|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
34-505 |
0e+00 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 584.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 34 DPSKL-LFIDGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAA 112
Cdd:PRK07514 15 DRDAPfIETPDGLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 113 HYIKDATPSILV---SCNEELDKV-FRDKIRVI---NEDKlaseAGSL-----NACTMIEHVEKS--DPASVCYTSGTTG 178
Cdd:PRK07514 94 YFIGDAEPALVVcdpANFAWLSKIaAAAGAPHVetlDADG----TGSLleaaaAAPDDFETVPRGadDLAAILYTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 179 LPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKNATVMMG 258
Cdd:PRK07514 170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRATVMMG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 259 VPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQG 338
Cdd:PRK07514 250 VPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 339 VGCRIAKN-----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLN 407
Cdd:PRK07514 330 VSLRVTDPetgaelppgeiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 408 VYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkLIGIMKKKVANYKVPKRVIVLDDLPRN 486
Cdd:PRK07514 410 VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlDEAA----ILAALKGRLARFKQPKRVFFVDELPRN 485
|
490
....*....|....*....
gi 32563687 487 HITKVQKNVLRDTYKNLFA 505
Cdd:PRK07514 486 TMGKVQKNLLREQYADLFA 504
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
37-498 |
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: 528.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 37 KLLFIDGDRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIK 116
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 117 DATPSILVscneeldkvfrdkirvinedklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLSNNAHD 196
Cdd:cd05941 82 DSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 197 IVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKF--EVEDCIKYMKNATVMMGVPTFFSRLLASKNFN- 273
Cdd:cd05941 121 LVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFdpKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHf 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 274 -------KEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIA-- 344
Cdd:cd05941 201 tdpqfarAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVde 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 ---------KNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVI-TGGLNVYPKELE 414
Cdd:cd05941 281 etgeplprgEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 415 DFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT--DEKEFEKKLigimKKKVANYKVPKRVIVLDDLPRNHITKVQ 492
Cdd:cd05941 361 RVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAalSLEELKEWA----KQRLAPYKRPRRLILVDELPRNAMGKVN 436
|
....*.
gi 32563687 493 KNVLRD 498
Cdd:cd05941 437 KKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
28-501 |
1.33e-149 |
|
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: 435.39 E-value: 1.33e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:COG0318 6 RRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVScneeldkvfrdkirvinedklaseagslnactmiehveksdpASVCYTSGTTGLPKGAILTH 187
Cdd:COG0318 85 AEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMK--NATVMMGVPTFFSR 265
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIEreRVTVLFGVPTMLAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 266 LLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMTTNPLN-GERKAGTVGPAVQGVGCRI 343
Cdd:COG0318 203 LLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSpVVTVNPEDpGERRPGSVGRPLPGVEVRI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 AKNGG----------IEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKEL 413
Cdd:COG0318 283 VDEDGrelppgevgeIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 414 EDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQ 492
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAElDAEE----LRAFLRERLARYKVPRRVEFVDELPRTASGKID 437
|
....*....
gi 32563687 493 KNVLRDTYK 501
Cdd:COG0318 438 RRALRERYA 446
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
28-497 |
6.67e-133 |
|
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: 393.08 E-value: 6.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVsCNEELdkvfrdkirvinEDKLASEAGSLNACTmiehVEKSDPASVCYTSGTTGLPKGAILTH 187
Cdd:cd05936 85 PRELEHILNDSGAKALI-VAVSF------------TDLLAAGAPLGERVA----LTPEDVAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSNNAHDIvRDW---GFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMK--NATVMMGVPTF 262
Cdd:cd05936 148 RNLVANALQI-KAWledLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRkhRVTIFPGVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMTTNPLNGERKAGTVGPAVQGVGC 341
Cdd:cd05936 227 YIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 342 RIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTeDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPK 411
Cdd:cd05936 307 KIVDDDGEELPPGEVgelwvrgpqvMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 412 ELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKV 491
Cdd:cd05936 386 EVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKI 462
|
....*.
gi 32563687 492 QKNVLR 497
Cdd:cd05936 463 LRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
32-493 |
7.86e-112 |
|
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: 338.05 E-value: 7.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEA 111
Cdd:cd17631 6 RRHPDRTALVFGGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 112 AHYIKDATPSILVScneeldkvfrdkirvinedklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLS 191
Cdd:cd17631 85 AYILADSGAKVLFD----------------------------------------DLALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 192 NNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE---DCIKYMKnATVMMGVPTFFSRLLA 268
Cdd:cd17631 125 WNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPEtvlDLIERHR-VTSFFLVPTMIQALLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 269 SKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERtGQVILERYGMTEAGVMTT--NPLNGERKAGTVGPAVQGVGCRIAKN 346
Cdd:cd17631 204 HPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFVEVRIVDP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 347 GGIEVKTN----------AIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDF 416
Cdd:cd17631 283 DGREVPPGevgeivvrgpHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 417 IDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQK 493
Cdd:cd17631 362 LYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAElDEDE----LIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
35-502 |
2.74e-111 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 339.47 E-value: 2.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVScNEELDKVFRD--------KIRVINEDKLASEAGSLNAC--TMIE---------HVEKSDPASVCYTSG 175
Cdd:PRK06187 99 LNDAEDRVVLV-DSEFVPLLAAilpqlptvRTVIVEGDGPAAPLAPEVGEyeELLAaasdtfdfpDIDENDAAAMLYTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNNAhDIVRDW-GFTGNDYNLHALPFYHVHGLYYSLHcSLFSHSTMIWRSKFEVEDCIKYM--KN 252
Cdd:PRK06187 178 TTGHPKGVVLSHRNLFLHS-LAVCAWlKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRFDPENLLDLIetER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 253 ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE-AGVMTTNPLN-----GE 326
Cdd:PRK06187 256 VTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtSPVVSVLPPEdqlpgQW 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 327 RKAGTVGPAVQGVGCRIAKNGG------------IEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIG 394
Cdd:PRK06187 336 TKRRSAGRPLPGVEARIVDDDGdelppdggevgeIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYIT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 395 GRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkLIGIMKKKVANYKV 473
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATlDAKE----LRAFLRGRLAKFKL 490
|
490 500
....*....|....*....|....*....
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVLRDTYKN 502
Cdd:PRK06187 491 PKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-499 |
8.19e-110 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 335.72 E-value: 8.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAhY 114
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAA-Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 I----------------------KDATPSI--LVSCNEELDKVFRDKIRVInEDKLASEAGSLNACTmiehVEKSDPASV 170
Cdd:PRK07656 97 IlargdakalfvlglflgvdysaTTRLPALehVVICETEEDDPHTEKMKTF-TDFLAAGDPAERAPE----VDPDDVADI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 CYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYM 250
Cdd:PRK07656 172 LFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 251 KN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG-QVILERYGMTEA-GVMTTNPLNGE 326
Cdd:PRK07656 252 ETerITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEAsGVTTFNRLDDD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 327 RK--AGTVGPAVQGVGCRIAKNGGIEVKTNA----------IFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIG 394
Cdd:PRK07656 332 RKtvAGTIGTAIAGVENKIVNELGEEVPVGEvgellvrgpnVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 395 GRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTdekefEKKLIGIMKKKVANYK 472
Cdd:PRK07656 412 DRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVlkPGAELT-----EEELIAYCREHLAKYK 486
|
490 500
....*....|....*....|....*..
gi 32563687 473 VPKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK07656 487 VPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
40-492 |
3.81e-101 |
|
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: 312.22 E-value: 3.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 40 FIDGDRKT--TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKD 117
Cdd:cd05911 2 QIDADTGKelTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 118 ATPSILVSCNEELDKV--------FRDKIRVINedklASEAGSLNACTM--------------IEHVEKSDPASVCYTSG 175
Cdd:cd05911 81 SKPKVIFTDPDGLEKVkeaakelgPKDKIIVLD----DKPDGVLSIEDLlsptlgeededlppPLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNN---AHDIVRDWgFTGNDYNLHALPFYHVHGLYYSLHCSLFSHsTMIWRSKFEVEDCIKYMKN 252
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANlsqVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGA-TVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 253 --ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGVMTTNPLNGERKA 329
Cdd:cd05911 235 ykITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 GTVGPAVQGVGCRIAKNGG-----------IEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSK 398
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGkdslgpnepgeICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 399 DMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEKEFEKKLIGIMKKKVANYK-VPKRV 477
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP---GEKLTEKEVKDYVAKKVASYKqLRGGV 471
|
490
....*....|....*
gi 32563687 478 IVLDDLPRNHITKVQ 492
Cdd:cd05911 472 VFVDEIPKSASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
39-404 |
6.09e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 309.63 E-value: 6.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 39 LFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDA 118
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TPSILV--------SCNEELDKVFRDKIRVINEDKLASEAGSLNACTMIEH--------VEKSDPASVCYTSGTTGLPKG 182
Cdd:pfam00501 93 GAKVLItddalkleELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADvpppppppPDPDDLAYIIYTSGTTGKPKG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 183 AILTHGSLSNNAHDI----VRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVED---CIKYMK--NA 253
Cdd:pfam00501 173 VMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDpaaLLELIEryKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGE---RKAG 330
Cdd:pfam00501 253 TVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDedlRSLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 TVGPAVQGVGCRIA-----------KNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKD 399
Cdd:pfam00501 333 SVGRPLPGTEVKIVddetgepvppgEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKD 412
|
....*
gi 32563687 400 MVITG 404
Cdd:pfam00501 413 QIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
166-492 |
9.54e-101 |
|
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: 306.13 E-value: 9.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYySLHCSLFSHSTMIWRSKFEVED 245
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 246 CIKYMKN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVM--TTN 321
Cdd:cd04433 80 ALELIERekVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTvaTGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 PLNGERKAGTVGPAVQGVGCRIAKNGG----------IEVKTNAIFAGYWKNPKKTAEeFTEDGWFKTGDVGHLDEDGYL 391
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGgelppgeigeLVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLGRLDEDGYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANY 471
Cdd:cd04433 239 YIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE---ELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 32563687 472 KVPKRVIVLDDLPRNHITKVQ 492
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
33-498 |
8.27e-98 |
|
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: 303.85 E-value: 8.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 33 SDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAA 112
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 113 HYIKDATPSILVSCNEELDKVFRDKIRV------INEDK----LASEAGSLNACT-------MIEHVEKSDPASVCYTSG 175
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGPASRAASKLglaileLALDVgvliRAPSAESLSNLLadkknakSEGVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCIKYmk 251
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSAstfwPDVRDY-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 252 NATVMMGVPTFFSRLLASKNFNKE-AFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMTTNPLN-GERK 328
Cdd:cd05926 238 NATWYTAVPTIHQILLNRPEPNPEsPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhQMTSNPLPpGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 329 AGTVGPAVqGVGCRI----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSK 398
Cdd:cd05926 318 PGSVGKPV-GVEVRIldedgeilppGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 399 DMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEK--VTdekefEKKLIGIMKKKVANYKVPKR 476
Cdd:cd05926 397 ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGasVT-----EEELRAFCRKHLAAFKVPKK 471
|
490 500
....*....|....*....|..
gi 32563687 477 VIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05926 472 VYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
43-497 |
2.88e-90 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 283.80 E-value: 2.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 43 GDRKTTYGEFVKRtgqyATALTEKynIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPS- 121
Cdd:PRK07787 22 GGRVLSRSDLAGA----ATAVAER--VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 122 ILVSCNEELDKVFRDKIRVinedklasEAGSLNActmIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDW 201
Cdd:PRK07787 96 WLGPAPDDPAGLPHVPVRL--------HARSWHR---YPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 202 GFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIK-YMKNATVMMGVPTFFSRLLASKNfNKEAFGNV 280
Cdd:PRK07787 165 QWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQaLSEGGTLYFGVPTVWSRIAADPE-AARALRGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 281 RVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKN------------GG 348
Cdd:PRK07787 244 RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEdggpvphdgetvGE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 349 IEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGR-SKDMVITGGLNVYPKELEDFIDTLPFVKESA 427
Cdd:PRK07787 324 LQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 428 VIASPHPDFGEAVVAIVVPSEKVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK07787 404 VVGVPDDDLGQRIVAYVVGADDVAAD-----ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
35-505 |
2.20e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 275.27 E-value: 2.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVmARVSKTTDT-AALYIACLQIGALYIPVNPGYTESEAAh 113
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDL-GLKKGDRV-AALGHNSDAyALLWLACARAGAVHVPVNFMLTGEELA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 114 YIKDATPSILVSCNEELDKVFRDKIRVINEDKL---------ASEAGSLNACTMIE---------HVEKSDPASVCYTSG 175
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLilslvlggrEAPGGWLDFADWAEagsvaepdvELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMK--NA 253
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEaeRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILER-YGMTEAGVMTT--NPLNGERKAG 330
Cdd:PRK08316 262 TSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNcYGQTEIAPLATvlGPEEHLRRPG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 TVGPAVQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:PRK08316 342 SAGRPVLNVETRVVDDDGNDVAPGEVgeivhrspqlMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVP-SEKVTDEKEfekkLIGIMKKKVANYKVPKRVIV 479
Cdd:PRK08316 421 IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPkAGATVTEDE----LIAHCRARLAGFKVPKRVIF 496
|
490 500
....*....|....*....|....*.
gi 32563687 480 LDDLPRNHITKVQKNVLRDTYKNLFA 505
Cdd:PRK08316 497 VDELPRNPSGKILKRELRERYAGAFT 522
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
45-499 |
2.26e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 276.88 E-value: 2.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKD------- 117
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDhgarvai 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 118 ----ATPSI-----------LVSCN--EELDKVFRDKIRV------INEDKLASEA------------GSLNACTMIEH- 161
Cdd:PRK05605 135 vwdkVAPTVerlrrttpletIVSVNmiAAMPLLQRLALRLpipalrKARAALTGPApgtvpwetlvdaAIGGDGSDVSHp 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 162 -VEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAH------DIVRDwgftGNDYNLHALPFYHVHGLYYSLHCSLFSHST 234
Cdd:PRK05605 215 rPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvPGLGD----GPERVLAALPMFHAYGLTLCLTLAVSIGGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 235 MIWRSKFEVEDCIKYMKN--ATVMMGVPTFFSRLL-ASKNFNKEAFGnVRVFISGSAPLSVSTIEEFRERTGQVILERYG 311
Cdd:PRK05605 291 LVLLPAPDIDLILDAMKKhpPTWLPGVPPLYEKIAeAAEERGVDLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 312 MTE-AGVMTTNPLNGERKAGTVGPAVQGVGCRIA------------KNGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFK 378
Cdd:PRK05605 370 LTEtSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVdpedpdetmpdgEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFR 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 379 TGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfek 458
Cdd:PRK05605 449 TGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPE--- 525
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 32563687 459 KLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK05605 526 GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
28-496 |
4.52e-79 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 255.56 E-value: 4.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVsCNEELDKV---FRDKIRVINEDKLASEAGSLNAcTMIEHVEKS--DPASVCYTSGTTGLPKG 182
Cdd:PRK06839 89 ENELIFQLKDSGTTVLF-VEKTFQNMalsMQKVSYVQRVISITSLKEIEDR-KIDNFVEKNesASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 183 AILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN--ATVMMGVP 260
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKhkVTVVMGVP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 261 TFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERtGQVILERYGMTEAG--VMTTNPLNGERKAGTVGPAVQG 338
Cdd:PRK06839 247 TIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSptVFMLSEEDARRKVGSIGKPVLF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 339 VGCR-IAKNGG---------IEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNV 408
Cdd:PRK06839 326 CDYElIDENKNkvevgevgeLLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 409 YPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTdekefEKKLIGIMKKKVANYKVPKRVIVLDDLPRN 486
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLI-----EKDVIEHCRLFLAKYKIPKEIVFLKELPKN 479
|
490
....*....|
gi 32563687 487 HITKVQKNVL 496
Cdd:PRK06839 480 ATGKIQKAQL 489
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-497 |
2.19e-78 |
|
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: 251.92 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVscn 127
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeLDKVFRDKirvinedklaseagslnactmiEHVEKSD-PASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGN 206
Cdd:cd05903 79 --VPERFRQF----------------------DPAAMPDaVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 207 DYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFI 284
Cdd:cd05903 135 DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREhgVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 285 SGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNG--ERKAGTVGPAVQGVGCRI----------AKNGGIEVK 352
Cdd:cd05903 215 CGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVvddtgatlapGVEGELLSR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 353 TNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASP 432
Cdd:cd05903 295 GPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563687 433 HPDFGEAVVAIVVPseKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05903 374 DERLGERACAVVVT--KSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
45-448 |
1.19e-77 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 254.64 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALtEKYNIKKGDRVmARVSKT------TDtaalyIACLQIGALYIPVNPGYTESEAAHYIKDA 118
Cdd:COG1022 39 QSLTWAEFAERVRALAAGL-LALGVKPGDRV-AILSDNrpewviAD-----LAILAAGAVTVPIYPTSSAEEVAYILNDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TPSIL-VSCNEELDKVFR--------DKIRVINEDKLASEAGSLN----------------ACTMIEHVEKSDPASVCYT 173
Cdd:COG1022 112 GAKVLfVEDQEQLDKLLEvrdelpslRHIVVLDPRGLRDDPRLLSldellalgrevadpaeLEARRAAVKPDDLATIIYT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 174 SGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCsLFSHSTMIWrskfeVEDcIKYMKNA 253
Cdd:COG1022 192 SGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAF-----AES-PDTLAED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 ------TVMMGVPTFFSRLLAS-------------KNFN--------------------------------------KEA 276
Cdd:COG1022 265 lrevkpTFMLAVPRVWEKVYAGiqakaeeagglkrKLFRwalavgrryararlagkspslllrlkhaladklvfsklREA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 277 FG-NVRVFISGSAPLSVSTIEEFRErTGQVILERYGMTE-AGVMTTNPLnGERKAGTVGPAVQGVGCRIAKNGGIEVKTN 354
Cdd:COG1022 345 LGgRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTEtSPVITVNRP-GDNRIGTVGPPLPGVEVKIAEDGEILVRGP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 AIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT-GGLNVYPKELEDFIDTLPFVKESAVIasph 433
Cdd:COG1022 423 NVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVV---- 498
|
490
....*....|....*...
gi 32563687 434 pdfGEA---VVAIVVPSE 448
Cdd:COG1022 499 ---GDGrpfLAALIVPDF 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
42-498 |
2.49e-77 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 252.73 E-value: 2.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 42 DGDRKT-TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATP 120
Cdd:COG0365 34 DGEERTlTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 121 SILVSCNE--ELDKVFRDKIRVineDKLASEAGSLNACTMI----------------------------EHVEKSDPASV 170
Cdd:COG0365 113 KVLITADGglRGGKVIDLKEKV---DEALEELPSLEHVIVVgrtgadvpmegdldwdellaaasaefepEPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 CYTSGTTGLPKGAILTHGSL-------SNNAHDIVR--------DWGF-TGndynlhalpfyHVHGLYYSLHC------- 227
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGGYlvhaattAKYVLDLKPgdvfwctaDIGWaTG-----------HSYIVYGPLLNgatvvly 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 228 ---SLFSHSTMIWR--SKFEVedcikymknaTVMMGVPTFFSRLLASKNFNKEAFG--NVRVFISGSAPLSVSTIEEFRE 300
Cdd:COG0365 259 egrPDFPDPGRLWEliEKYGV----------TVFFTAPTAIRALMKAGDEPLKKYDlsSLRLLGSAGEPLNPEVWEWWYE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 301 RTGQVILERYGMTEAG-VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTNAI------------FAGYWKNPKKT 367
Cdd:COG0365 329 AVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEgelvikgpwpgmFRGYWNDPERY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 368 AEEF--TEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV 445
Cdd:COG0365 409 RETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 32563687 446 PSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRnhiT---KVQKNVLRD 498
Cdd:COG0365 489 LKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPK---TrsgKIMRRLLRK 541
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
46-498 |
2.80e-77 |
|
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: 248.42 E-value: 2.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 46 KTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDAtpsilvs 125
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 126 cneeldkvfrdkirvinedklaseagslnactmieHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTG 205
Cdd:cd05912 73 -----------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 206 NDYNLHALPFYHVHGLYYSLHcSLFSHSTMIWRSKFEVEDCIKYMKNA--TVMMGVPTFFSRLLasKNFNKEAFGNVRVF 283
Cdd:cd05912 118 DDNWLCALPLFHISGLSILMR-SVIYGMTVYLVDKFDAEQVLHLINSGkvTIISVVPTMLQRLL--EILGEGYPNNLRCI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 284 ISGSAPLSVSTIEEFRERtGQVILERYGMTEAG--VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGG-------IEVKTN 354
Cdd:cd05912 195 LLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQppyevgeILLKGP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 AIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHP 434
Cdd:cd05912 274 NVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDD 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563687 435 DFGEAVVAIVVPSEKVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05912 353 KWGQVPVAFVVSERPISEE-----ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
45-446 |
2.14e-76 |
|
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: 247.12 E-value: 2.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALtEKYNIKKGDRV--MARVSktTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSI 122
Cdd:cd05907 4 QPITWAEFAEEVRALAKGL-IALGVEPGDRVaiLSRNR--PEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 123 LVscneeldkvfrdkirvinedklaseagslnactmiehVE-KSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDW 201
Cdd:cd05907 81 LF-------------------------------------VEdPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 202 GFTGNDYNLHALPFYHVH----GLYYSLH---CSLFSHSTMIWRSKF-EVEdcikymknATVMMGVPTFFSRL------- 266
Cdd:cd05907 124 PATEGDRHLSFLPLAHVFerraGLYVPLLagaRIYFASSAETLLDDLsEVR--------PTVFLAVPRVWEKVyaaikvk 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 267 ----LASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRErTGQVILERYGMTE-AGVMTTNPLnGERKAGTVGPAVQGVGC 341
Cdd:cd05907 196 avpgLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTEtSAVVTLNPP-GDNRIGTVGKPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 342 RIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT-GGLNVYPKELEDFIDTL 420
Cdd:cd05907 274 RIADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKAS 353
|
410 420
....*....|....*....|....*.
gi 32563687 421 PFVKESAVIASPHPdfgeAVVAIVVP 446
Cdd:cd05907 354 PLISQAVVIGDGRP----FLVALIVP 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-486 |
1.20e-75 |
|
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: 246.76 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGD--RKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTES 109
Cdd:cd05904 16 SAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 110 EAAHYIKDATPSILVSCNEELDKVFRDKIRVI----------NEDKLASEAGSLNACTmiEHVEKSDPASVCYTSGTTGL 179
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVlldsaefdslSFSDLLFEADEAEPPV--VVIKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 180 PKGAILTHGSLSNNAHDIVRDWG--FTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN--ATV 255
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERykVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 256 MMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAG---VMTTNPLNGERKAGT 331
Cdd:cd05904 253 LPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTESTgvvAMCFAPEKDRAKYGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 332 VGPAVQGVGCRIA-----------KNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:cd05904 333 VGRLVPNVEAKIVdpetgeslppnQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKEL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkligIMK---KKVANYKVPKR 476
Cdd:cd05904 413 IKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSlTEDE-------IMDfvaKQVAPYKKVRK 485
|
490
....*....|
gi 32563687 477 VIVLDDLPRN 486
Cdd:cd05904 486 VAFVDAIPKS 495
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
48-496 |
1.97e-74 |
|
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: 241.61 E-value: 1.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDAtpsilvscn 127
Cdd:cd05935 3 TYLELLEVVKKLASFLSNK-GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeldkvfrdkirvinedklaseagslNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGND 207
Cdd:cd05935 73 --------------------------GAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 208 YNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE---DCIKYMKnATVMMGVPTFFSRLLASKNFNKEAFGNVRVFI 284
Cdd:cd05935 127 VILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDREtalELIEKYK-VTFWTNIPTMLVDLLATPEFKTRDLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 285 SGSAPLSVSTIEEFRERTGQVILERYGMTEA-GVMTTNPLnGERKAGTVGPAVQGVGCRI-----------AKNGGIEVK 352
Cdd:cd05935 206 GGGAPMPPAVAEKLLKLTGLRFVEGYGLTETmSQTHTNPP-LRPKLQCLGIP*FGVDARVidietgrelppNEVGEIVVR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 353 TNAIFAGYWKNPKKTAEEFTEDG---WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVI 429
Cdd:cd05935 285 GPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVI 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563687 430 ASPHPDFGEAVVAIVVPSE----KVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd05935 365 SVPDERVGEEVKAFIVLRPeyrgKVTEE-----DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
28-503 |
2.93e-74 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 242.56 E-value: 2.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQsdPSKLLFIDGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRVmARVSKTTDTAALYI-ACLQIGALYIPVNPGY 106
Cdd:PRK03640 11 RAFLT--PDRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVKKGDRV-ALLMKNGMEMILVIhALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 107 TESEAAHYIKDATPSILVScneelDKVFRDKIRVINEDKLAS-EAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAIL 185
Cdd:PRK03640 87 SREELLWQLDDAEVKCLIT-----DDDFEAKLIPGISVKFAElMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 186 THGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLyyslhcSLFSHS-----TMIWRSKFEVEDCIKYMKN--ATVMMG 258
Cdd:PRK03640 162 TYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL------SILMRSviygmRVVLVEKFDAEKINKLLQTggVTIISV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 259 VPTFFSRLLA---SKNFNkeafGNVRVFISGSAPLSVSTIEEFRERTGQVIlERYGMTEAG--VMTTNPLNGERKAGTVG 333
Cdd:PRK03640 236 VSTMLQRLLErlgEGTYP----SSFRCMLLGGGPAPKPLLEQCKEKGIPVY-QSYGMTETAsqIVTLSPEDALTKLGSAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 334 PAVQGVGCRIAKN---------GGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITG 404
Cdd:PRK03640 311 KPLFPCELKIEKDgvvvppfeeGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 405 GLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTdekefEKKLIGIMKKKVANYKVPKRVIVLDDLP 484
Cdd:PRK03640 390 GENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT-----EEELRHFCEEKLAKYKVPKRFYFVEELP 464
|
490
....*....|....*....
gi 32563687 485 RNHITKVQKNVLRDTYKNL 503
Cdd:PRK03640 465 RNASGKLLRHELKQLVEEM 483
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
166-497 |
3.95e-73 |
|
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: 235.25 E-value: 3.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSK-FEVE 244
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 245 DCIKYMKN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG-QVILERYGMTEAGVMTTN 321
Cdd:cd05917 83 AVLEAIEKekCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 PLNG---ERKAGTVGPAVQGVGCRIA-KNGGIEVKTNA----------IFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDE 387
Cdd:cd05917 163 TRTDdsiEKRVNTVGRIMPHTEAKIVdPEGGIVPPVGVpgelcirgysVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 388 DGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDE--KEFekkligi 463
Cdd:cd05917 243 DGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEGAELTEEdiKAY------- 315
|
330 340 350
....*....|....*....|....*....|....
gi 32563687 464 MKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05917 316 CKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
28-499 |
1.75e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 238.17 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQsdPSKLLFID--GDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPG 105
Cdd:PRK09088 4 HARLQ--PQRLAAVDlaLGRRWTYAELDALVGRLAAVL-RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 106 YTESEAAHYIKDATPSILVSCneelDKVFRDKIRVINEDKLASEAGSLNACTMiEHVEKSDPASVCYTSGTTGLPKGAIL 185
Cdd:PRK09088 81 LSASELDALLQDAEPRLLLGD----DAVAAGRTDVEDLAAFIASADALEPADT-PSIPPERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 186 THGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN----ATVMMGVPT 261
Cdd:PRK09088 156 SERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDpalgITHYFCVPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 262 FFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERtGQVILERYGMTEAGVMTTNPLNGER---KAGTVGPAVQG 338
Cdd:PRK09088 236 MAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIPTPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 339 VGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNV 408
Cdd:PRK09088 315 VQTRVVDDqgndcpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 409 YPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDDLPRNHI 488
Cdd:PRK09088 395 YPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE---RIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
490
....*....|.
gi 32563687 489 TKVQKNVLRDT 499
Cdd:PRK09088 472 GKLQKARLRDA 482
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
48-496 |
1.92e-72 |
|
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: 236.58 E-value: 1.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDaTPSILVSCN 127
Cdd:TIGR01923 1 TWQDLDCEAAHLAKAL-KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLED-LDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 EELDKVFRDKIRVINEDKLASEAGSLNACTMIEhveksDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGND 207
Cdd:TIGR01923 79 SLLEEKDFQADSLDRIEAAGRYETSLSASFNMD-----QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 208 YNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKymkNATVMMG--VPTFFSRLLASKNFNKeafgNVRVFIS 285
Cdd:TIGR01923 154 NWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLLEMIA---NERVTHIslVPTQLNRLLDEGGHNE----NLRKILL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 286 GSAPLSVSTIEEFRERtGQVILERYGMTE-AGVMTTNPLNGERKAGTVGPAVQGVGCRI-----AKNGGIEVKTNAIFAG 359
Cdd:TIGR01923 227 GGSAIPAPLIEEAQQY-GLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkvdnkEGHGEIMVKGANLMKG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 360 YWkNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEA 439
Cdd:TIGR01923 306 YL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 440 VVAIVVPSEKVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:TIGR01923 385 PVAYIVSESDISQA-----KLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-497 |
1.33e-71 |
|
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: 233.72 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL 123
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAAL-GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 VScneeldkvfrdkirvinedklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGF 203
Cdd:cd05934 80 VV----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 204 TGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCIKYmkNATVMMGVPTFFSRLLASKNFNKEAFGN 279
Cdd:cd05934 120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSAsrfwSDVRRY--GATVTNYLGAMLSYLLAQPPSPDDRAHR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 280 VRVfiSGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTN----- 354
Cdd:cd05934 198 LRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGepgel 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 --------AIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKES 426
Cdd:cd05934 276 virglrgwGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563687 427 AVIASPHPDFGEAVVAIVV--PSEKVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05934 355 AVVAVPDEVGEDEVKAVVVlrPGETLDPE-----ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
35-497 |
2.90e-68 |
|
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: 227.64 E-value: 2.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKD-------ATPSILVSCNEELDKVFRDKIRVIN-------------EDKLASEAGSLNACTmiehVEKSDPASVCYTS 174
Cdd:cd05959 97 LEDsrarvvvVSGELAPVLAAALTKSEHTLVVLIVsggagpeagalllAELVAAEAEQLKPAA----THADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKGAILTHGSLSNNAHDIVRD-WGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCI-KYMK- 251
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVfKRIRr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 252 -NATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAG 330
Cdd:cd05959 253 yRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 TVGPAVQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:cd05959 333 TTGKPVPGYEVELRDEDGGDVADGEPgelyvrgpssATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVL 480
Cdd:cd05959 412 LKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFV 491
|
490
....*....|....*..
gi 32563687 481 DDLPRNHITKVQKNVLR 497
Cdd:cd05959 492 DELPKTATGKIQRFKLR 508
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
24-498 |
1.13e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 223.76 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 24 NIVSQAQlQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVN 103
Cdd:PRK07470 11 HFLRQAA-RRFPDRIALVWGDRSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 104 PGYTESEAAhYIKDATPSILVSCNEEldkvFRDKIRVINEDKL---------ASEAGSLNACTMIEH---------VEKS 165
Cdd:PRK07470 89 FRQTPDEVA-YLAEASGARAMICHAD----FPEHAAAVRAASPdlthvvaigGARAGLDYEALVARHlgarvanaaVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSL----SNNAHDIVRdwGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKF 241
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 EVEDCIKYMKNATV--MMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEA-GVM 318
Cdd:PRK07470 242 DPAEVWALVERHRVtnLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVtGNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 319 TTNPLNG-------ERKAGTVGPAVQGVGCRIAKNGGIEVKTN----------AIFAGYWKNPKKTAEEFtEDGWFKTGD 381
Cdd:PRK07470 322 TVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPPGetgeicvigpAVFAGYYNNPEANAKAF-RDGWFRTGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkL 460
Cdd:PRK07470 401 LGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPvDEAE----L 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 32563687 461 IGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-498 |
4.05e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 223.16 E-value: 4.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCN 127
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 ---EELDKVFRDK-----IRVINEDKLASEAGSLnACTMIEHVEK--------------------------------SDP 167
Cdd:PRK12492 131 mfgKLVQEVLPDTgieylIEAKMGDLLPAAKGWL-VNTVVDKVKKmvpayhlpqavpfkqalrqgrglslkpvpvglDDI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 168 ASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYN----------LHALPFYHVHGLYYSLHCSLFS--HSTM 235
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQplmkegqevmIAPLPLYHIYAFTANCMCMMVSgnHNVL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 236 IWRSKfEVEDCIKYMKN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMT 313
Cdd:PRK12492 290 ITNPR-DIPGFIKELGKwrFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 314 EAG-VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIE----------VKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDV 382
Cdd:PRK12492 369 ETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNElplgergelcIKGPQVMKGYWQQPEATAEALDAEGWFKTGDI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 383 GHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekkLIG 462
Cdd:PRK12492 449 AVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEE----LKA 524
|
490 500 510
....*....|....*....|....*....|....*.
gi 32563687 463 IMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK12492 525 YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
45-498 |
8.85e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 222.33 E-value: 8.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 SCNEELDKVFRDKIRVINEDKLASEAGSL---------NActMIEHVEK------------------------------- 164
Cdd:PRK05677 128 CLANMAHLAEKVLPKTGVKHVIVTEVADMlpplkrlliNA--VVKHVKKmvpayhlpqavkfndalakgagqpvteanpq 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 -SDPASVCYTSGTTGLPKGAILTHGSLSNN---AHDIVRDWGFTGNDYNLHALPFYHVHGlyYSLHCSLF----SHSTMI 236
Cdd:PRK05677 206 aDDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEGCEILIAPLPLYHIYA--FTFHCMAMmligNHNILI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 WRSKfEVEDCIKYMKNA--TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE 314
Cdd:PRK05677 284 SNPR-DLPAMVKELGKWkfSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 315 AG-VMTTNPLNGERkAGTVGPAVQGVGCRIAKNGGIE----------VKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVG 383
Cdd:PRK05677 363 TSpVVSVNPSQAIQ-VGTIGIPVPSTLCKVIDDDGNElplgevgelcVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 384 HLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGI 463
Cdd:PRK05677 442 LIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEH 518
|
490 500 510
....*....|....*....|....*....|....*
gi 32563687 464 MKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK05677 519 MRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-500 |
5.16e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 219.47 E-value: 5.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 15 LRAASSAANNIVSQaqLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDT-AALYIACL 93
Cdd:PRK06188 8 LHSGATYGHLLVSA--LKRYPDRPALVLGDTRLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVlMAIGAAQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 94 QiGALYIPVNPGYTESEAAHYIKDATPSILVscneeLDKV-FRDKIRVINED-----------------KLASEAGSLNA 155
Cdd:PRK06188 85 A-GLRRTALHPLGSLDDHAYVLEDAGISTLI-----VDPApFVERALALLARvpslkhvltlgpvpdgvDLLAAAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 156 CTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLhcSLFSHSTM 235
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLP--TLLRGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 236 IWRSKFEVE---DCIKYMK-NATvmMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYG 311
Cdd:PRK06188 237 IVLAKFDPAevlRAIEEQRiTAT--FLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 312 MTEAG----VMTT--NPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTNA----------IFAGYWKNPKKTAEEFtEDG 375
Cdd:PRK06188 315 QTEAPmvitYLRKrdHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEvgeicvrgplVMDGYWNRPEETAEAF-RDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 376 WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEK 454
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAvDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 32563687 455 EfekkLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:PRK06188 474 E----LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
44-498 |
6.41e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 219.45 E-value: 6.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL 123
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 VSCNEELDKV----------------FRDKIRVINEDKLA--------------------SEAGSLNACTMIEHVEKSDP 167
Cdd:PRK08314 113 IVGSELAPKVapavgnlrlrhvivaqYSDYLPAEPEIAVPawlraepplqalapggvvawKEALAAGLAPPPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 168 ASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE--- 244
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREaaa 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 245 DCIKYMKnATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMT-TNPL 323
Cdd:PRK08314 273 RLIERYR-VTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQThSNPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 324 NgERKAGTVGPAVQGVGCRI-----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTE-DG--WFKTGDVGHLDEDG 389
Cdd:PRK08314 352 D-RPKLQCLGIPTFGVDARVidpetleelppGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 390 YLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSE----KVTDEkefekKLIGIMK 465
Cdd:PRK08314 431 YFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPeargKTTEE-----EIIAWAR 505
|
490 500 510
....*....|....*....|....*....|...
gi 32563687 466 KKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK08314 506 EHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
40-502 |
8.97e-65 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 219.54 E-value: 8.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 40 FIDGDRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDA- 118
Cdd:PRK08974 42 FINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSg 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TPSILVSCN--EELDK-VFRDKIR-VINE---DKLASEAGSL------------------NACTMIE------------- 160
Cdd:PRK08974 122 AKAIVIVSNfaHTLEKvVFKTPVKhVILTrmgDQLSTAKGTLvnfvvkyikrlvpkyhlpDAISFRSalhkgrrmqyvkp 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 161 HVEKSDPASVCYTSGTTGLPKGAILTHGSLSNN-------AHDIVRDwgftGNDYNLHALPFYHVHGLyySLHCSLFSH- 232
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqakaaYGPLLHP----GKELVVTALPLYHIFAL--TVNCLLFIEl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 233 ---STMIWRSKfEVEDCIKYMKNA--TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVIL 307
Cdd:PRK08974 276 ggqNLLITNPR-DIPGFVKELKKYpfTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 308 ERYGMTEAG-VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIE----------VKTNAIFAGYWKNPKKTAEeFTEDGW 376
Cdd:PRK08974 355 EGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEvppgepgelwVKGPQVMLGYWQRPEATDE-VIKDGW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 377 FKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEf 456
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEE- 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 32563687 457 ekkLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKN 502
Cdd:PRK08974 513 ---LITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
22-500 |
1.73e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 218.49 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 22 ANNIVSQAQLQSDPSKLLFIDgdRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIP 101
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLG--NTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 102 VNPGYTESEAAHYIKDATPSILVS-------------CNEELDKVF----RDKIRVINEDKLASEAGslnACTMIEHVEK 164
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTeaalapvatavrdIVPLLSTVVvaggSSDDSVLGYEDLLAEAG---PAHAPVDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWG-FTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSK-F- 241
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGaDINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGaFd 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 --EVEDCIKYMKNATVMMgVPTFFSRLLASKNFNKEAFgNVRVFISGSAPLSVSTIEEFRER-TGQVILERYGMTEAGVM 318
Cdd:PRK07786 254 pgQLLDVLEAEKVTGIFL-VPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEMSPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 319 TTNpLNGE---RKAGTVGPAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHL 385
Cdd:PRK07786 332 TCM-LLGEdaiRKLGSVGKVIPTVAARVVDEnmndvpvgevGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 386 DEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKvTDEKEFEkKLIGIMK 465
Cdd:PRK07786 410 DEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND-DAALTLE-DLAEFLT 487
|
490 500 510
....*....|....*....|....*....|....*
gi 32563687 466 KKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:PRK07786 488 DRLARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
166-493 |
3.71e-64 |
|
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: 211.59 E-value: 3.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTH-GSLSnnahdIVRDWG----FTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSK 240
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLR-----AAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 241 FEVEDCIKYMKN--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG-QVILERYGMTEAGV 317
Cdd:cd17638 76 FDVDAILEAIERerITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 318 MT-TNPL-NGERKAGTVGPAVQGVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGG 395
Cdd:cd17638 156 ATmCRPGdDAETVATTCGRACPGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 396 RSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPK 475
Cdd:cd17638 236 RLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEE---DVIAWCRERLANYKVPR 312
|
330
....*....|....*...
gi 32563687 476 RVIVLDDLPRNHITKVQK 493
Cdd:cd17638 313 FVRFLDELPRNASGKVMK 330
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
48-498 |
4.51e-64 |
|
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: 214.12 E-value: 4.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVscn 127
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAI------LTHGSLSNNAHDI---- 197
Cdd:cd05972 78 ----------------------------------TDAEDPALIYFTSGTTGLPKGVLhthsypLGHIPTAAYWLGLrpdd 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 198 ----VRDWGFtgndynlhalpfyhVHGLYYSLHCSLFS--HSTMIWRSKFEVEDCIKYMKN--ATVMMGVPTFFsRLLAS 269
Cdd:cd05972 124 ihwnIADPGW--------------AKGAWSSFFGPWLLgaTVFVYEGPRFDAERILELLERygVTSFCGPPTAY-RMLIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGG- 348
Cdd:cd05972 189 QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGr 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 349 -----------IEVKTNAIFAGYWKNPKKTAEEFTEDgWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFI 417
Cdd:cd05972 269 elppgeegdiaIKLPPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 418 DTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05972 348 LEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
.
gi 32563687 498 D 498
Cdd:cd05972 428 D 428
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
45-496 |
8.73e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 217.21 E-value: 8.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 ScneeLDKVFRDKIRVINEDKL---------------------------------ASEAGSLNACTMIEH-----VE--- 163
Cdd:PRK06710 127 C----LDLVFPRVTNVQSATKIehvivtriadflpfpknllypfvqkkqsnlvvkVSESETIHLWNSVEKevntgVEvpc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 164 --KSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRdWGFT---GNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWR 238
Cdd:PRK06710 203 dpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ-WLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 239 SKFEVEDCIKYMKNATVMM--GVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG 316
Cdd:PRK06710 282 PKFDMKMVFEAIKKHKVTLfpGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 317 VMT-TNPLNGERKAGTVG---PAVQ--------GVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGH 384
Cdd:PRK06710 362 PVThSNFLWEKRVPGSIGvpwPDTEamimsletGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 385 LDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEKEFEKKLIGIM 464
Cdd:PRK06710 441 MDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTECSEEELNQFA 517
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 465 KKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK06710 518 RKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
42-498 |
2.90e-63 |
|
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: 214.42 E-value: 2.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 42 DGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPS 121
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 122 ILVSCNEELDKVfrDKIR---------VINEDKLASEAGS----------LNACTMIEH---VEKSDPASVCYTSGTTGL 179
Cdd:cd12119 100 VVFVDRDFLPLL--EAIAprlptvehvVVMTDDAAMPEPAgvgvlayeelLAAESPEYDwpdFDENTAAAICYTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 180 PKGAILTH-----GSLSNNAHDIVrdwGFTGNDYNLHALPFYHVH--GLYYSlhcSLFSHSTMIWRSKF-EVEDCIKYMK 251
Cdd:cd12119 178 PKGVVYSHrslvlHAMAALLTDGL---GLSESDVVLPVVPMFHVNawGLPYA---AAMVGAKLVLPGPYlDPASLAELIE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 252 --NATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVIlERYGMTEAGVMTT--NPLNGER 327
Cdd:cd12119 252 reGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVI-HAWGMTETSPLGTvaRPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 328 KAG---------TVGPAVQGVGCRIAKNGG------------IEVKTNAIFAGYWKNPKkTAEEFTEDGWFKTGDVGHLD 386
Cdd:cd12119 331 NLSedeqlalraKQGRPVPGVELRIVDDDGrelpwdgkavgeLQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 387 EDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEKEFEKKLIGIMKK 466
Cdd:cd12119 410 EDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE---GATVTAEELLEFLAD 486
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 467 KVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd12119 487 KVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
44-499 |
3.77e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 212.71 E-value: 3.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDA----- 118
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSgvrwv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 ------------------TPSILVSCNEELDKVFRDKIR------------VINEDKLASEAGSLNACTMIE---HVEKS 165
Cdd:PRK12583 122 icadafktsdyhamlqelLPGLAEGQPGALACERLPELRgvvslapapppgFLAWHELQARGETVSREALAErqaSLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSkfEVED 245
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPN--EAFD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 246 CIKYMK-----NATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPlsvSTIEEFRERTGQV----ILERYGMTEAG 316
Cdd:PRK12583 280 PLATLQaveeeRCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAP---CPIEVMRRVMDEMhmaeVQIAYGMTETS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 317 VMT-----TNPLngERKAGTVGPAVQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDGWFKTGD 381
Cdd:PRK12583 357 PVSlqttaADDL--ERRVETVGRTQPHLEVKVVDPDGATVPRGEIgelctrgysvMKGYWNNPEATAESIDEDGWMHTGD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDE--KEFe 457
Cdd:PRK12583 435 LATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRlhPGHAASEEelREF- 513
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32563687 458 kkligiMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK12583 514 ------CKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
40-497 |
1.55e-61 |
|
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: 207.70 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 40 FIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDAT 119
Cdd:cd05919 4 FYAADRSVTYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 120 PSILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVR 199
Cdd:cd05919 83 ARLVV-------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 200 DW-GFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMI----WRSKFEVEDCIKYMKnATVMMGVPTFFSRLLASKNFNK 274
Cdd:cd05919 126 EAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVlnpgWPTAERVLATLARFR-PTVLYGVPTFYANLLDSCAGSP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 275 EAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRI----------A 344
Cdd:cd05919 205 DALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLvdeeghtippG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 KNGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVK 424
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563687 425 ESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05919 364 EAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
44-500 |
1.76e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 209.37 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL 123
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 VsCNEELDKVFRDKIRVINED--KLASEAGSLNACTMIEHVEKSDPAS----------VCYTSGTTGLPKGAI--LTHGS 189
Cdd:PRK08276 88 I-VSAALADTAAELAAELPAGvpLLLVVAGPVPGFRSYEEALAAQPDTpiadetagadMLYSSGTTGRPKGIKrpLPGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 190 LSNNAHDIVR--DWGFTGNDYNLHAL--PFYHVHGLYYSLHCSLFSHsTMIWRSKFEVEDCIKYMKN--ATVMMGVPTFF 263
Cdd:PRK08276 167 PDEAPGMMLAllGFGMYGGPDSVYLSpaPLYHTAPLRFGMSALALGG-TVVVMEKFDAEEALALIERyrVTHSQLVPTMF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 264 SRLLASKNFNKEAF--GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTT-NPLNGERKAGTVGPAVQGV- 339
Cdd:PRK08276 246 VRMLKLPEEVRARYdvSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTViTSEDWLAHPGSVGKAVLGEv 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 340 ------GCRIAKN--GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPK 411
Cdd:PRK08276 326 rildedGNELPPGeiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 412 ELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKV 491
Cdd:PRK08276 406 EIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
....*....
gi 32563687 492 QKNVLRDTY 500
Cdd:PRK08276 486 YKRRLRDRY 494
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
35-500 |
4.35e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 208.20 E-value: 4.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVScNEELDKV--FRDKIRVINEDKLASE---AGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGS 189
Cdd:PRK06145 95 LGDAGAKLLLV-DEEFDAIvaLETPKIVIDAAAQADSrrlAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 190 LSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKNATVMMG--VPTFFSRLL 267
Cdd:PRK06145 174 LHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAwmAPVMLSRVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 268 ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRER-TGQVILERYGMTEAGVMTTNPLNGER--KAGTVGPAVQGVGCRIA 344
Cdd:PRK06145 254 TVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 ----------KNGGIEVKTNAIFAGYWKNPKKTAEEFTeDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELE 414
Cdd:PRK06145 334 dgagrwlppnMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 415 DFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKN 494
Cdd:PRK06145 413 RVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKR 489
|
....*.
gi 32563687 495 VLRDTY 500
Cdd:PRK06145 490 VLRDEL 495
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
38-504 |
6.96e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 209.28 E-value: 6.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 38 LLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAH---- 113
Cdd:PRK08315 35 LVYRDQGLRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYalnq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 114 ----------------YI----------KDATPSILVSCNE-ELDKVFR---DKIR-VINEDKLASEAGSLNAcTMIEHV 162
Cdd:PRK08315 114 sgckaliaadgfkdsdYVamlyelapelATCEPGQLQSARLpELRRVIFlgdEKHPgMLNFDELLALGRAVDD-AELAAR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 EKS----DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYH----VHGlyySLHCslFSH-S 233
Cdd:PRK08315 193 QATldpdDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHcfgmVLG---NLAC--VTHgA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 234 TMIWRS-KF---------EVEDCikymknaTVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG 303
Cdd:PRK08315 268 TMVYPGeGFdplatlaavEEERC-------TALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 304 -QVILERYGMTEAG-VMT----TNPLngERKAGTVGPAVQGVGCRIaknggIEVKTNAIFA----------------GYW 361
Cdd:PRK08315 341 mSEVTIAYGMTETSpVSTqtrtDDPL--EKRVTTVGRALPHLEVKI-----VDPETGETVPrgeqgelctrgysvmkGYW 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 362 KNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVV 441
Cdd:PRK08315 414 NDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVC 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 442 AIVVPSEKVT----DEKEFekkligiMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKNLF 504
Cdd:PRK08315 494 AWIILRPGATlteeDVRDF-------CRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEEL 553
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
45-499 |
8.26e-61 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 208.75 E-value: 8.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 scneeLDKVFRD------------------KIRVINEDklasEAGSLNACTMIEHVEKS------------DPASVC--- 171
Cdd:PRK13295 133 -----VPKTFRGfdhaamarrlrpelpalrHVVVVGGD----GADSFEALLITPAWEQEpdapailarlrpGPDDVTqli 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 172 YTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMK 251
Cdd:PRK13295 204 YTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 252 N--ATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNG--ER 327
Cdd:PRK13295 284 TegVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDpdER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 328 KAGTVGPAVQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFteDGWFKTGDVGHLDEDGYLTIGGRS 397
Cdd:PRK13295 364 ASTTDGCPLPGVEVRVVDADGAPLPAGQIgrlqvrgcsnFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRS 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 398 KDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDE--KEFEKkligimKKKVANYKV 473
Cdd:PRK13295 442 KDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVprPGQSLDFEemVEFLK------AQKVAKQYI 515
|
490 500
....*....|....*....|....*.
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK13295 516 PERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
166-498 |
1.57e-60 |
|
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: 201.79 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAhDIVRDW-GFTGNDYNLHALPFYHVHGLYyslhcslfshstMIWRS----- 239
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASA-AGLHSRlGFGGGDSWLLSLPLYHVGGLA------------ILVRSllaga 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 240 KFEVEDCIKYMKNATVMMG------VPTFFSRLLASKnFNKEAFGNVRVFISGSAPLSVSTIEEFRERtGQVILERYGMT 313
Cdd:cd17630 68 ELVLLERNQALAEDLAPPGvthvslVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 314 E-AGVMTTNPLNGErKAGTVGPAVQGVGCRIAKNGGIEVKTNAIFAGYWKNPkkTAEEFTEDGWFKTGDVGHLDEDGYLT 392
Cdd:cd17630 146 EtASQVATKRPDGF-GRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 393 IGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEkefekKLIGIMKKKVANYK 472
Cdd:cd17630 223 VLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA-----ELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*.
gi 32563687 473 VPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
35-498 |
2.26e-59 |
|
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: 203.30 E-value: 2.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAhY 114
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA-F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEELDKvfrdkirvinEDKLASEAGSLNActmIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd12118 96 ILRHSEAKVLFVDREFEY----------EDLLAEGDPDFEW---IPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRsKFEVE---DCIKyMKNATVMMGVPTFFSRLLASKN 271
Cdd:cd12118 163 LANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLR-KVDAKaiyDLIE-KHKVTHFCGAPTVLNMLANAPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 272 FNKEAF-GNVRVFISGSAPlSVSTIEEFrERTGQVILERYGMTEA-GVMTTNP-------LNGERKAGTVgpAVQGVgcR 342
Cdd:cd12118 241 SDARPLpHRVHVMTAGAPP-PAAVLAKM-EELGFDVTHVYGLTETyGPATVCAwkpewdeLPTEERARLK--ARQGV--R 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 343 IAKNGGIEV-------------KT--------NAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMV 401
Cdd:cd12118 315 YVGLEEVDVldpetmkpvprdgKTigeivfrgNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 402 ITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTdekefEKKLIGIMKKKVANYKVPKRViV 479
Cdd:cd12118 394 ISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVElkEGAKVT-----EEEIIAFCREHLAGFMVPKTV-V 467
|
490
....*....|....*....
gi 32563687 480 LDDLPRNHITKVQKNVLRD 498
Cdd:cd12118 468 FGELPKTSTGKIQKFVLRD 486
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
28-497 |
9.75e-59 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.06 E-value: 9.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDgDRKT--TYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPG 105
Cdd:PRK06087 30 QQTARAMPDKIAVVD-NHGAsyTYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 106 YTESE--------------AAHYIKDATPSILV-SCNEELDKVfrdkIRVINEDKLASEAGSLNACTMIEH--------- 161
Cdd:PRK06087 108 WREAElvwvlnkcqakmffAPTLFKQTRPVDLIlPLQNQLPQL----QQIVGVDKLAPATSSLSLSQIIADyeplttait 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 162 VEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKF 241
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 EVEDCIKYM--KNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERtGQVILERYGMTEAGVMT 319
Cdd:PRK06087 264 TPDACLALLeqQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 TNPL--NGERKAGTVGPAVQGVGCRI---------AKNGGIEVKTNA-IFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDE 387
Cdd:PRK06087 343 VVNLddPLSRFMHTDGYAAAGVEIKVvdearktlpPGCEGEEASRGPnVFMGYLDEPELTARALDEEGWYYSGDLCRMDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 388 DGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKvTDEKEFEKKLIGIMKKK 467
Cdd:PRK06087 423 AGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP-HHSLTLEEVVAFFSRKR 501
|
490 500 510
....*....|....*....|....*....|
gi 32563687 468 VANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK06087 502 VAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
32-500 |
2.30e-58 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 201.46 E-value: 2.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFI-DGDRKT-TYGEFVKRTGQYAtALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTES 109
Cdd:PRK13391 8 QTTPDKPAVImASTGEVvTYRELDERSNRLA-HLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 110 EAAHYIKDATPSILVSCNEELDKVFRDKIRV--INEDKLASEAGSLNACTMIEHVEKSDPASVC----------YTSGTT 177
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCpgVRHRLVLDGDGELEGFVGYAEAVAGLPATPIadeslgtdmlYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 178 GLPKG--AILTHGSLSNN---AHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFShSTMIWRSKFEVE---DCIKY 249
Cdd:PRK13391 167 GRPKGikRPLPEQPPDTPlplTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLG-GTVIVMEHFDAEqylALIEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 250 MKnATVMMGVPTFFSRLLASKNFNKEAF--GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEA-GVMTTNPLNGE 326
Cdd:PRK13391 246 YG-VTHTQLVPTMFSRMLKLPEEVRDKYdlSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGlGFTACDSEEWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 327 RKAGTVGPAVQGVgCRIAKNGGIEVKTNAI----FAG-----YWKNPKKTAEEFTEDG-WFKTGDVGHLDEDGYLTIGGR 396
Cdd:PRK13391 325 AHPGTVGRAMFGD-LHILDDDGAELPPGEPgtiwFEGgrpfeYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 397 SKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKR 476
Cdd:PRK13391 404 AAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRS 483
|
490 500
....*....|....*....|....
gi 32563687 477 VIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:PRK13391 484 IDFEDELPRLPTGKLYKRLLRDRY 507
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
41-500 |
5.42e-58 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 200.31 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMarVSKTTDTAAL--YIACLQIGALYIPVNPGYTESEAAHYIKDA 118
Cdd:PRK12406 6 ISGDRRRSFDELAQRAARAAGGL-AALGVRPGDCVA--LLMRNDFAFFeaAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TPSILVScNEELDKVFRDKI-------------RVINEDKLASEAGSLNACTM-----------IEHVEKSDPASVCYTS 174
Cdd:PRK12406 83 GARVLIA-HADLLHGLASALpagvtvlsvptppEIAAAYRISPALLTPPAGAIdwegwlaqqepYDGPPVPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKG---AILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHsTMIWRSKFEVE---DCIK 248
Cdd:PRK12406 162 GTTGHPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGG-VLVLQPRFDPEellQLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 249 YMKNATVMMgVPTFFSRLLASKNFNKEAF--GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTT-NPLNG 325
Cdd:PRK12406 241 RHRITHMHM-VPTMFIRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFaTSEDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 326 ERKAGTVGPAVQGVGCRIAKNGGIEVKTNAI------FAG-----YWKNPKKTAEeFTEDGWFKTGDVGHLDEDGYLTIG 394
Cdd:PRK12406 320 LSHPGTVGKAAPGAELRFVDEDGRPLPQGEIgeiysrIAGnpdftYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 395 GRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEFEKKLigimKKKVANYKV 473
Cdd:PRK12406 399 DRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATlDEADIRAQL----KARLAGYKV 474
|
490 500
....*....|....*....|....*..
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:PRK12406 475 PKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
72-497 |
6.69e-58 |
|
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: 198.82 E-value: 6.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 72 GDRVMARVSKTTDTAALYIACLQIGAL----YIPVNPGYTESEAAHYIKDATPSIlVSCNEELDKVFR-------DKIRV 140
Cdd:cd05922 18 GERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRI-VLADAGAADRLRdalpaspDPGTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 141 INEDKLASEAGSLNActmiEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHG 220
Cdd:cd05922 97 LDADGIRAARASAPA----HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 221 LYySLHCSLFSHSTMIWRSKFE-----VEDCIKYmkNATVMMGVPTFFSrLLASKNFNKEAFGNVRVFISGSAPLSVSTI 295
Cdd:cd05922 173 LS-VLNTHLLRGATLVLTNDGVlddafWEDLREH--GATGLAGVPSTYA-MLTRLGFDPAKLPSLRYLTQAGGRLPQETI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 296 EEFRE--RTGQVILeRYGMTEA-GVMTTNPLNGE-RKAGTVGPAVQGVGCRIAKNGGIEVKTNA----------IFAGYW 361
Cdd:cd05922 249 ARLREllPGAQVYV-MYGQTEAtRRMTYLPPERIlEKPGSIGLAIPGGEFEILDDDGTPTPPGEpgeivhrgpnVMKGYW 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 362 KNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPhPDFGEAVV 441
Cdd:cd05922 328 NDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 32563687 442 AIVVPSEKVTDekefeKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05922 407 LFVTAPDKIDP-----KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
43-493 |
4.49e-57 |
|
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: 196.51 E-value: 4.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 43 GDRKTTYGEFVKRTGQYATaLTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSI 122
Cdd:cd05914 4 GGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 123 LVSCNEEldkvfrdkirvinedklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWG 202
Cdd:cd05914 83 IFVSDED------------------------------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 203 FTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN-ATVMMGVP-------------------TF 262
Cdd:cd05914 127 LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAqVTPTLGVPvplviekifkmdiipkltlKK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNK-----------EAFG-NVRVFISGSAPLSvSTIEEFRERTGQVILERYGMTEAG-VMTTNPLNGERkA 329
Cdd:cd05914 207 FKFKLAKKINNRkirklafkkvhEAFGgNIKEFVIGGAKIN-PDVEEFLRTIGFPYTIGYGMTETApIISYSPPNRIR-L 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 GTVGPAVQGVGCRIAK------NGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT 403
Cdd:cd05914 285 GSAGKVIDGVEVRIDSpdpatgEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 404 G-GLNVYPKELEDFIDTLPFVKESAVI---------ASPHPDFgEAVVAIVVPSEKVTDEKEFEKKLigimKKKVANY-K 472
Cdd:cd05914 365 SsGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDF-LDVKALKQRNIIDAIKWEVRDKV----NQKVPNYkK 439
|
490 500
....*....|....*....|.
gi 32563687 473 VPKRVIVLDDLPRNHITKVQK 493
Cdd:cd05914 440 ISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3-499 |
5.60e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 198.61 E-value: 5.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 3 SRLVSSVHPQIGLRAASSAAN-----NIVSQAQLQsDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRV-- 75
Cdd:PRK07788 27 SGAVDLERPDNGLRLAADIRRygpfaGLVAHAARR-APDRAALIDERGTLTYAELDEQSNALARGLLAL-GVRAGDGVav 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 76 MARVSKttdtAALY--IACLQIGALYIPVNPGYteseAAHYIKDatpsilVSCNEELDKVFRD---------------KI 138
Cdd:PRK07788 105 LARNHR----GFVLalYAAGKVGARIILLNTGF----SGPQLAE------VAAREGVKALVYDdeftdllsalppdlgRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 139 RVINEDKLASEAGSLNACTMIEHVEKSDPAS----------VCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDY 208
Cdd:PRK07788 171 RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPlpkppkpggiVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 209 NLHALPFYHVHGLyysLHCSL-FSH-STMIWRSKFEVEDCIKYMKN--ATVMMGVPTFFSRLLA--SKNFNKEAFGNVR- 281
Cdd:PRK07788 251 TLLPAPMFHATGW---AHLTLaMALgSTVVLRRRFDPEATLEDIAKhkATALVVVPVMLSRILDlgPEVLAKYDTSSLKi 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 282 VFISGSApLSVSTIEEFRERTGQVILERYGMTEAGVMT-TNPLNGERKAGTVGPAVqgVGCRIA------------KNGG 348
Cdd:PRK07788 328 IFVSGSA-LSPELATRALEAFGPVLYNLYGSTEVAFATiATPEDLAEAPGTVGRPP--KGVTVKildengnevprgVVGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 349 IEVKTNAIFAGYWKNPKKTaeefTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAV 428
Cdd:PRK07788 405 IFVGNGFPFEGYTDGRDKQ----IIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563687 429 IASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIgimKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK07788 481 IGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYV---RDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
29-496 |
9.74e-57 |
|
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: 196.58 E-value: 9.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:cd05923 11 ASRAPDACAIADPARGLRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVSCN--EELDKVFRDKIRVINEDKLASEAGSLNACTMIE--HVEKSDPASVCYTSGTTGLPKGAI 184
Cdd:cd05923 90 AELAELIERGEMTAAVIAVdaQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEdpPREPEQPAFVFYTSGTTGLPKGAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 185 LTHGSLSNNAHDIVRDWGFTGNDYN--LHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMK--NATVMMGVP 260
Cdd:cd05923 170 IPQRAAESRVLFMSTQAGLRHGRHNvvLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEqeRVTSLFATP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 261 TFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNP-----------LNGERKA 329
Cdd:cd05923 250 THLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRdartgtemrpgFFSEVRI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 GTVGPAVQGV------GCRIAKNGGievktNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT 403
Cdd:cd05923 330 VRIGGSPDEAlangeeGELIVAAAA-----DAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 404 GGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGimkKKVANYKVPKRVIVLDDL 483
Cdd:cd05923 404 GGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDEL 480
|
490
....*....|...
gi 32563687 484 PRNHITKVQKNVL 496
Cdd:cd05923 481 PKNAMNKVLRRQL 493
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
172-498 |
8.19e-55 |
|
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: 191.05 E-value: 8.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 172 YTSGTTGLPKGaILTHGSLSNNAHDIVRDW----GFTGNDYNLHALPFYHVHGLYYSlHCSLFSHSTMIWRSKFEVEDCI 247
Cdd:cd05929 132 YSGGTTGRPKG-IKRGLPGGPPDNDTLMAAalgfGPGADSVYLSPAPLYHAAPFRWS-MTALFMGGTLVLMEKFDPEEFL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 248 KYMKNATVMMG--VPTFFSRLLA--SKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTnpL 323
Cdd:cd05929 210 RLIERYRVTFAqfVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTI--I 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 324 NGER---KAGTVGPAVQGVGCRIAKNGGiEVKTNAI----FAG-----YWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYL 391
Cdd:cd05929 288 NGEEwltHPGSVGRAVLGKVHILDEDGN-EVPPGEIgevyFANgpgfeYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANY 471
Cdd:cd05929 367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRY 446
|
330 340
....*....|....*....|....*..
gi 32563687 472 KVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05929 447 KCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
165-497 |
9.46e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 194.02 E-value: 9.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMI------WR 238
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVlatpqgYR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 239 SKfevedciKYMKN---------ATVMMGVPTFFSRLLASKnFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILER 309
Cdd:PRK07529 293 GP-------GVIANfwkiveryrINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 310 YGMTEAG-VMTTNPLNGERKAGTVG---P-----AVQGVG-------CRIAKNGGIEVKTNAIFAGYwKNPKKTAEEFTE 373
Cdd:PRK07529 365 YGLTEATcVSSVNPPDGERRIGSVGlrlPyqrvrVVILDDagrylrdCAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 374 DGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIV--VPSEKVT 451
Cdd:PRK07529 444 DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqlKPGASAT 523
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 32563687 452 DE--KEFEKKLIGimkKKVAnykVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK07529 524 EAelLAFARDHIA---ERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
3-498 |
4.19e-54 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 190.35 E-value: 4.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 3 SRLVSSVHPQIGLRAASSAANNIVSQAQL-----QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDR--V 75
Cdd:PRK13382 20 AGLIAPMRPDRYLRIVAAMRREGMGPTSGfaiaaQRCPDRPGLIDELGTLTWRELDERSDALAAAL-QALPIGEPRVvgI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 76 MARVSKTTDTAalYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVScNEE----LDKVFRDKIRVINEDKLASEAG 151
Cdd:PRK13382 99 MCRNHRGFVEA--LLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY-DEEfsatVDRALADCPQATRIVAWTDEDH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 152 SLNACTMIE-HVEKSDPAS------VCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYS 224
Cdd:PRK13382 176 DLTVEVLIAaHAGQRPEPTgrkgrvILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 225 LHCSLFShSTMIWRSKFEVEDCIKYMK--NATVMMGVPTFFSRL--LASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRE 300
Cdd:PRK13382 256 VLAASLA-CTIVTRRRFDPEATLDLIDrhRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 301 RTGQVILERYGMTEAGVMTT-NPLNGERKAGTVGPAVQGVGCRI----------AKNGGIEVKTNAIFAGYwkNPKKTAE 369
Cdd:PRK13382 335 QFGDVIYNNYNATEAGMIATaTPADLRAAPDTAGRPAEGTEIRIldqdfrevptGEVGTIFVRNDTQFDGY--TSGSTKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 370 efTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEK 449
Cdd:PRK13382 413 --FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 32563687 450 VTdekEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK13382 491 AS---ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
168-500 |
4.64e-53 |
|
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: 186.91 E-value: 4.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 168 ASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFE--VED 245
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDtfVED 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 246 cikyMKNA--TVMMGVP-------------------------TFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEF 298
Cdd:cd05932 220 ----VQRArpTLFFSVPrlwtkfqqgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 299 ReRTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFK 378
Cdd:cd05932 296 R-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGFLR 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 379 TGDVGHLDEDGYLTIGGRSKDMVITG-GLNVYPKELEDFIDTLPFVKESAVIAS--PHPdfgeavVAIVVPSE------K 449
Cdd:cd05932 375 TGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAP------LALVVLSEearlraD 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 450 VTDEKEFE---KKLIGIMKKKVANYKVPKRVIVLDD---LPRNHIT---KVQKNVLRDTY 500
Cdd:cd05932 449 AFARAELEaslRAHLARVNSTLDSHEQLAGIVVVKDpwsIDNGILTptlKIKRNVLEKAY 508
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-497 |
2.69e-52 |
|
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: 181.14 E-value: 2.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMI------WR 238
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVlagpagYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 239 SKFEVEDCIKYMKN--ATVMMGVPTFFSRLLAsKNFNKEaFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG 316
Cdd:cd05944 82 NPGLFDNFWKLVERyrITSLSTVPTVYAALLQ-VPVNAD-ISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 317 VMTT-NPLNGERKAGTVGPAVQGVGCRIAKNGGI-----EVKTNAIFAGYWKNP-----------KKTAeeFTEDGWFKT 379
Cdd:cd05944 160 CLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPgvfggylytegNKNA--FVADGWLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 380 GDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIV--VPSEKVTDEkefe 457
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlKPGAVVEEE---- 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 32563687 458 kKLIGIMKKKVANY-KVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05944 314 -ELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
48-501 |
8.04e-52 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 184.70 E-value: 8.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCN 127
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 ---EELDKVFRD------------------KIRVIN-----EDKLASEAGSLNACTMIE-------------HVEKSDPA 168
Cdd:PRK08751 132 nfgTTVQQVIADtpvkqvittglgdmlgfpKAALVNfvvkyVKKLVPEYRINGAIRFREalalgrkhsmptlQIEPDDIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 169 SVCYTSGTTGLPKGAILTHGSLSNN---AHDIVRDWGF--TGNDYNLHALPFYHVHGLYY-SLHCSLFSHSTMIWRSKFE 242
Cdd:PRK08751 212 FLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKleEGCEVVITALPLYHIFALTAnGLVFMKIGGCNHLISNPRD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 VEDCIKYMKNA--TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMT 319
Cdd:PRK08751 292 MPGFVKELKKTrfTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAAC 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 TNPLNGERKAGTVGPAV----------QGVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDG 389
Cdd:PRK08751 372 INPLTLKEYNGSIGLPIpstdacikddAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 390 YLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKligiMKKKVA 469
Cdd:PRK08751 452 FVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAH----ARANLT 527
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 470 NYKVPKRVIVLDDLPRNHITKVQKNVLRDTYK 501
Cdd:PRK08751 528 GYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
40-501 |
3.29e-51 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.91 E-value: 3.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 40 FIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRV---MARVSKTTDTAAlyiACLQIGALYIPVNPGYTESEAAHYIK 116
Cdd:PRK07059 42 FICMGKAITYGELDELSRALAAWLQSR-GLAKGARVaimMPNVLQYPVAIA---AVLRAGYVVVNVNPLYTPRELEHQLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 117 DA-TPSILVSCN--EELDKVF-RDKIR--------------------VINEDKLASEAGSLNACTMI------------- 159
Cdd:PRK07059 118 DSgAEAIVVLENfaTTVQQVLaKTAVKhvvvasmgdllgfkghivnfVVRRVKKMVPAWSLPGHVRFndalaegarqtfk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 160 -EHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA------HDIVRDWGFTGNDYN-LHALPFYHVHGLYYslhCSLFS 231
Cdd:PRK07059 198 pVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawLQPAFEKKPRPDQLNfVCALPLYHIFALTV---CGLLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 232 -----HSTMIWRSKfEVEDCIKYMKNATVMM--GVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQ 304
Cdd:PRK07059 275 mrtggRNILIPNPR-DIPGFIKELKKYQVHIfpAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGC 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 305 VILERYGMTE-AGVMTTNPLNGERKAGTVG---PAV-------QGVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTE 373
Cdd:PRK07059 354 PITEGYGLSEtSPVATCNPVDATEFSGTIGlplPSTevsirddDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 374 DGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSekvtDE 453
Cdd:PRK07059 434 DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK----DP 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 32563687 454 KEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYK 501
Cdd:PRK07059 510 ALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
35-496 |
5.03e-51 |
|
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: 180.03 E-value: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd05930 80 LEDSGAKLVL-------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPFYHVHGLyYSLHCSLFSHSTMIWRSKFEVED---CIKYMK--NATVMMGVPTFFSRLLAS 269
Cdd:cd05930 123 LWMQEAYPLTPGDRVLQFTSFSFDVSV-WEIFGALLAGATLVVLPEEVRKDpeaLADLLAeeGITVLHLTPSLLRLLLQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KNFnkEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILE-RYGMTEAGVMTT----NPLNGERKAGTVGPAVQGVGCRIA 344
Cdd:cd05930 202 LEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVnLYGPTEATVDATyyrvPPDDEEDGRVPIGRPIPNTRVYVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 KNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDGWF------KTGDVGHLDEDGYLTIGGRSKDMVITGGLNV 408
Cdd:cd05930 280 DENLRPVPPGVPgelyiggaglARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 409 YPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDDLPRNHI 488
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 32563687 489 TKVQKNVL 496
Cdd:cd05930 437 GKVDRKAL 444
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
35-502 |
8.91e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 180.36 E-value: 8.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYniKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKE--SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEELDKVFRDKIRVINEDKLASeagslnactMIEhVEKSDPASVC----------YTSGTTGLPKGAI 184
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDEEGRVIEIDEWKR---------MIE-KYLPTYAPIEnvqnapfymgFTSGSTGKPKAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 185 LTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHcSLFSHSTMIWRSKF---EVEDCIKyMKNATVMMGVPT 261
Cdd:PRK07638 163 RAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIS-TLYVGQTVHLMRKFipnQVLDKLE-TENISVMYTVPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 262 FFSRLLASKNFNKeafgNVRVFISGSAPLSVSTIEEFRERTGQVIL-ERYGMTEAGVMTT-NPLNGERKAGTVGPAVQGV 339
Cdd:PRK07638 241 MLESLYKENRVIE----NKMKIISSGAKWEAEAKEKIKNIFPYAKLyEFYGASELSFVTAlVDEESERRPNSVGRPFHNV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 340 GCRIAKNGGIEVKTNAI----------FAGYwKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVY 409
Cdd:PRK07638 317 QVRICNEAGEEVQKGEIgtvyvkspqfFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 410 PKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFekkligiMKKKVANYKVPKRVIVLDDLPRNHIT 489
Cdd:PRK07638 396 PEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSF-------CLQRLSSFKIPKEWHFVDEIPYTNSG 468
|
490
....*....|...
gi 32563687 490 KVQKNVLRDTYKN 502
Cdd:PRK07638 469 KIARMEAKSWIEN 481
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
166-491 |
1.23e-50 |
|
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: 175.67 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTH----GSLSNNAHDIVRDwgftGNDYNLHALPFYHVHGLYYSLHcSLFSHSTMIWRSKF 241
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErswiESFVCNEDLFNIS----GEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 EVEDCIKYMK--NATVMMGVPTFFsRLLASKNFNKEAfgnVRVFISGSAPLSVSTIEEFRERTGQ-VILERYGMTEAGVM 318
Cdd:cd17633 76 NPKSWIRKINqyNATVIYLVPTML-QALARTLEPESK---IKSIFSSGQKLFESTKKKLKNIFPKaNLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 319 TTNPLNGERKAGTVGPAVQGVGCRIAKNGG-----IEVKTNAIFAGYWKnpkktAEEFTEDGWFKTGDVGHLDEDGYLTI 393
Cdd:cd17633 152 TYNFNQESRPPNSVGRPFPNVEIEIRNADGgeigkIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 394 GGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVpSEKVTDekefeKKLIGIMKKKVANYKV 473
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS-GDKLTY-----KQLKRFLKQKLSRYEI 300
|
330
....*....|....*...
gi 32563687 474 PKRVIVLDDLPRNHITKV 491
Cdd:cd17633 301 PKKIIFVDSLPYTSSGKI 318
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
48-497 |
3.19e-50 |
|
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: 177.71 E-value: 3.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIkDATPSILVSCN 127
Cdd:cd05973 2 TFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRL-RTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeldkvfrdkirVINEDKLASeagslnactmiehveksDPASVCYTSGTTGLPKG------AILTHGSLSNNAHDIVRDW 201
Cdd:cd05973 80 ------------AANRHKLDS-----------------DPFVMMFTSGTTGLPKGvpvplrALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 202 GFtgndYNLhALPFYhVHGLYYSLHCSL-FSHSTMIWRSKFEVEDCIKYMKN--ATVMMGVPTFFsRLLASKNFNKEAF- 277
Cdd:cd05973 131 SF----WNA-ADPGW-AYGLYYAITGPLaLGHPTILLEGGFSVESTWRVIERlgVTNLAGSPTAY-RLLMAAGAEVPARp 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 -GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGER--KAGTVGPAVQGVGCRIAKNGGIEVKTN 354
Cdd:cd05973 204 kGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGPG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 -----AI---------FAGYWKNPKKTAEefteDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTL 420
Cdd:cd05973 284 epgrlAIdiansplmwFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEH 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 421 PFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05973 360 PAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
31-497 |
1.87e-49 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 177.87 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 31 LQSDPSKLLFIDGD--RKTTYGEfVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:PLN02246 33 LSEFSDRPCLIDGAtgRVYTYAD-VELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVSCNEELDKV----FRDKIRVINEDklASEAGSLNACTMIEHVEKS---------DPASVCYTSG 175
Cdd:PLN02246 112 AEIAKQAKASGAKLIITQSCYVDKLkglaEDDGVTVVTID--DPPEGCLHFSELTQADENElpeveispdDVVALPYSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNNAHDIVR----DWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE---DCIK 248
Cdd:PLN02246 190 TTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGallELIQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 249 YMKnATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVIL-ERYGMTEAG-------VMTT 320
Cdd:PLN02246 270 RHK-VTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGpvlamclAFAK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 321 NPLngERKAGTVGPAVQG---------VGCRIAKN--GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDG 389
Cdd:PLN02246 349 EPF--PVKSGSCGTVVRNaelkivdpeTGASLPRNqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 390 YLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSE--KVTDE--KEFekkligiMK 465
Cdd:PLN02246 427 ELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNgsEITEDeiKQF-------VA 499
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 466 KKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PLN02246 500 KQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-486 |
2.20e-49 |
|
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: 172.45 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLhCSLFSHSTMIWRSKFEVED 245
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLAL-ATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 246 CIKYM--KNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPlsvSTIEEFRERTGQVILERYGMTE-AGVMTTNP 322
Cdd:cd17637 80 ALELIeeEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTEtSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 323 LNgER--KAGTVGPAVQgVGC--------RIAKNGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLT 392
Cdd:cd17637 157 YR-ERpgSAGRPGPLVR-VRIvddndrpvPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 393 IGGRS--KDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTdekefEKKLIGIMKKKV 468
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGATLT-----ADELIEFVGSRI 308
|
330
....*....|....*...
gi 32563687 469 ANYKVPKRVIVLDDLPRN 486
Cdd:cd17637 309 ARYKKPRYVVFVEALPKT 326
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
46-498 |
5.51e-49 |
|
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: 176.50 E-value: 5.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 46 KTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVS 125
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 126 CNE---ELDKV------FRDKIRV--------INEDKLASEAGSLNACTMIEHvekSDPASVCYTSGTTGLPKGAILTHG 188
Cdd:cd05928 121 SDElapEVDSVasecpsLKTKLLVseksrdgwLNFKELLNEASTEHHCVETGS---QEPMAIYFTSGTTGSPKMAEHSHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 189 SLSNNAHDIVRDW-GFTGND--YNLHALpfyhvhGLYYSLHCSLFS----------HSTmiwrSKFEVEDCIKYMKN--A 253
Cdd:cd05928 198 SLGLGLKVNGRYWlDLTASDimWNTSDT------GWIKSAWSSLFEpwiqgacvfvHHL----PRFDPLVILKTLSSypI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 TVMMGVPTFFsRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVG 333
Cdd:cd05928 268 TTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 334 PAVQGVGCRIA-KNG-----------GIEVKTN---AIFAGYWKNPKKTAEEFTEDGWFkTGDVGHLDEDGYLTIGGRSK 398
Cdd:cd05928 347 KASPPYDVQIIdDNGnvlppgtegdiGIRVKPIrpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRAD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 399 DMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDEKEFEKKLIGIMKKKVANYKVPKR 476
Cdd:cd05928 426 DVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlaPQFLSHDPEQLTKELQQHVKSVTAPYKYPRK 505
|
490 500
....*....|....*....|..
gi 32563687 477 VIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05928 506 VEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
46-498 |
1.11e-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: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 46 KTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVS 125
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 126 cneeldkvfrdkirvineDklaseagslnactmiehvEKSDPASVCYTSGTTGLPKGAILTHGSLSNN------AHDIVR 199
Cdd:cd05971 85 ------------------D------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHlpgvqfPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 200 ----------DWGFTGNDYNLhALPFYHvHGLyyslhcSLFSHStmiwRSKFEVEDCIKYMKNATVMMGV--PTFFSRLL 267
Cdd:cd05971 129 rdgdlywtpaDWAWIGGLLDV-LLPSLY-FGV------PVLAHR----MTKFDPKAALDLMSRYGVTTAFlpPTALKMMR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 268 ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLN-GERKAGTVGPAVQGVGCRIAKN 346
Cdd:cd05971 197 QQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 347 GGIEVKTNAI------------FAGYWKNPKKTAEEFTEDgWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELE 414
Cdd:cd05971 277 NGTPLPPGEVgeiavelpdpvaFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 415 DFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKN 494
Cdd:cd05971 356 ECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
....
gi 32563687 495 VLRD 498
Cdd:cd05971 436 ELRA 439
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
28-499 |
1.12e-48 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 175.72 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK06155 28 ARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVscneeLDKVFRDKIRVINEDKLASEA---------------------GSLNACTMIEHVEKSD 166
Cdd:PRK06155 107 GPQLEHILRNSGARLLV-----VEAALLAALEAADPGDLPLPAvwlldapasvsvpagwstaplPPLDAPAPAAAVQPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 167 PASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYySLHCSLFSHSTMIWRSKFEVEDC 246
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVLEPRFSASGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 247 IKYMK--NATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPlsVSTIEEFRERTGQVILERYGMTEAGVMTTNPLn 324
Cdd:PRK06155 261 WPAVRrhGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTH- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 325 GERKAGTVGPAVQGVGCRIAKNGGIEVKTN-------------AIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYL 391
Cdd:PRK06155 338 GSQRPGSMGRLAPGFEARVVDEHDQELPDGepgelllradepfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANY 471
Cdd:PRK06155 417 RFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV---ALVRHCEPRLAYF 493
|
490 500
....*....|....*....|....*...
gi 32563687 472 KVPKRVIVLDDLPRNHITKVQKNVLRDT 499
Cdd:PRK06155 494 AVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
47-502 |
1.15e-48 |
|
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: 175.93 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 47 TTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDA-------- 118
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLrhiwqllg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TPSILVSCN--EELDKVfrDKIRVINEDKLASEAGSLNAC--TMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd05906 119 SPVVLTDAElvAEFAGL--ETLSGLPGIRVLSIEELLDTAadHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPFYHVHGL-YYSLHCsLFSHSTMIWRSKFEV-------EDCI-KYMKNATVMmgvPTFFSR 265
Cdd:cd05906 197 AGKIQHNGLTPQDVFLNWVPLDHVGGLvELHLRA-VYLGCQQVHVPTEEIladplrwLDLIdRYRVTITWA---PNFAFA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 266 LLA-------SKNFNkeaFGNVRVFISGSAPLSVSTIEEFRERTGQ------VILERYGMTE--AGVM-----TTNPLNG 325
Cdd:cd05906 273 LLNdlleeieDGTWD---LSSLRYLVNAGEAVVAKTIRRLLRLLEPyglppdAIRPAFGMTEtcSGVIysrsfPTYDHSQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 326 ERKAGTVGPAVQGVGCRI----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDeDGYLTIGG 395
Cdd:cd05906 350 ALEFVSLGRPIPGVSMRIvddegqllpeGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 396 RSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPH--PDFGEAVVAIV-VPSEKVTDEKEfekKLIGIMKKKVANYK 472
Cdd:cd05906 429 RTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVrdPGAETEELAIFfVPEYDLQDALS---ETLRAIRSVVSREV 505
|
490 500 510
....*....|....*....|....*....|....
gi 32563687 473 --VPKRVIVL--DDLPRNHITKVQKNVLRDTYKN 502
Cdd:cd05906 506 gvSPAYLIPLpkEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
45-484 |
1.33e-48 |
|
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: 174.44 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFvkRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGalYIPVNPGYTESEAA--HYIKDA-TPS 121
Cdd:cd05909 6 TSLTYRKL--LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRElrACIKLAgIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 122 ILVScneeldKVFRDKI------------RVINEDKLASEAGSLNACTMIEH----------------VEKSDPASVCYT 173
Cdd:cd05909 82 VLTS------KQFIEKLklhhlfdveydaRIVYLEDLRAKISKADKCKAFLAgkfppkwllrifgvapVQPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 174 SGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFS-----------HSTMIWRskfe 242
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSgikvvfhpnplDYKKIPE---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 vedcIKYMKNATVMMGVPTFFSRLLasKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMTTN 321
Cdd:cd05909 232 ----LIYDKKATILLGTPTFLRGYA--RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 PLNGERKAGTVGPAVQGVGCRIAK-----------NGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGY 390
Cdd:cd05909 306 TPQSPNKEGTVGRPLPGMEVKIVSvetheevpigeGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 391 LTIGGRSKDMVITGGLNVYPKELEDFI-DTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEkefekkLIGIMKK-KV 468
Cdd:cd05909 385 LTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSS------LNDILKNaGI 458
|
490
....*....|....*.
gi 32563687 469 ANYKVPKRVIVLDDLP 484
Cdd:cd05909 459 SNLAKPSYIHQVEEIP 474
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
32-496 |
3.58e-47 |
|
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: 170.59 E-value: 3.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGAlyIPVN--PGYTES 109
Cdd:cd05920 26 ARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVLalPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 110 EAAHYIKDATPSILVscneeldkvFRDKIRVINEDKLASEagslnactmiEHVEKSDPASVCYTSGTTGLPKGAILTHGS 189
Cdd:cd05920 103 ELSAFCAHAEAVAYI---------VPDRHAGFDHRALARE----------LAESIPEVALFLLSGGTTGTPKLIPRTHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 190 LSNNAHDIVRDWGFTGNDYNLHALPFYHvhglYYSLHC-----SLFSHSTMIWRSKFEVEDCIKYMK--NATVMMGVPTF 262
Cdd:cd05920 164 YAYNVRASAEVCGLDQDTVYLAVLPAAH----NFPLACpgvlgTLLAGGRVVLAPDPSPDAAFPLIEreGVTVTALVPAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEaGVMTTNPLN--GERKAGTVG-PAVQGV 339
Cdd:cd05920 240 VSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTRLDdpDEVIIHTQGrPMSPDD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 340 GCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVY 409
Cdd:cd05920 319 EIRVVDEEGNPVPPGEEgelltrgpytIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 410 PKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLigiMKKKVANYKVPKRVIVLDDLPRNHIT 489
Cdd:cd05920 399 AEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFL---RERGLAAYKLPDRIEFVDSLPLTAVG 475
|
....*..
gi 32563687 490 KVQKNVL 496
Cdd:cd05920 476 KIDKKAL 482
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
35-496 |
6.52e-47 |
|
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: 170.35 E-value: 6.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:TIGR03098 14 PDATALVHHDRTLTYAALSERVLALASGL-RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEELDKV---------FRDKIRV---------------INEDKLASEAGSLNACTMIEhvekSDPASV 170
Cdd:TIGR03098 93 LADCNVRLLVTSSERLDLLhpalpgchdLRTLIIVgdpahaseghpgeepASWPKLLALGDADPPHPVID----SDMAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 CYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLyySLHCSLFSH-STMIWRSKFEVEDCIKY 249
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGF--NQLTTAFYVgATVVLHDYLLPRDVLKA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 250 MKN--ATVMMGVPTFFSRlLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGVMTT-NPLNG 325
Cdd:TIGR03098 247 LEKhgITGLAAVPPLWAQ-LAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGLTEAFRSTYlPPEEV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 326 ERKAGTVGPAVQGVGCRIAKNGGIE---------VKTNAIFA-GYWKNPKKTAEEFTEDGWFK-----------TGDVGH 384
Cdd:TIGR03098 326 DRRPDSIGKAIPNAEVLVLREDGSEcapgeegelVHRGALVAmGYWNDPEKTAERFRPLPPFPgelhlpelavwSGDTVR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 385 LDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKefeKKLIGIM 464
Cdd:TIGR03098 406 RDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDR---AALLAEC 482
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 465 KKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:TIGR03098 483 RARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
31-486 |
7.88e-47 |
|
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: 168.96 E-value: 7.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 31 LQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESE 110
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 111 AAHYIKDATPSILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHGSL 190
Cdd:cd05945 80 IREILDAAKPALLI-------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 191 SNNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYyslhCSLFSHSTMIWRSKFEVEDC---IKYMKNA--TVMMGVPTF 262
Cdd:cd05945 123 VSFTNWMLSDFPLGPGDVFLNQAPFsfdLSVMDLY----PALASGATLVPVPRDATADPkqlFRFLAEHgiTVWVSTPSF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERT-GQVILERYGMTEAGV------MTTNPLNGERKAgTVGPA 335
Cdd:cd05945 199 AAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVavtyieVTPEVLDGYDRL-PIGYA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 336 VQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTED---GWFKTGDVGHLDEDGYLTIGGRSKDMVi 402
Cdd:cd05945 278 KPGAKLVILDEDGRPVPPGEKgelvisgpsvSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQV- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 403 tgGLNVYPKELEDfIDT----LPFVKESAVIASPHPDFGEAVVAIVVPSEKVT--DEKEFEKKLigimKKKVANYKVPKR 476
Cdd:cd05945 357 --KLNGYRIELEE-IEAalrqVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEagLTKAIKAEL----AERLPPYMIPRR 429
|
490
....*....|
gi 32563687 477 VIVLDDLPRN 486
Cdd:cd05945 430 FVYLDELPLN 439
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
17-490 |
3.37e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 168.91 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 17 AASSAANNIVSQAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIG 96
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 97 ALYIPVNPGYTESEAAHYIKDA-TPSILVS----CNEELDKVFRDKIRV-INEDKLASEAG---SLNACTMIEHVE---- 163
Cdd:PRK05852 93 LVVVPLDPALPIAEQRVRSQAAgARVVLIDadgpHDRAEPTTRWWPLTVnVGGDSGPSGGTlsvHLDAATEPTPATstpe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 164 --KSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIW--RS 239
Cdd:PRK05852 173 glRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 240 KFEVEDCIKYMK--NATVMMGVPTFFSRLL--ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEA 315
Cdd:PRK05852 253 RFSAHTFWDDIKavGATWYTAVPTIHQILLerAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 316 G--VMTTN---PLNGERKAGTVGPAVQGVGCRI------------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTeDGWFK 378
Cdd:PRK05852 333 ThqVTTTQiegIGQTENPVVSTGLVGRSTGAQIrivgsdglplpaGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 379 TGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfek 458
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE--- 488
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 459 KLIGIMKKKVANYKVPKRVIVLDDLPrnHITK 490
Cdd:PRK05852 489 ELVQFCRERLAAFEIPASFQEASGLP--HTAK 518
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
41-497 |
3.40e-46 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 169.59 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVmARVSKTTDtaaLYIACLQ----IGALYIPVNPGYTESEAAHYIK 116
Cdd:PLN02860 27 ISGNRRRTGHEFVDGVLSLAAGLLR-LGLRNGDVV-AIAALNSD---LYLEWLLavacAGGIVAPLNYRWSFEEAKSAML 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 117 DATPSILV---SCNEELDKVFRDKI-----RVINEDKLASEAGSLNACTMIEHVEK--------------SDPASVCYTS 174
Cdd:PLN02860 102 LVRPVMLVtdeTCSSWYEELQNDRLpslmwQVFLESPSSSVFIFLNSFLTTEMLKQralgtteldyawapDDAVLICFTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLhCSLFSHSTMIWRSKFEVEDCIKYMKN-- 252
Cdd:PLN02860 182 GTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIKQhn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 253 ATVMMGVPTFFSRLLA--SKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEA-------------- 315
Cdd:PLN02860 261 VTSMITVPAMMADLISltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEAcssltfmtlhdptl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 316 --------GVMTTNPLNGERKAGT-VGPAVQGVGCRI-----AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGD 381
Cdd:PLN02860 341 espkqtlqTVNQTKSSSVHQPQGVcVGKPAPHVELKIgldesSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEK---VTDEKEFEK 458
Cdd:PLN02860 421 IGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwSDNEKENAK 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 32563687 459 KLIGI---------MKKKVANYKVPKRVIVLDD-LPRNHITKVQKNVLR 497
Cdd:PLN02860 501 KNLTLssetlrhhcREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
29-500 |
3.86e-46 |
|
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: 168.96 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKT----TYGEFVKRTGQYATALTEKynIKKGDRVMARVSKTTDTAALYIACLQIGA----LYI 100
Cdd:cd05931 3 AAARPDRPAYTFLDDEGGReetlTYAELDRRARAIAARLQAV--GKPGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 101 PVNPGYTEsEAAHYIKDATPSILVSCNEELDKVFRDKIRVINEDKLASEAGSLNACT-----MIEHVEKSDPASVCYTSG 175
Cdd:cd05931 81 PTPGRHAE-RLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTsaadwPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGL--------YYSLHCSL-----FSHSTMIWrskfe 242
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLigglltplYSGGPSVLmspaaFLRRPLRW----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 vedcIKYM-KNATVMMGVPTFFSRLLASKnFNKEA-----FGNVRVFISGSAPLSVSTIEEFRERTG------QVILERY 310
Cdd:cd05931 235 ----LRLIsRYRATISAAPNFAYDLCVRR-VRDEDlegldLSSWRVALNGAEPVRPATLRRFAEAFApfgfrpEAFRPSY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 311 GMTEAGVM-TTNPLNGERKAGTV-------------------------GPAVQGVGCRIAKNGG-----------IEVKT 353
Cdd:cd05931 310 GLAEATLFvSGGPPGTGPVVLRVdrdalagravavaaddpaarelvscGRPLPDQEVRIVDPETgrelpdgevgeIWVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 354 NAIFAGYWKNPKKTAEEF------TEDGWFKTGDVGHLDeDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTL-PFVKES 426
Cdd:cd05931 390 PSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAhPALRPG 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32563687 427 AVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLddLPRNHI--T---KVQKNVLRDTY 500
Cdd:cd05931 469 CVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVL--VRPGSIprTssgKIQRRACRAAY 545
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
48-428 |
6.93e-46 |
|
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: 165.13 E-value: 6.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCN 127
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 EELDKVFRDKIRVINEDKLASEAgsLNACTMIEHVEK----SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGF 203
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAA--LDDAPAPPPPDApsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 204 TGND--YNLHALPF----YHVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKnATVMMGVPTFFSRLLASKNfnkEAF 277
Cdd:TIGR01733 159 DPDDrvLQFASLSFdasvEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHP-VTVLNLTPSLLALLAAALP---PAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 GNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGVMTTN-----PLNGERKAGTVGPAVQGVGCRIAKNGGIEV 351
Cdd:TIGR01733 235 ASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTAtlvdpDDAPRESPVPIGRPLANTRLYVLDDDLRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 352 KTNAI----------FAGYWKNPKKTAEEFTEDG--------WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKEL 413
Cdd:TIGR01733 315 PVGVVgelyiggpgvARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
|
410
....*....|....*
gi 32563687 414 EDFIDTLPFVKESAV 428
Cdd:TIGR01733 395 EAALLRHPGVREAVV 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-497 |
7.16e-46 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 167.55 E-value: 7.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFID--GD-RKTTYGEF---VKRTGQYATALtekyNIKKGDRVMARVskttDTAALYIACL----QIGAL 98
Cdd:PRK08008 17 ADVYGHKTALIFESsgGVvRRYSYLELneeINRTANLFYSL----GIRKGDKVALHL----DNCPEFIFCWfglaKIGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 99 YIPVNPGYTESEAAHYIKDATPSILVsCNEELDKVFR----------DKIRVINEDkLASEAGSLN--------ACTMIE 160
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLV-TSAQFYPMYRqiqqedatplRHICLTRVA-LPADDGVSSftqlkaqqPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 161 HVEKS--DPASVCYTSGTTGLPKGAILTHGSLSNNAHdiVRDW--GFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMI 236
Cdd:PRK08008 167 APPLStdDTAEILFTSGTTSRPKGVVITHYNLRFAGY--YSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 W-----RSKFEVEDCiKYmkNATVMMGVPTFFSRLL---ASKNFNKEAFGNVRVFIsgsaPLSVSTIEEFRERTGQVILE 308
Cdd:PRK08008 245 LlekysARAFWGQVC-KY--RATITECIPMMIRTLMvqpPSANDRQHCLREVMFYL----NLSDQEKDAFEERFGVRLLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 309 RYGMTEA--GVMTTNPlNGERKAGTVGPAVQGVGCRIAKNGGIEVKTN-------------AIFAGYWKNPKKTAEEFTE 373
Cdd:PRK08008 318 SYGMTETivGIIGDRP-GDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGeigeicikgvpgkTIFKEYYLDPKATAKVLEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 374 DGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-D 452
Cdd:PRK08008 397 DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETlS 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 32563687 453 EKEFekklIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK08008 477 EEEF----FAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
35-505 |
3.66e-45 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 166.73 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVsCNEELDKVFRDKIRV--------------INEDKLASEAGS----------------LNACTMIEHVEK 164
Cdd:PLN03102 107 LRHAKPKILF-VDRSFEPLAREVLHLlssedsnlnlpvifIHEIDFPKRPSSeeldyecliqrgeptpSLVARMFRIQDE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWR--SKFE 242
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRhvTAPE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 VEDCIKyMKNATVMMGVPTFFSRLLASKNFNKE-AFGNVRVFISGSAPLSVstIEEFRERTGQVILERYGMTEAgvmtTN 321
Cdd:PLN03102 266 IYKNIE-MHNVTHMCCVPTVFNILLKGNSLDLSpRSGPVHVLTGGSPPPAA--LVKKVQRLGFQVMHAYGLTEA----TG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 P------------------LNGERKAGTVGPAVQGVGCRIAKN-----------GGIEVKTNAIFAGYWKNPKKTAEEFt 372
Cdd:PLN03102 339 PvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKETqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAF- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 373 EDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTD 452
Cdd:PLN03102 418 KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETT 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 453 EKEFEKK-------LIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKNLFA 505
Cdd:PLN03102 498 KEDRVDKlvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVV 557
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
27-497 |
5.25e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 165.18 E-value: 5.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 27 SQAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDrVMARVSKTTDTAALYIACLQIGALYI-PVNPG 105
Cdd:PRK13390 5 THAQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDA-GLRTGD-VVALLSDNSPEALVVLWAALRSGLYItAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 106 YTESEAAHYIKDATPSILVScNEELDKVFRD-----KIRVI---NEDKLASEAGSLnACTMIEHVEKSDPASVCYTSGTT 177
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVA-SAALDGLAAKvgadlPLRLSfggEIDGFGSFEAAL-AGAGPRLTEQPCGAVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 178 GLPKG--AILTHGSLSNNAHDIVRD----WGFTGNDYNLHALPFYHVHGLYYslhCSLFsHS---TMIWRSKFEVEDCIK 248
Cdd:PRK13390 161 GFPKGiqPDLPGRDVDAPGDPIVAIarafYDISESDIYYSSAPIYHAAPLRW---CSMV-HAlggTVVLAKRFDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 249 YMKN--ATVMMGVPTFFSRLLASKNFNKEAF--GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMT-TNPL 323
Cdd:PRK13390 237 HVERyrITVTQMVPTMFVRLLKLDADVRTRYdvSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTfIDSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 324 NGERKAGTVGPAVQGVgCRIAKNGGIEVKTNAIFAGYWK----------NPKKTAE--EFTEDGWFKTGDVGHLDEDGYL 391
Cdd:PRK13390 317 DWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFErdrlpfrylnDPEKTAAaqHPAHPFWTTVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANY 471
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHY 475
|
490 500
....*....|....*....|....*.
gi 32563687 472 KVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK13390 476 KAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
48-498 |
1.46e-44 |
|
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: 164.24 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCN 127
Cdd:cd17642 46 SYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 EELDKVF--RDKIRVI--------NED----------KLASEAGSLNACTMI--EHVEKSDPASVCYTSGTTGLPKGAIL 185
Cdd:cd17642 125 KGLQKVLnvQKKLKIIktiiildsKEDykgyqclytfITQNLPPGFNEYDFKppSFDRDEQVALIMNSSGSTGLPKGVQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 186 THGSLSNNaHDIVRDWGFtGNDYN-----LHALPFYHVHGLYYSLHcSLFSHSTMIWRSKFEVEDCIKYMKNATVMMG-- 258
Cdd:cd17642 205 THKNIVAR-FSHARDPIF-GNQIIpdtaiLTVIPFHHGFGMFTTLG-YLICGFRVVLMYKFEEELFLRSLQDYKVQSAll 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 259 VPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG-QVILERYGMTE--AGVMTTNplNGERKAGTVGPA 335
Cdd:cd17642 282 VPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKlPGIRQGYGLTEttSAILITP--EGDDKPGAVGKV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 336 VQGVGCRIA-----------KNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITG 404
Cdd:cd17642 360 VPFFYAKVVdldtgktlgpnERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 405 GLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEkefEKKLIGIMKKKVANYK-VPKRVIVLDDL 483
Cdd:cd17642 440 GYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT---EKEVMDYVASQVSTAKrLRGGVKFVDEV 516
|
490
....*....|....*
gi 32563687 484 PRNHITKVQKNVLRD 498
Cdd:cd17642 517 PKGLTGKIDRRKIRE 531
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
45-496 |
1.75e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 164.83 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYAtALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:PRK06178 57 HVITYAELDELSDRFA-ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 SCNEELDKV--FRDKIRV-----------------------INEDKLASEA-----GSLNACT---MIEHVEKSDPASVC 171
Cdd:PRK06178 136 ALDQLAPVVeqVRAETSLrhvivtsladvlpaeptlplpdsLRAPRLAAAGaidllPALRACTapvPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 172 YTSGTTGLPKGAILTHGSL-----SNNAHDIVRDwgftGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMI----WRSKFE 242
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMvytaaAAYAVAVVGG----EDSVFLSFLPEFWIAGENFGLLFPLFSGATLVllarWDAVAF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 VEDCIKYMKNATVM--------MGVPTFFSRLLASknfnkeaFGNVRVfISGSAPLSVSTIEEFRERTGQVILE-RYGMT 313
Cdd:PRK06178 292 MAAVERYRVTRTVMlvdnavelMDHPRFAEYDLSS-------LRQVRV-VSFVKKLNPDYRQRWRALTGSVLAEaAWGMT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 314 E--------AGvMTTNPLNGERKAGTVGPAVQGVGCRI-----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFtED 374
Cdd:PRK06178 364 EthtcdtftAG-FQDDDFDLLSQPVFVGLPVPGTEFKIcdfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEAL-RD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 375 GWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEK 454
Cdd:PRK06178 442 GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GAD 518
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32563687 455 EFEKKLIGIMKKKVANYKVPKrVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK06178 519 LTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
29-497 |
2.12e-44 |
|
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: 163.78 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGAlyIPVN--PGY 106
Cdd:COG1021 33 RRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVFalPAH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 107 TESEAAHYIKDATPSILVscneeldkvFRDKIRVINEDKLASE-------------AGSLNACTMIEHVEKS-------- 165
Cdd:COG1021 110 RRAEISHFAEQSEAVAYI---------IPDRHRGFDYRALARElqaevpslrhvlvVGDAGEFTSLDALLAApadlsepr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 -DPASVCY---TSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPfyHVHGlyYSLHC-----SLFSHSTMI 236
Cdd:COG1021 181 pDPDDVAFfqlSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALP--AAHN--FPLSSpgvlgVLYAGGTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 WRSKFEVEDCIKYMK--NATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTG----QVilerY 310
Cdd:COG1021 257 LAPDPSPDTAFPLIEreRVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGctlqQV----F 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 311 GMTEAGVMTT---NPLngERKAGTVG----PA--VqgvgcRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEF 371
Cdd:COG1021 333 GMAEGLVNYTrldDPE--EVILTTQGrpisPDdeV-----RIVDEDGNPVPPGEVgelltrgpytIRGYYRAPEHNARAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 372 TEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT 451
Cdd:COG1021 406 TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPL 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 32563687 452 DEKEFEKKLIGimkKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:COG1021 486 TLAELRRFLRE---RGLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
43-497 |
4.91e-44 |
|
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: 161.11 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 43 GDRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSI 122
Cdd:cd05958 7 PEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 123 LVsCNEELdkvfrdkirvinedklaseagslnactmiEHVEksDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRD-W 201
Cdd:cd05958 87 AL-CAHAL-----------------------------TASD--DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNvL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 202 GFTGNDYNLHALPFYHVHGL--------YYSLHCSLFSHSTmiwrsKFEVEDCIKYMKnATVMMGVPTFFSRLLASKNFN 273
Cdd:cd05958 135 RLREDDRFVGSPPLAFTFGLggvllfpfGVGASGVLLEEAT-----PDLLLSAIARYK-PTVLFTAPTAYRAMLAHPDAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 274 KEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKT 353
Cdd:cd05958 209 GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 354 NAIF-------AGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKES 426
Cdd:cd05958 289 GTIGrlavrgpTGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEC 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563687 427 AVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05958 369 AVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
7-502 |
7.03e-44 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 163.09 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 7 SSVHPQIGLRAAS--SAANNIVSQAQLQSDPSKLLFIDGDrKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTD 84
Cdd:PLN02574 26 SSKHPPVPLPSDPnlDAVSFIFSHHNHNGDTALIDSSTGF-SISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 85 TAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCNEELDKVFRDKIRVInedkLASEAGSLNA--------- 155
Cdd:PLN02574 105 FPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVI----GVPENYDFDSkriefpkfy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 156 --------CTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVR------DWGFTGNDYnLHALPFYHVHGL 221
Cdd:PLN02574 181 elikedfdFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasqyEYPGSDNVY-LAALPMFHIYGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 222 yyslhcSLFS------HSTMIWRSKFEVEDCIKYMK--NATVMMGVPTFFSRLL-ASKNFNKEAFGNVRVFISGSAPLSV 292
Cdd:PLN02574 260 ------SLFVvgllslGSTIVVMRRFDASDMVKVIDrfKVTHFPVVPPILMALTkKAKGVCGEVLKSLKQVSCGAAPLSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 293 STIEEFRERTGQV-ILERYGMTEAGVMTTNPLNGE--RKAGTVG---PAVQG------VGCRI--AKNGGIEVKTNAIFA 358
Cdd:PLN02574 334 KFIQDFVQTLPHVdFIQGYGMTESTAVGTRGFNTEklSKYSSVGllaPNMQAkvvdwsTGCLLppGNCGELWIQGPGVMK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 359 GYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGE 438
Cdd:PLN02574 414 GYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563687 439 AVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKN 502
Cdd:PLN02574 494 IPVAFVVRRQGSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
8-498 |
1.67e-43 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 161.69 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 8 SVHPQIGLRAASSAANNIVSQAQLQSDpsKLLFIDG--DRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDT 85
Cdd:PLN02330 17 SRYPSVPVPDKLTLPDFVLQDAELYAD--KVAFVEAvtGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 86 AALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCNEELDKV--FRDKIRVINEDKLAS--------EAGSLNA 155
Cdd:PLN02330 94 GIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVkgLGLPVIVLGEEKIEGavnwkellEAADRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 156 CTMI-EHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWG--FTGNDYNLHALPFYHVHGLYYSLHCSLFSH 232
Cdd:PLN02330 174 DTSDnEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGpeMIGQVVTLGLIPFFHIYGITGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 233 STMIWRSKFEVEDCIKYMKNATVMMG--VPTFFSRLLasKNFNKEAFG----NVRVFISGSAPLSVSTIEEFRER-TGQV 305
Cdd:PLN02330 254 GKVVVMSRFELRTFLNALITQEVSFApiVPPIILNLV--KNPIVEEFDlsklKLQAIMTAAAPLAPELLTAFEAKfPGVQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 306 ILERYGMTEAGVMTT---NPLNGE--RKAGTVG---PAVQ------GVGCRIAKN--GGIEVKTNAIFAGYWKNPKKTAE 369
Cdd:PLN02330 332 VQEAYGLTEHSCITLthgDPEKGHgiAKKNSVGfilPNLEvkfidpDTGRSLPKNtpGELCVRSQCVMQGYYNNKEETDR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 370 EFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEK 449
Cdd:PLN02330 412 TIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPK 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 32563687 450 VtdeKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PLN02330 492 A---KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
48-497 |
1.18e-42 |
|
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: 157.28 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALtEKYNIKKGDRVmarVSKTTDTAALYI---ACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:cd05969 2 TFAQLKVLSARFANVL-KSLGVGKGDRV---FVLSPRSPELYFsmlGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 SCNEELDKVfrdkirvinedklaseagslnactmiehvEKSDPASVCYTSGTTGLPKGaiLTHgslsnnAHDIVRDWGFT 204
Cdd:cd05969 78 TTEELYERT-----------------------------DPEDPTLLHYTSGTTGTPKG--VLH------VHDAMIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 205 GN-DYNLHALPFYH-------VHGLYYSLHCSLFSHSTM-IWRSKFEVE---DCIKYMKnATVMMGVPTFFSRLLASKNF 272
Cdd:cd05969 121 GKyVLDLHPDDIYWctadpgwVTGTVYGIWAPWLNGVTNvVYEGRFDAEswyGIIERVK-VTVWYTAPTAIRMLMKEGDE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 273 NKEAF--GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG-VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGI 349
Cdd:cd05969 200 LARKYdlSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 350 EVKTN------------AIFAGYWKNPKKTAEEFTeDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFI 417
Cdd:cd05969 280 ELPPGtkgilalkpgwpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 418 DTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05969 359 MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
165-493 |
1.30e-42 |
|
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: 154.73 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSL-SNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV 243
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 244 EDCIKYMK--NATVMMGVPTFFSRL-LASKNFNKEAfGNVRVFISGSApLSVSTIEEFRERTGQV-ILERYGMTEAGVMT 319
Cdd:cd17635 81 KSLFKILTtnAVTTTCLVPTLLSKLvSELKSANATV-PSLRLIGYGGS-RAIAADVRFIEATGLTnTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 TNPL-NGERKAGTVGPAVQGVGCRIAKNGGIEV----------KTNAIFAGYWKNPKKTAEEFTeDGWFKTGDVGHLDED 388
Cdd:cd17635 159 CLPTdDDSIEINAVGRPYPGVDVYLAATDGIAGpsasfgtiwiKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERRED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 389 GYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKvtDEKEFEKKLIGIMKKKV 468
Cdd:cd17635 238 GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE--LDENAIRALKHTIRREL 315
|
330 340
....*....|....*....|....*
gi 32563687 469 ANYKVPKRVIVLDDLPRNHITKVQK 493
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
18-498 |
2.83e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 157.98 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 18 ASSAANNIVS--QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQI 95
Cdd:PRK06164 5 AAPRADTLASllDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 96 GALYIPVNPGYTESEAAHYIKDATPSILVS------------CNEELDKVFRDKIRVINEDKLASE-------------A 150
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARWLVVwpgfkgidfaaiLAAVPPDALPPLRAIAVVDDAADAtpapapgarvqlfA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 151 GSLNACTMIEHVEKSDP--ASVCYT-SGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGlYYSLHC 227
Cdd:PRK06164 164 LPDPAPPAAAGERAADPdaGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 228 SLFSHSTMIWRSKFEVEDCIKYMKNATV--MMGVPTFFSRLLASKNfNKEAFGNVRVF-ISGSAPLSVSTIEEFRERtGQ 304
Cdd:PRK06164 243 ALAGGAPLVCEPVFDAARTARALRRHRVthTFGNDEMLRRILDTAG-ERADFPSARLFgFASFAPALGELAALARAR-GV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 305 VILERYGMTE-----AGVMTTNPLNGERKAGTVgPAVQGVGCRIA-----------KNGGIEVKTNAIFAGYWKNPKKTA 368
Cdd:PRK06164 321 PLTGLYGSSEvqalvALQPATDPVSVRIEGGGR-PASPEARVRARdpqdgallpdgESGEIEIRAPSLMRGYLDNPDATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 369 EEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAvVAIVVPSE 448
Cdd:PRK06164 400 RALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVP-VAFVIPTD 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 32563687 449 KV-TDEKEfekkLIGIMKKKVANYKVPKRVIVLDDLP---RNHITKVQKNVLRD 498
Cdd:PRK06164 479 GAsPDEAG----LMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLRE 528
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
163-486 |
6.75e-42 |
|
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: 156.99 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 EKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWG----FTGNDYNLHALPFYHVhglYYSL-HCSLFSHSTMI- 236
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDVYISYLPLAHI---FERVvEALFLYHGAKIg 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 -WRS--KFEVEDcIKYMKnATVMMGVPTFFSRL-------------LASKNFN--------------------------- 273
Cdd:cd05927 189 fYSGdiRLLLDD-IKALK-PTVFPGVPRVLNRIydkifnkvqakgpLKRKLFNfalnyklaelrsgvvraspfwdklvfn 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 274 --KEAFG-NVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE--AGVMTTNPlnGERKAGTVGPAVQGVGCRI----- 343
Cdd:cd05927 267 kiKQALGgNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEctAGATLTLP--GDTSVGHVGGPLPCAEVKLvdvpe 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 ----AKN----GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMV-ITGGLNVYPKELE 414
Cdd:cd05927 345 mnydAKDpnprGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIE 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563687 415 DFIDTLPFVKESAVIASPHPDFgeaVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIvLDDLPRN 486
Cdd:cd05927 425 NIYARSPFVAQIFVYGDSLKSF---LVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAI-LEDLVRL 492
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
25-496 |
4.21e-41 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 154.78 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 25 IVSQAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNP 104
Cdd:PRK05857 20 VFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 105 GYTESEAAHYIKDATPSILV----------SCNEELDKVFRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTS 174
Cdd:PRK05857 99 NLPIAAIERFCQITDPAAALvapgskmassAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKGAILTHGSLSNnAHDIVRDWG-----FTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIW-RSKFEVEDCIK 248
Cdd:PRK05857 179 GTTGEPKAVLLANRTFFA-VPDILQKEGlnwvtWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGgENTTSLLEILT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 249 YMKNATVMMgVPTFFSRLLASKNFNKEAFGNVRVFISGSA---PLSVSTIEEFRERTGQVilerYGMTEAGVM-----TT 320
Cdd:PRK05857 258 TNAVATTCL-VPTLLSKLVSELKSANATVPSLRLVGYGGSraiAADVRFIEATGVRTAQV----YGLSETGCTalclpTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 321 NPLNGERKAGTVGPAVQGVGCRIAKNGG----------------IEVKTNAIFAGYWKNPKKTAEEFTeDGWFKTGDVGH 384
Cdd:PRK05857 333 DGSIVKIEAGAVGRPYPGVDVYLAATDGigptapgagpsasfgtLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 385 LDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDE--KEFEKKLIG 462
Cdd:PRK05857 412 RREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESaaRALKHTIAA 491
|
490 500 510
....*....|....*....|....*....|....
gi 32563687 463 IMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK05857 492 RFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
29-498 |
9.17e-40 |
|
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: 151.11 E-value: 9.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFID--GDRKT-TYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPG 105
Cdd:cd05970 27 AKEYPDKLALVWCDdaGEERIfTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 106 YTESEAAHYIKDA-------------------------TPSILVSCNEELDKVFrdkirvINEDKLASEA-GSLNACTMI 159
Cdd:cd05970 106 LTAKDIVYRIESAdikmivaiaednipeeiekaapecpSKPKLVWVGDPVPEGW------IDFRKLIKNAsPDFERPTAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 160 EHVEKSDPASVCYTSGTTGLPK----------GAILT----HGSLSNNAHDIVRD--WGFTgndynlhalpfyhVHGLYY 223
Cdd:cd05970 180 SYPCGEDILLVYFSSGTTGMPKmvehdftyplGHIVTakywQNVREGGLHLTVADtgWGKA-------------VWGKIY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 224 S---LHCSLFSHSTMIWRSKFEVEDCIKYmkNATVMMGVPTFFsRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRE 300
Cdd:cd05970 247 GqwiAGAAVFVYDYDKFDPKALLEKLSKY--GVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 301 RTGQVILERYGMTEAGVMTTNPLNGERKAGTVG-PAVQ---------GVGCRIAKNGGIEVKTN-----AIFAGYWKNPK 365
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGkPAPGyeidlidreGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 366 KTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV 445
Cdd:cd05970 404 KTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 32563687 446 PSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05970 483 LAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
42-446 |
3.95e-39 |
|
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: 148.28 E-value: 3.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 42 DGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVmarvSKTTDTAALYIACLQ----IGALYIPVNPGYTESEAAHYIKD 117
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGL-RSLGVKAGEKV----ALFADNSPRWLIADQgimaLGAVDVVRGSDSSVEELLYILNH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 118 ATPSILVSCNEEldkvfrdkirvinedklaseagslnactmiehvekSDPASVCYTSGTTGLPKGAILTHGSLsnnAHDI 197
Cdd:cd17640 76 SESVALVVENDS-----------------------------------DDLATIIYTSGTTGNPKGVMLTHANL---LHQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 198 VRDWGFTGNDYN---LHALPFYHVHGL---YYSLHCSLFSHSTMIwrsKFEVEDCIKYmkNATVMMGVP----TFFSRL- 266
Cdd:cd17640 118 RSLSDIVPPQPGdrfLSILPIWHSYERsaeYFIFACGCSQAYTSI---RTLKDDLKRV--KPHYIVSVPrlweSLYSGIq 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 267 --LASKNFNKEAF-------GNVRVFISG--SAPLSVSTieeFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPA 335
Cdd:cd17640 193 kqVSKSSPIKQFLflfflsgGIFKFGISGggALPPHVDT---FFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 336 VQGVGCRI-----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKD-MVIT 403
Cdd:cd17640 270 LPGTEIKIvdpegnvvlppGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLS 349
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 32563687 404 GGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGeavvAIVVP 446
Cdd:cd17640 350 NGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVP 388
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
46-502 |
6.20e-39 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 148.75 E-value: 6.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 46 KTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL-- 123
Cdd:PRK06018 39 RTTYAQIHDRALKVSQAL-DRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVit 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 ----VSCNEEL-DKVFRDKIRVINEDKLASEAGSL-NACTMIEHVEKSD------------PASVCYTSGTTGLPKGAIL 185
Cdd:PRK06018 118 dltfVPILEKIaDKLPSVERYVVLTDAAHMPQTTLkNAVAYEEWIAEADgdfawktfdentAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 186 THGS------LSNNAHDIvrdwGFTGNDYNLHALPFYHVH--GLYYSLHCS----LFSHSTMIWRSKFEVEDCIKymknA 253
Cdd:PRK06018 198 SHRSnvlhalMANNGDAL----GTSAADTMLPVVPLFHANswGIAFSAPSMgtklVMPGAKLDGASVYELLDTEK----V 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 TVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVIlERYGMTEAGVMTT--------NPLNG 325
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVR-HAWGMTEMSPLGTlaalkppfSKLPG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 326 ERKAG---TVGPAVQGVGCRIAKNGGIE------------VKTNAIFAGYWknpKKTAEEFTEDGWFKTGDVGHLDEDGY 390
Cdd:PRK06018 349 DARLDvlqKQGYPPFGVEMKITDDAGKElpwdgktfgrlkVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 391 LTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVAN 470
Cdd:PRK06018 426 MRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAK 502
|
490 500 510
....*....|....*....|....*....|..
gi 32563687 471 YKVPKRVIVLDDLPRNHITKVQKNVLRDTYKN 502
Cdd:PRK06018 503 WWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
157-482 |
5.71e-37 |
|
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: 142.74 E-value: 5.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 157 TMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAH---DIVRDWgFTGNDYNLHALPFYHVHGLYYSLhCSLF--- 230
Cdd:cd17639 80 AIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAglgDRVPEL-LGPDDRYLAYLPLAHIFELAAEN-VCLYrgg 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 231 -----SHSTMIWRSKFEVE-DCIKYmkNATVMMGVP----------------------TFFSRLLASKN----------- 271
Cdd:cd17639 158 tigygSPRTLTDKSKRGCKgDLTEF--KPTLMVGVPaiwdtirkgvlaklnpmgglkrTLFWTAYQSKLkalkegpgtpl 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 272 FNKEAF--------GNVRVFISGSAPLSVSTiEEFRERTGQVILERYGMTE--AGVMTTNPlnGERKAGTVGPAVQGVGC 341
Cdd:cd17639 236 LDELVFkkvraalgGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTEtcAGGTVQDP--GDLETGRVGPPLPCCEI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 342 RI-----------AKN--GGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT-GGLN 407
Cdd:cd17639 313 KLvdweeggystdKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEY 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 408 VYPKELEDFIDTLPFVKESAVIASPHPDFgeaVVAIVVPSEK------------------VTDEKEFEKK----LIGIMK 465
Cdd:cd17639 393 IALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEKhltklaekhgvinseweeLCEDKKLQKAvlksLAETAR 469
|
410
....*....|....*...
gi 32563687 466 K-KVANYKVPKRVIVLDD 482
Cdd:cd17639 470 AaGLEKFEIPQGVVLLDE 487
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
166-484 |
6.70e-37 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 145.45 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSK----F 241
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDptdaL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 EVEDCI-KYmkNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE-AGVMT 319
Cdd:PRK08633 863 GIAKLVaKH--RATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATEtSPVAS 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 TNPLNGER---------KAGTVGPAVQGVGCRI-----------AKNGGIEVKTNAIFAGYWKNPKKTAE---EFTEDGW 376
Cdd:PRK08633 941 VNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEvikDIDGIGW 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 377 FKTGDVGHLDEDGYLTIGGR----SK---DMVITGGlnvypkeLEDFI------DTLPFvkesAVIASPHPDFGEAVVAI 443
Cdd:PRK08633 1021 YVTGDKGHLDEDGFLTITDRysrfAKiggEMVPLGA-------VEEELakalggEEVVF----AVTAVPDEKKGEKLVVL 1089
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 32563687 444 VVPSEkvTDEKEFEKKLIgimKKKVANYKVPKRVIVLDDLP 484
Cdd:PRK08633 1090 HTCGA--EDVEELKRAIK---ESGLPNLWKPSRYFKVEALP 1125
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
35-486 |
1.70e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 141.95 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVmarvskttdtaALY-----------IACLQIGALYIPVN 103
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQ-GLGPGDHV-----------GIYarnrieyveamLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 104 PGYTESEAAHYIKDATPSILV----------SCNEELDKVfRDKIRVINEDKLASEAGSLNACTMIEH-------VEKS- 165
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVyerefaprvaEVLPRLPKL-RTLVVVEDGSGNDLLPGAVDYEDALAAgsperdfGERSp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHgslsnnaHDIVRDwGFTGNDY-------NLHAL----------------PFYHVHGLY 222
Cdd:PRK07798 164 DDLYLLYTGGTTGMPKGVMWRQ-------EDIFRV-LLGGRDFatgepieDEEELakraaagpgmrrfpapPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 223 YSLHCSLFSHSTMIWRS-KFEVEDCIKYM--KNATVMMGVPTFFSRLLASKNFNKEAF--GNVRVFISGSAPLSVSTIEE 297
Cdd:PRK07798 236 AAFAALFSGQTVVLLPDvRFDADEVWRTIerEKVNVITIVGDAMARPLLDALEARGPYdlSSLFAIASGGALFSPSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 298 FRERTGQVIL-ERYGMTEAGVM-TTNPLNGERKAGT------------------VGPAVQGVGcRIAKNGGIEVktnaif 357
Cdd:PRK07798 316 LLELLPNVVLtDSIGSSETGFGgSGTVAKGAVHTGGprftigprtvvldedgnpVEPGSGEIG-WIARRGHIPL------ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 358 aGYWKNPKKTAEEFTE-DG--WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHP 434
Cdd:PRK07798 389 -GYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 32563687 435 DFGEAVVAIVVPSEKVT-DEKEfekkLIGIMKKKVANYKVPKRVIVLDDLPRN 486
Cdd:PRK07798 468 RWGQEVVAVVQLREGARpDLAE----LRAHCRSSLAGYKVPRAIWFVDEVQRS 516
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
163-500 |
1.95e-36 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 140.13 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 EKSDPASVCY-TSGTTGLPKGAILTHGSLSNNAHdivrdwGFTG-------NDYNLhaLPFYHVHGLyyslhcslfshst 234
Cdd:PRK07445 117 PNLETGWIMIpTGGSSGQIRFAIHTWETLTASVQ------GFQRyfqlqqvNSFCV--LPLYHVSGL------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 235 M-IWRS-----KFEVED--CIKYMKNATVMMG------VPTFFSRLLASknfNKEAFGNVRVFISGSAPLSVSTIEEfrE 300
Cdd:PRK07445 176 MqFMRSfltggKLVILPykRLKSGQELPPNPSdfflslVPTQLQRLLQL---RPQWLAQFRTILLGGAPAWPSLLEQ--A 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 301 RTGQVILE-RYGMTE--AGVMTTNP---LNGERKAGTVGPAVQgVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTed 374
Cdd:PRK07445 251 RQLQLRLApTYGMTEtaSQIATLKPddfLAGNNSSGQVLPHAQ-ITIPANQTGNITIQAQSLALGYYPQILDSQGIFE-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 375 gwfkTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEK 454
Cdd:PRK07445 328 ----TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 32563687 455 EFEKKLigimKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:PRK07445 404 ELKTAI----KDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
35-496 |
2.36e-36 |
|
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: 140.41 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEELDKVFRDKIRVINEDKL-ASEAGSLNACtmiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNN 193
Cdd:cd12117 90 LADAGAKVLLTDRSLAGRAGGLEVAVVIDEALdAGPAGNPAVP-----VSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 194 AHDivRDWG-FTGNDYNLHA--LPF----YHVHG-LYYSLHCSLFSHSTMIwrSKFEVEDCIKyMKNATVMMGVPTFFsR 265
Cdd:cd12117 165 VKN--TNYVtLGPDDRVLQTspLAFdastFEIWGaLLNGARLVLAPKGTLL--DPDALGALIA-EEGVTVLWLTAALF-N 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 266 LLAskNFNKEAFGNVRVFISGSAPLSVSTIEEFRERT-GQVILERYGMTEAGVMTTNPL--NGERKAGTV--GPAVQGVG 340
Cdd:cd12117 239 QLA--DEDPECFAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTSHVvtELDEVAGSIpiGRPIANTR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 CRIAKNGGIEVKTNA---IFA-------GYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGGRSKDMVITG 404
Cdd:cd12117 317 VYVLDEDGRPVPPGVpgeLYVggdglalGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 405 GLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEkEFEKKLigimKKKVANYKVPKRVIVLDDLP 484
Cdd:cd12117 397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAA-ELRAFL----RERLPAYMVPAAFVVLDELP 471
|
490
....*....|..
gi 32563687 485 RNHITKVQKNVL 496
Cdd:cd12117 472 LTANGKVDRRAL 483
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
47-497 |
4.07e-36 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 141.46 E-value: 4.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 47 TTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVS- 125
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 126 --CNEELDKVFRD--KIRVI------NEDKLASEAGSLNACTMIEH-------------VEKSDPASVCYTSGTTGLPKG 182
Cdd:PRK05620 119 prLAEQLGEILKEcpCVRAVvfigpsDADSAAAHMPEGIKVYSYEAlldgrstvydwpeLDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 183 AILTHGSLSNNAHDI--VRDWGFTGNDYNLHALPFYHVhgLYYSLHCSLF-SHSTMIWR-SKFEVEDCIKYMKNAT--VM 256
Cdd:PRK05620 199 VVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHV--LSWGVPLAAFmSGTPLVFPgPDLSAPTLAKIIATAMprVA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 257 MGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTT--NP---LNGERKAG- 330
Cdd:PRK05620 277 HGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTvaRPpsgVSGEARWAy 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 --TVGPAVQGVGCRIAKN-----------GGIEVKTNAIFAGYWKNPKKT----------------AEEFTEDGWFKTGD 381
Cdd:PRK05620 357 rvSQGRFPASLEYRIVNDgqvmestdrneGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLI 461
Cdd:PRK05620 437 VGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLR 516
|
490 500 510
....*....|....*....|....*....|....*.
gi 32563687 462 GIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK05620 517 DQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
71-497 |
1.03e-35 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 141.32 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 71 KGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDaTPSILVSCNEELDKVFRDKiRVINEDKLASEA 150
Cdd:PRK06060 54 SGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARN-TEPALVVTSDALRDRFQPS-RVAEAAELMSEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 151 GSLNACTMiEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRD-WGFTGNDYNLHALPFYHVHGLYYSLHCSL 229
Cdd:PRK06060 132 ARVAPGGY-EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 230 FSHSTMIWRS---KFEVEDCIKYMKNATVMMGVPTFFSRLLASknFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV- 305
Cdd:PRK06060 211 ATGGSAVINSapvTPEAAAILSARFGPSVLYGVPNFFARVIDS--CSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 306 ILERYGMTEAG-VMTTNPLNgERKAGTVGPAVQGVGCRI-AKNG-----GIE----VKTNAIFAGYWKNPKKTaeeFTED 374
Cdd:PRK06060 289 ILDGIGSTEVGqTFVSNRVD-EWRLGTLGRVLPPYEIRVvAPDGttagpGVEgdlwVRGPAIAKGYWNRPDSP---VANE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 375 GWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVP-SEKVTDE 453
Cdd:PRK06060 365 GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVAtSGATIDG 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 32563687 454 ---KEFEKKLIgimkKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK06060 445 svmRDLHRGLL----NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
35-505 |
2.42e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 138.54 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNpgyTESEAAH- 113
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASAL-ARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLN---TRLDAASi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 114 -YIKDATPSILVSCNEELDKVFRD--------KIRVINEDKLASEAGSLNACTMIEH-VEKSDPA-------------SV 170
Cdd:PRK08162 108 aFMLRHGEAKVLIVDTEFAEVAREalallpgpKPLVIDVDDPEYPGGRFIGALDYEAfLASGDPDfawtlpadewdaiAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 CYTSGTTGLPKGAILTH-GSLSNNAHDIVrDWGFTGNDYNLHALPFYHVHGLYYSLHCSLfSHSTMIWRSKFEVEDCIKY 249
Cdd:PRK08162 188 NYTSGTTGNPKGVVYHHrGAYLNALSNIL-AWGMPKHPVYLWTLPMFHCNGWCFPWTVAA-RAGTNVCLRKVDPKLIFDL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 250 MKNATV--MMGVPTFFSRLLASKNFNKEAF-GNVRVFISGSAPlSVSTIEEFRERtGQVILERYGMTE----AGVMTTNP 322
Cdd:PRK08162 266 IREHGVthYCGAPIVLSALINAPAEWRAGIdHPVHAMVAGAAP-PAAVIAKMEEI-GFDLTHVYGLTEtygpATVCAWQP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 323 ----LNGERKA------GTVGPAVQGV--------------GCRIaknGGIEVKTNAIFAGYWKNPKKTAEEFtEDGWFK 378
Cdd:PRK08162 344 ewdaLPLDERAqlkarqGVRYPLQEGVtvldpdtmqpvpadGETI---GEIMFRGNIVMKGYLKNPKATEEAF-AGGWFH 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 379 TGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfe 457
Cdd:PRK08162 420 TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASaTEEE-- 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 32563687 458 kkLIGIMKKKVANYKVPKRViVLDDLPRNHITKVQKNVLRDTYKNLFA 505
Cdd:PRK08162 498 --IIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQAKSLKA 542
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
38-497 |
1.37e-34 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 136.95 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 38 LLFIDGDRKT--TYGEFVKRTGQYATALtEKYNIKKGDRV---MARvskttdTAALYIA---CLQIGALYIPVNPGYTES 109
Cdd:PRK04319 63 LRYLDASRKEkyTYKELKELSNKFANVL-KELGVEKGDRVfifMPR------IPELYFAllgALKNGAIVGPLFEAFMEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 110 EAAHYIKDATPSILVSCNEELDKVFRDK------IRVINEDK--------LASEAGSLNACTMIEHVEKSDPASVCYTSG 175
Cdd:PRK04319 136 AVRDRLEDSEAKVLITTPALLERKPADDlpslkhVLLVGEDVeegpgtldFNALMEQASDEFDIEWTDREDGAILHYTSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGSLSnnAHDIVRDWGF-----------------TGNDYNLHAlPFyhVHGLyyslhcslfshSTMIWR 238
Cdd:PRK04319 216 STGKPKGVLHVHNAML--QHYQTGKYVLdlheddvywctadpgwvTGTSYGIFA-PW--LNGA-----------TNVIDG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 239 SKFEVEDCIKYMK--NATVMMGVPTFFSRLL--ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE 314
Cdd:PRK04319 280 GRFSPERWYRILEdyKVTVWYTAPTAIRMLMgaGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 315 AG-VMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTN-----AI-------FAGYWKNPKKTAEEFtEDGWFKTGD 381
Cdd:PRK04319 360 TGgIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNrmgnlAIkkgwpsmMRGIWNNPEKYESYF-AGDWYVSGD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLI 461
Cdd:PRK04319 439 SAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIR 518
|
490 500 510
....*....|....*....|....*....|....*.
gi 32563687 462 GIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK04319 519 GFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
35-501 |
1.69e-34 |
|
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: 135.69 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRK---TTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGytesea 111
Cdd:cd05908 1 PEGIIFILGDKKekfVSYRHLREEALGYLGAL-QELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 112 ahyikdatpsilvSCNEELDKVFRdKIRVINEDKLASEAGSLnaCTMIEHVeksdpASVCYTSGTTGLPKGAILTHGSLS 191
Cdd:cd05908 74 -------------SNEEHKLKLNK-VWNTLKNPYLITEEEVL--CELADEL-----AFIQFSSGSTGDPKGVMLTHENLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 192 NNAHDIVRDWGFTGNDYNLHALPFYHVHGL-------------YYSLHCSLFSHSTMIWRSKFEvedcikymKNATVMMG 258
Cdd:cd05908 133 HNMFAILNSTEWKTKDRILSWMPLTHDMGLiafhlapliagmnQYLMPTRLFIRRPILWLKKAS--------EHKATIVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 259 VPTFFSRLLAsKNFNKEAFGN-----VRVFISGSAPLSVSTIEEFRERTGQVILER------YGMTEAGVMTTNP----- 322
Cdd:cd05908 205 SPNFGYKYFL-KTLKPEKANDwdlssIRMILNGAEPIDYELCHEFLDHMSKYGLKRnailpvYGLAEASVGASLPkaqsp 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 323 -----------LNGERKAGT------------VGPAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAE 369
Cdd:cd05908 284 fktitlgrrhvTHGEPEPEVdkkdsecltfveVGKPIDETDIRICDEdnkilpdgyiGHIQIRGKNVTPGYYNNPEATAK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 370 EFTEDGWFKTGDVGHLdEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDF---GEAVVAIVVP 446
Cdd:cd05908 364 VFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGVNNSntrNEEIFCFIEH 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 447 SEKVTDEKEFEKKLigimkKKVANYKVP---KRVIVLDDLPRNHITKVQKNVLRDTYK 501
Cdd:cd05908 443 RKSEDDFYPLGKKI-----KKHLNKRGGwqiNEVLPIRRIPKTTSGKVKRYELAQRYQ 495
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
45-443 |
5.00e-34 |
|
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: 135.24 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVnpgYTES--EAAHYIKDATPS- 121
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI---YQDSmaEEVAYLLNYTGAr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 122 -ILVSCNEELDKVF--RDKI--------------------RVINEDKLASEAGSLNAC------TMIEHVEKSDPASVCY 172
Cdd:cd17641 86 vVIAEDEEQVDKLLeiADRIpsvryviycdprgmrkyddpRLISFEDVVALGRALDRRdpglyeREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 173 TSGTTGLPKGAILTHGSLSNNAHDIVR-DWGFTGNDYnLHALPFYHVHGLYYSLHCSLF---------SHSTM------- 235
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAaDPLGPGDEY-VSVLPLPWIGEQMYSVGQALVcgfivnfpeEPETMmedlrei 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 236 ----------IW-------RSKFEVEDCIK------YMKNA-----TVMMGVPT---------FFSRLLASKNFNKEAFG 278
Cdd:cd17641 245 gptfvllpprVWegiaadvRARMMDATPFKrfmfelGMKLGlraldRGKRGRPVslwlrlaswLADALLFRPLRDRLGFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 279 NVRVFISGSAPLSVSTIEEFRErTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTNAIFA 358
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSPGVFV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 359 GYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKD-MVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPdFG 437
Cdd:cd17641 404 GYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRP-YL 482
|
....*.
gi 32563687 438 EAVVAI 443
Cdd:cd17641 483 TAFICI 488
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-491 |
5.57e-34 |
|
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: 135.40 E-value: 5.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 31 LQSDPSKLLFI-DGD-----RKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNP 104
Cdd:cd17634 63 LRENGDRTAIIyEGDdtsqsRTISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 105 GYTESEAAHYIKDATPSILVSCNEeldkvFRDKIRVINEDKLASEAGSLNAcTMIEHV---------------------- 162
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADG-----GVRAGRSVPLKKNVDDALNPNV-TSVEHVivlkrtgsdidwqegrdlwwrd 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 --------------EKSDPASVCYTSGTTGLPKGAILTHGslsnnAHDIVRDWGFTgNDYNLHALPFY-----------H 217
Cdd:cd17634 216 liakaspehqpeamNAEDPLFILYTSGTTGKPKGVLHTTG-----GYLVYAATTMK-YVFDYGPGDIYwctadvgwvtgH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 218 VHGLYYSLHC---SLFSHSTMIWRSKFEVEDCIKyMKNATVMMGVPTFFSRLLAS--KNFNKEAFGNVRVFISGSAPLSV 292
Cdd:cd17634 290 SYLLYGPLACgatTLLYEGVPNWPTPARMWQVVD-KHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 293 STIEEFRERTGQV---ILERYGMTEAGVMTTNPLNG--ERKAGTVGPAVQGVGCRIAKNGGIEVKTNAI----------- 356
Cdd:cd17634 369 EAYEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEgnlvitdpwpg 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 357 --FAGYWKNPKKTAEEF-TEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPH 433
Cdd:cd17634 449 qtRTLFGDHERFEQTYFsTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPH 528
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 434 PDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKV 491
Cdd:cd17634 529 AIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
41-501 |
9.43e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 134.06 E-value: 9.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGD-RKTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDAT 119
Cdd:PRK07008 33 VEGDiHRYTYRDCERRAKQLAQALA-ALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 120 PSILVscneeLDKVF--------------RDKIRVINEDKLASEAGSLNACTMIEHVEKSD---PA-------SVCYTSG 175
Cdd:PRK07008 112 DRYVL-----FDLTFlplvdalapqcpnvKGWVAMTDAAHLPAGSTPLLCYETLVGAQDGDydwPRfdenqasSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 176 TTGLPKGAILTHGS--LSNNAHDIVRDWGFTGNDYNLHALPFYHVH--GLYYS---LHCSL-FSHSTMIWRSKFEVEDci 247
Cdd:PRK07008 187 TTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNawGLPYSaplTGAKLvLPGPDLDGKSLYELIE-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 248 kyMKNATVMMGVPTFFSRLLASKNFNKEAFGNV-RVFISGSA--PlsvSTIEEFRERTGQVILERYGMTEAGVM-TTNPL 323
Cdd:PRK07008 265 --AERVTFSAGVPTVWLGLLNHMREAGLRFSTLrRTVIGGSAcpP---AMIRTFEDEYGVEVIHAWGMTEMSPLgTLCKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 324 NGERKAGTV----------GPAVQGVGCRIAKNGGIE------------VKTNAIFAGYWKNpkktAEEFTEDGWFKTGD 381
Cdd:PRK07008 340 KWKHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRElpwdgkafgdlqVRGPWVIDRYFRG----DASPLVDGWFPTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDEkefekK 459
Cdd:PRK07008 416 VATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVkrPGAEVTRE-----E 490
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32563687 460 LIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYK 501
Cdd:PRK07008 491 LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
35-503 |
3.52e-33 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 132.66 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRVmARVSKttDTAALYIACLQI---GALYIPVNPGYTESEA 111
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALA-KRSIGPGSTV-AVIAP--NIPAMYEAHFGVpmaGAVVNCVNIRLNAPTI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 112 AhYIKDATPSILVSCNEELDKVFRDKIRVINEDKLAS--------------EAGSLNACT---MIEH---VEKSDPA--- 168
Cdd:PLN02479 110 A-FLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSfkppllivigdptcDPKSLQYALgkgAIEYekfLETGDPEfaw 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 169 ----------SVCYTSGTTGLPKGAILTH-----GSLSNnahDIVrdWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHS 233
Cdd:PLN02479 189 kppadewqsiALGYTSGTTASPKGVVLHHrgaylMALSN---ALI--WGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 234 TMIWR--SKFEVEDCIKYMKnATVMMGVPTFFSRLL-ASKnfnKEAF----GNVRVFISGSAP----LSVSTIEEFRert 302
Cdd:PLN02479 264 NICLRqvTAKAIYSAIANYG-VTHFCAAPVVLNTIVnAPK---SETIlplpRVVHVMTAGAAPppsvLFAMSEKGFR--- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 303 gqvILERYGMTEAGVMTT-------------------NPLNGERKAGTVGPAV------QGVGCRIAKNGGIEVKTNAIF 357
Cdd:PLN02479 337 ---VTHTYGLSETYGPSTvcawkpewdslppeeqarlNARQGVRYIGLEGLDVvdtktmKPVPADGKTMGEIVMRGNMVM 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 358 AGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFG 437
Cdd:PLN02479 414 KGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 438 EAVVAIVVPSEKV--TDEKEFEKKLIGIMKKKVANYKVPKRViVLDDLPRNHITKVQKNVLRDTYKNL 503
Cdd:PLN02479 493 ESPCAFVTLKPGVdkSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLRAKAKEM 559
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
15-496 |
3.58e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 129.35 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 15 LRAASSAANNIVSQAQLQSD--PSKLLFIDGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRV--MARVSKTTDTAALyi 90
Cdd:PRK13383 27 LREASRGGTNPYTLLAVTAArwPGRTAIIDDDGALSYRELQRATESLARRLT-RDGVAPGRAVgvMCRNGRGFVTAVF-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 91 ACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCNEeldkvFRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPAS- 169
Cdd:PRK13383 104 AVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE-----FAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRi 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 170 VCYTSGTTGLPKG---AILTHGSLSNNAHDIVRDWGFTGNDYNLhALPFYHVHGLYYsLHCSLFSHSTMIWRSKFEVEDC 246
Cdd:PRK13383 179 VLLTSGTTGKPKGvprAPQLRSAVGVWVTILDRTRLRTGSRISV-AMPMFHGLGLGM-LMLTIALGGTVLTHRHFDAEAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 247 IKY--MKNATVMMGVPTFFSRLL--ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGV-MTTN 321
Cdd:PRK13383 257 LAQasLHRADAFTAVPVVLARILelPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALAT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 PLNGERKAGTVGPAVQGVGCRIAKNGGIEVK---TNAIFAGYWKNPKKTAE---EFTEDGWFKTGDVGHLDEDGYLTIGG 395
Cdd:PRK13383 337 PADLRDAPETVGKPVAGCPVRILDRNNRPVGprvTGRIFVGGELAGTRYTDgggKAVVDGMTSTGDMGYLDNAGRLFIVG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 396 RSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PSEKVTDEkefekKLIGIMKKKVANYKV 473
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlhPGSGVDAA-----QLRDYLKDRVSRFEQ 491
|
490 500
....*....|....*....|...
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK13383 492 PRDINIVSSIPRNPTGKVLRKEL 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
41-486 |
1.01e-31 |
|
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: 129.98 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDT-AALYiACLQIGALYIPVNPGYTESEAAHYIKDAT 119
Cdd:COG1020 496 VFGDQSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMvVALL-AVLKAGAAYVPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 120 PSILVSCNEELDKVFRDKIRVINEDKLASEAGSlnACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVR 199
Cdd:COG1020 574 ARLVLTQSALAARLPELGVPVLALDALALAAEP--ATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQR 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 200 DWGFTGNDYNLHALPFYH---VHGLYYSLhCS-----LFSHSTMiwrskFEVEDCIKYMK--NATVMMGVPTFFSRLLAS 269
Cdd:COG1020 652 RYGLGPGDRVLQFASLSFdasVWEIFGAL-LSgatlvLAPPEAR-----RDPAALAELLArhRVTVLNLTPSLLRALLDA 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KNfnkEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILE-RYGMTEAGVMTT----NPLNGERKAGTVGPAVQGVGCRI- 343
Cdd:COG1020 726 AP---EALPSLRLVLVGGEALPPELVRRWRARLPGARLVnLYGPTETTVDSTyyevTPPDADGGSVPIGRPIANTRVYVl 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 --AKN------------GGIEVktnAifAGYWKNPKKTAE-----EFTEDG--WFKTGDVGHLDEDG---YLtigGRSKD 399
Cdd:COG1020 803 daHLQpvpvgvpgelyiGGAGL---A--RGYLNRPELTAErfvadPFGFPGarLYRTGDLARWLPDGnleFL---GRADD 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 400 MV-ITGglnvYPKELEDfIDT----LPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLigiMKKKVANYKVP 474
Cdd:COG1020 875 QVkIRG----FRIELGE-IEAallqHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA---LALLLPPYMVP 946
|
490
....*....|..
gi 32563687 475 KRVIVLDDLPRN 486
Cdd:COG1020 947 AAVVLLLPLPLT 958
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
45-502 |
1.20e-31 |
|
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: 128.59 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILV 124
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 SCN------------EELDKVFR------DKIRVINEDKLASEAGS----------LNACTMIEH--VEKSDPASVCYTS 174
Cdd:cd05967 160 TAScgiepgkvvpykPLLDKALElsghkpHHVLVLNRPQVPADLTKpgrdldwselLAKAEPVDCvpVAATDPLYILYTS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKGAILTHGslsnnAHDIVRDWGFTgNDYNLHALPFYH-------VHGLYYSLHCSLFSHSTMI----------- 236
Cdd:cd05967 240 GTTGKPKGVVRDNG-----GHAVALNWSMR-NIYGIKPGDVWWaasdvgwVVGHSYIVYGPLLHGATTVlyegkpvgtpd 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 ----WR--SKFEVedcikymknaTVMMGVPTFFSRL----LASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVI 306
Cdd:cd05967 314 pgafWRviEKYQV----------NALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 307 LERYGMTEAG-VMTTNPLNGER---KAGTVGPAVQGVGCRIAKNGGIEVKTNAI-------------FAGYWKNPKKTAE 369
Cdd:cd05967 384 IDHWWQTETGwPITANPVGLEPlpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELgniviklplppgcLLTLWKNDERFKK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 370 EFTED--GWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPS 447
Cdd:cd05967 464 LYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLK 543
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 32563687 448 EKVT-DEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKN 502
Cdd:cd05967 544 EGVKiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
29-484 |
3.24e-31 |
|
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: 125.85 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:cd17646 6 EQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVScneelDKVFRDKIRVINEDKLASEAGSLNACTM--IEHVEKSDPASVCYTSGTTGLPKGAILT 186
Cdd:cd17646 85 DRLAYMLADAGPAVVLT-----TADLAARLPAGGDVALLGDEALAAPPATppLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 187 HGSLSNNAHDIVRDWGFTGNDYNLHALPfyhvhglyyslhcslFSHSTMIWrskfevEDCIKYMKNATVMMGVPT----- 261
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTP---------------LSFDVSVW------ELFWPLVAGARLVVARPGghrdp 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 262 ----------------FFSRLLasknfnkEAFGNV----------RVFISGSApLSVSTIEEFRERTGQVILERYGMTEA 315
Cdd:cd17646 219 aylaalirehgvttchFVPSML-------RVFLAEpaagscaslrRVFCSGEA-LPPELAARFLALPGAELHNLYGPTEA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 316 GV-MTTNPLNGERKAGTV--GPAVQGVGCRIAKN---------------GGIEVKTnaifaGYWKNPKKTAEEFTEDgWF 377
Cdd:cd17646 291 AIdVTHWPVRGPAETPSVpiGRPVPNTRLYVLDDalrpvpvgvpgelylGGVQLAR-----GYLGRPALTAERFVPD-PF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 378 -------KTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKV 450
Cdd:cd17646 365 gpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 32563687 451 TDEKEFEkkligiMKKKVAN----YKVPKRVIVLDDLP 484
Cdd:cd17646 445 AGPDTAA------LRAHLAErlpeYMVPAAFVVLDALP 476
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-496 |
4.27e-31 |
|
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: 125.48 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVsCNEELDKVFRDKIRVINEDKLASEAGSLNACTMiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd12116 80 LEDAEPALVL-TDDALPDRLPAGLPVLLLALAAAAAAPAAPRTP---VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPF-YHVHGLyySLHCSLFSHSTMIWRSKFEVEDCIKYM-----KNATVMMGVPTFFsRLLA 268
Cdd:cd12116 156 HSMRERLGLGPGDRLLAVTTYaFDISLL--ELLLPLLAGARVVIAPRETQRDPEALArlieaHSITVMQATPATW-RMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 269 SKNFNKEAfgNVRVFISGSApLSVSTIEEFRERTGQVIlERYGMTEAGVMTTN----------PLnGERKAGT------- 331
Cdd:cd12116 233 DAGWQGRA--GLTALCGGEA-LPPDLAARLLSRVGSLW-NLYGPTETTIWSTAarvtaaagpiPI-GRPLANTqvyvlda 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 332 ----VGPAVQGVGCrIaknGGIEVKTnaifaGYWKNPKKTAEEFTEDG-------WFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:cd12116 308 alrpVPPGVPGELY-I---GGDGVAQ-----GYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIAspHPDFGEA-VVAIVVPSEKVT-DEKEFEKKLigimKKKVANYKVPKRVI 478
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVV--REDGGDRrLVAYVVLKAGAApDAAALRAHL----RATLPAYMVPSAFV 452
|
490
....*....|....*...
gi 32563687 479 VLDDLPRNHITKVQKNVL 496
Cdd:cd12116 453 RLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
41-496 |
5.25e-31 |
|
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: 124.73 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATP 120
Cdd:cd17643 7 VDEDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 121 SILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRD 200
Cdd:cd17643 86 SLLL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 201 WGFTGND--YNLHALPF----YHVHG-LYYSLHCSLFSHSTMiwRSKFEVEDCIKYMKnATVMMGVPTFFSRLLASKNFN 273
Cdd:cd17643 129 FGFNEDDvwTLFHSYAFdfsvWEIWGaLLHGGRLVVVPYEVA--RSPEDFARLLRDEG-VTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 274 KEAFGNVRVFISGSAPLSVSTIEEFRERTG----QVIlERYGMTEAGVMTT-NPLN----GERKAGTVGPAVQGVGCRIA 344
Cdd:cd17643 206 GRDPLALRYVIFGGEALEAAMLRPWAGRFGldrpQLV-NMYGITETTVHVTfRPLDaadlPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 KNGGIEVKTNAIFA----------GYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTIGGRSKDMVITGGLN 407
Cdd:cd17643 285 DADGRPVPPGVVGElyvsgagvarGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 408 VYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLigiMKKKVANYKVPKRVIVLDDLPRNH 487
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRAL---LKELLPDYMVPARYVPLDALPLTV 441
|
....*....
gi 32563687 488 ITKVQKNVL 496
Cdd:cd17643 442 NGKLDRAAL 450
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
165-497 |
9.27e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 122.46 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNdyNLHALPFYHVHGLYYSLHcSLFSHSTMI---WRSKF 241
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQ--WLLALPAHHIAGLQVLVR-SVIAGSEPVeldVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 EVEDcikyMKNATVMMGVPTFFSRL----LASKNFNKEAFGNVRVF---ISGSAPLSVSTIEEFRErTGQVILERYGMTE 314
Cdd:PRK07824 112 DPTA----LPRAVAELGGGRRYTSLvpmqLAKALDDPAATAALAELdavLVGGGPAPAPVLDAAAA-AGINVVRTYGMSE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 315 -AGvmttnplngerkaGTV--GPAVQGVGCRIAkNGGIEVKTNAIFAGYwKNPKKTAEeFTEDGWFKTGDVGHLDeDGYL 391
Cdd:PRK07824 187 tSG-------------GCVydGVPLDGVRVRVE-DGRIALGGPTLAKGY-RNPVDPDP-FAEPGWFRTDDLGALD-DGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANY 471
Cdd:PRK07824 250 TVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE---ALRAHVARTLDRT 326
|
330 340
....*....|....*....|....*.
gi 32563687 472 KVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK07824 327 AAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
35-497 |
1.09e-30 |
|
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: 124.02 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRL-RALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVScneeldkvfrdkirvinedklaseagslnactmiEHveKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd17649 80 LEDSGAGLLLT----------------------------------HH--PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPFYH---VHGLYYSLHC--SLFSHSTMIWRSkfEVEDCIKYMKNATVMMGVPTFFSRLLAs 269
Cdd:cd17649 124 QATAERYGLTPGDRELQFASFNFdgaHEQLLPPLICgaCVVLRPDELWAS--ADELAEMVRELGVTVLDLPPAYLQQLA- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KNFNKEAFGN---VRVFISGSAPLSVSTIEefRERTGQVIL-ERYGMTEAGVMTT--NPLNGERKAGT---VGPAVQGVG 340
Cdd:cd17649 201 EEADRTGDGRppsLRLYIFGGEALSPELLR--RWLKAPVRLfNAYGPTEATVTPLvwKCEAGAARAGAsmpIGRPLGGRS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 CRIAKNGGIEVKTNA----------IFAGYWKNPKKTAEEFTEDG-------WFKTGDVGHLDEDGYLTIGGRSKDMVIT 403
Cdd:cd17649 279 AYILDADLNPVPVGVtgelyiggegLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 404 GGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIVVPsEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDL 483
Cdd:cd17649 359 RGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVL-RAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARL 436
|
490
....*....|....
gi 32563687 484 PRNHITKVQKNVLR 497
Cdd:cd17649 437 PLTPNGKLDRKALP 450
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
32-484 |
2.15e-30 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 123.85 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYNIKKgDRVMARVSKTTDTAALYIACLQIGALYIPVNPgYTESEA 111
Cdd:PRK04813 13 QTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDK-SPIIVFGHMSPEMLATFLGAVKAGHAYIPVDV-SSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 112 AHYIKDATPSILVSCNEELDkVFRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLS 191
Cdd:PRK04813 91 IEMIIEVAKPSLIIATEELP-LEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 192 NNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYYSLhCS---LFS-HSTMIWRSK--FEVedcIKYMkNATVMMGVPTF 262
Cdd:PRK04813 170 SFTNWMLEDFALPEGPQFLNQAPYsfdLSVMDLYPTL-ASggtLVAlPKDMTANFKqlFET---LPQL-PINVWVSTPSF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQ-VILERYGMTEAGVMTT------------NPLN-GERK 328
Cdd:PRK04813 245 ADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSaTIYNTYGPTEATVAVTsieitdemldqyKRLPiGYAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 329 AGTVGPAVQGVGCRIA--KNGGIEVKTNAIFAGYWKNPKKTAEEF-TEDGW--FKTGDVGHLDeDGYLTIGGRSkDMVIT 403
Cdd:PRK04813 325 PDSPLLIIDEEGTKLPdgEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLE-DGLLFYQGRI-DFQIK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 404 ggLNVYPKELED---FIDTLPFVKESAVIasPHPDFG--EAVVAIVVPSE-KVTDEKEFEKKLIGIMKKKVANYKVPKRV 477
Cdd:PRK04813 403 --LNGYRIELEEieqNLRQSSYVESAVVV--PYNKDHkvQYLIAYVVPKEeDFEREFELTKAIKKELKERLMEYMIPRKF 478
|
....*..
gi 32563687 478 IVLDDLP 484
Cdd:PRK04813 479 IYRDSLP 485
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
144-484 |
2.22e-30 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 125.85 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 144 DKLASEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYY 223
Cdd:PRK06814 772 DKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTG 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 224 SLHCSLFSH-------STMIWRSkfeVEDCIkYMKNATVMMGVPTFFSrllaskNFNKEA----FGNVRVFISGSAPLSV 292
Cdd:PRK06814 852 GLVLPLLSGvkvflypSPLHYRI---IPELI-YDTNATILFGTDTFLN------GYARYAhpydFRSLRYVFAGAEKVKE 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 293 STIEEFRERTGQVILERYGMTEAG-VMTTN-PLNGerKAGTVGPAVQGVGCRIAKNGGIE------VKTNAIFAGYWKNP 364
Cdd:PRK06814 922 ETRQTWMEKFGIRILEGYGVTETApVIALNtPMHN--KAGTVGRLLPGIEYRLEPVPGIDeggrlfVRGPNVMLGYLRAE 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 365 KKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIv 444
Cdd:PRK06814 1000 NPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILL- 1078
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 32563687 445 vpsekvTDEKEFEKK-LIGIMKKK-VANYKVPKRVIVLDDLP 484
Cdd:PRK06814 1079 ------TTASDATRAaFLAHAKAAgASELMVPAEIITIDEIP 1114
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
35-486 |
9.97e-30 |
|
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: 121.35 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYteseaahy 114
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 ikdatPSilvscneeldkvfrDKIRVINEDKLASeagslnacTMIehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd17648 73 -----PD--------------ERIQFILEDTGAR--------VVI--TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYnlHALPFYHVHGLYYSLH---CSLFSHSTMIWRS---KFEVEDCIKYMKN--ATVMMGVPTFFSRL 266
Cdd:cd17648 124 TSLSERYFGRDNGD--EAVLFFSNYVFDFFVEqmtLALLNGQKLVVPPdemRFDPDRFYAYINRekVTYLSGTPSVLQQY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 267 -LASKNFNKeafgnvRVFISGSApLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPL--NGERKAGTVGPAVQGVGCRI 343
Cdd:cd17648 202 dLARLPHLK------RVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFfpGDQRFDKSLGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 AKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDGW--------------FKTGDVGHLDEDGYLTIGGRSKD 399
Cdd:cd17648 275 LNDAMKRVPVGAVgelylggdgvARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 400 MVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAV-----VAIVVPSEKVTDEKEfekkLIGIMKKKVANYKVP 474
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYYLPEPGHVPESD----LLSFLRAKLPRYMVP 430
|
490
....*....|..
gi 32563687 475 KRVIVLDDLPRN 486
Cdd:cd17648 431 ARLVRLEGIPVT 442
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
165-450 |
2.04e-29 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 122.13 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVH-------GLYYSLHCSLFSHSTMiw 237
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYervnqivMLHYGVAVGFYQGDNL-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 238 rskfEVEDCIKYMKnATVMMGVPTFFSRL-------------LASKNFN------KEAF--------------------- 277
Cdd:PLN02736 299 ----KLMDDLAALR-PTIFCSVPRLYNRIydgitnavkesggLKERLFNaaynakKQALengknpspmwdrlvfnkikak 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 --GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAK---------- 345
Cdd:PLN02736 374 lgGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytsed 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 346 ----NGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMV-ITGGLNVYPKELEDFIDTL 420
Cdd:PLN02736 454 qpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKC 533
|
330 340 350
....*....|....*....|....*....|.
gi 32563687 421 PFVKESAViaspHPD-FGEAVVAIVVPSEKV 450
Cdd:PLN02736 534 KFVAQCFV----YGDsLNSSLVAVVVVDPEV 560
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-500 |
2.64e-29 |
|
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: 121.44 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 24 NIVSQAQ---LQSDPSKLLFI----DGDRKT-TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQI 95
Cdd:cd05968 61 NIVEQLLdkwLADTRTRPALRwegeDGTSRTlTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 96 GALYIPVNPGYTESEAAHYIKDATPSIL------------VSCNEELDKVFR-----DKIRVINEDKLASEAGSLNACTM 158
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALitadgftrrgreVNLKEEADKACAqcptvEKVVVVRHLGNDFTPAKGRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 159 IEHVEKS----------DPASVCYTSGTTGLPKGAILTHGSLSNNAhdiVRDWGFTGN-----------DYNLHALPFYH 217
Cdd:cd05968 220 DEEKETAgdgaerteseDPLMIIYTSGTTGKPKGTVHVHAGFPLKA---AQDMYFQFDlkpgdlltwftDLGWMMGPWLI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 218 VHGLYYSLHCSL------FSHSTMIWR--SKFEVedcikymknatVMMGVPTFFSRLLASKN---FNKEAFGNVRVFISG 286
Cdd:cd05968 297 FGGLILGATMVLydgapdHPKADRLWRmvEDHEI-----------THLGLSPTLIRALKPRGdapVNAHDLSSLRVLGST 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 287 SAPLSVSTIEEFRERTGQ---VILERYGMTE--AGVMTTNPLNgERKAGTVGPAVQGVGCRIAKNGGI----EVKTNAIF 357
Cdd:cd05968 366 GEPWNPEPWNWLFETVGKgrnPIINYSGGTEisGGILGNVLIK-PIKPSSFNGPVPGMKADVLDESGKparpEVGELVLL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 358 A-------GYWKNPKKTAEEFTE--DGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAV 428
Cdd:cd05968 445 ApwpgmtrGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAA 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563687 429 IASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTY 500
Cdd:cd05968 525 IGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAY 596
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
32-474 |
2.73e-29 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 119.98 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEA 111
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQ-GVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 112 AHyikdatpsILVSCNEELDKVFRDKIRVINEDKLaseagSLNACTMIEHVEKSD--PASVCYTSGTTGLPKGAILTHGS 189
Cdd:PRK09029 93 EE--------LLPSLTLDFALVLEGENTFSALTSL-----HLQLVEGAHAVAWQPqrLATMTLTSGSTGLPKAAVHTAQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 190 LSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYsLHCSLFSHSTMIWRSKFEVEDCIKYMKNATVmmgVPTFFSRLLAS 269
Cdd:PRK09029 160 HLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKQPLEQALAGCTHASL---VPTQLWRLLDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KnfnKEAFGNVRVFISGSApLSVSTIEEFRER-----TGqvilerYGMTEAGVMTTNPLNgERKAGtVGPAVQGVGCRIA 344
Cdd:PRK09029 236 R---SEPLSLKAVLLGGAA-IPVELTEQAEQQgircwCG------YGLTEMASTVCAKRA-DGLAG-VGSPLPGREVKLV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 kNGGIEVKTNAIFAGYWKNPKKTAeeFT-EDGWFKTGDVGHLDeDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFV 423
Cdd:PRK09029 304 -DGEIWLRGASLALGYWRQGQLVP--LVnDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLV 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 32563687 424 KESAVIASPHPDFGEAVVAIVvpsekVTDEKEFEKKLIGIMKKKVANYKVP 474
Cdd:PRK09029 380 QQVFVVPVADAEFGQRPVAVV-----ESDSEAAVVNLAEWLQDKLARFQQP 425
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
138-498 |
3.16e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 120.56 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 138 IRVINEDKLASE---AGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALP 214
Cdd:PRK07867 122 VRVINVDSPAWAdelAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 215 FYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCIKYmkNATVMMGVPTFFSRLLAS-------KNFNKEAFGNvrvf 283
Cdd:PRK07867 202 LFHSNAVMAGWAVALAAGASIALRRKFSAsgflPDVRRY--GATYANYVGKPLSYVLATperpddaDNPLRIVYGN---- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 284 iSGSAPlsvsTIEEFRERTGQVILERYGMTEAGV-MTTNPlngERKAGTVGPAVQGVG---------CRIAK--NGGIEV 351
Cdd:PRK07867 276 -EGAPG----DIARFARRFGCVVVDGFGSTEGGVaITRTP---DTPPGALGPLPPGVAivdpdtgteCPPAEdaDGRLLN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 352 KTNAI-----------FAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTL 420
Cdd:PRK07867 348 ADEAIgelvntagpggFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32563687 421 PFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEFEKKLIGimKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK07867 427 PDATEVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
30-498 |
3.34e-29 |
|
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: 121.13 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 30 QLQSDPSKLLFI----DGD--RKTTYGEFVKRTGQYATALTEKYnIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVN 103
Cdd:cd05966 62 HLKERGDKVAIIwegdEPDqsRTITYRELLREVCRFANVLKSLG-VKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 104 PGYTESEAAHYIKDATPSILVSCNEeldkVFRDKiRVINEDKLASEAgsLNACTMIEHV--------------------- 162
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVITADG----GYRGG-KVIPLKEIVDEA--LEKCPSVEKVlvvkrtggevpmtegrdlwwh 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 ---------------EKSDPASVCYTSGTTGLPKGAILTHGSlsnnahdivrdwgftgndYNLHAlpfyhvhglyyslhc 227
Cdd:cd05966 214 dlmakqspecepewmDSEDPLFILYTSGSTGKPKGVVHTTGG------------------YLLYA--------------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 228 slfsHSTMIWrsKFEVED-----C------------IKY---MKNATVMM--GVPTF--FSRL----------------L 267
Cdd:cd05966 261 ----ATTFKY--VFDYHPddiywCtadigwitghsyIVYgplANGATTVMfeGTPTYpdPGRYwdivekhkvtifytapT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 268 ASKNFNKeaFGN----------VRVFISGSAPLSVSTIEEFRERTGQ---VILERYGMTEAG-VMTTnPLNG--ERKAGT 331
Cdd:cd05966 335 AIRALMK--FGDewvkkhdlssLRVLGSVGEPINPEAWMWYYEVIGKercPIVDTWWQTETGgIMIT-PLPGatPLKPGS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 332 VGPAVQGVGCRIAKNGGIEVKTNA------------IFAGYWKNPKKTAEEFTED--GWFKTGDVGHLDEDGYLTIGGRS 397
Cdd:cd05966 412 ATRPFFGIEPAILDEEGNEVEGEVegylvikrpwpgMARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 398 KDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRV 477
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKI 571
|
570 580
....*....|....*....|.
gi 32563687 478 IVLDDLPRNHITKVQKNVLRD 498
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILRK 592
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
35-484 |
4.16e-29 |
|
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: 119.68 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAA-GVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCnEELDKVFRDKIRVINEDKLASEAGSLNACTMiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd12114 80 LADAGARLVLTD-GPDAQLDVAVFDVLILDLDALAAPAPPPPVD---VAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGND--YNLHALPF----YHVHGLyyslhcsLFSHSTMIWRSKFEVEDCIKYMK-----NATVMMGVPTFF 263
Cdd:cd12114 156 LDINRRFAVGPDDrvLALSSLSFdlsvYDIFGA-------LSAGATLVLPDEARRRDPAHWAElierhGVTLWNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 264 SRLLASKNFNKEAFGNVR-VFISGS-APLSV-STIEEFRERTGQVILEryGMTEAGVMTT----NPLNGERKAGTVGPAV 336
Cdd:cd12114 229 EMLLDVLEAAQALLPSLRlVLLSGDwIPLDLpARLRALAPDARLISLG--GATEASIWSIyhpiDEVPPDWRSIPYGRPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 337 QGVGCRIAKNGGIEVK---TNAIFA-------GYWKNPKKTAEEFTEDG----WFKTGDVGHLDEDGYLTIGGRSKDMVI 402
Cdd:cd12114 307 ANQRYRVLDPRGRDCPdwvPGELWIggrgvalGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 403 TGGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIVVPSEKVTdeKEFEKKLIGIMKKKVANYKVPKRVIVLDD 482
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGT--PIAPDALRAFLAQTLPAYMIPSRVIALEA 463
|
..
gi 32563687 483 LP 484
Cdd:cd12114 464 LP 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-497 |
8.95e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 121.43 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 19 SSAANNIVSQAQLQSDPSKLLFI----DGDRKTTYGEFVKRTGQYATALTEkyNIKKGDRVMARVSKTTDTAALYIACLQ 94
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFLaddpGEGVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 95 IGALYIPVNPgyTESEAAHY-------IKDATPSILVScneelDKVFRDKIRVINEDKLASEAGSLNACTMIE------- 160
Cdd:PRK05691 87 AGVIAVPAYP--PESARRHHqerllsiIADAEPRLLLT-----VADLRDSLLQMEELAAANAPELLCVDTLDPalaeawq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 161 --HVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGN--DYNLHALPFYHVHGLYYSLHCSLFSHSTMI 236
Cdd:PRK05691 160 epALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 WRS-KFEVEDCIKYMKNAT----VMMGVPTFFSRL----LASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRER------ 301
Cdd:PRK05691 240 LMSpAYFLERPLRWLEAISeyggTISGGPDFAYRLcserVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKfaacgf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 302 TGQVILERYGMTEAGVMTTNPLNGE---------------RKAGTVGPAVQGVG-------CRIAKNGGIEVKTN----- 354
Cdd:PRK05691 320 DPDSFFASYGLAEATLFVSGGRRGQgipaleldaealarnRAEPGTGSVLMSCGrsqpghaVLIVDPQSLEVLGDnrvge 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 ------AIFAGYWKNPKKTAEEFTE-DG--WFKTGDVGHLdEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDT-LPFVK 424
Cdd:PRK05691 400 iwasgpSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVR 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 425 ESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVAN--YKVPKRVIVLDD--LPRNHITKVQKNVLR 497
Cdd:PRK05691 479 KGRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEacQEAPSVVLLLNPgaLPKTSSGKLQRSACR 555
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
28-496 |
1.09e-28 |
|
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: 118.58 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFidGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:cd17655 6 QAEKTPDHTAVVF--EDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 EsEAAHYI-KDATPSILVScNEELDK--VFRDKIRVINEDKLASEAGslnacTMIEHVEKS-DPASVCYTSGTTGLPKGA 183
Cdd:cd17655 83 E-ERIQYIlEDSGADILLT-QSHLQPpiAFIGLIDLLDEDTIYHEES-----ENLEPVSKSdDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 184 ILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFY---HVHGLYYSLhcsLFSHSTMIWR--SKFEVEDCIKYMK--NATVM 256
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASL---LSGNTLYIVRkeTVLDGQALTQYIRqnRITII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 257 MGVPTFFSRLLASKNFNKEafgNVRVFISGSAPLSVSTIEEFRERTGQ--VILERYGMTEAGV--MTTNPLNGERKAGTV 332
Cdd:cd17655 233 DLTPAHLKLLDAADDSEGL---SLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdaSIYQYEPETDQQVSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 333 --GPAVQGVGCRIAKNGG----------IEVKTNAIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIG 394
Cdd:cd17655 310 piGKPLGNTRIYILDQYGrpqpvgvageLYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 395 GRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSE--KVTDEKEFekkligiMKKKVANYK 472
Cdd:cd17655 390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKelPVAQLREF-------LARELPDYM 462
|
490 500
....*....|....*....|....
gi 32563687 473 VPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd17655 463 IPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-496 |
1.36e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.65 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVSCNEELDKVFR-DKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILT 186
Cdd:PRK12467 598 QDRLAYMLDDSGVRLLLTQSHLLAQLPVpAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 187 HGSLSNNAHDIVRDWGFTGNDYNLHALPFyHVHGLYYSLHCSLFSHSTMIWRSK---FEVEDCIKYM--KNATVMMGVPT 261
Cdd:PRK12467 678 HGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMadQGVTVLKIVPS 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 262 FFSRLLASKNfNKEAFGNVRVFISGSApLSVSTIEEFRERTGQV-ILERYGMTEAGV-MTTNPLNGE---RKAGTVGPAV 336
Cdd:PRK12467 757 HLQALLQASR-VALPRPQRALVCGGEA-LQVDLLARVRALGPGArLINHYGPTETTVgVSTYELSDEerdFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 337 QGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTIGGRSKD 399
Cdd:PRK12467 835 ANLGLYILDHylnpvpvgvvGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDH 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 400 MVITGGLNVYPKELEDFIDTLPFVKESAVIASPHpDFGEAVVAIVVPSEKVTDEK--EFEKKLIGIMKKKVANYKVPKRV 477
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLVAYLVPAAVADGAEhqATRDELKAQLRQVLPDYMVPAHL 993
|
490
....*....|....*....
gi 32563687 478 IVLDDLPRNHITKVQKNVL 496
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-484 |
2.16e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYP 3142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVScNEELDKVFRDKIRVINEDKLASEAGSLNACTmieHVEKSDPASVCYTSGTTGLPKGAILTH 187
Cdd:PRK12316 3143 EERLAYMLEDSGAQLLLS-QSHLRLPLAQGVQVLDLDRGDENYAEANPAI---RTMPENLAYVIYTSGSTGKPKGVGIRH 3218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSNNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYYSLH--CSLFSHSTMIWRSKFEVEDCIKyMKNATVMMGVPTF 262
Cdd:PRK12316 3219 SALSNHLCWMQQAYGLGVGDRVLQFTTFsfdVFVEELFWPLMsgARVVLAGPEDWRDPALLVELIN-SEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKeaFGNVRVFISGSAPLSVSTIEefRERTGQVILERYGMTEAGVMTTNPLNGERKAGT--VGPAVQGVG 340
Cdd:PRK12316 3298 LQAFLEEEDAHR--CTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 CRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGGRSKDMVITG 404
Cdd:PRK12316 3374 CYILDGSLEPVPVGALgelylggeglARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIR 3453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 405 GLNVYPKELEDFIDTLPFVKESAVIAsphpDFGEAVVAIVVPSEKVTDEKEFEKKligIMKKKVANYKVPKRVIVLDDLP 484
Cdd:PRK12316 3454 GFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAGDLREALKA---HLKASLPEYMVPAHLLFLERMP 3526
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
35-496 |
3.41e-28 |
|
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: 117.19 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEELDKVFRDKIRVINEDKLASEAGSLNACTMiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSN-N 193
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYI---NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNlL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 194 AHDIVRDWGFTGNDYNLHALPFYHVhgLYYSLHCSLFSHSTM-IWR--SKFEVEDCIKYMKNATV-MMGVPTFFSRLLAS 269
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDV--CYQEIFSTLLSGGTLyIIReeTKRDVEQLFDLVKRHNIeVVFLPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 -KNFNKEAFGNVRVFISGSAPLSVStiEEFRE--RTGQVILER-YGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCR--- 342
Cdd:cd17656 236 eREFINRFPTCVKHIITAGEQLVIT--NEFKEmlHEHNVHLHNhYGPSETHVVTTYTINPEAEIPELPPIGKPISNTwiy 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 343 ----------IAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGGRSKDMVITGGL 406
Cdd:cd17656 314 ildqeqqlqpQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 407 NVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKkligiMKKKVANYKVPKRVIVLDDLPRN 486
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREY-----LAKQLPEYMIPSFFVPLDQLPLT 468
|
490
....*....|
gi 32563687 487 HITKVQKNVL 496
Cdd:cd17656 469 PNGKVDRKAL 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
43-497 |
3.41e-28 |
|
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: 117.53 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 43 GDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSI 122
Cdd:cd05915 21 EVHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 123 LVsCNEELDKVFRDKIRVIN---------------EDKLASEAGSLNActmIEHVEKSDPASVCYTSGTTGLPKGAILTH 187
Cdd:cd05915 100 LL-FDPNLLPLVEAIRGELKtvqhfvvmdekapegYLAYEEALGEEAD---PVRVPERAACGMAYTTGTTGLPKGVVYSH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 --GSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE---DCIKYMKnATVMMGVPTF 262
Cdd:cd05915 176 raLVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPAslvELFDGEG-VTFTAGVPTV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFG-NVRVFISGSAP----LSVSTIEEFRERTGQVILERYGMTEA----------------GVMTTN 321
Cdd:cd05915 255 WLALADYLESTGHRLKtLRRLVVGGSAAprslIARFERMGVEVRQGYGLTETSPVVVQnfvkshleslseeeklTLKAKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 322 PLNGERKAGTV-GPAVQGVGCRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:cd05915 335 GLPIPLVRLRVaDEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVvpseKVTDEKEFEKKLIGIMKKKVANYK-VPKRVIV 479
Cdd:cd05915 415 IKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV----VPRGEKPTPEELNEHLLKAGFAKWqLPDAYVF 490
|
490
....*....|....*...
gi 32563687 480 LDDLPRNHITKVQKNVLR 497
Cdd:cd05915 491 AEEIPRTSAGKFLKRALR 508
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
166-485 |
4.65e-28 |
|
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: 114.32 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSL--SNNAHDIVRDWgfTGNDYNLHALPFYHVHGLYYSL---HCSlfshSTMIWRSK 240
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALlaQALVLAVLQAI--DEGTVFLNSGPLFHIGTLMFTLatfHAG----GTNVFVRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 241 FEVE---DCIKYMKNATVMMGVPTffsrLLASKNFNKEAFGNVRVFISGSAP------LSVSTIEEFRERTGqvilerYG 311
Cdd:cd17636 75 VDAEevlELIEAERCTHAFLLPPT----IDQIVELNADGLYDLSSLRSSPAApewndmATVDTSPWGRKPGG------YG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 312 MTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTN----------AIFAGYWKNPKKTAEEFTeDGWFKTGD 381
Cdd:cd17636 145 QTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGevgeivargpTVMAGYWNRPEVNARRTR-GGWHHTND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVT-DEKEfekkL 460
Cdd:cd17636 224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASvTEAE----L 299
|
330 340
....*....|....*....|....*
gi 32563687 461 IGIMKKKVANYKVPKRVIVLDDLPR 485
Cdd:cd17636 300 IEHCRARIASYKKPKSVEFADALPR 324
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-485 |
4.72e-28 |
|
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: 117.06 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVscneeLDKVFRDKIRVINEDKLASEAGSLNACTMIEHV---EKSDPASVCYTSGTTGLPKGAIL 185
Cdd:cd17651 82 ERLAFMLADAGPVLVL-----THPALAGELAVELVAVTLLDQPGAAAGADAEPDpalDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 186 THGSLSN--NAHDIVRDWGFTGNDYNLHALPF-YHVHGLYYSLHCSlfshSTMIWRSKFEVEDCIKYM----KNATVMMG 258
Cdd:cd17651 157 PHRSLANlvAWQARASSLGPGARTLQFAGLGFdVSVQEIFSTLCAG----ATLVLPPEEVRTDPPALAawldEQRISRVF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 259 VPTFFSRLLASKNFNKEAFG-NVRVFISGSAPLSV-STIEEF-RERTGQVILERYGMTEAGVMTTNPLNGE----RKAGT 331
Cdd:cd17651 233 LPTVALRALAEHGRPLGVRLaALRYLLTGGEQLVLtEDLREFcAGLPGLRLHNHYGPTETHVVTALSLPGDpaawPAPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 332 VGPAVQGVGCRIAKNGGIEVKTN----------AIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGG 395
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGvpgelyiggaGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 396 RSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPK 475
Cdd:cd17651 393 RADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPS 469
|
490
....*....|
gi 32563687 476 RVIVLDDLPR 485
Cdd:cd17651 470 AFVLLDALPL 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
35-496 |
5.05e-28 |
|
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: 116.41 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNA 194
Cdd:cd17650 80 LEDSGAKLLL-------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 195 HDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIW---RSKFEVEDCIKYMKN--ATVMMGVPTFFSRLLAS 269
Cdd:cd17650 123 HAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVIcpdEVKLDPAALYDLILKsrITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 270 KNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQ--VILERYGMTEAGVMTT---NPLNGERKAGTV------------ 332
Cdd:cd17650 203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQgmRIINSYGVTEATIDSTyyeEGRDPLGDSANVpigrplpntamy 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 333 ------GPAVQGVGCRIAKNGGievktnAIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:cd17650 283 vlderlQPQPVGVAGELYIGGA------GVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 401 VITGGLNVYPKELEDFIDTLPFVKESAVIASpHPDFGEA-VVAIVVPSEKVtDEKEFEKKLIgimkKKVANYKVPKRVIV 479
Cdd:cd17650 357 VKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEArLCAYVVAAATL-NTAELRAFLA----KELPSYMIPSYYVQ 430
|
490
....*....|....*..
gi 32563687 480 LDDLPRNHITKVQKNVL 496
Cdd:cd17650 431 LDALPLTPNGKVDRRAL 447
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
172-429 |
2.43e-27 |
|
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: 115.53 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 172 YTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFT----GNDYNLHALPFYHVHGLYYSLHCSLfSHSTMIWrskFEVEDCI 247
Cdd:cd05933 157 YTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpatvGQESVVSYLPLSHIAAQILDIWLPI-KVGGQVY---FAQPDAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 248 KY-----MKNA--TVMMGVP-----------------TFFSRLLAS-----------KNFNKE----------------- 275
Cdd:cd05933 233 KGtlvktLREVrpTAFMGVPrvwekiqekmkavgaksGTLKRKIASwakgvgletnlKLMGGEspsplfyrlakklvfkk 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 276 -----AFGNVRVFISGSAPLSVSTIEEFRErTGQVILERYGMTE-AGVMTTNPLNGERkAGTVGPAVQGVGCRIAK---- 345
Cdd:cd05933 313 vrkalGLDRCQKFFTGAAPISRETLEFFLS-LNIPIMELYGMSEtSGPHTISNPQAYR-LLSCGKALPGCKTKIHNpdad 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 346 -NGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMVIT-GGLNVYPKELEDFIDT-LPF 422
Cdd:cd05933 391 gIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIEDAVKKeLPI 470
|
....*..
gi 32563687 423 VKESAVI 429
Cdd:cd05933 471 ISNAMLI 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-498 |
2.68e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.80 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 25 IVSQAQLQSDPSKLLFidGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNP 104
Cdd:PRK12467 3101 IEAQVARTPEAPALVF--GDQQLSYAELNRRANRLAHRLIAI-GVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDP 3177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 105 GYTESEAAHYIKDATPSILVSCN---EELDKVFRDKIRVINEDKLASEAgslNACTMIeHVEKSDPASVCYTSGTTGLPK 181
Cdd:PRK12467 3178 EYPRERLAYMIEDSGVKLLLTQAhllEQLPAPAGDTALTLDRLDLNGYS---ENNPST-RVMGENLAYVIYTSGSTGKPK 3253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 182 GAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYH---VHGLYYSLHC--SLFSHSTMIWRSKfEVEDCIKYmKNATVM 256
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFdgaQERFLWTLICggCLVVRDNDLWDPE-ELWQAIHA-HRISIA 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 257 MGVPTFFSRLLASKnfNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILER-YGMTEAGVMTTN---PLNG--ERKAG 330
Cdd:PRK12467 3332 CFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNgYGPTEAVVTVTLwkcGGDAvcEAPYA 3409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 TVGPAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTI 393
Cdd:PRK12467 3410 PIGRPVAGRSIYVLDGqlnpvpvgvaGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEY 3489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 394 GGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKV 473
Cdd:PRK12467 3490 LGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPADPQGDWRE---TLRDHLAASLPDYMV 3565
|
490 500
....*....|....*....|....*
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK12467 3566 PAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
155-498 |
1.14e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 113.20 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 155 ACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHST 234
Cdd:PRK13388 140 ALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 235 MIWRSKFE----VEDCIKYmkNATVMMGVPTFFSRLLAS-------KNFNKEAFGNvrvfisgsaPLSVSTIEEFRERTG 303
Cdd:PRK13388 220 VALPAKFSasgfLDDVRRY--GATYFNYVGKPLAYILATperpddaDNPLRVAFGN---------EASPRDIAEFSRRFG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 304 QVILERYGMTEAGVMTTNPLNGerKAGTVGPAVQGVG---------CRIAK---NGGIEVKTNAI-----------FAGY 360
Cdd:PRK13388 289 CQVEDGYGSSEGAVIVVREPGT--PPGSIGRGAPGVAiynpetlteCAVARfdaHGALLNADEAIgelvntagagfFEGY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 361 WKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAV 440
Cdd:PRK13388 367 YNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQV 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563687 441 VAIVVPSEKVT-DEKEFEKKLIGI--MKKKVAnykvPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK13388 446 MAALVLRDGATfDPDAFAAFLAAQpdLGTKAW----PRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-496 |
1.39e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 114.67 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:PRK12316 2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVSCNEELDKV-FRDKIRVINEDKLASEAGSLNACTMIEhVEKSDPASVCYTSGTTGLPKGAILTH 187
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRHLLERLpLPAGVARLPLDRDAEWADYPDTAPAVQ-LAGENLAYVIYTSGSTGLPKGVAVSH 2168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSNNAHDIVRDWGFTGNDYNLHALPFyHVHGLYYSLHCSLFSHSTMIWR--SKFEVEDCIKYMKNATVMMGV-PTFFS 264
Cdd:PRK12316 2169 GALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDfPPVYL 2247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 265 RLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGV-----------------MTTNPLNGE 326
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVtpllwkcrpqdpcgaayVPIGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 327 RKAGTVGPAVQGVGCRIAknGGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTIGGRSKD 399
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMA--GELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDH 2405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 400 MVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIVVPSEKVTDekeFEKKLIGIMKKKVANYKVPKRVIV 479
Cdd:PRK12316 2406 QVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAED---LLAELRAWLAARLPAYMVPAHWVV 2481
|
490
....*....|....*..
gi 32563687 480 LDDLPRNHITKVQKNVL 496
Cdd:PRK12316 2482 LERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
28-496 |
1.96e-26 |
|
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: 111.49 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGK-GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVSCNEELdkvfrdkirvinedklaseagslnactmiehveksdpASVCYTSGTTGLPKGAILTH 187
Cdd:cd17645 84 GERIAYMLADSSAKILLTNPDDL-------------------------------------AYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSNNAHDIVRDWGFTGNDYNLhalpfyhvhgLYYSlhcslFSHSTMIW-----------------RSKFEVEDCIKYM 250
Cdd:cd17645 127 HNLVNLCEWHRPYFGVTPADKSL----------VYAS-----FSFDASAWeifphltagaalhvvpsERRLDLDALNDYF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 251 KNAtvmmGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVStieefrERTGQVILERYGMTEAGVMTTN-PLNGERKA 329
Cdd:cd17645 192 NQE----GITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTVVATSfEIDKPYAN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 GTVGPAVQGVG----------CRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTI 393
Cdd:cd17645 262 IPIGKPIDNTRvyildealqlQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 394 GGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEkefekKLIGIMKKKVANYKV 473
Cdd:cd17645 342 LGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHE-----ELREWLKNDLPDYMI 416
|
490 500
....*....|....*....|...
gi 32563687 474 PKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKAL 439
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-485 |
2.01e-26 |
|
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: 110.16 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 172 YTSGTTGLPKGAILTHG---SLSNNAHDIVRDwGFTGNDYNLH------------ALPFYHVHGLYYSLHCSLFSHSTMI 236
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEdifRMLMGGADFGTG-EFTPSEDAHKaaaaaagtvmfpAPPLMHGTGSWTAFGGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 WRSKFEVEDCIKYMKN--ATVMMGVPTFFSRLL--ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVIL-ERYG 311
Cdd:cd05924 89 PDDRFDPEEVWRTIEKhkVTSMTIVGDAMARPLidALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLvDAFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 312 MTEAGVMTTNpLNGERKAGT-------------------VGPAVQGVGcRIAKNGGIEVktnaifaGYWKNPKKTAEEFT 372
Cdd:cd05924 169 SSETGFTGSG-HSAGSGPETgpftranpdtvvldddgrvVPPGSGGVG-WIARRGHIPL-------GYYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 373 E-DG--WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV--PS 447
Cdd:cd05924 240 EvDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQlrEG 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 32563687 448 EKVTDEkefekKLIGIMKKKVANYKVPKRVIVLDDLPR 485
Cdd:cd05924 320 AGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIER 352
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
48-498 |
1.05e-25 |
|
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: 109.83 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGAlyIPVNPGYTESEAAhyikdatpsiLVSCN 127
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGA--APAFINYNLSGDP----------LIHCL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeldKVFRDKIRVINEDklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGND 207
Cdd:cd05937 75 ----KLSGSRFVIVDPD---------------------DPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 208 YNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCikYMKNATVMMGVPTFFSRLLASKNFNKEAFGNVRVf 283
Cdd:cd05937 130 RTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSAsqfwKDV--RDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRV- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 284 ISGSApLSVSTIEEFRERTG-QVILERYGMTEAGVMTTNPLNGERKAGTVG--------------------PAVQGVgCR 342
Cdd:cd05937 207 AWGNG-LRPDIWERFRERFNvPEIGEFYAATEGVFALTNHNVGDFGAGAIGhhglirrwkfenqvvlvkmdPETDDP-IR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 343 IAKNGGIEV---------------KTNAIFAGYWKNPKKTAEEFTE------DGWFKTGDVGHLDEDGYLTIGGRSKDMV 401
Cdd:cd05937 285 DPKTGFCVRapvgepgemlgrvpfKNREAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 402 ITGGLNVYPKELEDFIDTLPFVKESAV--IASPHPDfGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKK-VANYKVPKRVI 478
Cdd:cd05937 365 RWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHD-GRAGCAAITLEESSAVPTEFTKSLLASLARKnLPSYAVPLFLR 443
|
490 500
....*....|....*....|
gi 32563687 479 VLDDLPRNHITKVQKNVLRD 498
Cdd:cd05937 444 LTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
166-484 |
1.05e-25 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 110.96 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 166 DPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHS-TMIWRS--KFE 242
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAeVFLYPSplHYR 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 VEDCIKYMKNATVMMGVPTFFSrllaskNFNKEA----FGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE-AGV 317
Cdd:PRK08043 446 IVPELVYDRNCTVLFGTSTFLG------NYARFAnpydFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcAPV 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 318 MTTN-PLNGerKAGTVGPAVQGVGCR------IAKNGGIEVKTNAIFAGYWK--NP-------KKTAEEFTEDGWFKTGD 381
Cdd:PRK08043 520 VSINvPMAA--KPGTVGRILPGMDARllsvpgIEQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGD 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIvvpsekVTDEKEFEKKLI 461
Cdd:PRK08043 598 IVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLF------TTDSELTREKLQ 671
|
330 340
....*....|....*....|....
gi 32563687 462 GIMKKK-VANYKVPKRVIVLDDLP 484
Cdd:PRK08043 672 QYAREHgVPELAVPRDIRYLKQLP 695
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-484 |
1.56e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.59 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVSCNEELDKV-FRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILT 186
Cdd:PRK12316 597 AERLAYMLEDSGVQLLLSQSHLGRKLpLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNR 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 187 HGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLyYSLHCSLFSHSTMIWRSK---FEVEDCIKYM--KNATVMMGVPT 261
Cdd:PRK12316 677 HRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPgdhRDPAKLVELInrEGVDTLHFVPS 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 262 FFSRLLASKNFnkEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGVMTTNPLNGERKAGTV--GPAVQG 338
Cdd:PRK12316 756 MLQAFLQDEDV--ASCTSLRRIVCSGEALPADAQEQVFAKLPQAgLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIAN 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 339 VGCRI----------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTIGGRSKDMVI 402
Cdd:PRK12316 834 LACYIldanlepvpvGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEYAGRIDHQVK 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 403 TGGLNVYPKELEDFIDTLPFVKESAVIASPhpdfGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDD 482
Cdd:PRK12316 914 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWRE---ALKAHLAASLPEYMVPAQWLALER 986
|
..
gi 32563687 483 LP 484
Cdd:PRK12316 987 LP 988
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-484 |
2.75e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 25 IVSQAQLQSDPSKLLFidGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNP 104
Cdd:PRK12316 4557 VAERARMTPDAVAVVF--DEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 105 GYTESEAAHYIKDATPSILVSCNEELdkvfrdkirvineDKLASEAGSlnACTMIEHVEK------SDPAS--------- 169
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLLTQSHLL-------------QRLPIPDGL--ASLALDRDEDwegfpaHDPAVrlhpdnlay 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 170 VCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFY---HVHGLYYSLHC--SLFSHSTMIWRSkfevE 244
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSfdgSHEGLYHPLINgaSVVIRDDSLWDP----E 4774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 245 DCIKYMKNATVMMGV-PTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEE-FRERTGQVILERYGMTEAGVMTTnp 322
Cdd:PRK12316 4775 RLYAEIHEHRVTVLVfPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVL-- 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 323 LNGERKAGTVGPAVQGVGCRIAKN-----------------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FK 378
Cdd:PRK12316 4853 LWKARDGDACGAAYMPIGTPLGNRsgyvldgqlnplpvgvaGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYR 4932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 379 TGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPdFGEAVVAIVVP-----SEKVTDE 453
Cdd:PRK12316 4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPqdpalADADEAQ 5011
|
490 500 510
....*....|....*....|....*....|.
gi 32563687 454 KEFEKKLIGIMKKKVANYKVPKRVIVLDDLP 484
Cdd:PRK12316 5012 AELRDELKAALRERLPEYMVPAHLVFLARMP 5042
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
70-414 |
3.87e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.05 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 70 KKGDRVMARVSKTTDTAALYIACLQIGA----LYIPVNPGYTESEAAhYIKDATPS-ILVS--CNEELDKVFRD-----K 137
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRiavpLFDPAEPGHVGRLHA-VLDDCTPSaILTTtdSAEGVRKFFRArpakeR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 138 IRVINEDKLASEAGSlnacTMIE-HVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFY 216
Cdd:PRK07769 156 PRVIAVDAVPDEVGA----TWVPpEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 217 HVHGLYYSLHCSLFSHSTMIWRSKFEVEDCIKYMKN-ATVMMGVPTFFSrllASKNFnkeAF------------------ 277
Cdd:PRK07769 232 HDMGLITVLLPALLGHYITFMSPAAFVRRPGRWIRElARKPGGTGGTFS---AAPNF---AFehaaarglpkdgeppldl 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 GNVRVFISGSAPLSVSTIEEFRERTG------QVILERYGMTEAGV-MTTNPLNGERK----------AGTVGP------ 334
Cdd:PRK07769 306 SNVKGLLNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLfVSTTPMDEEPTviyvdrdelnAGRFVEvpadap 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 335 -AVQGVGC-RIAKN-------------------GGIEVKTNAIFAGYWKNPKKTAEEF----------------TEDG-W 376
Cdd:PRK07769 386 nAVAQVSAgKVGVSewavivdpetaselpdgqiGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlW 465
|
410 420 430
....*....|....*....|....*....|....*...
gi 32563687 377 FKTGDVGhLDEDGYLTIGGRSKDMVITGGLNVYPKELE 414
Cdd:PRK07769 466 VRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
44-497 |
7.95e-25 |
|
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: 107.05 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL 123
Cdd:cd05940 1 DEALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 VScneeldkvfrdkirvinedklaseagslnactmiehveksDPASVCYTSGTTGLPKGAILTHGSLSnNAHDIVRDWGF 203
Cdd:cd05940 80 VV----------------------------------------DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 204 T-GNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCIKYmkNATVMMGVPTFFSRLLASKNFNKEAFG 278
Cdd:cd05940 119 AlPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSAsnfwDDIRKY--QATIFQYIGELCRYLLNQPPKPTERKH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 279 NVRVfISGSApLSVSTIEEFRERTG-QVILERYGMTEAgvmTTNPLNGERKAGTVG--PAVQGVGCRIA----------- 344
Cdd:cd05940 197 KVRM-IFGNG-LRPDIWEEFKERFGvPRIAEFYAATEG---NSGFINFFGKPGAIGrnPSLLRKVAPLAlvkydlesgep 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 345 ---KNG-GIEV----------KTNAI--FAGYWKNPKKTAEEFTE-----DGWFKTGDVGHLDEDGYLTIGGRSKDMVIT 403
Cdd:cd05940 272 irdAEGrCIKVprgepgllisRINPLepFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 404 GGLNVYPKELEDFIDTLPFVKESAVIASPHPDF-GEA-VVAIVVPSEKVTDEKEFEKKLigimKKKVANYKVPKRVIVLD 481
Cdd:cd05940 352 KGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAgMAAIVLQPNEEFDLSALAAHL----EKNLPGYARPLFLRLQP 427
|
490
....*....|....*.
gi 32563687 482 DLPRNHITKVQKNVLR 497
Cdd:cd05940 428 EMEITGTFKQQKVDLR 443
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
29-498 |
9.85e-25 |
|
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: 106.24 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTeKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLL-QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVSCNEeldkvfrdkirvinedklaseagslnactmiehveKSDPASVCYTSGTTGLPKGAILTHG 188
Cdd:cd17653 84 ARIQAILRTSGATLLLTTDS-----------------------------------PDDLAYIIFTSGSTGIPKGVMVPHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 189 SLSN---NAHDivrdwgftgndyNLHALPfyhvhglyYSLHCSLFSHStmIWRSKFEVEDCIKY---------------- 249
Cdd:cd17653 129 GVLNyvsQPPA------------RLDVGP--------GSRVAQVLSIA--FDACIGEIFSTLCNggtlvladpsdpfahv 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 250 MKNATVMMGVPTFFSRLlasknfNKEAFGNVRVFISGSAPLSVSTIEEFRErtGQVILERYGMTEAGVMTTNPLNGERKA 329
Cdd:cd17653 187 ARTVDALMSTPSILSTL------SPQDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 GTVGPAVQGVGCRIAKNGGIEV---KTNAIF-------AGYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGYLTI 393
Cdd:cd17653 259 VTIGKPIPNSTCYILDADLQPVpegVVGEICisgvqvaRGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 394 GGRSKDMVITGGLNVypkELEDFIDTL----PFVKESAVIASphpdfGEAVVAIVVPSEKVTDekefekKLIGIMKKKVA 469
Cdd:cd17653 339 LGREDNQVKVRGFRI---NLEEIEEVVlqsqPEVTQAAAIVV-----NGRLVAFVTPETVDVD------GLRSELAKHLP 404
|
490 500
....*....|....*....|....*....
gi 32563687 470 NYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:cd17653 405 SYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
48-449 |
1.48e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 106.91 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPG---------YTESEAAHYIkdA 118
Cdd:PRK09274 43 SFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGmgiknlkqcLAEAQPDAFI--G 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 119 TP-SILVSCneELDKVFRDKIRVIN-EDKLASEAGSLNacTMIEHVEKS----------DPASVCYTSGTTGLPKGAILT 186
Cdd:PRK09274 120 IPkAHLARR--LFGWGKPSVRRLVTvGGRLLWGGTTLA--TLLRDGAAApfpmadlapdDMAAILFTSGSTGTPKGVVYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 187 HGSLSNNAHDIVRDWGFTGNDYNLHALPFYhvhglyyslhcSLFSHS---TMIwrskfevedcIKYM---KNATV----- 255
Cdd:PRK09274 196 HGMFEAQIEALREDYGIEPGEIDLPTFPLF-----------ALFGPAlgmTSV----------IPDMdptRPATVdpakl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 256 -----------MMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRE--RTGQVILERYGMTEA---GVMT 319
Cdd:PRK09274 255 faaierygvtnLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEAlpiSSIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 TNPLNGERKAGT-------VGPAVQGVGCRI-------------------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTE 373
Cdd:PRK09274 335 SREILFATRAATdngagicVGRPVDGVEVRIiaisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAKIP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 374 DG----WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIAspHPDFGEAVVAIVVPSEK 449
Cdd:PRK09274 415 DGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG--VGVPGAQRPVLCVELEP 492
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
48-497 |
4.63e-24 |
|
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: 104.57 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEaahyikdatpsilvscn 127
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDD----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 eeldkvFRDKIrvinedklasEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNnAHDIVRDW-GFTGN 206
Cdd:cd05974 64 ------LRDRV----------DRGGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPV-GHLSTMYWiGLKPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 207 DYNLH-ALPFYHVHGlYYSLHCSLFSHSTMIW--RSKFEVEDCIKYMK--NATVMMGVPTFFsRLLASKNFNKEAFGnVR 281
Cdd:cd05974 127 DVHWNiSSPGWAKHA-WSCFFAPWNAGATVFLfnYARFDAKRVLAALVryGVTTLCAPPTVW-RMLIQQDLASFDVK-LR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 282 VFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGGIEVKTNAI----- 356
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEValdlg 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 357 -------FAGYWKNPKKTAEEFtEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVI 429
Cdd:cd05974 284 dtrpvglMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVV 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 430 ASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRvIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05974 363 PSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRR-LEFAELPKTISGKIRRVELR 429
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
148-453 |
1.14e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 104.92 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 148 SEAGSLNACTMIEHveKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDI-----VRDWGFTGNDYNLHALPFYHVHGLY 222
Cdd:PLN02861 205 SLMGSLDCELPPKQ--KTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkVTDRVATEEDSYFSYLPLAHVYDQV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 223 YSLHCSLFSHSTMIWRS--KFEVEDcIKYMKnATVMMGVPTFFSRL-------------LASKNFN-------------- 273
Cdd:PLN02861 283 IETYCISKGASIGFWQGdiRYLMED-VQALK-PTIFCGVPRVYDRIytgimqkissggmLRKKLFDfaynyklgnlrkgl 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 274 -----------------KEAFGN-VRVFISGSAPLSvSTIEEF-RERTGQVILERYGMTEA-GVMTTNPLNGERKAGTVG 333
Cdd:PLN02861 361 kqeeasprldrlvfdkiKEGLGGrVRLLLSGAAPLP-RHVEEFlRVTSCSVLSQGYGLTEScGGCFTSIANVFSMVGTVG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 334 PAVQGVGCRIAK-------------NGGIEVKTNAIFAGYWKNPKKTAEEFTeDGWFKTGDVGHLDEDGYLTIGGRSKDM 400
Cdd:PLN02861 440 VPMTTIEARLESvpemgydalsdvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 32563687 401 V-ITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFgeaVVAIVVPSEKVTDE 453
Cdd:PLN02861 519 FkLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESF---LVAVVVPDRQALED 569
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
68-444 |
9.51e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 101.62 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 68 NIKKGDRVmARVSKTT-DTAALYIACLQIG----ALYIPVNPGYTESEAAH---YIKDATPSILVScNEELdkvfrdkir 139
Cdd:PRK09192 70 GLKPGDRV-ALIAETDgDFVEAFFACQYAGlvpvPLPLPMGFGGRESYIAQlrgMLASAQPAAIIT-PDEL--------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 140 vinEDKLASEAGSLNACTMIEHVE------------KSDPASVCY---TSGTTGLPKGAILTHGSLSNNAHDIVRDwG-- 202
Cdd:PRK09192 139 ---LPWVNEATHGNPLLHVLSHAWfkalpeadvalpRPTPDDIAYlqySSGSTRFPRGVIITHRALMANLRAISHD-Glk 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 203 FTGNDYNLHALPFYHVHGL----YYSLHCSL---------FSHSTMIW-----RSK--------FEVEDCIKYMKNATVM 256
Cdd:PRK09192 215 VRPGDRCVSWLPFYHDMGLvgflLTPVATQLsvdylptrdFARRPLQWldlisRNRgtisysppFGYELCARRVNSKDLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 257 ------------------MGVPTFFSRLLASKNFNKEAFgnVRVFISGSAPLSVSTIEEFR----ERTGQVILERYGMTE 314
Cdd:PRK09192 295 eldlscwrvagigadmirPDVLHQFAEAFAPAGFDDKAF--MPSYGLAEATLAVSFSPLGSgivvEEVDRDRLEYQGKAV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 315 AgvmttnPLNGERKAGTV---GPAVQGVGCRIAKNGGIE----------VKTNAIFAGYWKNPKkTAEEFTEDGWFKTGD 381
Cdd:PRK09192 373 A------PGAETRRVRTFvncGKALPGHEIEIRNEAGMPlpervvghicVRGPSLMSGYFRDEE-SQDVLAADGWLDTGD 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563687 382 VGHLdEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIA-SPHPDFGEAVVAIV 444
Cdd:PRK09192 446 LGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAfSIAQENGEKIVLLV 508
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
45-484 |
3.53e-22 |
|
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: 99.07 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPsilv 124
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 scneeldKVFrdkirvINEDKlaseagslnactmiehveKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFT 204
Cdd:cd05910 76 -------DAF------IGIPK------------------ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 205 GNDYNLHALPFYHVHGLYYSLHCSL--FSHSTMIWRSKFEVEDCIKYMKnATVMMGVPTFFSRLLASKNFNKEAFGNVRV 282
Cdd:cd05910 125 PGEVDLATFPLFALFGPALGLTSVIpdMDPTRPARADPQKLVGAIRQYG-VSIVFGSPALLERVARYCAQHGITLPSLRR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 283 FISGSAPLSVSTIEEFRE--RTGQVILERYGMTEA---------GVMTTNPLNGERKAGT-VGPAVQGVGCRI------- 343
Cdd:cd05910 204 VLSAGAPVPIALAARLRKmlSDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGVRVRIieiddep 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 ------------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTEDG----WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLN 407
Cdd:cd05910 284 iaewddtlelprGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGT 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 408 VYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVpKRVIVLDDLP 484
Cdd:cd05910 364 LYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTQRI-GRFLIHPSFP 439
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
138-414 |
4.69e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 99.30 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 138 IRVIN-EDKLASEAGSlnactmIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFT-GNDYNLHALPF 215
Cdd:PRK07768 130 IRVLTvADLLAADPID------PVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 216 YHVHGLYYSLH------CSL-------FSHSTMIWrskfeVEDCIKYmkNATVMMGvPTF----FSRLLASKNfNKEAF- 277
Cdd:PRK07768 204 FHDMGMVGFLTvpmyfgAELvkvtpmdFLRDPLLW-----AELISKY--RGTMTAA-PNFayalLARRLRRQA-KPGAFd 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 -GNVRVFISGSAPLSVSTIEEFRE---RTG---QVILERYGMTEAGV----------MTTNP-----LNGERKA------ 329
Cdd:PRK07768 275 lSSLRFALNGAEPIDPADVEDLLDagaRFGlrpEAILPAYGMAEATLavsfspcgagLVVDEvdadlLAALRRAvpatkg 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 -----GTVGPAVQGVGCRIAKNGG----------IEVKTNAIFAGYwknpkKTAEEFT----EDGWFKTGDVGHLDEDGY 390
Cdd:PRK07768 355 ntrrlATLGPPLPGLEVRVVDEDGqvlpprgvgvIELRGESVTPGY-----LTMDGFIpaqdADGWLDTGDLGYLTEEGE 429
|
330 340
....*....|....*....|....
gi 32563687 391 LTIGGRSKDMVITGGLNVYPKELE 414
Cdd:PRK07768 430 VVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
45-485 |
5.26e-22 |
|
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: 99.43 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAH----------- 113
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLD-LGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLaklkhlfellk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 114 ----YIKDATP-------------SILVSCNEEldkvfrDKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTSGT 176
Cdd:cd05921 103 pglvFAQDAAPfaralaaifplgtPLVVSRNAV------AGRGAISFAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 177 TGLPKGAILTHGSLSNNAHDIVRDWGFTGND--YNLHALPFYHVHGLYYSLHCSLFSHSTM-IWRSK---FEVEDCIKYM 250
Cdd:cd05921 177 TGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLyIDDGKpmpGGFEETLRNL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 251 K--NATVMMGVPTFFSRLLASKNfNKEA-----FGNVRVFISGSAPLSVSTIEEFRERTGQVILER------YGMTEAGV 317
Cdd:cd05921 257 ReiSPTVYFNVPAGWEMLVAALE-KDEAlrrrfFKRLKLMFYAGAGLSQDVWDRLQALAVATVGERipmmagLGATETAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 318 MTTNPLNGERKAGTVGPAVQGVGCRIAKNGG---IEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGD------------- 381
Cdd:cd05921 336 TATFTHWPTERSGLIGLPAPGTELKLVPSGGkyeVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDaakladpddpakg 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 --------------------VGHLDEDGYLTIGGRSKDMVITGglnvypkELEDFIDTL--PFVKE-SAVIASPHPDFGE 438
Cdd:cd05921 416 lvfdgrvaedfklasgtwvsVGPLRARAVAACAPLVHDAVVAG-------EDRAEVGALvfPDLLAcRRLVGLQEASDAE 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 32563687 439 avvaiVVPSEKVTdeKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPR 485
Cdd:cd05921 489 -----VLRHAKVR--AAFRDRLAALNGEATGSSSRIARALLLDEPPS 528
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
70-444 |
6.83e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 99.05 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 70 KKGDRVMARVSKTTDTAALYIACLQIGA----LYIPVNPGYTESEAAhYIKDATPSILV-------SCNEELDKVFRD-K 137
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTiavpLFAPELPGHAERLDT-ALRDAEPTVVLtttaaaeAVEGFLRNLPRLrR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 138 IRVINEDKLASEAGSLNACTmieHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTgnDYNLHA---LP 214
Cdd:PRK12476 169 PRVIAIDAIPDSAGESFVPV---ELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL--DRNTHGvswLP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 215 FYHVHGL-------YYSLHCSLFSHSTMIWRSKFEVEDCIKYMKNATVMMGVPTFFSRLLASKNFNKEA----FGNVrVF 283
Cdd:PRK12476 244 LYHDMGLsmigfpaVYGGHSTLMSPTAFVRRPQRWIKALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGddidLSNV-VL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 284 ISGSAPLSVSTIEEFRERTGQVILER------YGMTEAG--VMTTNP------LNGERKAGTVGPAVQ----------GV 339
Cdd:PRK12476 323 IIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATlfVATIAPdaepsvVYLDREQLGAGRAVRvaadapnavaHV 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 340 GC-RIAKN-------------------GGIEVKTNAIFAGYWKNPKKTAEEF----------------TEDG--WFKTGD 381
Cdd:PRK12476 403 SCgQVARSqwavivdpdtgaelpdgevGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTGD 482
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563687 382 VG-HLDEDGYLTigGRSKDMVITGGLNVYPKELEDFI-DTLPFVKESAVIASPHPDFGEAVVAIV 444
Cdd:PRK12476 483 LGvYLDGELYIT--GRIADLIVIDGRNHYPQDIEATVaEASPMVRRGYVTAFTVPAEDNERLVIV 545
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
32-497 |
8.12e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 98.52 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 32 QSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSkttDTAALYI---ACLQIGAlyIPVNPGYT- 107
Cdd:PRK10946 34 HAASDAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLG---NVAEFYItffALLKLGV--APVNALFSh 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 -ESEAAHYIKDATPSILVS-------CNEELDKVFRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPAS------VCY- 172
Cdd:PRK10946 108 qRSELNAYASQIEPALLIAdrqhalfSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTATpspadeVAFf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 173 --TSGTTGLPKGAILTHgslsNNAHDIVRD----WGFTGNDYNLHALPFYH--------VHGLYYSLHCSLFSHSTmiwr 238
Cdd:PRK10946 188 qlSGGSTGTPKLIPRTH----NDYYYSVRRsveiCGFTPQTRYLCALPAAHnypmsspgALGVFLAGGTVVLAPDP---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 239 skfEVEDCI----KYMKNATVMmgVPTFFSRLLASKNF--NKEAFGNVRVFISGSAPLSVSTIEEFRERTG----QVile 308
Cdd:PRK10946 260 ---SATLCFplieKHQVNVTAL--VPPAVSLWLQAIAEggSRAQLASLKLLQVGGARLSETLARRIPAELGcqlqQV--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 309 rYGMTEAGVMTTNpLNG--ERKAGTVG-PAVQGVGCRIAKNGGIEVKTNAI----------FAGYWKNPKKTAEEFTEDG 375
Cdd:PRK10946 332 -FGMAEGLVNYTR-LDDsdERIFTTQGrPMSPDDEVWVADADGNPLPQGEVgrlmtrgpytFRGYYKSPQHNASAFDANG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 376 WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSE--KVTDE 453
Cdd:PRK10946 410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEplKAVQL 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 32563687 454 KEFekkligIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PRK10946 490 RRF------LREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
28-484 |
9.34e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 99.35 E-value: 9.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK10252 465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVSCNEELDKvFRDKIRVINEDKLASEAGSlnACTMIEHVEKSDPASVCYTSGTTGLPKGAILTH 187
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTADQLPR-FADVPDLTSLCYNAPLAPQ--GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 188 GSLSN-----NAHdivrdWGFTGNDYNLHALPfyhvhglyyslhCSlFSHStmIW--------------------RSKFE 242
Cdd:PRK10252 621 TAIVNrllwmQNH-----YPLTADDVVLQKTP------------CS-FDVS--VWeffwpfiagaklvmaepeahRDPLA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 243 VEDCIKYMKnATVMMGVPTF---FSRLLASKNFNKEAFGNVRVFISGSApLSVSTIEEFRERTGQVILERYGMTEAGV-M 318
Cdd:PRK10252 681 MQQFFAEYG-VTTTHFVPSMlaaFVASLTPEGARQSCASLRQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVdV 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 319 TTNPLNGERKAGT------VGPAVQGVGCRIAKN---------------GGIEVKTnaifaGYWKNPKKTAEEFTEDGW- 376
Cdd:PRK10252 759 SWYPAFGEELAAVrgssvpIGYPVWNTGLRILDArmrpvppgvagdlylTGIQLAQ-----GYLGRPDLTASRFIADPFa 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 377 -----FKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIA------SPHPDFGEAVVAIVV 445
Cdd:PRK10252 834 pgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinqaAATGGDARQLVGYLV 913
|
490 500 510
....*....|....*....|....*....|....*....
gi 32563687 446 PSEKVTDEKEfekKLIGIMKKKVANYKVPKRVIVLDDLP 484
Cdd:PRK10252 914 SQSGLPLDTS---ALQAQLRERLPPHMVPVVLLQLDQLP 949
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
35-484 |
1.04e-21 |
|
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: 97.32 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 35 PSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTD--TAALyiACLQIGALYIPVNPGYTESEAA 112
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAAR-GVGPERLVALALPRSAElvVAIL--AVLKAGAAYLPLDPAYPAERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 113 HYIKDATPSILvscneeldkvfrdkirvinedklaseagslnaCTMIEHveksdPASVCYTSGTTGLPKGAILTHGSLSN 192
Cdd:cd17652 78 YMLADARPALL--------------------------------LTTPDN-----LAYVIYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 193 NAHDIVRDWGFTGNDynlhalpfyHVhglyysLHCSLFSHSTMIWrskfevEDCIKYMKNATVMM--------GVPtfFS 264
Cdd:cd17652 121 LAAAQIAAFDVGPGS---------RV------LQFASPSFDASVW------ELLMALLAGATLVLapaeellpGEP--LA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 265 RLLASKNFN-------------KEAFGNVRVFISGSAPLSVSTIEefRERTGQVILERYGMTEAGVMTT--NPLNGERKA 329
Cdd:cd17652 178 DLLREHRIThvtlppaalaalpPDDLPDLRTLVVAGEACPAELVD--RWAPGRRMINAYGPTETTVCATmaGPLPGGGVP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 330 gTVGPAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLT 392
Cdd:cd17652 256 -PIGRPVPGTRVYVLDArlrpvppgvpGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 393 IGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYK 472
Cdd:cd17652 335 FLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYM 411
|
490
....*....|..
gi 32563687 473 VPKRVIVLDDLP 484
Cdd:cd17652 412 VPAAFVVLDALP 423
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-484 |
1.48e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 25 IVSQAQLQSDPSKLLFidGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNP 104
Cdd:PRK12467 1580 IEDQAAATPEAVALVF--GEQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 105 GYTESEAAHYIKDATPSILVSCNEELDKV-FRDKIRVINEDKLASEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGA 183
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGA 1736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 184 ILTHGSLSNNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYYSL--HCSLFSHSTMIWRSKfevEDCIKYM--KNATVM 256
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLSAADVVLQFTSFafdVSVWELFWPLinGARLVIAPPGAHRDP---EQLIQLIerQQVTTL 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 257 MGVPTFFSRLLaSKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV-ILERYGMTEAGVMTT-----NPLNGERKAG 330
Cdd:PRK12467 1814 HFVPSMLQQLL-QMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDVThwtcrRKDLEGRDSV 1892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 331 TVGPAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTI 393
Cdd:PRK12467 1893 PIGQPIANLSTYILDAslnpvpigvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEY 1972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 394 GGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIVVPS-EKVTDEKEFEKKLIGIMKK----KV 468
Cdd:PRK12467 1973 LGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQLVAYVVPTdPGLVDDDEAQVALRAILKNhlkaSL 2051
|
490
....*....|....*.
gi 32563687 469 ANYKVPKRVIVLDDLP 484
Cdd:PRK12467 2052 PEYMVPAHLVFLARMP 2067
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
29-496 |
2.44e-21 |
|
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: 96.62 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 29 AQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE 108
Cdd:cd12115 7 AQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 109 SEAAHYIKDATPSILVscneeldkvfrdkirvinedklaseagslnactmiehVEKSDPASVCYTSGTTGLPKGAILTHG 188
Cdd:cd12115 86 ERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 189 slsnNAHDIVRdWgfTGNDYNLHALPfyhvhglyyslhCSLFSHSTMIWRSKFE------VEDCIKYMKNA--------- 253
Cdd:cd12115 129 ----NAAAFLQ-W--AAAAFSAEELA------------GVLASTSICFDLSVFElfgplaTGGKVVLADNVlalpdlpaa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 ---TVMMGVPTFFSRLLasknfNKEAF-GNVRVFISGSAPLSVSTIEEFRER-TGQVILERYGMTEAGVMTTNPL--NGE 326
Cdd:cd12115 190 aevTLINTVPSAAAELL-----RHDALpASVRVVNLAGEPLPRDLVQRLYARlQVERVVNLYGPSEDTTYSTVAPvpPGA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 327 RKAGTVGPAVQGVGCRIAKNGGIEVKTNAI---------FA-GYWKNPKKTAEEFTEDGW------FKTGDVGHLDEDGY 390
Cdd:cd12115 265 SGEVSIGRPLANTQAYVLDRALQPVPLGVPgelyiggagVArGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 391 LTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVAN 470
Cdd:cd12115 345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPA 421
|
490 500
....*....|....*....|....*.
gi 32563687 471 YKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd12115 422 YMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
42-388 |
4.65e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 96.49 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 42 DGDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTE-----SEAAHYIK 116
Cdd:PRK08180 65 GGWRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 117 DATPS-ILVSCNEE----LDKVFRDKIRVI---NEDK------LASEAGSLNACTMIEHVEKSDP---ASVCYTSGTTGL 179
Cdd:PRK08180 144 LLTPGlVFADDGAAfaraLAAVVPADVEVVavrGAVPgraatpFAALLATPPTAAVDAAHAAVGPdtiAKFLFTSGSTGL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 180 PKGAILTHGSLSNNAHDIVRDWGFTGNDYN--LHALPFYHVHGLYYSLHCSLFSHSTM-IWRSK-----FEvedciKYMK 251
Cdd:PRK08180 224 PKAVINTHRMLCANQQMLAQTFPFLAEEPPvlVDWLPWNHTFGGNHNLGIVLYNGGTLyIDDGKptpggFD-----ETLR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 252 N-----ATVMMGVPTFFSRLLAS--------KNFnkeaFGNVRVFISGSAPLSVST---IEEFRERT-GQ--VILERYGM 312
Cdd:PRK08180 299 NlreisPTVYFNVPKGWEMLVPAlerdaalrRRF----FSRLKLLFYAGAALSQDVwdrLDRVAEATcGEriRMMTGLGM 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 313 TEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGG---IEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHL-DED 388
Cdd:PRK08180 375 TETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGGkleVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPA 454
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
13-474 |
6.81e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 96.10 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 13 IGLRAASSAANNI--VSQAQLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYI 90
Cdd:PRK08279 27 RTALITPDSKRSLgdVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 91 ACLQIGALYIPVNPGYTESEAAHYIKDATPSILVScNEELDKVFrDKIR----------VINEDKLASEAGSLNACTMIE 160
Cdd:PRK08279 106 GLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIV-GEELVEAF-EEARadlarpprlwVAGGDTLDDPEGYEDLAAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 161 HVEKSDPASVC-----------YTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGND--YNlhALPFYHVHGLYYSLHC 227
Cdd:PRK08279 184 GAPTTNPASRSgvtakdtafyiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDvlYC--CLPLYHNTGGTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 228 SLFSHSTMIWRSKFEV----EDCIKYmkNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFIsgSAPLSVSTIEEFRERTG 303
Cdd:PRK08279 262 VLAAGATLALRRKFSAsrfwDDVRRY--RATAFQYIGELCRYLLNQPPKPTDRDHRLRLMI--GNGLRPDIWDEFQQRFG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 304 -QVILERYGMTEAGVMTTNPLNgerKAGTVG--PAV---------------------QGVgCRIAKNGGI-----EVKTN 354
Cdd:PRK08279 338 iPRILEFYAASEGNVGFINVFN---FDGTVGrvPLWlahpyaivkydvdtgepvrdaDGR-CIKVKPGEVglligRITDR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 AIFAGYwknpkkTAEEFTE-----------DGWFKTGDVGHLDEDGYLT----IGG--RSKdmvitgGLNVYPKELEDFI 417
Cdd:PRK08279 414 GPFDGY------TDPEASEkkilrdvfkkgDAWFNTGDLMRDDGFGHAQfvdrLGDtfRWK------GENVATTEVENAL 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563687 418 DTLPFVKESAV--IASPHPDfGEA-VVAIVvpsekVTDEKEFE-KKLIGIMKKKVANYKVP 474
Cdd:PRK08279 482 SGFPGVEEAVVygVEVPGTD-GRAgMAAIV-----LADGAEFDlAALAAHLYERLPAYAVP 536
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
30-496 |
9.65e-21 |
|
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: 94.81 E-value: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 30 QLQSDPSKLLFIDGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTES 109
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSL-GVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 110 EAAHYIKDATPSILVSCNEELdkvfrdkirvinedklaseagslnactmiehveksdpASVCYTSGTTGLPKGAILTHGS 189
Cdd:cd17644 88 RLTYILEDAQISVLLTQPENL-------------------------------------AYVIYTSGSTGKPKGVMIEHQS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 190 LSNNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYYslhcSLFSHSTMIWRSK---FEVEDCIKYM-KNATVMMGVPTF 262
Cdd:cd17644 131 LVNLSHGLIKEYGITSSDRVLQFASIafdVAAEEIYV----TLLSGATLVLRPEemrSSLEDFVQYIqQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 263 FSRLLASKNFNKEAFG--NVRVFISGSAPLSVSTIEEFRERTGQVI--LERYGMTEAGVMTT-----NPLNGERKAGTVG 333
Cdd:cd17644 207 YWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATvcrltQLTERNITSVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 334 PAVQGVGCRIAKN----------GGIEVKTNAIFAGYWKNPKKTAEEFTEDGW--------FKTGDVGHLDEDGYLTIGG 395
Cdd:cd17644 287 RPIANTQVYILDEnlqpvpvgvpGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 396 RSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEfekKLIGIMKKKVANYKVPK 475
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPS 443
|
490 500
....*....|....*....|.
gi 32563687 476 RVIVLDDLPRNHITKVQKNVL 496
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
148-430 |
2.96e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 93.68 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 148 SEAGSLNACTMIEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFT-GNDYNLHALPFYHVHGLYYSLH 226
Cdd:PRK05851 135 ATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDaATDVGCSWLPLYHDMGLAFLLT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 227 CSL------------FSHSTMIWrskfevedcIKYMKNATV-MMGVPTFFSRLLA--SKNFNKEAFGNVRVFISGSAPLS 291
Cdd:PRK05851 215 AALagaplwlapttaFSASPFRW---------LSWLSDSRAtLTAAPNFAYNLIGkyARRVSDVDLGALRVALNGGEPVD 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 292 VSTIEEFRERTGQV------ILERYGMTEAGVMTTNPLNGE---------------RKAGTVGPAVQGVGCRIAKN---- 346
Cdd:PRK05851 286 CDGFERFATAMAPFgfdagaAAPSYGLAESTCAVTVPVPGIglrvdevttddgsgaRRHAVLGNPIPGMEVRISPGdgaa 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 347 -------GGIEVKTNAIFAGYwknpkKTAEEFTEDGWFKTGDVGHLDEDGyLTIGGRSKDMVITGGLNVYPKELEDFIDT 419
Cdd:PRK05851 366 gvagreiGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQ 439
|
330
....*....|.
gi 32563687 420 LPFVKESAVIA 430
Cdd:PRK05851 440 VRGVREGAVVA 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
165-503 |
3.71e-20 |
|
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: 92.99 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 165 SDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDynlHALPFY------HVHGLYYSLH-----CSLfshs 233
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSES---RVLQFAsytfdvSILEIFTTLAaggclCIP---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 234 tmiwrSKFE----VEDCIKYMKNATVMMgVPTFfSRLLasknfNKEAFGNVRVFISGSAPLSVSTIEEFRERTgqVILER 309
Cdd:cd05918 179 -----SEEDrlndLAGFINRLRVTWAFL-TPSV-ARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWADRV--RLINA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 310 YGMTEAGVMTT-NPLNGERKAGTVGPAVqGVGCRIAKNGGIE--VKTNAI----------FAGYWKNPKKTAEEFTED-G 375
Cdd:cd05918 245 YGPAECTIAATvSPVVPSTDPRNIGRPL-GATCWVVDPDNHDrlVPIGAVgelliegpilARGYLNDPEKTAAAFIEDpA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 376 W------------FKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFI-DTLPFVKESAVIASPHPDFGEA--V 440
Cdd:cd05918 324 WlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEVVVEVVKPKDGSSSpqL 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 441 VAIVVPSEKVTDEKEFEKKLIGI--------------MKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLRDTYKNL 503
Cdd:cd05918 404 VAFVVLDGSSSGSGDGDSLFLEPsdefralvaelrskLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
45-388 |
5.55e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.19 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 45 RKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAH----YIKD-AT 119
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDL-GLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHaklkHLFDlVK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 120 PS-ILVSCNEELDKVFR----DKIRVINEDKLASEAGS-----LNACTMIEHVEKS----DPASVC---YTSGTTGLPKG 182
Cdd:PRK12582 158 PRvVFAQSGAPFARALAaldlLDVTVVHVTGPGEGIASiafadLAATPPTAAVAAAiaaiTPDTVAkylFTSGSTGMPKA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 183 AILTHGSLSNNA--------------HDIVRDWgftgndynlhaLPFYHVHGLYYSLHCSLFSHSTM-IWRSK---FEVE 244
Cdd:PRK12582 238 VINTQRMMCANIamqeqlrprepdppPPVSLDW-----------MPWNHTMGGNANFNGLLWGGGTLyIDDGKplpGMFE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 245 DCIKYMK--NATVMMGVPTFFSrLLASKNFNKEA-----FGNVRVFISGSAPLSVSTIEEFRE----RTGQ--VILERYG 311
Cdd:PRK12582 307 ETIRNLReiSPTVYGNVPAGYA-MLAEAMEKDDAlrrsfFKNLRLMAYGGATLSDDLYERMQAlavrTTGHriPFYTGYG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 312 MTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAKNGG---IEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGH-LDE 387
Cdd:PRK12582 386 ATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGDkyeVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDP 465
|
.
gi 32563687 388 D 388
Cdd:PRK12582 466 D 466
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
167-451 |
7.00e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 92.96 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 167 PASVC---YTSGTTGLPKGAILTHgslsNNAHDIVR---------DWGFTGNDYNLHALPFYHV-----HGLYYSLHCSL 229
Cdd:PLN02430 219 PLDICtimYTSGTSGDPKGVVLTH----EAVATFVRgvdlfmeqfEDKMTHDDVYLSFLPLAHIldrmiEEYFFRKGASV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 230 -FSHSTMiwrskFEVEDCIKYMKnATVMMGVPTFFSR------------------------------------------- 265
Cdd:PLN02430 295 gYYHGDL-----NALRDDLMELK-PTLLAGVPRVFERihegiqkalqelnprrrlifnalykyklawmnrgyshkkaspm 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 266 --LLASKNFNKEAFGNVRVFISGSAPLSvSTIEEF-RERTGQVILERYGMTEAGVMTTNPLNGER-KAGTVGPAVQGVGC 341
Cdd:PLN02430 369 adFLAFRKVKAKLGGRLRLLISGGAPLS-TEIEEFlRVTSCAFVVQGYGLTETLGPTTLGFPDEMcMLGTVGAPAVYNEL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 342 RIAK-------------NGGIEVKTNAIFAGYWKNPKKTaEEFTEDGWFKTGDVGHLDEDGYLTIGGRSKDMV-ITGGLN 407
Cdd:PLN02430 448 RLEEvpemgydplgeppRGEICVRGKCLFSGYYKNPELT-EEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEY 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32563687 408 VYPKELEDFIDTLPFVKESAVIASphpDFGEAVVAIVVPSEKVT 451
Cdd:PLN02430 527 VALEYLENVYGQNPIVEDIWVYGD---SFKSMLVAVVVPNEENT 567
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
163-462 |
9.65e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 92.78 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 163 EKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWG-----FTGNDYNLHALPFYHV-----------HG------ 220
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIfdrvieecfiqHGaaigfw 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 221 -------------LYYSLHCSL--------------FSHSTMIWRSKFEVEDCIK--YMKNATVMMGVPTFFSRLLASKn 271
Cdd:PLN02614 301 rgdvklliedlgeLKPTIFCAVprvldrvysglqkkLSDGGFLKKFVFDSAFSYKfgNMKKGQSHVEASPLCDKLVFNK- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 272 FNKEAFGNVRVFISGSAPLSvSTIEEF-RERTGQVILERYGMTE--AGVMTTNPlNGERKAGTVGPAVQGVGCRI----- 343
Cdd:PLN02614 380 VKQGLGGNVRIILSGAAPLA-SHVESFlRVVACCHVLQGYGLTEscAGTFVSLP-DELDMLGTVGPPVPNVDIRLesvpe 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 344 --------AKNGGIEVKTNAIFAGYWKNPKKTAEEFTeDGWFKTGDVGHLDEDGYLTIGGRSKDMV-ITGGLNVYPKELE 414
Cdd:PLN02614 458 meydalasTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIE 536
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 32563687 415 DFIDTLPFVKESAVIASPHPDFgeaVVAIVVPSEKVTDEKEFEKKLIG 462
Cdd:PLN02614 537 NIYGEVQAVDSVWVYGNSFESF---LVAIANPNQQILERWAAENGVSG 581
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-484 |
1.97e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.54 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 28 QAQLQSDPSKLLFidGDRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYT 107
Cdd:PRK05691 2197 QAARTPQAPALTF--AGQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 108 ESEAAHYIKDATPSILVSCNEELDKVFRDKIRVIN---EDKLASEAG----SLNACTMIEHveksdPASVCYTSGTTGLP 180
Cdd:PRK05691 2274 LERLHYMIEDSGIGLLLSDRALFEALGELPAGVARwclEDDAAALAAysdaPLPFLSLPQH-----QAYLIYTSGSTGKP 2348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 181 KGAILTHGSLSNNAHDIVRDWGFTGNDYNLHalpFYHVH--GLYYSLHCSLFSHSTMIWRS--KFEVEDCIKYMKNATV- 255
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELH---FYSINfdAASERLLVPLLCGARVVLRAqgQWGAEEICQLIREQQVs 2425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 256 MMG-VPTFFSRL---LASKNfnkeAFGNVRVFISGSAPLSVSTIEEFRER-TGQVILERYGMTEAGVMTTNPLNGER--- 327
Cdd:PRK05691 2426 ILGfTPSYGSQLaqwLAGQG----EQLPVRMCITGGEALTGEHLQRIRQAfAPQLFFNAYGPTETVVMPLACLAPEQlee 2501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 328 KAGTVgPAVQGVGCRIA-------------KNGGIEVKTNAIFAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDE 387
Cdd:PRK05691 2502 GAASV-PIGRVVGARVAyildadlalvpqgATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRA 2580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 388 DGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEK--EFEKKLIGIMK 465
Cdd:PRK05691 2581 DGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAqaALREALKAHLK 2660
|
490
....*....|....*....
gi 32563687 466 KKVANYKVPKRVIVLDDLP 484
Cdd:PRK05691 2661 QQLPDYMVPAHLILLDSLP 2679
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
47-453 |
2.04e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 91.72 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 47 TTYGEFVKRTGQYATALtekynIKKGDRVMARVSKTTDTAALYIACLQ------IGALYIPVNPGytESEAAHYIKDATP 120
Cdd:PLN02387 107 ITYGQVFERVCNFASGL-----VALGHNKEERVAIFADTRAEWLIALQgcfrqnITVVTIYASLG--EEALCHSLNETEV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 121 SILVSCNEELDKV--FRDKI----RVI--NEDKLASEAGSLNAC----TMIEHVEK--------------SDPASVCYTS 174
Cdd:PLN02387 180 TTVICDSKQLKKLidISSQLetvkRVIymDDEGVDSDSSLSGSSnwtvSSFSEVEKlgkenpvdpdlpspNDIAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 175 GTTGLPKGAILTHGSLSNNA---HDIVRDWGftGNDYNLHALPFYHVhglyyslhCSLFSHSTMI-------WRSKFEVE 244
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVagvMTVVPKLG--KNDVYLAYLPLAHI--------LELAAESVMAavgaaigYGSPLTLT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 245 DC---IKY-------MKNATVMMGVPTFFSRL-------------LASKNF--------------------------NKE 275
Cdd:PLN02387 330 DTsnkIKKgtkgdasALKPTLMTAVPAILDRVrdgvrkkvdakggLAKKLFdiaykrrlaaiegswfgawglekllwDAL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 276 AF--------GNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTE--AGVMTTNPlnGERKAGTVGPAV--------- 336
Cdd:PLN02387 410 VFkkiravlgGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTEtcAGATFSEW--DDTSVGRVGPPLpccyvklvs 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 337 --QGvGCRIAKN----GGIEVKTNAIFAGYWKNPKKTAEEFTEDG----WFKTGDVGHLDEDGYLTIGGRSKDMV-ITGG 405
Cdd:PLN02387 488 weEG-GYLISDKpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHG 566
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 32563687 406 LNVYPKELEDFIDTLPFVKESAVIASPhpdFGEAVVAIVVPSEKVTDE 453
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYVDNIMVHADP---FHSYCVALVVPSQQALEK 611
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
44-497 |
3.86e-19 |
|
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: 90.18 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDA-TPSI 122
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSkAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 123 LVSCNEELDKVFRDKirvinedklaseagsLNACTMIEHVEKsdpasVC--YTSGTTGLPKGAILTHGSLSNNAHDIVRD 200
Cdd:cd05939 80 IFNLLDPLLTQSSTE---------------PPSQDDVNFRDK-----LFyiYTSGTTGLPKAAVIVHSRYYRIAAGAYYA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 201 WGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEV----EDCIKYmkNATVMMGVPTFFSRLLASKNFNKEA 276
Cdd:cd05939 140 FGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAsnfwDDCVKY--NCTIVQYIGEICRYLLAQPPSEEEQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 277 FGNVRVFISGSapLSVSTIEEFRERTG-QVILERYGMTEAgvmTTNPLNGERKAGTVG------PAVQGV---------- 339
Cdd:cd05939 218 KHNVRLAVGNG--LRPQIWEQFVRRFGiPQIGEFYGATEG---NSSLVNIDNHVGACGfnsrilPSVYPIrlikvdedtg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 340 -----------GCRIAKNG---GIEVKTNAI--FAGYWK---NPKKTAEE-FTE-DGWFKTGDVGHLDEDGYLTIGGRSK 398
Cdd:cd05939 293 elirdsdglciPCQPGEPGllvGKIIQNDPLrrFDGYVNegaTNKKIARDvFKKgDSAFLSGDVLVMDELGYLYFKDRTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 399 DMVITGGLNVYPKELEDFIDTLPFVKESAV--IASPHPDFGEAVVAIVVPSEKVtdekeFEKKLIGIMKKKVANYKVPKR 476
Cdd:cd05939 373 DTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKV-----DLDRFSAVLAKSLPPYARPQF 447
|
490 500
....*....|....*....|.
gi 32563687 477 VIVLDDLPRNHITKVQKNVLR 497
Cdd:cd05939 448 IRLLPEVDKTGTFKLQKTDLQ 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
161-475 |
3.88e-19 |
|
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: 90.43 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 161 HVEKSDPASVCYTSGTTGLPKGAILTHGSL---SNNAHDIvrdwGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIW 237
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVlqcSGFLSLC----GVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 238 RSKFEV----EDCIKYmkNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFIsGSApLSVSTIEEFRERTGQV-ILERYGM 312
Cdd:cd05938 216 KPKFSAsqfwDDCRKH--NVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAI-GNG-LRADVWREFLRRFGPIrIREFYGS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 313 TEAGVMTTNplngerKAGTVGpAVQGVGC---------------------RIAKNGGIEVKT------------NAIFAG 359
Cdd:cd05938 292 TEGNIGFFN------YTGKIG-AVGRVSYlykllfpfelikfdvekeepvRDAQGFCIPVAKgepgllvakitqQSPFLG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 360 YWKNP-----KKTAEEF-TEDGWFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPH 433
Cdd:cd05938 365 YAGDKeqtekKLLRDVFkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTV 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32563687 434 PDF-GEAVVAIVvpseKVTDEKEFE-KKLIGIMKKKVANYKVPK 475
Cdd:cd05938 445 PGHeGRIGMAAV----KLKPGHEFDgKKLYQHVREYLPAYARPR 484
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
164-398 |
9.54e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 89.65 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 164 KSDPASVCYTSGTTGLPKGAILTHGSLSNNAH---DIVRDW--GFTGNDYNLHALPFYHVhgLYYSLHCSLFSHSTMI-W 237
Cdd:PTZ00216 263 NDDLALIMYTSGTTGDPKGVMHTHGSLTAGILaleDRLNDLigPPEEDETYCSYLPLAHI--MEFGVTNIFLARGALIgF 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 238 RSKFEVEDciKYMK--------NATVMMGVPTFF---------------------------SRLLASKN------FNKEA 276
Cdd:PTZ00216 341 GSPRTLTD--TFARphgdltefRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdhayqSRLRALKEgkdtpyWNEKV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 277 F--------GNVRVFISGSAPLSVSTIEEFRERTGQVIlERYGMTEAGVMTTNPLNGERKAGTVGPAVQGVGCRIAK--- 345
Cdd:PTZ00216 419 FsapravlgGRVRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDtee 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563687 346 ---------NGGIEVKTNAIFAGYWKNPKKTAEEFTEDGWFKTGDVGHLDEDGYLTIGGRSK 398
Cdd:PTZ00216 498 ykhtdtpepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
48-452 |
3.91e-18 |
|
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: 87.51 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCN 127
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 128 EELDK---------------VF----------------RDK-----IRVINEDKLASEAGSLNACTMIEHVEKSDP-ASV 170
Cdd:cd17632 149 EHLDLaveavleggtpprlvVFdhrpevdahraalesaRERlaavgIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPlALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 CYTSGTTGLPKGAILTHgslsnnaHDIVRDW----GFTGND----YNLHALPFYHVHG---LYYSLH------------- 226
Cdd:cd17632 229 IYTSGSTGTPKGAMYTE-------RLVATFWlkvsSIQDIRppasITLNFMPMSHIAGrisLYGTLArggtayfaaasdm 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 227 CSLFSHSTMIWRSKF----EVEDCIKYMKNATVMMGVPTFFSRLLASKNFNKEAF-----GNVRVFISGSAPLSvSTIEE 297
Cdd:cd17632 302 STLFDDLALVRPTELflvpRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRervlgGRLLAAVCGSAPLS-AEMKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 298 FRERTGQV-ILERYGMTEAGVMTtnpLNGErkagTVGPAVQG------------VGCRIAKNGGIEVKTNAIFAGYWKNP 364
Cdd:cd17632 381 FMESLLDLdLHDGYGSTEAGAVI---LDGV----IVRPPVLDyklvdvpelgyfRTDRPHPRGELLVKTDTLFPGYYKRP 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 365 KKTAEEFTEDGWFKTGDV-GHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFgeaVVAI 443
Cdd:cd17632 454 EVTAEVFDEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAY---LLAV 530
|
....*....
gi 32563687 444 VVPSEKVTD 452
Cdd:cd17632 531 VVPTQDALA 539
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
159-417 |
5.56e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.79 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 159 IEHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHG-----LYYSLH--CSLFS 231
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGfnsctLFPLLSgvPVVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 232 HSTMIWRSKFEVEDcikyMKNATVMMGVPTFFSRLLASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQVILER-Y 310
Cdd:PRK06334 257 YNPLYPKKIVEMID----EAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQgY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 311 GMTEAG-VMTTNPLNGERKAGTVGPAVQGVGCRI-----------AKNGGIEVKTNAIFAGYWKN-PKKTAEEFTEDGWF 377
Cdd:PRK06334 333 GTTECSpVITINTVNSPKHESCVGMPIRGMDVLIvseetkvpvssGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWY 412
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 32563687 378 KTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFI 417
Cdd:PRK06334 413 VTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
44-497 |
7.32e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.88 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEKyNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSIL 123
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 124 VSCNEELDKVFRDKIRVINEDKLASEAG---SLNACTM----------------------------------IEHVEKSD 166
Cdd:PLN02654 197 ITCNAVKRGPKTINLKDIVDAALDESAKngvSVGICLTyenqlamkredtkwqegrdvwwqdvvpnyptkceVEWVDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 167 PASVCYTSGTTGLPKGAILTHG------------SLSNNAHDI---VRDWGF-TGNDYNLHAlPFYHVHGLYYSLHCSLF 230
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGVLHTTGgymvytattfkyAFDYKPTDVywcTADCGWiTGHSYVTYG-PMLNGATVLVFEGAPNY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 231 SHSTMIWrskfEVEDciKYmkNATVMMGVPTFFSRLL--ASKNFNKEAFGNVRVFISGSAPLSVSTIEEFRERTGQV--- 305
Cdd:PLN02654 356 PDSGRCW----DIVD--KY--KVTIFYTAPTLVRSLMrdGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSrcp 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 306 ILERYGMTEAGVMTTNPLNG--ERKAGTVGPAVQGVGCRIAKNGGIEVKTNAifAGY------WKNPKKTA---EEFTED 374
Cdd:PLN02654 428 ISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGKEIEGEC--SGYlcvkksWPGAFRTLygdHERYET 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 375 GWFK-------TGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPS 447
Cdd:PLN02654 506 TYFKpfagyyfSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 32563687 448 EKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVLR 497
Cdd:PLN02654 586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
125-401 |
1.82e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 85.54 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 SCNEELDKvfrDKIRVINEDKLASEAGSLNAC---------TMIEHVEKSDP---ASVCYTSGTTGLPKGAILTHGSLSN 192
Cdd:PTZ00342 255 LGPLEYDK---EKLEKIKDLKEKAKKLGISIIlfddmtknkTTNYKIQNEDPdfiTSIVYTSGTSGKPKGVMLSNKNLYN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 193 NA-----HDIVRDWGFtgnDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRS--KFEVEDCikYMKNATVMMGVPTFFSR 265
Cdd:PTZ00342 332 TVvplckHSIFKKYNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKdiNYFSKDI--YNSKGNILAGVPKVFNR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 266 LLAS-----------------------KNFNKEAFG-------------------NVRVFISGSAPLSVSTIEEFRERTG 303
Cdd:PTZ00342 407 IYTNimteinnlpplkrflvkkilslrKSNNNGGFSkflegithisskikdkvnpNLEVILNGGGKLSPKIAEELSVLLN 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 304 QVILERYGMTEAG----VMTTNPLNGERKAGTVGPAVQG--VGCRIAK------NGGIEVKTNAIFAGYWKNPKKTAEEF 371
Cdd:PTZ00342 487 VNYYQGYGLTETTgpifVQHADDNNTESIGGPISPNTKYkvRTWETYKatdtlpKGELLIKSDSIFSGYFLEKEQTKNAF 566
|
330 340 350
....*....|....*....|....*....|
gi 32563687 372 TEDGWFKTGDVGHLDEDGYLTIGGRSKDMV 401
Cdd:PTZ00342 567 TEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
281-491 |
4.78e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 80.08 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 281 RVFISGsAPLSVSTIEEFRERTGQViLERYGMTEAGVMTTNPlnGERKAGTVGPAVQGVGCRIAKNGG------IEVKTN 354
Cdd:PRK08308 216 AVMTSG-TPLPEAWFYKLRERTTYM-MQQYGCSEAGCVSICP--DMKSHLDLGNPLPHVSVSAGSDENapeeivVKMGDK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 AIFagywknpkktaeeftedgwfkTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHP 434
Cdd:PRK08308 292 EIF---------------------TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDP 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 32563687 435 DFGEAVVAIVVpSEKVTDEKEFEKKLIgimkKKVANYKVPKRVIVLDDLPRNHITKV 491
Cdd:PRK08308 351 VAGERVKAKVI-SHEEIDPVQLREWCI----QHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
412-486 |
5.71e-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: 69.88 E-value: 5.71e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563687 412 ELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEkvtDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRN 486
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKT 72
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
162-414 |
1.41e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 76.13 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 162 VEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDW-GFTGNDYNLHA-----LPFYHVHGLYYSLhcslfshstm 235
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfGDTGGVPPPDTtvvswLPFYHDMGLVLGV---------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 236 iwrskfevedCikymknATVMMGVPTFFS-------------RLLASK--------NFnkeAF----------------- 277
Cdd:PRK05850 227 ----------C------APILGGCPAVLTspvaflqrparwmQLLASNphafsaapNF---AFelavrktsdddmagldl 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 278 GNVRVFISGSAPLSVSTIEEFRERTGQ------VILERYGMTEAGVMTTNPLNGER-----------KAGTVGPAVQGVG 340
Cdd:PRK05850 288 GGVLGIISGSERVHPATLKRFADRFAPfnlretAIRPSYGLAEATVYVATREPGQPpesvrfdyeklSAGHAKRCETGGG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 C-------------RI-----------AKNGGIEVKTNAIFAGYWKNPKKTAEEF----------TEDG-WFKTGDVGHL 385
Cdd:PRK05850 368 TplvsygsprsptvRIvdpdtciecpaGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFI 447
|
330 340
....*....|....*....|....*....
gi 32563687 386 DeDGYLTIGGRSKDMVITGGLNVYPKELE 414
Cdd:PRK05850 448 S-EGELFIVGRIKDLLIVDGRNHYPDDIE 475
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
90-496 |
6.96e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 90 IACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCNEELDKVFR-DKIRVINEDKLASEAGSLNACTMieHVEKSDPA 168
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQaEGVSAIALDSLHLDSWPSQAPGL--HLHGDNLA 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 169 SVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGNDYNLHALPF---YHVHGLYYSL--HCSLFSHSTMIWRSKFEV 243
Cdd:PRK05691 1277 YVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsfdVSVWECFWPLitGCRLVLAGPGEHRDPQRI 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 244 EDCIKyMKNATVMMGVPT----FFSRLLASknfnkeAFGNVRVFISGSAPLSVSTIEEFRERTGQVILE-RYGMTEAGVM 318
Cdd:PRK05691 1357 AELVQ-QYGVTTLHFVPPllqlFIDEPLAA------ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHnRYGPTETAIN 1429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 319 TTN----PLNGERKAgtVGPAVQGVGCRIAKN---------------GGIevktnAIFAGYWKNPKKTAEEFT-----ED 374
Cdd:PRK05691 1430 VTHwqcqAEDGERSP--IGRPLGNVLCRVLDAelnllppgvagelciGGA-----GLARGYLGRPALTAERFVpdplgED 1502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 375 G--WFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIAspHPDF-GEAVVAIVVPSEKVT 451
Cdd:PRK05691 1503 GarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV--REGAaGAQLVGYYTGEAGQE 1580
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 32563687 452 DEKEfekKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK05691 1581 AEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
68-496 |
1.15e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 73.62 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 68 NIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVSCNE------------------E 129
Cdd:PTZ00237 113 NISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYgilndeiitftpnlkeaiE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 130 LDK--------VFRDKIRVINEDKLASE----AGSLNACTMIEH--------------VEKSDPASVCYTSGTTGLPKGA 183
Cdd:PTZ00237 193 LSTfkpsnvitLFRNDITSESDLKKIETiptiPNTLSWYDEIKKikennqspfyeyvpVESSHPLYILYTSGTTGNSKAV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 184 ILTHGSlsnNAHDIVRDWGFTGNDyNLHALPFYH-------VHGLYY---SLHCSLFSHSTMIWRSKfEVEDcikYMKNA 253
Cdd:PTZ00237 273 VRSNGP---HLVGLKYYWRSIIEK-DIPTVVFSHssigwvsFHGFLYgslSLGNTFVMFEGGIIKNK-HIED---DLWNT 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 254 TVMMGVPTFFSRLLASKNFNK---EA--------FGNVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAGVMT--- 319
Cdd:PTZ00237 345 IEKHKVTHTLTLPKTIRYLIKtdpEAtiirskydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGITYlyc 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 320 ----TNPLNgerkagTVGPAVQGVGCRIAKNGGIEVKTNAI------------FAG-YWKNPKKTAEEFTE-DGWFKTGD 381
Cdd:PTZ00237 425 yghiNIPYN------ATGVPSIFIKPSILSEDGKELNVNEIgevafklpmppsFATtFYKNDEKFKQLFSKfPGYYNSGD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 382 VGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVV----PSEKVTDEKEFE 457
Cdd:PTZ00237 499 LGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVlkqdQSNQSIDLNKLK 578
|
490 500 510
....*....|....*....|....*....|....*....
gi 32563687 458 KKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PTZ00237 579 NEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
47-496 |
3.24e-13 |
|
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: 71.35 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 47 TTYGEFVKRTGQYATALTEKYNIkkGDRVMA-RVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATPSILVS 125
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQT--EERAIGlRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 126 cNEELDKVFRDKIrvinedklaseagslnacTMIEHVEKSDPASVCY---TSGTTGLPKGAILTHGSLSNNAHDIVRDWG 202
Cdd:cd17654 95 -NKELDNAPLSFT------------------PEHRHFNIRTDECLAYvihTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 203 FTGNDYNLHAlPFYH----VHGLYYSLH--CSLFS--HSTMIWRSKFevEDCIKYMKNATVMMGVPTFFSRLLAS--KNF 272
Cdd:cd17654 156 ITSEDILFLT-SPLTfdpsVVEIFLSLSsgATLLIvpTSVKVLPSKL--ADILFKRHRITVLQATPTLFRRFGSQsiKST 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 273 NKEAFGNVRVFISGSAPLSVSTI------EEFRERTGQVilerYGMTEAGV-MTTNPLNGERKAGTVGPAVQGVGCRIAK 345
Cdd:cd17654 233 VLSATSSLRVLALGGEPFPSLVIlsswrgKGNRTRIFNI----YGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIEVRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 346 NGGIEVKTNaIFAGYWKNPKKTAEEFT--EDGWFKTGDVGHLdEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLPFV 423
Cdd:cd17654 309 QNGSEGTGQ-VFLGGLNRVCILDDEVTvpKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563687 424 KESAVIASphpDFGEAVVAIVVPSEKVTDEKEFEKKLigimkkkVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd17654 387 ESCAVTLS---DQQRLIAFIVGESSSSRIHKELQLTL-------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
44-498 |
1.24e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 67.09 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 44 DRKTTYGEFVKRTGQYATALTEkYNIKKGDRVmarvskttdtaALYI-----------ACLQIGALYIPVNPGYTESEAA 112
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKS-LGVKKGDRV-----------AIYMpmipeaavamlACARIGAVHSVVFGGFSAEALA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 113 HYIKDATPSILVSCNEeldkVFRdKIRVINEDKLASEAgsLNACTMIEHV---------------------EKSDPASV- 170
Cdd:PRK00174 164 DRIIDAGAKLVITADE----GVR-GGKPIPLKANVDEA--LANCPSVEKVivvrrtggdvdwvegrdlwwhELVAGASDe 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 171 C--------------YTSGTTGLPKGaILthgslsnnaHDivrdwgfTGNdYNLHAlpfyhvhglyyslhcslfsHSTMI 236
Cdd:PRK00174 237 CepepmdaedplfilYTSGSTGKPKG-VL---------HT-------TGG-YLVYA-------------------AMTMK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 237 WrsKFEVED-----C------------IKY---MKNATVMM--GVPTF--FSRllasknfnkeaFGNV----RVFISGSA 288
Cdd:PRK00174 280 Y--VFDYKDgdvywCtadvgwvtghsyIVYgplANGATTLMfeGVPNYpdPGR-----------FWEVidkhKVTIFYTA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 289 PLSVSTI----EEFRERT--------GQV----------------------ILERYGMTEAGVMTTNPLNG--ERKAGTV 332
Cdd:PRK00174 347 PTAIRALmkegDEHPKKYdlsslrllGSVgepinpeawewyykvvggercpIVDTWWQTETGGIMITPLPGatPLKPGSA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 333 GPAVQGVGCRIAKNGGIEVKTNAifAGY--------------WKNPKKTAEEF--TEDGWFKTGDVGHLDEDGYLTIGGR 396
Cdd:PRK00174 427 TRPLPGIQPAVVDEEGNPLEGGE--GGNlvikdpwpgmmrtiYGDHERFVKTYfsTFKGMYFTGDGARRDEDGYYWITGR 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 397 SKDMvitggLNV-------YpkELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVA 469
Cdd:PRK00174 505 VDDV-----LNVsghrlgtA--EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIG 577
|
570 580
....*....|....*....|....*....
gi 32563687 470 NYKVPKRVIVLDDLPRNHITKVQKNVLRD 498
Cdd:PRK00174 578 PIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
41-485 |
6.06e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 64.97 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 41 IDGDRKTTYGEFVKRTGQYATALTEkYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHYIKDATP 120
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRS-LGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 121 SILVS---------------------------------CNEELDKVFRDKIRviNEDKLASEAGSLNACTMIEHVEKSDP 167
Cdd:PRK10524 158 VLIVSadagsrggkvvpykplldeaialaqhkprhvllVDRGLAPMARVAGR--DVDYATLRAQHLGARVPVEWLESNEP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 168 ASVCYTSGTTGLPKGailthgslsnnahdIVRDWG----------------------FTGND--------YNLHA----- 212
Cdd:PRK10524 236 SYILYTSGTTGKPKG--------------VQRDTGgyavalatsmdtifggkagetfFCASDigwvvghsYIVYApllag 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 213 --------LPFYHVHGLYYSLhcslfshstmiwrskfeVEdciKYmkNATVMMGVPTFFsRLLasKNFNKEAFGN----- 279
Cdd:PRK10524 302 matimyegLPTRPDAGIWWRI-----------------VE---KY--KVNRMFSAPTAI-RVL--KKQDPALLRKhdlss 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 280 VRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEAG--VMTTNPLNGER--KAGTVGPAVQGVGCR-IAKNGGIEVKTN 354
Cdd:PRK10524 357 LRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGwpILAIARGVEDRptRLGSPGVPMYGYNVKlLNEVTGEPCGPN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 355 -----AIFA-------------------GYWKNPKKTAeeftedgwFKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYP 410
Cdd:PRK10524 437 ekgvlVIEGplppgcmqtvwgdddrfvkTYWSLFGRQV--------YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 411 KELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVP--SEKVTDE---KEFEKKLIGIMKKKVANYKVPKRVIVLDDLPR 485
Cdd:PRK10524 509 REIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPkdSDSLADRearLALEKEIMALVDSQLGAVARPARVWFVSALPK 588
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
38-188 |
1.84e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); 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. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 56.90 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 38 LLFIDGD---RKTTYGEFVKRTGQYATALtEKYNIKKGDRVMARVSKTTDTAALYIACLQIGALYIPVNPGYTESEAAHY 114
Cdd:cd05943 87 AIYAAEDgerTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 115 IKDATPSILVSCNEEL--DKVF--RDKIRVIN--------------------------------EDKLASE-AGSLNact 157
Cdd:cd05943 166 FGQIEPKVLFAVDAYTynGKRHdvREKVAELVkglpsllavvvvpytvaagqpdlskiakaltlEDFLATGaAGELE--- 242
|
170 180 190
....*....|....*....|....*....|.
gi 32563687 158 mIEHVEKSDPASVCYTSGTTGLPKGAILTHG 188
Cdd:cd05943 243 -FEPLPFDHPLYILYSSGTTGLPKCIVHGAG 272
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
173-485 |
4.85e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 55.16 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 173 TSGTTGLPKGAILTHGSLSNNAhDIV----RDWGFTGNDYNLHALPfYHV----HGLYYSLH---CSLFSHSTMIwrskf 241
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWA-ELFarslRAAGVRPGDRVQNAFG-YGLftggLGLHYGAErlgATVIPAGGGN----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 242 eVEDCIKYMK--NATVMMGVPTFFSRLL---ASKNFNKEAFGnVRVFISGSAPLSVSTIEEFRERTGQVILERYGMTEag 316
Cdd:COG1541 164 -TERQLRLMQdfGPTVLVGTPSYLLYLAevaEEEGIDPRDLS-LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 317 vmttnplngerkagtVGPAVqGVGCRiAKNGG--------IEV---KTNAIFA-GywknpkktaEE-------FTEDGW- 376
Cdd:COG1541 240 ---------------VGPGV-AYECE-AQDGLhiwedhflVEIidpETGEPVPeG---------EEgelvvttLTKEAMp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 377 ---FKTGDVGHLDED------GYLTIG---GRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDfGEAVVAIV 444
Cdd:COG1541 294 lirYRTGDLTRLLPEpcpcgrTHPRIGrilGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREG-GLDELTVR 372
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 32563687 445 VPSEKVTDEKEFEKKLIGIMKKKVanyKVPKRVIVL--DDLPR 485
Cdd:COG1541 373 VELAPGASLEALAEAIAAALKAVL---GLRAEVELVepGSLPR 412
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
90-496 |
8.45e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 90 IACLQIGALYIPVNPGYTESEAAHYIKDATPSILV---SCNE-------ELDKVFRDKIRVInEDKLASEAGSLNACTmi 159
Cdd:PRK05691 3788 VGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcsaACREqaralldELGCANRPRLLVW-EEVQAGEVASHNPGI-- 3864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 160 eHVEKSDPASVCYTSGTTGLPKGAILTHGSLSNNAHDIVRDWGFTGND---------YNLHALPFyhvhglyysLHCSLF 230
Cdd:PRK05691 3865 -YSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADviaqtasqsFDISVWQF---------LAAPLF 3934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 231 SHSTMIwrskfeVEDCIKYMKNA----------TVMMGVPTFFSRLLASknfNKEAFGNVRVFISGSAPLSVSTIEEFRE 300
Cdd:PRK05691 3935 GARVEI------VPNAIAHDPQGllahvqaqgiTVLESVPSLIQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQ 4005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 301 RTGQV-ILERYGMTEA---------------------GVMTTNP----LNGERK---AGTVGP---AVQGVGcriakngg 348
Cdd:PRK05691 4006 RYPQIgLVNAYGPAECsddvaffrvdlastrgsylpiGSPTDNNrlylLDEALElvpLGAVGElcvAGTGVG-------- 4077
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 349 ievktnaifAGYWKNPKKTAEEFTEDGW-------FKTGDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTLP 421
Cdd:PRK05691 4078 ---------RGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQA 4148
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563687 422 FVKESAVIASPHPDfGEAVVAIVVPSEKVTDEKEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:PRK05691 4149 EVREAAVAVQEGVN-GKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
341-496 |
1.08e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 54.45 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 CRIAKNGGIEVKTNAIFAGYWKNPKKTAEEFTeDGWF-----------------------------KTGDVGHLDEDGYL 391
Cdd:cd17647 310 CGIGEVGEIYVRAGGLAEGYRGLPELNKEKFV-NNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDC 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 392 TIGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVP---------------SEKVTDE--- 453
Cdd:cd17647 389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPrfdkpddesfaqedvPKEVSTDpiv 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 32563687 454 ------KEFEKKLIGIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:cd17647 469 kgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
341-496 |
3.19e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 46.98 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 341 CRIAKNGGIEVKTNAIFAGYWKNPKKTAEEF------TEDGW----------------------FKTGDVGHLDEDGYLT 392
Cdd:TIGR03443 616 CGVGEVGEIYVRAGGLAEGYLGLPELNAEKFvnnwfvDPSHWidldkennkperefwlgprdrlYRTGDLGRYLPDGNVE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 393 IGGRSKDMVITGGLNVYPKELEDFIDTLPFVKESAVIASPHPDFGEAVVAIVVPSEKVTDEKEFE--------------- 457
Cdd:TIGR03443 696 CCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKsevddeessdpvvkg 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 32563687 458 ----KKLI----GIMKKKVANYKVPKRVIVLDDLPRNHITKVQKNVL 496
Cdd:TIGR03443 776 likyRKLIkdirEYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
380-501 |
4.23e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 46.23 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 380 GDVGHLDEDGYLTIGGRSKDMVITGGLNVYPKELEDFIDTL-PFVKESAVIASPHPDFG--EAVVAIVV--PSEKVTDEK 454
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAAdESVLETAAIGVPPPGGGpeQLVIAAVLkdPPGSNPDLN 673
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 32563687 455 EFEKKL-IGIMKKKVANYKVpKRVIVLDDLPRNHITKVQKNVLRDTYK 501
Cdd:PLN03052 674 ELKKIFnSAIQKKLNPLFKV-SAVVIVPSFPRTASNKVMRRVLRQQLA 720
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
389-503 |
1.50e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 44.42 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 389 GYLTIGGRSKDMVITGGLNVYPKELEDFID-TLPFVKESAVIASPHPDFGEAVVAIVVPS--EKVTDEKEFEKKLIGIMK 465
Cdd:PLN03051 371 GYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLgeEKKGFDQARPEALQKKFQ 450
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 32563687 466 KKVAN-----YKVpKRVIVLDDLPRNHITKVQKNVLRDTYKNL 503
Cdd:PLN03051 451 EAIQTnlnplFKV-SRVKIVPELPRNASNKLLRRVLRDQLKKE 492
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
48-244 |
3.61e-03 |
|
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: 40.02 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 48 TYGEFVKRTGQYATALTEKYNIKKGDRVMARVSKTTD-TAALYiACLQIGALYIPVNPgyteSEAAHYIKDATPSILV-- 124
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDfVAAFY-GCLYAGVVPIPIEP----PDISQQLGFLLGTCKVrv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563687 125 -----SCNEELDK-VFRDKIRVINEDKLA----------SEAGSLNACTMIEHVEKSDPASVC--YTSGTTGLPKGAILT 186
Cdd:cd05905 91 altveACLKGLPKkLLKSKTAAEIAKKKGwpkildfvkiPKSKRSKLKKWGPHPPTRDGDTAYieYSFSSDGSLSGVAVS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32563687 187 HGSLSNNAHDIVRDWGFTGNDYNLHALPFYHVHGLYYSLHCSLFSHSTMIWRSKFEVE 244
Cdd:cd05905 171 HSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMK 228
|
|
| |
