|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
19-1407 |
0e+00 |
|
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: 2347.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 19 RWSSRLSALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATvlmkltlefstlfpASGLPTPYHILLTSFAILLFRYTPD 98
Cdd:TIGR03443 1 RWSERLDNPTLSVLPHDYLRPANNRLVEATYSLQLPSAEVT--------------AGGGSTPFIILLAAFAALVYRLTGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 99 PSLVICTSANASTKPLLLKLDIAAEMTFFDVLRQIMEREQEAQADD-VPITKLVDHIK------PEGPLYRVRFFDSTQV 171
Cdd:TIGR03443 67 EDIVLGTSSNKSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIgVPFDELSEHIQaakkleRTPPLFRLAFQDAPDN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 172 ESDASSSLTtdltlfllaaPSD-TPATRTSVPPLYLRLTYNSLLFTQSRITATLESLLQLLSSAAsHEPAHPIGALPLRT 250
Cdd:TIGR03443 147 QQTTYSTGS----------TTDlTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAAS-SNPDEPIGKVSLIT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 251 PNQSAALPDPAADLDWCGFVGAIPDIFSANAKAHPDRVCVVQSELAEGqtmmdgPSRGRRIFTYKQIDEASNILAHALLK 330
Cdd:TIGR03443 216 PSQKSLLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPSFLD------PSSKTRSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 331 NGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDYISDNLSL 410
Cdd:TIGR03443 290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDYIDKELEL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 411 RLLVPAIQLTSS-NVTGSRSDAGE-DILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGK 488
Cdd:TIGR03443 370 RTEIPALALQDDgSLVGGSLEGGEtDVLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 489 RFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIP 568
Cdd:TIGR03443 450 RFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIP 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 569 TLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLATQKDLIPAGQGMIDVQLLVVNR 648
Cdd:TIGR03443 530 SLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQLLVVNR 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 649 TDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNVERPDTLKEKNPAAAEHWFGIRDRMYRSGDLGRYL 727
Cdd:TIGR03443 610 NDRTQTCGVGEVGEIYVRAGGLAEGYLGlPELNAEKFVNNWFVDPSHWIDLDKENNKPEREFWLGPRDRLYRTGDLGRYL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 728 PDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPI-DGDELEGLMSASEAADDD 806
Cdd:TIGR03443 690 PDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdKSDELEEFKSEVDDEESS 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 807 EeidlktQMIRGVKKYRKLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDTSLLA-----PAPSAST 881
Cdd:TIGR03443 770 D------PVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAavaknRSASAAD 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 882 ADHTPTQKTIHDIWLSLLPSPPPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEIDLLRNA 961
Cdd:TIGR03443 844 EEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKG 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 962 D-LGGAGDGAIEAEKAV---DYAKDVELLSKELP-TFSALPADFATKELTVFLTGATGYLGAFILKDLLSRR---VRKVI 1033
Cdd:TIGR03443 924 EeLADEGDSEIEEEETVlelDYAKDAKTLVDSLPkSYPSRKELDASTPITVFLTGATGFLGSFILRDLLTRRsnsNFKVF 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1034 CLVRAKSADQGLQRLRDSGEGRGVWDEEWVKqdRIEAVIGDLAEEKFGLSQAEWDRVAEQTDAVLHNGAIVHWVYPYPKL 1113
Cdd:TIGR03443 1004 AHVRAKSEEAGLERLRKTGTTYGIWDEEWAS--RIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKL 1081
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1114 RAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAFVAKADEVVQAGGKGLLENDDLEAGRTGLNAGYGQSKWVAEKII 1193
Cdd:TIGR03443 1082 RDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYVNLSDELVQAGGAGIPESDDLMGSSKGLGTGYGQSKWVAEYII 1161
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1194 MEAGKKGLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEINNAIICCPVDHVARLSSLATLSSSASSAFNI 1273
Cdd:TIGR03443 1162 REAGKRGLRGCIVRPGYVTGDSKTGATNTDDFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAALNPPKESELAV 1241
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1274 MHVTGHPKIRFNDLLGSLQLYGYDVKRVEYVHWRTRLEQHVLET-QDNALFPLLHFVLDDLPTSTKSAELDDTNAQNL-- 1350
Cdd:TIGR03443 1242 AHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRKSLERFVIERsEDNALFPLLHFVLDDLPQSTKAPELDDTNAATSlk 1321
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 1351 --AAAAGEVRTS--GVTEKEIGLYIAWLIRAGFLESPQKKGK-SLPVLE--GGAMKAI----GRTTAG 1407
Cdd:TIGR03443 1322 adAAWTGVDVSSgaGVTEEQIGIYIAYLVKVGFLPAPTKTGAlPLPKIEisEAQLKLIasagGRGSAA 1389
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
284-868 |
0e+00 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 846.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 284 HPDRVCVVqselaEGQTMMDGPSRGrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVF 363
Cdd:cd17647 1 FPERTCVV-----ETPSLNSSKTRS---FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 364 SVVDPAYPPSRQTVYLSVSTPRALLVISSAGslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqya 443
Cdd:cd17647 73 SVIDPAYPPARQNIYLGVAKPRGLIVIRAAG------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 444 qtpagVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQL 523
Cdd:cd17647 104 -----VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 524 HVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGT 603
Cdd:cd17647 179 LVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGT 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 604 TETQRAVSYFAIPSVNEDSTFLATQKDLIPAGQGMIDVQLLVVNRTDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAE 682
Cdd:cd17647 259 TETQRAVSYFEVPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGlPELNKE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 683 KFVVNWFgqnVErPDTLKEKNPAAAE----HWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHL 758
Cdd:cd17647 339 KFVNNWF---VE-PDHWNYLDKDNNEpwrqFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHI 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 759 SRHPLVRENVTLVRRDKDEEKVLVSYFVPiDGDELEGLMSASEAADDDEEIDLktqMIRGVKKYRKLIRDIREYLKKKLP 838
Cdd:cd17647 415 SQHPLVRENITLVRRDKDEEPTLVSYIVP-RFDKPDDESFAQEDVPKEVSTDP---IVKGLIGYRKLIKDIREFLKKRLA 490
|
570 580 590
....*....|....*....|....*....|
gi 58269178 839 SYSVPAVYFPLHKLPLNPNGKIDKPALPFP 868
Cdd:cd17647 491 SYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-1108 |
4.69e-138 |
|
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: 457.78 E-value: 4.69e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 11 EELNQRLDRWSSRL-SALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEfstlfpaSGLpTPYHILLTSFA 89
Cdd:COG1020 202 EELARQLAYWRQQLaGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARR-------HGV-TLFMVLLAAFA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 90 ILLFRYTPDPSLVI-CTSAN-------------ASTkpLLLKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHI 154
Cdd:COG1020 274 LLLARYSGQDDVVVgTPVAGrprpeleglvgffVNT--LPLRVDLSGDPSFAELLARVRETLLAAYAhQDLPFERLVEEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 155 KPEGPLYRVRFFDSTQVESDASSSLTTDLTLFLLAAPSDTPATR-----TSVPP---LYLRLTYNSLLFTQSRITA---- 222
Cdd:COG1020 352 QPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKfdltlTVVETgdgLRLTLEYNTDLFDAATIERmagh 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 223 ---TLESLLqllssaasHEPAHPIGALPLRTPNQSAAL----PDPAADLDwcgFVGAIPDIFSANAKAHPDRVCVVqsel 295
Cdd:COG1020 432 lvtLLEALA--------ADPDQPLGDLPLLTAAERQQLlaewNATAAPYP---ADATLHELFEAQAARTPDAVAVV---- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 296 AEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQ 375
Cdd:COG1020 497 FGDQSL-----------TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 376 TVYLSVSTPRALLvisSAGSLAPSVSDYIsdnlslrllVPAIQLTSSNVTgsrsdagedilapyqQYAQTPAGVVLGPDS 455
Cdd:COG1020 566 AYMLEDAGARLVL---TQSALAARLPELG---------VPVLALDALALA---------------AEPATNPPVPVTPDD 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 456 PATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPG 535
Cdd:COG1020 619 LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPA 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 536 RLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAI 615
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEV 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 616 PSVNEDStflatqkDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFGQnve 694
Cdd:COG1020 779 TPPDADG-------GSVPIGRPIANTRVYVLDAHLQ--PVPVGVPGELYIGGAGLARGYLnRPELTAERFVADPFGF--- 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 695 rpdtlkeknPAAaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRD 774
Cdd:COG1020 847 ---------PGA---------RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARED 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 775 KDEEKVLVSYFVPidgdeleglmsASEAADDDEEIdlktqmirgvkkyrklirdiREYLKKKLPSYSVPAVYFPLHKLPL 854
Cdd:COG1020 909 APGDKRLVAYVVP-----------EAGAAAAAALL--------------------RLALALLLPPYMVPAAVVLLLPLPL 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 855 NPNGKIDKPALPFPDTsllAPAPSASTADHTPTQKTIHDIWLSLLPSPPPHITLDENFFDMGGHSILATRLIFEIRKAFV 934
Cdd:COG1020 958 TGNGKLDRLALPAPAA---AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 935 VnaplgLVFDKPTIAGQAAEIDLLRNADLGGAGDGAIEAEKAVDYAKDVELLSKELPTFSALPADFATKELTVFLTGATG 1014
Cdd:COG1020 1035 L-----LLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLL 1109
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1015 YLGAFILKDLLSRRVRKVICLVRAKSADQGLQRLRDSGEGRGVWDEEWVKQDRIEAVIGDLAEEKFGLSQAEWDRVAEQT 1094
Cdd:COG1020 1110 ALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLL 1189
|
1130
....*....|....
gi 58269178 1095 DAVLHNGAIVHWVY 1108
Cdd:COG1020 1190 LLLLLLLLLLLLLL 1203
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
285-865 |
1.02e-137 |
|
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: 429.64 E-value: 1.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVqselAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFS 364
Cdd:cd05930 1 PDAVAVV----DGDQSL-----------TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 VVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaq 444
Cdd:cd05930 66 PLDPSYPAERLAYILEDSGAKLVLT------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 445 tpagvvlGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLH 524
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 525 VPTADDIGTPGRLAEWMADSEVTVTHLTPAM-GQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGT 603
Cdd:cd05930 164 VLPEEVRKDPEALADLLAEEGITVLHLTPSLlRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 604 TETQRAVSYFAIPSVNEDStflatqkDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYL-DPTATAE 682
Cdd:cd05930 244 TEATVDATYYRVPPDDEED-------GRVPIGRPIPNTRVYVLDENLR--PVPPGVPGELYIGGAGLARGYLnRPELTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 683 KFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHP 762
Cdd:cd05930 315 RFVPNPFGPG----------------------ERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHP 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 763 LVRENVTLVRRDKDEEKVLVSYFVPidgdeleglmsaseaaDDDEEIDlktqmirgvkkyrklIRDIREYLKKKLPSYSV 842
Cdd:cd05930 373 GVREAAVVAREDGDGEKRLVAYVVP----------------DEGGELD---------------EEELRAHLAERLPDYMV 421
|
570 580
....*....|....*....|...
gi 58269178 843 PAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05930 422 PSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
313-768 |
4.79e-121 |
|
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: 383.54 E-value: 4.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKN-GLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVIS 391
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 SAGSLAPSVSDyisdnlsLRLLVPAIQLtssnvtgsrsDAGEDILAPyqqyaqTPAGVVLGPDSPATLSFTSGSTGIPKG 471
Cdd:TIGR01733 81 ALASRLAGLVL-------PVILLDPLEL----------AALDDAPAP------PPPDAPSGPDDLAYVIYTSGSTGRPKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRL-AEWMADSEVTVTH 550
Cdd:TIGR01733 138 VVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 551 LTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLatqkd 630
Cdd:TIGR01733 218 LTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 631 lIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFGQNVERpdtlkeknpaaaeh 709
Cdd:TIGR01733 293 -VPIGRPLANTRLYVLDDDLR--PVPVGVVGELYIGGPGVARGYLnRPELTAERFVPDPFAGGDGA-------------- 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 710 wfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENV 768
Cdd:TIGR01733 356 ------RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
1006-1306 |
1.26e-118 |
|
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: 372.37 E-value: 1.26e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSR-RVRKVICLVRAKSADQGLQRLRDSGEGRGVWDEEWVKQDRIEAVIGDLAEEKFGLSQ 1084
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRkNVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDELELSRIKVVVGDLSKPNLGLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1085 AEWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAFVAKADEvvqaggkg 1164
Cdd:cd05235 81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDE-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1165 llENDDLEAGRTGLNAGYGQSKWVAEKIIMEAGKKGLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEINN 1244
Cdd:cd05235 153 --ESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPISGA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58269178 1245 AIICCPVDHVARlsSLATLSSSASSAFNIMHVTGHPKIRFNDLLGSLQLYGYDVKRVEYVHW 1306
Cdd:cd05235 231 PLDLSPVDWVAR--AIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-982 |
2.46e-115 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 402.62 E-value: 2.46e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 12 ELNQRLDRWSSRLSA-LPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHILLTSFAI 90
Cdd:PRK12467 235 ERERQLAYWQEQLGGeHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGV--------TLFMVLLASFQT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 91 LLFRYTPDPslVICTSA-NAS-----TKPLL--------LKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHIK 155
Cdd:PRK12467 307 LLHRYSGQS--DIRIGVpNANrnrveTERLIgffvntqvLKAEVDPQASFLELLQQVKRTALGAQAhQDLPFEQLVEALQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 156 PE-----GPLYRVRFfdSTQVESDASSSLTTDLTLFLLAAPSDTPA----------TRTSVPPLYLRLTYNSLLFTQSRI 220
Cdd:PRK12467 385 PErslshSPLFQVMF--NHQNTATGGRDREGAQLPGLTVEELSWARhtaqfdlaldTYESAQGLWAAFTYATDLFEATTI 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 221 tATLESLLQLLSSAASHEPAHPIGALPL-RTPNQSAALPDPAADlDWCGFVGAIPDIFSANAKAHPDRVCVVQselaegq 299
Cdd:PRK12467 463 -ERLATHWRNLLEAIVAEPRRRLGELPLlDAEERARELVRWNAP-ATEYAPDCVHQLIEAQARQHPERPALVF------- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 300 tmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYL 379
Cdd:PRK12467 534 --------GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 380 SVSTPRALLVISSagslapsvsdyisdnLSLRLLVPAiqltssnvtGSRSDAGEDILAPYQQYAQTPAGVVLGPDSPATL 459
Cdd:PRK12467 606 DDSGVRLLLTQSH---------------LLAQLPVPA---------GLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYV 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 460 SFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAE 539
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAA 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 540 WMADSEVTVTHLTPAMGQ-LLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSV 618
Cdd:PRK12467 742 LMADQGVTVLKIVPSHLQaLLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDE 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 NEDStflatqkDLIPAGQGMIDVQLLVVNRtDRNiPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNVErpd 697
Cdd:PRK12467 822 ERDF-------GNVPIGQPLANLGLYILDH-YLN-PVPVGVVGELYIGGAGLARGYHRrPALTAERFVPDPFGADGG--- 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 698 tlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDE 777
Cdd:PRK12467 890 ------------------RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDA 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 778 EKVLVSYFVPIDGDEleglmSASEAADDDEeidlktqmirgvkkyrklirdIREYLKKKLPSYSVPAVYFPLHKLPLNPN 857
Cdd:PRK12467 951 GLQLVAYLVPAAVAD-----GAEHQATRDE---------------------LKAQLRQVLPDYMVPAHLLLLDSLPLTPN 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 858 GKIDKPALPFPDTSllaPAPSASTADHTPTQKTIHDIWLSLLPSPPphITLDENFFDMGGHSILATRLIFEIRKAFVVNA 937
Cdd:PRK12467 1005 GKLDRKALPKPDAS---AVQATFVAPQTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRLGIQV 1079
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 58269178 938 PLGLVFDKPTIAGQAAEIDLLRNADLGGAGDGAIEAEKAVDYAKD 982
Cdd:PRK12467 1080 PLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQE 1124
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
1006-1379 |
2.12e-105 |
|
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: 339.39 E-value: 2.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRVR-KVICLVRAKSADQGLQRLRDSGEGRGVWDEEWVkQDRIEAVIGDLAEEKFGLSQ 1084
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRSTRaKVICLVRADSEEHAMERLREALRSYRLWHENLA-MERIEVVAGDLSKPRLGLSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1085 AEWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAFVAkadevvqaggkG 1164
Cdd:TIGR01746 80 AEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLST-----------G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1165 LLENDDLEAGRTGLNAGYGQSKWVAEKIIMEAGKKGLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEINN 1244
Cdd:TIGR01746 149 VTEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQSPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1245 AIIC-CPVDHVARLSSLATLSSSASSAFNIMHVTGHPKIRFNDLLGSLQLYGYDVKRVEYVHWRTRLEQHVLETQD---N 1320
Cdd:TIGR01746 229 LTEDlTPVDFVARAIVALSSRPAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDTAKRDsrrY 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1321 ALFPLLHFVLD-DLPTSTKSAELDDTNAQNLAAAAGeVRTSGVTEKEIGLYIAWLIRAGF 1379
Cdd:TIGR01746 309 PLLPLLHFTGDaFESDETDTRNLDSRSTAEALEGDG-IREPSITAPLLHLYLQYLKEIGF 367
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-956 |
1.70e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 356.96 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 12 ELNQRLDRWSSRL-SALPSLALPTDYPRPSpaklVEAYQ----SMPIPSALATVLMKLTLEFS-TLFpasglptpyHILL 85
Cdd:PRK12316 235 EQERQLEYWRAQLgEEHPVLELPTDHPRPA----VPSYRgsryEFSIDPALAEALRGTARRQGlTLF---------MLLL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 86 TSFAILLFRYTPDPSL-VICTSANASTKPL-----------LLKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVD 152
Cdd:PRK12316 302 GAFNVLLHRYSGQTDIrVGVPIANRNRAEVegligffvntqVLRSVFDGRTRVATLLAGVKDTVLGAQAhQDLPFERLVE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 153 HIKPE-----GPLYRVRFFDSTQVESDASSSLTTDLTLFLLAAPSDTPA------TRTSVPPLYLRLTYNSLLFtQSRIT 221
Cdd:PRK12316 382 ALKVErslshSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTTQfdltldTYEKGGRLHAALTYATDLF-EARTV 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 222 ATLESLLQLLSSAASHEPAHPIGALPLrtpnqSAALPDPAADLDWcgfvgaipdifSANAKAHPDRVCVVQSELAEGQTM 301
Cdd:PRK12316 461 ERMARHWQNLLRGMVENPQARVDELPM-----LDAEERGQLVEGW-----------NATAAEYPLQRGVHRLFEEQVERT 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 302 MDGPSR--GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYL 379
Cdd:PRK12316 525 PEAPALafGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 380 SVStpRALLVISSAgslapsvsdYISDNLSLRLLVPAIQLtssnvtgsrsdagEDILAPYQQYAQTPAGVVLGPDSPATL 459
Cdd:PRK12316 605 EDS--GVQLLLSQS---------HLGRKLPLAAGVQVLDL-------------DRPAAWLEGYSEENPGTELNPENLAYV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 460 SFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAE 539
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 540 WMADSEVTVTHLTPAMGQ-LLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFaipsv 618
Cdd:PRK12316 741 LINREGVDTLHFVPSMLQaFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW----- 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 nedsTFLATQKDLIPAGQGMIDVQLLVVnrtDRNI-PCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNverp 696
Cdd:PRK12316 816 ----TCVEEGGDSVPIGRPIANLACYIL---DANLePVPVGVLGELYLAGRGLARGYHGrPGLTAERFVPSPFVAG---- 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 697 dtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRrdkd 776
Cdd:PRK12316 885 ------------------ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---- 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 777 EEKVLVSYFVPidgdeleglmsASEAADDDEeidlktqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNP 856
Cdd:PRK12316 943 DGKQLVGYVVL-----------ESEGGDWRE--------------------ALKAHLAASLPEYMVPAQWLALERLPLTP 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 857 NGKIDKPALPFPDTSLLAPAPSASTADhtpTQKTIHDIWLSLLPSPPphITLDENFFDMGGHSILATRLIFEIRKAFVVN 936
Cdd:PRK12316 992 NGKLDRKALPAPEASVAQQGYVAPRNA---LERTLAAIWQDVLGVER--VGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
|
970 980
....*....|....*....|....*...
gi 58269178 937 APLGLvFDKPTI--------AGQAAEID 956
Cdd:PRK12316 1067 SPRDL-FQHQTIrslalvakAGQATAAD 1093
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
274-865 |
7.52e-100 |
|
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: 328.47 E-value: 7.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 274 PDIFSANAKAHPDRVCVVqselaegqtmmdgpsRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCV 353
Cdd:cd17646 1 HALVAEQAARTPDAPAVV---------------DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVAL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 354 MGILKAGGVFSVVDPAYPPSRqtvylsvstpRALLVISSAgslapsvsdyisdnlslrllvPAIQLTSSNVTGSRSDAGE 433
Cdd:cd17646 66 LAVLKAGAAYLPLDPGYPADR----------LAYMLADAG---------------------PAVVLTTADLAARLPAGGD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 434 DILAPYQQYAQTPAG---VVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQ 510
Cdd:cd17646 115 VALLGDEALAAPPATpplVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 511 RDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAM-GQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQ 589
Cdd:cd17646 195 WELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMlRVFLAEPAAGSCASLRRVFCSGEALPPELAARFL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 590 SLAkNVCIINMYGTTETQRAVSYFAIPSVNEDSTflatqkdlIPAGQGMIDVQLLVVnrTDRNIPCAVGEMGEIYVRSGG 669
Cdd:cd17646 275 ALP-GAELHNLYGPTEAAIDVTHWPVRGPAETPS--------VPIGRPVPNTRLYVL--DDALRPVPVGVPGELYLGGVQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 670 LAEGYLD-PTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFR 748
Cdd:cd17646 344 LARGYLGrPALTAERFVPDPFGPG----------------------SRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 749 IELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglmsaSEAADDDEeidlktqmirgvkkyrklird 828
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAG---------AAGPDTAA--------------------- 451
|
570 580 590
....*....|....*....|....*....|....*..
gi 58269178 829 IREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd17646 452 LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-953 |
8.37e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 354.85 E-value: 8.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 12 ELNQRLDRWSSRL-SALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLT-LEFSTLFpasglptpyHILLTSFA 89
Cdd:PRK12467 1300 ERARQLAYWKAQLgGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALArREGVTLF---------MLLLASFQ 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 90 ILLFRYTPDPSL-VICTSAN---ASTKPLL--------LKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHIKP 156
Cdd:PRK12467 1371 TLLHRYSGQDDIrVGVPIANrnrAETEGLIgffvntqvLRAEVDGQASFQQLLQQVKQAALEAQAhQDLPFEQLVEALQP 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 157 E-----GPLYRVRFFDSTQVESDASS----SLTTDLTLFLLAAPSDTPATRTSVPPLYLRLTYNSLLFTQSRITaTLESL 227
Cdd:PRK12467 1451 ErslshSPLFQVMFNHQRDDHQAQAQlpglSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIE-RLAGH 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 228 LQLLSSAASHEPAHPIGALPLRTP----------NQSAALPDPAAdldwcgfvgAIPDIFSANAKAHPDRVCVVqselae 297
Cdd:PRK12467 1530 WLNLLQGLVADPERRLGELDLLDEaerrqilegwNATHTGYPLAR---------LVHQLIEDQAAATPEAVALV------ 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 298 gqtmmdgpsRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTV 377
Cdd:PRK12467 1595 ---------FGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAY 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 378 YLSVSTPRALLVISSagslapsvsdyisdnLSLRLLVPAiqltssnvtGSRS---DAGEDILApyqQYAQTPAGVVLGPD 454
Cdd:PRK12467 1666 MIEDSGIELLLTQSH---------------LQARLPLPD---------GLRSlvlDQEDDWLE---GYSDSNPAVNLAPQ 1718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 455 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTP 534
Cdd:PRK12467 1719 NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDP 1798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVTHLTPAMGQLLsAQATRQI---PTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVS 611
Cdd:PRK12467 1799 EQLIQLIERQQVTTLHFVPSMLQQL-LQMDEQVehpLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVT 1877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 612 YFAIPSVNEdstflaTQKDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFG 690
Cdd:PRK12467 1878 HWTCRRKDL------EGRDSVPIGQPIANLSTYILDASLN--PVPIGVAGELYLGGVGLARGYLNrPALTAERFVADPFG 1949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 691 qnveRPDTlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL 770
Cdd:PRK12467 1950 ----TVGS-----------------RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI 2008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 771 VrRDKDEEKVLVSYFVPIDgdeleglmsASEAADDDEEIDLKTQMirgvkkyrklirdiREYLKKKLPSYSVPAVYFPLH 850
Cdd:PRK12467 2009 A-QDGANGKQLVAYVVPTD---------PGLVDDDEAQVALRAIL--------------KNHLKASLPEYMVPAHLVFLA 2064
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 851 KLPLNPNGKIDKPALPFPDTSLLAPAPSASTadhTPTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFEIR 930
Cdd:PRK12467 2065 RMPLTPNGKLDRKALPAPDASELQQAYVAPQ---SELEQRLAAIWQDVLGL--EQVGLHDNFFELGGDSIISIQVVSRAR 2139
|
970 980
....*....|....*....|...
gi 58269178 931 KAFVVNAPLGLvFDKPTIAGQAA 953
Cdd:PRK12467 2140 QAGIRFTPKDL-FQHQTVQSLAA 2161
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
275-865 |
9.22e-99 |
|
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: 325.31 E-value: 9.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVqselAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:cd12117 1 ELFEEQAARTPDAVAVV----YGDRSL-----------TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLvisSAGSLAPSVSDyisdnlslrLLVPAIQLTSSNvtgsrsdaged 434
Cdd:cd12117 66 AVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL---TDRSLAGRAGG---------LEVAVVIDEALD----------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 435 ilapyqQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFpwMGKRFG-LDENSKYTMLSGIAHDPIQRDM 513
Cdd:cd12117 123 ------AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV--KNTNYVtLGPDDRVLQTSPLAFDASTFEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 514 FTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAK 593
Cdd:cd12117 195 WGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 594 NVCIINMYGTTETQRAVSYFAIPSvnedstfLATQKDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEG 673
Cdd:cd12117 275 GLRLVNGYGPTENTTFTTSHVVTE-------LDEVAGSIPIGRPIANTRVYVLDEDGR--PVPPGVPGELYVGGDGLALG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 674 YL-DPTATAEKFVvnwfgqnverpdtlkeknpaaaEHWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELG 752
Cdd:cd12117 346 YLnRPALTAERFV----------------------ADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELG 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 753 EIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdeleglmsASEAADDDEeidlktqmirgvkkyrklirdIREY 832
Cdd:cd12117 404 EIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV------------AEGALDAAE---------------------LRAF 450
|
570 580 590
....*....|....*....|....*....|...
gi 58269178 833 LKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd12117 451 LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
277-869 |
2.22e-95 |
|
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: 316.19 E-value: 2.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 277 FSANAKAHPDRVCVVqselAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGI 356
Cdd:cd17655 3 FEEQAEKTPDHTAVV----FEDQTL-----------TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 357 LKAGGVFSVVDPAYPPSRqtvylsvstprallvISsagslapsvsdYISDNLSLRLLvpaiqLTSSNVTGSRSDAGEDIL 436
Cdd:cd17655 68 LKAGGAYLPIDPDYPEER---------------IQ-----------YILEDSGADIL-----LTQSHLQPPIAFIGLIDL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 437 APYQQ---YAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDM 513
Cdd:cd17655 117 LDEDTiyhEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 514 FTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSL-A 592
Cdd:cd17655 197 FASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 593 KNVCIINMYGTTETQ-RAVSYFAIPSvnedstflATQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLA 671
Cdd:cd17655 277 TNPTITNAYGPTETTvDASIYQYEPE--------TDQQVSVPIGKPLGNTRIYILDQYGRPQP--VGVAGELYIGGEGVA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 672 EGYLD-PTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIE 750
Cdd:cd17655 347 RGYLNrPELTAEKFVDDPFVPG----------------------ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 751 LGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdeleglmsaseaadDDEEIDLKtqmirgvkkyrklirDIR 830
Cdd:cd17655 405 LGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV------------------SEKELPVA---------------QLR 451
|
570 580 590
....*....|....*....|....*....|....*....
gi 58269178 831 EYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPD 869
Cdd:cd17655 452 EFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
239-988 |
7.15e-93 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 333.46 E-value: 7.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 239 PAHPIGALPLRTPN-QSAALPDpaadldWCGFVGAIPD------IFSANAKAHPDRVCVVQSElaegqtmmdgpsrgrRI 311
Cdd:PRK12316 4518 PQRRLGELQLLEKAeQQRIVAL------WNRTDAGYPAtrcvhqLVAERARMTPDAVAVVFDE---------------EK 4576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVIS 391
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagslapsvsdyisdNLSLRLLVPAiqltssnvtGSRS---DAGEDilapYQQYAQTPAGVVLGPDSPATLSFTSGSTGI 468
Cdd:PRK12316 4657 ---------------HLLQRLPIPD---------GLASlalDRDED----WEGFPAHDPAVRLHPDNLAYVIYTSGSTGR 4708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 469 PKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPtADDIGTPGRLAEWMADSEVTV 548
Cdd:PRK12316 4709 PKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLWDPERLYAEIHEHRVTV 4787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 549 THLTPAMGQLLSAQATRQ--IPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNedstflA 626
Cdd:PRK12316 4788 LVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGD------A 4861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 627 TQKDLIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNverpdtlkeknpa 705
Cdd:PRK12316 4862 CGAAYMPIGTPLGNRSGYVLD--GQLNPLPVGVAGELYLGGEGVARGYLErPALTAERFVPDPFGAP------------- 4926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 706 aaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVtLVRRDKDEEKVLVSYF 785
Cdd:PRK12316 4927 --------GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV-VIAQEGAVGKQLVGYV 4997
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 786 VPIDgdeleglmsaSEAADDDE-EIDLKTQMirgvkkyrklirdiREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPA 864
Cdd:PRK12316 4998 VPQD----------PALADADEaQAELRDEL--------------KAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKA 5053
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 865 LPFPDTSLLApapSASTADHTPTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFD 944
Cdd:PRK12316 5054 LPQPDASLLQ---QAYVAPRSELEQQVAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQ 5128
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 58269178 945 KPTIAgqaaeiDLLRNADLGGAGDgaieaekAVDYAKDVELLSK 988
Cdd:PRK12316 5129 TPTLA------AFVELAAAAGSGD-------DEKFDDLEELLSE 5159
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
273-865 |
7.72e-91 |
|
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: 303.31 E-value: 7.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQSelaegqtmmDGPsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAW---------DGS------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRqtvylsvstprallvissagslapsvsdyisdnlsLRLLVpaiqltssnvtgsrsdag 432
Cdd:cd05918 66 MLAVLKAGGAFVPLDPSHPLQR-----------------------------------LQEIL------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 edilapyqqyAQTPAGVVL--GPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQ 510
Cdd:cd05918 93 ----------QDTGAKVVLtsSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 511 RDMFTPLFLGAQLHVPTADDIgtPGRLAEWMADSEVTVTHLTPAMGQLLSAQatrQIPTLKNAFFVGDVLTKRDCTRLqs 590
Cdd:cd05918 163 LEIFTTLAAGGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVARLLDPE---DVPSLRTLVLGGEALTQSDVDTW-- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 591 lAKNVCIINMYGTTETQRAVSYFAIPSvNEDSTFLatqkdlipaGQGmIDVQLLVVNRTDRNIPCAVGEMGEIYVRSGGL 670
Cdd:cd05918 236 -ADRVRLINAYGPAECTIAATVSPVVP-STDPRNI---------GRP-LGATCWVVDPDNHDRLVPIGAVGELLIEGPIL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 671 AEGYL-DPTATAEKFVvnwfgqnvERPDTLKEKNPaaaehwfGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRI 749
Cdd:cd05918 304 ARGYLnDPEKTAAAFI--------EDPAWLKQEGS-------GRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRV 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 750 ELGEIDTHLSRHPLVRENVT---LVRRDKDEEKVLVSyFVPIDGDELEGLMSASEAADDDEEidlktqmirgvkkYRKLI 826
Cdd:cd05918 369 ELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVA-FVVLDGSSSGSGDGDSLFLEPSDE-------------FRALV 434
|
570 580 590
....*....|....*....|....*....|....*....
gi 58269178 827 RDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05918 435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
277-866 |
6.49e-90 |
|
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: 300.80 E-value: 6.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 277 FSANAKAHPDRVCVVqselAEGQTmmdgpsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGI 356
Cdd:cd17651 1 FERQAARTPDAPALV----AEGRR-----------LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 357 LKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyiSDNLSLRLLVPAIQLTSSNVTGSRSDAGedil 436
Cdd:cd17651 66 LKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT---------------HPALAGELAVELVAVTLLDQPGAAAGAD---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 437 apyqqyaqTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTP 516
Cdd:cd17651 127 --------AEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFST 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 517 LFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQI---PTLKNAFFVGDVLT-----KRDCTRL 588
Cdd:cd17651 199 LCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGvrlAALRYLLTGGEQLVltedlREFCAGL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 589 QSLAknvcIINMYGTTETQRAVSYfaipsvnEDSTFLATQKDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSG 668
Cdd:cd17651 279 PGLR----LHNHYGPTETHVVTAL-------SLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR--PVPPGVPGELYIGGA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 669 GLAEGYL-DPTATAEKFVvnwfgqnverpdtlkeknpaaaEHWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGF 747
Cdd:cd17651 346 GLARGYLnRPELTAERFV----------------------PDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGF 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 748 RIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELeglmSASEaadddeeidlktqmirgvkkyrklir 827
Cdd:cd17651 404 RIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV----DAAE-------------------------- 453
|
570 580 590
....*....|....*....|....*....|....*....
gi 58269178 828 dIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17651 454 -LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
239-953 |
9.47e-90 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 323.65 E-value: 9.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 239 PAHPIGALPLRTPNQSAALPDpaadlDWcgfvgaipdifSANAKAHPDRVCVVQseLAEGQTMM--DGPSR--GRRIFTY 314
Cdd:PRK12467 3062 PAARLGELPTLAAHERRQVLH-----AW-----------NATAAAYPSERLVHQ--LIEAQVARtpEAPALvfGDQQLSY 3123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 315 KQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSag 394
Cdd:PRK12467 3124 AELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH-- 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 395 slapsvsdyisdnLSLRLLVPAiqltssnvTGSRSDAGEDILAPYQQyaQTPAGVVLGpDSPATLSFTSGSTGIPKGVKG 474
Cdd:PRK12467 3202 -------------LLEQLPAPA--------GDTALTLDRLDLNGYSE--NNPSTRVMG-ENLAYVIYTSGSTGKPKGVGV 3257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 475 RHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVpTADDIGTPGRLAEWMADSEVTVTHLTPA 554
Cdd:PRK12467 3258 RHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPA 3336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 555 MGQLLSAQATRQ-IPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSvneDSTFLATQkdlIP 633
Cdd:PRK12467 3337 YLQQFAEDAGGAdCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGG---DAVCEAPY---AP 3410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 634 AGQGMIDVQLLVVnrtDRNI-PCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNVERpdtlkeknpaaaehwf 711
Cdd:PRK12467 3411 IGRPVAGRSIYVL---DGQLnPVPVGVAGELYIGGVGLARGYHQrPSLTAERFVADPFSGSGGR---------------- 3471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 712 girdrMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDEEKVLVSYFVPidgd 791
Cdd:PRK12467 3472 -----LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVP---- 3541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 792 eleglmsaseaadDDEEIDLKTQMirgvkkyrklirdiREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDTS 871
Cdd:PRK12467 3542 -------------ADPQGDWRETL--------------RDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK 3594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 872 L----LAPAPSastadhtpTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPT 947
Cdd:PRK12467 3595 GsreyVAPRSE--------VEQQLAAIWADVLGV--EQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPT 3664
|
....*.
gi 58269178 948 IAGQAA 953
Cdd:PRK12467 3665 IAELAG 3670
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-952 |
2.01e-88 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 319.60 E-value: 2.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 12 ELNQRLDRWSSRL-SALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTlefstlfPASGLpTPYHILLTSFAI 90
Cdd:PRK12316 2784 EGARQLDYWRERLgGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALA-------RREGV-TLFMLLLASFQV 2855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 91 LLFRYTPDPSL-VICTSAN---ASTKPLL--------LKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHIKPE 157
Cdd:PRK12316 2856 LLHRYSGQSDIrVGVPIANrnrAETERLIgffvntqvLRAQVDAQLAFRDLLGQVKEQALGAQAhQDLPFEQLVEALQPE 2935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 158 GPLYRVRFFDSTQVESDASSSLTTDLTLFLLAAPSDTPATRTSVP--------PLYLRLTYNSLLFtQSRITATLESLLQ 229
Cdd:PRK12316 2936 RSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLAldtwesaeGLGASLTYATDLF-DARTVERLARHWQ 3014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 230 LLSSAASHEPAHPIGALPLRTPNQSAALPDpaadlDWcgfvgaipdifSANAKAHPDRVCVVQSELAEGQTMMDGPSR-- 307
Cdd:PRK12316 3015 NLLRGMVENPQRSVDELAMLDAEERGQLLE-----AW-----------NATAAEYPLERGVHRLFEEQVERTPDAVALaf 3078
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRAL 387
Cdd:PRK12316 3079 GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 LVISsagslapsvsdyisdNLSLRLlvpaiqltSSNVTGSRSDAGEDilapyqQYAQTPAGVVLGPDSPATLSFTSGSTG 467
Cdd:PRK12316 3159 LSQS---------------HLRLPL--------AQGVQVLDLDRGDE------NYAEANPAIRTMPENLAYVIYTSGSTG 3209
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 468 IPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVT 547
Cdd:PRK12316 3210 KPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD 3289
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 548 VTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCtrLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDStflat 627
Cdd:PRK12316 3290 VLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADL--QQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDA----- 3362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 628 qkdlIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNverpdtlkeknpaa 706
Cdd:PRK12316 3363 ----VPIGRPIANRACYILD--GSLEPVPVGALGELYLGGEGLARGYHNrPGLTAERFVPDPFVPG-------------- 3422
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 707 aehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLvrrdKDEEKVLVSYFV 786
Cdd:PRK12316 3423 --------ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVV 3490
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 787 PidgdeleglmsaseaadDDEEIDLKtqmirgvkkyrkliRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:PRK12316 3491 P-----------------EDEAGDLR--------------EALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 867 FPDTSLLAPAPSASTadhTPTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLvFDKP 946
Cdd:PRK12316 3540 RPDAALLQQDYVAPV---NELERRLAAIWADVLKL--EQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDL-FQHQ 3613
|
....*.
gi 58269178 947 TIAGQA 952
Cdd:PRK12316 3614 TIQGLA 3619
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
285-865 |
1.85e-87 |
|
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: 292.67 E-value: 1.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVqselAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFS 364
Cdd:cd17643 1 PEAVAVV----DEDRRL-----------TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 VVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaq 444
Cdd:cd17643 66 PIDPAYPVERIAFILADSGPSLLLT------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 445 tpagvvlGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLH 524
Cdd:cd17643 91 -------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 525 VPTADDIGTPGRLAEWMADSEVTVTHLTP-AMGQLLSA--QATRQIPTLKNAFFVGDVLTKRdctRLQSLAKNVC----- 596
Cdd:cd17643 164 VVPYEVARSPEDFARLLRDEGVTVLNQTPsAFYQLVEAadRDGRDPLALRYVIFGGEALEAA---MLRPWAGRFGldrpq 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 IINMYGTTETQRAVSYfaIPSVNEDstflATQKDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYLD 676
Cdd:cd17643 241 LVNMYGITETTVHVTF--RPLDAAD----LPAAAASPIGRPLPGLRVYVLDADGR--PVPPGVVGELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 -PTATAEKFVVNWFGqnverpdtlkeknpaaaehwfGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEID 755
Cdd:cd17643 313 rPELTAERFVANPFG---------------------GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIE 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 756 THLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELeglmsaseaadddeeidlktqmirgvkkyrkLIRDIREYLKK 835
Cdd:cd17643 372 AALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAA-------------------------------DIAELRALLKE 420
|
570 580 590
....*....|....*....|....*....|
gi 58269178 836 KLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd17643 421 LLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
1009-1256 |
2.74e-87 |
|
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: 284.50 E-value: 2.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1009 LTGATGYLGAFILKDLLSRR--VRKVICLVRAKSADQGLQRLRDSGEGRGVWDEEWVKQ-DRIEAVIGDLAEEKFGLSQA 1085
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTpdVKKIYLLVRAKDGESALERLRQELEKYPLFDALLKEAlERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 EWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQ-FSFISsTAVLDAEAFVAKADEVVQAGGKG 1164
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKpFHHVS-TAYVNGERGGLVEEKPYPEGEDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1165 LLENDDLEAGRTGLNAGYGQSKWVAEKIIMEAGKKGLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEINN 1244
Cdd:pfam07993 160 MLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSILG 239
|
250
....*....|....*.
gi 58269178 1245 ----AIICCPVDHVAR 1256
Cdd:pfam07993 240 dpdaVLDLVPVDYVAN 255
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
1006-1256 |
1.44e-86 |
|
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: 282.87 E-value: 1.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRVRKVICLVRAKSADQGLQRLRDSGEGRGVWDEEWvkQDRIEAVIGDLAEEKFGLSQA 1085
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERYGLWLELD--ASRVVVVAGDLTQPRLGLSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 EWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDaeafvakadevvQAGGKGL 1165
Cdd:COG3320 80 EFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAG------------PADRSGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1166 LENDDLEAGrTGLNAGYGQSKWVAEKIIMEAGKKGLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEINNA 1245
Cdd:COG3320 148 FEEDDLDEG-QGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPGLGDA 226
|
250
....*....|..
gi 58269178 1246 II-CCPVDHVAR 1256
Cdd:COG3320 227 RLnLVPVDYVAR 238
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
242-961 |
5.20e-85 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 308.81 E-value: 5.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 242 PIGALPLRTPNQSAALpdpaaDLDWCGFVGAIP------DIFSANAKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYK 315
Cdd:PRK12316 1973 ALGELALLDAGERQRI-----LADWDRTPEAYPrgpgvhQRIAEQAARAPEAIAVVF---------------GDQHLSYA 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 316 QIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVStpRALLVISSAGS 395
Cdd:PRK12316 2033 ELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDS--GAALLLTQRHL 2110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 396 LApsvsdyisdnlslRLLVPAiqltssnvtGSRSDAGEDILApYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGR 475
Cdd:PRK12316 2111 LE-------------RLPLPA---------GVARLPLDRDAE-WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 476 HYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVpTADDIGTPGRLAEWMADSEVTVTHLTPAM 555
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVY 2246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 556 GQLLSAQATRQ--IPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYF-AIPSVNEDSTFlatqkdlI 632
Cdd:PRK12316 2247 LQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWkCRPQDPCGAAY-------V 2319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 633 PAGQGMIDVQLLVVNrTDRNiPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGqnverpdtlkeknpaaaehwf 711
Cdd:PRK12316 2320 PIGRALGNRRAYILD-ADLN-LLAPGMAGELYLGGEGLARGYLNrPGLTAERFVPDPFS--------------------- 2376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 712 GIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVtLVRRDKDEEKVLVSYFVPIDGD 791
Cdd:PRK12316 2377 ASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV-VVAQDGASGKQLVAYVVPDDAA 2455
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 792 ELeglmsaseaadddeeidlktqmirgvkkyrkLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDTS 871
Cdd:PRK12316 2456 ED-------------------------------LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS 2504
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 872 LLApapSASTADHTPTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQ 951
Cdd:PRK12316 2505 QLR---QAYVAPQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAF 2579
|
730
....*....|
gi 58269178 952 AAEIDLLRNA 961
Cdd:PRK12316 2580 AASLESGQTS 2589
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
276-956 |
8.82e-83 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 298.11 E-value: 8.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 276 IFSANAKAH--PDrvcVVQSELAEGQTMM--DGP--SRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEM 349
Cdd:PRK10252 445 LAQVNATAVeiPE---TTLSALVAQQAAKtpDAPalADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 350 VVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRalLVISSAGSLApsvsdyisdnlslRLlvpaiqltssnvtgsrS 429
Cdd:PRK10252 522 TLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS--LLITTADQLP-------------RF----------------A 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 430 DAGEDILAPYQQYAQTPAGVVLG---PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAH 506
Cdd:PRK10252 571 DVPDLTSLCYNAPLAPQGAAPLQlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSF 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 507 DPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAM-----GQLLSAQATRQIPTLKNAFFVGDVLT 581
Cdd:PRK10252 651 DVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMlaafvASLTPEGARQSCASLRQVFCSGEALP 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 582 KRDCTRLQSLAkNVCIINMYGTTETQRAVSYFaiPSVNEDSTflATQKDLIPAGQGMIDVQLLVVNrtDRNIPCAVGEMG 661
Cdd:PRK10252 731 ADLCREWQQLT-GAPLHNLYGPTEAAVDVSWY--PAFGEELA--AVRGSSVPIGYPVWNTGLRILD--ARMRPVPPGVAG 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 662 EIYVRSGGLAEGYLD-PTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADD 740
Cdd:PRK10252 804 DLYLTGIQLAQGYLGrPDLTASRFIADPFAPG----------------------ERMYRTGDVARWLDDGAVEYLGRSDD 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 741 QIKIRGFRIELGEIDTHLSRHPLVRENVTLVR------RDKDEEKVLVSYFVPIDGDELEglmsaseaadddeeidlktq 814
Cdd:PRK10252 862 QLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLD-------------------- 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 815 mirgvkkyrklIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDTSLLAP--APSastadhTPTQKTIH 892
Cdd:PRK10252 922 -----------TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPgrAPK------TGTETIIA 984
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58269178 893 DIWLSLLPSPPPHItlDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEID 956
Cdd:PRK10252 985 AAFSSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
281-865 |
1.52e-81 |
|
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: 275.67 E-value: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVqselaegqtmmdgpSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:cd05945 1 AAANPDRPAVV--------------EGGRTL-TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYPPsrqtvylsvstPRALLVISSAGslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyq 440
Cdd:cd05945 66 HAYVPLDASSPA-----------ERIREILDAAK---------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 441 qyaqtPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLG 520
Cdd:cd05945 89 -----PALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 521 AQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATR---QIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCI 597
Cdd:cd05945 164 ATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFtpeSLPSLRHFLFCGEVLPHKTARALQQRFPDARI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 598 INMYGTTETQRAVSYFAIPsvNEDstflATQKDLIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYL-D 676
Cdd:cd05945 244 YNTYGPTEATVAVTYIEVT--PEV----LDGYDRLPIGYAKPGAKLVILD--EDGRPVPPGEKGELVISGPSVSKGYLnN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 PTATAEKFVVNWfGQnverpdtlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDT 756
Cdd:cd05945 316 PEKTAAAFFPDE-GQ------------------------RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEA 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 757 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDEleglmsaseaadddeeidlktqmirgvkkyRKLIRDIREYLKKK 836
Cdd:cd05945 371 ALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE------------------------------AGLTKAIKAELAER 420
|
570 580
....*....|....*....|....*....
gi 58269178 837 LPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05945 421 LPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
308-866 |
6.89e-79 |
|
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: 267.58 E-value: 6.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRAL 387
Cdd:cd17652 9 GDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 LvissagslapsvsdyisdnlslrllvpaiqlTSsnvtgsrsdagedilapyqqyaqtpagvvlgPDSPATLSFTSGSTG 467
Cdd:cd17652 89 L-------------------------------TT-------------------------------PDNLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 468 IPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVT 547
Cdd:cd17652 107 RPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 548 VTHLTPAmgqLLSAQATRQIPTLKNAFFVGDVltkrdCTR--LQSLAKNVCIINMYGTTETqravsyfaipSVNEDSTFL 625
Cdd:cd17652 187 HVTLPPA---ALAALPPDDLPDLRTLVVAGEA-----CPAelVDRWAPGRRMINAYGPTET----------TVCATMAGP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 626 ATQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGQnverpdtlkeknP 704
Cdd:cd17652 249 LPGGGVPPIGRPVPGTRVYVLDARLRPVP--PGVPGELYIAGAGLARGYLNrPGLTAERFVADPFGA------------P 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 705 AAaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSY 784
Cdd:cd17652 315 GS---------RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAY 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 785 FVPIDGdeleglmsaseAADDDEEIdlktqmirgvkkyrklirdiREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPA 864
Cdd:cd17652 386 VVPAPG-----------AAPTAAEL--------------------RAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
..
gi 58269178 865 LP 866
Cdd:cd17652 435 LP 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
306-865 |
3.61e-78 |
|
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: 266.85 E-value: 3.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 306 SRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPR 385
Cdd:cd12116 7 RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 386 ALLVissagslapsvSDYISDNLSLRLLVPAIqltssnvtgsrsdageDILAPYQQYAQTPAGVVlgPDSPATLSFTSGS 465
Cdd:cd12116 87 LVLT-----------DDALPDRLPAGLPVLLL----------------ALAAAAAAPAAPRTPVS--PDDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 466 TGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSE 545
Cdd:cd12116 138 TGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 546 VTVTHLTPAMGQLLSAQATRQIPTLKnAFFVGDVLTKRDCTRLQSLAKnvCIINMYGTTETqravsyfAIPSVnedSTFL 625
Cdd:cd12116 218 ITVMQATPATWRMLLDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVG--SLWNLYGPTET-------TIWST---AARV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 626 ATQKDLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFGqnverpdtlkeknP 704
Cdd:cd12116 285 TAAAGPIPIGRPLANTQVYVLDAALR--PVPPGVPGELYIGGDGVAQGYLGrPALTAERFVPDPFA-------------G 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 705 AAAehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDkDEEKVLVSY 784
Cdd:cd12116 350 PGS--------RLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 785 FVPIDGdeleglmsasEAADddeeidlktqmirgvkkyrklIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPA 864
Cdd:cd12116 421 VVLKAG----------AAPD---------------------AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKA 469
|
.
gi 58269178 865 L 865
Cdd:cd12116 470 L 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
273-866 |
8.66e-78 |
|
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: 265.45 E-value: 8.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVV----FEDQQL-----------TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTvylsvstprallvissagslapsvsdYISDNLSLRLLVPAiqltssnvtgsrsdag 432
Cdd:cd17644 67 LLAILKAGGAYVPLDPNYPQERLT--------------------------YILEDAQISVLLTQ---------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 edilapyqqyaqtpagvvlgPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRD 512
Cdd:cd17644 105 --------------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEE 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 513 MFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAF---FVG--DVLTKRDCTR 587
Cdd:cd17644 165 IYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLrlvIVGgeAVQPELVRQW 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 588 LQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDstflatQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRS 667
Cdd:cd17644 245 QKNVGNFIQLINVYGPTEATIAATVCRLTQLTER------NITSVPIGRPIANTQVYILDENLQPVP--VGVPGELHIGG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 668 GGLAEGYLD-PTATAEKFVVNWFGQNVErpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRG 746
Cdd:cd17644 317 VGLARGYLNrPELTAEKFISHPFNSSES--------------------ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRG 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 747 FRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPidgdELEGLMSASEaadddeeidlktqmirgvkkyrkli 826
Cdd:cd17644 377 FRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP----HYEESPSTVE------------------------- 427
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 58269178 827 rdIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17644 428 --LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
308-865 |
4.01e-77 |
|
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: 263.17 E-value: 4.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSvstpral 387
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 lvissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsDAGEDILapyqqyaqtpagvVLGPDSPATLSFTSGSTG 467
Cdd:cd17650 82 ------------------------------------------DSGAKLL-------------LTQPEDLAYVIYTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 468 IPKGVKGRHYSLTH-FFPWMgKRFGLDENS-KYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSE 545
Cdd:cd17650 107 KPKGVMVEHRNVAHaAHAWR-REYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 546 VTVTHLTPAMGQLLSAQATRQ---IPTLKNAFFVGDVLTKRD-CTRLQSLAKNVCIINMYGTTETQRAVSYFaipsvnED 621
Cdd:cd17650 186 ITLMESTPALIRPVMAYVYRNgldLSAMRLLIVGSDGCKAQDfKTLAARFGQGMRIINSYGVTEATIDSTYY------EE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 622 STFLATQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFGQNVerpdtlk 700
Cdd:cd17650 260 GRDPLGDSANVPIGRPLPNTAMYVLDERLQPQP--VGVAGELYIGGAGVARGYLnRPELTAERFVENPFAPGE------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 701 eknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKV 780
Cdd:cd17650 331 ---------------RMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEAR 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 781 LVSYFVPidgdeleglmsaseaaddDEEIDLktqmirgvkkyrkliRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:cd17650 396 LCAYVVA------------------AATLNT---------------AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 58269178 861 DKPAL 865
Cdd:cd17650 443 DRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-961 |
3.67e-76 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 280.52 E-value: 3.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 8 LTPEELNQRLDRWSSRLS-ALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHILLT 86
Cdd:PRK05691 857 LAQGEAARQLAYWKAQLGdEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQA--------TLFMVLLA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 87 SFAILLFRYTPDPSLVI-CTSANAS-----------TKPLLLKLDIAAEMTFFDVLRQIMEREQEAQAD-DVPITKLVDH 153
Cdd:PRK05691 929 AFQALLHRYSGQGDIRIgVPNANRPrletqglvgffINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHqDLPFEQLVEA 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 154 I--KPEGPLYRVRFfdsTQVESDASSslttDLTLFLLAAPSDTPATRTSVPPLYL--------RLT----YNSLLFTQSR 219
Cdd:PRK05691 1009 LpqAREQGLFQVMF---NHQQRDLSA----LRRLPGLLAEELPWHSREAKFDLQLhseedrngRLTlsfdYAAELFDAAT 1081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 220 ITAtLESLLQLLSSAASHEPAHPIGALPLRTPNQSAALpdpaadLDWCGFVGA-----IPDIFSANAKAHPDRVCVVqse 294
Cdd:PRK05691 1082 IER-LAEHFLALLEQVCEDPQRALGDVQLLDAAERAQL------AQWGQAPCApaqawLPELLNEQARQTPERIALV--- 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 295 laegqtmMDGPSRGrriftYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSR 374
Cdd:PRK05691 1152 -------WDGGSLD-----YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 375 QTVYLSVSTPRALLVISSAGSLAPSVSDyisdnlslrllVPAIQLTSSNVTGsrsdagedilapyqqYAQTPAGVVLGPD 454
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLLERLPQAEG-----------VSAIALDSLHLDS---------------WPSQAPGLHLHGD 1273
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 455 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTP 534
Cdd:PRK05691 1274 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDP 1353
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVTHLTPAMGQL-----LSAQATRqiptLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRA 609
Cdd:PRK05691 1354 QRIAELVQQYGVTTLHFVPPLLQLfidepLAAACTS----LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAIN 1429
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 610 VSYFAIPSvnEDSTFlatqkdlIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNW 688
Cdd:PRK05691 1430 VTHWQCQA--EDGER-------SPIGRPLGNVLCRVLD--AELNLLPPGVAGELCIGGAGLARGYLGrPALTAERFVPDP 1498
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 689 FGQNVErpdtlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENV 768
Cdd:PRK05691 1499 LGEDGA---------------------RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAA 1557
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 769 TLVRRDKDEEKvLVSYFvpidgdeleglmsASEAADDDEEIDLKTQmirgvkkyrklirdireyLKKKLPSYSVPAVYFP 848
Cdd:PRK05691 1558 VLVREGAAGAQ-LVGYY-------------TGEAGQEAEAERLKAA------------------LAAELPEYMVPAQLIR 1605
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 849 LHKLPLNPNGKIDKPALPFPDTSLlapapSASTADHTPTQKTIHDIWLSLLPSppPHITLDENFFDMGGHSILATRLIFE 928
Cdd:PRK05691 1606 LDQMPLGPSGKLDRRALPEPVWQQ-----REHVEPRTELQQQIAAIWREVLGL--PRVGLRDDFFALGGHSLLATQIVSR 1678
|
970 980 990
....*....|....*....|....*....|...
gi 58269178 929 IRKAFVVNAPLGLVFDKPTIAGQAAEIDLLRNA 961
Cdd:PRK05691 1679 TRQACDVELPLRALFEASELGAFAEQVARIQAA 1711
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
285-866 |
2.80e-75 |
|
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: 258.07 E-value: 2.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVQselaEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFS 364
Cdd:cd17649 1 PDAVALVF----GDQSL-----------SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 VVDPAYPPSRqtvylsvstprallvissagslapsvsdyisdnlsLRLLVpaiqltssnvtgsrSDAGedilapyqqyaq 444
Cdd:cd17649 66 PLDPEYPAER-----------------------------------LRYML--------------EDSG------------ 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 445 tpAGVVLG--PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQ 522
Cdd:cd17649 85 --AGLLLThhPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGAC 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 523 LHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQI----PTLKNAFFVGDVLTKRDCTRLQSLAknVCII 598
Cdd:cd17649 163 VVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGdgrpPSLRLYIFGGEALSPELLRRWLKAP--VRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 599 NMYGTTETqrAVSyfaiPSVNEDSTFLATQKDLIPAGQGMIDVQLLVVNrTDRNiPCAVGEMGEIYVRSGGLAEGYLD-P 677
Cdd:cd17649 241 NAYGPTEA--TVT----PLVWKCEAGAARAGASMPIGRPLGGRSAYILD-ADLN-PVPVGVTGELYIGGEGLARGYLGrP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 678 TATAEKFVVNWFGqnveRPDTlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTH 757
Cdd:cd17649 313 ELTAERFVPDPFG----APGS-----------------RLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 758 LSRHPLVREnVTLVRRDKDEEKVLVSYFVPIDGDELeglmsaseaADDDEEidlktqmirgvkkyrklirdIREYLKKKL 837
Cdd:cd17649 372 LLEHPGVRE-AAVVALDGAGGKQLVAYVVLRAAAAQ---------PELRAQ--------------------LRTALRASL 421
|
570 580
....*....|....*....|....*....
gi 58269178 838 PSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17649 422 PDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
275-865 |
3.89e-74 |
|
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: 254.55 E-value: 3.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:cd12115 3 DLVEAQAARTPDAIALVC---------------GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdaged 434
Cdd:cd12115 68 AVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 435 ilapyqqyaqtpagvvlGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDEnskytmLSGI-AHDPIQRD- 512
Cdd:cd12115 103 -----------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGVlASTSICFDl 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 513 ----MFTPLFLGAQLHVptADDIGTPGRLAewmADSEVTVTHLTP-AMGQLLSAQAtrqIPT-LKNAFFVGDVLTKRDCT 586
Cdd:cd12115 160 svfeLFGPLATGGKVVL--ADNVLALPDLP---AAAEVTLINTVPsAAAELLRHDA---LPAsVRVVNLAGEPLPRDLVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 587 RLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDStflatqkdlIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVR 666
Cdd:cd12115 232 RLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE---------VSIGRPLANTQAYVLDRALQ--PVPLGVPGELYIG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 667 SGGLAEGYL-DPTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIR 745
Cdd:cd12115 301 GAGVARGYLgRPGLTAERFLPDPFGPG----------------------ARLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 746 GFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELeglmsaseaadddeeidlktqmirgvkkyrkL 825
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-------------------------------L 407
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 58269178 826 IRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd12115 408 VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
273-865 |
2.30e-73 |
|
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: 252.42 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmdgpsRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:COG0318 1 LADLLRRAAARHPDRPALV---------------FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdag 432
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 edilapyqqyaqtpagvvlgpdspATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHD-PIQR 511
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 512 DMFTPLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQ---IPTLKNAFFVGDVLTKRDCTRL 588
Cdd:COG0318 159 GLLAPLLAGATLVLLPRFD---PERVLELIERERVTVLFGVPTMLARLLRHPEFArydLSSLRLVVSGGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 589 QSLAkNVCIINMYGTTETQRAVSYfaiPSVNEDSTFLATqkdlipAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSG 668
Cdd:COG0318 236 EERF-GVRIVEGYGLTETSPVVTV---NPEDPGERRPGS------VGRPLPGVEVRIVDEDGR--ELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 669 GLAEGYL-DPTATAEKFvvnwfgqnverpdtlkeknpaaaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGF 747
Cdd:COG0318 304 NVMKGYWnDPEATAEAF-----------------------------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGE 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 748 RIELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVLVsYFVPIDGDELeglmsaseaaddDEEidlktqmirgvkkyrkli 826
Cdd:COG0318 355 NVYPAEVEEVLAAHPGVAEaAVVGVPDEKWGERVVA-FVVLRPGAEL------------DAE------------------ 403
|
570 580 590
....*....|....*....|....*....|....*....
gi 58269178 827 rDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:COG0318 404 -ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
277-745 |
1.52e-71 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 246.07 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 277 FSANAKAHPDRVCVVqselaegqtmmdgPSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGI 356
Cdd:pfam00501 1 LERQAARTPDKTALE-------------VGEGRRL-TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 357 LKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslapSVSDYISDNLSLRLLVPAIQLTSSNVTGSRSDAGEDIL 436
Cdd:pfam00501 67 LKAGAVYVPLNPRLPAEELAYILEDSGAKVLIT---------DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 437 APYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGK----RFGLDENSKYTMLSGIAHD-PIQR 511
Cdd:pfam00501 138 EAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDfGLSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 512 DMFTPLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLL---SAQATRQIPTLKNAFFVGDVLTKRDCTRL 588
Cdd:pfam00501 218 GLLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLleaGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 589 QSLAKNVcIINMYGTTETqravsyfaIPSVNEDSTFLATQKDLIPAGQGMIDVQLLVVNrTDRNIPCAVGEMGEIYVRSG 668
Cdd:pfam00501 298 RELFGGA-LVNGYGLTET--------TGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVD-DETGEPVPPGEPGELCVRGP 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 669 GLAEGYL-DPTATAEKFvvnwfgqnverpdtlkeknpaaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIR 745
Cdd:pfam00501 368 GVMKGYLnDPELTAEAF----------------------------DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
285-866 |
2.85e-70 |
|
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: 244.31 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVQselaEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFS 364
Cdd:cd17656 2 PDAVAVVF----ENQKL-----------TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 VVDPAYPPSRQTVYLSVSTPRalLVISSAgslapSVSDYISDNLSLRLLVPAI--QLTSSNVTgsRSDAGEDILapyqqy 442
Cdd:cd17656 67 PIDPEYPEERRIYIMLDSGVR--VVLTQR-----HLKSKLSFNKSTILLEDPSisQEDTSNID--YINNSDDLL------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 443 aqtpagvvlgpdspaTLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQ 522
Cdd:cd17656 132 ---------------YIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 523 LHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSA--QATRQIPT-LKNAFFVGDVLTKRDCTRLQSLAKNVCIIN 599
Cdd:cd17656 197 LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSerEFINRFPTcVKHIITAGEQLVITNEFKEMLHEHNVHLHN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 600 MYGTTETQRAVSYFAIPSvnedstflATQKDLIPAGQGMIDVQLLVVNRTDRNIPCavGEMGEIYVRSGGLAEGYLD-PT 678
Cdd:cd17656 277 HYGPSETHVVTTYTINPE--------AEIPELPPIGKPISNTWIYILDQEQQLQPQ--GIVGELYISGASVARGYLNrQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 679 ATAEKFVVNWFGQNVerpdtlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHL 758
Cdd:cd17656 347 LTAEKFFPDPFDPNE----------------------RMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 759 SRHPLVRENVTLVRRDKDEEKVLVSYFVPIdgdeleglmsaseaadddEEIDlktqmirgvkkyrklIRDIREYLKKKLP 838
Cdd:cd17656 405 LNHPGVSEAVVLDKADDKGEKYLCAYFVME------------------QELN---------------ISQLREYLAKQLP 451
|
570 580
....*....|....*....|....*...
gi 58269178 839 SYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17656 452 EYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
276-866 |
7.49e-70 |
|
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: 242.07 E-value: 7.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 276 IFSANAKAHPDRVCVVQselaEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMG 355
Cdd:cd17645 3 LFEEQVERTPDHVAVVD----RGQSL-----------TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 356 ILKAGGVFSVVDPAYPPSRQTVYLSVSTprALLVISSAGSLApsvsdyisdnlslrllvpaiqltssnvtgsrsdagedi 435
Cdd:cd17645 68 VLKAGGAYVPIDPDYPGERIAYMLADSS--AKILLTNPDDLA-------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 436 lapYQQYaqtpagvvlgpdspatlsfTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFT 515
Cdd:cd17645 108 ---YVIY-------------------TSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 516 PLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHL-TPAMGQLLSAQATrqipTLKNAFFVGDVLTKrdctrlqSLAKN 594
Cdd:cd17645 166 HLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLpTGAAEQFMQLDNQ----SLRVLLTGGDKLKK-------IERKG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 595 VCIINMYGTTETQRAVSYFAIPSVNEDstflatqkdlIPAGQGMIDVQLLVVNRTdrNIPCAVGEMGEIYVRSGGLAEGY 674
Cdd:cd17645 235 YKLVNNYGPTENTVVATSFEIDKPYAN----------IPIGKPIDNTRVYILDEA--LQLQPIGVAGELCIAGEGLARGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 675 LD-PTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGE 753
Cdd:cd17645 303 LNrPELTAEKFIVHPFVPG----------------------ERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 754 IDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPidgdeleglmsaseaaddDEEIDlktqmirgvkkyrklIRDIREYL 833
Cdd:cd17645 361 IEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA------------------PEEIP---------------HEELREWL 407
|
570 580 590
....*....|....*....|....*....|...
gi 58269178 834 KKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17645 408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
285-865 |
4.00e-69 |
|
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: 241.02 E-value: 4.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVQSElaegQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFS 364
Cdd:cd12114 1 PDATAVICGD----GTL-----------TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 VVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDYISDNLSLrllvpaiqltssnvtgsrsDAGEDILAPyqqyaq 444
Cdd:cd12114 66 PVDIDQPAARREAILADAGARLVLTDGPDAQLDVAVFDVLILDLDA-------------------LAAPAPPPP------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 445 tpagVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLH 524
Cdd:cd12114 121 ----VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 525 VPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLL---SAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMY 601
Cdd:cd12114 197 LPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLldvLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 602 GTTETQRAVSYFAIPSVNEDSTflatqkdLIPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYL-DPTAT 680
Cdd:cd12114 277 GATEASIWSIYHPIDEVPPDWR-------SIPYGRPLANQRYRVLDPRGR--DCPDWVPGELWIGGRGVALGYLgDPELT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 681 AEKFVvnwfgqnvERPDtlkeknpaaaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSR 760
Cdd:cd12114 348 AARFV--------THPD----------------GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 761 HPLVRENVTLVRRDkDEEKVLVSYFVPIDGDEleglmSASEAAdddeeidlktqmirgvkkyrklirdIREYLKKKLPSY 840
Cdd:cd12114 404 HPGVARAVVVVLGD-PGGKRLAAFVVPDNDGT-----PIAPDA-------------------------LRAFLAQTLPAY 452
|
570 580
....*....|....*....|....*
gi 58269178 841 SVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd12114 453 MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
275-865 |
1.93e-65 |
|
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: 228.73 E-value: 1.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVvqsELAEGQtmmdgpsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:cd17653 1 DAFERIAAAHPDAVAV---ESLGGS------------LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAIL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdaged 434
Cdd:cd17653 66 AILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 435 ilapyqqyaqtpagvvlgPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMF 514
Cdd:cd17653 104 ------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 515 TPLFLGAQLHVPT-ADDIGTPGRlaewmadsEVTVTHLTPAMGQLLSAQatrQIPTLKNAFFVGDVLTkrdctrlQSLAK 593
Cdd:cd17653 166 STLCNGGTLVLADpSDPFAHVAR--------TVDALMSTPSILSTLSPQ---DFPNLKTIFLGGEAVP-------PSLLD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 594 ----NVCIINMYGTTETQRAVSYFAI-PSVNedstflatqkdlIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSG 668
Cdd:cd17653 228 rwspGRRLYNAYGPTECTISSTMTELlPGQP------------VTIGKPIPNSTCYILDADLQPVP--EGVVGEICISGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 669 GLAEGYL-DPTATAEKFVVNWFGQNVerpdtlkeknpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGF 747
Cdd:cd17653 294 QVARGYLgNPALTASKFVPDPFWPGS----------------------RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGF 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 748 RIELGEI-DTHLSRHPLVRENVTLVRRDkdeekVLVSYFVPIDGDeleglmsaseaadddeeidlktqmirgvkkyrklI 826
Cdd:cd17653 352 RINLEEIeEVVLQSQPEVTQAAAIVVNG-----RLVAFVTPETVD----------------------------------V 392
|
570 580 590
....*....|....*....|....*....|....*....
gi 58269178 827 RDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd17653 393 DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
12-953 |
2.21e-65 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 246.23 E-value: 2.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 12 ELNQRLDRWSSRL-SALPSLALPTDYPRPSpaklVEAYQSMPIPSALATVLMKLTLEFSTlfpASGLpTPYHILLTSFAI 90
Cdd:PRK05691 1914 ERQRQLDYWKAQLgNEHPLLELPADRPRPP----VQSHRGELYRFDLSPELAARVRAFNA---QRGL-TLFMTMTATLAA 1985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 91 LLFRYTPDPSLVICTSANASTKP------------LLLKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHIKPE 157
Cdd:PRK05691 1986 LLYRYSGQRDLRIGAPVANRIRPesegligaflntQVLRCQLDGQMSVSELLEQVRQTVIEGQShQDLPFDHLVEALQPP 2065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 158 -----GPLYRV------------RFFDSTQVESDASsslttdltlfllaapsDTPATRTSvppLYLR-----------LT 209
Cdd:PRK05691 2066 rsaayNPLFQVmcnvqrwefqqsRQLAGMTVEYLVN----------------DARATKFD---LNLEvtdldgrlgccLT 2126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 210 YNSLLFTQSRItATLESLLQLLSSAASHEPAHPIGALPLRTPNQSAALPDP------AADLDWCgfvgaIPDIFSANAKA 283
Cdd:PRK05691 2127 YSRDLFDEPRI-ARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSlageagEARLDQT-----LHGLFAAQAAR 2200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 284 HPDRVCVVQSelaeGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVF 363
Cdd:PRK05691 2201 TPQAPALTFA----GQTL-----------SYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 364 SVVDPAYPPSRQTVYLSVSTPRALL----VISSAGSLAPSVSDYisdnlSLrllvpaiqltssnvtgsrsdagEDILAPY 439
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLLsdraLFEALGELPAGVARW-----CL----------------------EDDAAAL 2318
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 440 QQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFL 519
Cdd:PRK05691 2319 AAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLC 2398
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 520 GAQLhVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFV--GDVLTKRDCTRLQSLAKNVCI 597
Cdd:PRK05691 2399 GARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCItgGEALTGEHLQRIRQAFAPQLF 2477
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 598 INMYGTTETqrAVSYFAIPSvnedstflatqKDLIPAGQGMIDVQLLVVNRT----DRNI-PCAVGEMGEIYVRSGGLAE 672
Cdd:PRK05691 2478 FNAYGPTET--VVMPLACLA-----------PEQLEEGAASVPIGRVVGARVayilDADLaLVPQGATGELYVGGAGLAQ 2544
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 673 GYLD-PTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIEL 751
Cdd:PRK05691 2545 GYHDrPGLTAERFVADPFAAD---------------------GGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIEL 2603
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 752 GEIDTHLSRHPLVRENVTLVrRDKDEEKVLVSYfvpidgdelegLMSASEAADDDEEIDLKTQmirgvkkyrklirdIRE 831
Cdd:PRK05691 2604 GEIESRLLEHPAVREAVVLA-LDTPSGKQLAGY-----------LVSAVAGQDDEAQAALREA--------------LKA 2657
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 832 YLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDtslLAPAPSASTADHTPTQKTIHDIWLSLLPSppPHITLDEN 911
Cdd:PRK05691 2658 HLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD---PELNRQAYQAPRSELEQQLAQIWREVLNV--ERVGLGDN 2732
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 58269178 912 FFDMGGHSILATRLIFEIRKAFVVNAPLGLvFDKPTIAGQAA 953
Cdd:PRK05691 2733 FFELGGDSILSIQVVSRARQLGIHFSPRDL-FQHQTVQTLAA 2773
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
285-866 |
3.03e-64 |
|
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: 226.13 E-value: 3.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVQSElaegqtmmdgpsrgRRIfTYKQIDEASNILAHALLKNGLQRG-EVVMVYAARSVEMVVCVMGILKAGGVF 363
Cdd:cd17648 1 PDRVAVVYGD--------------KRL-TYRELNERANRLAHYLLSVAEIRPdDLVGLVLDKSELMIIAILAVWKAGAAY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 364 SVVDPAYPPSRQTVYLSVStpRALLVISSAGSLApsvsdYISdnlslrllvpaiqltssnvtgsrsdagedilapyqqya 443
Cdd:cd17648 66 VPIDPSYPDERIQFILEDT--GARVVITNSTDLA-----YAI-------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 444 qtpagvvlgpdspatlsFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTML--SGIAHDPIQRDMFTPLFLGA 521
Cdd:cd17648 101 -----------------YTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 522 QLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAmgqLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVcIINMY 601
Cdd:cd17648 164 KLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGL-IINAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 602 GTTETqravsyfAIPSVNedSTFLATQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYLD-PTAT 680
Cdd:cd17648 240 GPTET-------TVTNHK--RFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP--VGAVGELYLGGDGVARGYLNrPELT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 681 AEKFVVNWFGQNVERPDtlkeknpaaaehwfGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSR 760
Cdd:cd17648 309 AERFLPNPFQTEQERAR--------------GRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALAS 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 761 HPLVRENVTLVRRDKD-----EEKVLVSYFVPIdgdelEGLMSASeaadddeeidlktqmirgvkkyrklirDIREYLKK 835
Cdd:cd17648 375 YPGVRECAVVAKEDASqaqsrIQKYLVGYYLPE-----PGHVPES---------------------------DLLSFLRA 422
|
570 580 590
....*....|....*....|....*....|.
gi 58269178 836 KLPSYSVPAVYFPLHKLPLNPNGKIDKPALP 866
Cdd:cd17648 423 KLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
276-963 |
8.11e-61 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 231.21 E-value: 8.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 276 IFSANAKAHPDRV---CVVQSelaegqtmmdgpsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK05691 3725 LFEAQVAAHPQRIaasCLDQQ------------------WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGM 3786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVS-TPraLLVISSA-GSLAPSVSDYISDNLSLRLLVpaiqltssnvtgsrsd 430
Cdd:PRK05691 3787 IVGSFKAGAGYLPLDPGLPAQRLQRIIELSrTP--VLVCSAAcREQARALLDELGCANRPRLLV---------------- 3848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 431 aGEDILApyQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVkgrhyslthffpwMGKRFGLDEN--SKYTMLSGIAHDP 508
Cdd:PRK05691 3849 -WEEVQA--GEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGV-------------MVEQRGMLNNqlSKVPYLALSEADV 3912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 IQRD------------MFTPLFlGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFV 576
Cdd:PRK05691 3913 IAQTasqsfdisvwqfLAAPLF-GARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPT 3991
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 577 GDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLatqkdliPAGQGMIDVQLLVVNRTDRNIPca 656
Cdd:PRK05691 3992 GEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYL-------PIGSPTDNNRLYLLDEALELVP-- 4062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 657 VGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFGqnverpdtlkeknpaaaehwfGIRDRMYRSGDLGRYLPDGRVECT 735
Cdd:PRK05691 4063 LGAVGELCVAGTGVGRGYVgDPLRTALAFVPHPFG---------------------APGERLYRTGDLARRRSDGVLEYV 4121
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 736 GRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDEEKVLVSYFVPIDGdeleglmsaseAADDDEeidlktqm 815
Cdd:PRK05691 4122 GRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV-QEGVNGKHLVGYLVPHQT-----------VLAQGA-------- 4181
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 816 irgvkkyrkLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPALPFPDTSLLapAPSASTADHTPTQKTIHDIW 895
Cdd:PRK05691 4182 ---------LLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL--QSQAYLAPRNELEQTLATIW 4250
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 896 LSLLPSppPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEIDLLRNADL 963
Cdd:PRK05691 4251 ADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGSAI 4316
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
281-865 |
2.86e-53 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 195.50 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQselaEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:PRK04813 12 AQTQPDFPAYDY----LGEKL-----------TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYPPSRQTVYLSVSTPRALLvissagslapSVSDYISDNLSLRLLvpaiqlTSSNVtgsrsdagEDILApyQ 440
Cdd:PRK04813 77 HAYIPVDVSSPAERIEMIIEVAKPSLII----------ATEELPLEILGIPVI------TLDEL--------KDIFA--T 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 441 QYAQTPAGVVLGPDSPATLsFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSkyTMLsgiAHDPIQRDM-----FT 515
Cdd:PRK04813 131 GNPYDFDHAVKGDDNYYII-FTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGP--QFL---NQAPYSFDLsvmdlYP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 516 PLFLGAQLHVPTADDIGTPGRLAEWMADSEVTVTHLTPA---MGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLA 592
Cdd:PRK04813 205 TLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 593 KNVCIINMYGTTETQRAVSyfAIPSVNEdstfLATQKDLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAE 672
Cdd:PRK04813 285 PSATIYNTYGPTEATVAVT--SIEITDE----MLDQYKRLPIGYAKPDSPLLIIDEEGTKLP--DGEQGEIVISGPSVSK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 673 GYL-DPTATAEKFVvnwfgqnverpdTLKEKnpaaaehwfgirdRMYRSGDLGrYLPDGRVECTGRADDQIKIRGFRIEL 751
Cdd:PRK04813 357 GYLnNPEKTAEAFF------------TFDGQ-------------PAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIEL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 752 GEIDTHLSRHPLVRENVTlVRRDKDeEKV--LVSYFVPIDGdeleglmsaseaaDDDEEIDLkTQMirgvkkyrklirdI 829
Cdd:PRK04813 411 EEIEQNLRQSSYVESAVV-VPYNKD-HKVqyLIAYVVPKEE-------------DFEREFEL-TKA-------------I 461
|
570 580 590
....*....|....*....|....*....|....*.
gi 58269178 830 REYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
456-861 |
3.89e-50 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 181.33 E-value: 3.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 456 PATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtPG 535
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 536 RLAEWMADSEVTVTHLTPAMGQLL---SAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVcIINMYGTTETQRAVSY 612
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLlkaPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 613 FAIPSVNEDSTflatqkdliPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYLdptataekfvvnwfgqn 692
Cdd:cd04433 158 GPPDDDARKPG---------SVGRPVPGVEVRIVDPDGG--ELPPGEIGELVVRGPSVMKGYW----------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 693 verpdtlkeKNPAAAEHWFgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVR 772
Cdd:cd04433 210 ---------NNPEATAAVD--EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 773 RDKDEEKVLVSYFVPIDGDELeglmsaseaaddDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKL 852
Cdd:cd04433 279 PDPEWGERVVAVVVLRPGADL------------DAE-------------------ELRAHVRERLAPYKVPRRVVFVDAL 327
|
....*....
gi 58269178 853 PLNPNGKID 861
Cdd:cd04433 328 PRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
310-860 |
8.87e-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: 155.06 E-value: 8.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 310 RIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLV 389
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 390 issagslAPSVSDYISDNLSLRLLVPAIQLTSSNVTGSRSdaGEDILAPYQQYAQT--PAGVVLGPDSPATLSFTSGSTG 467
Cdd:cd05911 89 -------DPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLS--IEDLLSPTLGEEDEdlPPPLKDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 468 IPKGVKGRHYSLT--HFFPWMgkRFGLDENSKYTMLsgiahdpiqrdMFTPLF-------------LGAQLHVPTADDIG 532
Cdd:cd05911 160 LPKGVCLSHRNLIanLSQVQT--FLYGNDGSNDVIL-----------GFLPLYhiyglfttlasllNGATVIIMPKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 533 TPGRLAEwmaDSEVTVTHLTPAMGQLL--SAQATR-QIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRA 609
Cdd:cd05911 227 LFLDLIE---KYKITFLYLVPPIAAALakSPLLDKyDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 610 VSYFAIPSVNEDSTflatqkdlipaGQGMIDVQLLVVNrTDRNIPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFvvnw 688
Cdd:cd05911 304 LTVNPDGDDKPGSV-----------GRLLPNVEAKIVD-DDGKDSLGPNEPGEICVRGPQVMKGYYnNPEATKETF---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 689 fgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENV 768
Cdd:cd05911 368 -----------------DEDGWL-------HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAA 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 769 TLVRRDKDEEKVLVSYFVPIDGDELeglmsaSEAadddeeidlktqmirgvkkyrklirDIREYLKKKLPSYS--VPAVY 846
Cdd:cd05911 424 VIGIPDEVSGELPRAYVVRKPGEKL------TEK-------------------------EVKDYVAKKVASYKqlRGGVV 472
|
570
....*....|....
gi 58269178 847 FpLHKLPLNPNGKI 860
Cdd:cd05911 473 F-VDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
273-865 |
4.05e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 153.80 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmdgpsRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVY---------------FDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSrQTVY-LSVSTPRALLVissAGSLAPSVSDyISDNLSLRLLVpaIQLTSSNVTGSRSDA 431
Cdd:PRK06187 73 YFAVPKIGAVLHPINIRLKPE-EIAYiLNDAEDRVVLV---DSEFVPLLAA-ILPQLPTVRTV--IVEGDGPAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 432 G--EDILApyQQYAqTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKY--------TML 501
Cdd:PRK06187 146 GeyEELLA--AASD-TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYlvivpmfhVHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 502 SGIahdpiqrdMFTPLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQ---ATRQIPTLKNAFFVGD 578
Cdd:PRK06187 223 WGL--------PYLALMAGAKQVIPRRFD---PENLLDLIETERVTFFFAVPTIWQMLLKApraYFVDFSSLRLVIYGGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 579 VLTKRDCTRLQSLAKnVCIINMYGTTETQRAVSyFAIPsvnEDSTFLATQKdLIPAGQGMIDVQLLVVNRTDRNIPCAVG 658
Cdd:PRK06187 292 ALPPALLREFKEKFG-IDLVQGYGMTETSPVVS-VLPP---EDQLPGQWTK-RRSAGRPLPGVEARIVDDDGDELPPDGG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 659 EMGEIYVRSGGLAEGYL-DPTATAEKFVVNWfgqnverpdtlkeknpaaaehwfgirdrmYRSGDLGRYLPDGRVECTGR 737
Cdd:PRK06187 366 EVGEIIVRGPWLMQGYWnRPEATAETIDGGW-----------------------------LHTGDVGYIDEDGYLYITDR 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 738 ADDQIKIRGFRIELGEIDTHLSRHPLVREN-VTLVRRDKDEEKVLVsYFVPIDGDELeglmsaseaaddDEEidlktqmi 816
Cdd:PRK06187 417 IKDVIISGGENIYPRELEDALYGHPAVAEVaVIGVPDEKWGERPVA-VVVLKPGATL------------DAK-------- 475
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 58269178 817 rgvkkyrklirDIREYLKKKLPSYSVP-AVYFpLHKLPLNPNGKIDKPAL 865
Cdd:PRK06187 476 -----------ELRAFLRGRLAKFKLPkRIAF-VDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
280-862 |
1.07e-35 |
|
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: 141.98 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 280 NAKAHPDRVCVVQselaegqtmmdgpsRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKA 359
Cdd:cd17631 4 RARRHPDRTALVF--------------GGRSL-TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 360 GGVFSVVDPayppsrqtvylsvstprallvissagslapsvsdyisdnlslRLLVPAIqltssnvtgsrsdagEDILApy 439
Cdd:cd17631 69 GAVFVPLNF------------------------------------------RLTPPEV---------------AYILA-- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 440 qqyaQTPAGVVLgpDSPATLSFTSGSTGIPKGVKGRHYSLTHffpwmgkrfgldenskYTMLSGIAHDPIQRDMF---TP 516
Cdd:cd17631 90 ----DSGAKVLF--DDLALLMYTSGTTGRPKGAMLTHRNLLW----------------NAVNALAALDLGPDDVLlvvAP 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 517 LFLGAQLHVPTADDI---GT--------PGRLAEWMADSEVTVTHLTPAMGQLLSAQ---ATRQIPTLKnAFFVGD---- 578
Cdd:cd17631 148 LFHIGGLGVFTLPTLlrgGTvvilrkfdPETVLDLIERHRVTSFFLVPTMIQALLQHprfATTDLSSLR-AVIYGGapmp 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 579 VLTKRDCtrlqsLAKNVCIINMYGTTETQRAVsyfaipsvnedsTFL---ATQKDLIPAGQGMIDVQLLVVNRTDRniPC 655
Cdd:cd17631 227 ERLLRAL-----QARGVKFVQGYGMTETSPGV------------TFLspeDHRRKLGSAGRPVFFVEVRIVDPDGR--EV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 656 AVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVEC 734
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNrPEATAAAFRDGWF-----------------------------HTGDLGRLDEDGYLYI 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 735 TGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELeglmsaseaaddDEEidlktq 814
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL------------DED------ 400
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 58269178 815 mirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDK 862
Cdd:cd17631 401 -------------ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
1007-1256 |
2.20e-35 |
|
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: 137.11 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLLSRrVRKVICLVRAKSADQGLQRLRDSGegrgvwdeewVKQDRIEAVIGDLAEEKFGLSQAE 1086
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLEN-GFKVLVLVRSESLGEAHERIEEAG----------LEADRVRVLEGDLTQPNLGLSAAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1087 WDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeafvakadevvqAG-GKGL 1165
Cdd:cd05263 70 SRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYV---------------AGnREGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1166 LENDDLEAGRTGLNaGYGQSKWVAEKIIMEAGKKgLSGWILRPGYVLGHSQTAVTNTDDFIWRMVKGCVQLGLIPEI--- 1242
Cdd:cd05263 135 IRETELNPGQNFKN-PYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLPMpgn 212
|
250
....*....|....*
gi 58269178 1243 -NNAIICCPVDHVAR 1256
Cdd:cd05263 213 kGARLNLVPVDYVAD 227
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
275-860 |
3.45e-35 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 142.94 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVqselaegqtmMDGPSRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:COG0365 13 NCLDRHAEGRGDKVALI----------WEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRAllVISSAGSLAPSVSDYISDNLSlrllvPAIQLTSS-------NVTGS 427
Cdd:COG0365 83 ACARIGAVHSPVFPGFGAEALADRIEDAEAKV--LITADGGLRGGKVIDLKEKVD-----EALEELPSlehvivvGRTGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 428 RSDAGEDI----LAPYQqyAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKR-FGLDENSKY---- 498
Cdd:COG0365 156 DVPMEGDLdwdeLLAAA--SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFwcta 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 499 -----TMLSGIahdpiqrdMFTPLFLGA-QLHVPTADDIGTPGRLAEWMADSEVTVTHLTPA-----MGQLLSAQATRQI 567
Cdd:COG0365 234 digwaTGHSYI--------VYGPLLNGAtVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTairalMKAGDEPLKKYDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 568 PTLKNAFFVGDVLTK------RDCTrlqslakNVCIINMYGTTETqraVSYFAIPSVNEDSTFLATQKdlipAGQGMiDV 641
Cdd:COG0365 306 SSLRLLGSAGEPLNPevwewwYEAV-------GVPIVDGWGQTET---GGIFISNLPGLPVKPGSMGK----PVPGY-DV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 642 QllVVNRTDRniPCAVGEMGEIYVRSG--GLAEGYL-DPTATAEKFvvnwfgqnverpdtlkeknpaaaehwFGIRDRMY 718
Cdd:COG0365 371 A--VVDEDGN--PVPPGEEGELVIKGPwpGMFRGYWnDPERYRETY--------------------------FGRFPGWY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 719 RSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREN-VTLVrrdKDEEK--VLVSYFVPIDGdeleg 795
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAaVVGV---PDEIRgqVVKAFVVLKPG----- 492
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58269178 796 lmsaseAADDDEeidlktqmirgvkkyrkLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:COG0365 493 ------VEPSDE-----------------LAKELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
309-866 |
3.40e-25 |
|
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: 110.07 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 309 RRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALL 388
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 389 VissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaqtpagvvlgpdSPATLSFTSGSTGI 468
Cdd:cd05934 81 V-----------------------------------------------------------------DPASILYTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 469 PKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMlsgiahdpiqrdmFTPLF-LGAQLHVPTADdIGTPGRLA--------E 539
Cdd:cd05934 96 PKGVVITHANLTFAGYYSARRFGLGEDDVYLT-------------VLPLFhINAQAVSVLAA-LSVGATLVllprfsasR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 540 WMAD---SEVTVTHLTPAMGQLLSAQATRQIPT---LKNAFF-VGDVLTKRD-CTRLqslakNVCIINMYGTTETQRAVs 611
Cdd:cd05934 162 FWSDvrrYGATVTNYLGAMLSYLLAQPPSPDDRahrLRAAYGaPNPPELHEEfEERF-----GVRLLEGYGMTETIVGV- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 612 yfAIPSVNEDSTFlatqkdliPAGQGMIDVQLLVVNRTDRniPCAVGEMGEIYVRSG---GLAEGYL-DPTATAEKFvvn 687
Cdd:cd05934 236 --IGPRDEPRRPG--------SIGRPAPGYEVRIVDDDGQ--ELPAGEPGELVIRGLrgwGFFKGYYnMPEATAEAM--- 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 688 wfgqnverpdtlkeknpaaaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE- 766
Cdd:cd05934 301 --------------------------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREa 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 767 NVTLVRRDKDEEKVLVsYFVPIDGDELeglmsaseaaddDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVP-AV 845
Cdd:cd05934 355 AVVAVPDEVGEDEVKA-VVVLRPGETL------------DPE-------------------ELFAFCEGQLAYFKVPrYI 402
|
570 580
....*....|....*....|.
gi 58269178 846 YFpLHKLPLNPNGKIDKPALP 866
Cdd:cd05934 403 RF-VDDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
306-865 |
4.23e-25 |
|
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: 110.86 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 306 SRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPR 385
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 386 ALLVissagslaPSVSDYISDNLSLRLLVPAIQLTSSNVTGSRSDAGEDI-LAPYQQYAQTPAGVVLGPDsPATLSFTSG 464
Cdd:cd05926 89 LVLT--------PKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLsNLLADKKNAKSEGVPLPDD-LALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 465 STGIPKGVKGRHYSL---------THffpwmgkRFGLDENSKYTMlsgiahdPiqrdMF----------TPLFLGAQLHV 525
Cdd:cd05926 160 TTGRPKGVPLTHRNLaasatnitnTY-------KLTPDDRTLVVM-------P----LFhvhglvasllSTLAAGGSVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 526 PtaddigtPGRLA----EWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAF-FVgdvltkRDCTrlQSLAKNVC---- 596
Cdd:cd05926 222 P-------PRFSAstfwPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLrFI------RSCS--ASLPPAVLeale 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 ------IINMYGTTETQRAVSYFAIP-------SVNedstflatqkdlIPAGqgmidVQLLVVNRTDRNIPcaVGEMGEI 663
Cdd:cd05926 287 atfgapVLEAYGMTEAAHQMTSNPLPpgprkpgSVG------------KPVG-----VEVRILDEDGEILP--PGVVGEI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 664 YVRSGGLAEGYL-DPTATAEK-FVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQ 741
Cdd:cd05926 348 CLRGPNVTRGYLnNPEANAEAaFKDGWF-----------------------------RTGDLGYLDADGYLFLTGRIKEL 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 742 IKIRGFRIELGEIDTHLSRHPLVRENVTlvrrdkdeekvlvsYFVPidgDELEGlmsaseaadddEEIDLKTQMirgVKK 821
Cdd:cd05926 399 INRGGEKISPLEVDGVLLSHPAVLEAVA--------------FGVP---DEKYG-----------EEVAAAVVL---REG 447
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 58269178 822 YRKLIRDIREYLKKKLPSYSVPA-VYFpLHKLPLNPNGKIDKPAL 865
Cdd:cd05926 448 ASVTEEELRAFCRKHLAAFKVPKkVYF-VDELPKTATGKIQRRKV 491
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
312-865 |
4.93e-25 |
|
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: 110.21 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVfsvvdpayppsrqtvylSVSTPRALlvis 391
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAI-----------------AVPLFALF---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdaGEDILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKG 471
Cdd:cd05971 66 ----------------------------------------GPEALEYRLSNSGASALVTDGSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRH---------YSLTH-FFP-------------WMGKRFGLDENSKYTMLSGIAHDPIQRDmftplflgaqlhvpta 528
Cdd:cd05971 106 ALHAHrvllghlpgVQFPFnLFPrdgdlywtpadwaWIGGLLDVLLPSLYFGVPVLAHRMTKFD---------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 529 ddigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKN--AFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTET 606
Cdd:cd05971 170 -----PKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKlrAIATGGESLGEELLGWAREQFGVEVNEFYGQTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 607 QRAVSYFAipsvnedstflatqkDLIPAGQGMI-------DVQLLvvnrTDRNIPCAVGEMGEIYVR---SGGLAEGYLD 676
Cdd:cd05971 245 NLVIGNCS---------------ALFPIKPGSMgkpipghRVAIV----DDNGTPLPPGEVGEIAVElpdPVAFLGYWNN 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDT 756
Cdd:cd05971 306 PSATEKKMAGDWL-----------------------------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 757 HLSRHPLVReNVTLVRRDKDEEKVLVSYFVpidgdelegLMSASEAADDdeeidlktqmirgvkkyrKLIRDIREYLKKK 836
Cdd:cd05971 357 CLLKHPAVL-MAAVVGIPDPIRGEIVKAFV---------VLNPGETPSD------------------ALAREIQELVKTR 408
|
570 580 590
....*....|....*....|....*....|
gi 58269178 837 LPSYSVP-AVYFPlHKLPLNPNGKIDKPAL 865
Cdd:cd05971 409 LAAHEYPrEIEFV-NELPRTATGKIRRREL 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
312-865 |
9.53e-25 |
|
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: 108.96 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFsvvdpayppsrqtvylsvstprallvis 391
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVY---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagslAPSVSDYISDNLSLRLlvpaiqltssnvtgSRSDAGedilapyqqyaqtpaGVVLGPDSPATLSFTSGSTGIPKG 471
Cdd:cd05972 53 -----VPLTTLLGPKDIEYRL--------------EAAGAK---------------AIVTDAEDPALIYFTSGTTGLPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRH-YSLTHffpWMGKRFGLDENSKYTMLSgIAhDP-----IQRDMFTPLFLGAQLHVPTADDIgTPGRLAEWMADSE 545
Cdd:cd05972 99 VLHTHsYPLGH---IPTAAYWLGLRPDDIHWN-IA-DPgwakgAWSSFFGPWLLGATVFVYEGPRF-DAERILELLERYG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 546 VTVTHLTPAMGQLLSAQ--ATRQIPTLKNAFFVGDVLTK------RDCTRLQslaknvcIINMYGTTETQRAVSYFAIPS 617
Cdd:cd05972 173 VTSFCGPPTAYRMLIKQdlSSYKFSHLRLVVSAGEPLNPeviewwRAATGLP-------IRDGYGQTETGLTVGNFPDMP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 618 VNEDSTFLATqkdliPAgqgmIDVQLLvvnrtDRN-IPCAVGEMGEIYVRSG--GLAEGYL-DPTATAEKFVVNWfgqnv 693
Cdd:cd05972 246 VKPGSMGRPT-----PG----YDVAII-----DDDgRELPPGEEGDIAIKLPppGLFLGYVgDPEKTEASIRGDY----- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 694 erpdtlkeknpaaaehwfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRR 773
Cdd:cd05972 307 ------------------------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 774 DKDEEKVLVSYFVPIDGDEleglmsaseaaDDDEeidlktqmirgvkkyrkLIRDIREYLKKKLPSYSVP-AVYFPLhKL 852
Cdd:cd05972 363 DPVRGEVVKAFVVLTSGYE-----------PSEE-----------------LAEELQGHVKKVLAPYKYPrEIEFVE-EL 413
|
570
....*....|...
gi 58269178 853 PLNPNGKIDKPAL 865
Cdd:cd05972 414 PKTISGKIRRVEL 426
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
275-865 |
1.52e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 109.84 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVQSELAEgqtmmdgpsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:PRK06087 27 DYWQQTARAMPDKIAVVDNHGAS--------------YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALlvissagsLAPSV---SDYISDNLSLRLLVPAIQ---LTSSNVTGSR 428
Cdd:PRK06087 93 ACLKVGAVSVPLLPSWREAELVWVLNKCQAKMF--------FAPTLfkqTRPVDLILPLQNQLPQLQqivGVDKLAPATS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 429 SDAGEDILAPYQQYAQTPAgvvLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDP 508
Cdd:PRK06087 165 SLSLSQIIADYEPLTTAIT---THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 -IQRDMFTPLFLGAQLhvpTADDIGTPGRLAEWMADSEVTVTH-LTPAMGQLLSA--QATRQIPTLKnaFFV--GDVLTK 582
Cdd:PRK06087 242 gFLHGVTAPFLIGARS---VLLDIFTPDACLALLEQQRCTCMLgATPFIYDLLNLleKQPADLSALR--FFLcgGTTIPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 583 ---RDCTRlqslaKNVCIINMYGTTETqraVSYFAIPSVNEDSTFLATqkdlipAGQGMIDVQLLVVNRTDRNIPCavGE 659
Cdd:PRK06087 317 kvaRECQQ-----RGIKLLSVYGSTES---SPHAVVNLDDPLSRFMHT------DGYAAAGVEIKVVDEARKTLPP--GC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 660 MGEIYVRSGGLAEGYLD-PTATAEkfvvnwfgqnverpdTLKEknpaaaEHWFgirdrmYrSGDLGRYLPDGRVECTGRA 738
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDePELTAR---------------ALDE------EGWY------Y-SGDLCRMDEAGYIKITGRK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 739 DDqIKIRGFR-IELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPidgdeleglmsaseaadddeeidlktqmir 817
Cdd:PRK06087 433 KD-IIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL------------------------------ 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 58269178 818 gVKKYRKL-IRDIREYL-KKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK06087 482 -KAPHHSLtLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
319-865 |
3.45e-24 |
|
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: 107.91 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 319 EASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGG----VFSVVDPAYPPSRQTVYLSVSTPRALLVISSAG 394
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 395 S-LAPSVSDYISDNLSLRLlvpaiqltsSNVTGSRSDAgedilapyqqyaqtpAGVVLGPDSPATLSFTSGSTGIPKGVK 473
Cdd:cd05922 81 DrLRDALPASPDPGTVLDA---------DGIRAARASA---------------PAHEVSHEDLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 474 GRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLhVPTADdiGTPGRlAEWMADSEVTVTHLT- 552
Cdd:cd05922 137 LSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATL-VLTND--GVLDD-AFWEDLREHGATGLAg 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 553 -PAMGQLLS--AQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFaipsvneDSTFLATQK 629
Cdd:cd05922 213 vPSTYAMLTrlGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYL-------PPERILEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 630 DLIpaGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYLDptataekfvvnwfgqnvERPDTLKEKNPAAAEH 709
Cdd:cd05922 286 GSI--GLAIPGGEFEILD--DDGTPTPPGEPGEIVHRGPNVMKGYWN-----------------DPPYRRKEGRGGGVLH 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 710 wfgirdrmyrSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTlvrrdkdeekvlvsyfVPID 789
Cdd:cd05922 345 ----------TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAA----------------VGLP 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 790 GDELEGLMSASEAADddeEIDLKtqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05922 399 DPLGEKLALFVTAPD---KIDPK---------------DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
305-804 |
2.17e-23 |
|
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: 105.67 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 305 PSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSrQTVYLSVSTP 384
Cdd:cd05923 23 PARGLRL-TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA-ELAELIERGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 385 RALLVISSAGSLAPSVSDYISDNLSLRLLVPaiqltssnvTGSRSDAGEDILAPYQqyaqtpagvvlGPDSPATLSFTSG 464
Cdd:cd05923 101 MTAAVIAVDAQVMDAIFQSGVRVLALSDLVG---------LGEPESAGPLIEDPPR-----------EPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 465 STGIPKGVKGRHYSLTHFFPWM----GKRFGLDENSKYTMlsgiahdPIQRDM-FTPLFLGA-----QLHVPTADDigtP 534
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMstqaGLRHGRHNVVLGLM-------PLYHVIgFFAVLVAAlaldgTYVVVEEFD---P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVTHLTPAMGQLL---SAQATRQIPTLKNAFFVGDVLTKRDCTRLQSlAKNVCIINMYGTTETQRAVs 611
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ-HLPGEKVNIYGTTEAMNSL- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 612 yfaipsVNEDSTflatqkdlipAGQGM-----IDVQLLVVNRTDRNIpCAVGEMGEIYVRSGGLA--EGYLD-PTATAEK 683
Cdd:cd05923 309 ------YMRDAR----------TGTEMrpgffSEVRIVRIGGSPDEA-LANGEEGELIVAAAADAafTGYLNqPEATAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 684 fvvnwfgqnverpdtlkeknpaaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPL 763
Cdd:cd05923 372 -----------------------------LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPG 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58269178 764 VRENVTLVRRDKDEEKVLVSYFVPIDG----DELEGLMSASEAAD 804
Cdd:cd05923 423 VTEVVVIGVADERWGQSVTACVVPREGtlsaDELDQFCRASELAD 467
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
273-865 |
2.21e-23 |
|
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: 105.34 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmdgpSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--------------FMGRKL-TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYppsrqtvylsvsTPRALlvissagslapsvsDYISDNLSLRLLVPAIQLTssnvtgsrsdag 432
Cdd:cd05936 66 YFGALKAGAVVVPLNPLY------------TPREL--------------EHILNDSGAKALIVAVSFT------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 eDILAPYqqyAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTH----FFPWMGKRFGLDENS--------KYTM 500
Cdd:cd05936 108 -DLLAAG---APLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVAnalqIKAWLEDLLEGDDVVlaalplfhVFGL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 501 LSGiahdpiqrdMFTPLFLGA-QLHVPTADDIGTpgrLAEwMADSEVTVTHLTPAMGQLLSAQAT---RQIPTLKNAFFV 576
Cdd:cd05936 184 TVA---------LLLPLALGAtIVLIPRFRPIGV---LKE-IRKHRVTIFPGVPTMYIALLNAPEfkkRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 577 GDVLTKRDCTRLQSLAkNVCIINMYGTTETQRAVSyfaipsVN--EDSTFLATqkdlipAGQGMIDVQLLVVNrtDRNIP 654
Cdd:cd05936 251 GAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVA------VNplDGPRKPGS------IGIPLPGTEVKIVD--DDGEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 655 CAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVE 733
Cdd:cd05936 316 LPPGEVGELWVRGPQVMKGYWnRPEETAEAFVDGWL-----------------------------RTGDIGYMDEDGYFF 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 734 CTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglMSASEaadddeeidlkt 813
Cdd:cd05936 367 IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG------ASLTE------------ 428
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 58269178 814 qmirgvkkyrkliRDIREYLKKKLPSYSVP-AVYFpLHKLPLNPNGKIDKPAL 865
Cdd:cd05936 429 -------------EEIIAFCREQLAGYKVPrQVEF-RDELPKSAVGKILRREL 467
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
273-865 |
3.04e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 105.37 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmDGPSRgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK07656 7 LPELLARAARRFGDKEAYV-----------FGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVIssaGSLAPSvsDY-ISDNLSLRLLVPAIQLTSSNVTGSRSDA 431
Cdd:PRK07656 72 ALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVL---GLFLGV--DYsATTRLPALEHVVICETEEDDPHTEKMKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 432 GEDILAPYQQYAQTPAgvvLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYtmlsgIAHDPiqr 511
Cdd:PRK07656 147 FTDFLAAGDPAERAPE---VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY-----LAANP--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 512 dMF----------TPLFLGAQ-LHVPTADdigtPGRLAEWMADSEVTVTHLTPAMGQLLsaqatRQIPTLKNAffvgDVL 580
Cdd:PRK07656 216 -FFhvfgykagvnAPLMRGATiLPLPVFD----PDEVFRLIETERITVLPGPPTMYNSL-----LQHPDRSAE----DLS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 581 TKRDC------------TRLQSLAKNVCIINMYGTTEtqravsyfAIPSVnedsTF--LATQKDLIP--AGQGMIDVQLL 644
Cdd:PRK07656 282 SLRLAvtgaasmpvallERFESELGVDIVLTGYGLSE--------ASGVT----TFnrLDDDRKTVAgtIGTAIAGVENK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 645 VVNRTDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEkfvvnwfgqnverpdTLKeknpaaAEHWFgirdrmyRSGDL 723
Cdd:PRK07656 350 IVNELGEEVP--VGEVGELLVRGPNVMKGYYdDPEATAA---------------AID------ADGWL-------HTGDL 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 724 GRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELeglmsaseaa 803
Cdd:PRK07656 400 GRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAEL---------- 469
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58269178 804 ddDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVP-AVYFpLHKLPLNPNGKIDKPAL 865
Cdd:PRK07656 470 --TEE-------------------ELIAYCREHLAKYKVPrSIEF-LDELPKNATGKVLKRAL 510
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
1006-1232 |
4.66e-23 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 101.21 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRVRkVICLVRAKSADQGLQRLrdsgegrgvwdeewvkqDRIEAVIGDLAEEkfglsqA 1085
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLARGHE-VVGLDRSPPGAANLAAL-----------------PGVEFVRGDLRDP------E 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 EWDRVAEQTDAVLHNGAIVH-WVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAeafvakadevvqagGKG 1164
Cdd:COG0451 57 ALAAALAGVDAVVHLAAPAGvGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYGD--------------GEG 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 1165 LLENDDLEAGRTglnaGYGQSKWVAEKIIMEAGKK-GLSGWILRPGYVLGHSQTAVTNtdDFIWRMVKG 1232
Cdd:COG0451 123 PIDEDTPLRPVS----PYGASKLAAELLARAYARRyGLPVTILRPGNVYGPGDRGVLP--RLIRRALAG 185
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
308-862 |
8.32e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.74 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRAL 387
Cdd:PRK06178 56 GHVI-TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 LVISSagsLAPSVSDyISDNLSLRLLV-----------PAIQLTSSNVTGSRSDAGE-DILAPYQQYAQTPAGVVLGPDS 455
Cdd:PRK06178 135 LALDQ---LAPVVEQ-VRAETSLRHVIvtsladvlpaePTLPLPDSLRAPRLAAAGAiDLLPALRACTAPVPLPPPALDA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 456 PATLSFTSGSTGIPKGVKGRH----------YSLTH----------FFP--WM-GKRFGLdenskytmlsgiahdpiqrd 512
Cdd:PRK06178 211 LAALNYTGGTTGMPKGCEHTQrdmvytaaaaYAVAVvggedsvflsFLPefWIaGENFGL-------------------- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 513 MFtPLFLGAQLHVptaddigtpgrLAEWMADS--------EVTVTHLT----------PAMGQ--LLSAQATRQIPTLKN 572
Cdd:PRK06178 271 LF-PLFSGATLVL-----------LARWDAVAfmaaveryRVTRTVMLvdnavelmdhPRFAEydLSSLRQVRVVSFVKK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 573 affvgdvLTKRDCTRLQSLAKNVCIINMYGTTETQRAvsyfaipsvnedstflatqkDLIPAGQGMIDVQL--------L 644
Cdd:PRK06178 339 -------LNPDYRQRWRALTGSVLAEAAWGMTETHTC--------------------DTFTAGFQDDDFDLlsqpvfvgL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 645 VVNRTDRNI-------PCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdr 716
Cdd:PRK06178 392 PVPGTEFKIcdfetgeLLPLGAEGEIVVRTPSLLKGYWNkPEATAEALRDGWL--------------------------- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 717 myRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdelegl 796
Cdd:PRK06178 445 --HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG------ 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 797 msaseaADDDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFpLHKLPLNPNGKIDK 862
Cdd:PRK06178 517 ------ADLTAA-------------------ALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRK 556
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
298-865 |
8.83e-23 |
|
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: 103.99 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 298 GQTMMDGPSRGRrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTV 377
Cdd:cd05959 19 DKTAFIDDAGSL---TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 378 YLSVSTPRALLVissAGSLAPSVSDYI-SDNLSLRLLVpaiqltssNVTGSRSDAGEDILA---PYQQYAQTPAGVvlGP 453
Cdd:cd05959 96 YLEDSRARVVVV---SGELAPVLAAALtKSEHTLVVLI--------VSGGAGPEAGALLLAelvAAEAEQLKPAAT--HA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 454 DSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKR-FGLDENSKYTMLSGIAHD-PIQRDMFTPLFLGAQ-LHVPTADd 530
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATtVLMPERP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 531 igTPGRLAEWMADSEVTVTHltpamgqllsaqatrQIPTLKNAFFVGDVLTKRDCTRL-------QSLAKNVC------- 596
Cdd:cd05959 242 --TPAAVFKRIRRYRPTVFF---------------GVPTLYAAMLAAPNLPSRDLSSLrlcvsagEALPAEVGerwkarf 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 ---IINMYGTTEtqrAVSYFAipSVNEDSTFLATQKDLIPAGQgmidVQLlvvnRTDRNIPCAVGEMGEIYVRSGGLAEG 673
Cdd:cd05959 305 gldILDGIGSTE---MLHIFL--SNRPGRVRYGTTGKPVPGYE----VEL----RDEDGGDVADGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 674 YLD-PTATAEKFVVNWfgqnverpdtlkeknpaaaehwfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELG 752
Cdd:cd05959 372 YWNnRDKTRDTFQGEW-----------------------------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPF 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 753 EIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELEGlmsaseaadddeeidlktqmirgvkkyrKLIRDIREY 832
Cdd:cd05959 423 EVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSE----------------------------ALEEELKEF 474
|
570 580 590
....*....|....*....|....*....|...
gi 58269178 833 LKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05959 475 VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
280-746 |
2.03e-22 |
|
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: 103.47 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 280 NAKAHPDRVCVvqselaegqTMMDGPSRGRRIFTYKQIDEASNILAHALLKNGlQRGEVVMVYAARSVEMVVCVMGILKA 359
Cdd:cd05931 2 RAAARPDRPAY---------TFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 360 GGVfsVVdPAYPPSR-------QTVyLSVSTPRAllVISSAGSLAPSVSDYISDNLSLRLLVPAIQLTSSNVtgsrsdag 432
Cdd:cd05931 72 GAI--AV-PLPPPTPgrhaerlAAI-LADAGPRV--VLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTS-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 edilapyqqyAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSkyTMLSGIahdPIQRD 512
Cdd:cd05931 138 ----------AADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWL---PLYHD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 513 M------FTPLFLGAQLH-VPTADDIGTPGRLAEWMADSEVTVThLTPAMGQLLSAQATR--QIPTL-----KNAFFVGD 578
Cdd:cd05931 203 MgligglLTPLYSGGPSVlMSPAAFLRRPLRWLRLISRYRATIS-AAPNFAYDLCVRRVRdeDLEGLdlsswRVALNGAE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 579 -VltkrDCTRLQS--------------------LAKNVCIINMyGTTETQRAVSYFAIPSVNEDSTFLATQKD----LIP 633
Cdd:cd05931 282 pV----RPATLRRfaeafapfgfrpeafrpsygLAEATLFVSG-GPPGTGPVVLRVDRDALAGRAVAVAADDPaareLVS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 634 AGQGMIDVQLLVVNrTDRNIPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFvvnwfgqnverpdtlKEKNPAAAEHWFg 712
Cdd:cd05931 357 CGRPLPDQEVRIVD-PETGRELPDGEVGEIWVRGPSVASGYWgRPEATAETF---------------GALAATDEGGWL- 419
|
490 500 510
....*....|....*....|....*....|....
gi 58269178 713 irdrmyRSGDLGrYLPDGRVECTGRADDQIKIRG 746
Cdd:cd05931 420 ------RTGDLG-FLHDGELYITGRLKDLIIVRG 446
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
273-865 |
3.79e-22 |
|
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: 102.15 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmDGPSRgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVV-----------DGERR----LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVfsvvdP--AYPPSRQT---VYLSVSTPRALLVISSAG--SLAPSVSDYISDNLSLRLLVpaiqltssnVT 425
Cdd:COG1021 92 FFALFRAGAI-----PvfALPAHRRAeisHFAEQSEAVAYIIPDRHRgfDYRALARELQAEVPSLRHVL---------VV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 426 GsrsDAGEDIlaPYQQYAQTPAGVVL---GPDSPATLSFTSGSTGIPKGVKGRH----YSLTHffpwMGKRFGLDENSKY 498
Cdd:COG1021 158 G---DAGEFT--SLDALLAAPADLSEprpDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVRA----SAEICGLDADTVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 499 TMLSGIAHDpiqrdmFT---PLFLGAqLHV-------PTADdigtPGRLAEWMADSEVTVTHLTPAM------------- 555
Cdd:COG1021 229 LAALPAAHN------FPlssPGVLGV-LYAggtvvlaPDPS----PDTAFPLIERERVTVTALVPPLallwldaaersry 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 556 -----------GQLLSAQATRQI-PTLknaffvgdvltkrDCTrLQSLaknvciinmYGTTETqrAVSYfaipsvnedsT 623
Cdd:COG1021 298 dlsslrvlqvgGAKLSPELARRVrPAL-------------GCT-LQQV---------FGMAEG--LVNY----------T 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 624 FLATQKDLIPAGQG-MI--DVQLLVVNRTDRniPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtl 699
Cdd:COG1021 343 RLDDPEEVILTTQGrPIspDDEVRIVDEDGN--PVPPGEVGELLTRGPYTIRGYYRaPEHNARAFTPDGF---------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 700 keknpaaaehwfgirdrmYRSGDLGRYLPDGRVECTGRADDQIkIRGfrielGE------IDTHLSRHPLVReNVTLVRR 773
Cdd:COG1021 411 ------------------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVH-DAAVVAM 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 774 DkDE---EKVlVSYFVPidgdeleglmsaseaadDDEEIDLKtqmirgvkkyrklirDIREYLK-KKLPSYSVPAVYFPL 849
Cdd:COG1021 466 P-DEylgERS-CAFVVP-----------------RGEPLTLA---------------ELRRFLReRGLAAFKLPDRLEFV 511
|
650
....*....|....*.
gi 58269178 850 HKLPLNPNGKIDKPAL 865
Cdd:COG1021 512 DALPLTAVGKIDKKAL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
312-862 |
5.00e-22 |
|
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: 100.92 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVIS 391
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 SAGSLapsvsDYISDnlslrllvpaiqltssnvtgsrsdagedilapyqqyaqtpagvvlgPDSPATLSFTSGSTGIPKG 471
Cdd:cd05903 82 RFRQF-----DPAAM----------------------------------------------PDAVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDP-IQRDMFTPLFLGAQLHVptaDDIGTPGRLAEWMADSEVTVTH 550
Cdd:cd05903 111 VMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 551 -LTPAMGQLLSA--QATRQIPTLKnAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSyfAIPSVNEDstflat 627
Cdd:cd05903 188 gATPFLTDLLNAveEAGEPLSRLR-TFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVT--SITPAPED------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 628 qKDLIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVRSGGLAEGYLDptataekfvvnwfgqnveRPDTLKEknpAAA 707
Cdd:cd05903 259 -RRLYTDGRPLPGVEIKVVD--DTGATLAPGVEGELLSRGPSVFLGYLD------------------RPDLTAD---AAP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 708 EHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVP 787
Cdd:cd05903 315 EGWF-------RTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 788 IDGDELEglmsaseaadddeeidlktqmirgvkkyrklIRDIREYL-KKKLPSYSVPAVYFPLHKLPLNPNGKIDK 862
Cdd:cd05903 388 KSGALLT-------------------------------FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
244-866 |
1.40e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 100.77 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 244 GALPLRTPNQSAALpdpAADLDWCGFVGAIPdifSANAKAHPDRVCVVQSElaeGQtmmdgpsrgrriFTYKQIDEASNI 323
Cdd:PRK07788 28 GAVDLERPDNGLRL---AADIRRYGPFAGLV---AHAARRAPDRAALIDER---GT------------LTYAELDEQSNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 324 LAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPsRQTVYLSVSTPRALLVISSagSLAPSVSDY 403
Cdd:PRK07788 87 LARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG-PQLAEVAAREGVKALVYDD--EFTDLLSAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 404 ISDNLSLRLLVPAIQLTSSNVTGSRS-----DAGEDILAPyqqYAQTPAGVVLgpdspatlsFTSGSTGIPKGVKGRHys 478
Cdd:PRK07788 164 PPDLGRLRAWGGNPDDDEPSGSTDETlddliAGSSTAPLP---KPPKPGGIVI---------LTSGTTGTPKGAPRPE-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 479 LTHFFPWMGkrfgldenskytMLSGIahdPIQRDMFT----PLF--LG-AQLHVPTA-----------DDIGTPGRLAEW 540
Cdd:PRK07788 230 PSPLAPLAG------------LLSRV---PFRAGETTllpaPMFhaTGwAHLTLAMAlgstvvlrrrfDPEATLEDIAKH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 541 MADSEVTVthltPAMGQllsaqatRQIPTLknaffvGDVLTKRDCTRLQ-------SLAKNVC----------IINMYGT 603
Cdd:PRK07788 295 KATALVVV----PVMLS-------RILDLG------PEVLAKYDTSSLKiifvsgsALSPELAtraleafgpvLYNLYGS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 604 TEtqraVSYFAIpsvnedstflATQKDLI--P--AGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYLDPta 679
Cdd:PRK07788 358 TE----VAFATI----------ATPEDLAeaPgtVGRPPKGVTVKILDENGNEVP--RGVVGRIFVGNGFPFEGYTDG-- 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 680 taekfvvnwfgqnverpdtlkeKNPAaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLS 759
Cdd:PRK07788 420 ----------------------RDKQ-------IIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLA 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 760 RHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglmsasEAADDDEeidlktqmirgvkkyrklirdIREYLKKKLPS 839
Cdd:PRK07788 471 GHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG----------AALDEDA---------------------IKDYVRDNLAR 519
|
650 660
....*....|....*....|....*...
gi 58269178 840 YSVP-AVYFpLHKLPLNPNGKIDKPALP 866
Cdd:PRK07788 520 YKVPrDVVF-LDELPRNPTGKVLKRELR 546
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
272-862 |
2.51e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 99.62 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 272 AIPDIFSANAKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVV 351
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF---------------GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 352 CVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDyisdnlslrlLVPAIQLTSSNVTGSRSDA 431
Cdd:PRK08316 77 LWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALA----------LLPVDTLILSLVLGGREAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 432 G--EDILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHffPWMGKRFGLDENSKYTMLSGIahdPI 509
Cdd:PRK08316 147 GgwLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVAGDMSADDIPLHAL---PL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 510 ----QRDMF--TPLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPA--MGQLLSAQ-ATRQIPTLKNAFFVGDVL 580
Cdd:PRK08316 222 yhcaQLDVFlgPYLYVGATNVILDAPD---PELILRTIEAERITSFFAPPTvwISLLRHPDfDTRDLSSLRKGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 581 TKRDCTRLQSLAKNVCIINMYGTTEtqravsyfaIPSVnedSTFLATQKDLI---PAGQGMIDVQLLVVNRTDRNIPcaV 657
Cdd:PRK08316 299 PVEVLKELRERLPGLRFYNCYGQTE---------IAPL---ATVLGPEEHLRrpgSAGRPVLNVETRVVDDDGNDVA--P 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 658 GEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTG 736
Cdd:PRK08316 365 GEVGEIVHRSPQLMLGYWDdPEKTAEAFRGGWF-----------------------------HSGDLGVMDEEGYITVVD 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 737 RADDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVlVSYFVPIDGDELeglmsaseaaddDEEidlktqm 815
Cdd:PRK08316 416 RKKDMIKTGGENVASREVEEALYTHPAVAEvAVIGLPDPKWIEAV-TAVVVPKAGATV------------TED------- 475
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 58269178 816 irgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDK 862
Cdd:PRK08316 476 ------------ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILK 510
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
271-865 |
3.09e-21 |
|
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: 99.66 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 271 GAIPDIFSANAKAHPDRVCV-VQSELAEgqtmmdgpsrgrRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEM 349
Cdd:cd05906 10 RTLLELLLRAAERGPTKGITyIDADGSE------------EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 350 VVCVMGILKAGGVFSVVDPayPPSRQTvylsvsTPRALLVISSAGSLA--PSVsdyisdnLSLRLLVPAI--QLTSSNVT 425
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTV--PPTYDE------PNARLRKLRHIWQLLgsPVV-------LTDAELVAEFagLETLSGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 426 GSRSDAGEDILAPYQQYAqtpaGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTH----------------FFPWMgkr 489
Cdd:cd05906 143 GIRVLSIEELLDTAADHD----LPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILArsagkiqhngltpqdvFLNWV--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 490 fGLDEnskytmLSGIAHDPIQrdmftPLFLGA-QLHVPTADDIGTPGRLAEWMADSEVTVThLTPAMGQLLSAQATRQIP 568
Cdd:cd05906 216 -PLDH------VGGLVELHLR-----AVYLGCqQVHVPTEEILADPLRWLDLIDRYRVTIT-WAPNFAFALLNDLLEEIE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 569 T-------LKNAFFVGDVLTKRDCTRLQSL-----AKNVCIINMYGTTETQRAVSY---FAIPSVNEDSTFLATqkdlip 633
Cdd:cd05906 283 DgtwdlssLRYLVNAGEAVVAKTIRRLLRLlepygLPPDAIRPAFGMTETCSGVIYsrsFPTYDHSQALEFVSL------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 634 aGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEKFVvnwfgqnverpdtlkeknpaaAEHWFg 712
Cdd:cd05906 357 -GRPIPGVSMRIVDDEGQLLP--EGEVGRLQVRGPVVTKGYYnNPEANAEAFT---------------------EDGWF- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 713 irdrmyRSGDLGrYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL---VRRDKDEEKVLVSYFVPid 789
Cdd:cd05906 412 ------RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAafaVRDPGAETEELAIFFVP-- 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 790 gdeleglmsaseaadddeEIDLKTQMIRgvkkyrkLIRDIREYLKKKL---PSYSVPavyFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05906 483 ------------------EYDLQDALSE-------TLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
309-865 |
3.76e-21 |
|
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: 98.30 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 309 RRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPayppsrqtvylsVSTPRALL 388
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------LLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 389 vissagslapsvsdYISDNLSLRLLVpaiqltssnvtgsRSDagedilapyqqyaqtpagvvlgpDSPATLSFTSGSTGI 468
Cdd:cd05919 76 --------------YIARDCEARLVV-------------TSA-----------------------DDIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 469 PKGVKGRHYSLTHFFPWMGKR-FGLDEN------SKYTMLSGIAHDpiqrdMFTPLFLGAQLHVptADDIGTPGRLAEWM 541
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMAREaLGLTPGdrvfssAKMFFGYGLGNS-----LWFPLAVGASAVL--NPGWPTAERVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 542 ADSEVTVTHLTPAMGQLLSAQAT---RQIPTLKNAFFVGDVLTKRDCTRLQSlAKNVCIINMYGTTETQRavsyfaipsv 618
Cdd:cd05919 179 ARFRPTVLYGVPTFYANLLDSCAgspDALRSLRLCVSAGEALPRGLGERWME-HFGGPILDGIGATEVGH---------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 nedsTFLATQKDLIPAGQGMIDV---QLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYldptataekfvvnWfgqnver 695
Cdd:cd05919 248 ----IFLSNRPGAWRLGSTGRPVpgyEIRLVDEEGHTIP--PGEEGDLLVRGPSAAVGY-------------W------- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 696 pdtlkeKNPAAAEHWFgiRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDK 775
Cdd:cd05919 302 ------NNPEKSRATF--NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPES 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 776 DEEKVLVSYFVPidgdeleglmsASEAADDDeeidlktqmirgvkkyrKLIRDIREYLKKKLPSYSVPAVYFPLHKLPLN 855
Cdd:cd05919 374 TGLSRLTAFVVL-----------KSPAAPQE-----------------SLARDIHRHLLERLSAHKVPRRIAFVDELPRT 425
|
570
....*....|
gi 58269178 856 PNGKIDKPAL 865
Cdd:cd05919 426 ATGKLQRFKL 435
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
311-865 |
8.05e-21 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 97.16 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 311 IFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTprallvi 390
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCH------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 391 ssagslapsvSDYISDNLslRLLVPAIQLTSSNVTgsrsdagEDILAPYqqyaqtpagvvlgpdSPATLSFTSGSTGIPK 470
Cdd:cd17654 89 ----------VSYLLQNK--ELDNAPLSFTPEHRH-------FNIRTDE---------------CLAYVIHTSGTTGTPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 471 GVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQL-HVPTADDIgTPGRLAEWMADS-EVTV 548
Cdd:cd17654 135 IVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlIVPTSVKV-LPSKLADILFKRhRITV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 549 THLTPAM----------GQLLSAQATRQIPTLKNAFFVGDVLTKrdcTRLQSLAKnVCIINMYGTTETQRAVSYFAIPSv 618
Cdd:cd17654 214 LQATPTLfrrfgsqsikSTVLSATSSLRVLALGGEPFPSLVILS---SWRGKGNR-TRIFNIYGITEVSCWALAYKVPE- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 nEDSTflatqkdlIPAGQGMIDvqlLVVNRTDRNIPCAVGEmgeiyVRSGGLAEGYLdptataekfvvnwfgqnveRPDT 698
Cdd:cd17654 289 -EDSP--------VQLGSPLLG---TVIEVRDQNGSEGTGQ-----VFLGGLNRVCI-------------------LDDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 699 LKEKNPAaaehwfgirdrMYRSGDLGRyLPDGRVECTGRADDQIKIRGFRIELGEIdthlsrhplvrenvtlvrrdkdeE 778
Cdd:cd17654 333 VTVPKGT-----------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLI-----------------------Q 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 779 KVLvsyfvpidgDELEGLMSASEAADDDEEIdlkTQMIRGVKKYRKLIRDIReylKKKLPSYSVPAVYFPLHKLPLNPNG 858
Cdd:cd17654 378 QVI---------ESCLGVESCAVTLSDQQRL---IAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHG 442
|
....*..
gi 58269178 859 KIDKPAL 865
Cdd:cd17654 443 KVDKSEL 449
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
273-766 |
2.27e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.05 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQSELAEGQTmmdgpsrgrRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAVRLGTGAP---------RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslaPSV---SDYISDNLSLRLLVPAIQlTSSNVTGSRS 429
Cdd:PRK13295 97 YLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV--------PKTfrgFDHAAMARRLRPELPALR-HVVVVGGDGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 430 DAGEDILAPYQQYAQTPAGVVL-----GPDSPATLSFTSGSTGIPKGVkgRHYSLTHF---FPWMgKRFGLDENSKYTML 501
Cdd:PRK13295 168 DSFEALLITPAWEQEPDAPAILarlrpGPDDVTQLIYTSGTTGEPKGV--MHTANTLManiVPYA-ERLGLGADDVILMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 502 SGIAHDP-IQRDMFTPLFLGAQLhvpTADDIGTPGRLAEWMADSEVTVTHL-TPAMGQLLSAQAT--RQIPTLKnAFFVG 577
Cdd:PRK13295 245 SPMAHQTgFMYGLMMPVMLGATA---VLQDIWDPARAAELIRTEGVTFTMAsTPFLTDLTRAVKEsgRPVSSLR-TFLCA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 578 DV-----LTKRDCTRLQSLaknvcIINMYGTTETQrAVSyFAIPsvnEDSTFLATQKDLIPagqgMIDVQLLVVNRTDRN 652
Cdd:PRK13295 321 GApipgaLVERARAALGAK-----IVSAWGMTENG-AVT-LTKL---DDPDERASTTDGCP----LPGVEVRVVDADGAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 653 IPcaVGEMGEIYVRSGGLAEGYLdptataekfvvnwfgqnvERPDTlkekNPAAAEHWFGirdrmyrSGDLGRYLPDGRV 732
Cdd:PRK13295 387 LP--AGQIGRLQVRGCSNFGGYL------------------KRPQL----NGTDADGWFD-------TGDLARIDADGYI 435
|
490 500 510
....*....|....*....|....*....|....*
gi 58269178 733 ECTGRADDQIkIRGFR-IELGEIDTHLSRHPLVRE 766
Cdd:PRK13295 436 RISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQ 469
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
304-865 |
3.25e-20 |
|
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: 96.16 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 304 GPSRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYA---ARSVEMVVCVMGIlkaGGVFSVVDPAYPPSrQTVY-L 379
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM---GAVLHTINPRLFPE-QIAYiI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 380 SVSTPRALLVissAGSLAPsvsdyISDNLSLRL-LVPAIQLTSSNVTGSRSDAG-----EDILApyqqyAQTPAGVVlgP 453
Cdd:cd12119 94 NHAEDRVVFV---DRDFLP-----LLEAIAPRLpTVEHVVVMTDDAAMPEPAGVgvlayEELLA-----AESPEYDW--P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 454 D----SPATLSFTSGSTGIPKGVKGRHYSLthFFPWMGKR----FGLDENSKYtMlsgiahdPIqrdmfTPLF------- 518
Cdd:cd12119 159 DfdenTAAAICYTSGTTGNPKGVVYSHRSL--VLHAMAALltdgLGLSESDVV-L-------PV-----VPMFhvnawgl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 519 ------LGAQLHVPTADDigTPGRLAEWMADSEVTVTHLTPAMGQ-LLSAQAT--RQIPTLKNAFFVGDVLTKRDCTRLq 589
Cdd:cd12119 224 pyaaamVGAKLVLPGPYL--DPASLAELIEREGVTFAAGVPTVWQgLLDHLEAngRDLSSLRRVVIGGSAVPRSLIEAF- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 590 sLAKNVCIINMYGTTETQrAVSYFAIP-------SVNEDSTFLATQKDLIPAgqgmidVQLLVVNRTDRNIPCAVGEMGE 662
Cdd:cd12119 301 -EERGVRVIHAWGMTETS-PLGTVARPpsehsnlSEDEQLALRAKQGRPVPG------VELRIVDDDGRELPWDGKAVGE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 663 IYVRSGGLAEGYLDPTATAEKFVVN-WFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQ 741
Cdd:cd12119 373 LQVRGPWVTKSYYKNDEESEALTEDgWL-----------------------------RTGDVATIDEDGYLTITDRSKDV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 742 IKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDK--DEEKVLVsyFVPIDGdeleglmsasEAADDDEeidlktqmirgv 819
Cdd:cd12119 424 IKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPkwGERPLAV--VVLKEG----------ATVTAEE------------ 479
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 58269178 820 kkyrklirdIREYLKKKLPSYSVP-AVYFpLHKLPLNPNGKIDKPAL 865
Cdd:cd12119 480 ---------LLEFLADKVAKWWLPdDVVF-VDEIPKTSTGKIDKKAL 516
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
1006-1255 |
4.97e-20 |
|
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: 92.75 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSR--RVRKVICLVRAKSADQGLQRLRDSGEGRGVWDEEWVKQ---DRIEAVIGDLAEEKF 1080
Cdd:cd05236 2 SVLITGATGFLGKVLLEKLLRScpDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRNLNPlfeSKIVPIEGDLSEPNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1081 GLSQAEWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQ-HHSKQFSFISSTAVldaEAFVAKADEVV- 1158
Cdd:cd05236 82 GLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRcKKLKAFVHVSTAYV---NGDRQLIEEKVy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1159 ------QAGGKGLLENDDLEAGRTGLNAGYGQ------SKWVAEKIIMEAgKKGLSGWILRPGYVLGHSQTAVTNTDDFi 1226
Cdd:cd05236 159 pppadpEKLIDILELMDDLELERATPKLLGGHpntytfTKALAERLVLKE-RGNLPLVIVRPSIVGATLKEPFPGWIDN- 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 58269178 1227 WRMVKG---CVQLGLIPEIN---NAII-CCPVDHVA 1255
Cdd:cd05236 237 FNGPDGlflAYGKGILRTMNadpNAVAdIIPVDVVA 272
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
275-865 |
6.83e-20 |
|
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: 94.70 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVqselaegqtmmDGPSRgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:cd05920 19 DLLARSAARHPDRIAVV-----------DGDRR----LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslapsvsdyisdnlslrllvpaiqltssnvtgSRSDAGED 434
Cdd:cd05920 84 ALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIV-------------------------------------PDRHAGFD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 435 ILAPYQQYAQTpagvvlGPDsPATLSFTSGSTGIPKGVKGRH----YSLTHFFPWMGkrfgLDENSKYTMLSGIAHdpiQ 510
Cdd:cd05920 127 HRALARELAES------IPE-VALFLLSGGTTGTPKLIPRTHndyaYNVRASAEVCG----LDQDTVYLAVLPAAH---N 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 511 RDMFTPLFLGAQL---HVPTADDiGTPGRLAEWMADSEVTVTHLTPAMGQL-LSAQA--TRQIPTLK------------N 572
Cdd:cd05920 193 FPLACPGVLGTLLaggRVVLAPD-PSPDAAFPLIEREGVTVTALVPALVSLwLDAAAsrRADLSSLRllqvggarlspaL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 573 AFFVGDVLtkrDCTRLQslaknvciinMYGTTETqrAVSYfaipsvnedsTFLATQKDLIPAGQGM---IDVQLLVVNRT 649
Cdd:cd05920 272 ARRVPPVL---GCTLQQ----------VFGMAEG--LLNY----------TRLDDPDEVIIHTQGRpmsPDDEIRVVDEE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 650 DRNIPcaVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmYRSGDLGRYLP 728
Cdd:cd05920 327 GNPVP--PGEEGELLTRGPYTIRGYYRaPEHNARAFTPDGF----------------------------YRTGDLVRRTP 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 729 DGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVTLVRrdkdeekvlvsyfVPidgDELEGLMSASEAADDDEE 808
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD-AAVVA-------------MP---DELLGERSCAFVVLRDPP 439
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 809 IDLktqmirgvkkyrkliRDIREYLKKK-LPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05920 440 PSA---------------AQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
310-865 |
6.93e-20 |
|
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: 94.28 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 310 RIFTYKQIDEASNILAHALL-KNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALL 388
Cdd:cd05941 10 DSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 389 vissagslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaqtpagvvlgpdSPATLSFTSGSTGI 468
Cdd:cd05941 90 ------------------------------------------------------------------DPALILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 469 PKGVKGRHYSLT-------------------HFFPWM---GKRFGLdenskytmlsgiahdpiqrdmFTPLFLGAQLHVP 526
Cdd:cd05941 104 PKGVVLTHANLAanvralvdawrwteddvllHVLPLHhvhGLVNAL---------------------LCPLFAGASVEFL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 527 TADDigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVG----------------DVLTkrdctRLQS 590
Cdd:cd05941 163 PKFD---PKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAaerlrlmvsgsaalpvPTLE-----EWEA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 591 LAKNVcIINMYGTTETQRAVSYFA----IP-SVnedstflatqkdlipaGQGMIDVQLLVVNRtDRNIPCAVGEMGEIYV 665
Cdd:cd05941 235 ITGHT-LLERYGMTEIGMALSNPLdgerRPgTV----------------GMPLPGVQARIVDE-ETGEPLPRGEVGEIQV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 666 RSGGLAEGYLD-PTATAEKFvvnwfgqnveRPDTlkeknpaaaehWFgirdrmyRSGDLGRYLPDGRVECTGR-ADDQIK 743
Cdd:cd05941 297 RGPSVFKEYWNkPEATKEEF----------TDDG-----------WF-------KTGDLGVVDEDGYYWILGRsSVDIIK 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 744 IRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglmsaSEAADddeeidlktqmirgvkkyr 823
Cdd:cd05941 349 SGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG---------AAALS------------------- 400
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 58269178 824 klIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05941 401 --LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
313-865 |
4.89e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 92.53 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISS 392
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 393 AGSLAPSVSDyisdnlslrlLVPAIQLTSsnVTGSRSDAG----EDILApyqQYAQTPAGVVLGPDSPATLSFTSGSTGI 468
Cdd:PRK07786 124 LAPVATAVRD----------IVPLLSTVV--VAGGSSDDSvlgyEDLLA---EAGPAHAPVDIPNDSPALIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 469 PKGVKGRH-----YSLTHFFPWmgkrfGLDENSKYTML-SGIAHDPIQRDMFTPLFLGAQ--LHVPTADDigtPGRLAEW 540
Cdd:PRK07786 189 PKGAVLTHanltgQAMTCLRTN-----GADINSDVGFVgVPLFHIAGIGSMLPGLLLGAPtvIYPLGAFD---PGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 541 MADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDcTRLQSLAK---NVCIINMYGTTEtqraVSYFAIPS 617
Cdd:PRK07786 261 LEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASD-TLLRQMAAtfpEAQILAAFGQTE----MSPVTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 618 VNEDstflATQKdLIPAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFgqnverp 696
Cdd:PRK07786 336 LGED----AIRK-LGSVGKVIPTVAARVVDENMNDVP--VGEVGEIVYRAPTLMSGYWnNPEATAEAFAGGWF------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 697 dtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKD 776
Cdd:PRK07786 402 ----------------------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 777 EEKVLVSYFVPidgdeleglmsaseaADDDEEIDLKtqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNP 856
Cdd:PRK07786 460 WGEVPVAVAAV---------------RNDDAALTLE---------------DLAEFLTDRLARYKHPKALEIVDALPRNP 509
|
....*....
gi 58269178 857 NGKIDKPAL 865
Cdd:PRK07786 510 AGKVLKTEL 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
273-766 |
8.83e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 92.09 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQSELAEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSL-----------TWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVfSVvdPAYP--PSRQTVY-LSVSTPRALLVisSAGSLAPSVSDYISDNLSLRLLV---PAIQLTSSNVTg 426
Cdd:COG1022 82 DLAILAAGAV-TV--PIYPtsSAEEVAYiLNDSGAKVLFV--EDQEQLDKLLEVRDELPSLRHIVvldPRGLRDDPRLL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 427 SRSD---AGEDILAPyQQYAQTPAGVvlGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSK------ 497
Cdd:COG1022 156 SLDEllaLGREVADP-AELEARRAAV--KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlsflp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 498 -----------YTMLSG--IAHDP----IQRDM--FTPLFLGAqlhVPtaddigtpgRLAEWMADS-EVTVTHLTPAMGQ 557
Cdd:COG1022 233 lahvfertvsyYALAAGatVAFAEspdtLAEDLreVKPTFMLA---VP---------RVWEKVYAGiQAKAEEAGGLKRK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 558 LLSA------------QATRQIPTLKNA-FFVGD--VLTK-RDCT--RLQ-------SLAKNVC---------IINMYGT 603
Cdd:COG1022 301 LFRWalavgrryararLAGKSPSLLLRLkHALADklVFSKlREALggRLRfavsggaALGPELArffralgipVLEGYGL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 604 TETqravsyFAIPSVNEDSTF-LATqkdlipAGQGMIDVQLlvvnrtdrnipcAVGEMGEIYVRSGGLAEGYL-DPTATA 681
Cdd:COG1022 381 TET------SPVITVNRPGDNrIGT------VGPPLPGVEV------------KIAEDGEILVRGPNVMKGYYkNPEATA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 682 EKFvvnwfgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIR-GFRIELGEIDTHLSR 760
Cdd:COG1022 437 EAF---------------------DADGWL-------HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKA 488
|
....*.
gi 58269178 761 HPLVRE 766
Cdd:COG1022 489 SPLIEQ 494
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
273-865 |
3.18e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 90.20 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF---------------GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRaLLVISSAgsLAPSVSDYISDNLSLrllvPAIQLTSSNVTGSrSDAG 432
Cdd:PRK06155 88 FLGCAWLGAIAVPINTALRGPQLEHILRNSGAR-LLVVEAA--LLAALEAADPGDLPL----PAVWLLDAPASVS-VPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 433 EDILAPYQQYAQTPAGVVLGPDSPATLsFTSGSTGIPKGVKGRHyslTHFFPW---MGKRFGLDENSK-YTMLSgIAHDP 508
Cdd:PRK06155 160 WSTAPLPPLDAPAPAAAVQPGDTAAIL-YTSGTTGPSKGVCCPH---AQFYWWgrnSAEDLEIGADDVlYTTLP-LFHTN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 IQRDMFTPLFLGAQLHVptaddigTP----GRLAEWMADSEVTVTHLTPAMGQLLSAQATR---QIPTLKNAFFVG---- 577
Cdd:PRK06155 235 ALNAFFQALLAGATYVL-------EPrfsaSGFWPAVRRHGATVTYLLGAMVSILLSQPAResdRAHRVRVALGPGvpaa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 578 --DVLTKRdctrlqslaKNVCIINMYGTTETQrAVSYFAIPSvnedstflatQKdliPAGQGMI--DVQLLVVNRTDRNI 653
Cdd:PRK06155 308 lhAAFRER---------FGVDLLDGYGSTETN-FVIAVTHGS----------QR---PGSMGRLapGFEARVVDEHDQEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 654 PcaVGEMGEIYVRS---GGLAEGYLdptATAEKFVVNWfgQNVerpdtlkeknpaaaehWFGIRDRMYRSgdlgrylPDG 730
Cdd:PRK06155 365 P--DGEPGELLLRAdepFAFATGYF---GMPEKTVEAW--RNL----------------WFHTGDRVVRD-------ADG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 731 RVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVLVSyFVPIDGDELEGLmsaseaadddeei 809
Cdd:PRK06155 415 WFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAaAVFPVPSELGEDEVMAA-VVLRDGTALEPV------------- 480
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 810 dlktqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK06155 481 ------------------ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
258-865 |
7.25e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.89 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 258 PDPAADLDWCGFVGAIpdIFSAnAKAHPDRVCvvqseLAEGQTMMDGPSRGRRIFTYKQideasniLAHALlknGLQRGE 337
Cdd:PRK06188 2 ATMADLLHSGATYGHL--LVSA-LKRYPDRPA-----LVLGDTRLTYGQLADRISRYIQ-------AFEAL---GLGTGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 338 VVMVYAARSVEmVVCVMGILKAGGV-FSVVDPAYPPSRQTVYLSVSTPRALLV-----ISSAGSLAPSVSdyisdnlSLR 411
Cdd:PRK06188 64 AVALLSLNRPE-VLMAIGAAQLAGLrRTALHPLGSLDDHAYVLEDAGISTLIVdpapfVERALALLARVP-------SLK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 412 LLVPAiqltssnvtgSRSDAGEDILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFG 491
Cdd:PRK06188 136 HVLTL----------GPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 492 LDENSKYTMLSGIAHdpIQRDMFTP-LFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAMGQLL---SAQATRQI 567
Cdd:PRK06188 206 WPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFD---PAEVLRAIEEQRITATFLVPTMIYALldhPDLRTRDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 568 PTLKNAFFVGDVLTKrdcTRLQSLAKNVCII--NMYGTTETQRAVSYFAipsvnEDSTFLATQKDLIPAGQGM--IDVQL 643
Cdd:PRK06188 281 SSLETVYYGASPMSP---VRLAEAIERFGPIfaQYYGQTEAPMVITYLR-----KRDHDPDDPKRLTSCGRPTpgLRVAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 644 LvvNRTDRniPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGD 722
Cdd:PRK06188 353 L--DEDGR--EVAQGEVGEICVRGPLVMDGYWNrPEETAEAFRDGWL-----------------------------HTGD 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 723 LGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVlVSYFVPidgdeleglmsASE 801
Cdd:PRK06188 400 VAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQvAVIGVPDEKWGEAV-TAVVVL-----------RPG 467
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58269178 802 AADDDEEIdlktqmIRGVKkyrklirdireylKKKLPSYSVPAVYFpLHKLPLNPNGKIDKPAL 865
Cdd:PRK06188 468 AAVDAAEL------QAHVK-------------ERKGSVHAPKQVDF-VDSLPLTALGKPDKKAL 511
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
455-865 |
7.70e-18 |
|
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: 86.23 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 455 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIgtp 534
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 grLAEWMADSEVTVTHLTPAM-GQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRlQSLAKNVCIINMYGTTETQRAVSYF 613
Cdd:cd17630 78 --LAEDLAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLRAVLLGGAPIPPELLE-RAADRGIPLYTTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 614 AiPSVNEDSTflatqkdlipAGQGMIDVQLLVVNRtdrnipcavgemGEIYVRSGGLAEGYLDPtataekfvvnwfgqnv 693
Cdd:cd17630 155 R-PDGFGRGG----------VGVLLPGRELRIVED------------GEIWVGGASLAMGYLRG---------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 694 erpdtlKEKNPAAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnvtlvrr 773
Cdd:cd17630 196 ------QLVPEFNEDGWF-------TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 774 dkdeekVLVsyfVPIDGDELeG-----LMSASEAADDDEeidlktqmirgvkkyrklirdIREYLKKKLPSYSVPAVYFP 848
Cdd:cd17630 256 ------AFV---VGVPDEEL-GqrpvaVIVGRGPADPAE---------------------LRAWLKDKLARFKLPKRIYP 304
|
410
....*....|....*..
gi 58269178 849 LHKLPLNPNGKIDKPAL 865
Cdd:cd17630 305 VPELPRTGGGKVDRRAL 321
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
1006-1217 |
8.41e-18 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 89.24 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLS-RRVRKVICLVRAKSADQgLQRLRDSgegrgvWDeewvkQDRIEAVIGDLAEEKFGLSq 1084
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDrRREATVHVLVRRQSLSR-LEALAAY------WG-----ADRVVPLVGDLTEPGLGLS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1085 AEWDRVAEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeafvakadevvqAGG-K 1163
Cdd:PRK07201 69 EADIAELGDIDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAV---------------AGDyE 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 58269178 1164 GLLENDDLEAGrTGLNAGYGQSKWVAEKIIMEAGkkGLSGWILRPGYVLGHSQT 1217
Cdd:PRK07201 134 GVFREDDFDEG-QGLPTPYHRTKFEAEKLVREEC--GLPWRVYRPAVVVGDSRT 184
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
273-861 |
1.86e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 87.63 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQSElaegqtmmdgpsrgRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGD--------------RRL-TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPsRQTVYL-SVSTPRALLVISsagSLAPSVSDYISDNLSLRLLVpAIQLTSSNVTGSRSDA 431
Cdd:PRK07798 70 MLGAFKARAVPVNVNYRYVE-DELRYLlDDSDAVALVYER---EFAPRVAEVLPRLPKLRTLV-VVEDGSGNDLLPGAVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 432 GEDILapyqqyAQTPAGVVLGPDSPATLSF--TSGSTGIPKGVKGRHyslthffpwmgkrfgldenskytmlsgiahdpi 509
Cdd:PRK07798 145 YEDAL------AAGSPERDFGERSPDDLYLlyTGGTTGMPKGVMWRQ--------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 510 qRDMFTPLFLGAQLhvPTADDIGTPGRLAEWMADSEVTVT-------H---LTPAMGQLLSAQATRQIPTLK-NA----- 573
Cdd:PRK07798 186 -EDIFRVLLGGRDF--ATGEPIEDEEELAKRAAAGPGMRRfpapplmHgagQWAAFAALFSGQTVVLLPDVRfDAdevwr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 574 ----------FFVGDVLTK-----------RDCTRLQSLA------------------KNVCIINMYGTTETqrAVSYFA 614
Cdd:PRK07798 263 tierekvnviTIVGDAMARplldaleargpYDLSSLFAIAsggalfspsvkeallellPNVVLTDSIGSSET--GFGGSG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 615 IPSVNEDSTFLATQKdlipagqgmIDVQLLVVNRTDRNIPCAVGEMGEIyVRSGGLAEGYL-DPTATAEKFVVnwfgqnv 693
Cdd:PRK07798 341 TVAKGAVHTGGPRFT---------IGPRTVVLDEDGNPVEPGSGEIGWI-ARRGHIPLGYYkDPEKTAETFPT------- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 694 erpdtlkeknpaaaehwfgIRDRMYR-SGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVrenvtlvr 772
Cdd:PRK07798 404 -------------------IDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV-------- 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 773 rdkdeEKVLVsyfVPID----GDELEGLMSASEAADDDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVP-AVYF 847
Cdd:PRK07798 457 -----ADALV---VGVPderwGQEVVAVVQLREGARPDLA-------------------ELRAHCRSSLAGYKVPrAIWF 509
|
650
....*....|....
gi 58269178 848 pLHKLPLNPNGKID 861
Cdd:PRK07798 510 -VDEVQRSPAGKAD 522
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
310-793 |
7.18e-17 |
|
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: 86.09 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 310 RIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRaLLV 389
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR-LLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 390 ISSAG-------SLAPSVSDYISDNLSLRLLVPAIQLTSSNVTGsrsDAGEDILAPYQQYAQTPA--GVVLGPDSPATLS 460
Cdd:cd17634 162 TADGGvragrsvPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDW---QEGRDLWWRDLIAKASPEhqPEAMNAEDPLFIL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 461 FTSGSTGIPKGVKGRHYSLTHFFPW-MGKRFGLDENSKYTMLSGI----AHDPIqrdMFTPLFLGAQ-LHVPTADDIGTP 534
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVgwvtGHSYL---LYGPLACGATtLLYEGVPNWPTP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVTHLTPAMGQLLSAQATRQI-----PTLKNAFFVGDVL---TKRDCTRlqSLAKNVC-IINMYGTTE 605
Cdd:cd17634 316 ARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIegtdrSSLRILGSVGEPInpeAYEWYWK--KIGKEKCpVVDTWWQTE 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 606 TqravSYFAIPSVnedstflatqKDLIPAGQG-----MIDVQLLVVNrtdrnipcavgemgeiyvrsgglAEGYLDPTAT 680
Cdd:cd17634 394 T----GGFMITPL----------PGAIELKAGsatrpVFGVQPAVVD-----------------------NEGHPQPGGT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 681 AEKFVVN--WFGQNVerpdTLKEKNPAAAEHWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHL 758
Cdd:cd17634 437 EGNLVITdpWPGQTR----TLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVL 512
|
490 500 510
....*....|....*....|....*....|....*....
gi 58269178 759 SRHPLVRENVTLVRRDKDEEKVLVSYFV----PIDGDEL 793
Cdd:cd17634 513 VAHPKVAEAAVVGIPHAIKGQAPYAYVVlnhgVEPSPEL 551
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
275-865 |
3.91e-16 |
|
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: 83.31 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVQ-SELAEgqtmmdgpsrgRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCV 353
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWcDDAGE-----------ERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 354 MGILKAGGVfSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDYISDNLSLRLLVpaiqltssNVTGSRSDAGE 433
Cdd:cd05970 90 LALHKLGAI-AIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKLV--------WVGDPVPEGWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 434 DI------LAPYQQYAQTPAGVvlGPDSPATLSFTSGSTGIPKGVKGRH-YSLTHFFpwMGKRF-GLDENSK-YTmlsgI 504
Cdd:cd05970 161 DFrkliknASPDFERPTANSYP--CGEDILLVYFSSGTTGMPKMVEHDFtYPLGHIV--TAKYWqNVREGGLhLT----V 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 505 AHDPIQRDMFTPLF----LGAQLHVPTADDIgTPGRLAEWMADSEVTVTHLTPAMGQ-LLSAQATR-QIPTLKNAFFVGD 578
Cdd:cd05970 233 ADTGWGKAVWGKIYgqwiAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRfLIREDLSRyDLSSLRYCTTAGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 579 VLTKRDCTRLQSLAkNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLatqkdliPAGQGMIDVqllvVNRTDRniPCAVG 658
Cdd:cd05970 312 ALNPEVFNTFKEKT-GIKLMEGFGQTETTLTIATFPWMEPKPGSMGK-------PAPGYEIDL----IDREGR--SCEAG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 659 EMGEIYVRsgglaegyldptaTAEKFVVNWFGQNVERPdtlkEKNpaaAEHWFgirDRMYRSGDLGRYLPDGRVECTGRA 738
Cdd:cd05970 378 EEGEIVIR-------------TSKGKPVGLFGGYYKDA----EKT---AEVWH---DGYYHTGDAAWMDEDGYLWFVGRT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 739 DDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTlvrrdkdeekvlvsyFVPidgDELEGlmsaseaadddEEIDLKTQMIR 817
Cdd:cd05970 435 DDLIKSSGYRIGPFEVESALIQHPAVLEcAVT---------------GVP---DPIRG-----------QVVKATIVLAK 485
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 58269178 818 GVKKYRKLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05970 486 GYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
281-865 |
8.87e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.16 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVqsELAEGqtmmdgpsrgrRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:PRK09088 5 ARLQPQRLAAV--DLALG-----------RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYPPSRQTVYLSVSTPRalLVISSAGslapsVSDYISDNLSLRLLVPAIqltssnvtgsrsdageDILAPyq 440
Cdd:PRK09088 72 AIYVPLNWRLSASELDALLQDAEPR--LLLGDDA-----VAAGRTDVEDLAAFIASA----------------DALEP-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 441 qyAQTPAgvvLGPDSPATLSFTSGSTGIPKGVKGRHYSL---THFFPWMGKrfgLDENSKYTMLSGIAH--------DPI 509
Cdd:PRK09088 127 --ADTPS---IPPERVSLILFTSGTSGQPKGVMLSERNLqqtAHNFGVLGR---VDAHSSFLCDAPMFHiiglitsvRPV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 510 qrdmftpLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHL--TPAMGQLLSAQATRQIPTLKN--AFFVGDVLTKRDC 585
Cdd:PRK09088 199 -------LAVGGSILVSNGFE---PKRTLGRLGDPALGITHYfcVPQMAQAFRAQPGFDAAALRHltALFTGGAPHAAED 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 586 TRlQSLAKNVCIINMYGTTEtqrAVSYFAIPSvneDSTFLATQkdLIPAGQGMIDVQLLVVNRTDRNipCAVGEMGEIYV 665
Cdd:PRK09088 269 IL-GWLDDGIPMVDGFGMSE---AGTVFGMSV---DCDVIRAK--AGAAGIPTPTVQTRVVDDQGND--CPAGVPGELLL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 666 RSGGLAEGYL-DPTATAEKFvvnwfgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKI 744
Cdd:PRK09088 338 RGPNLSPGYWrRPQATARAF---------------------TGDGWF-------RTGDIARRDADGFFWVVDRKKDMFIS 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 745 RGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELEglmsaseaadddeeidlktqmirgvkkyrk 824
Cdd:PRK09088 390 GGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLD------------------------------ 439
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 58269178 825 lIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK09088 440 -LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
273-684 |
1.47e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 82.02 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQSElaegqtmmdGPSRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAQRE---------PGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPP-SRQTVYL----SVSTPRALLVISSA---GSLApsvsdyisdnlSLRLLVPAIQLTSSNV 424
Cdd:PRK12582 122 TLAAMQAGVPAAPVSPAYSLmSHDHAKLkhlfDLVKPRVVFAQSGApfaRALA-----------ALDLLDVTVVHVTGPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 425 TGSRSDAGEDILA--PYQQYAQTPAGvvLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSK----- 497
Cdd:PRK12582 191 EGIASIAFADLAAtpPTAAVAAAIAA--ITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvsl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 498 ------YTMLSGIAHDPIqrdmftpLFLGAQLHVptadDIG--TPGRLAEWMAD-SEV--TVTHLTPAMGQLLsAQATRQ 566
Cdd:PRK12582 269 dwmpwnHTMGGNANFNGL-------LWGGGTLYI----DDGkpLPGMFEETIRNlREIspTVYGNVPAGYAML-AEAMEK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 567 IPTLKNAFFV--------GDVLTKRDCTRLQSLA-----KNVCIINMYGTTETQRAVSyfaipsvnedSTFLATQKDLIp 633
Cdd:PRK12582 337 DDALRRSFFKnlrlmaygGATLSDDLYERMQALAvrttgHRIPFYTGYGATETAPTTT----------GTHWDTERVGL- 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 58269178 634 AGQGMIDVQLLVVnrtdrnipcAVGEMGEIYVRSGGLAEGYL-DPTATAEKF 684
Cdd:PRK12582 406 IGLPLPGVELKLA---------PVGDKYEVRVKGPNVTPGYHkDPELTAAAF 448
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
1007-1213 |
2.26e-15 |
|
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: 78.87 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLLSRRVRkVICLVRAKSADQGLQRLRdsgegrgvwdeewvkqdrIEAVIGDLAEEKFgLSQAe 1086
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGYR-VRALVRSGSDAVLLDGLP------------------VEVVEGDLTDAAS-LAAA- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1087 wdrvAEQTDAVLHNGAIVHWVYPYPK-LRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAfVAKADEvvqaggkgl 1165
Cdd:cd05228 60 ----MKGCDRVFHLAAFTSLWAKDRKeLYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPP-DGRIDE--------- 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 58269178 1166 leNDDLEAGRTGLNagYGQSKWVAEKIIMEAGKKGLSGWILRPGYVLG 1213
Cdd:cd05228 126 --TTPWNERPFPND--YYRSKLLAELEVLEAAAEGLDVVIVNPSAVFG 169
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
281-737 |
2.66e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.71 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQSELAEGqtmmDGPSRGRRIfTYKQIDEASNILAHALLKNGLQRGE--VVMVYAarSVEMVVCVMGILK 358
Cdd:PRK09274 16 AQERPDQLAVAVPGGRGA----DGKLAYDEL-SFAELDARSDAIAHGLNAAGIGRGMraVLMVTP--SLEFFALTFALFK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 359 AGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSA-----------GSLAPSVsdyisdNLSLRLLVPAIQLTSSNVTGS 427
Cdd:PRK09274 89 AGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAhlarrlfgwgkPSVRRLV------TVGGRLLWGGTTLATLLRDGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 428 rsdagediLAPYQqyaqtpaGVVLGPDSPATLSFTSGSTGIPKGVKGRH-------YSLTHFFpwmgkrfgldenskytm 500
Cdd:PRK09274 163 --------AAPFP-------MADLAPDDMAAILFTSGSTGTPKGVVYTHgmfeaqiEALREDY----------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 501 lsGIAHDpiQRDMFT-PLF------LGAQLHVP--------TADdigtPGRLAEWMADSEVTVTHLTPA-MGQLLSAQAT 564
Cdd:PRK09274 211 --GIEPG--EIDLPTfPLFalfgpaLGMTSVIPdmdptrpaTVD----PAKLFAAIERYGVTNLFGSPAlLERLGRYGEA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 565 RQI--PTLKNAFFVGDVLTKRDCTRLQS-LAKNVCIINMYGTTEtqravsyfAIP-SVNEDSTFLATQKDLIPAGQGM-- 638
Cdd:PRK09274 283 NGIklPSLRRVISAGAPVPIAVIERFRAmLPPDAEILTPYGATE--------ALPiSSIESREILFATRAATDNGAGIcv 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 639 ---ID-VQLLVVNRTDRNIP-------CAVGEMGEIYVRSGGLAEGYLD-PTATAE-KfvvnwfgqnVERPDTlkeknpa 705
Cdd:PRK09274 355 grpVDgVEVRIIAISDAPIPewddalrLATGEIGEIVVAGPMVTRSYYNrPEATRLaK---------IPDGQG------- 418
|
490 500 510
....*....|....*....|....*....|..
gi 58269178 706 aaehwfGIRDRMyrsGDLGRYLPDGRVECTGR 737
Cdd:PRK09274 419 ------DVWHRM---GDLGYLDAQGRLWFCGR 441
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
308-971 |
3.43e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.75 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAArSVEMVVCVMGILKAGgVFSVvdPAYPPS-----RQTVYLSV- 381
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPS-GPDYVAAFFGCLYAG-VIAV--PAYPPEsarrhHQERLLSIi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 382 --STPRALLVISS-AGSLApSVSDYISDNLSLRLLVpaiqltssnvtgsrsDAGEDILApyqQYAQTPAgvvLGPDSPAT 458
Cdd:PRK05691 113 adAEPRLLLTVADlRDSLL-QMEELAAANAPELLCV---------------DTLDPALA---EAWQEPA---LQPDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 459 LSFTSGSTGIPKGVKGRHYSLTHFfPWMGKR-FGLDENSKYTMLSGIahdPIQRDM------FTPLFLGaqlhVP----- 526
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVAN-EQLIRHgFGIDLNPDDVIVSWL---PLYHDMgligglLQPIFSG----VPcvlms 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 527 TADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLS---AQATRQIPTLKN--AFFVGDVLTKRDCTRLQSLAKNVCIIN-- 599
Cdd:PRK05691 243 PAYFLERPLRWLEAISEYGGTISGGPDFAYRLCServSESALERLDLSRwrVAYSGSEPIRQDSLERFAEKFAACGFDpd 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 600 ----MYGTTETQRAVSY----FAIPSVNEDSTFLAtqKDLIPAGQGMIDV---------QLLVVNrTDRNIPCAVGEMGE 662
Cdd:PRK05691 323 sffaSYGLAEATLFVSGgrrgQGIPALELDAEALA--RNRAEPGTGSVLMscgrsqpghAVLIVD-PQSLEVLGDNRVGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 663 IYVRSGGLAEGYL-DPTATAEKFVvnwfgqnvERpdtlkeknpaAAEHWFgirdrmyRSGDLGrYLPDGRVECTGRADDQ 741
Cdd:PRK05691 400 IWASGPSIAHGYWrNPEASAKTFV--------EH----------DGRTWL-------RTGDLG-FLRDGELFVTGRLKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 742 IKIRGFRIELGEIDThlsrhpLVRENVTLVRRDKdeekvLVSYFVPIDGDELEGLmsaseAAdddeEIDLKTQMIrgvKK 821
Cdd:PRK05691 454 LIVRGHNLYPQDIEK------TVEREVEVVRKGR-----VAAFAVNHQGEEGIGI-----AA----EISRSVQKI---LP 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 822 YRKLIRDIREYLKKKLpsYSVPAVYFPLH--KLPLNPNGKIDKPA--LPFPDTSL----LAPAPSASTADHTPT-----Q 888
Cdd:PRK05691 511 PQALIKSIRQAVAEAC--QEAPSVVLLLNpgALPKTSSGKLQRSAcrLRLADGSLdsyaLFPALQAVEAAQTAAsgdelQ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 889 KTIHDIWLSLLPSPppHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEIDLLRNAdlGGAGD 968
Cdd:PRK05691 589 ARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAG--GGAAQ 664
|
...
gi 58269178 969 GAI 971
Cdd:PRK05691 665 AAI 667
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
271-865 |
1.13e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 78.66 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 271 GAIPDIFSANAKAHPDRVCVVQSELaegqtmmdgpsrGRRiFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMV 350
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQ------------ALR-YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 351 VCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISS---------AGSLAPSVSDYISDNLS------LRLLV- 414
Cdd:PRK12583 85 LTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyhamLQELLPGLAEGQPGALAcerlpeLRGVVs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 415 ----PAIQLTSSNVTGSRSDA--GEDILAPYQQyaqtpagvvLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGK 488
Cdd:PRK12583 165 lapaPPPGFLAWHELQARGETvsREALAERQAS---------LDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 489 RFGLDENSKYTMlsgiahdPIqrdmftPLF--------------LGAQLHVPTadDIGTPGRLAEWMADSEVTVTHLTPA 554
Cdd:PRK12583 236 SLGLTEHDRLCV-------PV------PLYhcfgmvlanlgcmtVGACLVYPN--EAFDPLATLQAVEEERCTALYGVPT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 555 M--GQLLSAQATR-QIPTLKNAFFVG---------DVLTKRDCTRLQsLAknvciinmYGTTETQRAvsyfaipsvneds 622
Cdd:PRK12583 301 MfiAELDHPQRGNfDLSSLRTGIMAGapcpievmrRVMDEMHMAEVQ-IA--------YGMTETSPV------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 623 TFLATQKDLIP-----AGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEKFvvnwfgqnverp 696
Cdd:PRK12583 359 SLQTTAADDLErrvetVGRTQPHLEVKVVDPDGATVP--RGEIGELCTRGYSVMKGYWnNPEATAESI------------ 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 697 dtlkeknpaAAEHWfgirdrMYrSGDLGRYLPDGRVECTGRADDQIkIRGFR-IELGEIDTHLSRHPLVRE-NVTLVRRD 774
Cdd:PRK12583 425 ---------DEDGW------MH-TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADvQVFGVPDE 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 775 KDEEKVLVsyFVPIDGDeleglmsasEAADDDEeidlktqmirgvkkyrklirdIREYLKKKLPSYSVPAVYFPLHKLPL 854
Cdd:PRK12583 488 KYGEEIVA--WVRLHPG---------HAASEEE---------------------LREFCKARIAHFKVPRYFRFVDEFPM 535
|
650
....*....|.
gi 58269178 855 NPNGKIDKPAL 865
Cdd:PRK12583 536 TVTGKVQKFRM 546
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
309-865 |
1.56e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.39 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 309 RRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALL 388
Cdd:PRK05852 41 RIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 389 VISSA-GSLAPSVSDYISDNLSlrlLVPAIQLTSSNVTGSRSDAGEDILApyqqyAQTPAGvvLGPDSpATLSFTSGSTG 467
Cdd:PRK05852 121 IDADGpHDRAEPTTRWWPLTVN---VGGDSGPSGGTLSVHLDAATEPTPA-----TSTPEG--LRPDD-AMIMFTGGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 468 IPKGVkgrhyslthffPWMGKRFGldeNSKYTMLSGIAHDPiqRD---MFTPLFLGAQLHVPTADDIGTPGRL------- 537
Cdd:PRK05852 190 LPKMV-----------PWTHANIA---SSVRAIITGYRLSP--RDatvAVMPLYHGHGLIAALLATLASGGAVllpargr 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 538 ----AEW--MADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAF--FVGDV---LTKRDCTRLQS--LAKNVCiinMYGTT 604
Cdd:PRK05852 254 fsahTFWddIKAVGATWYTAVPTIHQILLERAATEPSGRKPAAlrFIRSCsapLTAETAQALQTefAAPVVC---AFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 605 ETQRAVSYFAIPSVNEDSTFLATQKdliPAGQGMiDVQLLVVnRTDrNIPCAVGEMGEIYVRSGGLAEGYL-DPTATAEK 683
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENPVVSTG---LVGRST-GAQIRIV-GSD-GLPLPAGAVGEVWLRGTTVVRGYLgDPTITAAN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 684 FVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPL 763
Cdd:PRK05852 405 FTDGWL-----------------------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 764 VRENVTLVRRDKDEEKVLVSYFVPIDgdeleglmSASEAADddeeidlktqmirgvkkyrklirDIREYLKKKLPSYSVP 843
Cdd:PRK05852 456 VMEAAVFGVPDQLYGEAVAAVIVPRE--------SAPPTAE-----------------------ELVQFCRERLAAFEIP 504
|
570 580
....*....|....*....|..
gi 58269178 844 AVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK05852 505 ASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
276-862 |
1.59e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.16 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 276 IFSANAKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMG 355
Cdd:PRK07470 12 FLRQAARRFPDRIALVW---------------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 356 ILKAGGVFSvvdpayPPS-RQT----VYL-SVSTPRALLVISSAGSLAPSVSdyisdnlslrllVPAIQLTSSNVTGSrS 429
Cdd:PRK07470 77 AFRLGAVWV------PTNfRQTpdevAYLaEASGARAMICHADFPEHAAAVR------------AASPDLTHVVAIGG-A 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 430 DAGEDILAPYQQYAQTPAGVV-LGPDSPATLSFTSGSTGIPKGVkgrhySLTHffpwmGKRFGLDENSKYTMLSGIAHdp 508
Cdd:PRK07470 138 RAGLDYEALVARHLGARVANAaVDHDDPCWFFFTSGTTGRPKAA-----VLTH-----GQMAFVITNHLADLMPGTTE-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 iqRD---MFTPLFLGAQLH------------VPTAD--DIGTPGRLAE-WMADSEVTVthltPAMGQLL---SAQATRQI 567
Cdd:PRK07470 206 --QDaslVVAPLSHGAGIHqlcqvargaatvLLPSErfDPAEVWALVErHRVTNLFTV----PTILKMLvehPAVDRYDH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 568 PTLKNAFFVGDVLTKRDCTR-LQSLAKNVciinmygttetqraVSYFAIPSVNEDSTFL---------ATQKDLIPAG-- 635
Cdd:PRK07470 280 SSLRYVIYAGAPMYRADQKRaLAKLGKVL--------------VQYFGLGEVTGNITVLppalhdaedGPDARIGTCGfe 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 636 -QGMiDVQLLvvnrTDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgi 713
Cdd:PRK07470 346 rTGM-EVQIQ----DDEGRELPPGETGEICVIGPAVFAGYYNnPEANAKAFRDGWF------------------------ 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 714 rdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdel 793
Cdd:PRK07470 397 -----RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCV------- 464
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 794 eglmsASEAADDDEEidlktqmirgvkkyrklirDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDK 862
Cdd:PRK07470 465 -----ARDGAPVDEA-------------------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
8-157 |
4.45e-14 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 76.24 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 8 LTPEELNQRLDRWSSRLS-ALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHILLT 86
Cdd:cd19531 183 LQGEVLERQLAYWREQLAgAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALARREGA--------TLFMTLLA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 87 SFAILLFRYTPDPSLVICT-SAN---ASTKPLL--------LKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDH 153
Cdd:cd19531 255 AFQVLLHRYSGQDDIVVGTpVAGrnrAELEGLIgffvntlvLRTDLSGDPTFRELLARVRETALEAYAhQDLPFEKLVEA 334
|
....
gi 58269178 154 IKPE 157
Cdd:cd19531 335 LQPE 338
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
312-865 |
6.50e-14 |
|
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: 75.62 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFsvvdpayppsrqtvylsvstprallvis 391
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagslAPSVSDYISDNLSLRLlvpaiqltssnvtgSRSDAGEDILAPyQQYAQTPagvvlgPDSPATLSFTSGSTGIPKG 471
Cdd:cd05969 53 -----CPLFSAFGPEAIRDRL--------------ENSEAKVLITTE-ELYERTD------PEDPTLLHYTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLTHFFPWMGKRFGLDENSKY------TMLSGIAHDpiqrdMFTPLFLGAQLHVPTADdiGTPGRLAEWMADSE 545
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYVLDLHPDDIYwctadpGWVTGTVYG-----IWAPWLNGVTNVVYEGR--FDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 546 VTVTHLTPA-----MGQLLSAQATRQIPTLKNAFFVGDVLTKrDCTRLQSLAKNVCIINMYGTTET--QRAVSYFAIPsv 618
Cdd:cd05969 180 VTVWYTAPTairmlMKEGDELARKYDLSSLRFIHSVGEPLNP-EAIRWGMEVFGVPIHDTWWQTETgsIMIANYPCMP-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 nedstflatqkdLIPAGQGMI--DVQLLVVNRTDRNIPcaVGEMGEIYVRSG--GLAEGYL-DPTATAEKFVVNWfgqnv 693
Cdd:cd05969 257 ------------IKPGSMGKPlpGVKAAVVDENGNELP--PGTKGILALKPGwpSMFRGIWnDEERYKNSFIDGW----- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 694 erpdtlkeknpaaaehwfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRR 773
Cdd:cd05969 318 ------------------------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 774 DKDEEKVLVSYfvpidgdeleglmsaseaadddeeIDLKtqmiRGVKKYRKLIRDIREYLKKKLPSYSVPAVYFPLHKLP 853
Cdd:cd05969 374 DPLRGEIIKAF------------------------ISLK----EGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLP 425
|
570
....*....|..
gi 58269178 854 LNPNGKIDKPAL 865
Cdd:cd05969 426 KTRSGKIMRRVL 437
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
453-862 |
1.15e-13 |
|
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: 74.24 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 453 PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMlsgiahdPIqrdmftPLF---------LGAQL 523
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCI-------PV------PLFhcfgsvlgvLACLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 524 H----VPTADDIGTPGRLAEwMADSEVTVTHLTPAMG-QLLSAQATRQIP--TLKNAFFVGDVLTKRDCTRLQSL--AKN 594
Cdd:cd05917 68 HgatmVFPSPSFDPLAVLEA-IEKEKCTALHGVPTMFiAELEHPDFDKFDlsSLRTGIMAGAPCPPELMKRVIEVmnMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 595 VCIInmYGTTETQrAVSYFAIPsvnEDSTFlatqKDLIPAGQGMIDVQLLVVNRTDRNIPcAVGEMGEIYVRSGGLAEGY 674
Cdd:cd05917 147 VTIA--YGMTETS-PVSTQTRT---DDSIE----KRVNTVGRIMPHTEAKIVDPEGGIVP-PVGVPGELCIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 675 L-DPTATAEkfVVNwfgqnverpdtlkeknpaaaehwfgiRDRMYRSGDLGRYLPDGRVECTGRADDQIkIRGFR-IELG 752
Cdd:cd05917 216 WnDPEKTAE--AID--------------------------GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 753 EIDTHLSRHPLVRE-NVTLVRRDKDEEKVlVSYFVPIDGDELeglmsaseaaddDEEidlktqmirgvkkyrklirDIRE 831
Cdd:cd05917 267 EIEEFLHTHPKVSDvQVVGVPDERYGEEV-CAWIRLKEGAEL------------TEE-------------------DIKA 314
|
410 420 430
....*....|....*....|....*....|.
gi 58269178 832 YLKKKLPSYSVPAVYFPLHKLPLNPNGKIDK 862
Cdd:cd05917 315 YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
312-840 |
1.74e-13 |
|
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: 74.55 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVfSVvdPAYPpsrqtvylsvstprallvis 391
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV-PV--PIYP-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagSLAPSVSDYIsdnlslrllvpaiqltssnvtgsRSDAGEDILapyqqyaqtpagVVLGPDSPATLSFTSGSTGIPKG 471
Cdd:cd05907 63 ---TSSAEQIAYI-----------------------LNDSEAKAL------------FVEDPDDLATIIYTSGTTGRPKG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLTHFFPWMGKRFGLDENSKY-TMLSgIAHDPIQR-DMFTPLFLGAQLHVPTADDIGTPGrlaewMADSEVTVT 549
Cdd:cd05907 105 VMLSHRNILSNALALAERLPATEGDRHlSFLP-LAHVFERRaGLYVPLLAGARIYFASSAETLLDD-----LSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 550 HLTPAMGQLLSAQATRQI-PTLKNAFF---VGDVLTKRDC------TRLQS--LAKNVCIINMYGTTETQRAVSyfaips 617
Cdd:cd05907 179 LAVPRVWEKVYAAIKVKAvPGLKRKLFdlaVGGRLRFAASggaplpAELLHffRALGIPVYEGYGLTETSAVVT------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 618 vnedstfLATQKDLIPA--GQGMIDVQllvvnrtdrnipCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVvnwfgqnve 694
Cdd:cd05907 253 -------LNPPGDNRIGtvGKPLPGVE------------VRIADDGEILVRGPNVMLGYYkNPEATAEALD--------- 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 695 rpdtlkeknpaaAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFR-IELGEIDTHLSRHPLVRENVTLvrr 773
Cdd:cd05907 305 ------------ADGWL-------HTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKASPLISQAVVI--- 362
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58269178 774 dKDEEKVLVSYFVPiDGDELEGLMSASEAADDDEEiDLKTQmirgvKKYRKLIRDIREYLKKKLPSY 840
Cdd:cd05907 363 -GDGRPFLVALIVP-DPEALEAWAEEHGIAYTDVA-ELAAN-----PAVRAEIEAAVEAANARLSRY 421
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
455-862 |
2.97e-13 |
|
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: 72.44 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 455 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtP 534
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVTHLTPAMGQLLsAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETqravSYFa 614
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQAL-ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL----SFI- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 615 ipsvnedsTFLATQKDLIP--AGQGMIDVQLLVVNRTDrnipcavGEMGEIYVRSGGLAEGYLDptataekfvvnwfgqn 692
Cdd:cd17633 152 --------TYNFNQESRPPnsVGRPFPNVEIEIRNADG-------GEIGKIFVKSEMVFSGYVR---------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 693 verpdtLKEKNPaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVrenvtlvr 772
Cdd:cd17633 201 ------GGFSNP----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGI-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 773 rdkdEEKVLVSYfvpidGDELEGlmsaseaadddeEIDLKTQMIRGVKKyrkliRDIREYLKKKLPSYSVPAVYFPLHKL 852
Cdd:cd17633 257 ----EEAIVVGI-----PDARFG------------EIAVALYSGDKLTY-----KQLKRFLKQKLSRYEIPKKIIFVDSL 310
|
410
....*....|
gi 58269178 853 PLNPNGKIDK 862
Cdd:cd17633 311 PYTSSGKIAR 320
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
279-865 |
3.94e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 73.74 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 279 ANAKAHPDRVCVVQSElaegqtmmdgpsrgrRIFTYKQIDEASNILAHALLKN-GLQRGEVVMVYAARSVEMVVCVMGIL 357
Cdd:PRK06839 10 KRAYLHPDRIAIITEE---------------EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 358 KAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDYISdnlslrlLVPAIQLTSsnvTGSRSDAGEDILA 437
Cdd:PRK06839 75 KVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSY-------VQRVISITS---LKEIEDRKIDNFV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 438 PYqqyaqtpagvvlGPDSPATLSFTSGSTGIPKGVKGRHYSLthFFPWMGKRFGLD---ENSKYTMLSGIAHDPIQRDMF 514
Cdd:PRK06839 145 EK------------NESASFIICYTSGTTGKPKGAVLTQENM--FWNALNNTFAIDltmHDRSIVLLPLFHIGGIGLFAF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 515 TPLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNA--FFVGDVLTKRDCTRlQSLA 592
Cdd:PRK06839 211 PTLFAGGVIIVPRKFE---PTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVrwFYNGGAPCPEELMR-EFID 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 593 KNVCIINMYGTTETQravsyfaiPSVnedstFLATQKDLI----PAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSG 668
Cdd:PRK06839 287 RGFLFGQGFGMTETS--------PTV-----FMLSEEDARrkvgSIGKPVLFCDYELIDENKNKVE--VGEVGELLIRGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 669 GLAEGYLD-PTATAEKfvvnwfgqnverpdtlkeknpaaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGF 747
Cdd:PRK06839 352 NVMKEYWNrPDATEET-----------------------------IQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGE 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 748 RIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglMSASEAadddeeidlktqmirgvkkyrklir 827
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS------SVLIEK------------------------- 451
|
570 580 590
....*....|....*....|....*....|....*...
gi 58269178 828 DIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK06839 452 DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
281-865 |
6.16e-13 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 73.10 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:cd12118 14 AAVYPDRTSIVY---------------GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYPPSRQTVYLSVSTPRALLVISSagslapsvSDYISdnlslrLLvpaiqltssnvtgSRSDAGEDILAPYQ 440
Cdd:cd12118 79 AVLNALNTRLDAEEIAFILRHSEAKVLFVDRE--------FEYED------LL-------------AEGDPDFEWIPPAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 441 QYaqtpagvvlgpdSPATLSFTSGSTGIPKGVKGRH---Y--SLThffpwMGKRFGLDENSKY--TMlsgiahdpiqrDM 513
Cdd:cd12118 132 EW------------DPIALNYTSGTTGRPKGVVYHHrgaYlnALA-----NILEWEMKQHPVYlwTL-----------PM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 514 F---------TPLFLGAQ---LHVPTADDIgtpgrlaeWMADSEVTVTHL--TPAMGQLL---SAQATRQIPTLKNAFFV 576
Cdd:cd12118 184 FhcngwcfpwTVAAVGGTnvcLRKVDAKAI--------YDLIEKHKVTHFcgAPTVLNMLanaPPSDARPLPHRVHVMTA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 577 GDVLTKRDCTRLQSLAKNVCIInmYGTTETQRAVSyFAIPSVNEDSTFLATQKDLIpAGQGMIDV---QLLVVN-RTDRN 652
Cdd:cd12118 256 GAPPPAAVLAKMEELGFDVTHV--YGLTETYGPAT-VCAWKPEWDELPTEERARLK-ARQGVRYVgleEVDVLDpETMKP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 653 IPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGR 731
Cdd:cd12118 332 VPRDGKTIGEIVFRGNIVMKGYLkNPEATAEAFRGGWF-----------------------------HSGDLAVIHPDGY 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 732 VECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSyFVpidgdELEGLMSASEAadddeeidl 811
Cdd:cd12118 383 IEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FV-----ELKEGAKVTEE--------- 447
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 58269178 812 ktqmirgvkkyrklirDIREYLKKKLPSYSVP-AVYFplHKLPLNPNGKIDKPAL 865
Cdd:cd12118 448 ----------------EIIAFCREHLAGFMVPkTVVF--GELPKTSTGKIQKFVL 484
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
312-862 |
8.15e-13 |
|
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: 72.17 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPsrQTVYLSVSTPRALLVIS 391
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGP--KAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 SAGSLAPSVSDyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaqtpagvvlgpdsPATLSFTSGSTGIPKG 471
Cdd:cd05973 79 DAANRHKLDSD-----------------------------------------------------PFVMMFTSGTTGLPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLTHFFPWMgkRFGLDENSKYTMLSgiAHDP-----IQRDMFTPLFLGaqlhVPTADDIGTPGRLAEWMADSEV 546
Cdd:cd05973 106 VPVPLRALAAFGAYL--RDAVDLRPEDSFWN--AADPgwaygLYYAITGPLALG----HPTILLEGGFSVESTWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 547 TVTHLT--PAMGQLLSAQ----ATRQIPTLKNAFFVGDVLTKrDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIPS--V 618
Cdd:cd05973 178 GVTNLAgsPTAYRLLMAAgaevPARPKGRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 619 NEDStflatqkdlipAGQGMIDVQLLVVNRTDRNIPcaVGEMG--EIYVRSGGLAegyldptataekfvvnWFGqNVERP 696
Cdd:cd05973 257 HAGS-----------AGRAMPGWRVAVLDDDGDELG--PGEPGrlAIDIANSPLM----------------WFR-GYQLP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 697 DTlkeknPAAAEHWfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKD 776
Cdd:cd05973 307 DT-----PAIDGGY-------YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPE 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 777 EEKVLVSYFVPIDGDEleglmsASEAadddeeidlktqmirgvkkyrkLIRDIREYLKKKLPSYSVP-AVYFpLHKLPLN 855
Cdd:cd05973 375 RTEVVKAFVVLRGGHE------GTPA----------------------LADELQLHVKKRLSAHAYPrTIHF-VDELPKT 425
|
....*..
gi 58269178 856 PNGKIDK 862
Cdd:cd05973 426 PSGKIQR 432
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
453-865 |
1.05e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 71.36 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 453 PDSPATLSFTSGSTGIPKGVKGRHYSLThFFPWMGKRFgLDENSKYTMLSGIAHDPIQRDM---FTPLFLGAQLHVPTAD 529
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALN-SLFDPDDVLLCGLPLFHVNGSVvtlLTPLASGAHVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 530 DIGTPG------RLAE-WMADSEVTVThltPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKnVCIINMYG 602
Cdd:cd05944 79 GYRNPGlfdnfwKLVErYRITSLSTVP---TVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATG-LPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 603 TTETQRAVSyfaipsVNedstFLATQKDLIPAGQGM--IDVQLLVVNRTDRNI-PCAVGEMGEIYVRSGGLAEGYLDpta 679
Cdd:cd05944 155 LTEATCLVA------VN----PPDGPKRPGSVGLRLpyARVRIKVLDGVGRLLrDCAPDEVGEICVAGPGVFGGYLY--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 680 taekfvvnwfgqnverpdTLKEKNPAAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLS 759
Cdd:cd05944 222 ------------------TEGNKNAFVADGWL-------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 760 RHPLVRENVTLVRRDKDEEKVLVSYFvpidgdELEGLMSASEAAdddeeidlktqmirgvkkyrklirdIREYLKKKLPS 839
Cdd:cd05944 277 RHPAVAFAGAVGQPDAHAGELPVAYV------QLKPGAVVEEEE-------------------------LLAWARDHVPE 325
|
410 420
....*....|....*....|....*..
gi 58269178 840 Y-SVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:cd05944 326 RaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
442-865 |
1.76e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 71.35 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 442 YAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGA 521
Cdd:PRK07638 131 YLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 522 QLHV-PTAddigTPGRLAEWMADSEVTVTHLTPAMGQ-LLSAQATRQIPTLknAFFVGDVLTKRDCTRLQSLAKNVCIIN 599
Cdd:PRK07638 211 TVHLmRKF----IPNQVLDKLETENISVMYTVPTMLEsLYKENRVIENKMK--IISSGAKWEAEAKEKIKNIFPYAKLYE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 600 MYGTTETQravsyFAIPSVNEDSTFLATQkdlipAGQGMIDVQLLVVNRTDRNipCAVGEMGEIYVRSGGLAEGYLDPTA 679
Cdd:PRK07638 285 FYGASELS-----FVTALVDEESERRPNS-----VGRPFHNVQVRICNEAGEE--VQKGEIGTVYVKSPQFFMGYIIGGV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 680 TAEKFvvnwfgqnverpdtlkeknpaAAEHWFGIRdrmyrsgDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLS 759
Cdd:PRK07638 353 LAREL---------------------NADGWMTVR-------DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLH 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 760 RHPLVRENVTLVRRDkdeekvlvSYFvpidGDELEGLMSASEAAdddeeidlktqmirgvkkyrkliRDIREYLKKKLPS 839
Cdd:PRK07638 405 EHPAVDEIVVIGVPD--------SYW----GEKPVAIIKGSATK-----------------------QQLKSFCLQRLSS 449
|
410 420
....*....|....*....|....*.
gi 58269178 840 YSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
281-684 |
2.84e-12 |
|
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: 71.31 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQSElaegqtmmdGPSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:cd05921 5 ARQAPDRTWLAERE---------GNGGWRRV-TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYP-PSRQTVYLSvstprallviSSAGSLAPSVSdYISDNLSLRLLVPAIQLTSSNVTGSRSDAGEDILAPY 439
Cdd:cd05921 75 VPAAPVSPAYSlMSQDLAKLK----------HLFELLKPGLV-FAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 440 QQYAQTPAGVVL-------GPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGI--AHDPIQ 510
Cdd:cd05921 144 AELAATPPTAAVdaafaavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLpwNHTFGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 511 RDMFTP-LFLGAQLHVptadDIG--TPGRLAEWMAD-SEVTVT-HLTPAMGQLLSAQATRQIPTLKNAFF--------VG 577
Cdd:cd05921 224 NHNFNLvLYNGGTLYI----DDGkpMPGGFEETLRNlREISPTvYFNVPAGWEMLVAALEKDEALRRRFFkrlklmfyAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 578 DVLTKRDCTRLQSLAKNVC-----IINMYGTTETQravsyfaiPSVNeDSTFLATQKDLI--PAgQGmIDVQLlvvnrtd 650
Cdd:cd05921 300 AGLSQDVWDRLQALAVATVgeripMMAGLGATETA--------PTAT-FTHWPTERSGLIglPA-PG-TELKL------- 361
|
410 420 430
....*....|....*....|....*....|....*
gi 58269178 651 rnIPCavGEMGEIYVRSGGLAEGYL-DPTATAEKF 684
Cdd:cd05921 362 --VPS--GGKYEVRVKGPNVTPGYWrQPELTAQAF 392
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
275-803 |
3.00e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 70.93 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVQSElaegqtmmdgpsrgrRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVM 354
Cdd:PRK06164 14 SLLDAHARARPDAVALIDED---------------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 355 GILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLA-PSVSDYISDNLSLRLlvPAIQLTSSNVTGSRSDAGE 433
Cdd:PRK06164 79 ACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDfAAILAAVPPDALPPL--RAIAVVDDAADATPAPAPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 434 DILAPYQQYAQTP---AGVVLGPDSPATLSFT-SGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKY----------- 498
Cdd:PRK06164 157 ARVQLFALPDPAPpaaAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLlaalpfcgvfg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 499 --TMLSGIAHdpiqrdmftplflGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAMGQLLSAQA--TRQIPTLKnAF 574
Cdd:PRK06164 237 fsTLLGALAG-------------GAPLVCEPVFD---AARTARALRRHRVTHTFGNDEMLRRILDTAgeRADFPSAR-LF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 575 FVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQravSYFAIPSVNEDSTFLATQKDLIPAGQGmidvQLLVVNRTDRNIp 654
Cdd:PRK06164 300 GFASFAPALGELAALARARGVPLTGLYGSSEVQ---ALVALQPATDPVSVRIEGGGRPASPEA----RVRARDPQDGAL- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 655 CAVGEMGEIYVRSGGLAEGYLD-PTATAEKFvvnwfgqnveRPDTlkeknpaaaehWFgirdrmyRSGDLGRYLPDGRVE 733
Cdd:PRK06164 372 LPDGESGEIEIRAPSLMRGYLDnPDATARAL----------TDDG-----------YF-------RTGDLGYTRGDGQFV 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58269178 734 CTGRADDQIKIRGFRIELGEIDTHLSRHPLVReNVTLVRRDKDEEKVLVSYFVPIDGDEL--EGLMSASEAA 803
Cdd:PRK06164 424 YQTRMGDSLRLGGFLVNPAEIEHALEALPGVA-AAQVVGATRDGKTVPVAFVIPTDGASPdeAGLMAACREA 494
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
303-793 |
3.67e-12 |
|
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: 70.81 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 303 DGPSRG-RRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSV 381
Cdd:cd05967 73 DSPVTGtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 382 STPrALLVISSAGSLAPSVSDY---ISDNLSLRLLVPA--IQLTSSNVTGSRSDAGEDILAPYQQYAQTPAGVV-LGPDS 455
Cdd:cd05967 153 AKP-KLIVTASCGIEPGKVVPYkplLDKALELSGHKPHhvLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCVpVAATD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 456 PATLSFTSGSTGIPKGV---KGRH-----YSLTHFfpwmgkrFGLDENSKYTMLSGI----AHDPIqrdMFTPLFLGAQL 523
Cdd:cd05967 232 PLYILYTSGTTGKPKGVvrdNGGHavalnWSMRNI-------YGIKPGDVWWAASDVgwvvGHSYI---VYGPLLHGATT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 524 HVPTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLlsaQATRQIPTlknaffVGDVLTKRDCTRLQSL------------ 591
Cdd:cd05967 302 VLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAI---RAIRKEDP------DGKYIKKYDLSSLRTLflagerldpptl 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 592 -----AKNVCIINMYGTTETQRAVSyfAIPSVNEDSTflatqkdlIPAGQG---MIDVQLLVVNRTDRniPCAVGEMGEI 663
Cdd:cd05967 373 ewaenTLGVPVIDHWWQTETGWPIT--ANPVGLEPLP--------IKAGSPgkpVPGYQVQVLDEDGE--PVGPNELGNI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 664 YVrsgglaEGYLDPTATAekfvvnwfgqnverpdTLKEKNPAAAEHWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIK 743
Cdd:cd05967 441 VI------KLPLPPGCLL----------------TLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVIN 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 58269178 744 IRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDEL 793
Cdd:cd05967 499 VAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI 548
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
304-493 |
4.13e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 70.69 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 304 GPSRGRRiFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVST 383
Cdd:PRK04319 67 DASRKEK-YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 384 PRALLVissagslapsvsdyiSDNLSLRllVPAIQLTSSN---VTGSRSDAGEDILAPYQQYAQTPAG---VVLGPDSPA 457
Cdd:PRK04319 146 AKVLIT---------------TPALLER--KPADDLPSLKhvlLVGEDVEEGPGTLDFNALMEQASDEfdiEWTDREDGA 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 58269178 458 TLSFTSGSTGIPKGVKGRHYS-LTHffpWMGKRFGLD 493
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVHNAmLQH---YQTGKYVLD 242
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
308-865 |
5.08e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 70.43 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRAL 387
Cdd:PLN03102 36 GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 LVISSAGSLAPSVSDYISDNLSlRLLVPAIQLTSSNVTGSRSDAGEDILAPYQQYAQTPAGV-----VLGPDSPATLSFT 462
Cdd:PLN03102 116 FVDRSFEPLAREVLHLLSSEDS-NLNLPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLVarmfrIQDEHDPISLNYT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 463 SGSTGIPKGVKGRHYS--LTHFFPWMGKRFGLDENSKYTMlsgiahdpiqrdmftPLFL--GAQLHVPTADDIGTpgrla 538
Cdd:PLN03102 195 SGTTADPKGVVISHRGayLSTLSAIIGWEMGTCPVYLWTL---------------PMFHcnGWTFTWGTAARGGT----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 539 ewmadsEVTVTHLT-PAMGQLLSAQATRQ---IPTLKNAFFVGD------------VLTKRD------CTRLQSLAKNVc 596
Cdd:PLN03102 255 ------SVCMRHVTaPEIYKNIEMHNVTHmccVPTVFNILLKGNsldlsprsgpvhVLTGGSpppaalVKKVQRLGFQV- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 iINMYGTTETQRAVSYFAIPsvNEDSTFLATQKDLIPAGQGMIDVQLLVVN----RTDRNIPCAVGEMGEIYVRSGGLAE 672
Cdd:PLN03102 328 -MHAYGLTEATGPVLFCEWQ--DEWNRLPENQQMELKARQGVSILGLADVDvknkETQESVPRDGKTMGEIVIKGSSIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 673 GYL-DPTATAEKFVVNWFGqnverpdtlkeknpaaaehwfgirdrmyrSGDLGRYLPDGRVECTGRADDQIKIRGFRIEL 751
Cdd:PLN03102 405 GYLkNPKATSEAFKHGWLN-----------------------------TGDVGVIHPDGHVEIKDRSKDIIISGGENISS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 752 GEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdeleglMSASEAADDDEEIDLKTQMirgvkkyrkliRDIRE 831
Cdd:PLN03102 456 VEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV----------LEKGETTKEDRVDKLVTRE-----------RDLIE 514
|
570 580 590
....*....|....*....|....*....|....
gi 58269178 832 YLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PLN03102 515 YCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
273-477 |
1.05e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 69.52 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqselaegqtmmdgpSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALL--------------FEDQSI-SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGV-----FSVVDPAYPPSrqtvyLSVSTPRALLVissAGSLAPSVSDYISDNLSLRLLVPAIQLTSSNVTGS 427
Cdd:PRK08279 104 WLGLAKLGAVvallnTQQRGAVLAHS-----LNLVDAKHLIV---GEELVEAFEEARADLARPPRLWVAGGDTLDDPEGY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 58269178 428 RSDAGEDILAPYQQYAQTpAGVVLgpDSPATLSFTSGSTGIPKGVKGRHY 477
Cdd:PRK08279 176 EDLAAAAAGAPTTNPASR-SGVTA--KDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
273-482 |
1.56e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 68.68 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVQselaegqtmmdgPSRGRRiFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVY------------RDQGLR-WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSlapsvSDYISdnlSLRLLVP------AIQLTSSNV-- 424
Cdd:PRK08315 85 QFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKD-----SDYVA---MLYELAPelatcePGQLQSARLpe 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58269178 425 ------TGSRSDAG----EDILA-----PYQQYAQTPAGvvLGPDSPATLSFTSGSTGIPKGVkgrhySLTHF 482
Cdd:PRK08315 157 lrrvifLGDEKHPGmlnfDELLAlgravDDAELAARQAT--LDPDDPINIQYTSGTTGFPKGA-----TLTHR 222
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
280-865 |
1.71e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 68.50 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 280 NAKAHPDRVCVVQSELAEgqtmmdgpsrgrrIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKA 359
Cdd:PRK13390 6 HAQIAPDRPAVIVAETGE-------------QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 360 GGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVsdyiSDNLSLRLLVpaiqltssnvtGSRSDAgedilapY 439
Cdd:PRK13390 73 GLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKV----GADLPLRLSF-----------GGEIDG-------F 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 440 QQYAQTPAGVvlGP---DSP--ATLSFTSGSTGIPKGVK----GRHYSLTH--FFPWMGKRFGLDENSKYTMLSGIAHDp 508
Cdd:PRK13390 131 GSFEAALAGA--GPrltEQPcgAVMLYSSGTTGFPKGIQpdlpGRDVDAPGdpIVAIARAFYDISESDIYYSSAPIYHA- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 iqrdmfTPLFLGAQLHVptaddIGTPGRLAEWMaDSEVTVTHLtpamgQLLSAQATRQIPTLknafFV------GDVLTK 582
Cdd:PRK13390 208 ------APLRWCSMVHA-----LGGTVVLAKRF-DAQATLGHV-----ERYRITVTQMVPTM----FVrllkldADVRTR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 583 RDCTRLQSL--AKNVCIINMygttetQRAVSYFAIPSVNE--------DSTFLATQKDLipAGQGMIDVQLL----VVNR 648
Cdd:PRK13390 267 YDVSSLRAVihAAAPCPVDV------KHAMIDWLGPIVYEyyssteahGMTFIDSPDWL--AHPGSVGRSVLgdlhICDD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 649 TDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEkfvvnwfGQNVERPdtlkeknpaaaeHWFGIrdrmyrsGDLGRYL 727
Cdd:PRK13390 339 DGNELP--AGRIGTVYFERDRLPFRYLnDPEKTAA-------AQHPAHP------------FWTTV-------GDLGSVD 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 728 PDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDkdeekvlvsyfvPIDGDELEGLMsaseaaddde 807
Cdd:PRK13390 391 EDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPD------------PEMGEQVKAVI---------- 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 808 eidlktQMIRGVKKYRKLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK13390 449 ------QLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
889-949 |
1.81e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 60.65 E-value: 1.81e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58269178 889 KTIHDIWLSLLPSPPPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIA 949
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
308-766 |
1.90e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 68.45 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIfTYKQI-DEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRA 386
Cdd:PRK08314 33 GRAI-SYRELlEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 387 LLVISS-AGSLAPSV-------------SDYISDNLSLRllVPAIQLTS---SNVTGSRSDAGEDILAPyqqyAQTPAGV 449
Cdd:PRK08314 112 AIVGSElAPKVAPAVgnlrlrhvivaqySDYLPAEPEIA--VPAWLRAEpplQALAPGGVVAWKEALAA----GLAPPPH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 450 VLGPDSPATLSFTSGSTGIPKGVKGRHYSLTH----FFPWmgkrFGLDENSkyTMLSGIahdP------IQRDMFTPLFL 519
Cdd:PRK08314 186 TAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMAnavgSVLW----SNSTPES--VVLAVL---PlfhvtgMVHSMNAPIYA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 520 GAQLHVPTADDIGTPGRLaewMADSEVTVTHLTPAMGQLLSAQ---ATRQIPTLKNAFFVGDVLTKRDCTRLQSLAkNVC 596
Cdd:PRK08314 257 GATVVLMPRWDREAAARL---IERYRVTHWTNIPTMVVDFLASpglAERDLSSLRYIGGGGAAMPEAVAERLKELT-GLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 IINMYGTTET---------QRA-VSYFAIPSVNEDSTflatqkdlipagqgMIDVQLLvvnrtdrnIPCAVGEMGEIYVR 666
Cdd:PRK08314 333 YVEGYGLTETmaqthsnppDRPkLQCLGIPTFGVDAR--------------VIDPETL--------EELPPGEVGEIVVH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 667 SGGLAEGYLD-PTATAEKFVvnwfgqnverpdTLKEKnpaaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIR 745
Cdd:PRK08314 391 GPQVFKGYWNrPEATAEAFI------------EIDGK-------------RFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
490 500
....*....|....*....|.
gi 58269178 746 GFRIELGEIDTHLSRHPLVRE 766
Cdd:PRK08314 446 GFKVWPAEVENLLYKHPAIQE 466
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
641-796 |
5.20e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 66.94 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 641 VQLLVVNRTDRNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVvnwfgqnverpdtlkeknpaaAEHWFgirdrmyR 719
Cdd:PRK07787 302 VETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNrPDATAAAFT---------------------ADGWF-------R 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 720 SGDLGRYLPDGRVECTGR-ADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELEGL 796
Cdd:PRK07787 354 TGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADEL 431
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
312-810 |
8.01e-11 |
|
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: 66.31 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVis 391
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 392 sagslapsvsdyiSDNlslrllvpaiqltssnvtgsrsdagEDIlapyqqyaqtpagvvlgpdspATLSFTSGSTGIPKG 471
Cdd:cd05914 86 -------------SDE-------------------------DDV---------------------ALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLthffpwMGKRFGLDENSKYT----MLS--GIAHD-PIQRDMFTPLFLGAqlHVPTADDIGTPgrLAEWMADS 544
Cdd:cd05914 107 VMLTYRNI------VSNVDGVKEVVLLGkgdkILSilPLHHIyPLTFTLLLPLLNGA--HVVFLDKIPSA--KIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 545 EVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAK------------------------------- 593
Cdd:cd05914 177 QVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFkkvheafggnikefviggakinpdveeflrt 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 594 -NVCIINMYGTTETQRAVSYFAIPSVNEDStflatqkdlipAGQGMIDVQLlvvnRTDRNIPCAvgEMGEIYVRSGGLAE 672
Cdd:cd05914 257 iGFPYTIGYGMTETAPIISYSPPNRIRLGS-----------AGKVIDGVEV----RIDSPDPAT--GEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 673 GYL-DPTATAEKFVVN-WFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKI-RGFRI 749
Cdd:cd05914 320 GYYkNPEATAEAFDKDgWF-----------------------------HTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNI 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58269178 750 ELGEIDTHLSRHPLVRENVTLVRRDKdeeKVLVSYFVPIDGDELEGLMSASEAADDDEEID 810
Cdd:cd05914 371 YPEEIEAKINNMPFVLESLVVVQEKK---LVALAYIDPDFLDVKALKQRNIIDAIKWEVRD 428
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
285-860 |
1.01e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 65.75 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 285 PDRVCVVQselaEGQTMmdgpsrgrrifTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVfs 364
Cdd:PRK03640 16 PDRTAIEF----EEKKV-----------TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 365 vvdpayppsrqTVYLSVS-TPRALLvissagslapsvsdYISDNLSLRLLVPAIQLTSSNVTGSRSDAGEDILAPYQQya 443
Cdd:PRK03640 79 -----------AVLLNTRlSREELL--------------WQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEE-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 444 qtpagVVLGPDSP----ATLSFTSGSTGIPKGVKGRHYSltHFFPWMGK--RFGLDENSKYTMLSGIAHDPIQRDMFTPL 517
Cdd:PRK03640 132 -----AEIQEEFDldevATIMYTSGTTGKPKGVIQTYGN--HWWSAVGSalNLGLTEDDCWLAAVPIFHISGLSILMRSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 518 FLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAM-GQLLSAQATRQIPTLKNAFFVGDVLTKRDcTRLQSLAKNVC 596
Cdd:PRK03640 205 IYGMRVVLVEKFD---AEKINKLLQTGGVTIISVVSTMlQRLLERLGEGTYPSSFRCMLLGGGPAPKP-LLEQCKEKGIP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 597 IINMYGTTETqrAVSYFAIPSvnEDStflatQKDLIPAGQGMIDVQLLVVnrtDRNIPCAVGEMGEIYVRSGGLAEGYLD 676
Cdd:PRK03640 281 VYQSYGMTET--ASQIVTLSP--EDA-----LTKLGSAGKPLFPCELKIE---KDGVVVPPFEEGEIVVKGPNVTKGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 -PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGrYL-PDGRVECTGRADDQIKIRGFRIELGEI 754
Cdd:PRK03640 349 rEDATRETFQDGWF-----------------------------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEI 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 755 DTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdeleglmsASEAADDDEeidlktqmirgvkkyrklirdIREYLK 834
Cdd:PRK03640 399 EEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV------------KSGEVTEEE---------------------LRHFCE 445
|
570 580
....*....|....*....|....*.
gi 58269178 835 KKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:PRK03640 446 EKLAKYKVPKRFYFVEELPRNASGKL 471
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
715-953 |
1.14e-10 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 64.39 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 715 DRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLvsYFVPIDGDELE 794
Cdd:COG3433 76 AQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVG--LLLIVGAVAAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 795 GLMSASEAADDDEeidlktqmirgvkkyrklirdireylkkKLPSYSVPAVYFPLHKLPLNPNGKI--DKPALPFPDTSL 872
Cdd:COG3433 154 DGLAAAAALAALD----------------------------KVPPDVVAASAVVALDALLLLALKVvaRAAPALAAAEAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 873 LAPAPSASTADHTPTQKTIHDIWLSLLPSPPPHITLDENFFDMGGHSILATRLIFEIRKAFvVNAPLGLVFDKPTIAGQA 952
Cdd:COG3433 206 LAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWW 284
|
.
gi 58269178 953 A 953
Cdd:COG3433 285 A 285
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
642-865 |
2.13e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 65.25 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 642 QLLVVN-RTDRNIPCAVGEMGEIYVRSGGLAEGYL-DPTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyR 719
Cdd:PLN02479 383 GLDVVDtKTMKPVPADGKTMGEIVMRGNMVMKGYLkNPKANEEAFANGWF-----------------------------H 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 720 SGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglmsa 799
Cdd:PLN02479 434 SGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPG--------- 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 800 seaADDDEEidlktqmirgvkkyRKLIRDIREYLKKKLPSYSVP--AVYFPlhkLPLNPNGKIDKPAL 865
Cdd:PLN02479 505 ---VDKSDE--------------AALAEDIMKFCRERLPAYWVPksVVFGP---LPKTATGKIQKHVL 552
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
269-479 |
2.32e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.00 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 269 FVGAIPDIFSAN-----------AKAHPDRVCVVqselaegqtmmDGPSRgrRIFTYKQIDEASNILAHALLKNGLQRGE 337
Cdd:PLN02246 10 FRSKLPDIYIPNhlplhdycferLSEFSDRPCLI-----------DGATG--RVYTYADVELLSRRVAAGLHKLGIRQGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 338 VVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRqtVYLSVSTPRALLVISSAgSLAPSVSDYISDNlslrllvpai 417
Cdd:PLN02246 77 VVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE--IAKQAKASGAKLIITQS-CYVDKLKGLAEDD---------- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 418 qltssNVTGSRSDAGEDILAPYQQYAQT----PAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSL 479
Cdd:PLN02246 144 -----GVTVVTIDDPPEGCLHFSELTQAdeneLPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
882-956 |
2.40e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.94 E-value: 2.40e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 882 ADHTPTQKTIHDIWLSLLPSPPPHITLDENFF-DMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEID 956
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLE 76
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
313-860 |
3.83e-10 |
|
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: 63.65 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISS 392
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 393 AGSLApsvsdyisdnlslrllvpaiqltssnvtgsrsdagediLAPYqqyaqtpagvvlgpdspatlsfTSGSTGIPKGV 472
Cdd:cd05935 83 LDDLA--------------------------------------LIPY----------------------TSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 473 KGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDP-IQRDMFTPLFLGAQLHVPTADDIGTpgrLAEWMADSEVTV-TH 550
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWDRET---ALELIEKYKVTFwTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 551 LTPAMGQLLSAQ--ATRQIPTLKNAFFVGDVLTKRDCTRLQSLAkNVCIINMYGTTETQRAVSyfAIPSVNEDSTFLAtq 628
Cdd:cd05935 180 IPTMLVDLLATPefKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTH--TNPPLRPKLQCLG-- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 629 kdlIPAgqgmIDVQLLVVNRTDrNIPCAVGEMGEIYVRSGGLAEGYLD-PTATAEKFVvnwfgqnverpdTLKEKnpaaa 707
Cdd:cd05935 255 ---IP*----FGVDARVIDIET-GRELPPNEVGEIVVRGPQIFKGYWNrPEETEESFI------------EIKGR----- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 708 ehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVTLVRRDKDEEKVLVSYFVP 787
Cdd:cd05935 310 --------RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E-VCVISVPDERVGEEVKAFIV 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58269178 788 IDGdelEGLMSASEaadddeeidlktqmirgvkkyrkliRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:cd05935 381 LRP---EYRGKVTE-------------------------EDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
305-776 |
6.01e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.48 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 305 PSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGvfSVVdpayppsrqtvYLSVSTP 384
Cdd:PRK07768 24 PDAPVRH-TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGA--SLT-----------MLHQPTP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 385 RALLVISSAGSLApsVSDYISDNLSL--RLLVPAIQLTSSNvtGSRSDAGEDILAPyqqyaqTPAGVV-LGPDSPATLSF 461
Cdd:PRK07768 90 RTDLAVWAEDTLR--VIGMIGAKAVVvgEPFLAAAPVLEEK--GIRVLTVADLLAA------DPIDPVeTGEDDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 462 TSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKyTMLSGIahdPIQRDM------FTPLFLGAQL-HVPTADDIGTP 534
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETD-VMVSWL---PLFHDMgmvgflTVPMYFGAELvKVTPMDFLRDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 GRLAEWMADSEVTVThLTPA-----MGQLLSAQATRQ---IPTLKNAFFVGDVLTKRDCTRLQSLAKNV-----CIINMY 601
Cdd:PRK07768 236 LLWAELISKYRGTMT-AAPNfayalLARRLRRQAKPGafdLSSLRFALNGAEPIDPADVEDLLDAGARFglrpeAILPAY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 602 GTTETQRAVSY---FAIPSVNE-DSTFLATQKDLIPAGQG-----------MIDVQLLVVNRTDRNIPCAvgEMGEIYVR 666
Cdd:PRK07768 315 GMAEATLAVSFspcGAGLVVDEvDADLLAALRRAVPATKGntrrlatlgppLPGLEVRVVDEDGQVLPPR--GVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 667 SGGLAEGYLdptaTAEKFVvnwfgqnverpdtlkeknPAAAEH-WfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIR 745
Cdd:PRK07768 393 GESVTPGYL----TMDGFI------------------PAQDADgW-------LDTGDLGYLTEEGEVVVCGRVKDVIIMA 443
|
490 500 510
....*....|....*....|....*....|..
gi 58269178 746 GFRIELGEIDTHLSRHPLVRE-NVTLVRRDKD 776
Cdd:PRK07768 444 GRNIYPTDIERAAARVEGVRPgNAVAVRLDAG 475
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
1006-1213 |
6.41e-10 |
|
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. 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: 187543 [Multi-domain] Cd Length: 303 Bit Score: 61.98 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRVrKVICLVRAksadqgLQRLRDSGEGRGVWDEEWVkqdrieavigdlaeekfglsqa 1085
Cdd:cd05232 1 KVLVTGANGFIGRALVDKLLSRGE-EVRIAVRN------AENAEPSVVLAELPDIDSF---------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 ewDRVAEQTDAVLHNGAIVH-----WVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAFVAKADEvvqa 1160
Cdd:cd05232 52 --TDLFLGVDAVVHLAARVHvmndqGADPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVNGEGTVGAPFDE---- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 58269178 1161 ggkgllenDDLEAGRTglnaGYGQSKWVAEKIIMEAGKK-GLSGWILRPGYVLG 1213
Cdd:cd05232 126 --------TDPPAPQD----AYGRSKLEAERALLELGASdGMEVVILRPPMVYG 167
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
307-843 |
7.83e-10 |
|
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: 62.83 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 307 RGRRIFTYKQIDEASNILAHALLKN-GLQRGEVVMVYAARSVEMVVCVMGILKAGGVfsvvdPAYppsrqtvylsvstpr 385
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 386 allvissagslapsvsdyISDNLSLRLLVPAIqltssNVTGSRSdagedilapyqqyaqtpagVVLGPDSPATLSFTSGS 465
Cdd:cd05937 61 ------------------INYNLSGDPLIHCL-----KLSGSRF-------------------VIVDPDDPAILIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 466 TGIPKGV---KGRHYSLTHFFPwmgKRFGLDENSKytmlsgiahdpiqrdMFT--PLFLGAQLHVPTADDIGTPGRLAE- 539
Cdd:cd05937 99 TGLPKAAaisWRRTLVTSNLLS---HDLNLKNGDR---------------TYTcmPLYHGTAAFLGACNCLMSGGTLALs 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 540 --------W--MADSEVT-VTHLTPAMGQLLSAQATR--QIPTLKNAFFVG---DVLTK-RDctRLqslakNVCII-NMY 601
Cdd:cd05937 161 rkfsasqfWkdVRDSGATiIQYVGELCRYLLSTPPSPydRDHKVRVAWGNGlrpDIWERfRE--RF-----NVPEIgEFY 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 602 GTTE-----TQRAVSYFAIPSVNEDSTF--LATQKDLIPAGQGMIDVQLLVVNRTDRNIPCAVGEMGEIYVR----SGGL 670
Cdd:cd05937 234 AATEgvfalTNHNVGDFGAGAIGHHGLIrrWKFENQVVLVKMDPETDDPIRDPKTGFCVRAPVGEPGEMLGRvpfkNREA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 671 AEGYL-DPTATAEKFVVNWFgqnverpdtlkEKNpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRI 749
Cdd:cd05937 314 FQGYLhNEDATESKLVRDVF-----------RKG-----------DIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENV 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 750 ELGEIDTHLSRHPLVRE-NVTLVRrdkdeekvlvsyfVP-IDGDELEGLMSASEAADDDEEIDLKTqmirgvkkyrklir 827
Cdd:cd05937 372 STTEVADVLGAHPDIAEaNVYGVK-------------VPgHDGRAGCAAITLEESSAVPTEFTKSL-------------- 424
|
570
....*....|....*.
gi 58269178 828 dIREYLKKKLPSYSVP 843
Cdd:cd05937 425 -LASLARKNLPSYAVP 439
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
461-861 |
8.96e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 62.40 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 461 FTSGSTGIPKGVKGRHYSLthFFPWMGKR---FGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTP--- 534
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDI--FRMLMGGAdfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQtvv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 535 ---GRL---AEWMADSEVTVTHLT---PAMG----QLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMY 601
Cdd:cd05924 88 lpdDRFdpeEVWRTIEKHKVTSMTivgDAMArpliDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 602 GTTETQRAVSYFAIPSVNEDSTFLATQKDLIpagqgmidvqllVVNRTDRNIPCAVGEMGEIyVRSGGLAEGYL-DPTAT 680
Cdd:cd05924 168 GSSETGFTGSGHSAGSGPETGPFTRANPDTV------------VLDDDGRVVPPGSGGVGWI-ARRGHIPLGYYgDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 681 AEKFVvnwfgqnverpdtlkEKNPAaaehwfgirdRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSR 760
Cdd:cd05924 235 AETFP---------------EVDGV----------RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 761 HPLVRENVTLVRRDkdeEKVlvsyfvpidGDELEGLMSASEAADDDEEidlktqmirgvkkyrklirDIREYLKKKLPSY 840
Cdd:cd05924 290 HPAVYDVLVVGRPD---ERW---------GQEVVAVVQLREGAGVDLE-------------------ELREHCRTRIARY 338
|
410 420
....*....|....*....|.
gi 58269178 841 SVPAVYFPLHKLPLNPNGKID 861
Cdd:cd05924 339 KLPKQVVFVDEIERSPAGKAD 359
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
310-793 |
1.12e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 62.78 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 310 RIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPpSRQTVYLSVSTPRALLV 389
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL-REESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 390 ISSAgsLAPSVSDYISDNlslrllvpAIQLTSSNVTGSRSDAGEDILAPYQQYAQTPA----GVVLGPDSPATLSFTSGS 465
Cdd:PRK08008 115 TSAQ--FYPMYRQIQQED--------ATPLRHICLTRVALPADDGVSSFTQLKAQQPAtlcyAPPLSTDDTAEILFTSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 466 TGIPKGVKGRHYSLT---HFFPWMGKrfgLDENSKY-TMLSGIaHDPIQRDMFTPLF-LGAQLHVptaddIGTPGRLAEW 540
Cdd:PRK08008 185 TSRPKGVVITHYNLRfagYYSAWQCA---LRDDDVYlTVMPAF-HIDCQCTAAMAAFsAGATFVL-----LEKYSARAFW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 541 --MADSEVTVTHLTPAMGQLLSAQ---ATRQIPTLKNAFFVGDVLT--KRD-CTRLqslakNVCIINMYGTTETqravsy 612
Cdd:PRK08008 256 gqVCKYRATITECIPMMIRTLMVQppsANDRQHCLREVMFYLNLSDqeKDAfEERF-----GVRLLTSYGMTET------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 613 faIPSVNEDStflATQKDLIPA-GQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRsgGLA------EGYLDPTATAEKFv 685
Cdd:PRK08008 325 --IVGIIGDR---PGDKRRWPSiGRPGFCYEAEIRDDHNRPLP--AGEIGEICIK--GVPgktifkEYYLDPKATAKVL- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 686 vnwfgqnveRPDTlkeknpaaaehWFGIRDRMYRSGDLGRYLPDgrvectgRADDQIKIRGFRIELGEIDTHLSRHPLVR 765
Cdd:PRK08008 395 ---------EADG-----------WLHTGDTGYVDEEGFFYFVD-------RRCNMIKRGGENVSCVELENIIATHPKIQ 447
|
490 500
....*....|....*....|....*...
gi 58269178 766 ENVTLVRRDKDEEKVLVSYFVPIDGDEL 793
Cdd:PRK08008 448 DIVVVGIKDSIRDEAIKAFVVLNEGETL 475
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
274-865 |
1.21e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.40 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 274 PDIFsanAKAHPDRVCVVQselaegqtmmdgPSRGRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCV 353
Cdd:PRK13391 3 PGIH---AQTTPDKPAVIM------------ASTGEVV-TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 354 MGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSDYISdNLSLRLLVpaiqltssnvtgsrsdAGE 433
Cdd:PRK13391 67 WAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCP-GVRHRLVL----------------DGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 434 DILAPYQQYAQTPAGVvlgPDSP-------ATLSFTSGSTGIPKGVK--------GRHYSLTHFFpwmGKRFGLDENSKY 498
Cdd:PRK13391 130 GELEGFVGYAEAVAGL---PATPiadeslgTDMLYSSGTTGRPKGIKrplpeqppDTPLPLTAFL---QRLWGFRSDMVY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 499 TMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtPGRLAEWMADSEVTVTHLTPAM--GQLLSAQATRQ---IPTLKNA 573
Cdd:PRK13391 204 LSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFD---AEQYLALIEEYGVTHTQLVPTMfsRMLKLPEEVRDkydLSSLEVA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 574 FFVG---DVLTKRDCTRLQSlaknVCIINMYGTTEtqravsyfaipsvNEDSTFLATQKDLI---PAGQGMI-DVQLLvv 646
Cdd:PRK13391 281 IHAAapcPPQVKEQMIDWWG----PIIHEYYAATE-------------GLGFTACDSEEWLAhpgTVGRAMFgDLHIL-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 647 nrTDRNIPCAVGEMGEIYVRSGGLAEGYLDPTATAEkfvvnwfgqnverpdtlkeknpaaAEHwfgIRDRMYRSGDLGRY 726
Cdd:PRK13391 342 --DDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAE------------------------ARH---PDGTWSTVGDIGYV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 727 LPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPlvrenvtlvrrdkdeeKVL-VSYF-VPidgdeleglmsaseaaD 804
Cdd:PRK13391 393 DEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHP----------------KVAdAAVFgVP----------------N 440
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58269178 805 DD--EEIDLKTQMIRGVKKYRKLIRDIREYLKKKLPSYSVP-AVYFpLHKLPLNPNGKIDKPAL 865
Cdd:PRK13391 441 EDlgEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPrSIDF-EDELPRLPTGKLYKRLL 503
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
1006-1213 |
1.34e-09 |
|
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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: 187552 [Multi-domain] Cd Length: 331 Bit Score: 61.29 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRvrkvicLVRAKSADqglqrLRDSGEGRGVWDeewvkQDRIEAVIGDLAEEKFgLSQA 1085
Cdd:cd05241 1 SVLVTGGSGFFGERLVKQLLERG------GTYVRSFD-----IAPPGEALSAWQ-----HPNIEFLKGDITDRND-VEQA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 EwdrvaEQTDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeafvakadevvqAGGKGL 1165
Cdd:cd05241 64 L-----SGADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCGVQKFVYTSSSSV---------------IFGGQN 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 58269178 1166 LENDDLEAGRTGL-NAGYGQSKWVAEKIIMEA-GKKGLSGWILRPGYVLG 1213
Cdd:cd05241 124 IHNGDETLPYPPLdSDMYAETKAIAEIIVLEAnGRDDLLTCALRPAGIFG 173
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
1007-1213 |
2.61e-09 |
|
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: 59.23 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLLSRRVRkVICLVRAKSADQglqrlrdsgegrgvwdeeWVKQDRIEAVIGDLAEekfglsQAE 1086
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEKGYE-VIGLDRLTSASN------------------TARLADLRFVEGDLTD------RDA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1087 WDRVAEQT--DAVLHNGAIVHW----VYPYPKLRAaNVISTVTALQLCAQHHSKQFSFISSTAVldaeafVAKADEVVQa 1160
Cdd:pfam01370 56 LEKLLADVrpDAVIHLAAVGGVgasiEDPEDFIEA-NVLGTLNLLEAARKAGVKRFLFASSSEV------YGDGAEIPQ- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 58269178 1161 ggkglleNDDLEAGRTGLNAGYGQSKWVAEKIIMEAGKK-GLSGWILRPGYVLG 1213
Cdd:pfam01370 128 -------EETTLTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLFNVYG 174
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
313-765 |
2.91e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 61.32 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKNGLQRG--EVVMVYAarSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVI 390
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGmrAVLMVPP--GPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 391 SSAgslapsvsdyisdnlslrllvpaiqltssnvtgsrsdagedilapyqqyaqtpagvvlgpDSPATLSFTSGSTGIPK 470
Cdd:cd05910 82 PKA------------------------------------------------------------DEPAAILFTSGSTGTPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 471 GVKGRHYSLTHFFPWMGKRFgldenskytmlsGIAHDpiQRDMFT-PLF--LGAQLHV--------PTADDIGTPGRLAE 539
Cdd:cd05910 102 GVVYRHGTFAAQIDALRQLY------------GIRPG--EVDLATfPLFalFGPALGLtsvipdmdPTRPARADPQKLVG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 540 WMADSEVTVTHLTPAMGQLLS---AQATRQIPTLKNAFFVGDVLTKRDCTRLQS-LAKNVCIINMYGTTEtqravsyfAI 615
Cdd:cd05910 168 AIRQYGVSIVFGSPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLRKmLSDEAEILTPYGATE--------AL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 616 P-SVNEDSTFLATQKDLIPAGQGM-----ID-VQLLVVNRTDRNIP-------CAVGEMGEIYVrSGglaegyldPTATA 681
Cdd:cd05910 240 PvSSIGSRELLATTTAATSGGAGTcvgrpIPgVRVRIIEIDDEPIAewddtleLPRGEIGEITV-TG--------PTVTP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 682 ekfvvnwfgQNVERPD-TLKEKNPAAAEhwfGIRDRMyrsGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSR 760
Cdd:cd05910 311 ---------TYVNRPVaTALAKIDDNSE---GFWHRM---GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNT 375
|
....*
gi 58269178 761 HPLVR 765
Cdd:cd05910 376 HPGVR 380
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
310-770 |
3.11e-09 |
|
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: 61.35 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 310 RIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLV 389
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 390 ----------------ISSAGSLAPSVSDYISDNLSLRLLVPAiqltssnvtgsrsdAGEDILAPYQQYAQTPAGVVLGP 453
Cdd:cd05968 170 adgftrrgrevnlkeeADKACAQCPTVEKVVVVRHLGNDFTPA--------------KGRDLSYDEEKETAGDGAERTES 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 454 DSPATLSFTSGSTGIPKGVKGRHYSlthfFPW-----MGKRFGLDENSKYTMLS--GIAHDPIQrdMFTPLFLGAQLHV- 525
Cdd:cd05968 236 EDPLMIIYTSGTTGKPKGTVHVHAG----FPLkaaqdMYFQFDLKPGDLLTWFTdlGWMMGPWL--IFGGLILGATMVLy 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 526 PTADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATrqiptlknaffvgDVLTKRDCTRLQSLAK------------ 593
Cdd:cd05968 310 DGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGD-------------APVNAHDLSSLRVLGStgepwnpepwnw 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 594 --------NVCIINMYGTTETQRAV--SYFAIPSvnEDSTFLATqkdlIPagqGMIDVQLlvvnrTDRNIPcAVGEMGEI 663
Cdd:cd05968 377 lfetvgkgRNPIINYSGGTEISGGIlgNVLIKPI--KPSSFNGP----VP---GMKADVL-----DESGKP-ARPEVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 664 YVRSG--GLAEGYL-DPTATAEKFVVNWfgqnverpdtlkeknpaaaehwfgirDRMYRSGDLGRYLPDGRVECTGRADD 740
Cdd:cd05968 442 VLLAPwpGMTRGFWrDEDRYLETYWSRF--------------------------DNVWVHGDFAYYDEEGYFYILGRSDD 495
|
490 500 510
....*....|....*....|....*....|
gi 58269178 741 QIKIRGFRIELGEIDTHLSRHPLVRENVTL 770
Cdd:cd05968 496 TINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
281-476 |
3.36e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.43 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQSelaegqtmmdGPSRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:PRK08180 49 AQEAPDRVFLAER----------GADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAY-----PPSRQTVYLSVSTPrALLVISSAGSLAPSVSdyisdnlslrllvpAIQLTSSNVTGSRSDAGEDI 435
Cdd:PRK08180 119 VPYAPVSPAYslvsqDFGKLRHVLELLTP-GLVFADDGAAFARALA--------------AVVPADVEVVAVRGAVPGRA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 58269178 436 LAPYQQYAQTPAGV-------VLGPDSPATLSFTSGSTGIPKGVKGRH 476
Cdd:PRK08180 184 ATPFAALLATPPTAavdaahaAVGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
1006-1256 |
3.40e-09 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. 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. 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: 187538 [Multi-domain] Cd Length: 301 Bit Score: 59.98 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSR--RVRKViclVRAKSADQGLQRLRDSGEGRgvwdeewvkqDRIEAVIGDLAeekfgLS 1083
Cdd:cd05227 1 LVLVTGATGFIASHIVEQLLKAgyKVRGT---VRSLSKSAKLKALLKAAGYN----------DRLEFVIVDDL-----TA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1084 QAEWDRVAEQTDAVLHNGAIVHWVYPYPK---LRAAnVISTVTALQLCAQHHS-KQFSFISST-AVLDAEAfvAKADEVV 1158
Cdd:cd05227 63 PNAWDEALKGVDYVIHVASPFPFTGPDAEddvIDPA-VEGTLNVLEAAKAAGSvKRVVLTSSVaAVGDPTA--EDPGKVF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1159 QaggkgllEND--DLEAGRTGLNAGYGQSKWVAEKII---MEAGKKGLSGWILRPGYVLG----HSQTAVTNtdDFIWRM 1229
Cdd:cd05227 140 T-------EEDwnDLTISKSNGLDAYIASKTLAEKAAwefVKENKPKFELITINPGYVLGpsllADELNSSN--ELINKL 210
|
250 260
....*....|....*....|....*..
gi 58269178 1230 VKGCVqLGLIPEINNaiICCPVDHVAR 1256
Cdd:cd05227 211 LDGKL-PAIPPNLPF--GYVDVRDVAD 234
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
456-862 |
7.14e-09 |
|
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: 59.20 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 456 PATLSFTSGSTGIPKGVKGRHYSL---THFFPWMGKRFGLDENSkyTMLSGIAHDPIQRDMFTPLFLGAqLHVPTADDIg 532
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFfavPDILQKEGLNWVVGDVT--YLPLPATHIGGLWWILTCLIHGG-LCVTGGENT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 533 TPGRLAEWMADSEVTVTHLTP-AMGQLLS--AQATRQIPTLKNAFFVGDVLTKRDcTRLQSLAKNVCIINMYGTTETQRA 609
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPtLLSKLVSelKSANATVPSLRLIGYGGSRAIAAD-VRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 610 vsyfaipsvnedsTFLATQKDLIPA---GQGMIDVQLLVVNRTDRNIPCavGEMGEIYVRSGGLAEGYLD-PTATAEKFV 685
Cdd:cd17635 158 -------------LCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPS--ASFGTIWIKSPANMLGYWNnPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 686 VNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVR 765
Cdd:cd17635 223 DGWV-----------------------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 766 ENVTLVRRDKDEEKVLVSYFVpidgdeleglmsasEAADDDEEIdlktqmirgvkkyrklIRDIREYLKKKLPSYSVPAV 845
Cdd:cd17635 274 ECACYEISDEEFGELVGLAVV--------------ASAELDENA----------------IRALKHTIRRELEPYARPST 323
|
410
....*....|....*..
gi 58269178 846 YFPLHKLPLNPNGKIDK 862
Cdd:cd17635 324 IVIVTDIPRTQSGKVKR 340
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
718-865 |
8.75e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.14 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 718 YRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpidgdeleglm 797
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV----------- 562
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 798 saSEAADDDEEIDLKtqmirgvkkyrKLIRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PTZ00237 563 --LKQDQSNQSIDLN-----------KLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
273-479 |
1.03e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 59.61 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 273 IPDIFSANAKAHPDRVCVVqsELAEGQTmmdgpsrgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVC 352
Cdd:PLN02330 30 LPDFVLQDAELYADKVAFV--EAVTGKA-----------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRqtVYLSVSTPRALLVISSAGSLAPSVSdyisdnlslrLLVPAIQLTSSNVTGSRSdaG 432
Cdd:PLN02330 97 ALGIMAAGGVFSGANPTALESE--IKKQAEAAGAKLIVTNDTNYGKVKG----------LGLPVIVLGEEKIEGAVN--W 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 58269178 433 EDILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGVKGRHYSL 479
Cdd:PLN02330 163 KELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNL 209
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
258-860 |
1.24e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 59.24 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 258 PDPAADLDWCGfvGAIPDIFSANAKAHPDRvcvvqselaegqTMMDgpSRGRRIfTYKQIDEASNILAHALLKNGLQRGE 337
Cdd:PRK05605 21 PWTPHDLDYGD--TTLVDLYDNAVARFGDR------------PALD--FFGATT-TYAELGKQVRRAAAGLRALGVRPGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 338 VVMVYAARSVEMVVCVMGILKAGGVfsVV--DPAYPPSRQTVYLSVSTPRALLVISSAGSLAPSVSD------YISDNLS 409
Cdd:PRK05605 84 RVAIVLPNCPQHIVAFYAVLRLGAV--VVehNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRttpletIVSVNMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 410 ----------LRLLVPAIQLTSSNVTGSRSDAgedilAPYQQYAQTPAGVVLG--------PDSPATLSFTSGSTGIPKG 471
Cdd:PRK05605 162 aampllqrlaLRLPIPALRKARAALTGPAPGT-----VPWETLVDAAIGGDGSdvshprptPDDVALILYTSGTTGKPKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 472 VKGRHYSLT-------HFFPWMGKRfglDEnskyTMLSGIahdpiqrdmftPLF--LGAQLHVPTADDIGtpGRLA---- 538
Cdd:PRK05605 237 AQLTHRNLFanaaqgkAWVPGLGDG---PE----RVLAAL-----------PMFhaYGLTLCLTLAVSIG--GELVllpa 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 539 -------EWMADSEVTVTHLTPAMGQLLSAQATRQ---IPTLKNAFFVGDVLTKRDCTRLQSLAKNVcIINMYGTTET-- 606
Cdd:PRK05605 297 pdidlilDAMKKHPPTWLPGVPPLYEKIAEAAEERgvdLSGVRNAFSGAMALPVSTVELWEKLTGGL-LVEGYGLTETsp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 607 ---------QRAVSYFAIPsvnedstFLATqkdlipagqgmiDVQllVVNRTDRNIPCAVGEMGEIYVRSGGLAEGYL-D 676
Cdd:PRK05605 376 iivgnpmsdDRRPGYVGVP-------FPDT------------EVR--IVDPEDPDETMPDGEEGELLVRGPQVFKGYWnR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDT 756
Cdd:PRK05605 435 PEETAKSFLDGWF-----------------------------RTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 757 HLSRHPLVREN--VTLVRRDKDEEkvLVSYFVPIDGDELeglmsaseaaddDEEidlktqmirgvkkyrklirDIREYLK 834
Cdd:PRK05605 486 VLREHPGVEDAavVGLPREDGSEE--VVAAVVLEPGAAL------------DPE-------------------GLRAYCR 532
|
650 660
....*....|....*....|....*.
gi 58269178 835 KKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:PRK05605 533 EHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
319-865 |
1.32e-08 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 59.40 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 319 EASNILAHALlknGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFsvvdpaYPPSRQ----TVYLSVSTPRALLVISSAg 394
Cdd:cd05928 53 KAANVLSGAC---GLQRGDRVAVILPRVPEWWLVNVACIRTGLVF------IPGTIQltakDILYRLQASKAKCIVTSD- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 395 SLAPSVSDYISD--NLSLRLLVPAiqltssnvtgSRSDAGEDILAPYQQYAQTPAGVVLGPDSPATLSFTSGSTGIPKGV 472
Cdd:cd05928 123 ELAPEVDSVASEcpSLKTKLLVSE----------KSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 473 KGRHYSLTHFFPwMGKRFGLDENSKYTML----SGIAHDPIQrDMFTPLFLGAQL---HVPTADdigtPGRLAEWMADSE 545
Cdd:cd05928 193 EHSHSSLGLGLK-VNGRYWLDLTASDIMWntsdTGWIKSAWS-SLFEPWIQGACVfvhHLPRFD----PLVILKTLSSYP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 546 VTVTHLTPAMGQLLSAQ--ATRQIPTLKNAFFVGDVLTKRDCTRLQSLAkNVCIINMYGTTETQRAVSYFAIPSVNEDST 623
Cdd:cd05928 267 ITTFCGAPTVYRMLVQQdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQT-GLDIYEGYGQTETGLICANFKGMKIKPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 624 flatqkdlipaGQGMI--DVQllVVNRTDRNIPcaVGEMGEIYVRSG-----GLAEGYLD-PTATAEKfvvnwfgqnver 695
Cdd:cd05928 346 -----------GKASPpyDVQ--IIDDNGNVLP--PGTEGDIGIRVKpirpfGLFSGYVDnPEKTAAT------------ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 696 pdtlkeknpaaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDK 775
Cdd:cd05928 399 -----------------IRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 776 DEEKVLVSYFVpidgdelegLMSASEAADDDeeidlktqmirgvkkyrKLIRDIREYLKKKLPSYSVP-AVYFpLHKLPL 854
Cdd:cd05928 462 IRGEVVKAFVV---------LAPQFLSHDPE-----------------QLTKELQQHVKSVTAPYKYPrKVEF-VQELPK 514
|
570
....*....|.
gi 58269178 855 NPNGKIDKPAL 865
Cdd:cd05928 515 TVTGKIQRNEL 525
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
312-764 |
1.38e-08 |
|
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: 59.02 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 312 FTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVfSVvdPAYP---PSRQTVYLSVSTPRALL 388
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHI-SV--PLYPtlnPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 389 VissaGSLA--PSVSDYISDNLSLRLLVPAiqltssnVTGSRSDAGEDILAPYQQYAQTPagvVLGPDSPATLSFTSGST 466
Cdd:cd05932 84 V----GKLDdwKAMAPGVPEGLISISLPPP-------SAANCQYQWDDLIAQHPPLEERP---TRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 467 GIPKGVKGRHYSLTHFFPWMGKRFGLDENSKytMLS--GIAHdpIQRDMF---TPLFLGAQLHVPTADDIgtpgrLAEWM 541
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEENDR--MLSylPLAH--VTERVFvegGSLYGGVLVAFAESLDT-----FVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 542 ADSEVTVTHLTPAMGQLLSAQATRQIPTLK-----NAFFVGDVLTKR-------DCTRL----------------QSLAK 593
Cdd:cd05932 221 QRARPTLFFSVPRLWTKFQQGVQDKIPQQKlnlllKIPVVNSLVKRKvlkglglDQCRLagcgsapvppallewyRSLGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 594 NVCiiNMYGTTETQrAVSYFAIPSVNEDSTflatqkdlipAGQGMIDVQLlvvnrtdrnipcAVGEMGEIYVRSGGLAEG 673
Cdd:cd05932 301 NIL--EAYGMTENF-AYSHLNYPGRDKIGT----------VGNAGPGVEV------------RISEDGEILVRSPALMMG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 674 -YLDPTATAEKFvvnwfgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKI-RGFRIEL 751
Cdd:cd05932 356 yYKDPEATAEAF---------------------TADGFL-------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAP 407
|
490
....*....|...
gi 58269178 752 GEIDTHLSRHPLV 764
Cdd:cd05932 408 APIENKLAEHDRV 420
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
1009-1212 |
2.58e-08 |
|
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. 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 sythase 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: 187671 [Multi-domain] Cd Length: 354 Bit Score: 57.52 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1009 LTGATGYLGAFILKDLLSRrvrkviclvraksaDQGLQRLR--DSGEGRGVWDEEWVKQDRIEAVI--GDLAEEKFglsq 1084
Cdd:cd09811 4 VTGGGGFLGQHIIRLLLER--------------KEELKEIRvlDKAFGPELIEHFEKSQGKTYVTDieGDIKDLSF---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1085 aeWDRVAEQTDAVLHNGAIVHWVYP--YPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeAFVAKADEVVQAGg 1162
Cdd:cd09811 66 --LFRACQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEV----AGPNFKGRPIFNG- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 58269178 1163 kglLENDDLEAGRTglnAGYGQSKWVAEKIIMEAgkkglSGWILRPGYVL 1212
Cdd:cd09811 139 ---VEDTPYEDTST---PPYASSKLLAENIVLNA-----NGAPLKQGGYL 177
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
303-858 |
4.82e-08 |
|
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: 57.37 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 303 DGPSRgrriFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGgvfsvvdpayppsrqtvylSVS 382
Cdd:cd17640 1 KPPKR----ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG-------------------AVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 383 TPRallvissagslapsvsdyisdnlslrllvpaiqltssnvtGSRSDAGEdilaPYQQYAQTPAGVVL---GPDSPATL 459
Cdd:cd17640 58 VVR----------------------------------------GSDSSVEE----LLYILNHSESVALVvenDSDDLATI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 460 SFTSGSTGIPKGVKGRHYSLTHffpwmgkrfGLDENSKYtmlsgIAHDPIQRDM-FTPLFLGAQlhvptaddigtpgRLA 538
Cdd:cd17640 94 IYTSGTTGNPKGVMLTHANLLH---------QIRSLSDI-----VPPQPGDRFLsILPIWHSYE-------------RSA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 539 EW------MADSEVTVTHLTPAMgQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQ---------------------SL 591
Cdd:cd17640 147 EYfifacgCSQAYTSIRTLKDDL-KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKqflflfflsggifkfgisgggAL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 592 AK---------NVCIINMYGTTETQRAVSyFAIPSVNEDSTflatqkdlipAGQGMIDVQLLVVNrTDRNIPCAVGEMGE 662
Cdd:cd17640 226 PPhvdtffeaiGIEVLNGYGLTETSPVVS-ARRLKCNVRGS----------VGRPLPGTEIKIVD-PEGNVVLPPGEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 663 IYVRSGGLAEGYL-DPTATAEkfVVNwfgqnverpdtlkeknpaaAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQ 741
Cdd:cd17640 294 VWVRGPQVMKGYYkNPEATSK--VLD-------------------SDGWF-------NTGDLGWLTCGGELVLTGRAKDT 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 742 IKIR-GFRIELGEIDTHLSRHPLVrENVTLVRRDkdeEKVLVSYFVPiDGDELE------GLMSASEAADDDEEIDLktq 814
Cdd:cd17640 346 IVLSnGENVEPQPIEEALMRSPFI-EQIMVVGQD---QKRLGALIVP-NFEELEkwakesGVKLANDRSQLLASKKV--- 417
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 58269178 815 mirgVKKYRKLIRDIREylKKKLPSYSVPAVYFPLHKLPLNPNG 858
Cdd:cd17640 418 ----LKLYKNEIKDEIS--NRPGFKSFEQIAPFALLEEPFIENG 455
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
308-471 |
8.88e-08 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 56.42 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIfTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPrAL 387
Cdd:PRK07514 26 GLRY-TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEP-AL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 388 LVISSA--GSLAPsvsdyisdnLSLRLLVPAIQLTSSNVTGSRSDAGEDilAPyqqyaQTPAGVVLGPDSPATLSFTSGS 465
Cdd:PRK07514 104 VVCDPAnfAWLSK---------IAAAAGAPHVETLDADGTGSLLEAAAA--AP-----DDFETVPRGADDLAAILYTSGT 167
|
....*.
gi 58269178 466 TGIPKG 471
Cdd:PRK07514 168 TGRSKG 173
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
306-472 |
1.56e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 306 SRGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPR 385
Cdd:PRK05857 36 CDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 386 ALLVISSAGSLAPSVSDYISDnlslrllVPAIQLTSSnvtgsrSDAGEDILAPYQQYAQTPAGvvLGPDSPATLSFTSGS 465
Cdd:PRK05857 116 AALVAPGSKMASSAVPEALHS-------IPVIAVDIA------AVTRESEHSLDAASLAGNAD--QGSEDPLAMIFTSGT 180
|
....*..
gi 58269178 466 TGIPKGV 472
Cdd:PRK05857 181 TGEPKAV 187
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
690-860 |
2.46e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 54.66 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 690 GQNVERPDTLKEKnpaaaehwfgIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVT 769
Cdd:PRK08308 275 GSDENAPEEIVVK----------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 770 LVRRDkdeekvlvsyfvPIDGDELEGLMSASEAADDDEeidlktqmirgvkkyrklirdIREYLKKKLPSYSVPAVYFPL 849
Cdd:PRK08308 345 YRGKD------------PVAGERVKAKVISHEEIDPVQ---------------------LREWCIQHLAPYQVPHEIESV 391
|
170
....*....|.
gi 58269178 850 HKLPLNPNGKI 860
Cdd:PRK08308 392 TEIPKNANGKV 402
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
595-764 |
6.43e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 53.81 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 595 VCIINMYGTTETQRAVSyfaipsVNedstFLATQKDLIPAGQGM--IDVQLLVVNRTDRNI-PCAVGEMGEIYVRSGGLA 671
Cdd:PRK07529 359 VRIVEGYGLTEATCVSS------VN----PPDGERRIGSVGLRLpyQRVRVVILDDAGRYLrDCAVDEVGVLCIAGPNVF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 672 EGYLDPTataekfvvnwfgqnverpdtlKEKNPAAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIkIR-GFRIE 750
Cdd:PRK07529 429 SGYLEAA---------------------HNKGLWLEDGWL-------NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNID 479
|
170
....*....|....
gi 58269178 751 LGEIDTHLSRHPLV 764
Cdd:PRK07529 480 PAAIEEALLRHPAV 493
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
17-225 |
8.43e-07 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 53.15 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 17 LDRWSSRLSALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHILLTSFAILLFRYT 96
Cdd:cd19539 192 LDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARS--------SLFMVLLAAYCVLLRRYT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 97 PDPSLVICTSANASTKPLL------------LKLDIAAEMTFFDVLRQIMEREQEAQA-DDVPITKLVDHIKPEGPLYRV 163
Cdd:cd19539 264 GQTDIVVGTPVAGRNHPRFestvgffvnllpLRVDVSDCATFRDLIARVRKALVDAQRhQELPFQQLVAELPVDRDAGRH 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58269178 164 RFFD-STQVESDASSSlTTDLTLFLLAAPSDTPAT---------RTSVPPLYLRLTYNSLLFTQSRITATLE 225
Cdd:cd19539 344 PLVQiVFQVTNAPAGE-LELAGGLSYTEGSDIPDGakfdlnltvTEEGTGLRGSLGYATSLFDEETIQGFLA 414
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
377-966 |
1.10e-06 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 53.55 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 377 VYLSVSTPRALLVISSAGSLAPSVSDYISDNLSLRLLVPAIQLTSSNVTGSRSDAGEDILAPYQQYAQTPAGVVLGPDSP 456
Cdd:COG3319 67 ALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 457 ATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSKYTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGR 536
Cdd:COG3319 147 ALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLAL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 537 LAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFVGDVLTKRDCTRLQSLAKNVCIINMYGTTETQRAVSYFAIP 616
Cdd:COG3319 227 LAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 617 SVNEDSTFLAtqkdlIPAGQGMIDVQLLVVNRTDRNIPCAVGEMGEIYVRSGGLAEGYLDPTATAekfvvnwfgqnverp 696
Cdd:COG3319 307 AAPGVAGALG-----PIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAA--------------- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 697 dtlkeknPAAAEHWFGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKD 776
Cdd:COG3319 367 -------ALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 777 EEKVLVSYFVPIDGDELEGLMSASEAADddeeidlktqmirgvkkyrklirdireylkkkLPSYSVPAVYFPLHKLPLNP 856
Cdd:COG3319 440 AAAALAAAVVAAAALAAAALLLLLLLLL--------------------------------LPPPLPPALLLLLLLLLLLL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 857 NGKIDKPALPFPDtsllAPAPSASTADHTPTQKTIHDIWLSLLPspPPHITLDENFFDMGGHSILATRLIFEIRKAFVVN 936
Cdd:COG3319 488 LAALLLAAAAPAA----AAAAAAAPAPAAALELALALLLLLLLG--LGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561
|
570 580 590
....*....|....*....|....*....|
gi 58269178 937 APLGLVFDKPTIAGQAAEIDLLRNADLGGA 966
Cdd:COG3319 562 LLLLALLLAPTLAALAAALAAAAAAAALSP 591
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
1006-1213 |
1.43e-06 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 50.61 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSRRVRkVICLVRAKSADQGLQRlrdsgegrgvwdeewvkqDRIEAVIGDLAEEkfglsqA 1085
Cdd:COG0702 1 KILVTGATGFIGRRVVRALLARGHP-VRALVRDPEKAAALAA------------------AGVEVVQGDLDDP------E 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 EWDRVAEQTDAVLHngaIVHwvYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDAEAFvakadevvqaggkgl 1165
Cdd:COG0702 56 SLAAALAGVDAVFL---LVP--SGPGGDFAVDVEGARNLADAAKAAGVKRIVYLSALGADRDSPS--------------- 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 58269178 1166 lenddleagrtglnaGYGQSKWVAEKIIMEAgkkGLSGWILRPGYVLG 1213
Cdd:COG0702 116 ---------------PYLRAKAAVEEALRAS---GLPYTILRPGWFMG 145
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
1010-1239 |
1.80e-06 |
|
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
Pssm-ID: 366449 [Multi-domain] Cd Length: 279 Bit Score: 51.21 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1010 TGATGYLGAFILKDLLSRRVRKVIclvraKSADqglqrLRDSGEgrgvWDEEWVKQDRIEAVIGDLaeekfgLSQAEWDR 1089
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVREGELKEV-----RVFD-----LRESPE----LLEDFSKSNVIKYIQGDV------TDKDDLDN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1090 VAEQTDAVLHNGAI--VHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeAFVAKADEVVQAGGKGL-L 1166
Cdd:pfam01073 63 ALEGVDVVIHTASAvdVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEV----VGPNSYGQPILNGDEETpY 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 1167 ENDDLEAgrtglnagYGQSKWVAEKIIMEAGKKGLSG------WILRPGYVLGHSqtavtntDDFIWRMVKGCVQLGLI 1239
Cdd:pfam01073 139 ESTHQDA--------YPRSKAIAEKLVLKANGRPLKNggrlytCALRPAGIYGEG-------DRLLVPFIVNLAKLGLA 202
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
308-470 |
6.95e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 50.37 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 308 GRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVfsVVDPAYPPSRQ--TVYLSVSTPR 385
Cdd:PRK10946 45 GERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSelNAYASQIEPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 386 aLLVISSAGSLapsvsdyISDNLSLRLLVpaIQLTSSNVTGSRSDAGEDILApyQQYAQTPAGVVLGP---DSPATLSFT 462
Cdd:PRK10946 123 -LLIADRQHAL-------FSDDDFLNTLV--AEHSSLRVVLLLNDDGEHSLD--DAINHPAEDFTATPspaDEVAFFQLS 190
|
....*...
gi 58269178 463 SGSTGIPK 470
Cdd:PRK10946 191 GGSTGTPK 198
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
281-865 |
7.87e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 50.33 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 281 AKAHPDRVCVVQselaegqtmmdgpsrGRRIFTYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAG 360
Cdd:PRK08162 28 AEVYPDRPAVIH---------------GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 361 GVFSVVDPAYPPSRQTVYLSVSTPRALLVissagslAPSVSDYISDNLslrLLVPAIQLTSSNVTGSRSDAGEDILA-PY 439
Cdd:PRK08162 93 AVLNTLNTRLDAASIAFMLRHGEAKVLIV-------DTEFAEVAREAL---ALLPGPKPLVIDVDDPEYPGGRFIGAlDY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 440 QQYAQT--PAGVVLGPDS---PATLSFTSGSTGIPKGVKGRH---Y--SLTHFFPW-MGKRfgldenSKYtmlsgiahdp 508
Cdd:PRK08162 163 EAFLASgdPDFAWTLPADewdAIALNYTSGTTGNPKGVVYHHrgaYlnALSNILAWgMPKH------PVY---------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 509 iqrdMFT-PLF------------LGAQLHVPTADdiGTPGRLAEWMADSEVTvtHLTPA---MGQLLSA-QATRQIPTLK 571
Cdd:PRK08162 227 ----LWTlPMFhcngwcfpwtvaARAGTNVCLRK--VDPKLIFDLIREHGVT--HYCGApivLSALINApAEWRAGIDHP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 572 NAFFVGD------VLTKRDctrlqslAKNVCIINMYGTTETQRAVSYFAI-PSVNEDStfLATQKDLiPAGQG----MID 640
Cdd:PRK08162 299 VHAMVAGaappaaVIAKME-------EIGFDLTHVYGLTETYGPATVCAWqPEWDALP--LDERAQL-KARQGvrypLQE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 641 vQLLVVNR-TDRNIPcAVGE-MGEIYVRSGGLAEGYL-DPTATAEKFVVNWFgqnverpdtlkeknpaaaeHwfgirdrm 717
Cdd:PRK08162 369 -GVTVLDPdTMQPVP-ADGEtIGEIMFRGNIVMKGYLkNPKATEEAFAGGWF-------------------H-------- 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 718 yrSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSyFVpidgdELEGLM 797
Cdd:PRK08162 420 --TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA-FV-----ELKDGA 491
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 798 SASEAadddeeidlktqmirgvkkyrklirDIREYLKKKLPSYSVP-AVYFPlhKLPLNPNGKIDKPAL 865
Cdd:PRK08162 492 SATEE-------------------------EIIAHCREHLAGFKVPkAVVFG--ELPKTSTGKIQKFVL 533
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
20-167 |
9.97e-06 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 49.64 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 20 WSSRLS-ALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHILLTSFAILLFRYTPD 98
Cdd:pfam00668 198 WLEQLEgELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGT--------TLNDVLLAAYGLLLSRYTGQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 99 PSLVICT------SANASTKP------LLLKLDIAAEMTFFDVLRQIMEREQEAQ-ADDVPITKLVDHIKPEGPLYRVRF 165
Cdd:pfam00668 270 DDIVVGTpgsgrpSPDIERMVgmfvntLPLRIDPKGGKTFSELIKRVQEDLLSAEpHQGYPFGDLVNDLRLPRDLSRHPL 349
|
..
gi 58269178 166 FD 167
Cdd:pfam00668 350 FD 351
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
313-860 |
1.19e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.82 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKN-GLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPP-----------SRQTVYLS 380
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAremrhqfkdsgARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 381 V----------STPRALLVISSAGSLAPSVSDYISDNL--SLRLLVPAIQLtssnvtgSRSDAGEDILAPYQQYAQTPag 448
Cdd:PRK12492 131 MfgklvqevlpDTGIEYLIEAKMGDLLPAAKGWLVNTVvdKVKKMVPAYHL-------PQAVPFKQALRQGRGLSLKP-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 449 VVLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFG-LDENSKYTMLSGiahdpiQRDMFTPLFLgAQLHVPT 527
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqLGPDGQPLMKEG------QEVMIAPLPL-YHIYAFT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 528 AD------------------DI-GTPGRLAEWMADSEVTVTHLTPAmgqLLSAQATRQI--PTLKNAFFVGDVLTKRDCT 586
Cdd:PRK12492 275 ANcmcmmvsgnhnvlitnprDIpGFIKELGKWRFSALLGLNTLFVA---LMDHPGFKDLdfSALKLTNSGGTALVKATAE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 587 RLQSLAkNVCIINMYGTTETQRAVSyfAIPsvnedstfLATQKDLIPAGQGMIDVQLLVVNrtDRNIPCAVGEMGEIYVR 666
Cdd:PRK12492 352 RWEQLT-GCTIVEGYGLTETSPVAS--TNP--------YGELARLGTVGIPVPGTALKVID--DDGNELPLGERGELCIK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 667 SGGLAEGYLD-PTATAEKFvvnwfgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIR 745
Cdd:PRK12492 419 GPQVMKGYWQqPEATAEAL---------------------DAEGWF-------KTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 746 GFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGdeleglmsaseaadddeeidlktqmirGVKkyrkl 825
Cdd:PRK12492 471 GFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP---------------------------GLS----- 518
|
570 580 590
....*....|....*....|....*....|....*
gi 58269178 826 IRDIREYLKKKLPSYSVPAVYFPLHKLPLNPNGKI 860
Cdd:PRK12492 519 VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
429-762 |
1.39e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 49.29 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 429 SDAGEDILAPYQQyAQTPAGVVlGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGL--DENSKYTMlsgiah 506
Cdd:PRK07867 129 SPAWADELAAHRD-AEPPFRVA-DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLgpDDVCYVSM------ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 507 dpiqrdmftPLFLGAQLHVPTADDIGTPGRLA--------EWMAD-SEVTVTHLTpAMGQLLS-AQATRQIP-----TLK 571
Cdd:PRK07867 201 ---------PLFHSNAVMAGWAVALAAGASIAlrrkfsasGFLPDvRRYGATYAN-YVGKPLSyVLATPERPddadnPLR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 572 NAFfvGDVLTKRDCTRLQSlAKNVCIINMYGTTETqrAVSYFAIPSVNEDSTFLAtqkdliPAGQGMIDVqllvvnrtDR 651
Cdd:PRK07867 271 IVY--GNEGAPGDIARFAR-RFGCVVVDGFGSTEG--GVAITRTPDTPPGALGPL------PPGVAIVDP--------DT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 652 NIPCAVGEMGEIYVRSGGLAEGYLDPTATAEKFVVNWfgqnverpdtlkeKNPAA-AEHwfgIRDRMYRSGDLGRYLPDG 730
Cdd:PRK07867 332 GTECPPAEDADGRLLNADEAIGELVNTAGPGGFEGYY-------------NDPEAdAER---MRGGVYWSGDLAYRDADG 395
|
330 340 350
....*....|....*....|....*....|..
gi 58269178 731 RVECTGRADDQIKIRGFRIELGEIDTHLSRHP 762
Cdd:PRK07867 396 YAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
5-204 |
1.78e-05 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 49.02 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 5 ASELTPEEL-NQRLDRWSSRLSALPS-LALPTDYPRPSpaklVEAYQSMPIPSAL-ATVLMKLTlefSTLFPASGlpTPY 81
Cdd:cd19546 182 AGEDDRDSLiGDQIAYWRDALAGAPDeLELPTDRPRPV----LPSRRAGAVPLRLdAEVHARLM---EAAESAGA--TMF 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 82 HILLTSFAILLFRYTPDPSLVICTSANAST-------------KPLLLKLDIAAEMTFFDVLRQIMEREQEA-QADDVPI 147
Cdd:cd19546 253 TVVQAALAMLLTRLGAGTDVTVGTVLPRDDeegdlegmvgpfaRPLALRTDLSGDPTFRELLGRVREAVREArRHQDVPF 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58269178 148 TKLVDHIKPEGPLYRVRFFD-STQVESDASsslttdltlfllaAPSDT---PATRTSVPPL 204
Cdd:cd19546 333 ERLAELLALPPSADRHPVFQvALDVRDDDN-------------DPWDApelPGLRTSPVPL 380
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
13-173 |
2.98e-05 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 48.03 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 13 LNQRLDRWSSRLSALPS-LALPTDYPRPSPAKlveaYQSM----PIPSALATVLMKLTLEF-STLFpasglptpyHILLT 86
Cdd:cd19538 188 IARQLAYWKKQLAGLPDeIELPTDYPRPAESS----YEGGtltfEIDSELHQQLLQLAKDNnVTLF---------MVLQA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 87 SFAILLFRYTPDPSLVICTS----ANASTKP--------LLLKLDIAAEMTFfdvlRQIMER--EQEAQA---DDVPITK 149
Cdd:cd19538 255 GFAALLTRLGAGTDIPIGSPvagrNDDSLEDlvgffvntLVLRTDTSGNPSF----RELLERvkETNLEAyehQDIPFER 330
|
170 180 190
....*....|....*....|....*....|
gi 58269178 150 LVDHIKPEG-----PLYRVRF-FDSTQVES 173
Cdd:cd19538 331 LVEALNPTRsrsrhPLFQIMLaLQNTPQPS 360
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
640-843 |
3.01e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 48.12 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 640 DVQLLVVNRTDRNIPCAVGEMGEIYVRSGGLA--EGYLDPTATAEKFVVNWFGQNverpdtlkeknpaaaehwfgirDRM 717
Cdd:cd05940 267 ESGEPIRDAEGRCIKVPRGEPGLLISRINPLEpfDGYTDPAATEKKILRDVFKKG----------------------DAW 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 718 YRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTlvrrdkdeekvlvsYFVPIDGDELEGLM 797
Cdd:cd05940 325 FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV--------------YGVQVPGTDGRAGM 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 58269178 798 sASEAADDDEEIDLKtqmirgvkkyrKLIRDIREYlkkkLPSYSVP 843
Cdd:cd05940 391 -AAIVLQPNEEFDLS-----------ALAAHLEKN----LPGYARP 420
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
313-865 |
3.39e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 48.11 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLV--- 389
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCldl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 390 -------ISSAGSLAPSVSDYISDNLSL--RLLVPAIQLTSSNVTGSRSDAGE-DILAPYQQYAQTPAGVVLGPDSP-AT 458
Cdd:PRK06710 131 vfprvtnVQSATKIEHVIVTRIADFLPFpkNLLYPFVQKKQSNLVVKVSESETiHLWNSVEKEVNTGVEVPCDPENDlAL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 459 LSFTSGSTGIPKGVKGRHYSLTHfFPWMGKRFGLDENSKYTMLSGIAhdP------IQRDMFTPLFLGAQLHVPTADDIG 532
Cdd:PRK06710 211 LQYTGGTTGFPKGVMLTHKNLVS-NTLMGVQWLYNCKEGEEVVLGVL--PffhvygMTAVMNLSIMQGYKMVLIPKFDMK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 533 TpgrLAEWMADSEVTVTHLTPAMG-QLLSAqatrqiPTLKNAffvgDVLTKRDC--------TRLQSLAKNVC---IINM 600
Cdd:PRK06710 288 M---VFEAIKKHKVTLFPGAPTIYiALLNS------PLLKEY----DISSIRACisgsaplpVEVQEKFETVTggkLVEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 601 YGTTETqravsyfaipSVNEDSTFLATQKdlIPAGQGM--IDVQLLVVN-RTDRNIPcaVGEMGEIYVRSGGLAEGYLD- 676
Cdd:PRK06710 355 YGLTES----------SPVTHSNFLWEKR--VPGSIGVpwPDTEAMIMSlETGEALP--PGEIGEIVVKGPQIMKGYWNk 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 677 PTATAEKFVVNWFgqnverpdtlkeknpaaaehwfgirdrmyRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDT 756
Cdd:PRK06710 421 PEETAAVLQDGWL-----------------------------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 757 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIDGDELEglmsaseaaddDEEIDlktqmirgvkkyrklirdirEYLKKK 836
Cdd:PRK06710 472 VLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECS-----------EEELN--------------------QFARKY 520
|
570 580
....*....|....*....|....*....
gi 58269178 837 LPSYSVPAVYFPLHKLPLNPNGKIDKPAL 865
Cdd:PRK06710 521 LAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
313-529 |
4.47e-05 |
|
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: 47.74 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 313 TYKQIDEASNILAHALLKNGLQRGEVVMVYAARSVEMVVCVMGILKAGGVFSVVdpaYPP-SRQTVYLSVSTPRA-LLVI 390
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGI---YTTnSPEACQYVAETSEAnILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 391 SSAGSLAP--SVSDYisdnlsLRLLVPAIQLTSS------NVTGSRS--DAGEDIlaPYQQYAQTPAgvVLGPDSPATLS 460
Cdd:cd05933 87 ENQKQLQKilQIQDK------LPHLKAIIQYKEPlkekepNLYSWDEfmELGRSI--PDEQLDAIIS--SQKPNQCCTLI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58269178 461 FTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSK-------YTMLSGIAHDPIqrDMFTPLFLGAQLHVPTAD 529
Cdd:cd05933 157 YTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPLSHIAAQIL--DIWLPIKVGGQVYFAQPD 230
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
452-771 |
5.62e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 47.50 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 452 GPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRFGLDENSkyTMLSGIAhdPIQRDMFT-----PLFLGaqLHVP 526
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDD--VMMSFLP--PFHAYGFNsctlfPLLSG--VPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 527 TADDIGTPGRLAEWMADSEVTVTHLTPAMGQLLSAQATRQIPTLKNAFFV---GDVLTKRDCTRLQSLAKNVCIINMYGT 603
Cdd:PRK06334 255 FAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVvigGDAFKDSLYQEALKTFPHIQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 604 TETQRAVSYfaipsVNEDSTflatqKDLIPAGQGMIDVQLLVVNRtDRNIPCAVGEMGEIYVRSGGLAEGYL--DPTata 681
Cdd:PRK06334 335 TECSPVITI-----NTVNSP-----KHESCVGMPIRGMDVLIVSE-ETKVPVSSGETGLVLTRGTSLFSGYLgeDFG--- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 682 EKFVvnwfgqnverpdtlkeknPAAAEHWfgirdrmYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRH 761
Cdd:PRK06334 401 QGFV------------------ELGGETW-------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
330
....*....|...
gi 58269178 762 ---PLVRENVTLV 771
Cdd:PRK06334 456 fgqNAADHAGPLV 468
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
898-955 |
6.02e-05 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 43.01 E-value: 6.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 898 LLPSPPPHITLDENFFDMGGHSILATRLIFEIRKAFVVNAPLGLVFDKPTIAGQAAEI 955
Cdd:smart00823 25 LGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
713-782 |
7.56e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 47.07 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 713 IRdrmYRSGDLGRYLPD----GR-----VECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL-VRRDKDEEKVLV 782
Cdd:COG1541 295 IR---YRTGDLTRLLPEpcpcGRthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIvVDREGGLDELTV 371
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
453-746 |
1.83e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 45.94 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 453 PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMGKRfgLDENSKYTMLSGIahdPIQRDM------FTPLFLGA-QLHV 525
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNS--TEWKTKDRILSWM---PLTHDMgliafhLAPLIAGMnQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 526 PTADDIGTPgrlAEWMAD-SEVTVTHLT-PAMGQ--LLSAQATRQIP----TLKNAFFVG---------DVLTKRdCTRL 588
Cdd:cd05908 180 PTRLFIRRP---ILWLKKaSEHKATIVSsPNFGYkyFLKTLKPEKANdwdlSSIRMILNGaepidyelcHEFLDH-MSKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 589 qSLAKNvCIINMYGTTETQRAVSyfaIPSVNEDSTFLATQKDLIPAGQGMIDV--------------------QLLVVNR 648
Cdd:cd05908 256 -GLKRN-AILPVYGLAEASVGAS---LPKAQSPFKTITLGRRHVTHGEPEPEVdkkdsecltfvevgkpidetDIRICDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 649 TDRNIPcaVGEMGEIYVRSGGLAEGYL-DPTATAEKFvvnwfgqnverpdtlkeknpaAAEHWFgirdrmyRSGDLGrYL 727
Cdd:cd05908 331 DNKILP--DGYIGHIQIRGKNVTPGYYnNPEATAKVF---------------------TDDGWL-------KTGDLG-FI 379
|
330
....*....|....*....
gi 58269178 728 PDGRVECTGRADDQIKIRG 746
Cdd:cd05908 380 RNGRLVITGREKDIIFVNG 398
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
6-163 |
2.54e-04 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 45.11 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 6 SELTPE-ELNQRLDRWSSRLSALPS-LALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasglpTPYHI 83
Cdd:cd19540 180 DEDDPDsLAARQLAYWRETLAGLPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGA--------TLFMV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 84 LLTSFAILLFRY---------TP-----DPSL--VICTSANastkPLLLKLDIAAEMTFFDVLRQIMEREQEAQA-DDVP 146
Cdd:cd19540 252 LHAALAVLLSRLgagddipigTPvagrgDEALddLVGMFVN----TLVLRTDVSGDPTFAELLARVRETDLAAFAhQDVP 327
|
170 180
....*....|....*....|..
gi 58269178 147 ITKLVDHIKPEG-----PLYRV 163
Cdd:cd19540 328 FERLVEALNPPRstarhPLFQV 349
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
615-748 |
4.31e-04 |
|
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: 44.65 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 615 IPSVNEDStfLATQKDLIPAGQGMIDVQLLVVNRTDRNiPCAVGEMGEIYVRSGGLAEGYldptataekfvvnwFGQNVE 694
Cdd:cd05905 346 VVRLDERD--KPNSLPLQDSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGY--------------FLLDGE 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 695 RPDTLkeKNPAAAEHWFGIRDRMY-RSGDLGrYLpdGRVECT-------------GRADDQIKIRGFR 748
Cdd:cd05905 409 TNDTF--KVFPSTRLSTGITNNSYaRTGLLG-FL--RPTKCTdlnveehdllfvvGSIDETLEVRGLR 471
|
|
| UDP_G4E_3_SDR_e |
cd05240 |
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ... |
1007-1222 |
4.86e-04 |
|
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose 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: 187551 [Multi-domain] Cd Length: 306 Bit Score: 43.90 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLL-SRRVRKVIclvraksadqGLQRLRDSGEGRGVwdeEWVKQDrieaVIGDLAEEKFGLSQA 1085
Cdd:cd05240 1 ILVTGAAGGLGRLLARRLAaSPRVIGVD----------GLDRRRPPGSPPKV---EYVRLD----IRDPAAADVFREREA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1086 ewdrvaeqtDAVLHNGAIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVldaeaFVAKADEVVQaggkgL 1165
Cdd:cd05240 64 ---------DAVVHLAFILDPPRDGAERHRINVDGTQNVLDACAAAGVPRVVVTSSVAV-----YGAHPDNPAP-----L 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 58269178 1166 LENDDLeagRTGLNAGYGQSKWVAEKIIMEAGK--KGLSGWILRPGYVLGHSQTAVTNT 1222
Cdd:cd05240 125 TEDAPL---RGSPEFAYSRDKAEVEQLLAEFRRrhPELNVTVLRPATILGPGTRNTTRD 180
|
|
| SDR_a7 |
cd05262 |
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ... |
1007-1103 |
4.87e-04 |
|
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187572 [Multi-domain] Cd Length: 291 Bit Score: 43.88 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLLSRRVRkVICLVRaksADQGLQRLRDSGegrgvwdeewvkqdrIEAVIGDLAeekfglSQAE 1086
Cdd:cd05262 3 VFVTGATGFIGSAVVRELVAAGHE-VVGLAR---SDAGAAKLEAAG---------------AQVHRGDLE------DLDI 57
|
90
....*....|....*..
gi 58269178 1087 WDRVAEQTDAVLHNGAI 1103
Cdd:cd05262 58 LRKAAAEADAVIHLAFT 74
|
|
| SDR_e_a |
cd05226 |
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
1007-1213 |
5.27e-04 |
|
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) 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. 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. 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: 187537 [Multi-domain] Cd Length: 176 Bit Score: 42.39 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1007 VFLTGATGYLGAFILKDLLsRRVRKVICLVRAKSADQGLQRLRDSgegRGVWDEEWvKQDRIEAVIGDlaeekfglsqae 1086
Cdd:cd05226 1 ILILGATGFIGRALARELL-EQGHEVTLLVRNTKRLSKEDQEPVA---VVEGDLRD-LDSLSDAVQGV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1087 wdrvaeqtDAVLHngaIVHWVYPYPKLRAANVISTVTALQLCAQHHSKQFSFISSTAVLDaeafvakadevvqaggkgll 1166
Cdd:cd05226 64 --------DVVIH---LAGAPRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYG-------------------- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 58269178 1167 enDDLEAGRTGLNAGYGQSKWVAEKIIMEAGKKGLsgwILRPGYVLG 1213
Cdd:cd05226 113 --DLHEETEPSPSSPYLAVKAKTEAVLREASLPYT---IVRPGVIYG 154
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
703-766 |
5.97e-04 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 44.10 E-value: 5.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58269178 703 NPAAAEHwfGIRDRMYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 766
Cdd:cd05974 297 DPDKTAH--AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAE 358
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
534-768 |
1.84e-03 |
|
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: 42.26 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 534 PGRLAEWMADSEVTV-THLTPAMGQLLSAQAT--RQIPTLKNaffVGDVLTKRDCTRLQSLAkNVCIINMYGTTETQRAV 610
Cdd:cd17637 77 PAEALELIEEEKVTLmGSFPPILSNLLDAAEKsgVDLSSLRH---VLGLDAPETIQRFEETT-GATFWSLYGQTETSGLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 611 SYfaIPSVNEDSTflatqkdlipAGQGMIDVQLLVVNRTDRNIPcaVGEMGEIYVRSGGLAEGYldptataekfvvnWfg 690
Cdd:cd17637 153 TL--SPYRERPGS----------AGRPGPLVRVRIVDDNDRPVP--AGETGEIVVRGPLVFQGY-------------W-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 691 qnverpdtlkeKNPAAAEHWFgiRDRMYRSGDLGRYLPDGRVECTGR--ADDQIKIRGFRIELGEIDTHLSRHPLVRENV 768
Cdd:cd17637 204 -----------NLPELTAYTF--RNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVC 270
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
275-481 |
1.93e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 42.73 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 275 DIFSANAKAHPDRVCVVQSelaeGQTMmdgpsrgrrifTYKQIDEASNILAhALLKN--GLQRGEVVMVYAARSVEMVVC 352
Cdd:PRK08974 27 DMFEQAVARYADQPAFINM----GEVM-----------TFRKLEERSRAFA-AYLQNglGLKKGDRVALMMPNLLQYPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 353 VMGILKAGGVFSVVDPAYPPSRQTVYLSVSTPRALLVISS-AGSLAPSVSDY---------ISDNLS------------- 409
Cdd:PRK08974 91 LFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNfAHTLEKVVFKTpvkhviltrMGDQLStakgtlvnfvvky 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58269178 410 LRLLVP------AIQLTSSNVTGSRsdagedilapyQQYAQTpagvVLGPDSPATLSFTSGSTGIPKGVKgrhysLTH 481
Cdd:PRK08974 171 IKRLVPkyhlpdAISFRSALHKGRR-----------MQYVKP----ELVPEDLAFLQYTGGTTGVAKGAM-----LTH 228
|
|
| Gne_like_SDR_e |
cd05238 |
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ... |
1006-1209 |
4.05e-03 |
|
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: 40.83 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1006 TVFLTGATGYLGAFILKDLLSR--RVRKVICLVRAKSADQGLQRLRDsgegrgvwdeewvkqdrieaVIGDLAEEKfgLS 1083
Cdd:cd05238 2 KVLITGASGFVGQRLAERLLSDvpNERLILIDVVSPKAPSGAPRVTQ--------------------IAGDLAVPA--LI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 1084 QAewdRVAEQTDAVLHNGAIV--HWVYPYPKLRAANVISTVTALQLC-AQHHSKQFSFISSTAVLdaeafvakadevvqa 1160
Cdd:cd05238 60 EA---LANGRPDVVFHLAAIVsgGAEADFDLGYRVNVDGTRNLLEALrKNGPKPRFVFTSSLAVY--------------- 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 58269178 1161 gGKGLLENDDLEAGRTGLNAgYGQSKWVAEKIIMEAGKKG--------LSGWILRPG 1209
Cdd:cd05238 122 -GLPLPNPVTDHTALDPASS-YGAQKAMCELLLNDYSRRGfvdgrtlrLPTVCVRPG 176
|
|
| PLN02657 |
PLN02657 |
3,8-divinyl protochlorophyllide a 8-vinyl reductase |
991-1044 |
5.22e-03 |
|
3,8-divinyl protochlorophyllide a 8-vinyl reductase
Pssm-ID: 178263 [Multi-domain] Cd Length: 390 Bit Score: 40.90 E-value: 5.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 58269178 991 PTFSALPADFATK---ELTVFLTGATGYLGAFILKDLLsRRVRKVICLVRAKSADQG 1044
Cdd:PLN02657 44 ATAAAAAQSFRSKepkDVTVLVVGATGYIGKFVVRELV-RRGYNVVAVAREKSGIRG 99
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
8-96 |
5.50e-03 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 40.76 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58269178 8 LTPEELNQRLDRWSSRLS-ALPSLALPTDYPRPSPAKLVEAYQSMPIPSALATVLMKLTLEFSTlfpasGLPTpyhILLT 86
Cdd:cd20484 179 LAGAEGEEHRAYWKQQLSgTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSI-----NLST---VFLG 250
|
90
....*....|
gi 58269178 87 SFAILLFRYT 96
Cdd:cd20484 251 IFKLLLHRYT 260
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
717-766 |
6.31e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 40.89 E-value: 6.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 58269178 717 MYRSGDLGRYLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 766
Cdd:PRK00174 484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
692-766 |
7.94e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 40.41 E-value: 7.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58269178 692 NVERPDtlkeknPAAAEHWFgirdrmyRSGDLGRyLPDGRVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 766
Cdd:PRK07824 223 NPVDPD------PFAEPGWF-------RTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD 283
|
|
| |
