWDMVFAefhsevdrrLVDGADRAALeaqvkaelrenvlggRFvmALTGSAPI 388
Cdd:cd05944 80 YrnPGLFDNFwKLVeryRITSLSTVPTVYAALLQ---------VPVNADISSL---------------RF--AMSGAAPL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 389 SAEMTAWVESLLAdVHLVEGYGSTEA--GMVLN--DGMVRRPAV---IDYKLVDVPELGYFGTDQ----PYPRGELLVKT 457
Cdd:cd05944 134 PVELRARFEDATG-LPVVEGYGLTEAtcLVAVNppDGPKRPGSVglrLPYARVRIKVLDGVGRLLrdcaPDEVGEICVAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 458 QTMFPGYYQRpDVTAEVFDPDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNS 537
Cdd:cd05944 213 PGVFGGYLYT-EGNKNAFVADGWLNTGD-LGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 538 ---ARAYPLAVVvpsgdalsrhgieNLKP---VISESLQEVARAAGLQSYEIPRDFIIettpftLENGLLTGIRKLARPQ 611
Cdd:cd05944 291 dahAGELPVAYV-------------QLKPgavVEEEELLAWARDHVPERAAVPKHIEV------LEELPVTAVGKVFKPA 351
|
....*...
gi 489508543 612 LKKFYGER 619
Cdd:cd05944 352 LRADAIHR 359
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
85-257 |
1.09e-06 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 52.88 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAePAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:cd05968 91 TLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 S--------IDNLGDAVEVLAGHAPA-RLVVFDYHGKVDthreaVEAARARLAGSvtidtlAELIErgrALPATPIADSA 235
Cdd:cd05968 170 AdgftrrgrEVNLKEEADKACAQCPTvEKVVVVRHLGND-----FTPAKGRDLSY------DEEKE---TAGDGAERTES 235
|
170 180
....*....|....*....|..
gi 489508543 236 DDALaLLIYTSGSTGAPKGAMY 257
Cdd:cd05968 236 EDPL-MIIYTSGTTGKPKGTVH 256
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
217-535 |
1.12e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 52.72 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 217 AELIerGRALPATPIADSADDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGyPSITLNFMPMSHvgGRQV 296
Cdd:PRK13388 132 AELV--AAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTR-DDVCYVSMPLFH--SNAV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 297 LYG---TLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFA--EFHSEVDRRLVDGADRAALEAQVKAELRe 371
Cdd:PRK13388 207 MAGwapAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILAtpERPDDADNPLRVAFGNEASPRDIAEFSR- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 372 nvlggRFvmaltgsapisaemtawvesllaDVHLVEGYGSTE-AGMVLND-----GMVRRPAViDYKLVDvPElgyfgTD 445
Cdd:PRK13388 286 -----RF-----------------------GCQVEDGYGSSEgAVIVVREpgtppGSIGRGAP-GVAIYN-PE-----TL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 446 QPYPRGEL---------------LVKTQ--TMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLS 508
Cdd:PRK13388 331 TECAVARFdahgallnadeaigeLVNTAgaGFFEGYYNNPEATAERMR-HGMYWSGD-LAYRDADGWIYFAGRTADWMRV 408
|
330 340
....*....|....*....|....*..
gi 489508543 509 QGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK13388 409 DGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
85-317 |
1.35e-06 |
|
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: 52.35 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 SIDNLGDAVEvlaghaparlvvfdyhgKVDTHREAVEAARARLAGSVtIDTLAELIERGRAL-PATPIADSADDALALLI 243
Cdd:cd05905 94 VEACLKGLPK-----------------KLLKSKTAAEIAKKKGWPKI-LDFVKIPKSKRSKLkKWGPHPPTRDGDTAYIE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSFWR--KSSGWFEPSGypSITLNFMPMSHVGgrqVLYGTLS---NGGTAYFVAKSDLST 317
Cdd:cd05905 156 YSFSSDGSLSGVAVSHSSLLAHCRalKEACELYESR--PLVTVLDFKSGLG---LWHGCLLsvySGHHTILIPPELMKT 229
|
|
| RfbB |
COG1088 |
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis]; |
769-973 |
1.61e-06 |
|
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440705 [Multi-domain] Cd Length: 333 Bit Score: 51.62 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLALEWLDRM---DLVNgkLICLVRArSDEEAQARLDatfdsgdpylvrhyrelGAGRLEVLAGDK 845
Cdd:COG1088 2 MRILVTGGAGFIGSNFVRYLLAKYpgaEVVV--LDKLTYA-GNLENLADLE-----------------DDPRYRFVKGDI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 846 GEADLgLDRVtwqrLADT-VDLIVDPAALVnHVlPYSqLFGP------NAAGTAELLRLALT--GKRKPYIYTSTIAV-G 915
Cdd:COG1088 62 RDREL-VDEL----FAEHgPDAVVHFAAES-HV-DRS-IDDPaafvetNVVGTFNLLEAARKywVEGFRFHHVSTDEVyG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489508543 916 EQIPPEAFTEDADIRAISPtrriddsyangYANSKWAGEVLLREAHEQCGLPVTVFRC 973
Cdd:COG1088 134 SLGEDGPFTETTPLDPSSP-----------YSASKAASDHLVRAYHRTYGLPVVITRC 180
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
237-497 |
2.45e-06 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 51.12 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 237 DALALlIYTSGSTGAPKGAM-------YRESQVMSFWRKSSGwfepsgypSITLNFMPMSHVGGRQVLYGTLSNGGTAYF 309
Cdd:cd17637 1 DPFVI-IHTAAVAGRPRGAVlshgnliAANLQLIHAMGLTEA--------DVYLNMLPLFHIAGLNLALATFHAGGANVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 310 VAKSDLSTLFEDLALVRPTelcfvpriwdmVFAEF----HSEVDRRLVDGADRAALEAQVKAELRENVlgGRFvMALTGS 385
Cdd:cd17637 72 MEKFDPAEALELIEEEKVT-----------LMGSFppilSNLLDAAEKSGVDLSSLRHVLGLDAPETI--QRF-EETTGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 386 apisaemTAWVeslladvhlveGYGSTEAGMVLN-------DGMVRRPAVI-DYKLVDvpELgyfgtDQPYPR---GELL 454
Cdd:cd17637 138 -------TFWS-----------LYGQTETSGLVTlspyrerPGSAGRPGPLvRVRIVD--DN-----DRPVPAgetGEIV 192
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489508543 455 VKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFVY 497
Cdd:cd17637 193 VRGPLVFQGYWNLPELTAYTFR-NGWHHTGD-LGRFDEDGYLW 233
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
84-588 |
2.59e-06 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 51.40 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIA 163
Cdd:cd17645 22 QSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 TSIDNLgdavevlaghaparlvvfdyhgkvdthreaveaararlagsvtidtlaeliergralpatpiadsaddalALLI 243
Cdd:cd17645 101 TNPDDL----------------------------------------------------------------------AYVI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 244 YTSGSTGAPKGAMYRESQVMSF--WRKSSGWFEPSGYPSITLNFmpmSHVGGRQVLYGTLSNGGTAYFV---AKSDLSTL 318
Cdd:cd17645 111 YTSGSTGLPKGVMIEHHNLVNLceWHRPYFGVTPADKSLVYASF---SFDASAWEIFPHLTAGAALHVVpseRRLDLDAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 319 ---FEDLALVrpteLCFVPRIWDMVFAEFHSEVDRRLVDGADRaaLEAQVKAELRenvlggrfvmaltgsapisaemtaw 395
Cdd:cd17645 188 ndyFNQEGIT----ISFLPTGAAEQFMQLDNQSLRVLLTGGDK--LKKIERKGYK------------------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 396 veslladvhLVEGYGSTEAGMVLNDGMVRRP--AVIDYKLVDVPELGYFGTD---QPY-PRGELLVKTQTMFPGYYQRPD 469
Cdd:cd17645 237 ---------LVNNYGPTENTVVATSFEIDKPyaNIPIGKPIDNTRVYILDEAlqlQPIgVAGELCIAGEGLARGYLNRPE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 470 VTAEVFDPDGF------YRTGDiMAKVGPDQFV-YLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLVRQIFIYG---NSAR 539
Cdd:cd17645 308 LTAEKFIVHPFvpgermYRTGD-LAKFLPDGNIeFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVLAkedADGR 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489508543 540 AYPLAVVVPSGDAlsrhGIENLKPVISESLQEvaraaglqsYEIPRDFI 588
Cdd:cd17645 386 KYLVAYVTAPEEI----PHEELREWLKNDLPD---------YMIPTYFV 421
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
84-256 |
8.83e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.94 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 84 ETITYRELWARAGTLATALSAEPAirPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLqtSAPVTGLRpivteteptmia 163
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAGLIAVPL--SVPQGGAH------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 164 tsiDNLGDAVevLAGHAPArlVVFDYHGKVDTHREAVEAARARLAGSV-TIDTLAELIERGRALPATPIADSAddalaLL 242
Cdd:PRK05850 98 ---DERVSAV--LRDTSPS--VVLTTSAVVDDVTEYVAPQPGQSAPPViEVDLLDLDSPRGSDARPRDLPSTA-----YL 165
|
170
....*....|....
gi 489508543 243 IYTSGSTGAPKGAM 256
Cdd:PRK05850 166 QYTSGSTRTPAGVM 179
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
211-553 |
9.01e-06 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 49.49 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 211 VTIDTLAELIERGRALPATPIADSADDALALLIYTSGSTGAPK--------------GAMY----RESQVmsFWRKSSGW 272
Cdd:cd05974 59 LTPDDLRDRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPKlvehthrsypvghlSTMYwiglKPGDV--HWNISSPG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 273 FEPSGYPSItlnFMPMshvggrqvlygtlsNGGTAYFV---AKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEfhsevd 349
Cdd:cd05974 137 WAKHAWSCF---FAPW--------------NAGATVFLfnyARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 350 rrlvdgaDRAALeaqvKAELRENVLGGRfvmaltgsaPISAEMTAWVESLLAdVHLVEGYGSTEA--------GMVLNDG 421
Cdd:cd05974 194 -------DLASF----DVKLREVVGAGE---------PLNPEVIEQVRRAWG-LTIRDGYGQTETtalvgnspGQPVKAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 422 MVRRPaVIDYKLVDVPELGyfgtdQPYPRGELLVKTQTMFP-----GYYQRPDVTAEVFDpDGFYRTGDIMAKVGPDQFV 496
Cdd:cd05974 253 SMGRP-LPGYRVALLDPDG-----APATEGEVALDLGDTRPvglmkGYAGDPDKTAHAMR-GGYYRTGDIAMRDEDGYLT 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489508543 497 YLDRRNNVLKLSQGEfIAVSKLEAVFGDSPLVRQifiygnsarayplAVVVPSGDAL 553
Cdd:cd05974 326 YVGRADDVFKSSDYR-ISPFELESVLIEHPAVAE-------------AAVVPSPDPV 368
|
|
| CDP_TE_SDR_e |
cd05258 |
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ... |
769-973 |
2.99e-05 |
|
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187568 [Multi-domain] Cd Length: 337 Bit Score: 47.67 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLALEWLDRmdlvNGKLIClvrarsdeeaqarldatFDSgdpyLVRHYRELGAGRLEVLAGDKGE- 847
Cdd:cd05258 1 MRVLITGGAGFIGSNLARFFLKQ----GWEVIG-----------------FDN----LMRRGSFGNLAWLKANREDGGVr 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 848 ---ADL-GLDRVTwqRLADTVDLIVDPAALVNHVLPYS---QLFGPNAAGTAELLRLA-LTGKRKPYIYTSTIAV----G 915
Cdd:cd05258 56 fvhGDIrNRNDLE--DLFEDIDLIIHTAAQPSVTTSASsprLDFETNALGTLNVLEAArQHAPNAPFIFTSTNKVygdlP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489508543 916 EQIP-----------PEAFTEDAdiraISPTRRIDdSYANGYANSKWAGEVLLREAHEQCGLPVTVFRC 973
Cdd:cd05258 134 NYLPleeletryelaPEGWSPAG----ISESFPLD-FSHSLYGASKGAADQYVQEYGRIFGLKTVVFRC 197
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
179-535 |
4.36e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 47.37 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 179 HAPARLVVfdyhgkvdTHREAVEAARARLAGSVTIDT----LAELIERGRALPATPIADSADDaLALLIYTSGSTGAPKG 254
Cdd:PRK07867 99 HADCQLVL--------TESAHAELLDGLDPGVRVINVdspaWADELAAHRDAEPPFRVADPDD-LFMLIFTSGTSGDPKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 255 AMYRESQVMSFWRKSSGWFEPSG----YPSitlnfMPMSHvgGRQVLYG---TLSNGGTAYFVAKSDLSTLFEDLALVRP 327
Cdd:PRK07867 170 VRCTHRKVASAGVMLAQRFGLGPddvcYVS-----MPLFH--SNAVMAGwavALAAGASIALRRKFSASGFLPDVRRYGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 328 TELCFVPRIWDMVFAEFHSEVDRrlvdgadraaleaqvkaelrENVLggRFVMALTGSAPISAEMTAWVesllaDVHLVE 407
Cdd:PRK07867 243 TYANYVGKPLSYVLATPERPDDA--------------------DNPL--RIVYGNEGAPGDIARFARRF-----GCVVVD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 408 GYGSTEAGMvlndGMVRRP---------AVIDYKLVDvPElgyfgTDQPYPRGEL--------------LVKTQ--TMFP 462
Cdd:PRK07867 296 GFGSTEGGV----AITRTPdtppgalgpLPPGVAIVD-PD-----TGTECPPAEDadgrllnadeaigeLVNTAgpGGFE 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489508543 463 GYYQRPDVTAEVFDpDGFYRTGDiMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYG 535
Cdd:PRK07867 366 GYYNDPEADAERMR-GGVYWSGD-LAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYA 436
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
377-614 |
6.45e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 47.27 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 377 RFVMAltGSAPISAEM-TAWVESLlaDVHLVEGYGSTEAGMVL--NDGMVRRPAV-------IDYKLVDVPelgyfGTDQ 446
Cdd:PRK06814 910 RYVFA--GAEKVKEETrQTWMEKF--GIRILEGYGVTETAPVIalNTPMHNKAGTvgrllpgIEYRLEPVP-----GIDE 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 447 PyprGELLVKTQTMFPGYY--QRPDVTAEVfdPDGFYRTGDIMaKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAvfgd 524
Cdd:PRK06814 981 G---GRLFVRGPNVMLGYLraENPGVLEPP--ADGWYDTGDIV-TIDEEGFITIKGRAKRFAKIAGEMISLAAVEE---- 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 525 spLVRQIFIYGNSArayplAVVVPsgDAlsRHGiENL------KPVISESLQEVARAAGLQSYEIPRDFI-IETTPFtLE 597
Cdd:PRK06814 1051 --LAAELWPDALHA-----AVSIP--DA--RKG-ERIillttaSDATRAAFLAHAKAAGASELMVPAEIItIDEIPL-LG 1117
|
250
....*....|....*....
gi 489508543 598 NGLL--TGIRKLARPQLKK 614
Cdd:PRK06814 1118 TGKIdyVAVTKLAEEAAAK 1136
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
236-619 |
7.22e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 46.58 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 236 DDALALLIYTSGSTGAPKGAMYRESQVMSfwrKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVaksDL 315
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKGAMLTAAALTA---SADATHDRLGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVEL---DV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 316 STLFEDLALVRPTELCFVPRiwdmvfaEFHSEVDRRLVDG-ADRAALEAqvkaeLREnvlggrFVMALTGSAPISAEMTA 394
Cdd:PRK07824 108 SAGFDPTALPRAVAELGGGR-------RYTSLVPMQLAKAlDDPAATAA-----LAE------LDAVLVGGGPAPAPVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 395 WVESllADVHLVEGYGSTE-AGMVLNDGmvrRPavIDYKLVDVPElgyfgtdqpyprGELLVKTQTMFPGYyqRPDVTAE 473
Cdd:PRK07824 170 AAAA--AGINVVRTYGMSEtSGGCVYDG---VP--LDGVRVRVED------------GRIALGGPTLAKGY--RNPVDPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 474 VFDPDGFYRTGDIMAkVGPDQFVYLDRRNNVLKlSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYP---LAVVVPSG 550
Cdd:PRK07824 229 PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGqrvVAAVVGDG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 551 DALsrhgienlkPVISESLQEVARaaGLQSYEIPRDF-IIETTPftlenglLTGIRKLARPQLKKFYGER 619
Cdd:PRK07824 307 GPA---------PTLEALRAHVAR--TLDRTAAPRELhVVDELP-------RRGIGKVDRRALVRRFAGE 358
|
|
| UDP_GE_SDE_e |
cd05253 |
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ... |
770-1020 |
9.32e-05 |
|
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187563 [Multi-domain] Cd Length: 332 Bit Score: 46.18 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRMDLVNGkliclvrarsdeeaqarLDATFDSGDPYLVRHyrelgagRLEVLAGDKG--- 846
Cdd:cd05253 2 KILVTGAAGFIGFHVAKRLLERGDEVVG-----------------IDNLNDYYDVRLKEA-------RLELLGKSGGfkf 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 847 -EADLgLDRVTWQRLADTV--DLIVDPAA-------LVNhvlPYSqLFGPNAAGTAELLRLALTGKRKPYIYTSTIAV-- 914
Cdd:cd05253 58 vKGDL-EDREALRRLFKDHefDAVIHLAAqagvrysLEN---PHA-YVDSNIVGFLNLLELCRHFGVKHLVYASSSSVyg 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 915 -GEQIPpeaFTEDADIraisptrridDSYANGYANSKWAGEVLLREAHEQCGLPVTVFRcdmilADTSYtGQLNLPDM-- 991
Cdd:cd05253 133 lNTKMP---FSEDDRV----------DHPISLYAATKKANELMAHTYSHLYGIPTTGLR-----FFTVY-GPWGRPDMal 193
|
250 260 270
....*....|....*....|....*....|.
gi 489508543 992 --FTRLMLSlaatgiapGSFYELDAHGNRQR 1020
Cdd:cd05253 194 flFTKAILE--------GKPIDVFNDGNMSR 216
|
|
| UDP_AE_SDR_e |
cd05256 |
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ... |
771-972 |
9.80e-05 |
|
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187566 [Multi-domain] Cd Length: 304 Bit Score: 45.67 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 771 VLLTGATGFLGRYLALEWLDRMDLVNGkliclvrarsdeeaqarLDaTFDSGDPYLVRHyrelGAGRLEVLagdkgEADL 850
Cdd:cd05256 2 VLVTGGAGFIGSHLVERLLERGHEVIV-----------------LD-NLSTGKKENLPE----VKPNVKFI-----EGDI 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 851 GlDRVTWQRLADTVDLIVDPAAL------VNHVLPYSQLfgpNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFT 924
Cdd:cd05256 55 R-DDELVEFAFEGVDYVFHQAAQasvprsIEDPIKDHEV---NVLGTLNLLEAARKAGVKRFVYASSSSVYGDPPYLPKD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489508543 925 EDADIRAISPtrriddsyangYANSKWAGEVLLREAHEQCGLPVTVFR 972
Cdd:cd05256 131 EDHPPNPLSP-----------YAVSKYAGELYCQVFARLYGLPTVSLR 167
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
85-528 |
1.85e-04 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 45.69 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 85 TITYRELWARAGTLATALsaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:PRK08633 641 ELSYGKALTGALALARLL--KRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVIT 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 S------IDNLGDAVEVLAGhaPARLVVFDYHGKVDTHREAVEAARARLAGsvtidtlAELIERGRALPATPiadsadDA 238
Cdd:PRK08633 719 SrkflekLKNKGFDLELPEN--VKVIYLEDLKAKISKVDKLTALLAARLLP-------ARLLKRLYGPTFKP------DD 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 239 LALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSItLNFMPMSHVGGRQV-LYGTLSNG-GTAYFVAKSDLS 316
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVI-LSSLPFFHSFGLTVtLWLPLLEGiKVVYHPDPTDAL 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 317 TLFEDLALVRPTELCFVP----------RIWDMVFAEFhsevdRRLVDGADRaaLEAQVKAELREnvlggRFvmaltgsa 386
Cdd:PRK08633 863 GIAKLVAKHRATILLGTPtflrlylrnkKLHPLMFASL-----RLVVAGAEK--LKPEVADAFEE-----KF-------- 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 387 pisaemtawvesllaDVHLVEGYGSTEAGMV--LN----------------DGMVRRP----AVidyKLVDvPElgyfgT 444
Cdd:PRK08633 923 ---------------GIRILEGYGATETSPVasVNlpdvlaadfkrqtgskEGSVGMPlpgvAV---RIVD-PE-----T 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 445 DQPYPRGE---LLVK-TQTMfPGYYQRPDVTAEV---FDPDGFYRTGDImAKVGPDQFVYL-DRRNNVLKLSqGEFIAVS 516
Cdd:PRK08633 979 FEELPPGEdglILIGgPQVM-KGYLGDPEKTAEVikdIDGIGWYVTGDK-GHLDEDGFLTItDRYSRFAKIG-GEMVPLG 1055
|
490
....*....|....*.
gi 489508543 517 KLE----AVFGDSPLV 528
Cdd:PRK08633 1056 AVEeelaKALGGEEVV 1071
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
510-630 |
1.89e-04 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 46.00 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 510 GEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYpLAVVVPSGDA------LSRHGIENLKP---------------VISES 568
Cdd:PTZ00297 867 YEYVIAAELERIFSQSRYVNDIFLYADPSRPI-IAIVSPNRDTvefewrQSHCMGEGGGParqlgwtelvayassLLTAD 945
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489508543 569 LQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTELADS 630
Cdd:PTZ00297 946 FACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDVETT 1007
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
31-571 |
4.25e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 31 ITQAIDQPGVALPQLIRMVMEGYADRPALGQRALrfvtdPDSGRTMVELLPRF--------------ETITYRELWARAG 96
Cdd:PRK05691 1093 LEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPC-----APAQAWLPELLNEQarqtperialvwdgGSLDYAELHAQAN 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 97 TLATALSaEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSidnlgdavevl 176
Cdd:PRK05691 1168 RLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ----------- 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 177 aGHAPARLvvfdyhgkvdthreaveaARARLAGSVTIDTLaelieRGRALPAT-PIADSADDALALLIYTSGSTGAPKG- 254
Cdd:PRK05691 1236 -SHLLERL------------------PQAEGVSAIALDSL-----HLDSWPSQaPGLHLHGDNLAYVIYTSGSTGQPKGv 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 255 -----AMYRESQVMS----------FWRKSSGWFEPSGYPSitlnFMPMShVGGRQVLYGTLSNGGTAYFVAksdlstlf 319
Cdd:PRK05691 1292 gnthaALAERLQWMQatyalddsdvLMQKAPISFDVSVWEC----FWPLI-TGCRLVLAGPGEHRDPQRIAE-------- 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 320 edlaLVRP---TELCFVPRIWDMVF-----AEFHSEvdRRLVDGAdraalEAqVKAELRENVLggrfvmaltgsapisae 391
Cdd:PRK05691 1359 ----LVQQygvTTLHFVPPLLQLFIdeplaAACTSL--RRLFSGG-----EA-LPAELRNRVL----------------- 1409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 392 mtawveSLLADVHLVEGYGSTEAGMVL-------NDGM---VRRP------AVIDYKLVDVPelgyfgtdqPYPRGELLV 455
Cdd:PRK05691 1410 ------QRLPQVQLHNRYGPTETAINVthwqcqaEDGErspIGRPlgnvlcRVLDAELNLLP---------PGVAGELCI 1474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 456 KTQTMFPGYYQRPDVTAEVF--DPDG-----FYRTGDIMAKVGPDQFVYLDRRNNVLKLsQGEFIAVSKLEAVFGDSPLV 528
Cdd:PRK05691 1475 GGAGLARGYLGRPALTAERFvpDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLAQPGV 1553
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 489508543 529 RQIFIYGNSARAYPLAVVVPSGDALSRHGIENLKPVISESLQE 571
Cdd:PRK05691 1554 AQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPE 1596
|
|
| Gne_like_SDR_e |
cd05238 |
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ... |
770-959 |
4.30e-04 |
|
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187549 [Multi-domain] Cd Length: 305 Bit Score: 43.91 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLALEWLDRMDLVNGKLICLVRARSDEEAQARLDATFDSGDPYLVrhyRELGAGRLEV---LAGdkg 846
Cdd:cd05238 2 KVLITGASGFVGQRLAERLLSDVPNERLILIDVVSPKAPSGAPRVTQIAGDLAVPALI---EALANGRPDVvfhLAA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 847 eadlgldrvtwqrladtvdlIVDPAAlvnhVLPYSQLFGPNAAGTAELL-RLALTGKRKPYIYTSTIAVgEQIPPEAFTE 925
Cdd:cd05238 76 --------------------IVSGGA----EADFDLGYRVNVDGTRNLLeALRKNGPKPRFVFTSSLAV-YGLPLPNPVT 130
|
170 180 190
....*....|....*....|....*....|....
gi 489508543 926 DADirAISPtrriddsyANGYANSKWAGEVLLRE 959
Cdd:cd05238 131 DHT--ALDP--------ASSYGAQKAMCELLLND 154
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
446-488 |
4.33e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 44.21 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489508543 446 QPYPRGE---LLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMA 488
Cdd:PRK10946 373 NPLPQGEvgrLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVS 418
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
769-1042 |
4.53e-04 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 43.43 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 769 RTVLLTGATGFLGRYLALEWLDRMDLVNgkliCLVRARSDEEAQARldatfdsgdpylVRHyrelgagrlevLAGDKGEA 848
Cdd:cd05265 1 MKILIIGGTRFIGKALVEELLAAGHDVT----VFNRGRTKPDLPEG------------VEH-----------IVGDRNDR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 849 DlGLDRVTWQRladTVDLIVDpaalvnhVLPYSqlfgpnaAGTAELLRLALTGKRKPYIYTSTIAVGEQiPPEAFTEDAD 928
Cdd:cd05265 54 D-ALEELLGGE---DFDVVVD-------TIAYT-------PRQVERALDAFKGRVKQYIFISSASVYLK-PGRVITESTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 929 IRAISPTRRIDDSYangYANSKWAGEVLLREAHeqcGLPVTVFRCDMILADTSYTGQLNLpdMFTRLmlslaATG---IA 1005
Cdd:cd05265 115 LREPDAVGLSDPWD---YGRGKRAAEDVLIEAA---AFPYTIVRPPYIYGPGDYTGRLAY--FFDRL-----ARGrpiLV 181
|
250 260 270
....*....|....*....|....*....|....*..
gi 489508543 1006 PGsfyelDAHGNRQRAHydglpVEFVAEAICTLGTHS 1042
Cdd:cd05265 182 PG-----DGHSLVQFIH-----VKDLARALLGAAGNP 208
|
|
| Arna_like_SDR_e |
cd05257 |
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ... |
770-972 |
7.37e-04 |
|
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187567 [Multi-domain] Cd Length: 316 Bit Score: 43.06 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 770 TVLLTGATGFLGRYLAlEWLdrmdLVNGkliCLVRARSDeeaqarldatFDSGDPYLVRHYRELGagRLEVLAGDKgead 849
Cdd:cd05257 1 NVLVTGADGFIGSHLT-ERL----LREG---HEVRALDI----------YNSFNSWGLLDNAVHD--RFHFISGDV---- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 850 lgLDRVTWQRLADTVDLIVDPAALVN----HVLPYSqLFGPNAAGTAELLRLALTGKRKPYIYTSTIAV---GEQIPpea 922
Cdd:cd05257 57 --RDASEVEYLVKKCDVVFHLAALIAipysYTAPLS-YVETNVFGTLNVLEAACVLYRKRVVHTSTSEVygtAQDVP--- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489508543 923 FTEDADIRAISPTRRIddsyangYANSKWAGEVLLREAHEQCGLPVTVFR 972
Cdd:cd05257 131 IDEDHPLLYINKPRSP-------YSASKQGADRLAYSYGRSFGLPVTIIR 173
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
87-256 |
7.99e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALSAEpAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSI 166
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSA 3825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 167 DNLGDAVEVLAghaparlvvfdyhgkvdthrEAVEAARARLagsvtidTLAELIERGRALPATPIADSADDALALLIYTS 246
Cdd:PRK05691 3826 ACREQARALLD--------------------ELGCANRPRL-------LVWEEVQAGEVASHNPGIYSGPDNLAYVIYTS 3878
|
170
....*....|
gi 489508543 247 GSTGAPKGAM 256
Cdd:PRK05691 3879 GSTGLPKGVM 3888
|
|
| dTDP_GD_SDR_e |
cd05246 |
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ... |
887-973 |
1.86e-03 |
|
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187557 [Multi-domain] Cd Length: 315 Bit Score: 41.77 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 887 NAAGTAELLRLALTGKRKPYIYTSTIAV-GEQIPPEAFTEDADIRAISPtrriddsyangYANSKWAGEVLLREAHEQCG 965
Cdd:cd05246 101 NVLGTYTLLEAARKYGVKRFVHISTDEVyGDLLDDGEFTETSPLAPTSP-----------YSASKAAADLLVRAYHRTYG 169
|
....*...
gi 489508543 966 LPVTVFRC 973
Cdd:cd05246 170 LPVVITRC 177
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
87-595 |
2.40e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 87 TYRELWARAGTLATALsAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAV--SVPLQTSAPVTGLRPIVTETEPTMIAT 164
Cdd:PLN02479 47 TWAQTYQRCRRLASAL-AKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVvnCVNIRLNAPTIAFLLEHSKSEVVMVDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 165 SIDNLG-DAVEVLAGHA-----PARLVVFdyhGKVDTHREAVEAARARlaGSVTIDtlaELIERGRalPATPIADSAD-- 236
Cdd:PLN02479 126 EFFTLAeEALKILAEKKkssfkPPLLIVI---GDPTCDPKSLQYALGK--GAIEYE---KFLETGD--PEFAWKPPADew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 237 DALALLiYTSGSTGAPKGAM--YRESQVMSFwrksSG---WFEPSGypSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVA 311
Cdd:PLN02479 196 QSIALG-YTSGTTASPKGVVlhHRGAYLMAL----SNaliWGMNEG--AVYLWTLPMFHCNGWCFTWTLAALCGTNICLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 312 KSDLSTLFEDLALVRPTELCFVPRIWDMVfaefhsevdrrlvdgadraaleaqVKAELRENVLG-GRFVMALT-GSAPIS 389
Cdd:PLN02479 269 QVTAKAIYSAIANYGVTHFCAAPVVLNTI------------------------VNAPKSETILPlPRVVHVMTaGAAPPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 390 AEMTAWVESLLADVH---LVEGYG----------------STEAGMVLNDGmVRRPAVIDYKLVDVPelgyfgTDQPYPR 450
Cdd:PLN02479 325 SVLFAMSEKGFRVTHtygLSETYGpstvcawkpewdslppEEQARLNARQG-VRYIGLEGLDVVDTK------TMKPVPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489508543 451 -----GELLVKTQTMFPGYYQRPDVTAEVFDpDGFYRTGDIMAKvGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDS 525
Cdd:PLN02479 398 dgktmGEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVK-HPDGYIEIKDRSKDIIISGGENISSLEVENVVYTH 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489508543 526 PLVRQIFIYgnsARA------YPLAVVVPSGDALSRHgienlKPVISESLQEVARAAgLQSYEIPRDFIIETTPFT 595
Cdd:PLN02479 476 PAVLEASVV---ARPderwgeSPCAFVTLKPGVDKSD-----EAALAEDIMKFCRER-LPAYWVPKSVVFGPLPKT 542
|
|
| |
