|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
18-525 |
0e+00 |
|
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: 641.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNYphnnTQRFTYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHEL 97
Cdd:cd05941 1 DRIAIVDD----GDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 98 EYTITNSKSSMVLtnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfdinRNAQIIYTSGTTSRPKGVIATH 177
Cdd:cd05941 77 EYVITDSEPSLVL---------------------------------------------DPALILYTSGTTGRPKGVVLTH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 178 SNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRllesgvttDLEQPISLFM 257
Cdd:cd05941 112 ANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAIS--------RLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 258 AVPTIYSKLIKYVEENVKteKERQDIEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHGDR 337
Cdd:cd05941 184 GVPTIYTRLLQYYEAHFT--DPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 338 VSGSVGFPLPGVQVKINAEasstQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNSt 416
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDE----ETGEPL---PRGEVGEIQVRGPSVFKEYWNKPEATKEEFtDDGWFKTGDLGVVDED- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 417 GRFKILGRSSVDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQQRLA 496
Cdd:cd05941 334 GYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*....
gi 330846471 497 YYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-529 |
2.01e-126 |
|
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: 376.84 E-value: 2.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNyphnNTQRFTYNDLLNESAAISNQIT---FKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:COG0318 5 LRRAAARHPDRPALVF----GGRRLTYAELDARARRLAAALRalgVGPGD----RVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLTnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSG 165
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT----------------------------------------------ALILYTSG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGV 245
Cdd:COG0318 111 TTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 246 TTdleqpislFMAVPTIYSKLIKYVeenvktEKERQDiekaFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI 325
Cdd:COG0318 191 TV--------LFGVPTMLARLLRHP------EFARYD----LSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 326 GM-CLSNPL-HGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAFEDGW 403
Cdd:COG0318 253 SPvVTVNPEdPGERRPGSVGRPLPGVEVRIVDE-----DGRELPPG---EVGEIVVRGPNVMKGYWNDPEATAEAFRDGW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 404 FKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmS 483
Cdd:COG0318 325 LRTGDLGRLD-EDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL-D 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 330846471 484 YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLFTQ 529
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-524 |
4.52e-111 |
|
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: 338.38 E-value: 4.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNYphnnTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVP 87
Cdd:cd05936 5 LEEAARRFPDKTALIFM----GRKLTYRELDALAEAFAA--GLQNLGVQPgDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 88 LSISHPPHELEYTITNSKSsmvltnkenysmlaeigrKVGVQVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTT 167
Cdd:cd05936 79 LNPLYTPRELEHILNDSGA------------------KALIVAVSFTDLLAAGAPLGERVALTPEDV---AVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 168 SRPKGVIATHSNIEA---QVKALVEAWEWKkEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESG 244
Cdd:cd05936 138 GVPKGAMLTHRNLVAnalQIKAWLEDLLEG-DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 245 VTtdleqpisLFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE 324
Cdd:cd05936 217 VT--------IFPGVPTMYIALLNAPEFK----------KRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 325 IG--MCLsNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDG 402
Cdd:cd05936 279 TSpvVAV-NPLDGPRKPGSIGIPLPGTEVKIVDD-----DGEEL---PPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 403 WFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPm 482
Cdd:cd05936 350 WLRTGDIGYMDED-GYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL- 426
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 330846471 483 SYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLV 524
Cdd:cd05936 427 TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
9-523 |
9.30e-102 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 315.28 E-value: 9.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVnypHNNTQRFTYNDLLNESAAISNqiTFKKDDL-EQDRVS----------FLYpqsfdyvrtqWG 77
Cdd:PRK07514 8 ALRAAFADRDAPFIE---TPDGLRYTYGDLDAASARLAN--LLVALGVkPGDRVAvqvekspealALY----------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 78 IWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIE-IPEIGNGSPNKEVQHKIMPF-DIN 155
Cdd:PRK07514 73 TLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVEtLDADGTGSLLEAAAAAPDDFeTVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 156 RNAQ----IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKF 231
Cdd:PRK07514 153 RGADdlaaILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 DSKQVIDRLLESGVttdleqpislFMAVPTIYSKLIkyveenvktEKERQDIEKAfQRLRLMVSGSSA-LPETvKNDFME 310
Cdd:PRK07514 233 DPDAVLALMPRATV----------MMGVPTFYTRLL---------QEPRLTREAA-AHMRLFISGSAPlLAET-HREFQE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGHNLLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEASstqnGKPVFKDntkEVGELLVKGPQVFKEYFE 390
Cdd:PRK07514 292 RTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPET----GAELPPG---EIGMIEVKGPNVFKGYWR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 391 KKEATQEAF-EDGWFKTGDiVEKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVI 469
Cdd:PRK07514 365 MPEKTAEEFrADGFFITGD-LGKIDERGYVHIVGRGK-DLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 330846471 470 GAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK07514 443 TAVVVPKPGAAL-DEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
158-518 |
1.12e-92 |
|
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: 286.10 E-value: 1.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLwSGAMCEMMPKFDSKQVI 237
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALL-AGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTTdleqpislFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLL 317
Cdd:cd04433 82 ELIEREKVTI--------LLGVPTLLARLLKAPESA----------GYDLSSLRALVSGGAPLPPELLERFEEAPGIKLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 318 ERYGMTEIGMCLS--NPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEAT 395
Cdd:cd04433 144 NGYGLTETGGTVAtgPPDDDARKPGSVGRPVPGVEVRIVDP-----DGGEL---PPGEIGELVVRGPSVMKGYWNNPEAT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVY 475
Cdd:cd04433 216 AAVDEDGWYRTGDLGRLD-EDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 330846471 476 KKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd04433 294 RPGADL-DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
158-523 |
2.34e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 282.26 E-value: 2.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSkqvi 237
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTP---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 drlleSGVTTDLEQPISLFMAVPTIYSKLIkyveenvktekERQDIEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLL 317
Cdd:PRK07787 207 -----EAYAQALSEGGTLYFGVPTVWSRIA-----------ADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 318 ERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDNtKEVGELLVKGPQVFKEYFEKKEATQE 397
Cdd:PRK07787 271 ERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE-----DGGPVPHDG-ETVGELQVRGPTLFDGYLNRPDATAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AF-EDGWFKTGDIVEKDnSTGRFKILGRSSVDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVyk 476
Cdd:PRK07787 345 AFtADGWFRTGDVAVVD-PDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-- 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 330846471 477 kGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK07787 422 -GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-523 |
3.72e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 283.23 E-value: 3.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVnYPHnntQRFTYNDLLNESAAISN---QITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:PRK06187 12 LRHGARKHPDKEAVY-FDG---RRTTYAELDERVNRLANalrALGVKKGD----RVAVFDWNSHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEI------GRKV-----------GVQVIEIPEIGNGSPNKEVQHk 148
Cdd:PRK06187 84 HPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIlpqlptVRTVivegdgpaaplAPEVGEYEELLAAASDTFDFP- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 149 imPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGL-INILtcSLWSGAMCEM 227
Cdd:PRK06187 163 --DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWgLPYL--ALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 MPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSALPETVKND 307
Cdd:PRK06187 239 PRRFDPENLLDLIETERVTF--------FFAVPTIWQMLLKAPRAY----------FVDFSSLRLVIYGGAALPPALLRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 308 FMEISGHNLLERYGMTEIGMCLS-NPLH-----GDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDnTKEVGELLVKG 381
Cdd:PRK06187 301 FKEKFGIDLVQGYGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIVDD-----DGDELPPD-GGEVGEIIVRG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 382 PQVFKEYFEKKEATQEAFEDGWFKTGDI--VEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLG 459
Cdd:PRK06187 375 PWLMQGYWNRPEATAETIDGGWLHTGDVgyIDED---GYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 460 IPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK06187 451 VPDEKWGERPVAVVVLKPGATL-DAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
9-520 |
5.05e-83 |
|
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: 264.86 E-value: 5.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVnYPHnntQRFTYNDLLNESAAISNQIT---FKKddleQDRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:cd17631 1 LRRRARRHPDRTALV-FGG---RSLTYAELDERVNRLAHALRalgVAK----GDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVltnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfdINRNAQIIYTSG 165
Cdd:cd17631 73 VPLNFRLTPPEVAYILADSGAKVL--------------------------------------------FDDLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGV 245
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 246 TTdleqpislFMAVPTIYSKLIKYVeenvktEKERQDiekaFQRLRLMVSGSSALPETVKNDFMEIsGHNLLERYGMTEI 325
Cdd:cd17631 189 TS--------FFLVPTMIQALLQHP------RFATTD----LSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 326 GM--CLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGW 403
Cdd:cd17631 250 SPgvTFLSPEDHRRKLGSAGRPVFFVEVRIVDP-----DGREV---PPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGW 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 404 FKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmS 483
Cdd:cd17631 322 FHTGDLGRLD-EDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL-D 398
|
490 500 510
....*....|....*....|....*....|....*..
gi 330846471 484 YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:cd17631 399 EDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
33-525 |
5.85e-82 |
|
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: 263.79 E-value: 5.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTN 112
Cdd:cd05926 15 LTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 113 KEN-----------YSMLAEIGRKVGV-----QVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIAT 176
Cdd:cd05926 94 KGElgpasraasklGLAILELALDVGVlirapSAESLSNLLADKKNAKSEGVPLPDDL---ALILHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 177 HSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpisLF 256
Cdd:cd05926 171 HRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNAT--------WY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 257 MAVPTIYSKLIKYVEENVktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIG--MClSNPL- 333
Cdd:cd05926 243 TAVPTIHQILLNRPEPNP---------ESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPLp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 334 HGDRVSGSVGFPLpGVQVKINAEASSTQngKPVfkdntkEVGELLVKGPQVFKEYFEKKEATQE-AFEDGWFKTGDIVEK 412
Cdd:cd05926 313 PGPRKPGSVGKPV-GVEVRILDEDGEIL--PPG------VVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 DNS-----TGRFKilgrssvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAePMSYDDF 487
Cdd:cd05926 384 DADgylflTGRIK-------ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-SVTEEEL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 330846471 488 KMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
29-519 |
4.90e-80 |
|
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: 258.30 E-value: 4.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 29 NTQRFTYNDLLNESAAISNQitFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSS 107
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAG--LRKLGLKKgDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 108 MVLTNKENYSMLAEIGRKVGVQ------------VIEIPEIGNGSPNKEVQHKIMPF--DINRNAQIIYTSGTTSRPKGV 173
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKdkiivlddkpdgVLSIEDLLSPTLGEEDEDLPPPLkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 174 IATHSNIEA---QVKALVEAWEWKkEDHILEFLPLHHVHGLINILTCsLWSGAMCEMMPKFDSKQVIDRLLESGVTTdle 250
Cdd:cd05911 165 CLSHRNLIAnlsQVQTFLYGNDGS-NDVILGFLPLYHIYGLFTTLAS-LLNGATVIIMPKFDSELFLDLIEKYKITF--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 251 qpisLFMaVPTIYSKLIKYveenvkTEKERQDiekaFQRLRLMVSGSSALP----ETVKNDFmeiSGHNLLERYGMTEIG 326
Cdd:cd05911 240 ----LYL-VPPIAAALAKS------PLLDKYD----LSSLRVILSGGAPLSkelqELLAKRF---PNATIKQGYGMTETG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 327 MCLSNPLHGDRVSGSVGFPLPGVQVKINAEAsstqnGKPVFKDNtkEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFK 405
Cdd:cd05911 302 GILTVNPDGDDKPGSVGRLLPNVEAKIVDDD-----GKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFdEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 406 TGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYD 485
Cdd:cd05911 375 TGDIGYFD-EDGYLYIVDRKK-ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK-LTEK 451
|
490 500 510
....*....|....*....|....*....|....*
gi 330846471 486 DFKMWCQQRLA-YYKVPKVIQVKEEIPKNAMLKVN 519
Cdd:cd05911 452 EVKDYVAKKVAsYKQLRGGVVFVDEIPKSASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
9-433 |
2.94e-75 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 243.76 E-value: 2.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNYPHnntQRFTYNDLLNESAAISNQIT---FKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG---RRLTYRELDERANRLAAGLRalgVGKGD----RVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLTNKENY-SMLAEI--GRKVGVQVI---------EIPEIGNGSPNKEVQHKIMPFD 153
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALKlEELLEAlgKLEVVKLVLvldrdpvlkEEPLPEEAKPADVPPPPPPPPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 154 INRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWK----KEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMP 229
Cdd:pfam00501 154 PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 230 KFdskqviDRLLESGVTTDLEQ-PISLFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSALPETVKNDF 308
Cdd:pfam00501 234 GF------PALDPAALLELIERyKVTVLYGVPTLLNMLLEAGAPK----------RALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 309 MEISGHNLLERYGMTEIGMCLSNPLHGD---RVSGSVGFPLPGVQVKI-NAEasstqNGKPVFKDntkEVGELLVKGPQV 384
Cdd:pfam00501 298 RELFGGALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIvDDE-----TGEPVPPG---EPGELCVRGPGV 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 330846471 385 FKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNS 433
Cdd:pfam00501 370 MKGYLNDPELTAEAFdEDGWYRTGDLGRRD-EDGYLEIVGRKK-DQIKLG 417
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
31-523 |
1.30e-72 |
|
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: 237.19 E-value: 1.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISNQItFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL 110
Cdd:cd05934 2 RRWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 TnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEA 190
Cdd:cd05934 81 V-----------------------------------------DP---ASILYTSGTTGPPKGVVITHANLTFAGYYSARR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 191 WEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVT--TDLEQPISLFMAVPtiysklik 268
Cdd:cd05934 117 FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATvtNYLGAMLSYLLAQP-------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 269 yveenvKTEKERQdiekafQRLRlmVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPG 348
Cdd:cd05934 189 ------PSPDDRA------HRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 349 VQVKINAEasstqNGKPVfkdNTKEVGELLVK---GPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRS 425
Cdd:cd05934 255 YEVRIVDD-----DGQEL---PAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRD-ADGFFYFVDRK 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 426 SvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGaEPMSYDDFKMWCQQRLAYYKVPKVIQ 505
Cdd:cd05934 326 K-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQLAYFKVPRYIR 403
|
490
....*....|....*...
gi 330846471 506 VKEEIPKNAMLKVNKKDL 523
Cdd:cd05934 404 FVDDLPKTPTEKVAKAQL 421
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-523 |
1.99e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 239.42 E-value: 1.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 1 MHRLPSLqLFQNALKYKNRIAIVNYPhnntQRFTYNDLLNESAAISN---QITFKKDDleqdRVSFLYPQSFDYVRTQWG 77
Cdd:PRK07656 4 WMTLPEL-LARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAalaALGIGKGD----RVAIWAPNSPHWVIAALG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 78 IWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK----ENYSM---LAEIGRKVGVQVIEIPE-----------IGNG 139
Cdd:PRK07656 75 ALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGlflgVDYSAttrLPALEHVVICETEEDDPhtekmktftdfLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 140 SPNkEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSL 219
Cdd:PRK07656 155 DPA-ERAPEVDPDDV---ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 220 WSGAMCEMMPKFDSKQVIdRLLEsgvttdlEQPISLFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSA 299
Cdd:PRK07656 231 MRGATILPLPVFDPDEVF-RLIE-------TERITVLPGPPTMYNSLLQHPDRS----------AEDLSSLRLAVTGAAS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 300 LP-ETVKNDFMEISGHNLLERYGMTE-IGMCLSNPLHGDR--VSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVG 375
Cdd:PRK07656 293 MPvALLERFESELGVDIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIVNE-----LGEEV---PVGEVG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEE 454
Cdd:PRK07656 365 ELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLD-EEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 455 CAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK07656 443 AAVIGVPDERLGEVGKAYVVLKPGAE-LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
18-528 |
6.31e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 232.44 E-value: 6.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNyphnNTQRFTYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHEL 97
Cdd:PRK06839 17 DRIAIIT----EEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 98 EYTITNSKSSMVLTNKENYSMLAEIGRKVGVQvieiPEIGNGSPNKEVQHKIMPFDI---NRNAQIIYTSGTTSRPKGVI 174
Cdd:PRK06839 93 IFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ----RVISITSLKEIEDRKIDNFVEkneSASFIICYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 175 ATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGlINILTCSLW-SGAMCEMMPKFDSKQVIdRLLEsgvttdlEQPI 253
Cdd:PRK06839 169 LTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGG-IGLFAFPTLfAGGVIIVPRKFEPTKAL-SMIE-------KHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 254 SLFMAVPTIYSKLIkyveENVKTEKerqdieKAFQRLRLMVSGSSALPETVKNDFMEiSGHNLLERYGMTEIGMCLSNPL 333
Cdd:PRK06839 240 TVVMGVPTIHQALI----NCSKFET------TNLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVFMLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 334 HGD--RVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVE 411
Cdd:PRK06839 309 EEDarRKVGSIGKPVLFCDYELIDE-----NKNKV---EVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 412 KDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWC 491
Cdd:PRK06839 381 VDED-GFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV-LIEKDVIEHC 457
|
490 500 510
....*....|....*....|....*....|....*..
gi 330846471 492 QQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLFT 528
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-459 |
3.40e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 230.37 E-value: 3.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 2 HRLPSLqLFQNALKYKNRIAIvNYPHNNT-QRFTYNDLLNESAAISNqiTFKKDDLE-QDRVSFLYPQSFDYVRTQWGIW 79
Cdd:COG1022 11 DTLPDL-LRRRAARFPDRVAL-REKEDGIwQSLTWAEFAERVRALAA--GLLALGVKpGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 80 RSGGVAVPLSISHPPHELEYTITNSKSSMVLT-NKENYSMLAEIGRKVG--VQVIEI-PEIGNGSPN-----------KE 144
Cdd:COG1022 87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslRHIVVLdPRGLRDDPRllsldellalgRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 145 VQH---------KIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLInIL 215
Cdd:COG1022 167 VADpaelearraAVKPDDL---ATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERT-VS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 216 TCSLWSGAM---CEmmpkfDSKQVIDRLLESGVTtdleqpisLFMAVP----TIYSKLIKYVEEN--------------- 273
Cdd:COG1022 243 YYALAAGATvafAE-----SPDTLAEDLREVKPT--------FMLAVPrvweKVYAGIQAKAEEAgglkrklfrwalavg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 274 VKTEKERQDIEK-----AFQ------------------RLRLMVSGSSALPETVkNDFMEISGHNLLERYGMTEI-GMCL 329
Cdd:COG1022 310 RRYARARLAGKSpslllRLKhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 330 SNPLHGDRVsGSVGFPLPGVQVKINAEasstqngkpvfkdntkevGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGD 408
Cdd:COG1022 389 VNRPGDNRI-GTVGPPLPGVEVKIAED------------------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGD 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 330846471 409 IVEKDnSTGRFKILGRSSvDIIKNSGYK-ISALEIEREILDHPDIEECAVLG 459
Cdd:COG1022 450 IGELD-EDGFLRITGRKK-DLIVTSGGKnVAPQPIENALKASPLIEQAVVVG 499
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
4-523 |
1.64e-66 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 223.65 E-value: 1.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 4 LPSLQLFQNALKYKNRIAIVNYPhnNTQRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGG 83
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAA--TGRALTYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 84 VAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVG-VQVIEIPEIGNGSPNKEVQHKIMPF-DINRN--AQ 159
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVlLDSAEFDSLSFSDLLFEADEAEPPVvVIKQDdvAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALV--EAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHRNLIAMVAQFVagEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTTdleqpislFMAVPTIYSKLIKyveeNVKTEKERqdiekaFQRLRLMVSGSSALPETVKNDFMEISGH-NL 316
Cdd:cd05904 243 AAIERYKVTH--------LPVVPPIVLALVK----SPIVDKYD------LSSLRQIMSGAAPLGKELIEAFRAKFPNvDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIG----MCLsNPLHGDRVSGSVGFPLPGVQVKInaeaSSTQNGKPVFKDNTkevGELLVKGPQVFKEYFEKK 392
Cdd:cd05904 305 GQGYGMTESTgvvaMCF-APEKDRAKYGSVGRLVPNVEAKI----VDPETGESLPPNQT---GELWIRGPSIMKGYLNNP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 393 EATQEAF-EDGWFKTGDIVEKDNsTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGA 471
Cdd:cd05904 377 EATAATIdKEGWLHTGDLCYIDE-DGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMA 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 330846471 472 ILVYKKGAEpMSYDDFKMWCQQRLAYYK-VPKVIQVkEEIPKNAMLKVNKKDL 523
Cdd:cd05904 455 FVVRKPGSS-LTEDEIMDFVAKQVAPYKkVRKVAFV-DAIPKSPSGKILRKEL 505
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
158-522 |
2.55e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 224.88 E-value: 2.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVkALVEAW---EWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSK 234
Cdd:PRK05605 222 ALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWvpgLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDID 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLLESGVTtdleqpislFM-AVPTIYSKLIKyveenvKTEKERQDIEKafqrLRLMVSGSSALPETVKNDFMEISG 313
Cdd:PRK05605 301 LILDAMKKHPPT---------WLpGVPPLYEKIAE------AAEERGVDLSG----VRNAFSGAMALPVSTVELWEKLTG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 314 HNLLERYGMTEIG-MCLSNPLHGDRVSGSVGFPLPGVQVKInaeasstqngkpVFKDNTKEV------GELLVKGPQVFK 386
Cdd:PRK05605 362 GLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRI------------VDPEDPDETmpdgeeGELLVRGPQVFK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 387 EYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYG 466
Cdd:PRK05605 430 GYWNRPEETAKSFLDGWFRTGDVVVME-EDGFIRIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGS 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 467 QVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKD 522
Cdd:PRK05605 508 EEVVAAVVLEPGAA-LDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
12-512 |
4.97e-66 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 223.84 E-value: 4.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 12 NALKYKNRIAIVNYP-HNNTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLS 89
Cdd:COG0365 18 HAEGRGDKVALIWEGeDGEERTLTYAELRREVNRFAN--ALRALGVKKgDRVAIYLPNIPEAVIAMLACARIGAVHSPVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 90 ISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVgvqviEIPEIGNGSPNkeVQHKIMpfdINRNAQ---------- 159
Cdd:COG0365 96 PGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKE-----KVDEALEELPS--LEHVIV---VGRTGAdvpmegdldw 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 -----------------------IIYTSGTTSRPKGVIATHSNIEAQVKALVEAW-EWKKEDHILEFLPLHHVHGLINIL 215
Cdd:COG0365 166 dellaaasaefepeptdaddplfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFWCTADIGWATGHSYIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 216 TCSLWSGA---MCEMMPKFDSKQVIDRLLEsgvttdlEQPISLFMAVPTIYSKLIKYVEENVKtekeRQDiekaFQRLRL 292
Cdd:COG0365 246 YGPLLNGAtvvLYEGRPDFPDPGRLWELIE-------KYGVTVFFTAPTAIRALMKAGDEPLK----KYD----LSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 293 MVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRV-SGSVGFPLPGVQVKINAEasstqNGKPVFKDnt 371
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVDE-----DGNPVPPG-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 372 kEVGELLVKGPQ--VFKEYFEKKEATQEAF---EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREI 446
Cdd:COG0365 384 -EEGELVIKGPWpgMFRGYWNDPERYRETYfgrFPGWYRTGDGARRD-EDGYFWILGRSD-DVINVSGHRIGTAEIESAL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330846471 447 LDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmsyDD-----FKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:COG0365 461 VSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEP---SDelakeLQAHVREELGPYAYPREIEFVDELPK 528
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
33-523 |
2.66e-65 |
|
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: 217.98 E-value: 2.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLT 111
Cdd:cd05972 1 WSFRELKRESAKAAN--VLAKLGLRKgDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 112 NKENYSMlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnaqIIYTSGTTSRPKGVIATHSnieAQVKALVEAW 191
Cdd:cd05972 79 DAEDPAL-----------------------------------------IYFTSGTTGLPKGVLHTHS---YPLGHIPTAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 192 EWkkedhilefLPLH--HVH------GLINILTCSLWS----GA---MCEMmPKFDSKQVIDRLLESGVTTdleqpislF 256
Cdd:cd05972 115 YW---------LGLRpdDIHwniadpGWAKGAWSSFFGpwllGAtvfVYEG-PRFDAERILELLERYGVTS--------F 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 257 MAVPTIYSKLIKyveenvktekerQDIEK-AFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHG 335
Cdd:cd05972 177 CGPPTAYRMLIK------------QDLSSyKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 336 DRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVK--GPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKD 413
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAI-----IDDDGREL---PPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 414 NStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWC 491
Cdd:cd05972 317 ED-GYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|..
gi 330846471 492 QQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
59-520 |
2.50e-64 |
|
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: 215.71 E-value: 2.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMlaeigrkvgvqvieipeign 138
Cdd:cd05903 27 DVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERFRQF-------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 gspnkevQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCS 218
Cdd:cd05903 87 -------DPAAMPDAV---ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 219 LWSGAMCEMMPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEEnvktekerqdIEKAFQRLRLMVSGSS 298
Cdd:cd05903 157 LLLGAPVVLQDIWDPDKALALMREHGVTF--------MMGATPFLTDLLNAVEE----------AGEPLSRLRTFVCGGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 299 ALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHG--DRVSGSVGFPLPGVQVKINAEASSTQngkpvfkdNTKEVGE 376
Cdd:cd05903 219 TVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDDTGATL--------APGVEGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 377 LLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECA 456
Cdd:cd05903 291 LLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDED-GYLRITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 457 VLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:cd05903 369 VVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-518 |
6.26e-63 |
|
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: 214.15 E-value: 6.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 16 YKNRIAIVnYPHNntqRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPP 94
Cdd:cd05959 17 RGDKTAFI-DDAG---SLTYAELEAEARRVAG--ALRALGVKReERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 95 HELEYTITNSKSSMVLTNKENYSMLAEIGRKV---GVQVI----EIPEIGNGS-----PNKEVQHKIMPFDINRNAQIIY 162
Cdd:cd05959 91 DDYAYYLEDSRARVVVVSGELAPVLAAALTKSehtLVVLIvsggAGPEAGALLlaelvAAEAEQLKPAATHADDPAFWLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 163 TSGTTSRPKGVIATHSNIEA-------QVKALVEAwewkkeDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDS-K 234
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWtaelyarNVLGIRED------DVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTpA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLLEsgvttdlEQPiSLFMAVPTIYSKLIkyveeNVKTEKERqdiekAFQRLRLMVSGSSALPETVKNDFMEISGH 314
Cdd:cd05959 245 AVFKRIRR-------YRP-TVFFGVPTLYAAML-----AAPNLPSR-----DLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 315 NLLERYGMTEIG-MCLSNpLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDntkEVGELLVKGPQVFKEYFEKKE 393
Cdd:cd05959 307 DILDGIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELRDE-----DGGDVADG---EPGELYVRGPSSATMYWNNRD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 394 ATQEAFEDGWFKTGD-IVEKDNstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:cd05959 378 KTRDTFQGEWTRTGDkYVRDDD--GFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 330846471 473 LVYKKGAEP--MSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd05959 455 VVLRPGYEDseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
158-523 |
1.19e-61 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 207.97 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTTdleqpISLfmaVPTIYSKLIKyveenvktekerQDIEKAFQRLRLMVSGSSALPETVKNDFMEiSGHNLL 317
Cdd:cd05912 159 HLINSGKVTI-----ISV---VPTMLQRLLE------------ILGEGYPNNLRCILLGGGPAPKPLLEQCKE-KGIPVY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 318 ERYGMTEIG--MCLSNPLHGDRVSGSVGFPLPGVQVKInaeasSTQNGKPvfkdntKEVGELLVKGPQVFKEYFEKKEAT 395
Cdd:cd05912 218 QSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKI-----EDDGQPP------YEVGEILLKGPNVTKGYLNRPDAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVy 475
Cdd:cd05912 287 EESFENGWFKTGDIGYLDEE-GFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV- 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 330846471 476 kkGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05912 364 --SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-459 |
6.60e-61 |
|
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: 207.06 E-value: 6.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNQIT---FKKddleQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMV 109
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIalgVEP----GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 110 LTnkENYSMLAeigrkvgvqvieipeigngspnkevqhkimpfdinrnaQIIYTSGTTSRPKGVIATHSNIEAQVKALVE 189
Cdd:cd05907 82 FV--EDPDDLA--------------------------------------TIIYTSGTTGRPKGVMLSHRNILSNALALAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 190 AWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAmcemmpkfdsKQVIDRLLESGVtTDLE--QPiSLFMAVPTIYSKLI 267
Cdd:cd05907 122 RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGA----------RIYFASSAETLL-DDLSevRP-TVFLAVPRVWEKVY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 268 KYVEENVKTEKERQDIEKA-FQRLRLMVSGSSALPETVkNDFMEISGHNLLERYGMTEI-GMCLSNPLhGDRVSGSVGFP 345
Cdd:cd05907 190 AAIKVKAVPGLKRKLFDLAvGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETsAVVTLNPP-GDNRIGTVGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 346 LPGVQVKInaeasstqngkpvfkdntKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGR 424
Cdd:cd05907 268 LPGVEVRI------------------ADDGEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDED-GFLHITGR 328
|
410 420 430
....*....|....*....|....*....|....*.
gi 330846471 425 SSvDIIKNSGYK-ISALEIEREILDHPDIEECAVLG 459
Cdd:cd05907 329 KK-DLIITSGGKnISPEPIENALKASPLISQAVVIG 363
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
9-526 |
2.30e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 204.04 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNyphnNTQRFTYNDLLNESAAISNQIT---FKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:PRK03640 8 LKQRAFLTPDRTAIEF----EEKKVTFMELHEAVVSVAGKLAalgVKKGD----RVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLTNkENYsmlaeIGRKVGVQVIEIPEIGNGSpnKEVQHKIMPFDINRNAQIIYTSG 165
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLITD-DDF-----EAKLIPGISVKFAELMNGP--KEEAEIQEEFDLDEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDSKQVIDRLLESGV 245
Cdd:PRK03640 152 TTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 246 TTdleqpISlfmAVPTIYSKLIKYVEENVKTEKerqdiekafqrLRLMVSGSSALPETVkndfMEISGHN---LLERYGM 322
Cdd:PRK03640 231 TI-----IS---VVSTMLQRLLERLGEGTYPSS-----------FRCMLLGGGPAPKPL----LEQCKEKgipVYQSYGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 323 TEIG--MCLSNPLHGDRVSGSVGFPLPGVQVKInaeASSTQNGKPvfkdntKEVGELLVKGPQVFKEYFEKKEATQEAFE 400
Cdd:PRK03640 288 TETAsqIVTLSPEDALTKLGSAGKPLFPCELKI---EKDGVVVPP------FEEGEIVVKGPNVTKGYLNREDATRETFQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 401 DGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYkkgAE 480
Cdd:PRK03640 359 DGWFKTGDIGYLD-EEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK---SG 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 330846471 481 PMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:PRK03640 434 EVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
32-523 |
4.75e-59 |
|
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: 201.55 E-value: 4.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 32 RFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLT 111
Cdd:cd05935 1 SLTYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 112 NKEnysmLAEIgrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAW 191
Cdd:cd05935 80 GSE----LDDL-----------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 192 EWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpisLFMAVPTIYSKLIKYVE 271
Cdd:cd05935 121 GLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVT--------FWTNIPTMLVDLLATPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 272 ENvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE-IGMCLSNPlHGDRVSGSVGFPLPGVQ 350
Cdd:cd05935 193 FK----------TRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNP-PLRPKLQCLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 351 VKInaeaSSTQNGKPVfKDNtkEVGELLVKGPQVFKEYFEKKEATQEAF-EDG---WFKTGDIVEKDNStGRFKILGRSS 426
Cdd:cd05935 262 ARV----IDIETGREL-PPN--EVGEIVVRGPQIFKGYWNRPEETEESFiEIKgrrFFRTGDLGYMDEE-GYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 427 vDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAE-PMSYDDFKMWCQQRLAYYKVPKVIQ 505
Cdd:cd05935 334 -RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgKVTEEDIIEWAREQMAAYKYPREVE 412
|
490
....*....|....*...
gi 330846471 506 VKEEIPKNAMLKVNKKDL 523
Cdd:cd05935 413 FVDELPRSASGKILWRLL 430
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
34-523 |
5.91e-58 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 198.83 E-value: 5.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNk 113
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 enySMLAEigrkVGVQVIEIPEIGNGSPNKEVQHKIMPFDinRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEW 193
Cdd:TIGR01923 79 ---SLLEE----KDFQADSLDRIEAAGRYETSLSASFNMD--QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 194 KKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDskQVIDRLLESGVTTdleqpISLfmaVPTiysKLIKYVEEN 273
Cdd:TIGR01923 150 TEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLEMIANERVTH-----ISL---VPT---QLNRLLDEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 274 VKTEkerqdiekafqRLRLMVSGSSALPETVKNDFMEiSGHNLLERYGMTEigMC---LSNPLHGDRVSGSVGFPLPGVQ 350
Cdd:TIGR01923 216 GHNE-----------NLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTE--TCsqvTTATPEMLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 351 VKINaeasstqngkpvfKDNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDII 430
Cdd:TIGR01923 282 IKIK-------------VDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGE-GFLYVLGRRD-DLI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 431 KNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKgaePMSYDDFKMWCQQRLAYYKVPKVIQVKEEI 510
Cdd:TIGR01923 347 ISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES---DISQAKLIAYLTEKLAKYKVPIAFEKLDEL 423
|
490
....*....|...
gi 330846471 511 PKNAMLKVNKKDL 523
Cdd:TIGR01923 424 PYNASGKILRNQL 436
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
13-523 |
1.33e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 200.16 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 13 ALKYKNRIAIVNyphnNTQRFTY---NDLLNESAAISNQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLS 89
Cdd:PRK08316 21 ARRYPDKTALVF----GDRSWTYaelDAAVNRVAAALLDLGLKKGD----RVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 90 ISHPPHELEYTITNSKSSMVLTNKENYS----------------MLAEIGRKVGVQVIEIPEIGNGSPNKEVQHKImpfD 153
Cdd:PRK08316 93 FMLTGEELAYILDHSGARAFLVDPALAPtaeaalallpvdtlilSLVLGGREAPGGWLDFADWAEAGSVAEPDVEL---A 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 154 INRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDS 233
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 234 KQVIDRLLESGVTtdleqpiSLFmAVPTIYSKLIKyveenvktekeRQDIEKA-FQRLRLMVSGSSALPETVKNDFME-- 310
Cdd:PRK08316 250 ELILRTIEAERIT-------SFF-APPTVWISLLR-----------HPDFDTRdLSSLRKGYYGASIMPVEVLKELRErl 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 --ISGHNLlerYGMTEIGmclsnPLHG-------DRVSGSVGFPLPGVQVKINAEAsstqnGKPVFKDntkEVGELLVKG 381
Cdd:PRK08316 311 pgLRFYNC---YGQTEIA-----PLATvlgpeehLRRPGSAGRPVLNVETRVVDDD-----GNDVAPG---EVGEIVHRS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 382 PQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIP 461
Cdd:PRK08316 375 PQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEE-GYITVVDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330846471 462 NEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK08316 453 DPKWIEAVTAVVVPKAGAT-VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
59-525 |
1.10e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 196.02 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIPEIGN 138
Cdd:PRK06710 75 DRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIAD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 GSP---------------------------------NKEVQHKI-MPFDI-NRNAQIIYTSGTTSRPKGVIATHSNIEAQ 183
Cdd:PRK06710 155 FLPfpknllypfvqkkqsnlvvkvsesetihlwnsvEKEVNTGVeVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 184 VKALVEaWEW---KKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpisLFMAVP 260
Cdd:PRK06710 235 TLMGVQ-WLYnckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVT--------LFPGAP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 261 TIYSKLIkyveeNVKTEKErQDIEKafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIG-MCLSNPLHGDRVS 339
Cdd:PRK06710 306 TIYIALL-----NSPLLKE-YDISS----IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 340 GSVGFPLPGVQVKInaeaSSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRF 419
Cdd:PRK06710 376 GSIGVPWPDTEAMI----MSLETGEAL---PPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDED-GFF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 420 KILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYK 499
Cdd:PRK06710 448 YVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTE-CSEEELNQFARKYLAAYK 525
|
490 500
....*....|....*....|....*.
gi 330846471 500 VPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK06710 526 VPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
13-520 |
5.95e-55 |
|
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: 192.13 E-value: 5.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 13 ALKYKNRIAIVNYPHNNTQRFTYNDLLNESAAISNQ-ITFkkddleQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSIS 91
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALgISR------GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 92 HPPHELEYTITNSKSSMVLTNKE-NY-SMLAEigrkvgvqvieipeignGSPNKEVqhkIMPFDINRNAQIIYTSGTTSR 169
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREfEYeDLLAE-----------------GDPDFEW---IPPADEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 170 PKGVIATHSNieAQVKALVEAWEWKKEDH--ILEFLPLHHVHGLiniltCSLWSGAM------CemMPKFDSKQVIDRLL 241
Cdd:cd12118 148 PKGVVYHHRG--AYLNALANILEWEMKQHpvYLWTLPMFHCNGW-----CFPWTVAAvggtnvC--LRKVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 242 ESGVTTdleqpislFMAVPTIYSKLIKYVEEnvktekerqDIEKAFQRLRLMVSGSSALPETVKNdfMEISGHNLLERYG 321
Cdd:cd12118 219 KHKVTH--------FCGAPTVLNMLANAPPS---------DARPLPHRVHVMTAGAPPPAAVLAK--MEELGFDVTHVYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 322 MTE----IGMCLSNP----LHGDRVSGS-----VGFP-LPGVQVKinaeasSTQNGKPVFKDnTKEVGELLVKGPQVFKE 387
Cdd:cd12118 280 LTEtygpATVCAWKPewdeLPTEERARLkarqgVRYVgLEEVDVL------DPETMKPVPRD-GKTIGEIVFRGNIVMKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 388 YFEKKEATQEAFEDGWFKTGDI--VEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:cd12118 353 YLKNPEATAEAFRGGWFHSGDLavIHPD---GYIEIKDRSK-DIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 466 GQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIqVKEEIPKNAMLKVNK 520
Cdd:cd12118 429 GEVPCAFVELKEGAKV-TEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQK 481
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
33-518 |
1.88e-53 |
|
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: 187.65 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNQITFKKDDlEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTN 112
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVG-TGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 113 KENYSMLaeigrkvgvqvieipeigngspnkevqhkimpfdinrnaqIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWE 192
Cdd:cd05914 87 DEDDVAL----------------------------------------INYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 193 WKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSkQVIDRLLESGVTTDLEQPislfmaVPTIYSKLIKYVEE 272
Cdd:cd05914 127 LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS-AKIIALAFAQVTPTLGVP------VPLVIEKIFKMDII 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 273 NVKTEKE------------------RQDIEKAF-QRLRLMVSGSSALPETVKNDFMEIsGHNLLERYGMTEIGMCLSNPL 333
Cdd:cd05914 200 PKLTLKKfkfklakkinnrkirklaFKKVHEAFgGNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 334 HGDRVSGSVGFPLPGVQVKINAEasstqngkpvfkDNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEK 412
Cdd:cd05914 279 PNRIRLGSAGKVIDGVEVRIDSP------------DPATGEGEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 DNStGRFKILGRSSVDIIKNSGYKISALEIEREILDHPDIEECAVLgipNEEYGQVIGAILVY-----KKGAEPMSYDDF 487
Cdd:cd05914 347 DAE-GYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV---VQEKKLVALAYIDPdfldvKALKQRNIIDAI 422
|
490 500 510
....*....|....*....|....*....|....*..
gi 330846471 488 kMWC------QQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd05914 423 -KWEvrdkvnQKVPNYKKISKVKIVKEEFEKTPKGKI 458
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
3-523 |
3.78e-53 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 189.11 E-value: 3.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 3 RLPSL-QLFQNAL-KYKNRIAIVNYphnnTQRFTYNDLLNESAA----ISNQITFKKDDleqdRVSFLYPQSFDYVRTQW 76
Cdd:PRK08974 21 RYQSLvDMFEQAVaRYADQPAFINM----GEVMTFRKLEERSRAfaayLQNGLGLKKGD----RVALMMPNLLQYPIALF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 77 GIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIPEIGN------GS---------- 140
Cdd:PRK08974 93 GILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDqlstakGTlvnfvvkyik 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 141 --------PN----KEVQHK------IMPfDINRN--AQIIYTSGTTSRPKGVIATHSNIEA---QVKALVEAWEWKKED 197
Cdd:PRK08974 173 rlvpkyhlPDaisfRSALHKgrrmqyVKP-ELVPEdlAFLQYTGGTTGVAKGAMLTHRNMLAnleQAKAAYGPLLHPGKE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 198 HILEFLPLHHVHGLIniLTCSLwsgamcemmpkFDSKQVIDRLLES-----GVTTDLEQ-PISLFMAVPTIYSKLIKyvE 271
Cdd:PRK08974 252 LVVTALPLYHIFALT--VNCLL-----------FIELGGQNLLITNprdipGFVKELKKyPFTAITGVNTLFNALLN--N 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 272 ENVKtekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLS-NPLHGDRVSGSVGFPLPGVQ 350
Cdd:PRK08974 317 EEFQ--------ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 351 VKINAEAsstqnGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDII 430
Cdd:PRK08974 389 IKLVDDD-----GNEVPPG---EPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEE-GFLRIVDRKK-DMI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 431 KNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIgAILVYKKGaEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEI 510
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV-KIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDEL 536
|
570
....*....|...
gi 330846471 511 PKNAMLKVNKKDL 523
Cdd:PRK08974 537 PKSNVGKILRREL 549
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
32-520 |
6.39e-53 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 187.35 E-value: 6.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 32 RFTYNDLLNESAAISNQItfKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL 110
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAAL--RRLGVKReERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 TNKENYSMLAEIGRKVG--VQVIeipeIGNGSPNKEVQ-----------HKIMPFDINRNAQIIYTSGTTSRPKGVIATH 177
Cdd:TIGR02262 108 VSGALLPVIKAALGKSPhlEHRV----VVGRPEAGEVQlaellateseqFKPAATQADDPAFWLYSSGSTGMPKGVVHTH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 178 SNIeaQVKALVEAWE---WKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDS-KQVIDRLLesgvttdLEQPi 253
Cdd:TIGR02262 184 SNP--YWTAELYARNtlgIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTpDAVFDRLR-------RHQP- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 254 SLFMAVPTIYSKLIKyvEENVKTEKERqdiekafqRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIG-MCLSNp 332
Cdd:TIGR02262 254 TIFYGVPTLYAAMLA--DPNLPSEDQV--------RLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLhIFLSN- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 333 LHGDRVSGSVGFPLPGVQVKINAEAsstqnGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEK 412
Cdd:TIGR02262 323 LPGDVRYGTSGKPVPGYRLRLVGDG-----GQDVADG---EPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 dNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQ 492
Cdd:TIGR02262 395 -NDDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQT-ALETELKEHVK 471
|
490 500
....*....|....*....|....*...
gi 330846471 493 QRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:TIGR02262 472 DRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
30-523 |
1.61e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 186.43 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 30 TQRFTY---NDLLNESAAISNQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKS 106
Cdd:PRK08008 35 VRRYSYlelNEEINRTANLFYSLGIRKGD----KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 107 SMVLTNKENYSMLAEIGRKVGVQVIEIPEIGNGSPNKEvqhKIMPFDINRN-----------------AQIIYTSGTTSR 169
Cdd:PRK08008 111 SLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPADD---GVSSFTQLKAqqpatlcyapplstddtAEILFTSGTTSR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 170 PKGVIATHSNIeaQVKALVEAWE--WKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDS----KQVidRLLES 243
Cdd:PRK08008 188 PKGVVITHYNL--RFAGYYSAWQcaLRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSArafwGQV--CKYRA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 244 GVTTDLEQPISLFMAVPTiysklikyveenvkTEKERQdiekafQRLRLMVSgSSALPETVKNDFMEISGHNLLERYGMT 323
Cdd:PRK08008 264 TITECIPMMIRTLMVQPP--------------SANDRQ------HCLREVMF-YLNLSDQEKDAFEERFGVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 324 E-IGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKG---PQVFKEYFEKKEATQEAF 399
Cdd:PRK08008 323 EtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDD-----HNRPL---PAGEIGEICIKGvpgKTIFKEYYLDPKATAKVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 E-DGWFKTGDIVEKDNStGRFKILGRSsVDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKG 478
Cdd:PRK08008 395 EaDGWLHTGDTGYVDEE-GFFYFVDRR-CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 330846471 479 AEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK08008 473 ET-LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
59-527 |
3.82e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 185.75 E-value: 3.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNkenySMLAEIGRKV--GVQVIEIPEI 136
Cdd:PRK07786 68 DRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTE----AALAPVATAVrdIVPLLSTVVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 137 GNGSPN----------KEVQHKIMPFDINRN--AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHIlEFL- 203
Cdd:PRK07786 144 AGGSSDdsvlgyedllAEAGPAHAPVDIPNDspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDV-GFVg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 204 -PLHHVHGLINILTcSLWSGAMCEMMP--KFDSKQVIDRLLESGVTTdleqpisLFMaVPTIYSKLIkyveenvkteker 280
Cdd:PRK07786 223 vPLFHIAGIGSMLP-GLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTG-------IFL-VPAQWQAVC------------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 281 qDIEKAFQR---LRLMVSGSSALPETVKNDFMEI-SGHNLLERYGMTEIG--MCLsnpLHGD---RVSGSVGFPLPGVQV 351
Cdd:PRK07786 281 -AEQQARPRdlaLRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEMSpvTCM---LLGEdaiRKLGSVGKVIPTVAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 352 KINAEassTQNGKPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIK 431
Cdd:PRK07786 357 RVVDE---NMNDVPV-----GEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQD-EEGYVWVVDRKK-DMII 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 432 NSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIP 511
Cdd:PRK07786 427 SGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALP 506
|
490
....*....|....*.
gi 330846471 512 KNAMLKVNKKDLVKLF 527
Cdd:PRK07786 507 RNPAGKVLKTELRERY 522
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
4-518 |
1.59e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 184.39 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 4 LPSLQLFQN----ALKYKNRIAIVNYPHnntqRFTYNDLLNESAAIS----NQITFKKDDleqdRVSFLYPQSFDYVRTQ 75
Cdd:PRK08314 7 LPETSLFHNlevsARRYPDKTAIVFYGR----AISYRELLEEAERLAgylqQECGVRKGD----RVLLYMQNSPQFVIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 76 WGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQ-VI---------------------EI 133
Cdd:PRK08314 79 YAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhVIvaqysdylpaepeiavpawlrAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 134 PEIGNGSPNKEVQ-------------HKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVkalVEAWEWK---KED 197
Cdd:PRK08314 159 PPLQALAPGGVVAwkealaaglapppHTAGPDDL---AVLPYTSGTTGVPKGCMHTHRTVMANA---VGSVLWSnstPES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 198 HILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDsKQVIDRLLES-GVTTDLEQPISL--FMAVPTIysklikyveenv 274
Cdd:PRK08314 233 VVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWD-REAAARLIERyRVTHWTNIPTMVvdFLASPGL------------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 275 ktekERQDIEKafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE-IGMCLSNPLHGDRvSGSVGFPLPGVQVKI 353
Cdd:PRK08314 300 ----AERDLSS----LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 354 naeaSSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF-E-DG--WFKTGDIVEKDNStGRFKILGRSSvDI 429
Cdd:PRK08314 371 ----IDPETLEEL---PPGEVGEIVVHGPQVFKGYWNRPEATAEAFiEiDGkrFFRTGDLGRMDEE-GYFFITDRLK-RM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 430 IKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAE-PMSYDDFKMWCQQRLAYYKVPKVIQVKE 508
Cdd:PRK08314 442 INASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgKTTEEEIIAWAREHMAAYKYPRIVEFVD 521
|
570
....*....|
gi 330846471 509 EIPKNAMLKV 518
Cdd:PRK08314 522 SLPKSGSGKI 531
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
156-527 |
4.85e-51 |
|
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: 177.14 E-value: 4.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 156 RNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLInILTCSLWSGAMCEMMPKFDSKQ 235
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VidRLLESGVTTdleqpISLfmaVPTIYSKLIKyveenvktekERQDIEkAFQRLRLMVSGSSALPeTVKNDFMEISGHN 315
Cdd:cd17630 80 E--DLAPPGVTH-----VSL---VPTQLQRLLD----------SGQGPA-ALKSLRAVLLGGAPIP-PELLERAADRGIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 316 LLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqngkpvfkdntkevGELLVKGPQVFKEYFeKKEAT 395
Cdd:cd17630 138 LYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED------------------GEIWVGGASLAMGYL-RGQLV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVY 475
Cdd:cd17630 199 PEFNEDGWFTTKDLGELHAD-GRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 330846471 476 KKGAEPmsyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLF 527
Cdd:cd17630 277 RGPADP---AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
158-523 |
6.43e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 182.11 E-value: 6.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcsLWSGAMCEMMPKFDSKQVI 237
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPT--LLRGGTVIVLAKFDPAEVL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLEsgvttdleQPISLFMAVPT-IYSKLikyveenvktekERQDIEKA-FQRLRLMVSGSSALPETVKNDFMEISGHN 315
Cdd:PRK06188 249 RAIEE--------QRITATFLVPTmIYALL------------DHPDLRTRdLSSLETVYYGASPMSPVRLAEAIERFGPI 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 316 LLERYGMTEIGMCLS------NPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYF 389
Cdd:PRK06188 309 FAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALLDE-----DGREV---AQGEVGEICVRGPLVMDGYW 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 390 EKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVI 469
Cdd:PRK06188 381 NRPEETAEAFRDGWLHTGDVARED-EDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAV 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 330846471 470 GAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK06188 459 TAVVVLRPGAAV-DAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
11-525 |
2.75e-50 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 181.10 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 11 QNALKYKNRIAIVNyphNNTQRFTYNDLLNESAAISNQItfkkddLEQ-----DRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:PRK06087 31 QTARAMPDKIAVVD---NHGASYTYSALDHAASRLANWL------LAKgiepgDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLT----NKENYSMLA--------EIGRKVGV-------------QVIEipeigNGS 140
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAptlfKQTRPVDLIlplqnqlpQLQQIVGVdklapatsslslsQIIA-----DYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 141 PnkeVQHKImPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLW 220
Cdd:PRK06087 177 P---LTTAI-TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 221 SGAMCEMMPKFDSKQVIDRLLESGVTTDLEqpislfmAVPTIYSkLIKYVEENvktekerqdiEKAFQRLRLMVSGSSAL 300
Cdd:PRK06087 253 IGARSVLLDIFTPDACLALLEQQRCTCMLG-------ATPFIYD-LLNLLEKQ----------PADLSALRFFLCGGTTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 301 PETVKNDFMEiSGHNLLERYGMTE----IGMCLSNPLhgDRVSGSVGFPLPGVQVKinaeasstqngkpVFKDNTKEV-- 374
Cdd:PRK06087 315 PKKVARECQQ-RGIKLLSVYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIK-------------VVDEARKTLpp 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 375 ---GELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHP 450
Cdd:PRK06087 379 gceGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEA-GYIKITGRKK-DIIVRGGENISSREVEDILLQHP 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 451 DIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMW-CQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK06087 457 KIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
22-523 |
3.17e-50 |
|
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: 180.13 E-value: 3.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 22 IVNYPHNNTQ-RFTYNDLLNESAAISNQItfkkDDL---EQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHEL 97
Cdd:cd12119 14 IVSRTHEGEVhRYTYAEVAERARRLANAL----RRLgvkPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 98 EYTITNSKSSMVLTNKENYSMLAEI-GRKVGVQVIEIPEIGNGSPNK------EVQHKIMP---------FDINRNAQII 161
Cdd:cd12119 90 AYIINHAEDRVVFVDRDFLPLLEAIaPRLPTVEHVVVMTDDAAMPEPagvgvlAYEELLAAespeydwpdFDENTAAAIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNI--------EAQVKALVEAwewkkeDHILEFLPLHHVHGliniltcslW----SGAMCEM-- 227
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLvlhamaalLTDGLGLSES------DVVLPVVPMFHVNA---------WglpyAAAMVGAkl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 -MP-KFDSKQVIDRLLES-GVTtdleqpISLfmAVPTIYSKLIKYVEenvkteKERQDIEKafqrLRLMVSGSSALPETV 304
Cdd:cd12119 235 vLPgPYLDPASLAELIEReGVT------FAA--GVPTVWQGLLDHLE------ANGRDLSS----LRRVVIGGSAVPRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 305 KNDFMEIsGHNLLERYGMTE---IGMC--LSNPLHGD------RVSGSVGFPLPGVQVKINAEasstqNGKPVFKDNtKE 373
Cdd:cd12119 297 IEAFEER-GVRVIHAWGMTEtspLGTVarPPSEHSNLsedeqlALRAKQGRPVPGVELRIVDD-----DGRELPWDG-KA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 374 VGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIE 453
Cdd:cd12119 370 VGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATID-EDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 454 ECAVLGIPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd12119 448 EAAVIGVPHPKWGERPLAVVVLKEGATV-TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
59-523 |
6.93e-49 |
|
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: 174.57 E-value: 6.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKEnysmlaeigrkvgvqvieipeign 138
Cdd:cd05919 36 DRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD------------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 gspnkevqhkimpfDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKAL-VEAWEWKKEDHILEFLPLHHVHGLINILTC 217
Cdd:cd05919 92 --------------DI---AYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 218 SLWSGAMCEMMPKF-DSKQVIDRLLESGVTtdleqpisLFMAVPTIYSKLIkyVEENVKTEkerqdiekAFQRLRLMVSG 296
Cdd:cd05919 155 PLAVGASAVLNPGWpTAERVLATLARFRPT--------VLYGVPTFYANLL--DSCAGSPD--------ALRSLRLCVSA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 297 SSALPETVKNDFMEISGHNLLERYGMTEIG-MCLSNPLhGDRVSGSVGFPLPGVQVKINAEAsstqnGKPVFKDntkEVG 375
Cdd:cd05919 217 GEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRP-GAWRLGSTGRPVPGYEIRLVDEE-----GHTIPPG---EEG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEEC 455
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRD-ADGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 456 AVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05919 366 AVVAVPESTGLSRLTAFVVLKSPAAPQEslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-524 |
1.82e-48 |
|
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: 173.39 E-value: 1.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 28 NNTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKS 106
Cdd:cd05971 2 GTPEKVTFKELKTASNRFAN--VLKEIGLEKgDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 107 SMVLTNkenysmlaeigrkvgvqvieipeiGNGSPnkevqhkimpfdinrnAQIIYTSGTTSRPKGVIATHSNIEAQVKA 186
Cdd:cd05971 80 SALVTD------------------------GSDDP----------------ALIIYTSGTTGPPKGALHAHRVLLGHLPG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 187 LVEAWEWKKEDHILEFLPLHH--VHGLINILTCSLWSG--AMCEMMPKFDSKQVIDRLLESGVTTDLEQPISLfmavpti 262
Cdd:cd05971 120 VQFPFNLFPRDGDLYWTPADWawIGGLLDVLLPSLYFGvpVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTAL------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 263 ysKLIKYVEEnvktEKERQDIekafqRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSN-PLHGDRVSGS 341
Cdd:cd05971 193 --KMMRQQGE----QLKHAQV-----KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNcSALFPIKPGS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 342 VGFPLPGVQVKInaeasSTQNGKPVFKDntkEVGELLVKGPQ--VFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRF 419
Cdd:cd05971 262 MGKPIPGHRVAI-----VDDNGTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKD-SDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 420 KILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAY 497
Cdd:cd05971 333 WYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalAREIQELVKTRLAA 411
|
490 500
....*....|....*....|....*..
gi 330846471 498 YKVPKVIQVKEEIPKNAMLKVNKKDLV 524
Cdd:cd05971 412 HEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
34-523 |
1.35e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 173.80 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNS--KSSMVLT 111
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSgaKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 112 NKEnySMLAEIGRKVGVQVIEIPEIGNGSP-------NKEVQH--KIMPF----------------------DINRNAQI 160
Cdd:PRK05677 131 NMA--HLAEKVLPKTGVKHVIVTEVADMLPplkrlliNAVVKHvkKMVPAyhlpqavkfndalakgagqpvtEANPQADD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 161 I----YTSGTTSRPKGVIATHSNIEA---QVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKfds 233
Cdd:PRK05677 209 VavlqYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISN--- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 234 kqviDRLLESGVTTDLEQPISLFMAVPTIYSKLIkyveenvktekERQDIEKA-FQRLRLMVSGSSALPETVKNDFMEIS 312
Cdd:PRK05677 286 ----PRDLPAMVKELGKWKFSGFVGLNTLFVALC-----------NNEAFRKLdFSALKLTLSGGMALQLATAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 313 GHNLLERYGMTEIGMCLS-NPLHGDRVsGSVGFPLPGVQVK-INAEASSTQNGkpvfkdntkEVGELLVKGPQVFKEYFE 390
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSvNPSQAIQV-GTIGIPVPSTLCKvIDDDGNELPLG---------EVGELCVKGPQVMKGYWQ 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 391 KKEATQEAF-EDGWFKTGDI--VEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQ 467
Cdd:PRK05677 421 RPEATDEILdSDGWLKTGDIalIQED---GYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 468 VIGAILVYKKGaEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK05677 497 AIKVFVVVKPG-ETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
42-528 |
1.67e-47 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 173.49 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 42 SAAISNQITFKKDDLeqdrVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAE 121
Cdd:PLN02574 80 AAGLYHVMGVRQGDV----VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 122 IGrkvgVQVIEIPEIGN---GSPNKEVQHKIMPFD--------INRN--AQIIYTSGTTSRPKGVIATHSNIEAQVKALV 188
Cdd:PLN02574 156 LG----VPVIGVPENYDfdsKRIEFPKFYELIKEDfdfvpkpvIKQDdvAAIMYSSGTTGASKGVVLTHRNLIAMVELFV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 189 --EA--WEWKKEDHI-LEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIY 263
Cdd:PLN02574 232 rfEAsqYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTH--------FPVVPPIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 264 SKLIKyveenvkteKERQDIEKAFQRLRLMVSGSSALPETVKNDFMEISGH-NLLERYGMTEIGMCLSNPLHGDRVS--G 340
Cdd:PLN02574 304 MALTK---------KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHvDFIQGYGMTESTAVGTRGFNTEKLSkyS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 341 SVGFPLPGVQVKInAEASSTQNGKPvfkdntKEVGELLVKGPQVFKEYFEKKEATQ-EAFEDGWFKTGDIVEKDNStGRF 419
Cdd:PLN02574 375 SVGLLAPNMQAKV-VDWSTGCLLPP------GNCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDED-GYL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 420 KILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQQRLAYYK 499
Cdd:PLN02574 447 YIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKK 525
|
490 500
....*....|....*....|....*....
gi 330846471 500 VPKVIQVkEEIPKNAMLKVNKKDLVKLFT 528
Cdd:PLN02574 526 VRKVVFV-QSIPKSPAGKILRRELKRSLT 553
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-523 |
1.01e-46 |
|
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: 166.30 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGL-INILTCSLWSGAMCEMMPKFDSKQVID 238
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvLGVLACLTHGATMVFPSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 239 RLLEsgvttdlEQPISLFmAVPTIYSKLIkyveenvktekERQDIEK-AFQRLRL-MVSGSSALPETVKNDFMEISGHNL 316
Cdd:cd05917 87 AIEK-------EKCTALH-GVPTMFIAEL-----------EHPDFDKfDLSSLRTgIMAGAPCPPELMKRVIEVMNMKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTE----IGMCLSN-PLhgDRVSGSVGFPLPGVQVKI-NAEasstqnGKPVFKDNTKevGELLVKGPQVFKEYFE 390
Cdd:cd05917 148 TIAYGMTEtspvSTQTRTDdSI--EKRVNTVGRIMPHTEAKIvDPE------GGIVPPVGVP--GELCIRGYSVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 391 KKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVI 469
Cdd:cd05917 218 DPEKTAEAIdGDGWLHTGDLAVMDED-GYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 330846471 470 GAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05917 296 CAWIRLKEGAE-LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
160-514 |
1.13e-46 |
|
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: 165.91 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDSKQVIDR 239
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 240 LLESGVTtdleqpisLFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLmVSGSSAlPETVKNdFMEISGHNLLER 319
Cdd:cd17637 84 IEEEKVT--------LMGSFPPILSNLLDAAEKS----------GVDLSSLRH-VLGLDA-PETIQR-FEETTGATFWSL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 320 YGMTEIGMCLSNPLHGDRvSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF 399
Cdd:cd17637 143 YGQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIVDD-----NDRPV---PAGETGEIVVRGPLVFQGYWNLPELTAYTF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 EDGWFKTGDIvekdnstGRFK------ILGRSSV-DIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:cd17637 214 RNGWHHTGDL-------GRFDedgylwYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 330846471 473 LVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNA 514
Cdd:cd17637 287 CVLKPGATLTA-DELIEFVGSRIARYKKPRYVVFVEALPKTA 327
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
34-526 |
1.31e-46 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 169.82 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQItfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK 113
Cdd:cd05909 9 TYRKLLTGAIALARKL--AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 ENYSMLAEIGRKV---GVQVIEIPEIGNG----------------SPNKEVQHKIMPFDINRNAQIIYTSGTTSRPKGVI 174
Cdd:cd05909 87 QFIEKLKLHHLFDveyDARIVYLEDLRAKiskadkckaflagkfpPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 175 ATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPK-FDSKQVIDRLLESGVTtdleqpi 253
Cdd:cd05909 167 LSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKAT------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 254 sLFMAVPTIYSKLIKYVEenvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLS-NP 332
Cdd:cd05909 240 -ILLGTPTFLRGYARAAH------------PEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISvNT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 333 LHGDRVSGSVGFPLPGVQVKINAEASSTqngkPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEK 412
Cdd:cd05909 307 PQSPNKEGTVGRPLPGMEVKIVSVETHE----EV---PIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 DNStGRFKILGRSSvDIIKNSGYKISALEIEREILDH-PDIEECAVLGIPNEEYGQVIgaILVY-KKGAEPMSYDDF--- 487
Cdd:cd05909 380 DGE-GFLTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKI--VLLTtTTDTDPSSLNDIlkn 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 330846471 488 ----KMWcqqrlayykVPKVIQVKEEIPknaMLKVNKKDLVKL 526
Cdd:cd05909 456 agisNLA---------KPSYIHQVEEIP---LLGTGKPDYVTL 486
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
158-520 |
2.16e-46 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 164.98 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:cd17638 3 SDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 dRLLESgvttdleQPISLFMAVPTIYSKLIKyveenvktEKERQDIEKAfqRLRLMVSGSSALP-ETVKNDFMEISGHNL 316
Cdd:cd17638 83 -EAIER-------ERITVLPGPPTLFQSLLD--------HPGRKKFDLS--SLRAAVTGAATVPvELVRRMRSELGFETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMC-LSNPlhGDR---VSGSVGFPLPGVQVKInaeasstqngkpvfkdntKEVGELLVKGPQVFKEYFEKK 392
Cdd:cd17638 145 LTAYGLTEAGVAtMCRP--GDDaetVATTCGRACPGFEVRI------------------ADDGEVLVRGYNVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 393 EATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGA 471
Cdd:cd17638 205 EATAEAIdADGWLHTGDVGELDER-GYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 330846471 472 ILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:cd17638 283 FVVARPGVT-LTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
59-523 |
3.81e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 168.45 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNkenySMLAEiGRKVGVQVIE-IPEIG 137
Cdd:PRK09088 48 ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD----DAVAA-GRTDVEDLAAfIASAD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 138 NGSPNKEVqhkimPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAqvkALVEAWEWKKEDHILEFL---PLHHVHGLINI 214
Cdd:PRK09088 123 ALEPADTP-----SIPPERVSLILFTSGTSGQPKGVMLSERNLQQ---TAHNFGVLGRVDAHSSFLcdaPMFHIIGLITS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 215 LTCSLWSGAMCEMMPKFDSKQVIDRLlesgvtTDLEQPISLFMAVPTIYSKLikyveenvkteKERQDIE-KAFQRLRLM 293
Cdd:PRK09088 195 VRPVLAVGGSILVSNGFEPKRTLGRL------GDPALGITHYFCVPQMAQAF-----------RAQPGFDaAALRHLTAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 294 VSGSSALPETVKNDFMEiSGHNLLERYGMTEIGMCLSNPLHGDRV---SGSVGFPLPGVQVKI-NAEASSTQNGKPvfkd 369
Cdd:PRK09088 258 FTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDVIrakAGAAGIPTPTVQTRVvDDQGNDCPAGVP---- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 370 ntkevGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILD 448
Cdd:PRK09088 333 -----GELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRD-ADGFFWVVDRKK-DMFISGGENVYPAEIEAVLAD 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 449 HPDIEECAVLGIPNEEYGQViGAILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK09088 406 HPGIRECAVVGMADAQWGEV-GYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
18-523 |
1.28e-45 |
|
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: 165.78 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNyphnNTQRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHEL 97
Cdd:cd05930 2 DAVAVVD----GDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 98 EYTITNSKSSMVLTnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfDINRNAQIIYTSGTTSRPKGVIATH 177
Cdd:cd05930 77 AYILEDSGAKLVLT-----------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 178 SNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILtCSLWSGAMCEMMPK---FDSKQVIDRLLESGVTtdleqpis 254
Cdd:cd05930 116 RGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF-GALLAGATLVVLPEevrKDPEALADLLAEEGIT-------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 255 LFMAVPTIYSKLIKYVEenvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEI-SGHNLLERYGMTEIGM------ 327
Cdd:cd05930 187 VLHLTPSLLRLLLQELE------------LAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVdatyyr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 328 CLSNPLHGDRVsgSVGFPLPGVQVKI-NAeasstqNGKPVfKDNtkEVGELLVKGPQVFKEYFEKKEATQEAFEDGWF-- 404
Cdd:cd05930 255 VPPDDEEDGRV--PIGRPIPNTRVYVlDE------NLRPV-PPG--VPGELYIGGAGLARGYLNRPELTAERFVPNPFgp 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 405 -----KTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGA 479
Cdd:cd05930 324 germyRTGDLV-RWLPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 330846471 480 EPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05930 402 EL-DEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
157-527 |
1.82e-45 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 167.37 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 157 NAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCeMMP---KFDS 233
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPargRFSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 234 KQVIDRLLESGVTtdleqpisLFMAVPTIYSKLIkyveENVKTEKERQDIEKafqrLRLMVSGSSALPETVKNDFMEISG 313
Cdd:PRK05852 257 HTFWDDIKAVGAT--------WYTAVPTIHQILL----ERAATEPSGRKPAA----LRFIRSCSAPLTAETAQALQTEFA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 314 HNLLERYGMTEIgmclSNPLHGDRVSGSVGFPLPGVQVKINAEASSTQ------NGKPVFKDntkEVGELLVKGPQVFKE 387
Cdd:PRK05852 321 APVVCAFGMTEA----THQVTTTQIEGIGQTENPVVSTGLVGRSTGAQirivgsDGLPLPAG---AVGEVWLRGTTVVRG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 388 YFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQ 467
Cdd:PRK05852 394 YLGDPTITAANFTDGWLRTGDLGSLS-AAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGE 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 468 VIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLF 527
Cdd:PRK05852 472 AVAAVIVPRESAPP-TAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
59-523 |
1.85e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 166.60 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVI---EIPE 135
Cdd:PRK06145 53 DVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAaqaDSRR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 136 IGNGSPNKEVQHKIMPFDINRnaqIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINIL 215
Cdd:PRK06145 133 LAQGGLEIPPQAAVAPTDLVR---LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 216 TCSLWSGAMCEMMPKFDSKQVIDRLLESGVTTDLEQPI--SLFMAVPtiysklikyveenvktEKERQDIEKafqrLRLM 293
Cdd:PRK06145 210 IAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVmlSRVLTVP----------------DRDRFDLDS----LAWC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 294 VSGSSALPETVKNDFMEI-SGHNLLERYGMTEigMCLSNPL--HGDRVS--GSVGFPLPGVQVKINAEASSTqngkpvFK 368
Cdd:PRK06145 270 IGGGEKTPESRIRDFTRVfTRARYIDAYGLTE--TCSGDTLmeAGREIEkiGSTGRALAHVEIRIADGAGRW------LP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 369 DNTKevGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNSTgrFKILGRSSVDIIKNSGYKISALEIEREILD 448
Cdd:PRK06145 342 PNMK--GEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEG--FLYLTDRKKDMIISGGENIASSEVERVIYE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 449 HPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK06145 418 LPEVAEAAVIGVHDDRWGERITAVVVLNPGAT-LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
27-512 |
6.21e-45 |
|
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: 166.13 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 27 HNNTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSK 105
Cdd:cd05970 42 AGEERIFTFAELADYSDKTAN--FFKAMGIGKgDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 106 SSMVLTNKENY------SMLAEIGRK-----VGVQVIE-----IPEIGNGSPNKEVQHKiMPFDINRNAQIIY-TSGTTS 168
Cdd:cd05970 120 IKMIVAIAEDNipeeieKAAPECPSKpklvwVGDPVPEgwidfRKLIKNASPDFERPTA-NSYPCGEDILLVYfSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 169 RPKGVIATHSnieAQVKALVEAWEWkkedHILEFLPLHhvhgliniLTC--SLWSGAM-----------CEM----MPKF 231
Cdd:cd05970 199 MPKMVEHDFT---YPLGHIVTAKYW----QNVREGGLH--------LTVadTGWGKAVwgkiygqwiagAAVfvydYDKF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 DSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIkyveenvktekeRQDIEK-AFQRLRLMVSGSSALPETVKNDFME 310
Cdd:cd05970 264 DPKALLEKLSKYGVTT--------FCAPPTIYRFLI------------REDLSRyDLSSLRYCTTAGEALNPEVFNTFKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGHNLLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLV---KGPQV--F 385
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDL-----IDREGRSC---EAGEEGEIVIrtsKGKPVglF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 386 KEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:cd05970 396 GGYYKDAEKTAEVWHDGYYHTGDAAWMDED-GYLWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 330846471 466 GQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:cd05970 474 GQVVKATIVLAKGYEPSEelKKELQDHVKKVTAPYKYPRIVEFVDELPK 522
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-523 |
3.66e-44 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 164.00 E-value: 3.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNYPHNNTQRFTYNDLLNESAAIS-NQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVP 87
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGlHKLGIRQGD----VVMLLLPNCPEFVLAFLGASRRGAVTTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 88 LSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIPEIGNG----------SPNKEVQHKIMPFDInrn 157
Cdd:PLN02246 105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGclhfseltqaDENELPEVEISPDDV--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATH----SNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDs 233
Cdd:PLN02246 182 VALPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFE- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 234 kqvIDRLLEsgvttdLEQPISLFMA--VPTIYSKLIKyveenvKTEKERQDIEKafqrLRLMVSGSSALPETVKNDFM-E 310
Cdd:PLN02246 261 ---IGALLE------LIQRHKVTIApfVPPIVLAIAK------SPVVEKYDLSS----IRMVLSGAAPLGKELEDAFRaK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGHNLLERYGMTEIG----MCLS---NPLhgDRVSGSVGfplpgvQVKINAEA--------SSTQNGKPvfkdntkevG 375
Cdd:PLN02246 322 LPNAVLGQGYGMTEAGpvlaMCLAfakEPF--PVKSGSCG------TVVRNAELkivdpetgASLPRNQP---------G 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNSTGRFkILGRSSvDIIKNSGYKISALEIEREILDHPDIEE 454
Cdd:PLN02246 385 EICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELF-IVDRLK-ELIKYKGFQVAPAELEALLISHPSIAD 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 455 CAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYK-VPKVIQVkEEIPKNAMLKVNKKDL 523
Cdd:PLN02246 463 AAVVPMKDEVAGEVPVAFVVRSNGSE-ITEDEIKQFVAKQVVFYKrIHKVFFV-DSIPKAPSGKILRKDL 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
58-523 |
1.26e-43 |
|
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: 161.52 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 58 QDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIpEIG 137
Cdd:cd05923 53 GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSD-LVG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 138 NGSPnkEVQHKIMPFDINRNAQ---IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDH--ILEFLPLHHVHGLI 212
Cdd:cd05923 132 LGEP--ESAGPLIEDPPREPEQpafVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHnvVLGLMPLYHVIGFF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 213 NILTCSL-WSGAMCemMPKFDSKQVIDRLLESgvttdlEQPISLFmAVPTIYSKLIKYVE---ENVKTekerqdiekafq 288
Cdd:cd05923 210 AVLVAALaLDGTYV--VVEEFDPADALKLIEQ------ERVTSLF-ATPTHLDALAAAAEfagLKLSS------------ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 289 rLRLMVSGSSALPETV---KNDFMEISGHNLlerYGMTEIGMCLSNPlhgDRVSGSVGFPLPGVQVKINAEASSTQNGKP 365
Cdd:cd05923 269 -LRHVTFAGATMPDAVlerVNQHLPGEKVNI---YGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVRIGGSPDEALA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 366 VFKDntkevGELLVK--GPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIE 443
Cdd:cd05923 342 NGEE-----GELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPS-GDVRILGRVD-DMIISGGENIHPSEIE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 444 REILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGaePMSYDDFKMWCQ-QRLAYYKVPKVIQVKEEIPKNAMLKVNKKD 522
Cdd:cd05923 415 RVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQ 492
|
.
gi 330846471 523 L 523
Cdd:cd05923 493 L 493
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
28-464 |
1.86e-43 |
|
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: 160.60 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 28 NNTQRFTYNDLLNEsaaISNQITFKKD-DLEQDRVSFLYPQSfdyvRTQW-----GIWRSGGVAVPLSISHPPHELEYTI 101
Cdd:cd17640 1 KPPKRITYKDLYQE---ILDFAAGLRSlGVKAGEKVALFADN----SPRWliadqGIMALGAVDVVRGSDSSVEELLYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 102 TNSKSS-MVLTNKENysmlaeigrkvgvqvieipeigngspnkevqhkimpfDInrnAQIIYTSGTTSRPKGVIATHSNI 180
Cdd:cd17640 74 NHSESVaLVVENDSD-------------------------------------DL---ATIIYTSGTTGNPKGVMLTHANL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 181 EAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKF---DSKQVidrllesgvttdleQPiSLFM 257
Cdd:cd17640 114 LHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTlkdDLKRV--------------KP-HYIV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 258 AVP----TIYSKLIKYVeenVKTEKERQDIEKAF---QRLRLMVSGSSALPETVkNDFMEISGHNLLERYGMTEIGMCLS 330
Cdd:cd17640 179 SVPrlweSLYSGIQKQV---SKSSPIKQFLFLFFlsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 331 NPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDNTKevGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDI 409
Cdd:cd17640 255 ARRLKCNVRGSVGRPLPGTEIKIVDP-----EGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDL 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 410 VEKdNSTGRFKILGRSSVDIIKNSGYKISALEIEREILDHPDIEECAVLG----------IPNEE 464
Cdd:cd17640 328 GWL-TCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNFE 391
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
59-523 |
2.24e-43 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 162.11 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNS--KSSMVLtnkENYS------------------- 117
Cdd:PRK07059 74 ARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSgaEAIVVL---ENFAttvqqvlaktavkhvvvas 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 118 ---MLAEIG-------RKVG--VQVIEIPE-------IGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHS 178
Cdd:PRK07059 151 mgdLLGFKGhivnfvvRRVKkmVPAWSLPGhvrfndaLAEGARQTFKPVKLGPDDV---AFLQYTGGTTGVSKGATLLHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 179 NIEAQVKALvEAW---EWKKEDHILEF-----LPLHHVHGLInilTCSLWS---GAMCEMMPK-FDSKQVIDRLLESgvt 246
Cdd:PRK07059 228 NIVANVLQM-EAWlqpAFEKKPRPDQLnfvcaLPLYHIFALT---VCGLLGmrtGGRNILIPNpRDIPGFIKELKKY--- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 247 tdleqPISLFMAVPTIYSKLIKYveenvktekerQDIEKA-FQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI 325
Cdd:PRK07059 301 -----QVHIFPAVNTLYNALLNN-----------PDFDKLdFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSET 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 326 GMCLS-NPLHGDRVSGSVGFPLPGVQVKINAEASstqNGKPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEA-FEDGW 403
Cdd:PRK07059 365 SPVATcNPVDATEFSGTIGLPLPSTEVSIRDDDG---NDLPL-----GEPGEICIRGPQVMAGYWNRPDETAKVmTADGF 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 404 FKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAepMS 483
Cdd:PRK07059 437 FRTGDVGVMD-ERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA--LT 512
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 330846471 484 YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK07059 513 EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
151-526 |
2.51e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 162.82 E-value: 2.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCeMMPK 230
Cdd:PRK07529 209 PIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHV-VLAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 231 ---FDSKQVIDRLLESgvttdLEQ-PISLFMAVPTIYSKLikyveenVKTEKERQDIEKafqrLRLMVSGSSALPETVKN 306
Cdd:PRK07529 288 pqgYRGPGVIANFWKI-----VERyRINFLSGVPTVYAAL-------LQVPVDGHDISS----LRYALCGAAPLPVEVFR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 307 DFMEISGHNLLERYGMTEiGMCLS--NPLHGDRVSGSVGFPLPGVQVKInaeASSTQNGKPVFKDNTKEVGELLVKGPQV 384
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTE-ATCVSsvNPPDGERRIGSVGLRLPYQRVRV---VILDDAGRYLRDCAVDEVGVLCIAGPNV 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 385 FKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEE 464
Cdd:PRK07529 428 FSGYLEAAHNKGLWLEDGWLNTGDLGRID-ADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAH 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 465 YGQVIGAILVYKKGAEpMSYDDFKMWCQ----QRLAyykVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:PRK07529 506 AGELPVAYVQLKPGAS-ATEAELLAFARdhiaERAA---VPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-529 |
3.03e-42 |
|
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: 154.56 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 154 INRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGA-MCEMMPK-F 231
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVLAGPAgY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 DSKQVID---RLLEsgvttdlEQPISLFMAVPTIYSKLIKyVEENvktekerQDIEKafqrLRLMVSGSSALPETVKNDF 308
Cdd:cd05944 81 RNPGLFDnfwKLVE-------RYRITSLSTVPTVYAALLQ-VPVN-------ADISS----LRFAMSGAAPLPVELRARF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 309 MEISGHNLLERYGMTEiGMCLS--NPLHGDRVSGSVGFPLPGVQVKINAEASSTQNGKPVFKDntkEVGELLVKGPQVFK 386
Cdd:cd05944 142 EDATGLPVVEGYGLTE-ATCLVavNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRDCAPD---EVGEICVAGPGVFG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 387 EYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYG 466
Cdd:cd05944 218 GYLYTEGNKNAFVADGWLNTGDLGRLD-ADGYLFITGRAK-DLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 467 QVIGAILVYKKGAEpMSYDDFKMWCQQRLA-YYKVPKVIQVKEEIPKNAMLKVNKKDLVKLFTQ 529
Cdd:cd05944 296 ELPVAYVQLKPGAV-VEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-520 |
4.56e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 158.29 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 23 VNYPHNNTQRFTYNDLlnesAAISNQITFKKDDL---EQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEY 99
Cdd:PRK13295 46 VRLGTGAPRRFTYREL----AALVDRVAVGLARLgvgRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 100 TITNSKSSMVLTNKE--NY---SMLAEIGRKVGV--QVIEIPEIGNGS-------PNKEVQ---------HKIMPFDInr 156
Cdd:PRK13295 122 MLKHAESKVLVVPKTfrGFdhaAMARRLRPELPAlrHVVVVGGDGADSfeallitPAWEQEpdapailarLRPGPDDV-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 157 nAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQV 236
Cdd:PRK13295 200 -TQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 237 IDRLLESGVTtdleqpisLFMAVPTIYSKLIKYVEENvktekeRQDIEkafqRLRLMVSGSSALPETVKNDFMEISGHNL 316
Cdd:PRK13295 279 AELIRTEGVT--------FTMASTPFLTDLTRAVKES------GRPVS----SLRTFLCAGAPIPGALVERARAALGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGM----CLSNPLhgDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDntkEVGELLVKGPQVFKEYFEKK 392
Cdd:PRK13295 341 VSAWGMTENGAvtltKLDDPD--ERASTTDGCPLPGVEVRVVDA-----DGAPLPAG---QIGRLQVRGCSNFGGYLKRP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 393 EATQEAFeDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:PRK13295 411 QLNGTDA-DGWFDTGDLARIDAD-GYIRISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAF 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 330846471 473 LVYKKGaEPMSYDDFKMWC-QQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:PRK13295 488 VVPRPG-QSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
29-520 |
4.92e-42 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 158.00 E-value: 4.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 29 NTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSS 107
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAH--ALAAAGVKRgDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 108 MVLTNKENYSMLAEIGRKV-------------------GVQVIEIPEIGNGSPNKEVQhkimPFDInrnAQIIYTSGTTS 168
Cdd:PRK06155 121 LLVVEAALLAALEAADPGDlplpavwlldapasvsvpaGWSTAPLPPLDAPAPAAAVQ----PGDT---AAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 169 RPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDSKQVIDRLLESG--VT 246
Cdd:PRK06155 194 PSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSASGFWPAVRRHGatVT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 247 TDLEQPISLFMAVPtiysklikyveenvKTEKERQdiekafQRLRLMVSGssALPETVKNDFMEISGHNLLERYGMTEIG 326
Cdd:PRK06155 273 YLLGAMVSILLSQP--------------ARESDRA------HRVRVALGP--GVPAALHAAFRERFGVDLLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 327 MCLSNPlHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDntkEVGELLVKGPQVF---KEYFEKKEATQEAFEDGW 403
Cdd:PRK06155 331 FVIAVT-HGSQRPGSMGRLAPGFEARVVDE-----HDQELPDG---EPGELLLRADEPFafaTGYFGMPEKTVEAWRNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 404 FKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKG--AEP 481
Cdd:PRK06155 402 FHTGDRVVRDAD-GWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGtaLEP 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 330846471 482 msyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:PRK06155 480 ---VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQK 515
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
15-523 |
5.89e-42 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 158.12 E-value: 5.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 15 KYKNRIAIVNYPHNNTQRFTynDLLNE--SAAISNQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISH 92
Cdd:PRK08751 37 KFADRPAYHSFGKTITYREA--DQLVEqfAAYLLGELQLKKGD----RVALMMPNCLQYPIATFGVLRAGLTVVNVNPLY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 93 PPHELEYTITNSKSSmVLTNKENYSMLAE--IGRKVGVQVIE-------------------------IPE--IGNGSPNK 143
Cdd:PRK08751 111 TPRELKHQLIDSGAS-VLVVIDNFGTTVQqvIADTPVKQVITtglgdmlgfpkaalvnfvvkyvkklVPEyrINGAIRFR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 144 EV-----QHKIMPFDINRN--AQIIYTSGTTSRPKGVIATHSNIEAQVKalvEAWEW--------KKEDHILEFLPLHHV 208
Cdd:PRK08751 190 EAlalgrKHSMPTLQIEPDdiAFLQYTGGTTGVAKGAMLTHRNLVANMQ---QAHQWlagtgkleEGCEVVITALPLYHI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 209 HGLI-NILTCSLWSGAMCEMMPKFDSKQVIDRLLESgvttdleqPISLFMAVPTIYSKLIKYVEENvktekerqdiEKAF 287
Cdd:PRK08751 267 FALTaNGLVFMKIGGCNHLISNPRDMPGFVKELKKT--------RFTAFTGVNTLFNGLLNTPGFD----------QIDF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 288 QRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI--GMCLsNPLHGDRVSGSVGFPLPGVQVKINAEASSTQNgkp 365
Cdd:PRK08751 329 SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETspAACI-NPLTLKEYNGSIGLPIPSTDACIKDDAGTVLA--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 366 vfkdnTKEVGELLVKGPQVFKEYFEKKEATQEAFE-DGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIER 444
Cdd:PRK08751 405 -----IGEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMD-EQGFVYIVDRKK-DMILVSGFNVYPNEIED 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 445 EILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAepMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK08751 478 VIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA--LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
31-523 |
9.55e-42 |
|
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: 155.48 E-value: 9.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL 110
Cdd:cd05945 15 RTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 TnkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEA 190
Cdd:cd05945 94 A-----------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 191 WEWKKEDHILEFLPLH---HVHGLIniltCSLWSGAMCEMMPK---FDSKQVIDRLLESGVTTdleqpislFMAVPTIYS 264
Cdd:cd05945 133 FPLGPGDVFLNQAPFSfdlSVMDLY----PALASGATLVPVPRdatADPKQLFRFLAEHGITV--------WVSTPSFAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 265 KLIKyveenvktekERQDIEKAFQRLRLMVSGSSALPETVKNDFME-ISGHNLLERYGMTEI-GMCLSN-----PLHG-D 336
Cdd:cd05945 201 MCLL----------SPTFTPESLPSLRHFLFCGEVLPHKTARALQQrFPDARIYNTYGPTEAtVAVTYIevtpeVLDGyD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 337 RVSgsVGFPLPGVQVKInaeasSTQNGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAF--EDG--WFKTGDIVEK 412
Cdd:cd05945 271 RLP--IGYAKPGAKLVI-----LDEDGRPVPPG---EKGELVISGPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGDLVRL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 DNsTGRFKILGRssVDI-IKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWC 491
Cdd:cd05945 341 EA-DGLLFYRGR--LDFqVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAEL 417
|
490 500 510
....*....|....*....|....*....|..
gi 330846471 492 QQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05945 418 AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
158-520 |
1.02e-41 |
|
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: 152.80 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALV-EAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQV 236
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 237 IDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEENVKTEKerqdiekafqRLRLMVSGSSALPETVKNDFMEISGHNL 316
Cdd:cd17635 84 FKILTTNAVTT--------TCLVPTLLSKLVSELKSANATVP----------SLRLIGYGGSRAIAADVRFIEATGLTNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMCLSNPLHGDRVS-GSVGFPLPGVQVKINAeasstQNGKPVFKDntkEVGELLVKGPQVFKEYFEKKEAT 395
Cdd:cd17635 146 AQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAA-----TDGIAGPSA---SFGTIWIKSPANMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAFEDGWFKTGDIVEKdNSTGRFKILGRSSVDIIKnSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVY 475
Cdd:cd17635 218 AEVLIDGWVNTGDLGER-REDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 330846471 476 KKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:cd17635 296 SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
15-520 |
2.99e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 156.09 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 15 KYKNRIAIVNYPHNntQRFTYNDLLNESAAISN---QITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSIS 91
Cdd:PRK12583 30 RFPDREALVVRHQA--LRYTWRQLADAVDRLARgllALGVQPGD----RVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 92 HPPHELEYTITNSKSSMVLT-----NKENYSMLAEIgrkvgvqvieIPEIGNGSPNkEVQHKIMP-------FDIN---- 155
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICadafkTSDYHAMLQEL----------LPGLAEGQPG-ALACERLPelrgvvsLAPApppg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 156 ---------------------RNAQ--------IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLH 206
Cdd:PRK12583 173 flawhelqargetvsrealaeRQASldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 207 HVHGLI-NILTCsLWSGAmCEMMPK--FDSKQVIDRLLESGVTTdleqpislFMAVPTIYsklIKYVEEnvkteKERQDI 283
Cdd:PRK12583 253 HCFGMVlANLGC-MTVGA-CLVYPNeaFDPLATLQAVEEERCTA--------LYGVPTMF---IAELDH-----PQRGNF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 284 EKAFQRLRLMvSGSSALPETVKNDFMEISGHNLLERYGMTEIG-----MCLSNPLhgDRVSGSVGFPLPGVQVK-INAEA 357
Cdd:PRK12583 315 DLSSLRTGIM-AGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSpvslqTTAADDL--ERRVETVGRTQPHLEVKvVDPDG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 358 SSTQNGkpvfkdntkEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYK 436
Cdd:PRK12583 392 ATVPRG---------EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQ-GYVRIVGRSK-DMIIRGGEN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 437 ISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGaEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAML 516
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG-HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTG 539
|
....
gi 330846471 517 KVNK 520
Cdd:PRK12583 540 KVQK 543
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
76-523 |
3.54e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 155.20 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 76 WGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNkENYSMLAEIGRKVGVQVIEIPEIGNGSPNKEVQH-------- 147
Cdd:PRK07470 75 FAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICH-ADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEAlvarhlga 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 148 KIMPFDINRN--AQIIYTSGTTSRPKGVIATHSN----IEAQVKALVEAWewKKEDHILEFLPLHH---VHGLINILtcs 218
Cdd:PRK07470 154 RVANAAVDHDdpCWFFFTSGTTGRPKAAVLTHGQmafvITNHLADLMPGT--TEQDASLVVAPLSHgagIHQLCQVA--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 219 lwSGAMCEMMP--KFDSKQVIDRLLESGVTTdleqpislFMAVPTIysklIKYVEENVKTEKE----------------R 280
Cdd:PRK07470 229 --RGAATVLLPseRFDPAEVWALVERHRVTN--------LFTVPTI----LKMLVEHPAVDRYdhsslryviyagapmyR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 281 QDIEKAFQRLrlmvsgssalpetvkndfmeisGHNLLERYGMTEIGMC---LSNPLH------GDRVsGSVGFPLPGVQV 351
Cdd:PRK07470 295 ADQKRALAKL----------------------GKVLVQYFGLGEVTGNitvLPPALHdaedgpDARI-GTCGFERTGMEV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 352 KINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIK 431
Cdd:PRK07470 352 QIQDD-----EGREL---PPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLD-ARGFLYITGRAS-DMYI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 432 NSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAePMSYDDFKMWCQQRLAYYKVPKVIQVKEEIP 511
Cdd:PRK07470 422 SGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA-PVDEAELLAWLDGKVARYKLPKRFFFWDALP 500
|
490
....*....|..
gi 330846471 512 KNAMLKVNKKDL 523
Cdd:PRK07470 501 KSGYGKITKKMV 512
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
33-512 |
3.66e-41 |
|
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: 153.81 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNQIT---FKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMV 109
Cdd:cd05969 1 YTFAQLKVLSARFANVLKslgVGKGD----RVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 110 LTNKENYSMLaeigrkvgvqvieipeigngspnkevqhkimpfDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVE 189
Cdd:cd05969 77 ITTEELYERT---------------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 190 AWEWKKEDHILEFLPLHHVHGLI-NILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpisLFMAVPTIYSKLIK 268
Cdd:cd05969 124 VLDLHPDDIYWCTADPGWVTGTVyGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVT--------VWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 269 YVEENVKTEKErqdiekafQRLRLMVSGSSAL-PETVKNDfMEISGHNLLERYGMTEIG-MCLSNPLHGDRVSGSVGFPL 346
Cdd:cd05969 196 EGDELARKYDL--------SSLRFIHSVGEPLnPEAIRWG-MEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 347 PGVQVKInaeasSTQNGKPVFKDntkEVGELLVKG--PQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGR 424
Cdd:cd05969 267 PGVKAAV-----VDENGNELPPG---TKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDED-GYFWFVGR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 425 SSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSY--DDFKMWCQQRLAYYKVPK 502
Cdd:cd05969 338 AD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkEEIINFVRQKLGAHVAPR 416
|
490
....*....|
gi 330846471 503 VIQVKEEIPK 512
Cdd:cd05969 417 EIEFVDNLPK 426
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1-525 |
6.00e-41 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 154.55 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 1 MHRLpslqLFQNALKYKNRIAIVNypHNNTqrFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIW 79
Cdd:TIGR03098 2 LHHL----LEDAAARLPDATALVH--HDRT--LTYAALSERVLALAS--GLRGLGLARgERVAIYLDKRLETVTAMFGAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 80 RSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSML------AEIGRKVgVQVIEIPEIGNGSPNKEVQ------- 146
Cdd:TIGR03098 72 LAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgCHDLRTL-IIVGDPAHASEGHPGEEPAswpklla 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 147 -------HKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSL 219
Cdd:TIGR03098 151 lgdadppHPVIDSDM---AAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF-NQLTTAF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 220 WSGAMCEMMPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLikyveenvktekERQDI-EKAFQRLRLMVSGSS 298
Cdd:TIGR03098 227 YVGATVVLHDYLLPRDVLKALEKHGITG--------LAAVPPLWAQL------------AQLDWpESAAPSLRYLTNSGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 299 ALP-ETVKNDFMEISGHNLLERYGMTE-IGMCLSNPLHGDRVSGSVGFPLPGVQVKI-NAEASSTQNGkpvfkdntkEVG 375
Cdd:TIGR03098 287 AMPrATLSRLRSFLPNARLFLMYGLTEaFRSTYLPPEEVDRRPDSIGKAIPNAEVLVlREDGSECAPG---------EEG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAF------EDG--------WfkTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALE 441
Cdd:TIGR03098 358 ELVHRGALVAMGYWNDPEKTAERFrplppfPGElhlpelavW--SGDTVRRDEE-GFLYFVGRRD-EMIKTSGYRVSPTE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 442 IEREILDHPDIEECAVLGIPNEEYGQVIgAILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKK 521
Cdd:TIGR03098 434 VEEVAYATGLVAEAVAFGVPDPTLGQAI-VLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRK 512
|
....
gi 330846471 522 DLVK 525
Cdd:TIGR03098 513 ALAK 516
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
32-523 |
2.14e-40 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 151.48 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 32 RFTYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL- 110
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALc 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 ----TNKENYSMLAeigrkvgvqvieipeigngspnkevqhkimpfdinrnaqiiYTSGTTSRPKGVIATHSNieaqVKA 186
Cdd:cd05958 90 ahalTASDDICILA-----------------------------------------FTSGTTGAPKATMHFHRD----PLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 187 LVEAW-----EWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpisLFMAVPT 261
Cdd:cd05958 125 SADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPT--------VLFTAPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 262 IYSKLIKyveenvKTEKERQDIEKafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE-IGMCLSNPlHGDRVSG 340
Cdd:cd05958 197 AYRAMLA------HPDAAGPDLSS----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISAR-PGDARPG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 341 SVGFPLPGVQVKINAEAsstqnGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQeaFEDGWFKTGDIVEKDnSTGRFK 420
Cdd:cd05958 266 ATGKPVPGYEAKVVDDE-----GNPV---PDGTIGRLAVRGPTGCRYLADKRQRTY--VQGGWNITGDTYSRD-PDGYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 421 ILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKG--AEPMSYDDFKMWCQQRLAYY 498
Cdd:cd05958 335 HQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGviPGPVLARELQDHAKAHIAPY 413
|
490 500
....*....|....*....|....*
gi 330846471 499 KVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05958 414 KYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
147-523 |
3.90e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 153.05 E-value: 3.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 147 HKIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEA---QVKALVEA--------WEWKKEDHILEfLPLHHVHGLInil 215
Cdd:PRK12492 199 LKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlQVRACLSQlgpdgqplMKEGQEVMIAP-LPLYHIYAFT--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 216 tcslwSGAMCEMMPKFDSKQVIDRLLESGVTTDLEQ-PISLFMAVPTIYSKLIKYveenvkteKERQDIEkaFQRLRLMV 294
Cdd:PRK12492 275 -----ANCMCMMVSGNHNVLITNPRDIPGFIKELGKwRFSALLGLNTLFVALMDH--------PGFKDLD--FSALKLTN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 295 SGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRVS-GSVGFPLPGVQVK-INAEASSTQNGkpvfkdntk 372
Cdd:PRK12492 340 SGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKvIDDDGNELPLG--------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 373 EVGELLVKGPQVFKEYFEKKEATQEAFE-DGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPD 451
Cdd:PRK12492 411 ERGELCIKGPQVMKGYWQQPEATAEALDaEGWFKTGDIAVID-PDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPK 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330846471 452 IEECAVLGIPNEEYGQVIGAILVYKKGAepMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK12492 489 VANCAAIGVPDERSGEAVKLFVVARDPG--LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
57-459 |
7.08e-40 |
|
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: 151.47 E-value: 7.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 57 EQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK--ENYSMLAEIGRKVGVQVIEIP 134
Cdd:cd05932 30 PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKldDWKAMAPGVPEGLISISLPPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 135 EIGN-----------GSPNKEvqhKIMPFDiNRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFL 203
Cdd:cd05932 110 SAANcqyqwddliaqHPPLEE---RPTRFP-EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 204 PLHHVHGLINILTCSLWSGAMCEMMPKFDSkqvidrllesgVTTDLE--QPiSLFMAVPTIYSKLIKYVEENVKTEK--- 278
Cdd:cd05932 186 PLAHVTERVFVEGGSLYGGVLVAFAESLDT-----------FVEDVQraRP-TLFFSVPRLWTKFQQGVQDKIPQQKlnl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 279 ----------ERQDIEKA--FQRLRLMVSGSSALPETVKNDFMEIsGHNLLERYGMTE--IGMCLSNPlhGDRVSGSVGF 344
Cdd:cd05932 254 llkipvvnslVKRKVLKGlgLDQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTEnfAYSHLNYP--GRDKIGTVGN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 345 PLPGVQVKINaeasstqngkpvfkdntkEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILG 423
Cdd:cd05932 331 AGPGVEVRIS------------------EDGEILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELD-ADGNLTITG 391
|
410 420 430
....*....|....*....|....*....|....*..
gi 330846471 424 RSSvDIIKNS-GYKISALEIEREILDHPDIEECAVLG 459
Cdd:cd05932 392 RVK-DIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
158-481 |
1.48e-39 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 150.44 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVE-AWEWKKE-DHILEFLPLHHVHGLINILTCSLWSGAMCemmpkFDSKQ 235
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPELLGPdDRYLAYLPLAHIFELAAENVCLYRGGTIG-----YGSPR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLESGVTTDLE--QPiSLFMAVPTIYSKLIKYVEENV--KTEKERQDIEKAFQ----------------------- 288
Cdd:cd17639 166 TLTDKSKRGCKGDLTefKP-TLMVGVPAIWDTIRKGVLAKLnpMGGLKRTLFWTAYQsklkalkegpgtplldelvfkkv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 289 ------RLRLMVSGSSAL-PETVKndFMEISGHNLLERYGMTEI--GMCLSNPlhGDRVSGSVGFPLPGVQVKInaeaSS 359
Cdd:cd17639 245 raalggRLRYMLSGGAPLsADTQE--FLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKL----VD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 360 TQNGKpVFKDNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKIS 438
Cdd:cd17639 317 WEEGG-YSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFH-PDGTLKIIDRKK-DLVKLQNGEYI 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 330846471 439 ALE-IEREILDHPDIEECAVLGIPNEEYgqVIGAILVYKKGAEP 481
Cdd:cd17639 394 ALEkLESIYRSNPLVNNICVYADPDKSY--PVAIVVPNEKHLTK 435
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
34-457 |
5.71e-39 |
|
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: 147.03 E-value: 5.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK 113
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 ENYSMLAEIGRKVG-VQVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWE 192
Cdd:TIGR01733 81 ALASRLAGLVLPVIlLDPLELAALDDAPAPPPPDAPSGPDDL---AYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 193 WKKEDHILEFLPLHHVHGLINILTCslWSGAMCEMMPKFDSKQVIDRLLEsgvTTDLEQPISLFMAVPTIYSKLIkyvee 272
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGA--LLAGATLVVPPEDEERDDAALLA---ALIAEHPVTVLNLTPSLLALLA----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 273 nvktekerQDIEKAFQRLRLMVSGSSALPETVKNDFMEISG----HNLlerYGMTEI-GMCLSNPLHGDRVSG----SVG 343
Cdd:TIGR01733 228 --------AALPPALASLRLVILGGEALTPALVDRWRARGPgarlINL---YGPTETtVWSTATLVDPDDAPRespvPIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 344 FPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF---------EDGWFKTGDIVeKDN 414
Cdd:TIGR01733 297 RPLANTRLYVLDD-----DLRPV---PVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLV-RYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 330846471 415 STGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAV 457
Cdd:TIGR01733 368 PDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-520 |
4.64e-38 |
|
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: 144.97 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 33 FTYNDLLNESAAISNQITfkkddlEQ-----DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSS 107
Cdd:cd05973 1 LTFGELRALSARFANALQ------ELgvgpgDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 108 MVLTNKENYSMLAEigrkvgvqvieipeigngspnkevqhkiMPFdinrnaQIIYTSGTTSRPKGVIATHSNIEAQVKAL 187
Cdd:cd05973 75 LVVTDAANRHKLDS----------------------------DPF------VMMFTSGTTGLPKGVPVPLRALAAFGAYL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 188 VEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMP-KFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKL 266
Cdd:cd05973 121 RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVIERLGVTN--------LAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 267 IKY---VEENVKTekerqdiekafqRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRV--SGS 341
Cdd:cd05973 193 MAAgaeVPARPKG------------RLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPvhAGS 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 342 VGFPLPGVQVKinaeasstqngkpVFKDNTKEVGEL--------LVKGPQV-FKEYFEKKeatQEAFEDGWFKTGDIVEK 412
Cdd:cd05973 261 AGRAMPGWRVA-------------VLDDDGDELGPGepgrlaidIANSPLMwFRGYQLPD---TPAIDGGYYLTGDTVEF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 413 DNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMW 490
Cdd:cd05973 325 DPD-GSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPalADELQLH 402
|
490 500 510
....*....|....*....|....*....|
gi 330846471 491 CQQRLAYYKVPKVIQVKEEIPKNAMLKVNK 520
Cdd:cd05973 403 VKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-523 |
1.44e-37 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 145.51 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 4 LPSLQLfQNALKYKNRIAIVNYPHNNTqrFTYNDLLNESAAISNQIT---FKKDDLeqdrVSFLYPQSFDYVRTQWGIWR 80
Cdd:PLN02330 30 LPDFVL-QDAELYADKVAFVEAVTGKA--VTYGEVVRDTRRFAKALRslgLRKGQV----VVVVLPNVAEYGIVALGIMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 81 SGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYS----------MLAEIGRKVGVQVIEIPEIGNGSPNKEVQHKIM 150
Cdd:PLN02330 103 AGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGkvkglglpviVLGEEKIEGAVNWKELLEAADRAGDTSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAW--EWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMM 228
Cdd:PLN02330 183 QTDL---CALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgpEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 229 PKFDSKQVIDRLLESGVTTdleQPIslfmaVPTIYSKLIK--YVEENvktekerqDIEKAfqRLRLMVSGSSAL-PETVK 305
Cdd:PLN02330 260 SRFELRTFLNALITQEVSF---API-----VPPIILNLVKnpIVEEF--------DLSKL--KLQAIMTAAAPLaPELLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 306 NDFMEISGHNLLERYGMTEiGMCLSnPLHGDRVSG-------SVGFPLPGVQVK-INAEasstqNGKPVFKDNTkevGEL 377
Cdd:PLN02330 322 AFEAKFPGVQVQEAYGLTE-HSCIT-LTHGDPEKGhgiakknSVGFILPNLEVKfIDPD-----TGRSLPKNTP---GEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNSTGRFkILGRSSvDIIKNSGYKISALEIEREILDHPDIEECA 456
Cdd:PLN02330 392 CVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIF-IVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAA 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330846471 457 VLGIPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PLN02330 470 VVPLPDEEAGEIPAACVVINPKAKE-SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-524 |
1.97e-37 |
|
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: 143.73 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGG----VAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLaeigRKVGVQ----- 129
Cdd:cd05922 19 ERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL----RDALPAspdpg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 130 -VIEIPEI---GNGSPNKEVQHKimpfDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPL 205
Cdd:cd05922 95 tVLDADGIraaRASAPAHEVSHE----DL---ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 206 HHVHGLiNILTCSLWSGAmcemmpkfdsKQVI--DRLLESGVTTDL-EQPISLFMAVPTIYSKLikyveenvktekERQD 282
Cdd:cd05922 168 SYDYGL-SVLNTHLLRGA----------TLVLtnDGVLDDAFWEDLrEHGATGLAGVPSTYAML------------TRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 283 IEKA-FQRLRLMVSGSSALPETVKNDFME-ISGHNLLERYGMTEI--GMCLSNPLHGDRVSGSVGFPLPGVQVKI-NAEA 357
Cdd:cd05922 225 FDPAkLPSLRYLTQAGGRLPQETIARLRElLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEIlDDDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 358 SSTQNGkpvfkdntkEVGELLVKGPQVFKEYF-EKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYK 436
Cdd:cd05922 305 TPTPPG---------EPGEIVHRGPNVMKGYWnDPPYRRKEGRGGGVLHTGDLARRDED-GFLFIVGRRD-RMIKLFGNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 437 ISALEIEREILDHPDIEECAVLGIPnEEYGQVIGAILVYKKGAEPmsyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAML 516
Cdd:cd05922 374 ISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDP---KDVLRSLAERLPPYKVPATVRVVDELPLTASG 449
|
....*...
gi 330846471 517 KVNKKDLV 524
Cdd:cd05922 450 KVDYAALR 457
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
59-529 |
2.04e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 145.18 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTnkenYSMLAEIGRKVGVQ--------- 129
Cdd:PRK06178 84 DRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA----LDQLAPVVEQVRAEtslrhvivt 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 130 ----------VIEIPEIGNGSPNK-EVQHKIMPF-------------DINRNAQIIYTSGTTSRPKGVIATHSN-IEAQV 184
Cdd:PRK06178 160 sladvlpaepTLPLPDSLRAPRLAaAGAIDLLPAlractapvplpppALDALAALNYTGGTTGMPKGCEHTQRDmVYTAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 185 KALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdleqpiSLFMAVPTiys 264
Cdd:PRK06178 240 AAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVT-------RTVMLVDN--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 265 klikYVEENVKTEKERQDIeKAFQRLRlMVSGSSALPETVKNDFMEISGHNLLE-RYGMTEIGMC--------------L 329
Cdd:PRK06178 310 ----AVELMDHPRFAEYDL-SSLRQVR-VVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETHTCdtftagfqdddfdlL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 330 SNPLHgdrvsgsVGFPLPGVQVKInaeaSSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDI 409
Cdd:PRK06178 384 SQPVF-------VGLPVPGTEFKI----CDFETGELL---PLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDI 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 410 VEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAePMSYDDFKM 489
Cdd:PRK06178 450 GKIDEQ-GFLHYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA-DLTAAALQA 526
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 330846471 490 WCQQRLAYYKVPkVIQVKEEIPKNAMLKVNKKDLVKLFTQ 529
Cdd:PRK06178 527 WCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEE 565
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
155-525 |
4.04e-37 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 144.56 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 155 NRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKFDSK 234
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALA-MLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEENvKTEKERQDIEKafqrlrlMVSGSSALPETVKNDFMEI-SG 313
Cdd:PLN02860 251 AALQAIKQHNVTS--------MITVPAMMADLISLTRKS-MTWKVFPSVRK-------ILNGGGSLSSRLLPDAKKLfPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 314 HNLLERYGMTEIGMCLS----------------------NPLHGDRVSGS-VGFPLPGVQVKINAEASSTqngkpvfkdn 370
Cdd:PLN02860 315 AKLFSAYGMTEACSSLTfmtlhdptlespkqtlqtvnqtKSSSVHQPQGVcVGKPAPHVELKIGLDESSR---------- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 371 tkeVGELLVKGPQVFKEYF-EKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDH 449
Cdd:PLN02860 385 ---VGRILTRGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWIDKA-GNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQH 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 450 PDIEECAVLGIPNEEYGQVIGAI-------------LVYKKGAEPMSYDDFKMWC-QQRLAYYKVPK-VIQVKEEIPKNA 514
Cdd:PLN02860 460 PGVASVVVVGVPDSRLTEMVVACvrlrdgwiwsdneKENAKKNLTLSSETLRHHCrEKNLSRFKIPKlFVQWRKPFPLTT 539
|
410
....*....|.
gi 330846471 515 MLKVnKKDLVK 525
Cdd:PLN02860 540 TGKI-RRDEVR 549
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
59-523 |
4.89e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 143.30 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKvGVQVIEI---PE 135
Cdd:PRK12406 37 DCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPA-GVTVLSVptpPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 136 I--------GNGSPNKE--------VQHKimPFDINRNAQ---IIYTSGTTSRPKGV---IATHSNIEAQVKALVEAWEW 193
Cdd:PRK12406 116 IaaayrispALLTPPAGaidwegwlAQQE--PYDGPPVPQpqsMIYTSGTTGHPKGVrraAPTPEQAAAAEQMRALIYGL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 194 KKEDHILEFLPLHH----VHGLIniltcSLWSGAMCEMMPKFDSKQVIDRLLESGVTTdleqpisLFMaVPTIYSKLIKY 269
Cdd:PRK12406 194 KPGIRALLTGPLYHsapnAYGLR-----AGRLGGVLVLQPRFDPEELLQLIERHRITH-------MHM-VPTMFIRLLKL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 270 VEEnvktEKERQDIEKafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEIGMC--------LSNPlhgdrvsGS 341
Cdd:PRK12406 261 PEE----VRAKYDVSS----LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVtfatsedaLSHP-------GT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 342 VGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQV--FKeYFEKKEATQEAFEDGWFKTGDI--VEKDnstG 417
Cdd:PRK12406 326 VGKAAPGAELRFVDE-----DGRPL---PQGEIGEIYSRIAGNpdFT-YHNKPEKRAEIDRGGFITSGDVgyLDAD---G 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 418 RFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAY 497
Cdd:PRK12406 394 YLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAT-LDEADIRAQLKARLAG 471
|
490 500
....*....|....*....|....*.
gi 330846471 498 YKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK12406 472 YKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
162-520 |
5.28e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 143.93 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATH--------SNIEAqvkalveaWEWKKEDHILEFLPLHHVHGLiniltCSLWSGAM------Cem 227
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgaylnalSNILA--------WGMPKHPVYLWTLPMFHCNGW-----CFPWTVAAragtnvC-- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 MPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEEnvktekERQDIEkafQRLRLMVSGSsALPETVKND 307
Cdd:PRK08162 254 LRKVDPKLIFDLIREHGVTH--------YCGAPIVLSALINAPAE------WRAGID---HPVHAMVAGA-APPAAVIAK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 308 fMEISGHNLLERYGMTE----IGMCLSNPlHGDRVSGSVGFPLPGVQ-VKINAEASST----QNGKPVFKDNtKEVGELL 378
Cdd:PRK08162 316 -MEEIGFDLTHVYGLTEtygpATVCAWQP-EWDALPLDERAQLKARQgVRYPLQEGVTvldpDTMQPVPADG-ETIGEIM 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 379 VKGPQVFKEYFEKKEATQEAFEDGWFKTGD--IVEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECA 456
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAFAGGWFHTGDlaVLHPD---GYIKIKDRSK-DIIISGGENISSIEVEDVLYRHPAVLVAA 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 457 VLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIqVKEEIPKNAMLKVNK 520
Cdd:PRK08162 469 VVAKPDPKWGEVPCAFVELKDGAS-ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQK 530
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
162-518 |
5.83e-37 |
|
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: 139.08 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKFDSKQVIDrll 241
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKFNPKSWIR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 242 esgvtTDLEQPISLFMAVPTIYSKLIKyVEENVKTekerqdiekafqrLRLMVSGSSALPETVKNDFMEISGH-NLLERY 320
Cdd:cd17633 83 -----KINQYNATVIYLVPTMLQALAR-TLEPESK-------------IKSIFSSGQKLFESTKKKLKNIFPKaNLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 321 GMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEASStqngkpvfkdntkEVGELLVKGPQVFKEYFEKKEATqeafE 400
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGG-------------EIGKIFVKSEMVFSGYVRGGFSN----P 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 401 DGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVigAILVYKkgAE 480
Cdd:cd17633 207 DGWMSVGDIGYVDEE-GYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI--AVALYS--GD 280
|
330 340 350
....*....|....*....|....*....|....*...
gi 330846471 481 PMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd17633 281 KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
12-511 |
1.67e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 138.76 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 12 NALKYKNRIAIvnypHNNTQRFTYNDLLNESAAISNQITFKKDdlEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSIS 91
Cdd:PRK07638 10 HASLQPNKIAI----KENDRVLTYKDWFESVCKVANWLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 92 HPPHELEYTITNSKSSMVLTNKENYSMLAEigrkVGVQVIEIPE----IGN----GSPNKEVQHKimPFDINrnaqiiYT 163
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTERYKLNDLPD----EEGRVIEIDEwkrmIEKylptYAPIENVQNA--PFYMG------FT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 164 SGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKFDSKQVIDRLles 243
Cdd:PRK07638 152 SGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIS-TLYVGQTVHLMRKFIPNQVLDKL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 244 gvttDLEQpISLFMAVPTIYSKLIKyveenvktekerqdiEKAF--QRLRLMVSGSSaLPETVKNDFMEISGH-NLLERY 320
Cdd:PRK07638 228 ----ETEN-ISVMYTVPTMLESLYK---------------ENRVieNKMKIISSGAK-WEAEAKEKIKNIFPYaKLYEFY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 321 GMTEIG-MCLSNPLHGDRVSGSVGFPLPGVQVKINAEAsstqnGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAF 399
Cdd:PRK07638 287 GASELSfVTALVDEESERRPNSVGRPFHNVQVRICNEA-----GEEVQKG---EIGTVYVKSPQFFMGYIIGGVLARELN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILvykKGA 479
Cdd:PRK07638 359 ADGWMTVRDVGYED-EEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGS 433
|
490 500 510
....*....|....*....|....*....|..
gi 330846471 480 EpmSYDDFKMWCQQRLAYYKVPKVIQVKEEIP 511
Cdd:PRK07638 434 A--TKQQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
82-424 |
3.75e-35 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 138.50 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 82 GGVAVPLSISHPPHELEYTITNSKSSMVLTNKenysmlaeigrkvGVQVI---EIPEIGNGSPNKEVQHKimPFDInrnA 158
Cdd:cd05927 56 SLVTVPLYDTLGPEAIEYILNHAEISIVFCDA-------------GVKVYsleEFEKLGKKNKVPPPPPK--PEDL---A 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 159 QIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWE----WKKEDHILEFLPLHHVHGLINILTC-------SLWSGAMCEM 227
Cdd:cd05927 118 TICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHIFERVVEALFlyhgakiGFYSGDIRLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 MPkfDSK-----------QVIDRLLESGVTTDLEQPISLFMAVPTIYSKLIKYVEENVKTEKERQD------IEKAF-QR 289
Cdd:cd05927 198 LD--DIKalkptvfpgvpRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDklvfnkIKQALgGN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 290 LRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI--GMCLSNPlhGDRVSGSVGFPLPGVQVKInaeASSTQNGKPVF 367
Cdd:cd05927 276 VRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKL---VDVPEMNYDAK 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 368 KDNTKevGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKdNSTGRFKILGR 424
Cdd:cd05927 351 DPNPR--GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEW-LPNGTLKIIDR 405
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
31-523 |
7.23e-35 |
|
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: 136.65 E-value: 7.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISNQITfkkdDLE---QDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSS 107
Cdd:cd12116 11 RSLSYAELDERANRLAARLR----ARGvgpGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 108 MVLTNKENYSMLAeigrkVGVQVIEIPEIGNGSPNKEVQHKIMPfdiNRNAQIIYTSGTTSRPKGVIATHSNIEAQVKAL 187
Cdd:cd12116 87 LVLTDDALPDRLP-----AGLPVLLLALAAAAAAPAAPRTPVSP---DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 188 VEAWEWKKEDH------------ILE-FLPlhhvhgliniltcsLWSGAMCEMMPKFDSKQVID--RLLEsgvttdlEQP 252
Cdd:cd12116 159 RERLGLGPGDRllavttyafdisLLElLLP--------------LLAGARVVIAPRETQRDPEAlaRLIE-------AHS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 253 ISLFMAVPTIYsKLIKYVEenvktekerqdiEKAFQRLRLMVsGSSALPETVKNDFMEISG--HNLlerYGMTE--IGMC 328
Cdd:cd12116 218 ITVMQATPATW-RMLLDAG------------WQGRAGLTALC-GGEALPPDLAARLLSRVGslWNL---YGPTEttIWST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 329 LSnplhgdRVSGS-----VGFPLPGVQVKINAEAsstqnGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDG- 402
Cdd:cd12116 281 AA------RVTAAagpipIGRPLANTQVYVLDAA-----LRPV---PPGVPGELYIGGDGVAQGYLGRPALTAERFVPDp 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 403 -------WFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGaiLVY 475
Cdd:cd12116 347 fagpgsrLYRTGDLVRRR-ADGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVA--YVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 330846471 476 KKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd12116 423 LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
152-527 |
1.86e-34 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 136.42 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 152 FDINRNAQIIYTSGTTSRPKGVIATH-SNI-EAQVKALVEAWEWKKEDHILEFLPLHHVHGliniltcslWSGAMCE--- 226
Cdd:PRK06018 174 FDENTAAGMCYTSGTTGDPKGVLYSHrSNVlHALMANNGDALGTSAADTMLPVVPLFHANS---------WGIAFSApsm 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 227 ----MMP--KFDSKQVIDRLlesgvttDLEQpISLFMAVPTIYSKLIKYVEENVKTekerqdiekaFQRLRLMVSGSSAL 300
Cdd:PRK06018 245 gtklVMPgaKLDGASVYELL-------DTEK-VTFTAGVPTVWLMLLQYMEKEGLK----------LPHLKMVVCGGSAM 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 301 PETVKNDFMEIsGHNLLERYGMTE---IGMCLSNPLHGDRVSGSV--------GFPLPGVQVKINAEAsstqnGKPVFKD 369
Cdd:PRK06018 307 PRSMIKAFEDM-GVEVRHAWGMTEmspLGTLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDA-----GKELPWD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 370 NtKEVGELLVKGPQVFKEYFekKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDH 449
Cdd:PRK06018 381 G-KTFGRLKVRGPAVAAAYY--RVDGEILDDDGFFDTGDVATID-AYGYMRITDRSK-DVIKSGGEWISSIDLENLAVGH 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 450 PDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLF 527
Cdd:PRK06018 456 PKVAEAAVIGVYHPKWDERPLLIVQLKPGETA-TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2-443 |
3.52e-34 |
|
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: 135.49 E-value: 3.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 2 HRLPSLqLFQNALKYKNRIaiVNYPHNNT--QRFTYNDLLNESAAISNQITFKKDdLEQDRVSFLYPQSFDYVRTQWGIW 79
Cdd:cd05906 10 RTLLEL-LLRAAERGPTKG--ITYIDADGseEFQSYQDLLEDARRLAAGLRQLGL-RPGDSVILQFDDNEDFIPAFWACV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 80 RSGGVAVPLSISHpphelEYTITNSK------------SSMVLTNKENYSMLAEIGRKVGVQVIEIPEIGNGS--PNKEV 145
Cdd:cd05906 86 LAGFVPAPLTVPP-----TYDEPNARlrklrhiwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLdtAADHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 146 QHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLIniltcslwsgaMC 225
Cdd:cd05906 161 LPQSRPDDL---ALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV-----------EL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 226 EMMPkfdskqvidrllesgVTTDLEQ---PISLFMAVPT-------------------IYSKLIKYVEENvktekERQDI 283
Cdd:cd05906 227 HLRA---------------VYLGCQQvhvPTEEILADPLrwldlidryrvtitwapnfAFALLNDLLEEI-----EDGTW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 284 EkaFQRLRLMVSGSSALPETVKNDFMEisghnLLERY-----------GMTEI--GMCLSNPLHGDRVSG-----SVGFP 345
Cdd:cd05906 287 D--LSSLRYLVNAGEAVVAKTIRRLLR-----LLEPYglppdairpafGMTETcsGVIYSRSFPTYDHSQalefvSLGRP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 346 LPGVQVKINAEassTQNGKPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNstGRFKILGR 424
Cdd:cd05906 360 IPGVSMRIVDD---EGQLLPE-----GEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDN--GNLTITGR 429
|
490
....*....|....*....
gi 330846471 425 SSVDIIKNsGYKISALEIE 443
Cdd:cd05906 430 TKDTIIVN-GVNYYSHEIE 447
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
9-523 |
4.73e-34 |
|
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: 134.38 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 9 LFQNALKYKNRIAIVNYPHnntqRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPL 88
Cdd:cd05920 21 LARSAARHPDRIAVVDGDR----RLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 89 SISHPPHELEYTITNSKSSMVLTNKENYSMlaeIGRKVGVQVIE-IPEIgngspnkevqhkimpfdinrnAQIIYTSGTT 167
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIVPDRHAGF---DHRALARELAEsIPEV---------------------ALFLLSGGTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 168 SRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHvhgliNI-LTC-----SLWSGAMCEMMPKFDSKQVIDRLL 241
Cdd:cd05920 152 GTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NFpLACpgvlgTLLAGGRVVLAPDPSPDAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 242 ESGVT-TDLeqpislfmaVPTIYSKLIKYVEenvkteKERQDIekafQRLRLMVSGSSALPETVKNDFMEISGHNLLERY 320
Cdd:cd05920 227 REGVTvTAL---------VPALVSLWLDAAA------SRRADL----SSLRLLQVGGARLSPALARRVPPVLGCTLQQVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 321 GMTEIGMC---LSNPlhGDRVSGSVGFPL-PGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQ 396
Cdd:cd05920 288 GMAEGLLNytrLDDP--DEVIIHTQGRPMsPDDEIRVVDE-----EGNPV---PPGEEGELLTRGPYTIRGYYRAPEHNA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 397 EAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVY 475
Cdd:cd05920 358 RAFtPDGFYRTGDLVRRTPD-GYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 330846471 476 KKgaEPMSYDDFKMWCQQR-LAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd05920 436 RD--PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
8-523 |
5.71e-34 |
|
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: 134.38 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLFQN-ALKYKNRIAIVNyphnNTQRFTYNDLlNESAaisNQI--TFKKDDLEQDR-VSFLYPQSFDYVRTQWGIWRSGG 83
Cdd:cd17655 1 ELFEEqAEKTPDHTAVVF----EDQTLTYREL-NERA---NQLarTLREKGVGPDTiVGIMAERSLEMIVGILGILKAGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 84 VAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRkvgVQVIEIPEIGNGsPNKEVQHKIMPFDInrnAQIIYT 163
Cdd:cd17655 73 AYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFIGL---IDLLDEDTIYHE-ESENLEPVSKSDDL---AYVIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 164 SGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKfDSKQVIDRLLEs 243
Cdd:cd17655 146 SGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFA-SLLSGNTLYIVRK-ETVLDGQALTQ- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 244 gvtTDLEQPISLFMAVPTiYSKLIKYVEenvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHN--LLERYG 321
Cdd:cd17655 223 ---YIRQNRITIIDLTPA-HLKLLDAAD------------DSEGLSLKHLIVGGEALSTELAKKIIELFGTNptITNAYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 322 MTEIGMCLS----NPLHGDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQE 397
Cdd:cd17655 287 PTETTVDASiyqyEPETDQQVSVPIGKPLGNTRIYI-----LDQYGRPQ---PVGVAGELYIGGEGVARGYLNRPELTAE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AFEDGWF-------KTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIG 470
Cdd:cd17655 359 KFVDDPFvpgermyRTGDLA-RWLPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLC 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 330846471 471 AILVYKKGAEPmsyDDFKMWCQQRLAYYKVPK-VIQVkEEIPKNAMLKVNKKDL 523
Cdd:cd17655 437 AYIVSEKELPV---AQLREFLARELPDYMIPSyFIKL-DEIPLTPNGKVDRKAL 486
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
8-523 |
8.57e-34 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 134.58 E-value: 8.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLFQNALKYK---NRIAIVNyPHNNTQrFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGG 83
Cdd:cd17642 19 QLHKAMKRYAsvpGTIAFTD-AHTGVN-YSYAEYLEMSVRLAE--ALKKYGLKQnDRIAVCSENSLQFFLPVIAGLFIGV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 84 VAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVG-VQVIEIPE--------------IGNGSPNKEVQHK 148
Cdd:cd17642 95 GVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKiIKTIIILDskedykgyqclytfITQNLPPGFNEYD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 149 IMPFDINRNAQ---IIYTSGTTSRPKGVIATHSNIEAQVKALVE---AWEWKKEDHILEFLPLHHVHGLINILTcSLWSG 222
Cdd:cd17642 175 FKPPSFDRDEQvalIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIPFHHGFGMFTTLG-YLICG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 223 AMCEMMPKFDSKQVIDRLLESGVTtdleqpiSLFMaVPTIYSKLIKYveenvkTEKERQDIEKafqrLRLMVSGSSALPE 302
Cdd:cd17642 254 FRVVLMYKFEEELFLRSLQDYKVQ-------SALL-VPTLFAFFAKS------TLVDKYDLSN----LHEIASGGAPLSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 303 TVKNDFMEISGHNLLER-YGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKInaeaSSTQNGKPVfkdNTKEVGELLVKG 381
Cdd:cd17642 316 EVGEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKV----VDLDTGKTL---GPNERGELCVKG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 382 PQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGI 460
Cdd:cd17642 389 PMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDED-GHFFIVDRLK-SLIKYKGYQVPPAELESILLQHPKIFDAGVAGI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 461 PNEEYGQVIGAILVYKKGA-----EPMSYDDFKMWCQQRLAyykvPKVIQVkEEIPKNAMLKVNKKDL 523
Cdd:cd17642 467 PDEDAGELPAAVVVLEAGKtmtekEVMDYVASQVSTAKRLR----GGVKFV-DEVPKGLTGKIDRRKI 529
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
59-524 |
3.15e-33 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 132.12 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEytitnskssmvltnkenysMLAEIGRKVGVQVIE-IPEIG 137
Cdd:cd05929 43 DGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC-------------------AIIEIKAAALVCGLFtGGGAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 138 NGSPNKEV----QHKIMPFDINRNAQIIYTSGTTSRPKGVIATHS----NIEAQVKALVEAWeWKKEDHILEFLPLHHVH 209
Cdd:cd05929 104 DGLEDYEAaeggSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPggppDNDTLMAAALGFG-PGADSVYLSPAPLYHAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 210 GLINILTcSLWSGAMCEMMPKFDSKQVIdRLLESGVTTDLEqpislfmAVPTIYSKLIKyVEENVKtekERQDiekaFQR 289
Cdd:cd05929 183 PFRWSMT-ALFMGGTLVLMEKFDPEEFL-RLIERYRVTFAQ-------FVPTMFVRLLK-LPEAVR---NAYD----LSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 290 LRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE-IGMC-------LSNPlhgdrvsGSVGFPLPGVqVKINAEasstq 361
Cdd:cd05929 246 LKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTiingeewLTHP-------GSVGRAVLGK-VHILDE----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 362 NGKPVfkdNTKEVGELLVKGPQVFkEYFEKKEATQEAF-EDGWFKTGDI--VEKDnstgRFKILGRSSVDIIKNSGYKIS 438
Cdd:cd05929 313 DGNEV---PPGEIGEVYFANGPGF-EYTNDPEKTAAARnEGGWSTLGDVgyLDED----GYLYLTDRRSDMIISGGVNIY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 439 ALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSY--DDFKMWCQQRLAYYKVPKVIQVKEEIPKNAML 516
Cdd:cd05929 385 PQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaEELIAFLRDRLSRYKCPRSIEFVAELPRDDTG 464
|
....*...
gi 330846471 517 KVNKKDLV 524
Cdd:cd05929 465 KLYRRLLR 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
151-523 |
4.96e-33 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 134.28 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLinilTCSLWsGAMCEMMP- 229
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGL----TVTLW-LPLLEGIKv 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 230 -----KFDSKQVIDRLLESGVTtdleqpisLFMAVPT---IYSKlikyveeNVKTEKERqdiekaFQRLRLMVSGSSALP 301
Cdd:PRK08633 853 vyhpdPTDALGIAKLVAKHRAT--------ILLGTPTflrLYLR-------NKKLHPLM------FASLRLVVAGAEKLK 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 302 ETVKNDFMEISGHNLLERYGMTEIG--MCLSNP---------LHGDRvSGSVGFPLPGVQVKInaeaSSTQNGKPVfkdN 370
Cdd:PRK08633 912 PEVADAFEEKFGIRILEGYGATETSpvASVNLPdvlaadfkrQTGSK-EGSVGMPLPGVAVRI----VDPETFEEL---P 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 371 TKEVGELLVKGPQVFKEYFEKKEATQEAFED----GWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREI 446
Cdd:PRK08633 984 PGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDED-GFLTITDRYS-RFAKIGGEMVPLGAVEEEL 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 447 LD--HPDIEECAVLGIPNEEYGQVIgaILVYKKGAEPMSYddfkmwCQQRLAYYKVP------KVIQVkEEIPknaMLKV 518
Cdd:PRK08633 1062 AKalGGEEVVFAVTAVPDEKKGEKL--VVLHTCGAEDVEE------LKRAIKESGLPnlwkpsRYFKV-EALP---LLGS 1129
|
....*
gi 330846471 519 NKKDL 523
Cdd:PRK08633 1130 GKLDL 1134
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
160-523 |
1.29e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 131.03 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCeMMPKFDSK---QV 236
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIV-TRRRFDPEatlDL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 237 IDRllesgvttdlEQPISLFMaVPTIYSKLIKYVEENVKTEKERQdiekafqrLRLMVSGSSALPETVKNDFMEISGHNL 316
Cdd:PRK13382 280 IDR----------HRATGLAV-VPVMFDRIMDLPAEVRNRYSGRS--------LRFAAASGSRMRPDVVIAFMDQFGDVI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGM-CLSNPLHGDRVSGSVGFPLPGVQVKI-NAEASSTQNGkpvfkdntkEVGELLVKGPQVFKEYfekKEA 394
Cdd:PRK13382 341 YNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRIlDQDFREVPTG---------EVGTIFVRNDTQFDGY---TSG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 395 TQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILV 474
Cdd:PRK13382 409 STKDFHDGFMASGDVGYLDEN-GRLFVVGRDD-EMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 330846471 475 YKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK13382 487 LKPGASATP-ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
13-520 |
1.99e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 130.70 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 13 ALKYKNRIAIVnYPHNNTqRFTY---NDLLNESAAISNQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLS 89
Cdd:PRK08315 26 AARYPDREALV-YRDQGL-RWTYrefNEEVDALAKGLLALGIEKGD----RVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 90 ISHPPHELEYTITNSKSSMVLTNKE----NY-SMLAEIGRKVGVQ---------------VI--------------EIPE 135
Cdd:PRK08315 100 PAYRLSELEYALNQSGCKALIAADGfkdsDYvAMLYELAPELATCepgqlqsarlpelrrVIflgdekhpgmlnfdELLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 136 IGNGSPN---KEVQHKIMPFD-INrnaqIIYTSGTTSRPKGVIATHSNI--------EAQvkALVEawewkkEDHILEFL 203
Cdd:PRK08315 180 LGRAVDDaelAARQATLDPDDpIN----IQYTSGTTGFPKGATLTHRNIlnngyfigEAM--KLTE------EDRLCIPV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 204 PLHH----VHGLINILTcslwSGA-MCEMMPKFDSKQVidrlLEsgvTTDLEQPISLFmAVPTIYsklIkyveenvkTEK 278
Cdd:PRK08315 248 PLYHcfgmVLGNLACVT----HGAtMVYPGEGFDPLAT----LA---AVEEERCTALY-GVPTMF---I--------AEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 279 ERQDIEKA-FQRLRLMVSGSSALPETVkndfME--ISGHNLLE---RYGMTEI--GMCLSN---PLHgDRVSgSVGFPLP 347
Cdd:PRK08315 305 DHPDFARFdLSSLRTGIMAGSPCPIEV----MKrvIDKMHMSEvtiAYGMTETspVSTQTRtddPLE-KRVT-TVGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 348 GVQVKINAEASstqnGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNStGRFKILGRSS 426
Cdd:PRK08315 379 HLEVKIVDPET----GETVPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEE-GYVNIVGRIK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 427 vDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQV 506
Cdd:PRK08315 451 -DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAT-LTEEDVRDFCRGKIAHYKIPRYIRF 528
|
570
....*....|....
gi 330846471 507 KEEIPKNAMLKVNK 520
Cdd:PRK08315 529 VDEFPMTVTGKIQK 542
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
162-523 |
6.44e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.48 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVI--ATHSNIEA---QVKALVEAWEWKKEDHI-LEFLPLHHVHGLiniltcsLWSGAMCEM------MP 229
Cdd:PRK08276 147 YSSGTTGRPKGIKrpLPGLDPDEapgMMLALLGFGMYGGPDSVyLSPAPLYHTAPL-------RFGMSALALggtvvvME 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 230 KFDSKQVIdRLLESGVTTDLEqpislfmAVPTIYSKLIKYVEEnvktEKERQDIEKafqrLRLMVSGSSALPETVKNDFM 309
Cdd:PRK08276 220 KFDAEEAL-ALIERYRVTHSQ-------LVPTMFVRMLKLPEE----VRARYDVSS----LRVAIHAAAPCPVEVKRAMI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 310 EISGHNLLERYGMTE-IGMCLSNPLHGDRVSGSVGFPLPGVqVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEY 388
Cdd:PRK08276 284 DWWGPIIHEYYASSEgGGVTVITSEDWLAHPGSVGKAVLGE-VRILDE-----DGNEL---PPGEIGTVYFEMDGYPFEY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 389 FEKKEATQEAFED-GWFKTGDI--VEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:PRK08276 355 HNDPEKTAAARNPhGWVTVGDVgyLDED---GYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEM 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 466 GQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK08276 431 GERVKAVVQPADGADAGDalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
152-527 |
4.18e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 126.74 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 152 FDINRNAQIIYTSGTTSRPKGVIATH--SNIEAQVKALVEAWEWKKEDHILEFLPLHHVH--GLIniltcslWSGAM--C 225
Cdd:PRK07008 173 FDENQASSLCYTSGTTGNPKGALYSHrsTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNawGLP-------YSAPLtgA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 226 EMM---PKFDSKQVIDRLLESGVTtdleqpislFMA-VPTIYSKLIKYVEEN-VKtekerqdiekaFQRLRLMVSGSSAL 300
Cdd:PRK07008 246 KLVlpgPDLDGKSLYELIEAERVT---------FSAgVPTVWLGLLNHMREAgLR-----------FSTLRRTVIGGSAC 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 301 PETVKNDFMEISGHNLLERYGMTEIG----MCLSNPLHGDRVSGSV-------GFPLPGVQVKINAEasstqNGKPVFKD 369
Cdd:PRK07008 306 PPAMIRTFEDEYGVEVIHAWGMTEMSplgtLCKLKWKHSQLPLDEQrkllekqGRVIYGVDMKIVGD-----DGRELPWD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 370 NtKEVGELLVKGPQVFKEYFeKKEATqeAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDH 449
Cdd:PRK07008 381 G-KAFGDLQVRGPWVIDRYF-RGDAS--PLVDGWFPTGDVATID-ADGFMQITDRSK-DVIKSGGEWISSIDIENVAVAH 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 450 PDIEECAVLGIPNEEYGQVIGAILVYKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLF 527
Cdd:PRK07008 455 PAVAEAACIACAHPKWDERPLLVVVKRPGAE-VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
160-514 |
8.70e-31 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 122.41 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQvkALVEAW--EWKKEDHILEFLPLHHVhGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQ--ALVLAVlqAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 dRLLESgvttdlEQPISLFMAVPTIYskliKYVEENvktEKERQDIeKAFQRLRLMVSGSSALPETVKNDFMEISGhnll 317
Cdd:cd17636 82 -ELIEA------ERCTHAFLLPPTID----QIVELN---ADGLYDL-SSLRSSPAAPEWNDMATVDTSPWGRKPGG---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 318 erYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEAsstqnGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQE 397
Cdd:cd17636 143 --YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDED-----GREV---PDGEVGEIVARGPTVMAGYWNRPEVNAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AFEDGWFKTGDIvEKDNSTGRFKILGrSSVDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKK 477
Cdd:cd17636 213 RTRGGWHHTNDL-GRREPDGSLSFVG-PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP 290
|
330 340 350
....*....|....*....|....*....|....*..
gi 330846471 478 GAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNA 514
Cdd:cd17636 291 GAS-VTEAELIEHCRARIASYKKPKSVEFADALPRTA 326
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
162-523 |
1.62e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 125.34 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNieAQVKALVEAWEWKKEDHI--LEFLPLHHVHGLiniltCSLWS-GAMCEM---MPKFDSKQ 235
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNALIWGMNEGAvyLWTLPMFHCNGW-----CFTWTlAALCGTnicLRQVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEEnvktekerQDIEKAFQRLRLMVSGSSALPETVKNdfMEISGHN 315
Cdd:PLN02479 275 IYSAIANYGVTH--------FCAAPVVLNTIVNAPKS--------ETILPLPRVVHVMTAGAAPPPSVLFA--MSEKGFR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 316 LLERYGMTEI----GMCLSNPlHGDRVSgsvgfplPGVQVKINA------------EASSTQNGKPVFKDNtKEVGELLV 379
Cdd:PLN02479 337 VTHTYGLSETygpsTVCAWKP-EWDSLP-------PEEQARLNArqgvryigleglDVVDTKTMKPVPADG-KTMGEIVM 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 380 KGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLG 459
Cdd:PLN02479 408 RGNMVMKGYLKNPKANEEAFANGWFHSGDLGVK-HPDGYIEIKDRSK-DIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 460 IPNEEYGQVIGAILVYKKGA----EPMSYDDFKMWCQQRLAYYKVPKVIqVKEEIPKNAMLKVNKKDL 523
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPGVdksdEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
119-491 |
1.63e-30 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 125.98 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 119 LAEIGRKVGVQVIEIPEI---GNGSPNKEVQHKimPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKK 195
Cdd:PLN02736 187 LPSLPSGTGVEIVTYSKLlaqGRSSPQPFRPPK--PEDV---ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYP 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 196 EDHILEFLPLHHVHGLINILTCsLWSGAMCemmpKFDSKQVIdRLLEsgvttDLE--QPiSLFMAVP----TIYSKLIKY 269
Cdd:PLN02736 262 SDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNL-KLMD-----DLAalRP-TIFCSVPrlynRIYDGITNA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 270 VEE---------NVKTEKERQDIEKA-----------FQ--------RLRLMVSGSSALPETVKnDFMEIS-GHNLLERY 320
Cdd:PLN02736 330 VKEsgglkerlfNAAYNAKKQALENGknpspmwdrlvFNkikaklggRVRFMSSGASPLSPDVM-EFLRICfGGRVLEGY 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 321 GMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKIN--AEASSTQNGKPVFKdntkevGELLVKGPQVFKEYFEKKEATQEA 398
Cdd:PLN02736 409 GMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvPEMNYTSEDQPYPR------GEICVRGPIIFKGYYKDEVQTREV 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 399 F-EDGWFKTGDI---VEKdnstGRFKILGRSSvDIIK-NSGYKISALEIEREILDHPDIEECAVlgipneeYGQVIGAIL 473
Cdd:PLN02736 483 IdEDGWLHTGDIglwLPG----GRLKIIDRKK-NIFKlAQGEYIAPEKIENVYAKCKFVAQCFV-------YGDSLNSSL 550
|
410 420
....*....|....*....|....*....
gi 330846471 474 VYKKGAEP-----------MSYDDFKMWC 491
Cdd:PLN02736 551 VAVVVVDPevlkawaasegIKYEDLKQLC 579
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
8-523 |
1.83e-30 |
|
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: 124.24 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLF-QNALKYKNRIAIVNyphnNTQRFTYNDLlNESAaisNQITfkkDDLEQ------DRVSFLYPQSFDYVRTQWGIWR 80
Cdd:cd12117 1 ELFeEQAARTPDAVAVVY----GDRSLTYAEL-NERA---NRLA---RRLRAagvgpgDVVGVLAERSPELVVALLAVLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 81 SGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVgVQVIEIPEIGNGSPNkevqhkiMPFDINRNAQI 160
Cdd:cd12117 70 AGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV-VIDEALDAGPAGNPA-------VPVSPDDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 161 IYTSGTTSRPKGVIATHSNIEAQVK--ALVEAWEwkkEDHILEFLPLHhvhglINILTCSLW----SGAMCEMMPK---F 231
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVKntNYVTLGP---DDRVLQTSPLA-----FDASTFEIWgallNGARLVLAPKgtlL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 DSKQVIDRLLESGVTTdLEQPISLFMAVptiysklikyVEENVKtekerqdiekAFQRLR-LMVSGSSALPETVKNDFME 310
Cdd:cd12117 214 DPDALGALIAEEGVTV-LWLTAALFNQL----------ADEDPE----------CFAGLReLLTGGEVVSPPHVRRVLAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGHNLLERYGMTE---IGMCLSNPlHGDRVSGSV--GFPLPGVQVKInaeasSTQNGKPVFKDntkEVGELLVKGPQVF 385
Cdd:cd12117 273 CPGLRLVNGYGPTEnttFTTSHVVT-ELDEVAGSIpiGRPIANTRVYV-----LDEDGRPVPPG---VPGELYVGGDGLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 386 KEYFEKKEATQE-----AFEDG--WFKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVL 458
Cdd:cd12117 344 LGYLNRPALTAErfvadPFGPGerLYRTGDLA-RWLPDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 459 GIPNEEYGQVIGAILVykkGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd12117 422 VREDAGGDKRLVAYVV---AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
290-529 |
2.44e-30 |
|
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: 124.49 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 290 LRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEiGMC----LSNPLhgDRVSGSVGFPL-PGVQVKINAEasstqNGK 364
Cdd:COG1021 302 LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVnytrLDDPE--EVILTTQGRPIsPDDEVRIVDE-----DGN 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 365 PVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSsVDIIKNSGYKISALEIE 443
Cdd:COG1021 374 PV---PPGEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRT-PDGYLVVEGRA-KDQINRGGEKIAAEEVE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 444 REILDHPDIEECAVLGIPNEEYGQVIGAILVyKKGAEPmSYDDFKMWCQQR-LAYYKVPKVIQVKEEIPKNAMLKVNKKD 522
Cdd:COG1021 449 NLLLAHPAVHDAAVVAMPDEYLGERSCAFVV-PRGEPL-TLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKA 526
|
....*..
gi 330846471 523 LVKLFTQ 529
Cdd:COG1021 527 LRAALAA 533
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
59-523 |
1.43e-29 |
|
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: 120.94 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTnkenysmlaeigrkvgvqvieipeign 138
Cdd:cd17649 38 VRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT--------------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 gspnkevQHKimpfdinRN-AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHH---VHGLINI 214
Cdd:cd17649 91 -------HHP-------RQlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFdgaHEQLLPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 215 LTCslwsGAmCEMM---PKFDSKQVIDRLLESGVTTDLeqpislfmAVPTIYskLIKYVEENVKTEKERQdiekafQRLR 291
Cdd:cd17649 157 LIC----GA-CVVLrpdELWASADELAEMVRELGVTVL--------DLPPAY--LQQLAEEADRTGDGRP------PSLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 292 LMVSGSSAL-PETVKNDFMeiSGHNLLERYGMTE--IGMCLSNPLHGDRVSGS---VGFPLPGVQVKINAEAsstqnGKP 365
Cdd:cd17649 216 LYIFGGEALsPELLRRWLK--APVRLFNAYGPTEatVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDAD-----LNP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 366 VFKDntkEVGELLVKGPQVFKEYFEKKEATQEAF------EDG--WFKTGDIVE-KDNstGRFKILGRssVD-IIKNSGY 435
Cdd:cd17649 289 VPVG---VTGELYIGGEGLARGYLGRPELTAERFvpdpfgAPGsrLYRTGDLARwRDD--GVIEYLGR--VDhQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 436 KISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAM 515
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*...
gi 330846471 516 LKVNKKDL 523
Cdd:cd17649 442 GKLDRKAL 449
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
59-530 |
2.27e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 121.34 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEI--------GRKVGVQV 130
Cdd:PRK13391 50 DHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALlkqcpgvrHRLVLDGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 131 IEIPEIGNGSPNKEVQHKIMPFDINRNAQIIYTSGTTSRPKGVIA--THSNIEAQV---KALVEAWEWKKEDHILEFLPL 205
Cdd:PRK13391 130 GELEGFVGYAEAVAGLPATPIADESLGTDMLYSSGTTGRPKGIKRplPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 206 HHVHGL-INILTCSLwsGAMCEMMPKFDSKQVIDRLLESGVTTDleqpislfMAVPTIYSKLIKYVEEnvktEKERQDIE 284
Cdd:PRK13391 210 YHSAPQrAVMLVIRL--GGTVIVMEHFDAEQYLALIEEYGVTHT--------QLVPTMFSRMLKLPEE----VRDKYDLS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 285 KafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE-IGMCLSNPLHGDRVSGSVGFPLPGVqVKINAEasstqNG 363
Cdd:PRK13391 276 S----LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHILDD-----DG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 364 KPVFKdntKEVGELLVKGPQVFkEYFEKKEATQEAF--EDGWFKTGDI--VEKDnstgRFKILGRSSVDIIKNSGYKISA 439
Cdd:PRK13391 346 AELPP---GEPGTIWFEGGRPF-EYLNDPAKTAEARhpDGTWSTVGDIgyVDED----GYLYLTDRAAFMIISGGVNIYP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 440 LEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMsyDDFKM----WCQQRLAYYKVPKVIQVKEEIPKNAM 515
Cdd:PRK13391 418 QEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPG--PALAAeliaFCRQRLSRQKCPRSIDFEDELPRLPT 495
|
490
....*....|....*
gi 330846471 516 LKVNKKDLVKLFTQN 530
Cdd:PRK13391 496 GKLYKRLLRDRYWGN 510
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
160-526 |
1.02e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 119.65 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINiLTCSLWSGAMCEMMPKFDSKQVIDR 239
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAH-LTLAMALGSTVVLRRRFDPEATLED 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 240 LLESGVTTdleqpislFMAVPTIYSKLIKyVEENVKtekERQDIekafQRLRLMVSGSSALPETVKNDFMEISG---HNL 316
Cdd:PRK07788 291 IAKHKATA--------LVVVPVMLSRILD-LGPEVL---AKYDT----SSLKIIFVSGSALSPELATRALEAFGpvlYNL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 lerYGMTEIGMC-LSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFE---KK 392
Cdd:PRK07788 355 ---YGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKILDE-----NGNEV---PRGVVGRIFVGNGFPFEGYTDgrdKQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 393 EAtqeafeDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:PRK07788 424 II------DGLLSSGDVGYFD-EDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAF 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 330846471 473 LVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:PRK07788 496 VVKAPGAALDE-DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
160-523 |
1.22e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 119.34 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVE---AW-EWKKEDHILEFLPLHHVHGLINILTCsLWSGAMCeMMPKFDSKQ 235
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAVPDILQKeglNWvTWVVGETTYSPLPATHIGGLWWILTC-LMHGGLC-VTGGENTTS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLESGVTTDLeqpislfmAVPTIYSKLIKyveenvktekERQDIEKAFQRLRLMV-SGSSALPETVKndFMEISGH 314
Cdd:PRK05857 252 LLEILTTNAVATTC--------LVPTLLSKLVS----------ELKSANATVPSLRLVGyGGSRAIAADVR--FIEATGV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 315 NLLERYGMTEIG---MCLsnPLHGDRVS----GSVGFPLPGVQVKINAEasstQNGKPVFKD--NTKEVGELLVKGPQVF 385
Cdd:PRK05857 312 RTAQVYGLSETGctaLCL--PTDDGSIVkieaGAVGRPYPGVDVYLAAT----DGIGPTAPGagPSASFGTLWIKSPANM 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 386 KEYFEKKEATQEAFEDGWFKTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLER-REDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 466 GQVIGAILVYKKGAEPMSYDDFKmwcQQRLAYYK-------VPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK05857 464 GALVGLAVVASAELDESAARALK---HTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
59-523 |
2.69e-28 |
|
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: 117.41 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeign 138
Cdd:cd17643 38 DRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTDPDDL---------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 gspnkevqhkimpfdinrnAQIIYTSGTTSRPKGVIATHSNieaqVKALVEAWEWkkedhILEFLP------LHH----- 207
Cdd:cd17643 96 -------------------AYVIYTSGSTGRPKGVVVSHAN----VLALFAATQR-----WFGFNEddvwtlFHSyafdf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 208 ----VHGliniltcSLWSGAMCEMMPKFDSKQVID--RLLESGVTTDLEQpislfmaVPTIYSKLIkyveENVKTEKERQ 281
Cdd:cd17643 148 svweIWG-------ALLHGGRLVVVPYEVARSPEDfaRLLRDEGVTVLNQ-------TPSAFYQLV----EAADRDGRDP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 282 DiekafqRLRLMVSGSSALPETVKNDFMEISGHN---LLERYGMTEIGMCLS-NPLHGDRVSGS----VGFPLPGVQVKI 353
Cdd:cd17643 210 L------ALRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 354 naeasSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWF--------KTGDIVeKDNSTGRFKILGRS 425
Cdd:cd17643 284 -----LDADGRPV---PPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmyRTGDLA-RRLPDGELEYLGRA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 426 SvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQ 505
Cdd:cd17643 355 D-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADI-AELRALLKELLPDYMVPARYV 432
|
490
....*....|....*...
gi 330846471 506 VKEEIPKNAMLKVNKKDL 523
Cdd:cd17643 433 PLDALPLTVNGKLDRAAL 450
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
160-525 |
2.89e-28 |
|
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: 118.34 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKgvIATHSNIEAQVKALVEAWEWK--KEDHILEFLPlhhVHGLINILTCSL---WSGAMC---EMMPKF 231
Cdd:cd05928 179 IYFTSGTTGSPK--MAEHSHSSLGLGLKVNGRYWLdlTASDIMWNTS---DTGWIKSAWSSLfepWIQGACvfvHHLPRF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 DSKQVIDRLLEsgvttdleQPISLFMAVPTIYSKLikyVEENVKTEKerqdiekaFQRLRLMVSGSSALPETVKNDFMEI 311
Cdd:cd05928 254 DPLVILKTLSS--------YPITTFCGAPTVYRML---VQQDLSSYK--------FPSLQHCVTGGEPLNPEVLEKWKAQ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 312 SGHNLLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDNTKEVGeLLVKgPQ----VFKE 387
Cdd:cd05928 315 TGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-----NGNVLPPGTEGDIG-IRVK-PIrpfgLFSG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 388 YFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQ 467
Cdd:cd05928 388 YVDNPEKTAATIRGDFYLTGDRGIMD-EDGYFWFMGRAD-DVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGE 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 468 VIGAILVYkkGAEPMSYDDFKMW--CQQRL----AYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:cd05928 466 VVKAFVVL--APQFLSHDPEQLTkeLQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
145-523 |
6.12e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 117.81 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 145 VQHKIMPFDINrnaqiiYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSG-A 223
Cdd:PLN03102 182 IQDEHDPISLN------YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGtS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 224 MCemMPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIkyveenvktEKERQDIEKAFQRLRLMVSGSSALPET 303
Cdd:PLN03102 256 VC--MRHVTAPEIYKNIEMHNVTH--------MCCVPTVFNILL---------KGNSLDLSPRSGPVHVLTGGSPPPAAL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 304 VKNdfMEISGHNLLERYGMTE-IGMCL-------------SNPLHGDRVSGSVGFPLPGVQVKinaeasSTQNGKPVFKD 369
Cdd:PLN03102 317 VKK--VQRLGFQVMHAYGLTEaTGPVLfcewqdewnrlpeNQQMELKARQGVSILGLADVDVK------NKETQESVPRD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 370 NtKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDI--VEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREIL 447
Cdd:PLN03102 389 G-KTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVgvIHPD---GHVEIKDRSK-DIIISGGENISSVEVENVLY 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 448 DHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKM---------WCQQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:PLN03102 464 KYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLvtrerdlieYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
|
....*
gi 330846471 519 NKKDL 523
Cdd:PLN03102 544 LKPKL 548
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
8-526 |
1.16e-27 |
|
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: 118.04 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLF-QNALKYKNRIAIVnypHNNtQRFTYNDLLNESAAISNQItfkkddLEQ-----DRVSFLYPQSFDYVRTQWGIWRS 81
Cdd:COG1020 480 ELFeAQAARTPDAVAVV---FGD-QSLTYAELNARANRLAHHL------RALgvgpgDLVGVCLERSLEMVVALLAVLKA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 82 GGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGrkvgVQVIEIPEIG-NGSPNKEVQHKIMPFDInrnAQI 160
Cdd:COG1020 550 GAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELG----VPVLALDALAlAAEPATNPPVPVTPDDL---AYV 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 161 IYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHH---VHGLIniltCSLWSGAMCEMMPKFDSK--Q 235
Cdd:COG1020 623 IYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEIF----GALLSGATLVLAPPEARRdpA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLEsgvttdlEQPISLFMAVPTIYSKLIKYVEEnvktekerqdiekAFQRLRLMVSGSSALPETVKNDFMEISG-- 313
Cdd:COG1020 699 ALAELLA-------RHRVTVLNLTPSLLRALLDAAPE-------------ALPSLRLVLVGGEALPPELVRRWRARLPga 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 314 --HNLlerYGMTE--IGMCLSNPLHGDRVSGSV--GFPLPGVQVKI-NAeasstqNGKP----VfkdntkeVGELLVKGP 382
Cdd:COG1020 759 rlVNL---YGPTEttVDSTYYEVTPPDADGGSVpiGRPIANTRVYVlDA------HLQPvpvgV-------PGELYIGGA 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 383 QVFKEYFEKKEATQEAF------EDG--WFKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEE 454
Cdd:COG1020 823 GLARGYLNRPELTAERFvadpfgFPGarLYRTGDLA-RWLPDGNLEFLGRAD-DQVKIRGFRIELGEIEAALLQHPGVRE 900
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330846471 455 CAVLGIPNEEYGQVIGAILVYKKGAEPmsyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNamLKVNKKDLVKL 526
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAA---AAALLRLALALLLPPYMVPAAVVLLLPLP--LTGNGKLDRLA 967
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
81-525 |
3.92e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 114.78 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 81 SGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIPE--------IGNGSPNKEVQhkimPF 152
Cdd:PRK07867 77 SGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAwadelaahRDAEPPFRVAD----PD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 153 DInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFD 232
Cdd:PRK07867 153 DL---FMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 233 SKQVIDRLLESGVT--TDLEQPISLFMAVPtiysklikyveenvktekERQDieKAFQRLRLMVsGSSALPETVkNDFME 310
Cdd:PRK07867 230 ASGFLPDVRRYGATyaNYVGKPLSYVLATP------------------ERPD--DADNPLRIVY-GNEGAPGDI-ARFAR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGHNLLERYGMTEIGMCLS-NPlhgDRVSGSVGFPLPGVQVkINAEaSSTQNGKPVFKDN-----TKEVGELL-VKGPQ 383
Cdd:PRK07867 288 RFGCVVVDGFGSTEGGVAITrTP---DTPPGALGPLPPGVAI-VDPD-TGTECPPAEDADGrllnaDEAIGELVnTAGPG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 384 VFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNE 463
Cdd:PRK07867 363 GFEGYYNDPEADAERMRGGVYWSGDLAYRD-ADGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 464 EYGQVIGAILVYKKGAE--PMSYDDFkMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK07867 441 VVGDQVMAALVLAPGAKfdPDAFAEF-LAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
138-530 |
9.76e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 112.78 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 138 NGSPNKEVQHKIMpfdinrnaqiIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEdHILEFLPLHHVHGLINILTc 217
Cdd:PRK07445 113 QGILPNLETGWIM----------IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQV-NSFCVLPLYHVSGLMQFMR- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 218 SLWSGAMCEMMPKfdskqvidRLLESGVTTDLEQP---ISLfmaVPTiysKLIKYVEENVKTEKERQDIekafqrlrlMV 294
Cdd:PRK07445 181 SFLTGGKLVILPY--------KRLKSGQELPPNPSdffLSL---VPT---QLQRLLQLRPQWLAQFRTI---------LL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 295 SGSSALPEtvkndfmeisghnLLER-----------YGMTEIG--MCLSNP---LHGDRvsgSVGFPLPGVQVKINAEAs 358
Cdd:PRK07445 238 GGAPAWPS-------------LLEQarqlqlrlaptYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIPANQ- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 359 stqngkpvfkdntkeVGELLVKGPQVFKEYFEKKEATQEAFEdgwfkTGDIVEKDNStGRFKILGRSSVDIIkNSGYKIS 438
Cdd:PRK07445 301 ---------------TGNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQ-GYLHILGRNSQKII-TGGENVY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 439 ALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKkgAEPMSYDDFKMWCQQRLAYYKVPKV-IQVkEEIPKNAMLK 517
Cdd:PRK07445 359 PAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPK--DPSISLEELKTAIKDQLSPFKQPKHwIPV-PQLPRNPQGK 435
|
410
....*....|...
gi 330846471 518 VNKKDLVKLFTQN 530
Cdd:PRK07445 436 INRQQLQQIAVQR 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-525 |
3.07e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.10 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 7 LQLFQNALK-YKNRIAIVNyphnNTQRFTYNDLlNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVA 85
Cdd:PRK12467 515 HQLIEAQARqHPERPALVF----GEQVLSYAEL-NRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAY 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 86 VPLSISHPPHELEYTITNSKSSMVLTNKEnysMLAEIGRKVGVQVIEIPEIGNGSPNKEVQHKIMPFDINRNAQIIYTSG 165
Cdd:PRK12467 590 VPLDPEYPQDRLAYMLDDSGVRLLLTQSH---LLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSG 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPK---FDSKQVIDRLLE 242
Cdd:PRK12467 667 STGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFG-ALASGATLHLLPPdcaRDAEAFAALMAD 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 243 SGVTTdLEQPISLFMAVptiysklikyveenvkTEKERQDIEKafqRLRLMVSGSSALPETVKNDFMEIS-GHNLLERYG 321
Cdd:PRK12467 746 QGVTV-LKIVPSHLQAL----------------LQASRVALPR---PQRALVCGGEALQVDLLARVRALGpGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 322 MTEIGMCLSN-PLHGD-RVSGSV--GFPLPGVQVKInaeASSTQNGKPVfkdntKEVGELLVKGPQVFKEYFEKKEATQE 397
Cdd:PRK12467 806 PTETTVGVSTyELSDEeRDFGNVpiGQPLANLGLYI---LDHYLNPVPV-----GVVGELYIGGAGLARGYHRRPALTAE 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AF------EDG--WFKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVI 469
Cdd:PRK12467 878 RFvpdpfgADGgrLYRTGDLA-RYRADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV 955
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 470 gAILVYKKGAEPMSY----DDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK12467 956 -AYLVPAAVADGAEHqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
23-480 |
4.97e-26 |
|
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: 111.56 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 23 VNYPHNNTQRFTYNDLLNESAAISNQITfkKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYT-- 100
Cdd:cd05931 15 LDDEGGREETLTYAELDRRARAIAARLQ--AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 101 -ITNSKSSMVLTNKENYSMLAEIGRKVGV----QVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIA 175
Cdd:cd05931 93 iLADAGPRVVLTTAAALAAVRAFAASRPAagtpRLLVVDLLPDTSAADWPPPSPDPDDI---AYLQYTSGSTGTPKGVVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 176 THSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMP--KFDSKQV--IDRLLESGVTtdleq 251
Cdd:cd05931 170 THRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaAFLRRPLrwLRLISRYRAT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 252 pislFMAVPTI-YSKLIKYVeenvkTEKERQDIEkaFQRLRLMVSGSSAL-PETVKNDFMEISGHNLLER-----YGMTE 324
Cdd:cd05931 245 ----ISAAPNFaYDLCVRRV-----RDEDLEGLD--LSSWRVALNGAEPVrPATLRRFAEAFAPFGFRPEafrpsYGLAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 325 IGMCLSNP---------------LHGDRVSG-----------SVGFPLPGVQVKI-NAEasstqnGKPVFKDNtkEVGEL 377
Cdd:cd05931 314 ATLFVSGGppgtgpvvlrvdrdaLAGRAVAVaaddpaarelvSCGRPLPDQEVRIvDPE------TGRELPDG--EVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQVFKEYFEKKEATQEAF-------EDGWFKTGD---IVEkdnstGRFKILGRSSvDIIKNSGYKISALEIEREIL 447
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDlgfLHD-----GELYITGRLK-DLIIVRGRNHYPQDIEATAE 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 330846471 448 DHPD---IEECAVLGIPNEEYGQVIGAILVYKKGAE 480
Cdd:cd05931 460 EAHPalrPGCVAAFSVPDDGEERLVVVAEVERGADP 495
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
158-411 |
7.35e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 111.51 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDH--ILEFLPLHHVHGLINILTCSLWSGA---MCEMMP--- 229
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGGNHNLGIVLYNGGtlyIDDGKPtpg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 230 KFDskQVIDRLLESgvttdleQPISLFMaVPTIYSKLIKYVEenvkteKERQDIEKAFQRLRLMVSGSSALPETVKNDFM 309
Cdd:PRK08180 292 GFD--ETLRNLREI-------SPTVYFN-VPKGWEMLVPALE------RDAALRRRFFSRLKLLFYAGAALSQDVWDRLD 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 310 EISGHNLLER------YGMTEIG-MCLSnpLHGDRV-SGSVGFPLPGVQVKInaeasSTQNGKPvfkdntkevgELLVKG 381
Cdd:PRK08180 356 RVAEATCGERirmmtgLGMTETApSATF--TTGPLSrAGNIGLPAPGCEVKL-----VPVGGKL----------EVRVKG 418
|
250 260 270
....*....|....*....|....*....|.
gi 330846471 382 PQVFKEYFEKKEATQEAF-EDGWFKTGDIVE 411
Cdd:PRK08180 419 PNVTPGYWRAPELTAEAFdEEGYYRSGDAVR 449
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
151-424 |
7.44e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 111.99 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKAL----VEAWEWKKEDHI-LEFLPLHHV--HGLINILtcsLWSGA 223
Cdd:PTZ00216 260 PENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALedrlNDLIGPPEEDETyCSYLPLAHImeFGVTNIF---LARGA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 224 M-CEMMPkfdskqvidRLLESgvTT-----DLEQ--PiSLFMAVPTIYSKLIKYVEEN---VKTEKeRQDIEKAFQ---- 288
Cdd:PTZ00216 337 LiGFGSP---------RTLTD--TFarphgDLTEfrP-VFLIGVPRIFDTIKKAVEAKlppVGSLK-RRVFDHAYQsrlr 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 289 -------------------------RLRLMVSGSSAL-PETvkNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRVSGSV 342
Cdd:PTZ00216 404 alkegkdtpywnekvfsapravlggRVRAMLSGGGPLsAAT--QEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 343 GFPLPGVQVKI--NAEASSTQNGKPVfkdntkevGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRF 419
Cdd:PTZ00216 482 GQLLKGVEMKLldTEEYKHTDTPEPR--------GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIA-ANGTL 552
|
....*
gi 330846471 420 KILGR 424
Cdd:PTZ00216 553 RIIGR 557
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
160-523 |
8.99e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 110.86 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVI---ATHSNIEAQVkALVEAWEWKKEDHILEFLPLHHVHGL-INILTCSLwsGAMCEMMPKFDSKQ 235
Cdd:PRK13383 179 VLLTSGTTGKPKGVPrapQLRSAVGVWV-TILDRTRLRTGSRISVAMPMFHGLGLgMLMLTIAL--GGTVLTHRHFDAEA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRllesgvtTDLEQPISlFMAVPTIYSKLIKYveenvkteKERQDIEKAFQRLRLMVSGSSALPETVKNDFMEISGHN 315
Cdd:PRK13383 256 ALAQ-------ASLHRADA-FTAVPVVLARILEL--------PPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 316 LLERYGMTEIGM-CLSNPLHGDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQVFKEYfekKEA 394
Cdd:PRK13383 320 LYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRI-----LDRNNRPV---GPRVTGRIFVGGELAGTRY---TDG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 395 TQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILV 474
Cdd:PRK13383 389 GGKAVVDGMTSTGDMGYLDNA-GRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVV 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 330846471 475 YKKGAEpMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK13383 467 LHPGSG-VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
8-523 |
1.20e-25 |
|
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: 109.57 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLF-QNALKYKNRIAIVNyphnNTQRFTYNDLlNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAV 86
Cdd:cd17645 2 QLFeEQVERTPDHVAVVD----RGQSLTYKQL-NEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 87 PLSISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSGT 166
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILLTNPDDL-----------------------------------------AYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 167 TSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMP---KFDSKQVIDRLLES 243
Cdd:cd17645 116 TGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFP-HLTAGAALHVVPserRLDLDALNDYFNQE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 244 GVTtdleqpislfmavptiysklIKYVeenvKTEKERQDIEKAFQRLRLMVSGSSALPETVKNdfmeisGHNLLERYGMT 323
Cdd:cd17645 195 GIT--------------------ISFL----PTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK------GYKLVNNYGPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 324 EIG-MCLSNPLHGDRVSGSVGFPLPGVQVKINAEASSTQngkPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAF--- 399
Cdd:cd17645 245 ENTvVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ---PI-----GVAGELCIAGEGLARGYLNRPELTAEKFivh 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 ----EDGWFKTGDIVEKDNStGRFKILGRssVD-IIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILV 474
Cdd:cd17645 317 pfvpGERMYRTGDLAKFLPD-GNIEFLGR--LDqQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 330846471 475 YKKGAEPmsyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17645 394 APEEIPH---EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
31-523 |
1.75e-25 |
|
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: 109.67 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISNQITFKKDDLEqDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL 110
Cdd:cd17646 22 RTLTYRELDERANRLAHLLRARGVGPE-DRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 TNKENYSMLAEIGRKVGVQVIEIPEIGNGSPNKEVQhkimPFDInrnAQIIYTSGTTSRPKGVIATHsnieaqvKALVEA 190
Cdd:cd17646 101 TTADLAARLPAGGDVALLGDEALAAPPATPPLVPPR----PDNL---AYVIYTSGSTGRPKGVMVTH-------AGIVNR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 191 WEWKKEDHILE--------------------FLPLHhvhgliniltcslwSGAmCEMMPKFDSKQVIDRLL----ESGVT 246
Cdd:cd17646 167 LLWMQDEYPLGpgdrvlqktplsfdvsvwelFWPLV--------------AGA-RLVVARPGGHRDPAYLAalirEHGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 247 TdleqpiSLFmaVPtiySKLIKYVEEnvktekerQDIEKAfQRLRLMVSGSSALPETVKNDFMEISG---HNLlerYGMT 323
Cdd:cd17646 232 T------CHF--VP---SMLRVFLAE--------PAAGSC-ASLRRVFCSGEALPPELAARFLALPGaelHNL---YGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 324 E--IGMcLSNPLHGDRVSGSV--GFPLPGVQVKINAEAsstqnGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF 399
Cdd:cd17646 289 EaaIDV-THWPVRGPAETPSVpiGRPVPNTRLYVLDDA-----LRPV---PVGVPGELYLGGVQLARGYLGRPALTAERF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 EDGWF-------KTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:cd17646 360 VPDPFgpgsrmyRTGDLARW-RPDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGY 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 330846471 473 LVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17646 438 VVPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
162-523 |
5.29e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 107.65 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNIEA--------------QVKALVEAWEWKKEDHILEFLPlhhvhgliniltcslWSGAMCEM 227
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSYPVghlstmywiglkpgDVHWNISSPGWAKHAWSCFFAP---------------WNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 M---PKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKyveenvktekerQDIEKAFQRLRLMVSGSSALPETV 304
Cdd:cd05974 157 LfnyARFDAKRVLAALVRYGVTT--------LCAPPTVWRMLIQ------------QDLASFDVKLREVVGAGEPLNPEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 305 KNDFMEISGHNLLERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKI-NAEASSTQNGKPVFK-DNTKEVGelLVKGp 382
Cdd:cd05974 217 IEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALlDPDGAPATEGEVALDlGDTRPVG--LMKG- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 383 qvfkeYFEKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPN 462
Cdd:cd05974 294 -----YAGDPDKTAHAMRGGYYRTGDIAMRDED-GYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPD 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 463 EEYGQVIGAILVYKKGAEP---MSYDDFKmWCQQRLAYYKVPKVIQVKeEIPKNAMLKVNKKDL 523
Cdd:cd05974 367 PVRLSVPKAFIVLRAGYEPspeTALEIFR-FSRERLAPYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
158-459 |
7.04e-25 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 108.28 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGA-------------- 223
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFivnfpeepetmmed 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 224 MCEMMPKF----------DSKQVIDRLLESGvttdleqPISLFM----------AVPTIYSKLIKYVEENVKTEKERQDI 283
Cdd:cd17641 241 LREIGPTFvllpprvwegIAADVRARMMDAT-------PFKRFMfelgmklglrALDRGKRGRPVSLWLRLASWLADALL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 284 EKA------FQRLRLMVSGSSAL-PETVknDFMEISGHNLLERYGMTEigMCLSNPLH--GDRVSGSVGFPLPGVQVKIN 354
Cdd:cd17641 314 FRPlrdrlgFSRLRSAATGGAALgPDTF--RFFHAIGVPLKQLYGQTE--LAGAYTVHrdGDVDPDTVGVPFPGTEVRID 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 355 aeasstqngkpvfkdntkEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDiVEKDNSTGRFKILGRSSvDIIKNS 433
Cdd:cd17641 390 ------------------EVGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGD-AGYFKENGHLVVIDRAK-DVGTTS 449
|
330 340
....*....|....*....|....*..
gi 330846471 434 -GYKISALEIEREILDHPDIEECAVLG 459
Cdd:cd17641 450 dGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
153-511 |
3.38e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.98 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 153 DINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFD 232
Cdd:PRK06164 179 DPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 233 SKQVIDRLLESGVTTDLeqpislfmAVPTIYSKLIKyveenvkTEKERQDiekaFQRLRLM-----VSGSSALPETVKND 307
Cdd:PRK06164 258 AARTARALRRHRVTHTF--------GNDEMLRRILD-------TAGERAD----FPSARLFgfasfAPALGELAALARAR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 308 FMEISGhnlleRYGMTE-IGMCLSNPLHGD---RVSGSvGFPL-PGVQVKInaeaSSTQNGKpVFKDNtkEVGELLVKGP 382
Cdd:PRK06164 319 GVPLTG-----LYGSSEvQALVALQPATDPvsvRIEGG-GRPAsPEARVRA----RDPQDGA-LLPDG--ESGEIEIRAP 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 383 QVFKEYFEKKEATQEAF-EDGWFKTGDIvEKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIP 461
Cdd:PRK06164 386 SLMRGYLDNPDATARALtDDGYFRTGDL-GYTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 330846471 462 NEEYGQVIgAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIP 511
Cdd:PRK06164 464 RDGKTVPV-AFVIPTDGASP-DEAGLMAACREALAGFKVPARVQVVEAFP 511
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
17-512 |
5.40e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 105.75 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 17 KNRIAIVNYPHNNTQRFTYNDLLNESAAISNqiTFKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPH 95
Cdd:PRK04319 58 KDKVALRYLDASRKEKYTYKELKELSNKFAN--VLKELGVEKgDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 96 ELEYTITNSKSSMVLTNKENYsmlaeigRKVGVQ-------VIEIPEIGNGSPNKEVQHKIM-----PFDI---NRNAQI 160
Cdd:PRK04319 136 AVRDRLEDSEAKVLITTPALL-------ERKPADdlpslkhVLLVGEDVEEGPGTLDFNALMeqasdEFDIewtDREDGA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 161 I--YTSGTTSRPKGVIATHsnieaqvKALVEAW---EWK---KEDHILE---------------FLPLhhVHGLINILtc 217
Cdd:PRK04319 209 IlhYTSGSTGKPKGVLHVH-------NAMLQHYqtgKYVldlHEDDVYWctadpgwvtgtsygiFAPW--LNGATNVI-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 218 slwSGAmcemmpKFDSKQVIdRLLEsgvttdlEQPISLFMAVPTIYSKLIKYVEENVKtekeRQDiekaFQRLRLMVSGS 297
Cdd:PRK04319 278 ---DGG------RFSPERWY-RILE-------DYKVTVWYTAPTAIRMLMGAGDDLVK----KYD----LSSLRHILSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 298 SAL-PETVKNDfMEISGHNLLERYGMTEIG-MCLSNPLHGDRVSGSVGFPLPGVQVKInaeASSTQNGKPVFkdntkEVG 375
Cdd:PRK04319 333 EPLnPEVVRWG-MKVFGLPIHDNWWMTETGgIMIANYPAMDIKPGSMGKPLPGIEAAI---VDDQGNELPPN-----RMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 EL-LVKG-PQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIE 453
Cdd:PRK04319 404 NLaIKKGwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMD-EDGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330846471 454 ECAVLGIPNEEYGQVIGAILVYKKGAEPMsyDDFKM----WCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:PRK04319 482 EAGVIGKPDPVRGEIIKAFVALRPGYEPS--EELKEeirgFVKKGLGAHAAPREIEFKDKLPK 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-525 |
1.36e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.81 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 60 RVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKenySMLAEIGRKVGVQVIEIPEIGN- 138
Cdd:PRK12316 2055 RVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR---HLLERLPLPAGVARLPLDRDAEw 2131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 -GSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLhHVHGLINILTC 217
Cdd:PRK12316 2132 aDYPDTAPAVQLAGENL---AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFH 2207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 218 SLWSGAMCEMMPK--FDSKQVIDRLLESGVTTdleqpislfMAVPTIYSKLIKYVEEnvktekerqdIEKAFQRLRLMVS 295
Cdd:PRK12316 2208 PLLNGARVLIRDDelWDPEQLYDEMERHGVTI---------LDFPPVYLQQLAEHAE----------RDGRPPAVRVYCF 2268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 296 GSSALP-ETVKNDFMEISGHNLLERYGMTEIGMclsNPLH--GDRVSGSVGFPLPGVQVKINAEASSTQNG-KPVfkdNT 371
Cdd:PRK12316 2269 GGEAVPaASLRLAWEALRPVYLFNGYGPTEAVV---TPLLwkCRPQDPCGAAYVPIGRALGNRRAYILDADlNLL---AP 2342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 372 KEVGELLVKGPQVFKEYFEKKEATQEAFEDGWF--------KTGDIVeKDNSTGRFKILGRssVD-IIKNSGYKISALEI 442
Cdd:PRK12316 2343 GMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlyRTGDLA-RYRADGVVEYLGR--IDhQVKIRGFRIELGEI 2419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 443 EREILDHPDIEECAVLGIPNEEyGQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKD 522
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLL-AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKA 2497
|
...
gi 330846471 523 LVK 525
Cdd:PRK12316 2498 LPK 2500
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-514 |
1.63e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 103.81 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 58 QDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEI-GRKVGVQVIeiPEI 136
Cdd:PRK07798 53 GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVlPRLPKLRTL--VVV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 137 GNGSPNkEVQHKIMPFD------------INRNAQ---IIYTSGTTSRPKGVIATHSNI-EAQ-----------VKALVE 189
Cdd:PRK07798 131 EDGSGN-DLLPGAVDYEdalaagsperdfGERSPDdlyLLYTGGTTGMPKGVMWRQEDIfRVLlggrdfatgepIEDEEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 190 AWEWKKEDHILEFL---PLHHVHGLINILTcSLWSGAMCEMMP--KFDSkqviDRLLEsgvTTDLEQPISLF-----MAV 259
Cdd:PRK07798 210 LAKRAAAGPGMRRFpapPLMHGAGQWAAFA-ALFSGQTVVLLPdvRFDA----DEVWR---TIEREKVNVITivgdaMAR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 260 PtiyskLIKYVEEnvkteKERQDIEkafqRLRLMVSGSSALPETVKNDFMEISGH-NLLERYGMTEIGMCLSnpLHGDRV 338
Cdd:PRK07798 282 P-----LLDALEA-----RGPYDLS----SLFAIASGGALFSPSVKEALLELLPNvVLTDSIGSSETGFGGS--GTVAKG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 339 SGSVGFPlpgvqvKINAEASSTqngkpVFKDNTKEV--GE----LLVKGPQVFKEYFEKKEATQEAFE--DG--WFKTGD 408
Cdd:PRK07798 346 AVHTGGP------RFTIGPRTV-----VLDEDGNPVepGSgeigWIARRGHIPLGYYKDPEKTAETFPtiDGvrYAIPGD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 409 I--VEKDnstGRFKILGRSSVDIikNS-GYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmSYD 485
Cdd:PRK07798 415 RarVEAD---GTITLLGRGSVCI--NTgGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARP-DLA 488
|
490 500
....*....|....*....|....*....
gi 330846471 486 DFKMWCQQRLAYYKVPKVIQVKEEIPKNA 514
Cdd:PRK07798 489 ELRAHCRSSLAGYKVPRAIWFVDEVQRSP 517
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
158-529 |
2.29e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 101.66 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKA----LVEAWEWkkedhiLEFLPLHHVHGLiNILTCSLWSGA--MCEMMPK- 230
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADAthdrLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSepVELDVSAg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 231 FDSKQV---IDRLLESGVTTDLeqpislfmaVPTiysKLIKYVEENVKTEkerqdiekAFQRLRLMVSGSSALPETVKnD 307
Cdd:PRK07824 111 FDPTALpraVAELGGGRRYTSL---------VPM---QLAKALDDPAATA--------ALAELDAVLVGGGPAPAPVL-D 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 308 FMEISGHNLLERYGMTEI-GMCLSNplhgdrvsgsvGFPLPGVQVKInaeasstqngkpvfkdntkEVGELLVKGPQVFK 386
Cdd:PRK07824 170 AAAAAGINVVRTYGMSETsGGCVYD-----------GVPLDGVRVRV-------------------EDGRIALGGPTLAK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 387 EYfeKKEATQEAF-EDGWFKTGDIVEKDNstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:PRK07824 220 GY--RNPVDPDPFaEPGWFRTDDLGALDD--GVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRL 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 466 GQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLFTQ 529
Cdd:PRK07824 295 GQRVVAAVVGDGGPAP-TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
18-523 |
3.19e-23 |
|
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: 102.16 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNyphnNTQRFTYNdLLNESAaisNQITFKKDDLEQDR---VSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPP 94
Cdd:cd17650 2 DAIAVSD----ATRQLTYR-ELNERA---NQLARTLRGLGVAPgsvVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 95 HELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSGTTSRPKGVI 174
Cdd:cd17650 74 ERLQYMLEDSGAKLLLTQPEDL-----------------------------------------AYVIYTSGTTGKPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 175 ATHSNIEAQVKAlveaweWKKEDHiLEFLPLHHVHglINILTCSLWSGAMCEMMpKFDSKQVI---DRLLESGVTTDL-- 249
Cdd:cd17650 113 VEHRNVAHAAHA------WRREYE-LDSFPVRLLQ--MASFSFDVFAGDFARSL-LNGGTLVIcpdEVKLDPAALYDLil 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 250 EQPISLFMAVPTIYSKLIKYVEENvktekerqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGHN--LLERYGMTEIGM 327
Cdd:cd17650 183 KSRITLMESTPALIRPVMAYVYRN----------GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 328 CLSN-PLHGDRVSGS----VGFPLPGVQVKInaeASSTQNGKPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAFEDG 402
Cdd:cd17650 253 DSTYyEEGRDPLGDSanvpIGRPLPNTAMYV---LDERLQPQPV-----GVAGELYIGGAGVARGYLNRPELTAERFVEN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 403 WF-------KTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEEcAVLGIPNEEYGQviGAILVY 475
Cdd:cd17650 325 PFapgermyRTGDLA-RWRADGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGE--ARLCAY 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 330846471 476 KKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17650 400 VVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
77-443 |
6.77e-23 |
|
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: 102.44 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 77 GIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTnkENYSMLAEIGR--------KVGVQV--------------IEIP 134
Cdd:cd05933 52 GAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV--ENQKQLQKILQiqdklphlKAIIQYkeplkekepnlyswDEFM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 135 EIGNGSPNKEVQHKIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWK----KEDHILEFLPLHHVHG 210
Cdd:cd05933 130 ELGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpatvGQESVVSYLPLSHIAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 211 -LINILTCSLWSGAMCemmpkFDSKqviDRLLESGVTTDLEQPISLFMAVPTIYSKL---IKYV---------------- 270
Cdd:cd05933 210 qILDIWLPIKVGGQVY-----FAQP---DALKGTLVKTLREVRPTAFMGVPRVWEKIqekMKAVgaksgtlkrkiaswak 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 271 ----EENVKT-------------------EKERQDIekAFQRLRLMVSGSSALPETVKNDFMEISgHNLLERYGMTEIGM 327
Cdd:cd05933 282 gvglETNLKLmggespsplfyrlakklvfKKVRKAL--GLDRCQKFFTGAAPISRETLEFFLSLN-IPIMELYGMSETSG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 328 C--LSNPlhGDRVSGSVGFPLPGVQVKInaeasstqngkpvFKDNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWF 404
Cdd:cd05933 359 PhtISNP--QAYRLLSCGKALPGCKTKI-------------HNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIdEDGWL 423
|
410 420 430
....*....|....*....|....*....|....*....
gi 330846471 405 KTGDIVEKDNStGRFKILGRSSVDIIKNSGYKISALEIE 443
Cdd:cd05933 424 HSGDLGKLDED-GFLYITGRIKELIITAGGENVPPVPIE 461
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-512 |
6.79e-23 |
|
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: 100.15 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNI---EAQVKALVEAWEWKKEDHILEFL-----------PLHHVHGLINILTCSLWSGAMC 225
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDAHKAAAaaagtvmfpapPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 226 EMMPKFDSKQVIdRLLEsgvttdlEQPISLFMAVPTIYSK-LIKYVEENVKTekerqDIEKafqrLRLMVSGSSALPETV 304
Cdd:cd05924 88 LPDDRFDPEEVW-RTIE-------KHKVTSMTIVGDAMARpLIDALRDAGPY-----DLSS----LFAISSGGALLSPEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 305 KNDFMEISGH-NLLERYGMTEIGMCLSN-PLHGDRVSGSVGFPLPGVQVkinaeasSTQNGKPVFKDnTKEVGELLVKGp 382
Cdd:cd05924 151 KQGLLELVPNiTLVDAFGSSETGFTGSGhSAGSGPETGPFTRANPDTVV-------LDDDGRVVPPG-SGGVGWIARRG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 383 QVFKEYFEKKEATQEAFE--DG--WFKTGDI--VEKDnstGRFKILGRSSVDIikNS-GYKISALEIEREILDHPDIEEC 455
Cdd:cd05924 222 HIPLGYYGDEAKTAETFPevDGvrYAVPGDRatVEAD---GTVTLLGRGSVCI--NTgGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 330846471 456 AVLGIPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:cd05924 297 LVVGRPDERWGQEVVAVVQLREGAGV-DLEELREHCRTRIARYKLPKQVVFVDEIER 352
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
60-523 |
1.02e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 60 RVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKEnysMLAEIGRKVGVQVIEIPEIGNG 139
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH---LQARLPLPDGLRSLVLDQEDDW 1702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 140 SPNKEVQHKIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLH---HVHGLINilt 216
Cdd:PRK12467 1703 LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAfdvSVWELFW--- 1779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 217 cSLWSGAMCEMMP---KFDSKQVIDRLLESGVTTdLEQPISLFMAvptiyskLIKYVEENVKTEKerqdiekafqrLRLM 293
Cdd:PRK12467 1780 -PLINGARLVIAPpgaHRDPEQLIQLIERQQVTT-LHFVPSMLQQ-------LLQMDEQVEHPLS-----------LRRV 1839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 294 VSGSSALPETVKNDFMEISGHN-LLERYGMTEIGM------CLSNPLHGdRVSGSVGFPLPGVQVKInaeASSTQNGKPV 366
Cdd:PRK12467 1840 VCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVdvthwtCRRKDLEG-RDSVPIGQPIANLSTYI---LDASLNPVPI 1915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 367 fkdntKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWF--------KTGDIVeKDNSTGRFKILGRssVD-IIKNSGYKI 437
Cdd:PRK12467 1916 -----GVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlyRTGDLA-RYRADGVIEYLGR--IDhQVKIRGFRI 1987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 438 SALEIEREILDHPDIEECAVLGIPNEEYGQVIG------AILVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIP 511
Cdd:PRK12467 1988 ELGEIEARLREQGGVREAVVIAQDGANGKQLVAyvvptdPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMP 2067
|
490
....*....|..
gi 330846471 512 KNAMLKVNKKDL 523
Cdd:PRK12467 2068 LTPNGKLDRKAL 2079
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
59-523 |
1.53e-22 |
|
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: 100.88 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKEnYSMLAEIGRKVGVQVIEIPEIGN 138
Cdd:cd17651 46 DLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPA-LAGELAVELVAVTLLDQPGAAAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 GSPNKEVqhkimPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLH---HVHGLINIL 215
Cdd:cd17651 125 ADAEPDP-----ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 216 TCslwsGAmCEMMPKFDSKQVIDRLLESGVTTDLEQpisLFMavPTIyskLIKYVEENVKTEKERQdiekafQRLRLMVS 295
Cdd:cd17651 200 CA----GA-TLVLPPEEVRTDPPALAAWLDEQRISR---VFL--PTV---ALRALAEHGRPLGVRL------AALRYLLT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 296 GSSALP--ETVKNDFMEISGHNLLERYGMTE--IGMCLSNPL----HGDRVsgSVGFPLPGVQVKINAEAsstqnGKPVf 367
Cdd:cd17651 261 GGEQLVltEDLREFCAGLPGLRLHNHYGPTEthVVTALSLPGdpaaWPAPP--PIGRPIDNTRVYVLDAA-----LRPV- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 368 kdNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGW------FKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISAL 440
Cdd:cd17651 333 --PPGVPGELYIGGAGLARGYLNRPELTAERFvPDPFvpgarmYRTGDLARWLPD-GELEFLGRAD-DQVKIRGFRIELG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 441 EIEREILDHPDIEECAVLGIPNEEYGQVIGAILVykkgAEPMSYDDFKMWCQQ---RLAYYKVPKVIQVKEEIPKNAMLK 517
Cdd:cd17651 409 EIEAALARHPGVREAVVLAREDRPGEKRLVAYVV----GDPEAPVDAAELRAAlatHLPEYMVPSAFVLLDALPLTPNGK 484
|
....*.
gi 330846471 518 VNKKDL 523
Cdd:cd17651 485 LDRRAL 490
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
60-523 |
1.73e-22 |
|
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: 100.02 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 60 RVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigng 139
Cdd:cd17652 39 LVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTPDNL----------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 140 spnkevqhkimpfdinrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHhVHGLINILTCSL 219
Cdd:cd17652 96 ------------------AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 220 WSGAMCEMMPKFDSK---QVIDRLLESGVTTdLEQPISLFMAVPTiysklikyveenvktekerqdiEKAFQRLRLMVSG 296
Cdd:cd17652 157 LAGATLVLAPAEELLpgePLADLLREHRITH-VTLPPAALAALPP----------------------DDLPDLRTLVVAG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 297 SSALPETVKNdfmEISGHNLLERYGMTEIGMC--LSNPLHGDRVSgSVGFPLPGVQVKI-NAEASSTQNGKPvfkdntke 373
Cdd:cd17652 214 EACPAELVDR---WAPGRRMINAYGPTETTVCatMAGPLPGGGVP-PIGRPVPGTRVYVlDARLRPVPPGVP-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 374 vGELLVKGPQVFKEYFEKKEATQEAF------EDG--WFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIERE 445
Cdd:cd17652 282 -GELYIAGAGLARGYLNRPGLTAERFvadpfgAPGsrMYRTGDLARWRAD-GQLEFLGRAD-DQVKIRGFRIELGEVEAA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 446 ILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPmSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17652 359 LTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAP-TAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
29-525 |
3.12e-22 |
|
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: 99.31 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 29 NTQRFTYNDLlnesAAISNQITFKKDDLEQ---DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSK 105
Cdd:cd17653 19 LGGSLTYGEL----DAASNALANRLLQLGVvpgDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 106 SSMVLTNKenysmlaeigrkvgvqvieipeigngSPNkevqhkimpfDInrnAQIIYTSGTTSRPKGVIATHSNIEaqvk 185
Cdd:cd17653 95 ATLLLTTD--------------------------SPD----------DL---AYIIFTSGSTGIPKGVMVPHRGVL---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 186 alveawewkkedHILEFLP--LHHVHGLINILTCSlwsgamcemmPKFD-SKQVIDRLLESGVT----------TDLEQP 252
Cdd:cd17653 132 ------------NYVSQPParLDVGPGSRVAQVLS----------IAFDaCIGEIFSTLCNGGTlvladpsdpfAHVART 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 253 ISLFMAVPTIYSKLikyveenvktekERQDiekaFQRLRLMVSGSSALPETVKNDFMEisGHNLLERYGMTEIGMCLSNP 332
Cdd:cd17653 190 VDALMSTPSILSTL------------SPQD----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 333 LHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDntkEVGELLVKGPQVFKEYFEKKEATQEAF-----EDGW--FK 405
Cdd:cd17653 252 ELLPGQPVTIGKPIPNSTCYILDA-----DLQPVPEG---VVGEICISGVQVARGYLGNPALTASKFvpdpfWPGSrmYR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 406 TGDIVEKDNStGRFKILGRSSVDiIKNSGYKISALEIEREILDHPDIEECAVLgipneeygQVIGAILVYKKGAEPMSYD 485
Cdd:cd17653 324 TGDYGRWTED-GGLEFLGREDNQ-VKVRGFRINLEEIEEVVLQSQPEVTQAAA--------IVVNGRLVAFVTPETVDVD 393
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 330846471 486 DFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:cd17653 394 GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
96-524 |
3.20e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 100.10 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 96 ELEYTITNSKSSMVLTNKENYSMLAEIGRKvGVQVIE---------IPEIGNGSPNKEVQHKiMPFdinrnaQIIYTSGT 166
Cdd:PRK13388 90 ALAADIRRADCQLLVTDAEHRPLLDGLDLP-GVRVLDvdtpayaelVAAAGALTPHREVDAM-DPF------MLIFTSGT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 167 TSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVT 246
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGAT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 247 --TDLEQPISLFMAVPtiysklikyveenvktekERQDieKAFQRLRLMVsGSSALPETvKNDFMEISGHNLLERYGMTE 324
Cdd:PRK13388 242 yfNYVGKPLAYILATP------------------ERPD--DADNPLRVAF-GNEASPRD-IAEFSRRFGCQVEDGYGSSE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 325 IGMCLSNPlhGDRVSGSVGFPLPGVQV------KINAEASSTQNGKPVFKDNTkeVGELLVK-GPQVFKEYFEKKEATQE 397
Cdd:PRK13388 300 GAVIVVRE--PGTPPGSIGRGAPGVAIynpetlTECAVARFDAHGALLNADEA--IGELVNTaGAGFFEGYYNNPEATAE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYG-QVIGAILVyk 476
Cdd:PRK13388 376 RMRHGMYWSGDLAYRD-ADGWIYFAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGdQVMAALVL-- 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 330846471 477 kgAEPMSYD-----DFkMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLV 524
Cdd:PRK13388 452 --RDGATFDpdafaAF-LAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
162-523 |
5.89e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.18 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLl 241
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNIL- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 242 esgvtTDLEQPIslFMAVPTIYSKLIKYVEENvktekerqdiekaFQRLRLMVSGSsALPETVkndFMEISGHN--LLER 319
Cdd:PRK08308 187 -----RNTPQHI--LYAVPLMLHILGRLLPGT-------------FQFHAVMTSGT-PLPEAW---FYKLRERTtyMMQQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 320 YGMTEIGmCLSnpLHGD-RVSGSVGFPLPGVQVKINAeasstqngkpvfkdNTKEVGELLVKgpqvfkeyfekkEATQEA 398
Cdd:PRK08308 243 YGCSEAG-CVS--ICPDmKSHLDLGNPLPHVSVSAGS--------------DENAPEEIVVK------------MGDKEI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 399 FedgwfkTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKG 478
Cdd:PRK08308 294 F------TKDLGYKS-ERGTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 330846471 479 AEPmsyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK08308 366 IDP---VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
8-523 |
8.86e-22 |
|
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: 98.28 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLF-QNALKYKNRIAIVNyphnNTQRFTYNDL---LNESAAISNQITFKKDDLeqdrVSFLYPQSFDYVRTQWGIWRSGG 83
Cdd:cd17644 4 QLFeEQVERTPDAVAVVF----EDQQLTYEELntkANQLAHYLQSLGVKSESL----VGICVERSLEMIIGLLAILKAGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 84 VAVPLSISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYT 163
Cdd:cd17644 76 AYVPLDPNYPQERLTYILEDAQISVLLTQPENL-----------------------------------------AYVIYT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 164 SGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKfdskQVIdRLLES 243
Cdd:cd17644 115 SGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYV-TLLSGATLVLRPE----EMR-SSLED 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 244 GVTTDLEQPISLFMAVPTIYSKLIKYVEenvktekerQDIEKAFQRLRLMVSGSSA-LPETVkNDFMEISGH--NLLERY 320
Cdd:cd17644 189 FVQYIQQWQLTVLSLPPAYWHLLVLELL---------LSTIDLPSSLRLVIVGGEAvQPELV-RQWQKNVGNfiQLINVY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 321 GMTE--IGMCLSNPL---HGDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEAT 395
Cdd:cd17644 259 GPTEatIAATVCRLTqltERNITSVPIGRPIANTQVYI-----LDENLQPV---PVGVPGELHIGGVGLARGYLNRPELT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAF---------EDGWFKTGDIVeKDNSTGRFKILGRssVD-IIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:cd17644 331 AEKFishpfnsseSERLYKTGDLA-RYLPDGNIEYLGR--IDnQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPG 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 466 GQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17644 408 NKRLVAYIVPHYEESPST-VELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
66-529 |
9.69e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.85 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 66 PQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKenySMLAEIGRKVGVQVIEIPEIG-NGSPNKE 144
Cdd:PRK12467 3153 ERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA---HLLEQLPAPAGDTALTLDRLDlNGYSENN 3229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 145 VQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAM 224
Cdd:PRK12467 3230 PSTRVMGENL---AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLW-TLICGGC 3305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 225 CEMMPK--FDSKQVIDRLLESGVTTdLEQPISlfmavptiysklikYVEENVKTEKERqdiekAFQRLRLMVSGSSALP- 301
Cdd:PRK12467 3306 LVVRDNdlWDPEELWQAIHAHRISI-ACFPPA--------------YLQQFAEDAGGA-----DCASLDIYVFGGEAVPp 3365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 302 ---ETVKNDFMEISGHNLlerYGMTEigmCLSNPLH----GDRVSGSVGFPLpGVQVKINAEASSTQNGKPVfkdNTKEV 374
Cdd:PRK12467 3366 aafEQVKRKLKPRGLTNG---YGPTE---AVVTVTLwkcgGDAVCEAPYAPI-GRPVAGRSIYVLDGQLNPV---PVGVA 3435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 375 GELLVKGPQVFKEYFEKKEATQEAFEDGWF--------KTGDIVeKDNSTGRFKILGRssVD-IIKNSGYKISALEIERE 445
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlyRTGDLA-RYRADGVIEYLGR--IDhQVKIRGFRIELGEIEAR 3512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 446 ILDHPDIEECAVLGIPNEEyGQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK12467 3513 LLQHPSVREAVVLARDGAG-GKQLVAYVVPADPQGDWR-ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
....
gi 330846471 526 LFTQ 529
Cdd:PRK12467 3591 PDAK 3594
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-523 |
2.48e-21 |
|
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: 96.96 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIvnypHNNTQRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHEL 97
Cdd:cd12114 2 DATAV----ICGDGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 98 EYTITNSKSSMVLTNKENYSMLAEIGRkvgvqVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATH 177
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFD-----VLILDLDALAAPAPPPPVDVAPDDL---AYVIFTSGSTGTPKGVMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 178 SNIEAQVKALVEAWEWKKEDHILEFLPLHH---VHGLINILTcslwSGAMCeMMPKFDSKQVIDRLLEsgvttDLEQ-PI 253
Cdd:cd12114 149 RAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFGALS----AGATL-VLPDEARRRDPAHWAE-----LIERhGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 254 SLFMAVPTIYSKLIKYVEenvktekerqDIEKAFQRLRL-MVSG---SSALPETVKNDFmeiSGHNLLERYGMTEiGMCL 329
Cdd:cd12114 219 TLWNSVPALLEMLLDVLE----------AAQALLPSLRLvLLSGdwiPLDLPARLRALA---PDARLISLGGATE-ASIW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 330 SN-----PLHGDRVSGSVGFPLPGVQVKINAeasstQNGKPVfKDNTkeVGELLVKGPQVFKEYFEKKEATQEAF---ED 401
Cdd:cd12114 285 SIyhpidEVPPDWRSIPYGRPLANQRYRVLD-----PRGRDC-PDWV--PGELWIGGRGVALGYLGDPELTAARFvthPD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 402 G--WFKTGDIvekdnstGRFK------ILGRssVDI-IKNSGYKISALEIEREILDHPDIEECAVLGIpNEEYGQVIGAI 472
Cdd:cd12114 357 GerLYRTGDL-------GRYRpdgtleFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAF 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 330846471 473 LVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd12114 427 VVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-492 |
3.25e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 97.22 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 117 SMLAEIGRKVGVQVI---EIPEIGNGSPNKEVQHKImpfDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEW 193
Cdd:PLN02861 185 SEQKEEAEELGVSCFsweEFSLMGSLDCELPPKQKT---DI---CTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 194 K-----KEDHILEFLPLHHVHGLINILTC-------SLWSGAMCEMMpkfDSKQVIDRLLESGVT-------TDLEQPIS 254
Cdd:PLN02861 259 TdrvatEEDSYFSYLPLAHVYDQVIETYCiskgasiGFWQGDIRYLM---EDVQALKPTIFCGVPrvydriyTGIMQKIS 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 255 --------LFMAVptiYSKLIKYVEENVKTEK-----ERQDIEKAFQ----RLRLMVSGSSALPETVKnDFMEI-SGHNL 316
Cdd:PLN02861 336 sggmlrkkLFDFA---YNYKLGNLRKGLKQEEasprlDRLVFDKIKEglggRVRLLLSGAAPLPRHVE-EFLRVtSCSVL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTE-IGMCLSNPLHGDRVSGSVGFPLPGVQVKINaeaSSTQNGKPVFKDNTKevGELLVKGPQVFKEYFEKKEAT 395
Cdd:PLN02861 412 SQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLE---SVPEMGYDALSDVPR--GEICLRGNTLFSGYHKRQDLT 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 396 QEAFEDGWFKTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKISALE-IEREILDHPDIEECAVLGIPNEEYgqVIGAILV 474
Cdd:PLN02861 487 EEVLIDGWFHTGDIGEW-QPNGAMKIIDRKK-NIFKLSQGEYVAVEnLENTYSRCPLIASIWVYGNSFESF--LVAVVVP 562
|
410 420
....*....|....*....|...
gi 330846471 475 YKKGAEPM-----SYDDFKMWCQ 492
Cdd:PLN02861 563 DRQALEDWaannnKTGDFKSLCK 585
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
160-512 |
4.50e-21 |
|
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: 96.88 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIeaqvkALVEAWEWKkedHILEFLP---------LHHVHGLINILTCSLWSGA---MCEM 227
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGY-----LVYAATTMK---YVFDYGPgdiywctadVGWVTGHSYLLYGPLACGAttlLYEG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 MPKFDSK----QVIDRlleSGVTtdleqpiSLFMAvPTIYSKLIKYVEENVktekERQDIEKafqrLRLMVS-GSSALPE 302
Cdd:cd17634 309 VPNWPTParmwQVVDK---HGVN-------ILYTA-PTAIRALMAAGDDAI----EGTDRSS----LRILGSvGEPINPE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 303 TVKNDFMEISGHN--LLERYGMTEIG--MCLSNPLHGDRVSGSVGFPLPGVQVKINAEASSTQNGKpvfkdntkEVGELL 378
Cdd:cd17634 370 AYEWYWKKIGKEKcpVVDTWWQTETGgfMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGG--------TEGNLV 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 379 VKGP------QVFKEYFEKKEATQEAFEDGWFkTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDI 452
Cdd:cd17634 442 ITDPwpgqtrTLFGDHERFEQTYFSTFKGMYF-SGDGARRD-EDGYYWITGRSD-DVINVAGHRLGTAEIESVLVAHPKV 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330846471 453 EECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:cd17634 519 AEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPelYAELRNWVRKEIGPLATPDVVHWVDSLPK 580
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
158-461 |
9.01e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 95.74 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiniltcSLwsgAMCEMMPKFDSKQVI 237
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGP------AL---GMTSVIPDMDPTRPA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 ----DRLLES----GVTTdleqpisLFMAvPTIYSKLIKYVEENVKTekerqdiekaFQRLRLMVSGSSALPETVKNDFM 309
Cdd:PRK09274 248 tvdpAKLFAAieryGVTN-------LFGS-PALLERLGRYGEANGIK----------LPSLRRVISAGAPVPIAVIERFR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 310 EISGHN--LLERYGMTE---IGMCLSNPLHGDRVSGS-------VGFPLPGVQVKI----NAEASSTQNGKPVfkdNTKE 373
Cdd:PRK09274 310 AMLPPDaeILTPYGATEalpISSIESREILFATRAATdngagicVGRPVDGVEVRIiaisDAPIPEWDDALRL---ATGE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 374 VGELLVKGPQVFKEYFEKKEATQEA-FEDG----WFKTGDIVEKDnSTGRFKILGRSS--VDIIKNSGYKIsalEIEREI 446
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLD-AQGRLWFCGRKAhrVETAGGTLYTI---PCERIF 462
|
330
....*....|....*
gi 330846471 447 LDHPDIEECAVLGIP 461
Cdd:PRK09274 463 NTHPGVKRSALVGVG 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
8-523 |
1.40e-20 |
|
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: 94.31 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLF-QNALKYKNRIAIVNyphnNTQRFTYNDLLNESAAISNQITFKKDDLEQdRVSFLYPQSFDYVRTQWGIWRSGGVAV 86
Cdd:cd12115 3 DLVeAQAARTPDAIALVC----GDESLTYAELNRRANRLAARLRAAGVGPES-RVGVCLERTPDLVVALLAVLKAGAAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 87 PLSISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSGT 166
Cdd:cd12115 78 PLDPAYPPERLRFILEDAQARLVLTDPDDL-----------------------------------------AYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 167 TSRPKGVIATHSNIEAQVKalveaweWKKEDHILEFlplhhvhgliniLTCSLWSGAMC------EMM-PKFDSKQVIdr 239
Cdd:cd12115 117 TGRPKGVAIEHRNAAAFLQ-------WAAAAFSAEE------------LAGVLASTSICfdlsvfELFgPLATGGKVV-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 240 lLESGVTTDLEQP----ISLFMAVPTIYSKLIKY--VEENVKT-----EKERQDIekaFQRLRlmvsgssALPETVKndf 308
Cdd:cd12115 176 -LADNVLALPDLPaaaeVTLINTVPSAAAELLRHdaLPASVRVvnlagEPLPRDL---VQRLY-------ARLQVER--- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 309 meisGHNLlerYGMTEI----GMCLSNPLHGDRVsgSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQV 384
Cdd:cd12115 242 ----VVNL---YGPSEDttysTVAPVPPGASGEV--SIGRPLANTQAYV-----LDRALQPV---PLGVPGELYIGGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 385 FKEYFEKKEATQEAF-----EDG--WFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAV 457
Cdd:cd12115 305 ARGYLGRPGLTAERFlpdpfGPGarLYRTGDLVRWR-PDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVV 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 458 LGIPNEEYGQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd12115 383 VAIGDAAGERRLVAYIVAEPGAAGLV-EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-526 |
1.53e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 95.80 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEA---QVKALVEAwewKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSK 234
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLAnraQVAARIDF---SPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHY 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLL-ESGVT----TDLeqpislF------MAVPtiYSklikyveenvktekerqdiekaFQRLRLMVSGSSALPET 303
Cdd:PRK06814 873 RIIPELIyDTNATilfgTDT------FlngyarYAHP--YD----------------------FRSLRYVFAGAEKVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 304 VKNDFMEISGHNLLERYGMTEIG--MCLSNPLHgDRvSGSVGFPLPGVQVKInaeasstqngKPVfkDNTKEVGELLVKG 381
Cdd:PRK06814 923 TRQTWMEKFGIRILEGYGVTETApvIALNTPMH-NK-AGTVGRLLPGIEYRL----------EPV--PGIDEGGRLFVRG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 382 PQVFKEYFE-KKEATQEAFEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREI--LDhPDIEEcAVL 458
Cdd:PRK06814 989 PNVMLGYLRaENPGVLEPPADGWYDTGDIVTID-EEGFITIKGRAK-RFAKIAGEMISLAAVEELAaeLW-PDALH-AAV 1064
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 459 GIPNEEYGQVIgaILVYKkgAEPMSYDDFKMWCQQR-LAYYKVPKVIQVKEEIPknaMLKVNKKDLVKL 526
Cdd:PRK06814 1065 SIPDARKGERI--ILLTT--ASDATRAAFLAHAKAAgASELMVPAEIITIDEIP---LLGTGKIDYVAV 1126
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
30-518 |
1.66e-20 |
|
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: 94.86 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 30 TQRFTYNDLLNESAAISNQItfKKDDLEQ-DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSM 108
Cdd:cd05968 89 SRTLTYGELLYEVKRLANGL--RALGVGKgDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 109 VLTN------------KENYSMLAE---------IGRKVGVQVIEIP--------EIGNGSPNKEVQHKIMPFdinrnaQ 159
Cdd:cd05968 167 LITAdgftrrgrevnlKEEADKACAqcptvekvvVVRHLGNDFTPAKgrdlsydeEKETAGDGAERTESEDPL------M 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEaqVKALVEAW---EWKKEDHILEFLPLHHVHG-------LINILTCSLWSGAmcemmP 229
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAGFP--LKAAQDMYfqfDLKPGDLLTWFTDLGWMMGpwlifggLILGATMVLYDGA-----P 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 230 KFDSKqviDRLLEsgvTTDLEQPISLFMAvPTIYSKLIKYVEENVKTEkerqdiekafQRLRLMVSGSSALP-------- 301
Cdd:cd05968 314 DHPKA---DRLWR---MVEDHEITHLGLS-PTLIRALKPRGDAPVNAH----------DLSSLRVLGSTGEPwnpepwnw 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 302 --ETVkndfmeISGHNLLERY-GMTEI-GMCLSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdnTKEVGEL 377
Cdd:cd05968 377 lfETV------GKGRNPIINYsGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVLDE-----SGKPA----RPEVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQV--FKEYFEKKEATQEA----FEDGWFKtGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPD 451
Cdd:cd05968 442 VLLAPWPgmTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYD-EEGYFYILGRSD-DTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 452 IEECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
151-464 |
2.03e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 94.88 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKAL---VEAWEWK--KEDHILEFLPLHHV----------------- 208
Cdd:PLN02430 219 PLDI---CTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFEDKmtHDDVYLSFLPLAHIldrmieeyffrkgasvg 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 209 --HGLINILTCSLWsgamcEMMPKFDS--KQVIDRLLEsGVTTDLEQ--PISLFmavptIYSKLIKYVEENVK---TEKE 279
Cdd:PLN02430 296 yyHGDLNALRDDLM-----ELKPTLLAgvPRVFERIHE-GIQKALQElnPRRRL-----IFNALYKYKLAWMNrgySHKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 280 RQDIEK--AFQ--------RLRLMVSGSSALPETVKnDFMEIS-------GHNLLERYGMTEIG----MCLSnplhgdrv 338
Cdd:PLN02430 365 ASPMADflAFRkvkaklggRLRLLISGGAPLSTEIE-EFLRVTscafvvqGYGLTETLGPTTLGfpdeMCML-------- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 339 sGSVGfpLPGVQVKINAEASSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKdNSTGR 418
Cdd:PLN02430 436 -GTVG--APAVYNELRLEEVPEMGYDPL---GEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEI-LPNGV 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 419 FKILGRSSvDIIKNSGYKISALEIEREILDHPDI-EECAVLG-----------IPNEE 464
Cdd:PLN02430 509 LKIIDRKK-NLIKLSQGEYVALEYLENVYGQNPIvEDIWVYGdsfksmlvavvVPNEE 565
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-526 |
9.31e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 60 RVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKEnysMLAEIGRKVGVQVIEIPEIGN- 138
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSH---LLQRLPIPDGLASLALDRDEDw 4679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 139 -GSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLH---HVHGLINI 214
Cdd:PRK12316 4680 eGFPAHDPAVRLHPDNL---AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSfdgSHEGLYHP 4756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 215 LTCslwsGAmCEMMPK---FDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEEnvktekerqDIEKAfqRLR 291
Cdd:PRK12316 4757 LIN----GA-SVVIRDdslWDPERLYAEIHEHRVTV--------LVFPPVYLQQLAEHAER---------DGEPP--SLR 4812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 292 LMVSGSSAL-PETVKNDFMEISGHNLLERYGMTEigmCLSNPLHGD--------RVSGSVGFPLPGVQVKINAEASSTQn 362
Cdd:PRK12316 4813 VYCFGGEAVaQASYDLAWRALKPVYLFNGYGPTE---TTVTVLLWKardgdacgAAYMPIGTPLGNRSGYVLDGQLNPL- 4888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 363 gkPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAF------EDG--WFKTGDIVeKDNSTGRFKILGRssVD-IIKNS 433
Cdd:PRK12316 4889 --PV-----GVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGgrLYRTGDLA-RYRADGVIDYLGR--VDhQVKIR 4958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 434 GYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI------LVYKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVK 507
Cdd:PRK12316 4959 GFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFL 5038
|
490
....*....|....*....
gi 330846471 508 EEIPKNAMLKVNKKDLVKL 526
Cdd:PRK12316 5039 ARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
18-523 |
1.22e-19 |
|
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: 91.77 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNyphnNTQRFTYNDLlNESAaisNQIT-------FKKDDLeqdrVSFLYPQSFDYVRTQWGIWRSGGVAVPLSI 90
Cdd:cd17656 3 DAVAVVF----ENQKLTYREL-NERS---NQLArflrekgVKKDSI----VAIMMERSAEMIVGILGILKAGGAFVPIDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 91 SHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRkvgVQVIEIPEIGNGSPNKevqhkimpFDINRNAQ----IIYTSGT 166
Cdd:cd17656 71 EYPEERRIYIMLDSGVRVVLTQRHLKSKLSFNKS---TILLEDPSISQEDTSN--------IDYINNSDdllyIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 167 TSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPKfDSKQVIDRLLESGVT 246
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFS-TLLSGGTLYIIRE-ETKRDVEQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 247 TDLEQPIslfmaVPTIYSKLIKyveenvkteKERQDIEKAFQRLRLMVSGSSAL--PETVKNDFME--ISGHNlleRYGM 322
Cdd:cd17656 218 HNIEVVF-----LPVAFLKFIF---------SEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEhnVHLHN---HYGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 323 TE---IGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEASSTQngkPVfkdntKEVGELLVKGPQVFKEYFEKKEATQEAF 399
Cdd:cd17656 281 SEthvVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQ---PQ-----GIVGELYISGASVARGYLNRQELTAEKF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 EDGWF-------KTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAI 472
Cdd:cd17656 353 FPDPFdpnermyRTGDLARY-LPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAY 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 330846471 473 LVykkGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17656 431 FV---MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
320-512 |
2.48e-19 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 91.47 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 320 YGMTEIGMCLSNPLHG--DRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGP------------QVF 385
Cdd:cd05966 388 WWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAILDE-----EGNEV---EGEVEGYLVIKRPwpgmartiygdhERY 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 386 KE-YFEKkeatqeafEDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEE 464
Cdd:cd05966 460 EDtYFSK--------FPGYYFTGDGARRD-EDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDI 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330846471 465 YGQVIGAILVYKKGAEPMSY--DDFKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:cd05966 530 KGEAIYAFVTLKDGEEPSDElrKELRKHVRKEIGPIATPDKIQFVPGLPK 579
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
58-523 |
6.03e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.00 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 58 QDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEIGRKVGVQVIEIPEIG 137
Cdd:PRK05691 2238 QVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAAA 2317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 138 -NGSPNKEVQHKIMPfdiNRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILT 216
Cdd:PRK05691 2318 lAAYSDAPLPFLSLP---QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLV 2394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 217 cSLWSGAmcemmpkfdskQVIDRL-----LESGVTTDLEQPISLFMAVPTIYSKLIKYVEEnvktekerqdiEKAFQRLR 291
Cdd:PRK05691 2395 -PLLCGA-----------RVVLRAqgqwgAEEICQLIREQQVSILGFTPSYGSQLAQWLAG-----------QGEQLPVR 2451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 292 LMVSGSSAL-PETVKNDFMEISGHNLLERYGMTE-IGMCLSNPLHGDRVSGSVGFPLpGVQVKINAEASSTQNGKPVFKD 369
Cdd:PRK05691 2452 MCITGGEALtGEHLQRIRQAFAPQLFFNAYGPTEtVVMPLACLAPEQLEEGAASVPI-GRVVGARVAYILDADLALVPQG 2530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 370 NTkevGELLVKGPQVFKEYFEKKEATQEAF------EDG--WFKTGDIVeKDNSTGRFKILGRSSVDiIKNSGYKISALE 441
Cdd:PRK05691 2531 AT---GELYVGGAGLAQGYHDRPGLTAERFvadpfaADGgrLYRTGDLV-RLRADGLVEYVGRIDHQ-VKIRGFRIELGE 2605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 442 IEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDF----KMWCQQRLAYYKVPKVIQVKEEIPKNAMLK 517
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
|
....*.
gi 330846471 518 VNKKDL 523
Cdd:PRK05691 2686 LDRRAL 2691
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
158-527 |
8.31e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.46 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEdHILEFL---PLHHVhgliniLTcslWSGAMCEMM---Pkf 231
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVT-HGESFLccvPIYHV------LS---WGVPLAAFMsgtP-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 232 dskqvidrLLESGVTTD---LEQPISLFM-----AVPTIYSKLIKYVEenvKTEKERQDiekafqrLRLMVSGSSALPET 303
Cdd:PRK05620 252 --------LVFPGPDLSaptLAKIIATAMprvahGVPTLWIQLMVHYL---KNPPERMS-------LQEIYVGGSAVPPI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 304 VKNDFMEISGHNLLERYGMTE---IGMcLSNPLHGdrVSG--------SVG-FPLpGVQVKInaeasstQNGKPVFKDNT 371
Cdd:PRK05620 314 LIKAWEERYGVDVVHVWGMTEtspVGT-VARPPSG--VSGearwayrvSQGrFPA-SLEYRI-------VNDGQVMESTD 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 372 KEVGELLVKGPQVFKEYFEK-----------------KEATQEAFEDGWFKTGDI--VEKDnstGRFKILGRSSvDIIKN 432
Cdd:PRK05620 383 RNEGEIQVRGNWVTASYYHSpteegggaastfrgedvEDANDRFTADGWLRTGDVgsVTRD---GFLTIHDRAR-DVIRS 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 433 SGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPM--SYDDFKMWCQQRLAYYKVPKVIQVKEEI 510
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTreTAERLRDQLRDRLPNWMLPEYWTFVDEI 538
|
410
....*....|....*..
gi 330846471 511 PKNAMLKVNKKDLVKLF 527
Cdd:PRK05620 539 DKTSVGKFDKKDLRQHL 555
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
158-410 |
2.25e-18 |
|
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: 88.26 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKED--HILEFLPLHHVHGLINILTCSLWSGAMCEMmpkfDSKQ 235
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI----DDGK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLESGVTTDLEQPISLFMAVPTIYSKLIKYVEenvKTEKERqdiEKAFQRLRLMVSGSSALPETVKNDFMEIS--- 312
Cdd:cd05921 244 PMPGGFEETLRNLREISPTVYFNVPAGWEMLVAALE---KDEALR---RRFFKRLKLMFYAGAGLSQDVWDRLQALAvat 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 313 -GHN--LLERYGMTEIGMCLSNpLHGDR-VSGSVGFPLPGVQVKInaeasSTQNGKPvfkdntkevgELLVKGPQVFKEY 388
Cdd:cd05921 318 vGERipMMAGLGATETAPTATF-THWPTeRSGLIGLPAPGTELKL-----VPSGGKY----------EVRVKGPNVTPGY 381
|
250 260
....*....|....*....|...
gi 330846471 389 FEKKEATQEAF-EDGWFKTGDIV 410
Cdd:cd05921 382 WRQPELTAQAFdEEGFYCLGDAA 404
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
158-480 |
3.87e-18 |
|
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: 87.16 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKfdskqvi 237
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPT------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 drllesgvttdleqpiSLFMAVPTIYSKLI---------------KYVEENVKTEKERqdiEKAFQRLRLMVSGSSALPE 302
Cdd:cd05908 182 ----------------RLFIRRPILWLKKAsehkativsspnfgyKYFLKTLKPEKAN---DWDLSSIRMILNGAEPIDY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 303 TVKNDFME-ISGHNL-----LERYGMTE--IGMCLSN------PLHGDRVSGSVGFPLPGVQVKINAEASSTQNGKPV-- 366
Cdd:cd05908 243 ELCHEFLDhMSKYGLkrnaiLPVYGLAEasVGASLPKaqspfkTITLGRRHVTHGEPEPEVDKKDSECLTFVEVGKPIde 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 367 ----FKDNTKE------VGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDNstGRFKILGRSSvDIIKNSGY 435
Cdd:cd05908 323 tdirICDEDNKilpdgyIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIRN--GRLVITGREK-DIIFVNGQ 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 330846471 436 KISALEIEREILDHPDIE--ECAVLGIPNEEYGQ-VIGAILVYKKGAE 480
Cdd:cd05908 400 NVYPHDIERIAEELEGVElgRVVACGVNNSNTRNeEIFCFIEHRKSED 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
67-525 |
4.54e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 67 QSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSMLAEigrkvGVQVIEIPEIGNGSPNKEVQ 146
Cdd:PRK12316 3116 RSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQ-----GVQVLDLDRGDENYAEANPA 3190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 147 HKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLhHVHGLINILTCSLWSGAmce 226
Cdd:PRK12316 3191 IRTMPENL---AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGA--- 3263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 227 mmpkfdSKQVIDRLLESGVTTDLEQPISLFMAVPTIYSKLIKYVEENVKTEKERQdiekafqrLRLMVSGSSALPETVKN 306
Cdd:PRK12316 3264 ------RVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTS--------LKRIVCGGEALPADLQQ 3329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 307 DFmeISGHNLLERYGMTEIGMclsNPLHGDRVSGSVGFPLPGVQVKINAEASSTQNGKPVFKDNtkeVGELLVKGPQVFK 386
Cdd:PRK12316 3330 QV--FAGLPLYNLYGPTEATI---TVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGA---LGELYLGGEGLAR 3401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 387 EYFEKKEATQEAFEDGWFKTGDIVEKDNSTGRFKILG----RSSVD-IIKNSGYKISALEIEREILDHPDIEECAVLGIP 461
Cdd:PRK12316 3402 GYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGvieyIGRVDhQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD 3481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 462 neeyGQVIGAILVyKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVK 525
Cdd:PRK12316 3482 ----GRQLVAYVV-PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-523 |
4.95e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 78 IWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKEnysMLAEIGRKVGVQVIEIPEIGNGSPNKEVQHKIMPFDINRN 157
Cdd:PRK12316 581 ILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH---LGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENL 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHhvhgliniLTCSLW-------SGAMCEMMPK 230
Cdd:PRK12316 658 AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFS--------FDVSVWeffwplmSGARLVVAAP 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 231 FDSkqvidRLLESGVTTDLEQPISLFMAVPTIYSKLIKyvEENVKtekerqdiekAFQRLRLMVSGSSALP-ETVKNDFM 309
Cdd:PRK12316 730 GDH-----RDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVA----------SCTSLRRIVCSGEALPaDAQEQVFA 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 310 EISGHNLLERYGMTE--IGMCLSNPLHGDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQVFKE 387
Cdd:PRK12316 793 KLPQAGLYNLYGPTEaaIDVTHWTCVEEGGDSVPIGRPIANLACYI-----LDANLEPV---PVGVLGELYLAGRGLARG 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 388 YFEKKEATQEAF-----EDG--WFKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGI 460
Cdd:PRK12316 865 YHGRPGLTAERFvpspfVAGerMYRTGDLA-RYRADGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 942
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330846471 461 PNEeygQVIGAILVYKKGAEPMSydDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK12316 943 DGK---QLVGYVVLESEGGDWRE--ALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
58-525 |
6.60e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 86.72 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 58 QDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKENYSmLAEIGRKVGVQVIEIPE-- 135
Cdd:cd05915 49 GDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLP-LVEAIRGELKTVQHFVVmd 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 136 ---------IGNGSPNKEvqhKIMPFDINRNAQIIYTSGTTSRPKGVIATH--SNIEAQVKALVEAWEWKKEDHILEFLP 204
Cdd:cd05915 128 ekapegylaYEEALGEEA---DPVRVPERAACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 205 LHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTTdleqpislFMAVPTIYSKLikyveenvktEKERQDIE 284
Cdd:cd05915 205 MFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTF--------TAGVPTVWLAL----------ADYLESTG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 285 KAFQRLRLMVSGSSALPEtVKNDFMEISGHNLLERYGMTEI-GM---CLSNPlHGDRVSGSVGFPLPGvQVKINAEASST 360
Cdd:cd05915 267 HRLKTLRRLVVGGSAAPR-SLIARFERMGVEVRQGYGLTETsPVvvqNFVKS-HLESLSEEEKLTLKA-KTGLPIPLVRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 361 QNGKPV---FKDNTKEVGELLVKGPQVFKEYFEKKEATQ-EAFEDGWFKTGD--IVEKDnstGRFKILGRSSvDIIKNSG 434
Cdd:cd05915 344 RVADEEgrpVPKDGKALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDiaVWDEE---GYVEIKDRLK-DLIKSGG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 435 YKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKgAEPMSyDDFKMWCQQRLAYYK-VPKVIQVKEEIPKN 513
Cdd:cd05915 420 EWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG-EKPTP-EELNEHLLKAGFAKWqLPDAYVFAEEIPRT 497
|
490
....*....|..
gi 330846471 514 AMLKVNKKDLVK 525
Cdd:cd05915 498 SAGKFLKRALRE 509
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
153-523 |
9.93e-18 |
|
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: 85.95 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 153 DINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFD 232
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 233 SKQVIDRLLESGVTtdleqpisLFMAVptiySKLIKYVEENVKTEKERQdiekafQRLRlMVSGSSALPEtVKNDFMEis 312
Cdd:cd05937 165 ASQFWKDVRDSGAT--------IIQYV----GELCRYLLSTPPSPYDRD------HKVR-VAWGNGLRPD-IWERFRE-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 313 ghnlleRYGMTEIG---------MCLSNPLHGDRVSGSVGFPLPGVQVKINAE----ASSTQNGKPVFKDNT-------- 371
Cdd:cd05937 223 ------RFNVPEIGefyaategvFALTNHNVGDFGAGAIGHHGLIRRWKFENQvvlvKMDPETDDPIRDPKTgfcvrapv 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 372 KEVGELLVKGP----QVFKEYFEKKEATQ-----EAFEDG--WFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISAL 440
Cdd:cd05937 297 GEPGEMLGRVPfknrEAFQGYLHNEDATEsklvrDVFRKGdiYFRTGDLLRQD-ADGRWYFLDRLG-DTFRWKSENVSTT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 441 EIEREILDHPDIEECAVLGI--PNEEyGQVIGAILVYKKGAEPMSYDDFKMW---CQQRLAYYKVPKVIQVKEEIPKNAM 515
Cdd:cd05937 375 EVADVLGAHPDIAEANVYGVkvPGHD-GRAGCAAITLEESSAVPTEFTKSLLaslARKNLPSYAVPLFLRLTEEVATTDN 453
|
....*...
gi 330846471 516 LKVNKKDL 523
Cdd:cd05937 454 HKQQKGVL 461
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
114-425 |
2.24e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 85.54 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 ENYSMLAEIGRKVGVQVIEIPEIGNgspNKEVQHKIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEW 193
Cdd:PTZ00342 266 EKIKDLKEKAKKLGISIILFDDMTK---NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIF 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 194 KK--EDHILEFLPLHHVHGLINILTCsLWSGAMCEMMPK---------FDSK--------QVIDRLLeSGVTTDLEQ--P 252
Cdd:PTZ00342 343 KKynPKTHLSYLPISHIYERVIAYLS-FMLGGTINIWSKdinyfskdiYNSKgnilagvpKVFNRIY-TNIMTEINNlpP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 253 ISLFMaVPTIYS--------KLIKYVEENVKTEKERQDieKAFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTE 324
Cdd:PTZ00342 421 LKRFL-VKKILSlrksnnngGFSKFLEGITHISSKIKD--KVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 325 IGMCLSNPLHGDRVSGSVGFPL-PGVQVKInaeaSSTQNGKPvfKDNTKEvGELLVKGPQVFKEYFEKKEATQEAF-EDG 402
Cdd:PTZ00342 498 TTGPIFVQHADDNNTESIGGPIsPNTKYKV----RTWETYKA--TDTLPK-GELLIKSDSIFSGYFLEKEQTKNAFtEDG 570
|
330 340
....*....|....*....|...
gi 330846471 403 WFKTGDIVEKdNSTGRFKILGRS 425
Cdd:PTZ00342 571 YFKTGDIVQI-NKNGSLTFLDRS 592
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
158-419 |
2.30e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 85.10 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATH----SNIeAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEM-----M 228
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQrmmcANI-AMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIddgkpL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 229 P-KFDskQVIDRLLESGVTTdleqpislFMAVPTIYSKLIKYVEenvKTEKERqdiEKAFQRLRLMVSGSSALPETVKND 307
Cdd:PRK12582 302 PgMFE--ETIRNLREISPTV--------YGNVPAGYAMLAEAME---KDDALR---RSFFKNLRLMAYGGATLSDDLYER 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 308 FMEIS----GHN--LLERYGMTEI-GMCLSNPLHGDRVsGSVGFPLPGVQVKInAEASSTQngkpvfkdntkevgELLVK 380
Cdd:PRK12582 366 MQALAvrttGHRipFYTGYGATETaPTTTGTHWDTERV-GLIGLPLPGVELKL-APVGDKY--------------EVRVK 429
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 330846471 381 GPQVFKEYFEKKEATQEAF-EDGWFKTGDivekdnsTGRF 419
Cdd:PRK12582 430 GPNVTPGYHKDPELTAAAFdEEGFYRLGD-------AARF 462
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
286-529 |
3.11e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 84.66 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 286 AFQRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEiGMC----LSNPlhGDRVSGSVGFPL-PGVQVKINAEasst 360
Cdd:PRK10946 298 QLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE-GLVnytrLDDS--DERIFTTQGRPMsPDDEVWVADA---- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 361 qNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISA 439
Cdd:PRK10946 371 -DGNPL---PQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSID-PDGYITVVGREK-DQINRGGEKIAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 440 LEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMwcQQRLAYYKVPKVIQVKEEIPKNAMLKVN 519
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRRFLR--EQGIAEFKLPDRVECVDSLPLTAVGKVD 522
|
250
....*....|
gi 330846471 520 KKDLVKLFTQ 529
Cdd:PRK10946 523 KKQLRQWLAS 532
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-410 |
3.36e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 84.81 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK 113
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 ENYSM------------------------------------LAEIGRKVGVQVIEIPEIGNGSPNKEVQhkiMPFDINRN 157
Cdd:cd17632 149 EHLDLaveavleggtpprlvvfdhrpevdahraalesarerLAAVGIPVTTLTLIAVRGRDLPPAPLFR---PEPDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIeAQVKALVEAWEWKKEDH--ILEFLPLHHVHGLiNILTCSLWSGAMCEMMPKFDSKQ 235
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLV-ATFWLKVSSIQDIRPPAsiTLNFMPMSHIAGR-ISLYGTLARGGTAYFAAASDMST 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLlesgvttDLEQPISLFMaVPTIY--------SKLIKYV---------EENVKTEKeRQDIEKAfqRLRLMVSGSS 298
Cdd:cd17632 304 LFDDL-------ALVRPTELFL-VPRVCdmlfqryqAELDRRSvagadaetlAERVKAEL-RERVLGG--RLLAAVCGSA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 299 ALPETVKNdFMEIS-GHNLLERYGMTEIGMCLsnplhgdrVSGSVGFPlPGVQVKIN--AEASSTQNGKPVFKdntkevG 375
Cdd:cd17632 373 PLSAEMKA-FMESLlDLDLHDGYGSTEAGAVI--------LDGVIVRP-PVLDYKLVdvPELGYFRTDRPHPR------G 436
|
410 420 430
....*....|....*....|....*....|....*.
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAF-EDGWFKTGDIV 410
Cdd:cd17632 437 ELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVM 472
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
158-460 |
3.49e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 84.05 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTcslwsGAMCEMMP----KFDS 233
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLT-----SVIPDMDPtrpaRADP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 234 KQVIDRLLESGVTTDLeqpislfmAVPTIYSKLIKYVEENVKTekerqdiekaFQRLRLMVSGSSALPETVKNDFMEI-- 311
Cdd:cd05910 163 QKLVGAIRQYGVSIVF--------GSPALLERVARYCAQHGIT----------LPSLRRVLSAGAPVPIALAARLRKMls 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 312 SGHNLLERYGMTE---IGMCLSNPLHGDRVSGS-------VGFPLPGVQVKI----NAEASSTQNGKPVfkdNTKEVGEL 377
Cdd:cd05910 225 DEAEILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIieidDEPIAEWDDTLEL---PRGEIGEI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQVFKEYFEKKEATQEA-FEDG----WFKTGDIVEKDNStGRFKILGRSSVDIIkNSGYKISALEIEREILDHPDI 452
Cdd:cd05910 302 TVTGPTVTPTYVNRPVATALAkIDDNsegfWHRMGDLGYLDDE-GRLWFCGRKAHRVI-TTGGTLYTEPVERVFNTHPGV 379
|
....*...
gi 330846471 453 EECAVLGI 460
Cdd:cd05910 380 RRSALVGV 387
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
8-525 |
3.57e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 84.18 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 8 QLFQNALKYKNRIAIvnypHNNTQRFTYNDLLNESAAISNQItfKKDDLEQDRVSFLY-PQSFDYVRTQWGIWRSGGVAV 86
Cdd:PRK04813 7 TIEEFAQTQPDFPAY----DYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVFgHMSPEMLATFLGAVKAGHAYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 87 PLSISHPPHELEYTITNSKSSMVL-TNKENYSMLaeigrkvGVQVIEIPEIGNGSPNKEVQHKIMPFDINRNAQIIYTSG 165
Cdd:PRK04813 81 PVDVSSPAERIEMIIEVAKPSLIIaTEELPLEIL-------GIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNieaqvkaLVEAWEWKKEDHIL----EFL---PLHHVHGLINILTCsLWSGAMCEMMPK---FDSKQ 235
Cdd:PRK04813 154 TTGKPKGVQISHDN-------LVSFTNWMLEDFALpegpQFLnqaPYSFDLSVMDLYPT-LASGGTLVALPKdmtANFKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 236 VIDRLLESgvttdleqPISLFMAVPTiysklikyveenvktekerqdiekaFQRLRLMVSGSSA--LPETvkNDFM---E 310
Cdd:PRK04813 226 LFETLPQL--------PINVWVSTPS-------------------------FADMCLLDPSFNEehLPNL--THFLfcgE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ISGH----NLLER---------YGMTEIGMCLS------------NPLhgdrvsgSVGFPLPGVQVKINAEasstqNGKP 365
Cdd:PRK04813 271 ELPHktakKLLERfpsatiyntYGPTEATVAVTsieitdemldqyKRL-------PIGYAKPDSPLLIIDE-----EGTK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 366 VFkdnTKEVGELLVKGPQVFKEYFEKKEATQEAF--EDGW--FKTGDIVEKDNstGRFKILGRssVDI-IKNSGYKISAL 440
Cdd:PRK04813 339 LP---DGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLED--GLLFYQGR--IDFqIKLNGYRIELE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 441 EIEREILDHPDIEECAVLGI-PNEEYGQVIGAILVYKKGAEpmsyDDFKMW------CQQRLAYYKVPKVIQVKEEIPKN 513
Cdd:PRK04813 412 EIEQNLRQSSYVESAVVVPYnKDHKVQYLIAYVVPKEEDFE----REFELTkaikkeLKERLMEYMIPRKFIYRDSLPLT 487
|
570
....*....|..
gi 330846471 514 AMLKVNKKDLVK 525
Cdd:PRK04813 488 PNGKIDRKALIE 499
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
18-523 |
4.30e-17 |
|
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: 83.60 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 18 NRIAIVNyphnNTQRFTYNDLlNESAaisNQITF--------KKDDLeqdrVSFLYPQSFDYVRTQWGIWRSGGVAVPLS 89
Cdd:cd17648 2 DRVAVVY----GDKRLTYREL-NERA---NRLAHyllsvaeiRPDDL----VGLVLDKSELMIIAILAVWKAGAAYVPID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 90 ISHPPHELEYTITNSKSSMVLTNKENYsmlaeigrkvgvqvieipeigngspnkevqhkimpfdinrnAQIIYTSGTTSR 169
Cdd:cd17648 70 PSYPDERIQFILEDTGARVVITNSTDL-----------------------------------------AYAIYTSGTTGK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 170 PKGVIATHSNIEAQVKALVEAWEWKKE-DHILEFLPLHHVHGLINILTCSLWSGAMCEMMP---KFDSKQVIDRLLESGV 245
Cdd:cd17648 109 PKGVLVEHGSVVNLRTSLSERYFGRDNgDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPdemRFDPDRFYAYINREKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 246 TtdleqpisLFMAVPTIYSkLIKYVEENvktekerqdiekafqRLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI 325
Cdd:cd17648 189 T--------YLSGTPSVLQ-QYDLARLP---------------HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 326 GMCLSNPLH--GDRVSGSVGFPLPGVQVKInaeasSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAF---- 399
Cdd:cd17648 245 TVTNHKRFFpgDQRFDKSLGRPVRNTKCYV-----LNDAMKRV---PVGAVGELYLGGDGVARGYLNRPELTAERFlpnp 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 400 -------EDG----WFKTGDIVEKDNStGRFKILGRSSVDIiKNSGYKISALEIEREILDHPDIEECAVlgIPNEEYGQV 468
Cdd:cd17648 317 fqteqerARGrnarLYKTGDLVRWLPS-GELEYLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAV--VAKEDASQA 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 469 IGAI---LV--YKKGAEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:cd17648 393 QSRIqkyLVgyYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
59-444 |
9.03e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.12 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGvavPLSISHPP----------HELEYTITNSKSSMVLTNkENYSMLAEIGRKVGV 128
Cdd:PRK07768 55 DAVAVLAGAPVEIAPTAQGLWMRGA---SLTMLHQPtprtdlavwaEDTLRVIGMIGAKAVVVG-EPFLAAAPVLEEKGI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 129 QVIEIPEIGNGSPnkevqhkIMPFDINRNAQIIY--TSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKE-DHILEFLPL 205
Cdd:PRK07768 131 RVLTVADLLAADP-------IDPVETGEDDLALMqlTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 206 HHVHGLINILTCSLWSGamCEmmpkfdskqvidrlLESGVTTDleqpislFMAVPTIYSKLI-KY-----VEEN-----V 274
Cdd:PRK07768 204 FHDMGMVGFLTVPMYFG--AE--------------LVKVTPMD-------FLRDPLLWAELIsKYrgtmtAAPNfayalL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 275 KTEKERQDIEKAF--QRLRLMVSGSSALPETVKNDFMEISGHNLLER------YGMTEIGMCLS----------NPLHGD 336
Cdd:PRK07768 261 ARRLRRQAKPGAFdlSSLRFALNGAEPIDPADVEDLLDAGARFGLRPeailpaYGMAEATLAVSfspcgaglvvDEVDAD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 337 RVSG----------------SVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGPQVFKEYFEKK--EATQEA 398
Cdd:PRK07768 341 LLAAlrravpatkgntrrlaTLGPPLPGLEVRVVDE-----DGQVL---PPRGVGVIELRGESVTPGYLTMDgfIPAQDA 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 330846471 399 feDGWFKTGDI---VEKdnstGRFKILGRSSvDIIKNSGYKISALEIER 444
Cdd:PRK07768 413 --DGWLDTGDLgylTEE----GEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-523 |
1.58e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.68 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 77 GIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNKenySMLAEIGRKVGVQVIEIPEIGngSPNKEVQHKIMPFDINR 156
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS---HLLERLPQAEGVSAIALDSLH--LDSWPSQAPGLHLHGDN 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 157 NAQIIYTSGTTSRPKGVIATHSnieaqvkALVEAWEWKKEDHILE--------------------FLPLhhvhglinILT 216
Cdd:PRK05691 1275 LAYVIYTSGSTGQPKGVGNTHA-------ALAERLQWMQATYALDdsdvlmqkapisfdvsvwecFWPL--------ITG 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 217 CSLWSGAMCEMMpkfDSKQVIDRLLESGVTTdleqpislFMAVPTIyskLIKYVEENVKTEkerqdiekaFQRLRLMVSG 296
Cdd:PRK05691 1340 CRLVLAGPGEHR---DPQRIAELVQQYGVTT--------LHFVPPL---LQLFIDEPLAAA---------CTSLRRLFSG 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 297 SSALPETVKNDFME----ISGHNlleRYGMTEIGMclsNPLH-------GDRVsgSVGFPLPGVQVKI-NAEASSTQNGK 364
Cdd:PRK05691 1397 GEALPAELRNRVLQrlpqVQLHN---RYGPTETAI---NVTHwqcqaedGERS--PIGRPLGNVLCRVlDAELNLLPPGV 1468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 365 PvfkdntkevGELLVKGPQVFKEYFEKKEATQEAF------EDG--WFKTGDIVeKDNSTGRFKILGRSSVDiIKNSGYK 436
Cdd:PRK05691 1469 A---------GELCIGGAGLARGYLGRPALTAERFvpdplgEDGarLYRTGDRA-RWNADGALEYLGRLDQQ-VKLRGFR 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 437 ISALEIEREILDHPDIEECAVLgipneEYGQVIGAILV--YKKGAEP-MSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKN 513
Cdd:PRK05691 1538 VEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVgyYTGEAGQeAEAERLKAALAAELPEYMVPAQLIRLDQMPLG 1612
|
490
....*....|
gi 330846471 514 AMLKVNKKDL 523
Cdd:PRK05691 1613 PSGKLDRRAL 1622
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
31-523 |
2.14e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 81.98 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISnQITFKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVL 110
Cdd:PRK13390 23 EQVSYRQLDDDSAALA-RVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 111 TNKENYSMLAEIGRKVGVQVIEIPEI-GNGSPNKEVQHKIMPF-DINRNAQIIYTSGTTSRPKG---------VIATHSN 179
Cdd:PRK13390 102 ASAALDGLAAKVGADLPLRLSFGGEIdGFGSFEAALAGAGPRLtEQPCGAVMLYSSGTTGFPKGiqpdlpgrdVDAPGDP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 180 IEAQVKALveaWEWKKEDHILEFLPLHHVHGLiniLTCSLWS--GAMCEMMPKFDSKQVIdRLLEsgvttdlEQPISLFM 257
Cdd:PRK13390 182 IVAIARAF---YDISESDIYYSSAPIYHAAPL---RWCSMVHalGGTVVLAKRFDAQATL-GHVE-------RYRITVTQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 258 AVPTIYSKLIKyVEENVKTekeRQDIEKafqrLRLMVSGSSALPETVKNDFMEISGHNLLERYGMTEI-GMCLSNPlhGD 336
Cdd:PRK13390 248 MVPTMFVRLLK-LDADVRT---RYDVSS----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAhGMTFIDS--PD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 337 RVS--GSVGFPLPGVQVKINAEASSTQNGkpvfkdntkEVGELLVKGPQVFKEYFEKKEATQEAFEDG---WFKTGDIVE 411
Cdd:PRK13390 318 WLAhpGSVGRSVLGDLHICDDDGNELPAG---------RIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 412 KDNStGRFKILGRSSVDIIkNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKM 489
Cdd:PRK13390 389 VDED-GYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelARELID 466
|
490 500 510
....*....|....*....|....*....|....
gi 330846471 490 WCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK13390 467 YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
162-514 |
7.44e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.85 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 162 YTSGTTSRPKGVIATHSNIEAQVKALV-EAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGamcemmpkfdSKQVIDRL 240
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG----------GSAVINSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 241 ---LESGVTTDLEQPISLFMAVPTIYSKLIKYVEENvktekerqdiekAFQRLRLMVSGSSALPETVKNDFME-ISGHNL 316
Cdd:PRK06060 222 pvtPEAAAILSARFGPSVLYGVPNFFARVIDSCSPD------------SFRSLRCVVSAGEALELGLAERLMEfFGGIPI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMC-LSNPLHGDRVsGSVGFPLPGVQVKINAE--ASSTQNGKpvfkdntkevGELLVKGPQVFKEYFEKKE 393
Cdd:PRK06060 290 LDGIGSTEVGQTfVSNRVDEWRL-GTLGRVLPPYEIRVVAPdgTTAGPGVE----------GDLWVRGPAIAKGYWNRPD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 394 ATQEafEDGWFKTGDIVEKDNSTGRFKILGRSSVDIIknSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAIL 473
Cdd:PRK06060 359 SPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVI--GGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFL 434
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 330846471 474 VYKKGA--EPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNA 514
Cdd:PRK06060 435 VATSGAtiDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTP 477
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
34-464 |
9.03e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.86 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 34 TYNDLLNESAAISNQITFKKDDleqdRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKSSMVLTNK 113
Cdd:PRK06334 47 SYNQVRKAVIALATKVSKYPDQ----HIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 114 ENYSMLAEI---GRKVGVQVIEIPEIgngspNKEVQ--HKI-------MPF------------DINRNAQIIYTSGTTSR 169
Cdd:PRK06334 123 QLMQHLAQThgeDAEYPFSLIYMEEV-----RKELSfwEKCrigiymsIPFewlmrwfgvsdkDPEDVAVILFTSGTEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 170 PKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSG-----AMCEMMPkfdsKQVIDRLLESG 244
Cdd:PRK06334 198 PKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGvpvvfAYNPLYP----KKIVEMIDEAK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 245 VTtdleqpisLFMAVPTIYSKLIkyveenvKTEKERqdiEKAFQRLRLMVSGSSALPETVKNDFMEISGH-NLLERYGMT 323
Cdd:PRK06334 274 VT--------FLGSTPVFFDYIL-------KTAKKQ---ESCLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 324 EIGMCLS-NPLHGDRVSGSVGFPLPGVQVKINAEASSTqngkPVfkdNTKEVGELLVKGPQVFKEYFEKKEaTQEAFE-- 400
Cdd:PRK06334 336 ECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETKV----PV---SSGETGLVLTRGTSLFSGYLGEDF-GQGFVElg 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 401 -DGWFKTGDIVEKDNStGRFKILGRSS--VDIiknsGYKISALEIEREIL-------DHPDIEECAVLGIPNEE 464
Cdd:PRK06334 408 gETWYVTGDLGYVDRH-GELFLKGRLSrfVKI----GAEMVSLEALESILmegfgqnAADHAGPLVVCGLPGEK 476
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
59-229 |
2.01e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 79.00 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPL-SISHPPH--ELEYTITNSKSSMVLTNKENYSMLAEIGRKVGV----QVI 131
Cdd:PRK07769 80 DRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAkerpRVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 132 EIPEIgngsPNkEVQHKIMPFDINRN--AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVH 209
Cdd:PRK07769 160 AVDAV----PD-EVGATWVPPEANEDtiAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDM 234
|
170 180
....*....|....*....|
gi 330846471 210 GLINILTCSLWSGAMCEMMP 229
Cdd:PRK07769 235 GLITVLLPALLGHYITFMSP 254
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
11-527 |
2.33e-15 |
|
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: 78.35 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 11 QNALKYKNRIAIvnypHNNTQRFTYNDLLNESAAISNQITFKKDDLEqDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSI 90
Cdd:cd05918 7 ERARSQPDAPAV----CAWDGSLTYAELDRLSSRLAHHLRSLGVGPG-VFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 91 SHPPHELEYTITNSKSSMVLTNkenysmlaeigrkvgvqvieipeigngspnkevqhkimpfDINRNAQIIYTSGTTSRP 170
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTS----------------------------------------SPSDAAYVIFTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 171 KGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHH-VHgLINILTcSLWSGAM-CeMMPKFDSKQ----VIDRLlesG 244
Cdd:cd05918 122 KGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFdVS-ILEIFT-TLAAGGClC-IPSEEDRLNdlagFINRL---R 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 245 VTTdleqpisLFMaVPTIySKLIKyvEENVKTekerqdiekafqrLRLMVSGSSALPETVKNDFmeISGHNLLERYGMTE 324
Cdd:cd05918 196 VTW-------AFL-TPSV-ARLLD--PEDVPS-------------LRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 325 --IGMCLSNPLHGDRVSgSVGFPLPGVQVKINAEasstqngkpvfkDNTK-----EVGELLVKGPQVFKEYFEKKEATQE 397
Cdd:cd05918 250 ctIAATVSPVVPSTDPR-NIGRPLGATCWVVDPD------------NHDRlvpigAVGELLIEGPILARGYLNDPEKTAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 398 AF-ED-GW------------FKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDH-PDIEECAV--LGI 460
Cdd:cd05918 317 AFiEDpAWlkqegsgrgrrlYRTGDLV-RYNPDGSLEYVGRKD-TQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 461 PNEEYGQVIGAILVYK--KGAEPMSYDDF--------------KMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLV 524
Cdd:cd05918 395 KDGSSSPQLVAFVVLDgsSSGSGDGDSLFlepsdefralvaelRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALR 474
|
...
gi 330846471 525 KLF 527
Cdd:cd05918 475 ELA 477
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
31-523 |
3.98e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 78.93 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 31 QRFTYNDLLNESAAISNQitfkkddLEQ------DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNS 104
Cdd:PRK10252 482 YQFSYREMREQVVALANL-------LRErgvkpgDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 105 KSSMVLTNKEnysmlaEIGRKVGVQVIEIPEIGNGSPNKEVQHKIM--PFDInrnAQIIYTSGTTSRPKGVIATHsniea 182
Cdd:PRK10252 555 RPSLLITTAD------QLPRFADVPDLTSLCYNAPLAPQGAAPLQLsqPHHT---AYIIFTSGSTGRPKGVMVGQ----- 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 183 qvKALVEAWEWKKE-------DHILEFLPlhhvhgliniltC----SLW-------SGAmCEMMPKFDS-------KQVI 237
Cdd:PRK10252 621 --TAIVNRLLWMQNhypltadDVVLQKTP------------CsfdvSVWeffwpfiAGA-KLVMAEPEAhrdplamQQFF 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRlleSGVTTDLEQP--ISLFMAVPTIysklikyveenvktekerQDIEKAFQRLRLMVSGSSALPETVKNDFMEISG-- 313
Cdd:PRK10252 686 AE---YGVTTTHFVPsmLAAFVASLTP------------------EGARQSCASLRQVFCSGEALPADLCREWQQLTGap 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 314 -HNLlerYGMTEIGMCLSN-PLHGDRVSGSVGFPLPgvqvkInaeasstqnGKPVFkdNTK--------------EVGEL 377
Cdd:PRK10252 745 lHNL---YGPTEAAVDVSWyPAFGEELAAVRGSSVP-----I---------GYPVW--NTGlrildarmrpvppgVAGDL 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQVFKEYFEKKEATQEAFEDGWF-------KTGDIVE-KDNstGRFKILGRSSvDIIKNSGYKISALEIEREILDH 449
Cdd:PRK10252 806 YLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARwLDD--GAVEYLGRSD-DQLKIRGQRIELGEIDRAMQAL 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 450 PDIEECAVL------GIPNEEYGQVIGAILVYKKGAePMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK10252 883 PDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGL-PLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
160-441 |
8.05e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 77.37 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKE-----DHILEFLPLHHVHGLInILTCSLWSGAMCEMMpKFDSK 234
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAaltvkDVYLSYLPLAHIFDRV-IEECFIQHGAAIGFW-RGDVK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLLESgvttdleQPiSLFMAVPTI----YSKLIK------------------YVEENVKTEKERQDIEKAFQRL-- 290
Cdd:PLN02614 306 LLIEDLGEL-------KP-TIFCAVPRVldrvYSGLQKklsdggflkkfvfdsafsYKFGNMKKGQSHVEASPLCDKLvf 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 291 -----------RLMVSGSSALPETVKNDFMEISGHNLLERYGMTE--IGMCLSNPLHGDRVsGSVGFPLPGVQVKInaEA 357
Cdd:PLN02614 378 nkvkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDML-GTVGPPVPNVDIRL--ES 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 358 SSTQNGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKdNSTGRFKILGRSSvDIIKNSGYKI 437
Cdd:PLN02614 455 VPEMEYDAL---ASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEW-QPNGSMKIIDRKK-NIFKLSQGEY 529
|
....
gi 330846471 438 SALE 441
Cdd:PLN02614 530 VAVE 533
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
441-514 |
8.64e-15 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 69.11 E-value: 8.64e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330846471 441 EIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGAEPMSyDDFKMWCQQRLAYYKVPKVIQVKEEIPKNA 514
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLE-EELVAHVREELGPYAVPKEVVFVDELPKTR 73
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
317-482 |
9.67e-15 |
|
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: 76.97 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMCLSNPLHG----DRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVKGP---------- 382
Cdd:cd05967 384 IDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVLDE-----DGEPV---GPNELGNIVIKLPlppgclltlw 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 383 ---QVFKE-YFEKkeatqeafEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVL 458
Cdd:cd05967 456 kndERFKKlYLSK--------FPGYYDTGDAGYKDED-GYLFIMGRTD-DVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
170 180
....*....|....*....|....
gi 330846471 459 GIPNEEYGQVIGAILVYKKGAEPM 482
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKIT 549
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
132-431 |
1.01e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 77.08 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 132 EIPEIGNGSPnkevQHKIMPF--DInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAW-EWKKEDHILEFLPLHHV 208
Cdd:PLN02387 232 EVEKLGKENP----VDPDLPSpnDI---AVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 209 HGLINILT-----CSLWSGAMCEMMpkfDSKQVIDRllesGVTTDLE--QPiSLFMAVPTIYSKL----IKYVEENVKTE 277
Cdd:PLN02387 305 LELAAESVmaavgAAIGYGSPLTLT---DTSNKIKK----GTKGDASalKP-TLMTAVPAILDRVrdgvRKKVDAKGGLA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 278 KERQDI-------------------EKAF--------------QRLRLMVSGSSAL-PETVKndFMEIS-GHNLLERYGM 322
Cdd:PLN02387 377 KKLFDIaykrrlaaiegswfgawglEKLLwdalvfkkiravlgGRIRFMLSGGAPLsGDTQR--FINIClGAPIGQGYGL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 323 TEI--GMCLSNPlhGDRVSGSVGFPLPGVQVK-INAEAsstqnGKPVFKDNTKEVGELLVKGPQVFKEYFEKKEATQEAF 399
Cdd:PLN02387 455 TETcaGATFSEW--DDTSVGRVGPPLPCCYVKlVSWEE-----GGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVY 527
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 330846471 400 ---EDG--WFKTGDIvekdnstGRF------KILGRSSvDIIK 431
Cdd:PLN02387 528 kvdERGmrWFYTGDI-------GQFhpdgclEIIDRKK-DIVK 562
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
59-446 |
2.44e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.36 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPlsiSHPP-----HELE---YTITNSKSSMVLTNKENYSMLAEIGRKVGV-- 128
Cdd:PRK05691 65 DRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPesarrHHQErllSIIADAEPRLLLTVADLRDSLLQMEELAAAna 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 129 -QVIEIPEIGNGSPNKEVQHKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAW--EWKKEDHILEFLPL 205
Cdd:PRK05691 142 pELLCVDTLDPALAEAWQEPALQPDDI---AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 206 HHVHGLINILTCSLWSGAMCEMM-PKFdskqvidrllesgvttDLEQPISLFMAV----------PTIYSKLIkyVEENV 274
Cdd:PRK05691 219 YHDMGLIGGLLQPIFSGVPCVLMsPAY----------------FLERPLRWLEAIseyggtisggPDFAYRLC--SERVS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 275 KTEKERQDIekafQRLRLMVSGSSALPETVKNDFME------ISGHNLLERYGMTEIGMCLSNPLHGDRVS--------- 339
Cdd:PRK05691 281 ESALERLDL----SRWRVAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaeal 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 340 ---------GSV----GFPLPGVQVKInAEASSTQngkpVFKDNtkEVGELLVKGPQVFKEYFEKKEATQEAF--EDG-- 402
Cdd:PRK05691 357 arnraepgtGSVlmscGRSQPGHAVLI-VDPQSLE----VLGDN--RVGEIWASGPSIAHGYWRNPEASAKTFveHDGrt 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 330846471 403 WFKTGDI-VEKDNS---TGRFKilgrssvDIIKNSGYKISALEIEREI 446
Cdd:PRK05691 430 WLRTGDLgFLRDGElfvTGRLK-------DMLIVRGHNLYPQDIEKTV 470
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
322-512 |
4.19e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 75.18 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 322 MTEIGMCLSNPLHG--DRVSGSVGFPLPGVQVKINAEasstqNGKPVfKDNTKevGELLVKGP------------QVFKE 387
Cdd:PRK00174 404 QTETGGIMITPLPGatPLKPGSATRPLPGIQPAVVDE-----EGNPL-EGGEG--GNLVIKDPwpgmmrtiygdhERFVK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 388 -YFEKkeatqeaFEDGWFkTGDIVEKDnSTGRFKILGRssVD-IIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEY 465
Cdd:PRK00174 476 tYFST-------FKGMYF-TGDGARRD-EDGYYWITGR--VDdVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIK 544
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 330846471 466 GQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPK 512
Cdd:PRK00174 545 GQGIYAFVTLKGGEEPSDelRKELRNWVRKEIGPIAKPDVIQFAPGLPK 593
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
151-501 |
6.09e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 74.14 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLiNILTCSLWSGAMCEMMPK 230
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQ-GIVWRWLYAGATLVVRDK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 231 FDSKQVIdrlleSGVTTdleqpISLfmaVPTIYSKLIKYVEENVKTekerqdieKAFqrlrLMvsGSSALPetvkndfme 310
Cdd:PRK09029 210 QPLEQAL-----AGCTH-----ASL---VPTQLWRLLDNRSEPLSL--------KAV----LL--GGAAIP--------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 isgHNLLER-----------YGMTEIG--MCLSnplHGDRVSGsVGFPLPGVQVKInaeasstqngkpvfkdntkEVGEL 377
Cdd:PRK09029 254 ---VELTEQaeqqgircwcgYGLTEMAstVCAK---RADGLAG-VGSPLPGREVKL-------------------VDGEI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 378 LVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNstGRFKILGRssvdiIKN----SGYKISALEIEREILDHPDIE 453
Cdd:PRK09029 308 WLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQN--GELTILGR-----LDNlffsGGEGIQPEEIERVINQHPLVQ 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 330846471 454 ECAVLGIPNEEYGQVIGAILVYKKGAEPMSYDDfkmWCQQRLAYYKVP 501
Cdd:PRK09029 381 QVFVVPVADAEFGQRPVAVVESDSEAAVVNLAE---WLQDKLARFQQP 425
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
161-526 |
7.25e-14 |
|
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: 73.54 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 161 IYTSGTTSRPKGVIATHSNIeaqVKALVEAWEW---KKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:cd05940 87 IYTSGTTGLPKAAIISHRRA---WRGGAFFAGSggaLPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFW 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTtdleqpislfmAVPTIySKLIKYVEENVKTEKERQdiekafQRLRlMVSGSSALPEtVKNDFMEISG-HNL 316
Cdd:cd05940 164 DDIRKYQAT-----------IFQYI-GELCRYLLNQPPKPTERK------HKVR-MIFGNGLRPD-IWEEFKERFGvPRI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMCLSNPlhgDRVSGSVGFpLPGVQ--------VKINAEasstqNGKPV-------FKDNTKEVGELL--V 379
Cdd:cd05940 224 AEFYAATEGNSGFINF---FGKPGAIGR-NPSLLrkvaplalVKYDLE-----SGEPIrdaegrcIKVPRGEPGLLIsrI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 380 KGPQVFKEYFEKKEAT----QEAFEDG--WFKTGDIVeKDNSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIE 453
Cdd:cd05940 295 NPLEPFDGYTDPAATEkkilRDVFKKGdaWFNTGDLM-RLDGEGFWYFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330846471 454 ECAVLG--IPNEEyGQVIGAILVYKKGaEPMSYDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:cd05940 373 EANVYGvqVPGTD-GRAGMAAIVLQPN-EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
158-525 |
5.38e-13 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 71.44 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFW 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTtdleqpisLFMAVptiySKLIKYVEENVKTEKERQdiekafQRLRLMVsGSSALPEtVKNDFMEISG-HNL 316
Cdd:PRK08279 282 DDVRRYRAT--------AFQYI----GELCRYLLNQPPKPTDRD------HRLRLMI-GNGLRPD-IWDEFQQRFGiPRI 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 317 LERYGMTEIGMCLSNPlhgDRVSGSVGF-PLPGVQ----VKINAEasstqNGKPVFKDN-------TKEVGELLVK---- 380
Cdd:PRK08279 342 LEFYAASEGNVGFINV---FNFDGTVGRvPLWLAHpyaiVKYDVD-----TGEPVRDADgrcikvkPGEVGLLIGRitdr 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 381 GPqvfkeyFE---KKEAT-----QEAFEDG--WFKTGDIVEKDN-----------STGRFKilgrssvdiiknsGYKISA 439
Cdd:PRK08279 414 GP------FDgytDPEASekkilRDVFKKGdaWFNTGDLMRDDGfghaqfvdrlgDTFRWK-------------GENVAT 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 440 LEIEREILDHPDIEECAVLG--IPNEEyGQVIGAILVYKKGAEPmsydDFKMWCQ---QRLAYYKVPKVIQVKEEIPKNA 514
Cdd:PRK08279 475 TEVENALSGFPGVEEAVVYGveVPGTD-GRAGMAAIVLADGAEF----DLAALAAhlyERLPAYAVPLFVRLVPELETTG 549
|
410
....*....|.
gi 330846471 515 MLKVNKKDLVK 525
Cdd:PRK08279 550 TFKYRKVDLRK 560
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
158-424 |
8.15e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.89 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVI 237
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTTDLEQpISLFMAVptiYSKLIKYVEenvktekerqdiekaFQRLRLMVSGSSALPETVKNDFMEISGHNLL 317
Cdd:PRK08043 448 PELVYDRNCTVLFG-TSTFLGN---YARFANPYD---------------FARLRYVVAGAEKLQESTKQLWQDKFGLRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 318 ERYGMTEIGMCLSNPLHGDRVSGSVGFPLPGVQVKINAEASSTQNGKpvfkdntkevgeLLVKGPQVFKEYF--EK---- 391
Cdd:PRK08043 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGR------------LQLKGPNIMNGYLrvEKpgvl 576
|
250 260 270
....*....|....*....|....*....|....*..
gi 330846471 392 ----KEATQEAFEDGWFKTGDIVEKDnSTGRFKILGR 424
Cdd:PRK08043 577 evptAENARGEMERGWYDTGDIVRFD-EQGFVQIQGR 612
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
59-481 |
1.98e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 69.65 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHP-------PHELEYTITNSKSSMVLTNKENYSMLAEI-----GRKV 126
Cdd:PRK09192 75 DRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPAAIITPDELLPWVNEAthgnpLLHV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 127 G--VQVIEIPEIGNGSPnkevqhKIMPFDInrnAQIIYTSGTTSRPKGVIATHSNIEAQVKALV-EAWEWKKEDHILEFL 203
Cdd:PRK09192 155 LshAWFKALPEADVALP------RPTPDDI---AYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 204 PLHHVHGLINILtcslwsgamceMMPkfdskqvidrlLESGVTTDLeQPISLFMAVPTIYSKLIKYVEENVK-------- 275
Cdd:PRK09192 226 PFYHDMGLVGFL-----------LTP-----------VATQLSVDY-LPTRDFARRPLQWLDLISRNRGTISysppfgye 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 276 --TEKERQDIEKAFQRLRLMVSGSSA---LPETVKNdFME------ISGHNLLERYGMTEIGMCLSNPLHG--------- 335
Cdd:PRK09192 283 lcARRVNSKDLAELDLSCWRVAGIGAdmiRPDVLHQ-FAEafapagFDDKAFMPSYGLAEATLAVSFSPLGsgivveevd 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 336 -DRVSGS------------------VGFPLPGVQVKINAEAsstqnGKPVfkdNTKEVGELLVKGPQVFKEYFEKKEATQ 396
Cdd:PRK09192 362 rDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEA-----GMPL---PERVVGHICVRGPSLMSGYFRDEESQD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 397 EAFEDGWFKTGDIVEKDNstGRFKILGRSSVDIIKNsGYKISALEIEREILDHPDIE--ECAVLGIPNEEYGQVIgaILV 474
Cdd:PRK09192 434 VLAADGWLDTGDLGYLLD--GYLYITGRAKDLIIIN-GRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV--LLV 508
|
....*..
gi 330846471 475 YKKGAEP 481
Cdd:PRK09192 509 QCRISDE 515
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
151-530 |
7.56e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.84 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 151 PFDINRNAQIIYTSGTTSRPKGVIatHSNIEAQVkALVEAWEWKKEDHILEFLPLHHVHGLINI---LTCSLWSGAMCEM 227
Cdd:PTZ00237 250 PVESSHPLYILYTSGTTGNSKAVV--RSNGPHLV-GLKYYWRSIIEKDIPTVVFSHSSIGWVSFhgfLYGSLSLGNTFVM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 228 mpkFDSKQVIDRLLESGVTTDLEQ-PISLFMAVPTIYSKLIKYvEENVKTEKERQDIekafQRLRLMVSGSSALPETVKN 306
Cdd:PTZ00237 327 ---FEGGIIKNKHIEDDLWNTIEKhKVTHTLTLPKTIRYLIKT-DPEATIIRSKYDL----SNLKEIWCGGEVIEESIPE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 307 DFMEISGHNLLERYGMTEIGMC-LSNPLHGDRVSGSVGFPLPGVQVKINAEasstqNGKPVfkdNTKEVGELLVK--GPQ 383
Cdd:PTZ00237 399 YIENKLKIKSSRGYGQTEIGITyLYCYGHINIPYNATGVPSIFIKPSILSE-----DGKEL---NVNEIGEVAFKlpMPP 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 384 VFKEYFEKKEatqEAFED------GWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAV 457
Cdd:PTZ00237 471 SFATTFYKND---EKFKQlfskfpGYYNSGDLGFKDEN-GYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLVLECCS 545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 458 LGIPNEEYGQVIGAILVYKKGAEPMSYDDFKMWCQ------QRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKLFTQN 530
Cdd:PTZ00237 546 IGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEinniitQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDS 624
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
160-526 |
4.08e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 65.69 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 160 IIYTSGTTSRPKGVIATHSNIEAQVKALVE-AWEWKKED--------------HILEFLPLhhvhglINILTCSLWSGAm 224
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTDvywctadcgwitghSYVTYGPM------LNGATVLVFEGA- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 225 cemmPKF-DSKQVIDRLLESGVTtdleqpisLFMAVPTIYSKLIKYVEENVKTekerqdiekaFQRLRLMVSGSSALP-- 301
Cdd:PLN02654 353 ----PNYpDSGRCWDIVDKYKVT--------IFYTAPTLVRSLMRDGDEYVTR----------HSRKSLRVLGSVGEPin 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 302 ETVKNDFMEISGHN---LLERYGMTEIGMCLSNPLHG--DRVSGSVGFPLPGVQVKINAEasstqNGKPVFKDNTkevGE 376
Cdd:PLN02654 411 PSAWRWFFNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDE-----KGKEIEGECS---GY 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 377 LLVKG--PQVFKEYF---EKKEATQEAFEDGWFKTGDIVEKDNStGRFKILGRSSvDIIKNSGYKISALEIEREILDHPD 451
Cdd:PLN02654 483 LCVKKswPGAFRTLYgdhERYETTYFKPFAGYYFSGDGCSRDKD-GYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQ 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330846471 452 IEECAVLGIPNEEYGQVIGAILVYKKGaEPMSYDDFK---MWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEG-VPYSEELRKsliLTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
17-458 |
2.41e-10 |
|
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: 62.49 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 17 KNRIAIVNYPHNNTQRFTYNDLLNESAAISNQITfKKDDLEQDRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHE 96
Cdd:cd17654 1 PDRPALIIDQTTSDTTVSYADLAEKISNLSNFLR-KKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 97 LEYTITNSKSSMVLTNKENYSMLAeigrkvgvqvieipeigngSPNKEVQHKIMPFDINRnAQIIYTSGTTSRPKGVIAT 176
Cdd:cd17654 80 SLTVMKKCHVSYLLQNKELDNAPL-------------------SFTPEHRHFNIRTDECL-AYVIHTSGTTGTPKIVAVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 177 HSNIEAQVKALVEAWEWKKEDhILEFLPLHHVHGLINILTCSLWSGAMCEMMPkfDSKQVIDRLLESgvTTDLEQPISLF 256
Cdd:cd17654 140 HKCILPNIQHFRSLFNITSED-ILFLTSPLTFDPSVVEIFLSLSSGATLLIVP--TSVKVLPSKLAD--ILFKRHRITVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 257 MAVPTIY----SKLIKyvEENVKtekerqdiekAFQRLRLMVSGSSALP-----ETVKNDFMEISGHNLlerYGMTEIGm 327
Cdd:cd17654 215 QATPTLFrrfgSQSIK--STVLS----------ATSSLRVLALGGEPFPslvilSSWRGKGNRTRIFNI---YGITEVS- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 328 CLSNPLHGDRVSGSV--GFPLPGVQVKINAEASSTQNGKpVFKDNTKEVGELlvkgpqvfKEYFEKKEATqeafedgWFK 405
Cdd:cd17654 279 CWALAYKVPEEDSPVqlGSPLLGTVIEVRDQNGSEGTGQ-VFLGGLNRVCIL--------DDEVTVPKGT-------MRA 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 330846471 406 TGDIVEKDNstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVL 458
Cdd:cd17654 343 TGDFVTVKD--GELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAVT 392
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
340-479 |
4.60e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 62.27 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 340 GSVGFPLPGVQVKINAEASstqnGKPVfKDNTKevGELLVKGP-------------QVF-KEYFEkkeatqeAFEDGWFK 405
Cdd:PRK10524 411 GSPGVPMYGYNVKLLNEVT----GEPC-GPNEK--GVLVIEGPlppgcmqtvwgddDRFvKTYWS-------LFGRQVYS 476
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330846471 406 TGD--IVEKDnstGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLGIPNEEYGQVIGAILVYKKGA 479
Cdd:PRK10524 477 TFDwgIRDAD---GYYFILGRTD-DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSD 548
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
30-526 |
4.30e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 58.59 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 30 TQRFTYNDLLNESAAISN---QITFKKDDLeqdrVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYTITNSKS 106
Cdd:cd05939 1 DRHWTFRELNEYSNKVANffqAQGYRSGDV----VALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 107 SMVLTNKENYSMLAeigrkvgvqvieIPEIGNGSPNKEVQHKIMpfdinrnaqIIYTSGTTSRPKGVIATHSNIEAQVKA 186
Cdd:cd05939 77 KALIFNLLDPLLTQ------------SSTEPPSQDDVNFRDKLF---------YIYTSGTTGLPKAAVIVHSRYYRIAAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 187 LVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWSGAMCEMMPKFDSKQVIDRLLESGVTtdLEQPIslfmavptiySKL 266
Cdd:cd05939 136 AYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCT--IVQYI----------GEI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 267 IKYVEENVKTEKERQdiekafQRLRLMVsgSSALPETVKNDFMEISG-HNLLERYGMTEigmCLSNPLHGDRVSGSVGFP 345
Cdd:cd05939 204 CRYLLAQPPSEEEQK------HNVRLAV--GNGLRPQIWEQFVRRFGiPQIGEFYGATE---GNSSLVNIDNHVGACGFN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 346 ---LPGVQ----VKIN---AEASSTQNGKPVfKDNTKEVGELLVKGPQ-----VFKEYFEKKEATQEAFE------DGWF 404
Cdd:cd05939 273 sriLPSVYpirlIKVDedtGELIRDSDGLCI-PCQPGEPGLLVGKIIQndplrRFDGYVNEGATNKKIARdvfkkgDSAF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 405 KTGDIVEKDNsTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPDIEECAVLG--IPNEEYGQVIGAILVYKKGAEPm 482
Cdd:cd05939 352 LSGDVLVMDE-LGYLYFKDRTG-DTFRWKGENVSTTEVEGILSNVLGLEDVVVYGveVPGVEGRAGMAAIVDPERKVDL- 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 330846471 483 syDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDLVKL 526
Cdd:cd05939 429 --DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-523 |
7.97e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 158 AQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHILEFLPLHHVHGLINILTCSLWsGAMCEMMPK---FDSK 234
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNaiaHDPQ 3950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 235 QVIDRLLESGVTTdLEqpislfmAVPTIYSKLIkyveenvktEKERQdiekAFQRLRLMVSGSSALPETVkndfmeisGH 314
Cdd:PRK05691 3951 GLLAHVQAQGITV-LE-------SVPSLIQGML---------AEDRQ----ALDGLRWMLPTGEAMPPEL--------AR 4001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 315 NLLERYgmTEIGmcLSNPLHGDRVSGSVGFplpgvqvkINAEASSTQN-----GKPVfkDNTK--------------EVG 375
Cdd:PRK05691 4002 QWLQRY--PQIG--LVNAYGPAECSDDVAF--------FRVDLASTRGsylpiGSPT--DNNRlylldealelvplgAVG 4067
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 376 ELLVKGPQVFKEYFEKKEATQEAF--------EDGWFKTGDIVEKdNSTGRFKILGRssVD-IIKNSGYKISALEIEREI 446
Cdd:PRK05691 4068 ELCVAGTGVGRGYVGDPLRTALAFvphpfgapGERLYRTGDLARR-RSDGVLEYVGR--IDhQVKIRGYRIELGEIEARL 4144
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330846471 447 LDHPDIEECAVlGIPNEEYGQVIGAILVYKKGAEPMS--YDDFKMWCQQRLAYYKVPKVIQVKEEIPKNAMLKVNKKDL 523
Cdd:PRK05691 4145 HEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGalLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
59-212 |
1.30e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 57.26 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEYT---ITNSKSSMVLTNKenySMLAEIGRKVGVQ------ 129
Cdd:PRK05850 60 DRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTS---AVVDDVTEYVAPQpgqsap 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 130 -VIEIPEIGNGSPNKEVqhkIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKEDH------ILEF 202
Cdd:PRK05850 137 pVIEVDLLDLDSPRGSD---ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVpppdttVVSW 213
|
170
....*....|
gi 330846471 203 LPLHHVHGLI 212
Cdd:PRK05850 214 LPFYHDMGLV 223
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
59-229 |
2.39e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 56.67 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 59 DRVSFLYPQSFDYVRTQWGIWRSGGVAVPL-SISHPPH--ELEYTITNSKSSMVLTN---KENY-SMLAEIGRKVGVQVI 131
Cdd:PRK12476 93 DRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPGHaeRLDTALRDAEPTVVLTTtaaAEAVeGFLRNLPRLRRPRVI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 132 EIPEIgngsPNKE-VQHKIMPFDINRNAQIIYTSGTTSRPKGVIATHSNIEAQVKALVEAWEWKKED-HILEFLPLHHVH 209
Cdd:PRK12476 173 AIDAI----PDSAgESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNtHGVSWLPLYHDM 248
|
170 180
....*....|....*....|
gi 330846471 210 GLINILTCSLWSGAMCEMMP 229
Cdd:PRK12476 249 GLSMIGFPAVYGGHSTLMSP 268
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
38-457 |
2.35e-07 |
|
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: 53.51 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 38 LLNESAAISNQITFKKddLEQ------------------DRVSFLYPQSFDYVRTQWGIWRSGGVAVPLSISHPPHELEY 99
Cdd:cd05905 4 LLDSKGKEATTLTWGK--LLSraekiaavlqkkvglkpgDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 100 TITNSKSSMVLTNKENYSML----------AEIGRKVG----VQVIEIPEIGNGSPNKEVQHKIMpfDINRNAQIIYTSG 165
Cdd:cd05905 82 LLGTCKVRVALTVEACLKGLpkkllksktaAEIAKKKGwpkiLDFVKIPKSKRSKLKKWGPHPPT--RDGDTAYIEYSFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 166 TTSRPKGVIATHSNIEAQVKALVEAWEWKKEDHIleFLPLHHVHGLiniltcSLWSGAMCEMMpkfdskqvidrlleSGV 245
Cdd:cd05905 160 SDGSLSGVAVSHSSLLAHCRALKEACELYESRPL--VTVLDFKSGL------GLWHGCLLSVY--------------SGH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 246 TT------DLEQPISLFMAVPTIYS------------KLIKYVEENVKTEKERQDIekaFQRLR-LMVSG----SSALPE 302
Cdd:cd05905 218 HTilippeLMKTNPLLWLQTLSQYKvrdayvklrtlhWCLKDLSSTLASLKNRDVN---LSSLRmCMVPCenrpRISSCD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 303 TVKNDFmeiSGHNLLERYGMTEIGmCLSNPL----------------------HG-----DRVSGS------VGFPLPGV 349
Cdd:cd05905 295 SFLKLF---QTLGLSPRAVSTEFG-TRVNPFicwqgtsgpepsrvyldmralrHGvvrldERDKPNslplqdSGKVLPGA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 350 QVKI-NAEasstqnGKPVFKDNtkEVGELLVKGPQVFKEYFEKKEATQEAFEDGWFKTGDIVEKDNS---TGRFKILGRS 425
Cdd:cd05905 371 QVAIvNPE------TKGLCKDG--EIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSyarTGLLGFLRPT 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 330846471 426 S--------------VDIIKNS----GYKISALEIEREILD-HPDIEECAV 457
Cdd:cd05905 443 KctdlnveehdllfvVGSIDETlevrGLRHHPSDIEATVMRvHPYRGRCAV 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
154-525 |
2.90e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 53.06 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 154 INRNAQIIYTSGTTSRPKGVIATHSNIeAQVKALVEAWEWKKEDHILEFLPLHHVHG-LINILTCsLWSGAMCEMMPKFD 232
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSSGfLLGIGGC-IELGATCVLKPKFS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 233 SKQVIDRLLESGVTtdleqpislfmavptiyskLIKYVEE------NVKTEKERQDiekafQRLRLMVsGSSALPETVKn 306
Cdd:cd05938 221 ASQFWDDCRKHNVT-------------------VIQYIGEllrylcNQPQSPNDRD-----HKVRLAI-GNGLRADVWR- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 307 DFMEISGH-NLLERYGMTEIGMCLSNplHGDRVsGSVG---------FPLPGVQVKIN-AEASSTQNGK--PVFKDntkE 373
Cdd:cd05938 275 EFLRRFGPiRIREFYGSTEGNIGFFN--YTGKI-GAVGrvsylykllFPFELIKFDVEkEEPVRDAQGFciPVAKG---E 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 374 VGELLVKGPQV--FKEYFEKKEATQ-----EAFEDG--WFKTGDIVEKDnSTGRFKILGRSSvDIIKNSGYKISALEIEr 444
Cdd:cd05938 349 PGLLVAKITQQspFLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQD-QQNFLYFHDRVG-DTFRWKGENVATTEVA- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 445 EILDHPD-IEECAVLG--IPNEEyGQVIGAILVYKKGAEPmsydDFKMWCQQRLAY---YKVPKVIQVKEEIPKNAMLKV 518
Cdd:cd05938 426 DVLGLLDfLQEVNVYGvtVPGHE-GRIGMAAVKLKPGHEF----DGKKLYQHVREYlpaYARPRFLRIQDSLEITGTFKQ 500
|
....*..
gi 330846471 519 NKKDLVK 525
Cdd:cd05938 501 QKVRLVE 507
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
163-460 |
1.04e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 51.31 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 163 TSGTTSRPKGVIATHSNIEAQVKALVEAWEW-KKEDHILEFLPLHHVHGLINILTcSLWSGAMCEMMPK--FDSKQV--I 237
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLdAATDVGCSWLPLYHDMGLAFLLT-AALAGAPLWLAPTtaFSASPFrwL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 238 DRLLESGVTtdleqpislFMAVPTI-YSKLIKYveenvktekERQDIEKAFQRLRLMVSGSsalpETVKNDFME------ 310
Cdd:PRK05851 239 SWLSDSRAT---------LTAAPNFaYNLIGKY---------ARRVSDVDLGALRVALNGG----EPVDCDGFErfatam 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 311 ----ISGHNLLERYGMTEIGMCLSNPLHG-----DRVSGS----------VGFPLPGVQVKINAEASSTQNgkpvfkdNT 371
Cdd:PRK05851 297 apfgFDAGAAAPSYGLAESTCAVTVPVPGiglrvDEVTTDdgsgarrhavLGNPIPGMEVRISPGDGAAGV-------AG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330846471 372 KEVGELLVKGPQVFKEYFekKEATQEAfeDGWFKTGDIVEKdnSTGRFKILGRSSvDIIKNSGYKISALEIEREILDHPD 451
Cdd:PRK05851 370 REIGEIEIRGASMMSGYL--GQAPIDP--DDWFPTGDLGYL--VDGGLVVCGRAK-ELITVAGRNIFPTEIERVAAQVRG 442
|
....*....
gi 330846471 452 IEECAVLGI 460
Cdd:PRK05851 443 VREGAVVAV 451
|
|
| |
