|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
84-614 |
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: 676.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 84 ESIAVTAHEKSHSYHQLILSAVKISNLLTGADlrsvkgngenKHLGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALS 163
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALG----------KDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 164 YPEAELLHVMNDSDITMILstedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheisg 243
Cdd:cd05941 71 YPLAELEYVITDSEPSLVL------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 dDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVR 323
Cdd:cd05941 90 -DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 GIWQRwresypqdqtKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTASATAARQLRLMMCGSSALPLPVMQKWETITGH 403
Cdd:cd05941 169 EVAIS----------RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGH 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS--CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFID 481
Cdd:cd05941 239 TLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGepLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GGFFKTGDAARVDEDGYYVILGRTNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikr 561
Cdd:cd05941 319 DGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG--- 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 747052525 562 kreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05941 396 ------AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
68-619 |
3.26e-145 |
|
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: 428.46 E-value: 3.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRgsiSPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRsvkgngenkhlGGARVGIVAKPSPEFVAGV 147
Cdd:COG0318 1 LADLLRRAAAR---HPDRPALVFGGRRLTYAELDARARRLAAALRALGVG-----------PGDRVALLLPNSPEFVVAF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILStedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeld 227
Cdd:COG0318 67 LAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 228 gtrclqeteipheisgddpALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAP 307
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 308 LYAGSTVEFMPKFSVRGIWQ---RWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMC 384
Cdd:COG0318 164 LLAGATLVLLPRFDPERVLElieRER-------------VTVLFGVPTMLARLLRHPEFARYDLSS--------LRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 GSSALPLPVMQKWETITGHVLLERYGMTE-FVMAISNPL-KGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKS 461
Cdd:COG0318 223 GGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVTVNPEdPGERRPGSVGRPLPGVEVRIVDEDGReLPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSLFKEYWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLP 541
Cdd:COG0318 303 PNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRK-KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVP 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 542 DKDYGEAVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:COG0318 381 DEKWGERVVAFVVLRPG----------AELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-613 |
1.24e-122 |
|
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: 371.13 E-value: 1.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd05936 13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQP-----------GDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEDHQELMKAiavktsaqmsllpsvpsvstksteldhtingeldgtrcLQETEIPHEIS 242
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVSFTDLLAA--------------------------------------GAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAW---GYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPK 319
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWledLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWET 399
Cdd:cd05936 203 FRPIGVLK----------EIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSS--------LRLCISGGAPLPVEVAERFEE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTEFVMAIS-NPLKGKRKGGTVGKPLPGVQAKIIAEDGscdNV----EVGELCIKSPSLFKEYWNLPEV 474
Cdd:cd05936 265 LTGVPIVEGYGLTETSPVVAvNPLDGPRKPGSIGIPLPGTEVKIVDDDG---EElppgEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 475 TKQSFIDGgFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIII 554
Cdd:cd05936 342 TAEAFVDG-WLRTGDIGYMDEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 555 PNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05936 420 LKEG----------ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
82-618 |
2.65e-120 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 366.12 E-value: 2.65e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSH-SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPL 160
Cdd:PRK07514 15 DRDAPFIETPDGLRyTYGDLDAASARLANLLVALGVKP-----------GDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 161 ALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKtsaqmsllPSVPSVSTksteLDHTINGEL-DGTRCLQETEIPH 239
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAA--------AGAPHVET----LDADGTGSLlEAAAAAPDDFETV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPK 319
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGIWQRWRESypqdqtkaddavTVFTGVPTMYTRLIQgyeamDPALqtaSATAARQLRLMMCGSSALPLPVMQKWET 399
Cdd:PRK07514 232 FDPDAVLALMPRA------------TVMMGVPTFYTRLLQ-----EPRL---TREAAAHMRLFISGSAPLLAETHREFQE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKII-AEDG-SCDNVEVGELCIKSPSLFKEYWNLPEVTKQ 477
Cdd:PRK07514 292 RTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTdPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 SFIDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPnp 557
Cdd:PRK07514 372 EFRADGFFITGDLGKIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVP-- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 558 eikrkreeelKPALTLEELSMWA--KEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK07514 449 ----------KPGAALDEAAILAalKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
104-613 |
5.29e-119 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 362.00 E-value: 5.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 104 AVKISNL-LTGADLRSVKGNGENKHLGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMIL 182
Cdd:PRK07787 18 AVRIGGRvLSRSDLAGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 183 stedhqelmkaiaVKTSAQMSLLPSVP-SVSTKStelDHTingeldgtrclqeteiPHEISGDDPALIIYTSGTTGKPKG 261
Cdd:PRK07787 98 -------------GPAPDDPAGLPHVPvRLHARS---WHR----------------YPEPDPDAPALIVYTSGTTGPPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 262 VVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQrwresypqdqtKAD 341
Cdd:PRK07787 146 VVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQ-----------ALS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 342 DAVTVFTGVPTMYTRLiqgyeAMDPALQTASATAarqlRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNP 421
Cdd:PRK07787 215 EGGTLYFGVPTVWSRI-----AADPEAARALRGA----RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 422 LKGKRKGGTVGKPLPGVQAKIIAEDGS---CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGY 498
Cdd:PRK07787 286 ADGERRPGWVGLPLAGVETRLVDEDGGpvpHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 499 YVILGRTNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpalTLEELSM 578
Cdd:PRK07787 366 HRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV------------AADELID 433
|
490 500 510
....*....|....*....|....*....|....*
gi 747052525 579 WAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK07787 434 FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
245-607 |
5.66e-111 |
|
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: 336.18 E-value: 5.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFnALLAPLYAGSTVEFMPKFSVRG 324
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIQGYEAMDPALqtasataaRQLRLMMCGSSALPLPVMQKWETITGHV 404
Cdd:cd04433 80 ALELIER----------EKVTILLGVPTLLARLLKAPESAGYDL--------SSLRALVSGGAPLPPELLERFEEAPGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 405 LLERYGMTE--FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFID 481
Cdd:cd04433 142 LVNGYGLTEtgGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGgELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 gGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikr 561
Cdd:cd04433 222 -GWYRTGDLGRLDEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG--- 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 747052525 562 kreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKV 607
Cdd:cd04433 297 -------ADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
83-618 |
1.91e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 315.59 E-value: 1.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRsvkgngenkhlGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRALGVK-----------KGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEDHQELMKAIAvktsaqmSLLPSVPSV---STKSTELDHTINGELDGTRCLQETEIP- 238
Cdd:PRK06187 89 RLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIL-------PQLPTVRTViveGDGPAAPLAPEVGEYEELLAAASDTFDf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 239 HEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMP 318
Cdd:PRK06187 162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW-GLPYLALMAGAKQVIPR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KFSVRGIWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIQgyeamDPAlqtASATAARQLRLMMCGSSALPLPVMQKWE 398
Cdd:PRK06187 241 RFDPENLLDLIET----------ERVTFFFAVPTIWQMLLK-----APR---AYFVDFSSLRLVIYGGAALPPALLREFK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 TITGHVLLERYGMTEF--VMAISNP----LKGKRKGGTVGKPLPGVQAKIIAEDGS---CDNVEVGELCIKSPSLFKEYW 469
Cdd:PRK06187 303 EKFGIDLVQGYGMTETspVVSVLPPedqlPGQWTKRRSAGRPLPGVEARIVDDDGDelpPDGGEVGEIIVRGPWLMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 470 NLPEVTKqSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAV 549
Cdd:PRK06187 383 NRPEATA-ETIDGGWLHTGDVGYIDEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERP 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 550 CAIIIPnpeikrKREEELKPaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK06187 461 VAVVVL------KPGATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
83-513 |
8.49e-99 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 307.70 E-value: 8.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHE-KSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:pfam00501 9 PDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGK-----------GDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILsTEDHQELMKAIAVKTSAQMSLLPSVPSVSTKSTELDHTINGELDGtrclQETEIPHEI 241
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAD----VPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDPALIIYTSGTTGKPKGVVHTHKGVLAQV----QMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFM 317
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 PKFSVRGIWQRWR--ESYPqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQ 395
Cdd:pfam00501 233 PGFPALDPAALLEliERYK---------VTVLYGVPTLLNMLLEAGAPKRALLSS--------LRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWETITGHVLLERYGMTE---FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV--EVGELCIKSPSLFKEYWN 470
Cdd:pfam00501 296 RFRELFGGALVNGYGLTEttgVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPpgEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 747052525 471 LPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVG 513
Cdd:pfam00501 376 DPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKK-DQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
88-619 |
1.36e-98 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 312.05 E-value: 1.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 88 VTAHEKSHSYHQLILSAVKISNLLTGADLRsvKGNgenkhlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEA 167
Cdd:COG0365 33 EDGEERTLTYAELRREVNRFANALRALGVK--KGD---------RVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 168 ELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQ--MSLLPSVPSV-STKSTELDHTINGELDGTRCLQETEIPHEI--- 241
Cdd:COG0365 102 ALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDeaLEELPSLEHViVVGRTGADVPMEGDLDWDELLAAASAEFEPept 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAW-GYTSTDHFLhCLP-LHHVHGLFNALLAPLYAGSTVeFM-- 317
Cdd:COG0365 182 DADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFW-CTAdIGWATGHSYIVYGPLLNGATV-VLye 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 --PKFSVRGIWqrWR--ESYpqdqtkaddAVTVFTGVPTMYTRLIQgyeAMDPALQTASATAarqLRLMMCGSSALPLPV 393
Cdd:COG0365 260 grPDFPDPGRL--WEliEKY---------GVTVFFTAPTAIRALMK---AGDEPLKKYDLSS---LRLLGSAGEPLNPEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEFVMA-ISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKS--PSLFKEYW 469
Cdd:COG0365 323 WEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVDEDGnPVPPGEEGELVIKGpwPGMFRGYW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 470 NLPEVTKQSFID--GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:COG0365 403 NDPERYRETYFGrfPGWYRTGDGARRDEDGYFWILGRSD-DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQ 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747052525 548 AVCAIIIPNPEIkrKREEELKpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:COG0365 482 VVKAFVVLKPGV--EPSDELA-----KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
78-609 |
4.74e-97 |
|
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: 303.76 E-value: 4.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 78 RGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVA 157
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAK-----------GDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 158 VPLALSYPEAELLHVMNDSDITMILstedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqetei 237
Cdd:cd17631 73 VPLNFRLTPPEVAYILADSGAKVLF------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 pheisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFM 317
Cdd:cd17631 98 ------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 PKFSVRGIWqrwresypqdQTKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKW 397
Cdd:cd17631 172 RKFDPETVL----------DLIERHRVTSFFLVPTMIQALLQHPRFATTDLSS--------LRAVIYGGAPMPERLLRAL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 ETItGHVLLERYGMTEFVMAIS--NPLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEV 474
Cdd:cd17631 234 QAR-GVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFVEVRIVDPDGReVPPGEVGEIVVRGPHVMAGYWNRPEA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 475 TKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIII 554
Cdd:cd17631 313 TAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 555 PNPEIKrkreeelkpaLTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNK 609
Cdd:cd17631 391 PRPGAE----------LDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
82-614 |
1.46e-95 |
|
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: 301.92 E-value: 1.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:cd05926 2 DAPALVVPGSTPALTYADLAELVDDLARQLAALGIKK-----------GDRVAIALPNGLEFVVAFLAAARAGAVVAPLN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILSTEDhqELMKAIAVKTSAQMSLLPSVPSVSTKSTELD-HTINGELDGTRCLQETEIPHE 240
Cdd:cd05926 71 PAYKKAEFEFYLADLGSKLVLTPKG--ELGPASRAASKLGLAILELALDVGVLIRAPSaESLSNLLADKKNAKSEGVPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 isgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKF 320
Cdd:cd05926 149 ---DDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 321 SVRGIWQrWRESYpqdqtkaddAVTVFTGVPTMYTRLIQGYEAmdpalqtASATAARQLRLMMCGSSALPLPVMQKWETI 400
Cdd:cd05926 226 SASTFWP-DVRDY---------NATWYTAVPTIHQILLNRPEP-------NPESPPPKLRFIRSCSASLPPAVLEALEAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 401 TGHVLLERYGMTEFVMAI-SNPLK-GKRKGGTVGKPLpGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQ 477
Cdd:cd05926 289 FGAPVLEAYGMTEAAHQMtSNPLPpGPRKPGSVGKPV-GVEVRILDEDGEiLPPGVVGEICLRGPNVTRGYLNNPEANAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 SFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPnp 557
Cdd:cd05926 368 AAFKDGWFRTGDLGYLDADGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL-- 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 558 eikrkreeELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05926 445 --------REGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
65-615 |
1.86e-90 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 289.11 E-value: 1.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 65 NSILMELVKAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLtgadlrsvkgngenKHLG---GARVGIVAKPSP 141
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAAL--------------AALGigkGDRVAIWAPNSP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 142 EFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDhqelmkaiavktsaqmsLLPSVPSVSTKSTELDHT 221
Cdd:PRK07656 67 HWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL-----------------FLGVDYSATTRLPALEHV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 222 INGELDGTRCL--------------QETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDH 287
Cdd:PRK07656 130 VICETEEDDPHtekmktftdflaagDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 288 FLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIQgYEAmdpa 367
Cdd:PRK07656 210 YLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIET----------ERITVLPGPPTMYNSLLQ-HPD---- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 368 lqtASATAARQLRLMMCGSSALPLPVMQKWETITG-HVLLERYGMTEFV-MAISNPLKGKRKG--GTVGKPLPGVQAKII 443
Cdd:PRK07656 275 ---RSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLDDDRKTvaGTIGTAIAGVENKIV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 444 AEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQSfIDG-GFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALE 521
Cdd:PRK07656 352 NELGEEVPVgEVGELLVRGPNVMKGYYDDPEATAAA-IDAdGWLHTGDLGRLDEEGYLYIVDRKK-DMFIVGGFNVYPAE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 522 IEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPR 601
Cdd:PRK07656 430 VEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP----------GAELTEEELIAYCREHLAKYKVPRSIEFLDELPK 499
|
570
....*....|....
gi 747052525 602 NAMGKVNKKELKKQ 615
Cdd:PRK07656 500 NATGKVLKRALREK 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
130-608 |
3.03e-87 |
|
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: 279.87 E-value: 3.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQElmkaiAVKTSAQmsLLPSVP 209
Cdd:cd05911 35 GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLE-----KVKEAAK--ELGPKD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SV-STKSTELDHTINGELDGTRCLQETE---IPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWG--YT 283
Cdd:cd05911 108 KIiVLDDKPDGVLSIEDLLSPTLGEEDEdlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYgnDG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 284 STDHFLHCLPLHHVHGLFNALLAPLYaGSTVEFMPKFSVR---GIWQRWResypqdqtkaddaVTVFTGVPTMYTRLiqg 360
Cdd:cd05911 188 SNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSElflDLIEKYK-------------ITFLYLVPPIAAAL--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 361 yeAMDPALQTASAtaaRQLRLMMCGSSALPLPVMQKWETITGHV-LLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQ 439
Cdd:cd05911 251 --AKSPLLDKYDL---SSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 440 AKIIAEDGsCDNV---EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYK 516
Cdd:cd05911 326 AKIVDDDG-KDSLgpnEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK-ELIKYKGFQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 517 LSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYK-------- 588
Cdd:cd05911 404 VAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP----------GEKLTEKEVKDYVAKKVASYKqlrggvvf 473
|
490 500
....*....|....*....|
gi 747052525 589 IPnclllweSLPRNAMGKVN 608
Cdd:cd05911 474 VD-------EIPKSASGKIL 486
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
130-612 |
1.37e-79 |
|
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: 258.18 E-value: 1.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITmilstedhqelmkaIAVKTSAQmsllpsvp 209
Cdd:cd05935 26 GDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK--------------VAVVGSEL-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 svstksteldhtingeldgtrclqeteipheisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFL 289
Cdd:cd05935 84 ----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVIL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 290 HCLPLHHVHGLFNALLAPLYAGSTVEFMpkfsvrGIWQrwRESYPQDQTKAddAVTVFTGVPTMYTRLIQGYEAMDPALQ 369
Cdd:cd05935 130 ACLPLFHVTGFVGSLNTAVYVGGTYVLM------ARWD--RETALELIEKY--KVTFWTNIPTMLVDLLATPEFKTRDLS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 370 TasataarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAI-SNPlKGKRKGGTVGKPLPGVQAKII-AEDG 447
Cdd:cd05935 200 S--------LKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQThTNP-PLRPKLQCLGIP*FGVDARVIdIETG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 448 S-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFI-DGG--FFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIE 523
Cdd:cd05935 271 ReLPPNEVGEIVVRGPQIFKGYWNRPEETEESFIeIKGrrFFRTGDLGYMDEEGYFFFVDRVK-RMINVSGFKVWPAEVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 524 AVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKREEelkpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNA 603
Cdd:cd05935 350 AKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE--------EDIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 747052525 604 MGKVNKKEL 612
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
130-615 |
3.75e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 260.66 E-value: 3.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKT------SAQMS 203
Cdd:PRK08314 61 GDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLrlrhviVAQYS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 204 -LLP-----SVPSVSTKSTEL-DHTINGELDGTRCLQETEIP--HEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVq 274
Cdd:PRK08314 141 dYLPaepeiAVPAWLRAEPPLqALAPGGVVAWKEALAAGLAPppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 275 MLTDAW-GYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPkfsvrgiwqRWresypqDQTKADDA-----VTVFT 348
Cdd:PRK08314 220 VGSVLWsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---------RW------DREAAARLieryrVTHWT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 349 GVPTMYTRLIqgyeaMDPALqtasatAARQLRLMMC---GSSALPLPVMQKWETITGHVLLERYGMTEfVMA--ISNPlK 423
Cdd:PRK08314 285 NIPTMVVDFL-----ASPGL------AERDLSSLRYiggGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAqtHSNP-P 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 424 GKRKGGTVGKPLPGVQAKII-----AE--DGscdnvEVGELCIKSPSLFKEYWNLPEVTKQSFI--DGG-FFKTGDAARV 493
Cdd:PRK08314 352 DRPKLQCLGIPTFGVDARVIdpetlEElpPG-----EVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGKrFFRTGDLGRM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 494 DEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKREEelkpaltl 573
Cdd:PRK08314 427 DEEGYFFITDRLKRMI-NASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTE-------- 497
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 747052525 574 EELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK08314 498 EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
130-577 |
1.31e-77 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 258.11 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILsTEDHQELMKAIAVKtsAQMSLLPSVP 209
Cdd:COG1022 65 GDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLF-VEDQEQLDKLLEVR--DELPSLRHIV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTIN--GEL--DGTRCLQETEI---PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGY 282
Cdd:COG1022 142 VLDPRGLRDDPRLLslDELlaLGREVADPAELearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 283 TSTDHFLHCLPLHHVHGLFNALLApLYAGSTVefmpkfsvrgiwqrwreSYPQDQTK-ADD----AVTVFTGVP----TM 353
Cdd:COG1022 222 GPGDRTLSFLPLAHVFERTVSYYA-LAAGATV-----------------AFAESPDTlAEDlrevKPTFMLAVPrvweKV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 354 YTRLIQGYEAMDP--------ALQTASATAAR--------------------------------QLRLMMCGSSALPlPV 393
Cdd:COG1022 284 YAGIQAKAEEAGGlkrklfrwALAVGRRYARArlagkspslllrlkhaladklvfsklrealggRLRFAVSGGAALG-PE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEFVMAIS-NPLkGKRKGGTVGKPLPGVQAKIiAEDGscdnvevgELCIKSPSLFKEYWNLP 472
Cdd:COG1022 363 LARFFRALGIPVLEGYGLTETSPVITvNRP-GDNRIGTVGPPLPGVEVKI-AEDG--------EILVRGPNVMKGYYKNP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 473 EVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKV-GGYKLSALEIEAVLLEHPTISECCVLGlPDKDYgeaVCA 551
Cdd:COG1022 433 EATAEAFDADGWLHTGDIGELDEDGFLRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG-DGRPF---LAA 507
|
490 500
....*....|....*....|....*..
gi 747052525 552 IIIPNPE-IKRKREEELKPALTLEELS 577
Cdd:COG1022 508 LIVPDFEaLGEWAEENGLPYTSYAELA 534
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
130-613 |
1.78e-76 |
|
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: 249.90 E-value: 1.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILStedhqelmkaiavktsaqmsllpsvp 209
Cdd:cd05934 28 GDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 svstksteldhtingeldgtrclqeteipheisgdDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFL 289
Cdd:cd05934 82 -----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 290 HCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWRESypqdqtkaddAVTVFTGVPTMYTRLIQGYEAMDPalq 369
Cdd:cd05934 127 TVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRY----------GATVTNYLGAMLSYLLAQPPSPDD--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 370 tasatAARQLRLmmCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS- 448
Cdd:cd05934 194 -----RAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQe 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 449 CDNVEVGELCIKS---PSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAV 525
Cdd:cd05934 267 LPAGEPGELVIRGlrgWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRK-KDMIRRRGENISSAEVERA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 526 LLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikrkreeeLKPALTL--EELSMWAKEKLAPYKIPNCLLLWESLPRNA 603
Cdd:cd05934 345 ILRHPAVREAAVVAVPDEVGEDEVKAVVV------------LRPGETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412
|
490
....*....|
gi 747052525 604 MGKVNKKELK 613
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
132-613 |
1.30e-74 |
|
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: 247.28 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 132 RVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSditmilstedhqelmKAIAVKTSAQmsLLPSVPSV 211
Cdd:cd05959 56 RVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS---------------RARVVVVSGE--LAPVLAAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 212 STKSTELDHTI---NGELDGTRCLQETEIPHEISG---------DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT-D 278
Cdd:cd05959 119 LTKSEHTLVVLivsGGAGPEAGALLLAELVAAEAEqlkpaathaDDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYArN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 AWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKF-SVRGIWQRWRESYPqdqtkaddavTVFTGVPTMYTRL 357
Cdd:cd05959 199 VLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRP----------TVFFGVPTLYAAM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 358 iqgyeamdPALQTASATAARQLRlmMCGSSALPLP--VMQKWETITGHVLLERYGMTEFV-MAISNpLKGKRKGGTVGKP 434
Cdd:cd05959 269 --------LAAPNLPSRDLSSLR--LCVSAGEALPaeVGERWKARFGLDILDGIGSTEMLhIFLSN-RPGRVRYGTTGKP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 435 LPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVG 513
Cdd:cd05959 338 VPGYEVELRDEDGGDVADgEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRAD-DMLKVS 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 514 GYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKrkreeelKPALTLEELSMWAKEKLAPYKIPNCL 593
Cdd:cd05959 416 GIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE-------DSEALEEELKEFVKDRLAPYKYPRWI 488
|
490 500
....*....|....*....|
gi 747052525 594 LLWESLPRNAMGKVNKKELK 613
Cdd:cd05959 489 VFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
83-612 |
2.35e-74 |
|
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: 244.74 E-value: 2.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGP-----------GDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheis 242
Cdd:cd05930 70 SYPAERLAYILEDSGAKLVLTD---------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNaLLAPLYAGSTVEFMPKFSV 322
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEEVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RGIWQ--RWRESYpqdqtkaddAVTVFTGVPTMYTRLiqgyeamdpaLQTASATAARQLRLMMCGSSALPLPVMQKW-ET 399
Cdd:cd05930 171 KDPEAlaDLLAEE---------GITVLHLTPSLLRLL----------LQELELAALPSLRLVLVGGEALPPDLVRRWrEL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTEFVMAIS--NPLKGKRKGGTV--GKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEV 474
Cdd:cd05930 232 LPGARLVNLYGPTEATVDATyyRVPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPgVPGELYIGGAGLARGYLNRPEL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 475 TKQSFIDGGFF------KTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEA 548
Cdd:cd05930 312 TAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRI-DDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKR 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 549 VCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd05930 391 LVAYVVPDEG----------GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
142-614 |
1.25e-73 |
|
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: 242.67 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 142 EFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILstedhqelmkaiavktsaqmsllpsvpsvstksteldht 221
Cdd:cd05903 38 EFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--------------------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 222 INGELDGTRclqeteipHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLF 301
Cdd:cd05903 79 VPERFRQFD--------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 302 NALLAPLYAGSTVEFMpkfsvrgiwQRWresypqDQTKA-----DDAVTVFTGVPTMYTRLIQGYEAMDPALqtasataa 376
Cdd:cd05903 151 YGFTLPLLLGAPVVLQ---------DIW------DPDKAlalmrEHGVTFMMGATPFLTDLLNAVEEAGEPL-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 377 RQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKG--KRKGGTVGKPLPGVQAKIIAEDGSC-DNVE 453
Cdd:cd05903 208 SRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDDTGATlAPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 454 VGELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTIS 533
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGR-SKDIIIRGGENIPVLEVEDLLLGHPGVI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 534 ECCVLGLPDKDYGEAVCAIIIPNPeikrkreeelkPA-LTLEEL-SMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKE 611
Cdd:cd05903 366 EAAVVALPDERLGERACAVVVTKS-----------GAlLTFDELvAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFR 434
|
...
gi 747052525 612 LKK 614
Cdd:cd05903 435 LRE 437
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
130-619 |
1.37e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 246.45 E-value: 1.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAV---PLalsYPEAELLH----------VMNDSDITMILSTEDHQELMKAIAV 196
Cdd:PRK05605 82 GDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPL---YTAHELEHpfedhgarvaIVWDKVAPTVERLRRTTPLETIVSV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 197 KTSAQMSL-------LPsVPSVSTKSTEL----DHTINGE--LDGTRCLQETEIPH-EISGDDPALIIYTSGTTGKPKGV 262
Cdd:PRK05605 159 NMIAAMPLlqrlalrLP-IPALRKARAALtgpaPGTVPWEtlVDAAIGGDGSDVSHpRPTPDDVALILYTSGTTGKPKGA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 263 VHTHKGVLAQVQMlTDAW--GYTSTDH-FLHCLPLHHVHGL-FNALLAPlYAGSTVEFMPKFSVRGIWQRWRESYPqdqt 338
Cdd:PRK05605 238 QLTHRNLFANAAQ-GKAWvpGLGDGPErVLAALPMFHAYGLtLCLTLAV-SIGGELVLLPAPDIDLILDAMKKHPP---- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 339 kaddavTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFV-MA 417
Cdd:PRK05605 312 ------TWLPGVPPLYEKIAEAAEERGVDLSG--------VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpII 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 418 ISNPLKGKRKGGTVGKPLPGVQAKII-AEDGSCD--NVEVGELCIKSPSLFKEYWNLPEVTKQSFIDgGFFKTGDAARVD 494
Cdd:PRK05605 378 VGNPMSDDRRPGYVGVPFPDTEVRIVdPEDPDETmpDGEEGELLVRGPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVME 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 495 EDGYYVILGRTNADIMkVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikrkreeeLKPALTLE 574
Cdd:PRK05605 457 EDGFIRIVDRIKELII-TGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVV------------LEPGAALD 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 747052525 575 E--LSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PRK05605 524 PegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
75-618 |
4.03e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 240.53 E-value: 4.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 75 VANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGaDLRSVKGNgenkhlggaRVGIVAKPSPEFVAGVLGTWFSG 154
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIY-ELNVKKGE---------RIAILSQNSLEYIVLLFAIAKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 155 GVAVPLALSYPEAELLHVMNDSDITMILSTEDHQelmkAIAVKTSAQMSLLPSVpSVSTKSTELDHTINGELDGtrclqe 234
Cdd:PRK06839 78 CIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQ----NMALSMQKVSYVQRVI-SITSLKEIEDRKIDNFVEK------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 235 teipheiSGDDPALIIYTSGTTGKPKGvvhthkGVLAQVQML------TDAWGYTSTDHFLHCLPLHHVHGLFNALLAPL 308
Cdd:PRK06839 147 -------NESASFIICYTSGTTGKPKG------AVLTQENMFwnalnnTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 309 YAGSTVEFMPKFsvrgiwqrwresypqDQTKA-----DDAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMM 383
Cdd:PRK06839 214 FAGGVIIVPRKF---------------EPTKAlsmieKHKVTVVMGVPTIHQALINCSKFETTNLQS--------VRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPLPVMQKWETiTGHVLLERYGMTE-----FVMAISNplkGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGEL 457
Cdd:PRK06839 271 NGGAPCPEELMREFID-RGFLFGQGFGMTEtsptvFMLSEED---ARRKVGSIGKPVLFCDYELIDENKNKVEVgEVGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 458 CIKSPSLFKEYWNLPEVTKQSfIDGGFFKTGDAARVDEDGYYVILGRTNADIMKvGGYKLSALEIEAVLLEHPTISECCV 537
Cdd:PRK06839 347 LIRGPNVMKEYWNRPDATEET-IQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINKLSDVYEVAV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 538 LGLPDKDYGEAVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLA 617
Cdd:PRK06839 425 VGRQHVKWGEIPIAFIVKKS----------SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
.
gi 747052525 618 D 618
Cdd:PRK06839 495 S 495
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-576 |
2.69e-70 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 234.41 E-value: 2.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILsTEDhqelmkaiavktsaqmsllpsvp 209
Cdd:cd05907 30 GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF-VED----------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 svstksteldhtingeldgtrclqeteipheisGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFL 289
Cdd:cd05907 86 ---------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 290 HCLPLHHVHGLFNALLAPLYAGSTVEFMPkfSVRGIWQRWRESYPqdqtkaddavTVFTGVPTMYTRLIQGYEAMD-PAL 368
Cdd:cd05907 133 SFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRP----------TVFLAVPRVWEKVYAAIKVKAvPGL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 369 QTASATAAR--QLRLMMCGSSALPLPVMQKWETItGHVLLERYGMTEF--VMAISNPlkGKRKGGTVGKPLPGVQAKiIA 444
Cdd:cd05907 201 KRKLFDLAVggRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETsaVVTLNPP--GDNRIGTVGKPLPGVEVR-IA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 445 EDgscdnvevGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKV-GGYKLSALEIE 523
Cdd:cd05907 277 DD--------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK-DLIITsGGKNISPEPIE 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 747052525 524 AVLLEHPTISECCVLGlPDKDYgeaVCAIIIPNPEIKRK-REEELKPALTLEEL 576
Cdd:cd05907 348 NALKASPLISQAVVIG-DGRPF---LVALIVPDPEALEAwAEEHGIAYTDVAEL 397
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
96-614 |
2.38e-69 |
|
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: 231.07 E-value: 2.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 96 SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMND 175
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRK-----------GDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 176 SDITMILSTEDhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheisgdDPALIIYTSGT 255
Cdd:cd05972 71 AGAKAIVTDAE----------------------------------------------------------DPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 256 TGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTV--EFMPKFSVRgIWQRWRESY 333
Cdd:cd05972 93 TGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVfvYEGPRFDAE-RILELLERY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 334 PqdqtkaddaVTVFTGVPTMYTRLIQgyeamdpalQTASATAARQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTE 413
Cdd:cd05972 172 G---------VTSFCGPPTAYRMLIK---------QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 414 FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIK--SPSLFKEYWNLPEVTKQSFIdGGFFKTGDA 490
Cdd:cd05972 234 TGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGReLPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 491 ARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikRKREEELKPA 570
Cdd:cd05972 313 AYRDEDGYFWFVGR-ADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVV------LTSGYEPSEE 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 747052525 571 LTlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05972 386 LA-EELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
130-537 |
4.02e-69 |
|
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: 229.84 E-value: 4.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMkaiavktsAQMSLLPSVP 209
Cdd:TIGR01733 25 GDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRL--------AGLVLPVILL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTksteldhtingELDGTRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFL 289
Cdd:TIGR01733 97 DPLE-----------LAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 290 HCLPLHHVHGLFnALLAPLYAGSTVEFMPKFSVR---GIWQRWRESYPqdqtkaddaVTVFTGVPTMYTRLIqgyEAMDP 366
Cdd:TIGR01733 166 QFASLSFDASVE-EIFGALLAGATLVVPPEDEERddaALLAALIAEHP---------VTVLNLTPSLLALLA---AALPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 367 ALQTasataarqLRLMMCGSSALPLPVMQKWETITGHV-LLERYGMTE---FVMAISNPLKGKRKGGTV--GKPLPGVQA 440
Cdd:TIGR01733 233 ALAS--------LRLVILGGEALTPALVDRWRARGPGArLINLYGPTEttvWSTATLVDPDDAPRESPVpiGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 441 KIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF--------FKTGDAARVDEDGYYVILGRTNADImK 511
Cdd:TIGR01733 305 YVLDDDLRpVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLGRIDDQV-K 383
|
410 420
....*....|....*....|....*.
gi 747052525 512 VGGYKLSALEIEAVLLEHPTISECCV 537
Cdd:TIGR01733 384 IRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
240-614 |
1.22e-67 |
|
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: 226.07 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPK 319
Cdd:cd05912 73 DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGIWQRWRESypqdqtkaddAVTVFTGVPTMYTRLIQGYEAMDPAlqtasataarQLRLMMCGSSALPLPVMQKWET 399
Cdd:cd05912 152 FDAEQVLHLINSG----------KVTIISVVPTMLQRLLEILGEGYPN----------NLRCILLGGGPAPKPLLEQCKE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 iTGHVLLERYGMTEFVMAIS--NPLKGKRKGGTVGKPLPGVQAKIiaEDGSCDNVEVGELCIKSPSLFKEYWNLPEVTKQ 477
Cdd:cd05912 212 -KGIPVYQSYGMTETCSQIVtlSPEDALNKIGSAGKPLFPVELKI--EDDGQPPYEVGEILLKGPNVTKGYLNRPDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 SFIDGgFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNP 557
Cdd:cd05912 289 SFENG-WFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 558 EIkrkreeelkpalTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05912 367 PI------------SEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
83-618 |
5.20e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 227.51 E-value: 5.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKK-----------GDRVAALGHNSDAYALLWLACARAGAVHVPVNF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILsTEDhqelmkAIAVKTSAQMSLLPSVPSVSTKSTELDHTINGELDGTRCLQETEIPH--- 239
Cdd:PRK08316 94 MLTGEELAYILDHSGARAFL-VDP------ALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEpdv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQ-VQMLTDAwGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP 318
Cdd:PRK08316 167 ELADDDLAQILYTSGTESLPKGAMLTHRALIAEyVSCIVAG-DMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQgyeamDPALQTASATAarqLRLMMCGSSALPLPVMQKwe 398
Cdd:PRK08316 246 APDPELILR----------TIEAERITSFFAPPTVWISLLR-----HPDFDTRDLSS---LRKGYYGASIMPVEVLKE-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 titghvLLER---------YGMTEfvMA----ISNPLKGKRKGGTVGKPLPGVQAKIIAEDGScdNV---EVGELCIKSP 462
Cdd:PRK08316 306 ------LRERlpglrfyncYGQTE--IAplatVLGPEEHLRRPGSAGRPVLNVETRVVDDDGN--DVapgEVGEIVHRSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 463 SLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPD 542
Cdd:PRK08316 376 QLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPD 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 543 KDYGEAVCAIIIPnpeikrkREEElkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK08316 454 PKWIEAVTAVVVP-------KAGA---TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
133-612 |
1.92e-66 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 225.58 E-value: 1.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSaqmsLLPSVPSVS 212
Cdd:cd05904 60 VLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVV----LLDSAEFDS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 TKSTELDHtingELDGTRCLQEteiphEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDH--FLH 290
Cdd:cd05904 136 LSFSDLLF----EADEAEPPVV-----VIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEdvFLC 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 291 CLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRG---IWQRWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPA 367
Cdd:cd05904 207 VLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEEllaAIERYK-------------VTHLPVVPPIVLALVKSPIVDKYD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 368 LqtasataaRQLRLMMCGSSALPLPVMQKWETITGHV-LLERYGMTE---FVMAISNPLKGKRKGGTVGKPLPGVQAKII 443
Cdd:cd05904 274 L--------SSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 444 -AEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALE 521
Cdd:cd05904 346 dPETGESLPPnQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLK-ELIKYKGFQVAPAE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 522 IEAVLLEHPTISECCVLGLPDKDYGEavcaiiIPNPEIKRKREEELKPaltlEELSMWAKEKLAPYKIPNCLLLWESLPR 601
Cdd:cd05904 425 LEALLLSHPEILDAAVIPYPDEEAGE------VPMAFVVRKPGSSLTE----DEIMDFVAKQVAPYKKVRKVAFVDAIPK 494
|
490
....*....|.
gi 747052525 602 NAMGKVNKKEL 612
Cdd:cd05904 495 SPSGKILRKEL 505
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
78-616 |
3.55e-66 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 224.46 E-value: 3.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 78 RGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVA 157
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKK-----------GDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 158 VPLALSYPEAELLHVMNDSDITMILsTEDhqELMKAIAVKTSAQMSLLPSVPsvstksteldhtingeldgtrcLQETEI 237
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLI-TDD--DFEAKLIPGISVKFAELMNGP----------------------KEEAEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 PHEISGDDPALIIYTSGTTGKPKGVVHTHK-----GVLAQVQMltdawGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGS 312
Cdd:PRK03640 135 QEEFDLDEVATIMYTSGTTGKPKGVIQTYGnhwwsAVGSALNL-----GLTEDDCWLAAVPIFHISGL-SILMRSVIYGM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 313 TVEFMPKFSVRGIwqrwresypqDQTKADDAVTVFTGVPTMYTRLIQgyeamdpalQTASATAARQLRLMMCGSSALPLP 392
Cdd:PRK03640 209 RVVLVEKFDAEKI----------NKLLQTGGVTIISVVSTMLQRLLE---------RLGEGTYPSSFRCMLLGGGPAPKP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 393 VMQKWETiTGHVLLERYGMTEFVMAIS--NPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNVEVGELCIKSPSLFKEYWN 470
Cdd:PRK03640 270 LLEQCKE-KGIPVYQSYGMTETASQIVtlSPEDALTKLGSAGKPLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 471 LPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVC 550
Cdd:PRK03640 349 REDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 551 AIIIPNPEIkrkreeelkpalTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQL 616
Cdd:PRK03640 427 AFVVKSGEV------------TEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
130-617 |
9.30e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 225.31 E-value: 9.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAI----AVKTSAQMSL- 204
Cdd:PRK06178 83 GDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVraetSLRHVIVTSLa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 205 --LPSVPSVSTKSTELDHTI--NGELDGTRCLQETEIP---HEISGDDPALIIYTSGTTGKPKGVVHTHKgvlaqvQMLT 277
Cdd:PRK06178 163 dvLPAEPTLPLPDSLRAPRLaaAGAIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHTQR------DMVY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 278 DAWGYTSTDH-------FLHCLPLHHVHGLFNALLAPLYAGSTVEFMpkfsvrgiwQRWresypqdqtkadDAVTVFTGV 350
Cdd:PRK06178 237 TAAAAYAVAVvggedsvFLSFLPEFWIAGENFGLLFPLFSGATLVLL---------ARW------------DAVAFMAAV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 351 P----TMYTRLIQGY-EAMD-PAlqtASATAARQLRLMMCGSSALPL-PVM-QKWETITGHVLLE-RYGMTE------FV 415
Cdd:PRK06178 296 EryrvTRTVMLVDNAvELMDhPR---FAEYDLSSLRQVRVVSFVKKLnPDYrQRWRALTGSVLAEaAWGMTEthtcdtFT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 416 MAI--------SNPLkgkrkggTVGKPLPGVQAKIiaedgsCDNV--------EVGELCIKSPSLFKEYWNLPEVTKQSF 479
Cdd:PRK06178 373 AGFqdddfdllSQPV-------FVGLPVPGTEFKI------CDFEtgellplgAEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 480 IDgGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEi 559
Cdd:PRK06178 440 RD-GWLHTGDIGKIDEQGFLHYLGR-RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG- 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 560 krkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLwESLPRNAMGKVNKKELKKQLA 617
Cdd:PRK06178 517 ---------ADLTAAALQAWCRENMAVYKVPEIRIV-DALPMTATGKVRKQDLQALAE 564
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
130-615 |
2.34e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 223.89 E-value: 2.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILsTEDHQELMkAIAVKTSaqmsllpsVP 209
Cdd:PRK07786 67 GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV-TEAALAPV-ATAVRDI--------VP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTINGELDGTRCLQETEIPH---EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGY-TST 285
Cdd:PRK07786 137 LLSTVVVAGGSSDDSVLGYEDLLAEAGPAHapvDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 286 DHFLHCLPLHHVHGLFNALLAPLYAGSTV-----EFMPKFSVrgiwqrwresypqDQTKADDAVTVFTgVPTMYTrliqg 360
Cdd:PRK07786 217 DVGFVGVPLFHIAGIGSMLPGLLLGAPTViyplgAFDPGQLL-------------DVLEAEKVTGIFL-VPAQWQ----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 361 yeamdpALQTASATAARQLRLMMCGSSALPLP---VMQKWETITGHVLLERYGMTEfvMA-ISNPLKGK---RKGGTVGK 433
Cdd:PRK07786 278 ------AVCAEQQARPRDLALRVLSWGAAPASdtlLRQMAATFPEAQILAAFGQTE--MSpVTCMLLGEdaiRKLGSVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 434 PLPGVQAKIIAEDgsCDNV---EVGELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIM 510
Cdd:PRK07786 350 VIPTVAARVVDEN--MNDVpvgEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKK-DMI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 511 KVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelKPALTLEELSMWAKEKLAPYKIP 590
Cdd:PRK07786 426 ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---------DAALTLEDLAEFLTDRLARYKHP 496
|
490 500
....*....|....*....|....*
gi 747052525 591 NCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK07786 497 KALEIVDALPRNPAGKVLKTELRER 521
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
87-613 |
7.64e-63 |
|
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: 214.26 E-value: 7.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 87 AVTAHEKSHSYHQLILSAVKISNLLTGAdLRSVKGNgenkhlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPE 166
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGE-LGIVPGN---------RVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 167 AELLHVMNDSDITMILstedhqelmkaiavktsaqmsllpsvpsvstksteLDHtingeldgtrclQETeipheiSGDDP 246
Cdd:cd05958 73 KELAYILDKARITVAL-----------------------------------CAH------------ALT------ASDDI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 247 ALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT-DAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPkfsvrgi 325
Cdd:cd05958 100 CILAFTSGTTGAPKATMHFHRDPLASADRYAvNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 326 wqrwrESYPQD--QTKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGH 403
Cdd:cd05958 173 -----EATPDLllSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSS--------LRKCVSAGEALPAALHRAWKEATGI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTE-FVMAISNPlKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKSPSLfkeYWNLPEVTKQSFID 481
Cdd:cd05958 240 PIIDGIGSTEmFHIFISAR-PGDARPGATGKPVPGYEAKVVDDEGnPVPDGTIGRLAVRGPTG---CRYLADKRQRTYVQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkr 561
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV-- 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 747052525 562 kreeeLKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05958 393 -----IPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
130-615 |
2.21e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 215.24 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLalsYPEAEL---LHVMNDSDITMILStEDHQELMKAIAVKTSAqmsllP 206
Cdd:PRK06188 62 GDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLGSLddhAYVLEDAGISTLIV-DPAPFVERALALLARV-----P 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 207 SVPSV-STKSTELDHTINGELD--GTRCLQETEIPheisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYT 283
Cdd:PRK06188 133 SLKHVlTLGPVPDGVDLLAAAAkfGPAPLVAAALP-----PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 284 STDHFLHCLPLHHVHGLFnaLLAPLYAGSTVEFMPKFSvrgiwqrwresyPQD--QTKADDAVTVFTGVPTMYTRLiqgy 361
Cdd:PRK06188 208 ADPRFLMCTPLSHAGGAF--FLPTLLRGGTVIVLAKFD------------PAEvlRAIEEQRITATFLVPTMIYAL---- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 362 eaMD-PALQTASATAarqLRLMMCGSSAL-PLPVMQKWETItGHVLLERYGMTEFVMAIS------NPLKGKRKGGTVGK 433
Cdd:PRK06188 270 --LDhPDLRTRDLSS---LETVYYGASPMsPVRLAEAIERF-GPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 434 PLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKV 512
Cdd:PRK06188 344 PTPGLRVALLDEDGReVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKK-DMIVT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 513 GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRkreeelkpalTLEELSMWAKEKLAPYKIPNC 592
Cdd:PRK06188 422 GGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAV----------DAAELQAHVKERKGSVHAPKQ 491
|
490 500
....*....|....*....|...
gi 747052525 593 LLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK06188 492 VDFVDSLPLTALGKPDKKALRAR 514
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
130-613 |
8.49e-62 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 213.39 E-value: 8.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFvagvLGTWFS----GGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQmslL 205
Cdd:PRK08008 62 GDKVALHLDNCPEF----IFCWFGlakiGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATP---L 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 206 PSVPSVSTKSTELDHTINgeLDGTRCLQETEIPHE--ISGDDPALIIYTSGTTGKPKGVVHTHKGVLaqVQMLTDAW--G 281
Cdd:PRK08008 135 RHICLTRVALPADDGVSS--FTQLKAQQPATLCYAppLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 282 YTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWREsYpqdqtKAddavTVFTGVPTMYTRLIqgy 361
Cdd:PRK08008 211 LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCK-Y-----RA----TITECIPMMIRTLM--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 362 eamdpaLQTASATaARQ--LRLMMcgsSALPLPVMQK--WETITGHVLLERYGMTE-FVMAISNPLKGKRKGGTVGKPLP 436
Cdd:PRK08008 278 ------VQPPSAN-DRQhcLREVM---FYLNLSDQEKdaFEERFGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 437 GVQAKIIAEDG-SCDNVEVGELCIK---SPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGY-YVILGRTNadIMK 511
Cdd:PRK08008 348 CYEAEIRDDHNrPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFfYFVDRRCN--MIK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 512 VGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKrkreeelkpaLTLEELSMWAKEKLAPYKIPN 591
Cdd:PRK08008 426 RGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET----------LSEEEFFAFCEQNMAKFKVPS 495
|
490 500
....*....|....*....|..
gi 747052525 592 CLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK08008 496 YLEIRKDLPRNCSGKIIKKNLK 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
241-613 |
1.11e-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: 211.17 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQML-TDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPK 319
Cdd:cd05919 88 TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 fsvrgiwqrWRESYPQDQTKADDAVTVFTGVPTMYTRLIqgyeamdpALQTASATAARQLRLMMCGSSALPLPVMQKWET 399
Cdd:cd05919 168 ---------WPTAERVLATLARFRPTVLYGVPTFYANLL--------DSCAGSPDALRSLRLCVSAGEALPRGLGERWME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKSPSLFKEYWNLPEVTKQS 478
Cdd:cd05919 231 HFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGhTIPPGEEGDLLVRGPSAAVGYWNNPEKSRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPe 558
Cdd:cd05919 311 F-NGGWYRTGDKFCRDADGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS- 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 559 ikrkreeELKPALTL-EELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05919 388 -------PAAPQESLaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
76-612 |
1.58e-61 |
|
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: 212.19 E-value: 1.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 76 ANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLtgadlrSVKGNGEnkhlgGARVGIVAKPSPEFVAGVLGTWFSGG 155
Cdd:cd17655 4 EEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTL------REKGVGP-----DTIVGIMAERSLEMIVGILGILKAGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 156 VAVPLALSYPEAELLHVMNDSDITMILSTEDHQElmkaiavktsaqmsllpsvpsvstKSTELDHTINGELDGTRCLQET 235
Cdd:cd17655 73 AYLPIDPDYPEERIQYILEDSGADILLTQSHLQP------------------------PIAFIGLIDLLDEDTIYHEESE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 236 EIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglFNA----LLAPLYAG 311
Cdd:cd17655 129 NLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS-----FDAsvteIFASLLSG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 312 STVEFMPKFSVRGIwQRWRESYPQDQtkaddaVTVFTGVPTmytrLIQGYEAMDpalqtasATAARQLRLMMCGSSALPL 391
Cdd:cd17655 204 NTLYIVRKETVLDG-QALTQYIRQNR------ITIIDLTPA----HLKLLDAAD-------DSEGLSLKHLIVGGEALST 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 392 PVMQKWETITGH--VLLERYGMTEFVM--AISNPLKGKRKGGTV--GKPLPGVQAKIIAEDGSCDNVEV-GELCIKSPSL 464
Cdd:cd17655 266 ELAKKIIELFGTnpTITNAYGPTETTVdaSIYQYEPETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVaGELYIGGEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 465 FKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:cd17655 346 ARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQV-KIRGYRIELGEIEARLLQHPDIKEAVVI 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 539 GLPDKDYGEAVCAIIIPNPEikrkreeelkpaLTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17655 425 ARKDEQGQNYLCAYIVSEKE------------LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
208-614 |
3.10e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 214.82 E-value: 3.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 208 VPSVSTKSTELDHTINGELDGTRClQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDH 287
Cdd:PRK07529 178 VPLIRRKAHARILDFDAELARQPG-DRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 288 FLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRG------IW---QRWResypqdqtkaddaVTVFTGVPTMYTRLI 358
Cdd:PRK07529 257 VFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGpgvianFWkivERYR-------------INFLSGVPTVYAALL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 359 Q-GYEAMDpalqTASataarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAIS-NPLKGKRKGGTVGKPLP 436
Cdd:PRK07529 324 QvPVDGHD----ISS------LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSvNPPDGERRIGSVGLRLP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 437 GVQAKIIAEDGS------CDNVEVGELCIKSPSLFKEYWNlPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIM 510
Cdd:PRK07529 394 YQRVRVVILDDAgrylrdCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLII 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 511 KvGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIipnpeikrkreeELKP--ALTLEELSMWAKEKLA-PY 587
Cdd:PRK07529 473 R-GGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV------------QLKPgaSATEAELLAFARDHIAeRA 539
|
410 420
....*....|....*....|....*..
gi 747052525 588 KIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:PRK07529 540 AVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
243-614 |
1.27e-60 |
|
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: 205.79 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSV 322
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RG------IW---QRWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPAlqtasataarQLRLMMCGSSALPLPV 393
Cdd:cd05944 81 RNpglfdnFWklvERYR-------------ITSLSTVPTVYAALLQVPVNADIS----------SLRFAMSGAAPLPVEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEFVMAIS-NPLKGKRKGGTVGKPLPGVQAKIIAEDGS------CDNVEVGELCIKSPSLFK 466
Cdd:cd05944 138 RARFEDATGLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrdCAPDEVGEICVAGPGVFG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 467 EYWNlPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYG 546
Cdd:cd05944 218 GYLY-TEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAK-DLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747052525 547 EAVCAIIipnpeikrkreeELKP--ALTLEELSMWAKEKLAPY-KIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05944 296 ELPVAYV------------QLKPgaVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
132-614 |
6.04e-60 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 208.15 E-value: 6.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 132 RVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEdhqelmkaiavktsaqmSLLPSVPSV 211
Cdd:TIGR02262 57 RVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG-----------------ALLPVIKAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 212 STKSTELDHTI------NGELDGTRCL---QETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT-DAWG 281
Cdd:TIGR02262 120 LGKSPHLEHRVvvgrpeAGEVQLAELLateSEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYArNTLG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 282 YTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP-KFSVRGIWQRWRESYPqdqtkaddavTVFTGVPTMYTRLIQg 360
Cdd:TIGR02262 200 IREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGeRPTPDAVFDRLRRHQP----------TIFYGVPTLYAAMLA- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 361 yeamDPALQTasataARQLRLMMCGSSALPLP--VMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGV 438
Cdd:TIGR02262 269 ----DPNLPS-----EDQVRLRLCTSAGEALPaeVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 439 QAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIdGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKL 517
Cdd:TIGR02262 340 RLRLVGDGGQdVADGEPGELLISGPSSATMYWNNRAKSRDTFQ-GEWTRSGDKYVRNDDGSYTYAGRTD-DMLKVSGIYV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 518 SALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkREEELKpaltlEELSMWAKEKLAPYKIPNCLLLWE 597
Cdd:TIGR02262 418 SPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRP-----GQTALE-----TELKEHVKDRLAPYKYPRWIVFVD 487
|
490
....*....|....*..
gi 747052525 598 SLPRNAMGKVNKKELKK 614
Cdd:TIGR02262 488 DLPKTATGKIQRFKLRE 504
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-613 |
1.16e-59 |
|
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: 205.81 E-value: 1.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 95 HSYHQLILSAVKISNLLtgadlrsvKGNGENKhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL--------KSLGVGK---GDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 175 DSDITMILSTEDHQELMkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheiSGDDPALIIYTSG 254
Cdd:cd05969 70 NSEAKVLITTEELYERT--------------------------------------------------DPEDPTLLHYTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 255 TTGKPKGVVHTHKGVLAQVQmlTDAW--GYTSTDHFLHCLPLHHVHGLFNALLAPLYAGST-VEFMPKFSVRgiwqRWRE 331
Cdd:cd05969 100 TTGTPKGVLHVHDAMIFYYF--TGKYvlDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTnVVYEGRFDAE----SWYG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 332 sypqdqTKADDAVTVFTGVPTMYTRLiqgyeaMDPALQTASATAARQLRLMMCGSSALPlPVMQKW-ETITGHVLLERYG 410
Cdd:cd05969 174 ------IIERVKVTVWYTAPTAIRML------MKEGDELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWW 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 411 MTEF-VMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKS--PSLFKEYWNLPEVTKQSFIDGgFFK 486
Cdd:cd05969 241 QTETgSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNeLPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG-WYL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 487 TGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKreEE 566
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPS--DE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 747052525 567 LKpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05969 397 LK-----EEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
68-620 |
3.11e-59 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 207.05 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRGSISPeSIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGV 147
Cdd:PRK05852 18 IADLVEVAATRLPEAP-ALVVTADRIAISYRDLARLVDDLAGQLTRSGLLP-----------GDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMN--DSDITMILSTEDHQELMKA-----IAVKTSAQMSLLPSVPSVSTKSTELDH 220
Cdd:PRK05852 86 LAASRADLVVVPLDPALPIAEQRVRSQaaGARVVLIDADGPHDRAEPTtrwwpLTVNVGGDSGPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 221 TINGELDGTRclqeteipheisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGL 300
Cdd:PRK05852 166 PATSTPEGLR-------------PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 301 FNALLAPLYAGSTVeFMP---KFSVRGIWqrwresypqDQTKADDAvTVFTGVPTMYTRLIQgyeamDPALQTASATAAr 377
Cdd:PRK05852 233 IAALLATLASGGAV-LLPargRFSAHTFW---------DDIKAVGA-TWYTAVPTIHQILLE-----RAATEPSGRKPA- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 378 QLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFV-MAISNPLKGKRKG-------GTVGKPlPGVQAKIIAEDG-S 448
Cdd:PRK05852 296 ALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThQVTTTQIEGIGQTenpvvstGLVGRS-TGAQIRIVGSDGlP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 449 CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLE 528
Cdd:PRK05852 375 LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLAS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 529 HPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVN 608
Cdd:PRK05852 453 HPNVMEAAVFGVPDQLYGEAVAAVIVPRESA----------PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
|
570
....*....|..
gi 747052525 609 KKELKKQLADQV 620
Cdd:PRK05852 523 RRAVAEQFGHSV 534
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
244-613 |
5.25e-59 |
|
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: 201.35 E-value: 5.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFM-PKFSV 322
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQgyEAMDPALQTASataarqLRLMMCGSSALPLPVMQKwetitg 402
Cdd:cd05917 82 LAVLE----------AIEKEKCTALHGVPTMFIAELE--HPDFDKFDLSS------LRTGIMAGAPCPPELMKR------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 403 hvLLER---------YGMTEF--VMAISNPLKG-KRKGGTVGKPLPGVQAKIIAEDGSCDNV--EVGELCIKSPSLFKEY 468
Cdd:cd05917 138 --VIEVmnmkdvtiaYGMTETspVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVPPvgVPGELCIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 469 WNLPEVTKQSfIDG-GFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:cd05917 216 WNDPEKTAEA-IDGdGWLHTGDLAVMDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGE 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 548 AVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05917 294 EVCAWIRLKEG----------AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
68-615 |
7.45e-59 |
|
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: 205.79 E-value: 7.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRGsisPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGV 147
Cdd:TIGR03098 2 LHHLLEDAAARL---PDATALVHHDRTLTYAALSERVLALASGLRGLGLAR-----------GERVAIYLDKRLETVTAM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDH-----------QELMKAIAVKTSAQMSLLPSVPSVSTkst 216
Cdd:TIGR03098 68 FGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERldllhpalpgcHDLRTLIIVGDPAHASEGHPGEEPAS--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 217 eldhtingeLDGTRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHH 296
Cdd:TIGR03098 145 ---------WPKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 297 VHGlFNALLAPLYAGSTVEFMpkfsvrgiwqrwreSY--PQDQTKA--DDAVTVFTGVPTMYTRLIQgyeamdpaLQTaS 372
Cdd:TIGR03098 216 DYG-FNQLTTAFYVGATVVLH--------------DYllPRDVLKAleKHGITGLAAVPPLWAQLAQ--------LDW-P 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 373 ATAARQLRLMMCGSSALPLPVMQKWETITGHV-LLERYGMTE-FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS-C 449
Cdd:TIGR03098 272 ESAAPSLRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGLTEaFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSeC 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 450 DNVEVGELCIKSPSLFKEYWNLPEVTKQSF-----------IDGGFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLS 518
Cdd:TIGR03098 352 APGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpgelhLPELAVWSGDTVRRDEEGFLYFVGRRDEMI-KTSGYRVS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 519 ALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkrEEELKPALTLEELsmwaKEKLAPYKIPNCLLLWES 598
Cdd:TIGR03098 431 PTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPG------GEELDRAALLAEC----RARLPNYMVPALIHVRQA 500
|
570
....*....|....*..
gi 747052525 599 LPRNAMGKVNKKELKKQ 615
Cdd:TIGR03098 501 LPRNANGKIDRKALAKE 517
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
245-609 |
8.65e-59 |
|
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: 200.19 E-value: 8.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPKFSvrg 324
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 iwqrwresyPQDQTK--ADDAVTVFTGVPTMYTRLIQGYEAMDPALqtasataaRQLRLMmcgsSALPLP-VMQKWETIT 401
Cdd:cd17637 77 ---------PAEALEliEEEKVTLMGSFPPILSNLLDAAEKSGVDL--------SSLRHV----LGLDAPeTIQRFEETT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 GHVLLERYGMTEFVMAISNPlKGKRKGGTVGKPLPGVQAKIIAEDGscDNV---EVGELCIKSPSLFKEYWNLPEVTKQS 478
Cdd:cd17637 136 GATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDND--RPVpagETGEIVVRGPLVFQGYWNLPELTAYT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FiDGGFFKTGDAARVDEDGYYVILGRTNA-DIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNP 557
Cdd:cd17637 213 F-RNGWHHTGDLGRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 747052525 558 eikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNK 609
Cdd:cd17637 292 ----------GATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
245-616 |
2.46e-58 |
|
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: 198.71 E-value: 2.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFnALLAPLYAGSTVEFMPKfsvrg 324
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLER----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 iwqRWresyPQDQTKADDAVTVFTGVPTMYTRLIQgyeamDPALQTASATaarqLRLMMCGSSALPLPVMQK-----WET 399
Cdd:cd17630 75 ---NQ----ALAEDLAPPGVTHVSLVPTQLQRLLD-----SGQGPAALKS----LRAVLLGGAPIPPELLERaadrgIPL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGhvllerYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIiaedgscdnVEVGELCIKSPSLFKEYWNLPEVtkQSF 479
Cdd:cd17630 139 YTT------YGMTETASQVATKRPDGFGRGGVGVLLPGRELRI---------VEDGEIWVGGASLAMGYLRGQLV--PEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 480 IDGGFFKTGDAARVDEDGYYVILGRtnADIMKV-GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPE 558
Cdd:cd17630 202 NEDGWFTTKDLGELHADGRLTVLGR--ADNMIIsGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 559 IkrkreeelkpalTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQL 616
Cdd:cd17630 280 A------------DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
130-612 |
4.18e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 204.88 E-value: 4.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTE-------DHQELMKAIAVKTSAQM 202
Cdd:PRK06710 74 GDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDlvfprvtNVQSATKIEHVIVTRIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 203 SLLPS-----VPSVSTKSTEL------DHTIN------GELD-GTRCLQETEipheisgDDPALIIYTSGTTGKPKGVVH 264
Cdd:PRK06710 154 DFLPFpknllYPFVQKKQSNLvvkvseSETIHlwnsveKEVNtGVEVPCDPE-------NDLALLQYTGGTTGFPKGVML 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 265 THKGVLAQVQMLTDaWGYTSTDH---FLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWRESypqdqtkad 341
Cdd:PRK06710 227 THKNLVSNTLMGVQ-WLYNCKEGeevVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKH--------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 342 dAVTVFTGVPTMYTRLIQgyeamDPALQTASATAarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFV-MAISN 420
Cdd:PRK06710 297 -KVTLFPGAPTIYIALLN-----SPLLKEYDISS---IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 PLKGKRKGGTVGKPLPGVQAKIIA-EDGSC-DNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDgGFFKTGDAARVDEDGY 498
Cdd:PRK06710 368 FLWEKRVPGSIGVPWPDTEAMIMSlETGEAlPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGF 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 499 YVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikRKREEELKPaltlEELSM 578
Cdd:PRK06710 447 FYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV------LKEGTECSE----EELNQ 515
|
490 500 510
....*....|....*....|....*....|....
gi 747052525 579 WAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:PRK06710 516 FARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
82-617 |
1.68e-57 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 202.67 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVT-AHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPL 160
Cdd:PRK06087 36 MPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEP-----------GDRVAFQLPGWCEFTIIYLACLKVGAVSVPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 161 ALSYPEAELLHVMNDSDITMILS-----TEDHQELMKAIA--VKTSAQMSLL----PSVPSVStksteLDHTINgelDGT 229
Cdd:PRK06087 105 LPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQnqLPQLQQIVGVdklaPATSSLS-----LSQIIA---DYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 230 RClqETEIPheISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLY 309
Cdd:PRK06087 177 PL--TTAIT--THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 310 AGSTVEFMPKF-SVRGIWQRWRESypqdqtkaddaVTVFTG-VPTMYTrLIQGYEAMDPALQTasataarqLRLMMCGSS 387
Cdd:PRK06087 253 IGARSVLLDIFtPDACLALLEQQR-----------CTCMLGaTPFIYD-LLNLLEKQPADLSA--------LRFFLCGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 388 ALPLPVMQK-WETitGHVLLERYGMTEFV-MAISNPLKG-KRKGGTVGKPLPGVQAKIIAED------GscdnvEVGELC 458
Cdd:PRK06087 313 TIPKKVAREcQQR--GIKLLSVYGSTESSpHAVVNLDDPlSRFMHTDGYAAAGVEIKVVDEArktlppG-----CEGEEA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:PRK06087 386 SRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 539 GLPDKDYGEAVCAIIIPNPEIKRkreeelkpaLTLEELSMW-AKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLA 617
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPHHS---------LTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIM 535
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
68-620 |
1.93e-57 |
|
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: 209.71 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRgsiSPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGV 147
Cdd:COG1020 478 LHELFEAQAAR---TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGP-----------GDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQElmkaiavktsaqmsllpSVPSVSTKSTELDHTINGELD 227
Cdd:COG1020 544 LAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAA-----------------RLPELGVPVLALDALALAAEP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 228 GTRclqeteIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHH---VHGLFNAL 304
Cdd:COG1020 607 ATN------PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWEIFGAL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 305 LaplyAGSTVEFMPKFSVRGI--WQRWRESYpqdqtkaddAVTVFTGVPTMYTRLIQgyeamdpalqtASATAARQLRLM 382
Cdd:COG1020 681 L----SGATLVLAPPEARRDPaaLAELLARH---------RVTVLNLTPSLLRALLD-----------AAPEALPSLRLV 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 383 MCGSSALPLPVMQKWETITGHV-LLERYGMTEF-VMAISNPL-KGKRKGGTV--GKPLPGVQAKIIAEDGS-C-DNVeVG 455
Cdd:COG1020 737 LVGGEALPPELVRRWRARLPGArLVNLYGPTETtVDSTYYEVtPPDADGGSVpiGRPIANTRVYVLDAHLQpVpVGV-PG 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 456 ELCIKSPSLFKEYWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRtNADIMKVGGYK--LSalEIEAVL 526
Cdd:COG1020 816 ELYIGGAGLARGYLNRPELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGR-ADDQVKIRGFRieLG--EIEAAL 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 527 LEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:COG1020 893 LQHPGVREAVVVAREDAPGDKRLVAYVVPEAG----------AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGK 962
|
570
....*....|....
gi 747052525 607 VNKKELKKQLADQV 620
Cdd:COG1020 963 LDRLALPAPAAAAA 976
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
70-609 |
3.18e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 199.23 E-value: 3.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 70 ELVKAVANRGSiSPESIAVTAHEKSHSYHQLILSAVKISnlltgadlRSVKGNGENKhlgGARVGIVAKPSPEFVAGVLG 149
Cdd:PRK12583 22 DAFDATVARFP-DREALVVRHQALRYTWRQLADAVDRLA--------RGLLALGVQP---GDRVGIWAPNCAEWLLTQFA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 150 TWFSGGVAVPLALSYPEAELLHVMNDSDITMILS-----TEDH----QELMKAIAVK-----TSAQMSLLPSVPSVSTKS 215
Cdd:PRK12583 90 TARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYhamlQELLPGLAEGqpgalACERLPELRGVVSLAPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 216 TE---LDHTINGELDGTRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCL 292
Cdd:PRK12583 170 PPgflAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 293 PLHHVHGLFNALLAPLYAGSTVefmpkfsvrgiwqrwreSYPQD--------QTKADDAVTVFTGVPTMYTRliqgyEAM 364
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGACL-----------------VYPNEafdplatlQAVEEERCTALYGVPTMFIA-----ELD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 365 DPALQTASATAarqLRLMMCGSSALPLPVMQKW--ETITGHVLLErYGMTE-----FVMAISNPLkgKRKGGTVGKPLPG 437
Cdd:PRK12583 308 HPQRGNFDLSS---LRTGIMAGAPCPIEVMRRVmdEMHMAEVQIA-YGMTEtspvsLQTTAADDL--ERRVETVGRTQPH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 438 VQAKIIAEDG-SCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYK 516
Cdd:PRK12583 382 LEVKVVDPDGaTVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSK-DMIIRGGEN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 517 LSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIipnpeikrkreeELKP--ALTLEELSMWAKEKLAPYKIPNCLL 594
Cdd:PRK12583 461 IYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWV------------RLHPghAASEEELREFCKARIAHFKVPRYFR 528
|
570
....*....|....*
gi 747052525 595 LWESLPRNAMGKVNK 609
Cdd:PRK12583 529 FVDEFPMTVTGKVQK 543
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
240-614 |
5.66e-56 |
|
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: 197.85 E-value: 5.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKG-VL-AQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVefm 317
Cdd:cd12119 159 DFDENTAAAICYTSGTTGNPKGVVYSHRSlVLhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLV--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 pkfsvrgiwqrwresYPQDQTKADDA--------VTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSAL 389
Cdd:cd12119 236 ---------------LPGPYLDPASLaelieregVTFAAGVPTVWQGLLDHLEANGRDLSS--------LRRVVIGGSAV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 390 PLPVMQKWE-----TITGhvllerYGMTEF--VMAISNPLKGKRKGG---------TVGKPLPGVQAKIIAEDGSC---D 450
Cdd:cd12119 293 PRSLIEAFEergvrVIHA------WGMTETspLGTVARPPSEHSNLSedeqlalraKQGRPVPGVELRIVDDDGRElpwD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 451 NVEVGELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHP 530
Cdd:cd12119 367 GKAVGELQVRGPWVTKSYYKNDEESEALT-EDGWLRTGDVATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHP 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 531 TISECCVLGLPDKDYGEAVCAIIIPnpeikrkREEElkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKK 610
Cdd:cd12119 445 AVAEAAVIGVPHPKWGERPLAVVVL-------KEGA---TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKK 514
|
....
gi 747052525 611 ELKK 614
Cdd:cd12119 515 ALRE 518
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
83-612 |
1.67e-55 |
|
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: 194.77 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDA-----------GDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheis 242
Cdd:cd05945 74 SSPAERIREILDAAKPALLIAD---------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQV-QMLTDAwGYTSTDHFLHCLPLH---HVHGLFNALLaplyAGSTVEFMP 318
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTnWMLSDF-PLGPGDVFLNQAPFSfdlSVMDLYPALA----SGATLVPVP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KfSVRGIWQRWRESYPQDQtkaddaVTVFTGVPTMYTRLIqgyeaMDPALQTASATAARQlrLMMCGsSALPLPVMQKWE 398
Cdd:cd05945 171 R-DATADPKQLFRFLAEHG------ITVWVSTPSFAAMCL-----LSPTFTPESLPSLRH--FLFCG-EVLPHKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 TIT-GHVLLERYGMTEFVMA-----ISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNL 471
Cdd:cd05945 236 QRFpDARIYNTYGPTEATVAvtyieVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPgEKGELVISGPSVSKGYLNN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 472 PEVTKQSF--IDG-GFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEA 548
Cdd:cd05945 316 PEKTAAAFfpDEGqRAYRTGDLVRLEADGLLFYRGRLDFQV-KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTE 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 549 VCAIIIPNPEIKRKREEELKpaltlEELsmwaKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd05945 395 LIAFVVPKPGAEAGLTKAIK-----AEL----AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
70-612 |
4.18e-54 |
|
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: 191.65 E-value: 4.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 70 ELVKAVANRgsiSPESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvKGNGEnkhlgGARVGIVAKPSPEFVAGVLG 149
Cdd:cd12117 1 ELFEEQAAR---TPDAVAVVYGDRSLTYAELNERANRLARRLRA------AGVGP-----GDVVGVLAERSPELVVALLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 150 TWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEdhqelmkaiavkTSAQMSLLPSVPSVStksteldhtingeLDGT 229
Cdd:cd12117 67 VLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDR------------SLAGRAGGLEVAVVI-------------DEAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 230 RCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAWGYTSTDHFLHCLPLHhvhglFNA----LL 305
Cdd:cd12117 122 DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLA-----FDAstfeIW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 APLYAGSTVEFMPKfsvrgiwqrwreSYPQDQTKADDAVTVfTGVPTMY--TRLIQGYEAMDPAlqtasatAARQLRLMM 383
Cdd:cd12117 196 GALLNGARLVLAPK------------GTLLDPDALGALIAE-EGVTVLWltAALFNQLADEDPE-------CFAGLRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPLPVMQKW-ETITGHVLLERYGMTE-------FVMAisnplKGKRKGGTV--GKPLPGVQAKIIAEDGS-CDNV 452
Cdd:cd12117 256 TGGEVVSPPHVRRVlAACPGLRLVNGYGPTEnttfttsHVVT-----ELDEVAGSIpiGRPIANTRVYVLDEDGRpVPPG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVL 526
Cdd:cd12117 331 VPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRID-DQVKIRGFRIELGEIEAAL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 527 LEHPTISECCVLGLPDKDYGEAVCAIIIPnpeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:cd12117 410 RAHPGVREAVVVVREDAGGDKRLVAYVVA------------EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGK 477
|
....*.
gi 747052525 607 VNKKEL 612
Cdd:cd12117 478 VDRRAL 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
238-613 |
5.51e-54 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 193.50 E-value: 5.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDH----------FLHCLPLHHVHGLFNALLAP 307
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGqplmkegqevMIAPLPLYHIYAFTANCMCM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 308 LYAGS-TVEFMPKFSVRGI---WQRWResypqdqtkaddaVTVFTGVPTMYTRLiqgyeaMD-PALQTASATAarqLRLM 382
Cdd:PRK12492 281 MVSGNhNVLITNPRDIPGFikeLGKWR-------------FSALLGLNTLFVAL------MDhPGFKDLDFSA---LKLT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 383 MCGSSALPLPVMQKWETITGHVLLERYGMTEFV-MAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIK 460
Cdd:PRK12492 339 NSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLgERGELCIK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGL 540
Cdd:PRK12492 419 GPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGV 497
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 541 PDKDYGEAVCAIIIPnpeikrkREeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK12492 498 PDERSGEAVKLFVVA-------RD----PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
70-612 |
6.98e-54 |
|
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: 191.33 E-value: 6.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 70 ELVKAVANRGsisPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLG 149
Cdd:cd17646 2 ALVAEQAART---PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGP-----------EDRVAVLLPRSADLVVALLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 150 TWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDhqelmkaiavktsaqmslLPSVPSVSTKSTELDHTINGELDGT 229
Cdd:cd17646 68 VLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTAD------------------LAARLPAGGDVALLGDEALAAPPAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 230 RCLQETEipheisGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglF----NALL 305
Cdd:cd17646 130 PPLVPPR------PDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLS-----FdvsvWELF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 APLYAGSTVEFM-------PKFSVRGIwqrwresypqdqtkADDAVTVFTGVPTMytrliqgyeaMDPALQTASATAARQ 378
Cdd:cd17646 199 WPLVAGARLVVArpgghrdPAYLAALI--------------REHGVTTCHFVPSM----------LRVFLAEPAAGSCAS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 379 LRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISN-PLKGKRKGGTV--GKPLPGVQAKIIAEDGSCDNVEV- 454
Cdd:cd17646 255 LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLDDALRPVPVGVp 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 455 GELCIKSPSLFKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLE 528
Cdd:cd17646 335 GELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 529 HPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVN 608
Cdd:cd17646 414 HPAVTHAVVVARAAPAGAARLVGYVVPAAG---------AAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLD 484
|
....
gi 747052525 609 KKEL 612
Cdd:cd17646 485 RAAL 488
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
130-615 |
1.80e-53 |
|
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: 191.14 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTsaqmsllpsvP 209
Cdd:cd05928 67 GDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASEC----------P 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTINGELDGTRCLQETEIPH---EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAW-GYTST 285
Cdd:cd05928 137 SLKTKLLVSEKSRDGWLNFKELLNEASTEHhcvETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTAS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 286 DHFLHCLPLHHVHGLFNALLAPLYAGSTV--EFMPKFSVRGIWQRWrESYPqdqtkaddaVTVFTGVPTMYTRLIQgyea 363
Cdd:cd05928 217 DIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHHLPRFDPLVILKTL-SSYP---------ITTFCGAPTVYRMLVQ---- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 364 mdpalQTASATAARQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKII 443
Cdd:cd05928 283 -----QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQII 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 444 AEDGscdNV----EVGELCIK-SP----SLFKEYWNLPEVTKQSfIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGG 514
Cdd:cd05928 358 DDNG---NVlppgTEGDIGIRvKPirpfGLFSGYVDNPEKTAAT-IRGDFYLTGDRGIMDEDGYFWFMGRAD-DVINSSG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 515 YKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKREEELkpaltLEELSMWAKEKLAPYKIPNCLL 594
Cdd:cd05928 433 YRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQL-----TKELQQHVKSVTAPYKYPRKVE 507
|
490 500
....*....|....*....|.
gi 747052525 595 LWESLPRNAMGKVNKKELKKQ 615
Cdd:cd05928 508 FVQELPKTVTGKIQRNELRDK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-613 |
2.29e-53 |
|
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: 189.19 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 124 ENKHLGGARVGIVAKPSPEFVAGVLGTWFSGG----VAVPLALSYPEAELLHVMNDSDItmilstedhqelmkAIAVKTS 199
Cdd:cd05922 12 EAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGG--------------RIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 200 AQMSLLPSVPSVSTKSTELdhtINGE-LDGTRCLQETeipHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTD 278
Cdd:cd05922 78 GAADRLRDALPASPDPGTV---LDADgIRAARASAPA---HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 AWGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPKFSV-RGIWQRWRESypqdqtkaddAVTVFTGVPTMY--- 354
Cdd:cd05922 152 YLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLdDAFWEDLREH----------GATGLAGVPSTYaml 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 355 TRLIqgyeaMDPAlqtasatAARQLRLMMCGSSALPLPVMQKW-ETITGHVLLERYGMTEF--VMAISNPLKGKRKGGTV 431
Cdd:cd05922 221 TRLG-----FDPA-------KLPSLRYLTQAGGRLPQETIARLrELLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 432 GKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRtNADIM 510
Cdd:cd05922 289 GLAIPGGEFEILDDDGTpTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGR-RDRMI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 511 KVGGYKLSALEIEAVLLEHPTISECCVLGLPDkDYGEAVCAIIipnpeikrkreeELKPALTLEELSMWAKEKLAPYKIP 590
Cdd:cd05922 368 KLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFV------------TAPDKIDPKDVLRSLAERLPPYKVP 434
|
490 500
....*....|....*....|...
gi 747052525 591 NCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05922 435 ATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
130-617 |
9.95e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 188.09 E-value: 9.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILStEDHQELMKAIAVktsaqmsllpsvp 209
Cdd:PRK09088 47 GERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG-DDAVAAGRTDVE------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 svstksteldhtingELDGTRCLQETEIPHE---ISGDDPALIIYTSGTTGKPKGVVHTHK---------GVLAQVqmlt 277
Cdd:PRK09088 113 ---------------DLAAFIASADALEPADtpsIPPERVSLILFTSGTSGQPKGVMLSERnlqqtahnfGVLGRV---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 278 dawgyTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVE----FMPKFSVRgiwqrwRESYPqdqtkaDDAVTVFTGVPTM 353
Cdd:PRK09088 174 -----DAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILvsngFEPKRTLG------RLGDP------ALGITHYFCVPQM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 354 yTRLIQGYEAMDPAlqtasatAARQLRLMMCGSSALPLPVMQKWETiTGHVLLERYGMTE----FVMAIsNPLKGKRKGG 429
Cdd:PRK09088 237 -AQAFRAQPGFDAA-------ALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEagtvFGMSV-DCDVIRAKAG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 430 TVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRtNAD 508
Cdd:PRK09088 307 AAGIPTPTVQTRVVDDQGNdCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDR-KKD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 509 IMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAPYK 588
Cdd:PRK09088 386 MFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA----------PLDLERIRSHLSTRLAKYK 455
|
490 500
....*....|....*....|....*....
gi 747052525 589 IPNCLLLWESLPRNAMGKVNKKELKKQLA 617
Cdd:PRK09088 456 VPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
83-613 |
1.37e-52 |
|
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: 186.81 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGP-----------EVRVGIALERSLEMVVALLAILKAGGAYVPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEdhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheis 242
Cdd:cd17649 70 EYPAERLRYMLEDSGAGLLLTHH--------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhHVHGLFNALLAPLYAGSTVEFMPKfsv 322
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPD--- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 rGIWQRWRESYPQDQtkaDDAVTVfTGVPTMYtrliqGYEAMDPALQTASATAARqLRLMMCGSSALPLPVMQKWETItG 402
Cdd:cd17649 169 -ELWASADELAEMVR---ELGVTV-LDLPPAY-----LQQLAEEADRTGDGRPPS-LRLYIFGGEALSPELLRRWLKA-P 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 403 HVLLERYGMTEFV---MAISNPLKGKRKGGTV--GKPLPGVQAKIIAED-GSCDNVEVGELCIKSPSLFKEYWNLPEVTK 476
Cdd:cd17649 237 VRLFNAYGPTEATvtpLVWKCEAGAARAGASMpiGRPLGGRSAYILDADlNPVPVGVTGELYIGGEGLARGYLGRPELTA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 477 QSFIDGGFF-------KTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDkDYGEAV 549
Cdd:cd17649 317 ERFVPDPFGapgsrlyRTGDLARWRDDGVIEYLGRVDHQV-KIRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQL 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 550 CAIIIPnpeikrkREEELKPALtLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd17649 395 VAYVVL-------RAAAAQPEL-RAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
70-618 |
2.32e-52 |
|
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: 188.05 E-value: 2.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 70 ELVKAVANRgsiSPESIAVTAHEKSHSYHQLilsAVKISNL---LTGADLRSvkgngenkhlgGARVgIVAKP-SPEFVA 145
Cdd:COG1021 29 DLLRRRAER---HPDRIAVVDGERRLSYAEL---DRRADRLaagLLALGLRP-----------GDRV-VVQLPnVAEFVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 146 GVLGTWFSGgvAVP-LAL-SYPEAELLHVMNDSD-ITMILSTE----DHQELMKAIAvktsaqmSLLPSVPSV-----ST 213
Cdd:COG1021 91 VFFALFRAG--AIPvFALpAHRRAEISHFAEQSEaVAYIIPDRhrgfDYRALARELQ-------AEVPSLRHVlvvgdAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 214 KSTELDHTINGELDGtrclqeteIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLP 293
Cdd:COG1021 162 EFTSLDALLAAPADL--------SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 294 LHHvhglfNA------LLAPLYAGSTVEFMPKFSvrgiwqrwresypqdqtkADDA--------VTVFTGVPTMYTRLIQ 359
Cdd:COG1021 234 AAH-----NFplsspgVLGVLYAGGTVVLAPDPS------------------PDTAfpliererVTVTALVPPLALLWLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 360 GYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEfvmaisnplkgkrkG----------- 428
Cdd:COG1021 291 AAERSRYDLSS--------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--------------Glvnytrlddpe 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 429 ----GTVGKPL-PGVQAKIIAEDGscDNV---EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYV 500
Cdd:COG1021 349 evilTTQGRPIsPDDEVRIVDEDG--NPVppgEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLV 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 501 ILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelkpALTLEELSMWA 580
Cdd:COG1021 427 VEGRAK-DQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGE-----------PLTLAELRRFL 494
|
570 580 590
....*....|....*....|....*....|....*....
gi 747052525 581 KEK-LAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:COG1021 495 RERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
117-613 |
3.52e-52 |
|
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: 185.33 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 117 RSVKGNGENKhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPL-ALSYPEAeLLHVMNDSDITMILStedhqelmkaia 195
Cdd:cd05971 21 NVLKEIGLEK---GDRVGVFLSQGPECAIAHIAILRSGAIAVPLfALFGPEA-LEYRLSNSGASALVT------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 196 vktsaqmsllpsvpsvstksteldhtingelDGTrclqeteipheisgDDPALIIYTSGTTGKPKGVVHTHK---GVLAQ 272
Cdd:cd05971 85 -------------------------------DGS--------------DDPALIIYTSGTTGPPKGALHAHRvllGHLPG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 273 VQM------------LTDA-WGYtstdhflhclplhhVHGLFNALLAPLYAGSTV--EFMPKFSVRGIWQrwresypqdq 337
Cdd:cd05971 120 VQFpfnlfprdgdlyWTPAdWAW--------------IGGLLDVLLPSLYFGVPVlaHRMTKFDPKAALD---------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 338 TKADDAVTVFTGVPTMYTRLIQGYEAMDPAlqtasataARQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMA 417
Cdd:cd05971 176 LMSRYGVTTAFLPPTALKMMRQQGEQLKHA--------QVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 418 ISN-PLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPS--LFKEYWNLPEVTKQSFIdGGFFKTGDAARV 493
Cdd:cd05971 248 IGNcSALFPIKPGSMGKPIPGHRVAIVDDNGTpLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMA-GDWLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 494 DEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrKREEELKpaltl 573
Cdd:cd05971 327 DSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE--TPSDALA----- 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 747052525 574 EELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05971 399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
96-607 |
3.77e-52 |
|
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: 186.11 E-value: 3.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 96 SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMND 175
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGT-----------GDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 176 SDITMILSTEDhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheisgDDPALIIYTSGT 255
Cdd:cd05914 78 SEAKAIFVSDE---------------------------------------------------------DDVALINYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 256 TGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVrgiwqrwresyPQ 335
Cdd:cd05914 101 TGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS-----------AK 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 336 DQTKADDAVTVFTGVPTMY----------------TRLIQgyEAMDPALQTASATAARQ---------LRLMMCGSSALP 390
Cdd:cd05914 170 IIALAFAQVTPTLGVPVPLviekifkmdiipkltlKKFKF--KLAKKINNRKIRKLAFKkvheafggnIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 391 LPVMQKWETItGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGScdnVEVGELCIKSPSLFKEYWN 470
Cdd:cd05914 248 PDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPA---TGEGEIIVRGPNVMKGYYK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 471 LPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIMKVGGYKLSALEIEAVLLEHPTISECCVlGLPDKDygeaVC 550
Cdd:cd05914 324 NPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLV-VVQEKK----LV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747052525 551 AIIIPNPE---IKRKREEELKPALtLEELSMWAKEKLAPY-KIPNCLLLWESLPRNAMGKV 607
Cdd:cd05914 399 ALAYIDPDfldVKALKQRNIIDAI-KWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKI 458
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
41-613 |
3.99e-52 |
|
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: 187.70 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 41 LSVFSLKVPSFRSFQYrlfssdthnsilmELVKAVANrgsISPESIAVT-----AHEKSHSYHQLILSAVKISNLLTGAD 115
Cdd:cd05970 5 HNNFSINVPENFNFAY-------------DVVDAMAK---EYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 116 LRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDH---QELMK 192
Cdd:cd05970 69 IGK-----------GDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDnipEEIEK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 193 AIavktsaqmsllPSVPSVSTKSTELDHTINGELDGTRCLQET----EIPH---EISGDDPALIIYTSGTTGKPKGVVHT 265
Cdd:cd05970 138 AA-----------PECPSKPKLVWVGDPVPEGWIDFRKLIKNAspdfERPTansYPCGEDILLVYFSSGTTGMPKMVEHD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 266 HkgvlaqvqmlTDAWGYTSTDHFLHCLPLHHVH------GLFNALLAPLY----AGSTVeF---MPKFSVRGIWQRWRES 332
Cdd:cd05970 207 F----------TYPLGHIVTAKYWQNVREGGLHltvadtGWGKAVWGKIYgqwiAGAAV-FvydYDKFDPKALLEKLSKY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 333 ypqdqtkaddAVTVFTGVPTMYTRLIQgyeamdpalQTASATAARQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMT 412
Cdd:cd05970 276 ----------GVTTFCAPPTIYRFLIR---------EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 413 EFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCI-----KSPSLFKEYWNLPEVTKQSFIDGgFFK 486
Cdd:cd05970 337 ETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGrSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAEVWHDG-YYH 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 487 TGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKreEE 566
Cdd:cd05970 416 TGDAAWMDEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPS--EE 492
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 747052525 567 LKpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05970 493 LK-----KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
244-619 |
7.03e-52 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 187.18 E-value: 7.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVefmpkfSVR 323
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATA------VLQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 GIWqrwresypqDQTKA-----DDAVTvFTGVPTMYtrliqgyeAMDPA-LQTASATAARQLRLMMCGSSALPLPVMQKW 397
Cdd:PRK13295 271 DIW---------DPARAaelirTEGVT-FTMASTPF--------LTDLTrAVKESGRPVSSLRTFLCAGAPIPGALVERA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 ETITGHVLLERYGMTE--FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEV 474
Cdd:PRK13295 333 RAALGAKIVSAWGMTEngAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAgQIGRLQVRGCSNFGGYLKRPQL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 475 TKQSFidGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIII 554
Cdd:PRK13295 413 NGTDA--DGWFDTGDLARIDADGYIRISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVV 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 555 PNPeikrkreeelKPALTLEELSMWAKE-KLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PRK13295 490 PRP----------GQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
96-614 |
1.85e-50 |
|
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: 182.15 E-value: 1.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 96 SYHQLILSAVKISNLLtgadlrsvkgngENKHLGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMND 175
Cdd:cd05909 9 TYRKLLTGAIALARKL------------AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 176 SDITMILSTEDHQE---LMKAIAVKTSAQMSLLPSVPSVSTKSTELDHTINGeldgtRCLQETEIP----HEISGDDPAL 248
Cdd:cd05909 77 AGIKTVLTSKQFIEklkLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAG-----KFPPKWLLRifgvAPVQPDDPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 249 IIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKfsvrgiwqr 328
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPN--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 329 wresyPQDQTK----ADDA-VTVFTGVPTMYTrliqGYeamdpaLQTASATAARQLRLMMCGSSALPLPVMQKWETITGH 403
Cdd:cd05909 223 -----PLDYKKipelIYDKkATILLGTPTFLR----GY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTEF--VMAISNPLKGKRKgGTVGKPLPGVQAKIIAEDGSCDnVEVGE---LCIKSPSLFKEYWNLPEVTKQS 478
Cdd:cd05909 288 RILEGYGTTECspVISVNTPQSPNKE-GTVGRPLPGMEVKIVSVETHEE-VPIGEgglLLVRGPNVMLGYLNEPELTSFA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FIDgGFFKTGDAARVDEDGYYVILGRTNAdIMKVGGYKLSALEIEAVLLEH-PTISECCVLGLPDKDYGEAVCAIIIPnp 557
Cdd:cd05909 366 FGD-GWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT-- 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 558 eikrkreeelkPALTLEELSMWAKE-KLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05909 442 -----------TDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
111-614 |
2.98e-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: 180.02 E-value: 2.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 111 LTGADLRSVKGNGEN--KHLG---GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTE 185
Cdd:cd05973 1 LTFGELRALSARFANalQELGvgpGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 186 DHQelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipHEISgDDPALIIYTSGTTGKPKGVVHT 265
Cdd:cd05973 81 ANR--------------------------------------------------HKLD-SDPFVMMFTSGTTGLPKGVPVP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 266 HKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAG-STVEFMPKFSVRGIWQrwresypqdqTKADDAV 344
Cdd:cd05973 110 LRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWR----------VIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 345 TVFTGVPTMYTRLIQGyeamdpalqTASATAARQLRLMMCGSSALPL-PVMQKWETIT-GHVLLERYGMTEFVMAISN-- 420
Cdd:cd05973 180 TNLAGSPTAYRLLMAA---------GAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANhh 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 PLKGKRKGGTVGKPLPGVQAKIIAEDGscDNV---EVGELCI---KSPSL-FKEYWNLPevtkQSFIDGGFFKTGDAARV 493
Cdd:cd05973 251 ALEHPVHAGSAGRAMPGWRVAVLDDDG--DELgpgEPGRLAIdiaNSPLMwFRGYQLPD----TPAIDGGYYLTGDTVEF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 494 DEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkrEEELKPALTl 573
Cdd:cd05973 325 DPDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG------GHEGTPALA- 396
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 747052525 574 EELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05973 397 DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
238-613 |
5.36e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.14 E-value: 5.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQV-QMltDAW---GYTSTDH-----FLHCLPLHHVHGL-FNALLAp 307
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQM--EAWlqpAFEKKPRpdqlnFVCALPLYHIFALtVCGLLG- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 308 LYAGSTVEFMPkfSVRGIWQRWRE--SYPqdqtkaddaVTVFTGVPTMYTRLIQ--GYEAMDPAlqtasataarQLRLMM 383
Cdd:PRK07059 275 MRTGGRNILIP--NPRDIPGFIKElkKYQ---------VHIFPAVNTLYNALLNnpDFDKLDFS----------KLIVAN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPLPVMQKWETITGHVLLERYGMTEFV-MAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKS 461
Cdd:PRK07059 334 GGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGnDLPLGEPGEICIRG 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLP 541
Cdd:PRK07059 414 PQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747052525 542 DKDYGEAVCAIIIpnpeikRKreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK07059 493 DEHSGEAVKLFVV------KK-----DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
241-613 |
5.55e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 182.27 E-value: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLA---QVQMLTDAWGYTSTDHFLHCLPLHHVHGL-FNALLAPLYAGSTVEF 316
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNEGCEILIAPLPLYHIYAFtFHCMAMMLIGNHNILI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 -----MPKFsVRGIwQRWResypqdqtkaddaVTVFTGVPTMYTRLIQ--GYEAMDpalqtASAtaarqLRLMMCGSSAL 389
Cdd:PRK05677 284 snprdLPAM-VKEL-GKWK-------------FSGFVGLNTLFVALCNneAFRKLD-----FSA-----LKLTLSGGMAL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 390 PLPVMQKWETITGHVLLERYGMTEFVMAIS-NPLKGKRKGgTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKE 467
Cdd:PRK05677 339 QLATAERWKEVTGCAICEGYGMTETSPVVSvNPSQAIQVG-TIGIPVPSTLCKVIDDDGNELPLgEVGELCVKGPQVMKG 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:PRK05677 418 YWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGE 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 548 AVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK05677 497 AIKVFVVVKP----------GETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
130-615 |
6.60e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 181.93 E-value: 6.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEdhqelmkaiAVKTS--AQM--SLL 205
Cdd:PRK08315 68 GDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD---------GFKDSdyVAMlyELA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 206 PsvpsvstkstELDHTINGELDGTR--CLQET------------------------------EIPHEISGDDPALIIYTS 253
Cdd:PRK08315 139 P----------ELATCEPGQLQSARlpELRRViflgdekhpgmlnfdellalgravddaelaARQATLDPDDPINIQYTS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 254 GTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFM-PKFSvrgiwqrwres 332
Cdd:PRK08315 209 GTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPgEGFD----------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 333 yPQD--QTKADDAVTVFTGVPTMYtrlIqgyeAM--DPALQTASATAarqLRL-MMCGSSAlPLPVMQKWE--------T 399
Cdd:PRK08315 278 -PLAtlAAVEEERCTALYGVPTMF---I----AEldHPDFARFDLSS---LRTgIMAGSPC-PIEVMKRVIdkmhmsevT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITghvllerYGMTE-----FVMAISNPLKgkRKGGTVGKPLPGVQAKIIAEDgSCDNV---EVGELCIKSPSLFKEYWNL 471
Cdd:PRK08315 346 IA-------YGMTEtspvsTQTRTDDPLE--KRVTTVGRALPHLEVKIVDPE-TGETVprgEQGELCTRGYSVMKGYWND 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 472 PEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCA 551
Cdd:PRK08315 416 PEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGR-IKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCA 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 552 IIIPnpeikrkREEElkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK08315 495 WIIL-------RPGA---TLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
83-612 |
1.72e-49 |
|
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: 179.00 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRP-----------GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEDHQELmkaiavktsaqmsllpsVPSVSTKSTELDHTINGELDGTrclqeteiPHEIS 242
Cdd:cd12114 70 DQPAARREAILADAGARLVLTDGPDAQL-----------------DVAVFDVLILDLDALAAPAPPP--------PVDVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHH---VHGLFnallAPLYAGSTVeFMPK 319
Cdd:cd12114 125 PDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIF----GALSAGATL-VLPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGIWQRWREsypqdqTKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWET 399
Cdd:cd12114 200 EARRRDPAHWAE------LIERHGVTLWNSVPALLEMLLDVLEAAQALLPS--------LRLVLLSGDWIPLDLPARLRA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHV-LLERYGMTEfvMAI-SN-----PLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNL 471
Cdd:cd12114 266 LAPDArLISLGGATE--ASIwSIyhpidEVPPDWRSIPYGRPLANQRYRVLDPRGRdCPDWVPGELWIGGRGVALGYLGD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 472 PEVTKQSFID----GGFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDkDYGE 547
Cdd:cd12114 344 PELTAARFVThpdgERLYRTGDLGRYRPDGTLEFLGRRDGQV-KVRGYRIELGEIEAALQAHPGVARAVVVVLGD-PGGK 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 548 AVCAIIIPNPEIkrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd12114 422 RLAAFVVPDNDG---------TPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
69-620 |
6.42e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 177.66 E-value: 6.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 69 MELVKAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLtgadlRSVKGngENKhlggaRVGIVAKPSPEFVAGVL 148
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWL-----NEKES--KNK-----TIAILLENRIEFLQLFA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 149 GTWFSGGVAVPLALSYPEAELLHVMNDSDITMILsTEDHqelmkaiavktsaqmsLLPSVPSVSTKSTELDH---TINGE 225
Cdd:PRK07638 69 GAAMAGWTCVPLDIKWKQDELKERLAISNADMIV-TERY----------------KLNDLPDEEGRVIEIDEwkrMIEKY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 226 LDgtrclqeTEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALL 305
Cdd:PRK07638 132 LP-------TYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 ApLYAGSTVEFMPKFSVRGIwqrwresypQDQTKADDaVTVFTGVPTMYTRLIQGYEAMDPALQTASATAArqlrlmmcg 385
Cdd:PRK07638 205 T-LYVGQTVHLMRKFIPNQV---------LDKLETEN-ISVMYTVPTMLESLYKENRVIENKMKIISSGAK--------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 386 ssaLPLPVMQKWETITGHV-LLERYGMTE--FVMAISnPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKS 461
Cdd:PRK07638 265 ---WEAEAKEKIKNIFPYAkLYEFYGASElsFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGeEVQKGEIGTVYVKS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSLFKEYWNLPEVTKQSFIDGgFFKTGDAARVDEDGYYVILGRTNADIMkVGGYKLSALEIEAVLLEHPTISECCVLGLP 541
Cdd:PRK07638 341 PQFFMGYIIGGVLARELNADG-WMTVRDVGYEDEEGFIYIVGREKNMIL-FGGINIFPEEIESVLHEHPAVDEIVVIGVP 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 542 DKDYGEAVCAIIipnpeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PRK07638 419 DSYWGEKPVAII--------------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
83-612 |
1.54e-48 |
|
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: 175.96 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGP-----------GDRVALALPRSAELIVALLAILKAGGAYVPIDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheis 242
Cdd:cd17643 70 AYPVERIAFILADSGPSLLLTD---------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHClplHH------VHGLFNALlapLYAGSTVef 316
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLF---HSyafdfsVWEIWGAL---LHGGRLV-- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 MPKFSVRgiwqRWRESYPqdQTKADDAVTVFTGVPTMYTRLIQGyeamdpALQTASATAArqLRLMMCGSSALPLPVMQK 396
Cdd:cd17643 164 VVPYEVA----RSPEDFA--RLLRDEGVTVLNQTPSAFYQLVEA------ADRDGRDPLA--LRYVIFGGEALEAAMLRP 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 397 WETITGHV---LLERYGMTE---FVM--AISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKE 467
Cdd:cd17643 230 WAGRFGLDrpqLVNMYGITEttvHVTfrPLDAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPgVVGELYVSGAGVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGL 540
Cdd:cd17643 310 YLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQV-KIRGFRIELGEIEAALATHPSVRDAAVIVR 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747052525 541 PDKDYGEAVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17643 389 EDEPGDTRLVAYVVADDG----------AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
241-620 |
2.47e-48 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 177.73 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT----DAWGYTSTDH-FLHCLPLHHVHGLFNALLAPLYAGSTVE 315
Cdd:PLN02574 195 IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNvYLAALPMFHIYGLSLFVVGLLSLGSTIV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 316 FMPKFSVrgiwqrwresypQDQTKADD--AVTVFTGVPTMYTRLIQgyeamdpALQTASATAARQLRLMMCGSSALPLPV 393
Cdd:PLN02574 275 VMRRFDA------------SDMVKVIDrfKVTHFPVVPPILMALTK-------KAKGVCGEVLKSLKQVSCGAAPLSGKF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHV-LLERYGMTEFVMAISNPLKGK--RKGGTVGKPLPGVQAKIIA-EDGSC-DNVEVGELCIKSPSLFKEY 468
Cdd:PLN02574 336 IQDFVQTLPHVdFIQGYGMTESTAVGTRGFNTEklSKYSSVGLLAPNMQAKVVDwSTGCLlPPGNCGELWIQGPGVMKGY 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 469 WNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEA 548
Cdd:PLN02574 416 LNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEI 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 747052525 549 VCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PLN02574 495 PVAFVVRRQG----------STLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSV 556
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
130-613 |
3.20e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 177.39 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEdhqELMKAIAVKtsaQMSLLPSVP 209
Cdd:PRK04319 98 GDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP---ALLERKPAD---DLPSLKHVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTINGELDGTRCLQETEIPHeISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQvqMLTDAWGytstdhfl 289
Cdd:PRK04319 172 LVGEDVEEGPGTLDFNALMEQASDEFDIEW-TDREDGAILHYTSGSTGKPKGVLHVHNAMLQH--YQTGKYV-------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 290 hcLPLHH------------VHGLFNALLAPLYAGST-----VEFMPkfsvrgiwQRWresYpqdQTKADDAVTVFTGVPT 352
Cdd:PRK04319 241 --LDLHEddvywctadpgwVTGTSYGIFAPWLNGATnvidgGRFSP--------ERW---Y---RILEDYKVTVWYTAPT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 353 MYTRLIQgyeamdpalqtASATAARQLRLmmcgsSAL--------PL-PVMQKW-ETITGHVLLERYGMTEF--VMaISN 420
Cdd:PRK04319 305 AIRMLMG-----------AGDDLVKKYDL-----SSLrhilsvgePLnPEVVRWgMKVFGLPIHDNWWMTETggIM-IAN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 PLKGKRKGGTVGKPLPGVQAKIIAEDGscDNVE---VGELCIKS--PSLFKEYWNLPEVTKQSFIdGGFFKTGDAARVDE 495
Cdd:PRK04319 368 YPAMDIKPGSMGKPLPGIEAAIVDDQG--NELPpnrMGNLAIKKgwPSMMRGIWNNPEKYESYFA-GDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 496 DGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrKREEELKpaltlEE 575
Cdd:PRK04319 445 DGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--EPSEELK-----EE 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 747052525 576 LSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK04319 517 IRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
83-612 |
3.51e-48 |
|
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: 175.61 E-value: 3.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17651 9 PDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGP-----------GDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILStedHQELMKAIAVKTSAQMSLLPSvpsvstksteldhtingeldGTRCLQETEIPHEIS 242
Cdd:cd17651 78 AYPAERLAFMLADAGPVLVLT---HPALAGELAVELVAVTLLDQP--------------------GAAAGADAEPDPALD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLH---HVHGLFNALLaplyAGSTVEFMP- 318
Cdd:cd17651 135 ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLC----AGATLVLPPe 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 --KFSVRGIWQRWREsypQDQTKADdavtvftgVPTMYTRLIqgYEAMDPALQTASAtaarqLRLMMCGSSALPL-PVMQ 395
Cdd:cd17651 211 evRTDPPALAAWLDE---QRISRVF--------LPTVALRAL--AEHGRPLGVRLAA-----LRYLLTGGEQLVLtEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWETITGHVLLE-RYGMTE--FVMAISNPLKGKRKGGT--VGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYW 469
Cdd:cd17651 273 EFCAGLPGLRLHnHYGPTEthVVTALSLPGDPAAWPAPppIGRPIDNTRVYVLDAALRpVPPGVPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 470 NLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDK 543
Cdd:cd17651 353 NRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGR-ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 544 DYGEAVCAIIIPNPEiKRKREEELKPALtleelsmwaKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17651 432 PGEKRLVAYVVGDPE-APVDAAELRAAL---------ATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
111-615 |
4.03e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 175.86 E-value: 4.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 111 LTGADL--RSVKGNGENKHLG---GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTE 185
Cdd:PRK08276 12 VTYGELeaRSNRLAHGLRALGlreGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 186 DHQELMKAIAVKTSAQMSLLPSVPsvstksteldhtinGELDGTRCLQE-------TEIPHEISGDDpalIIYTSGTTGK 258
Cdd:PRK08276 92 ALADTAAELAAELPAGVPLLLVVA--------------GPVPGFRSYEEalaaqpdTPIADETAGAD---MLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 259 PKGVVH--THKGVL-AQVQMLT--DAWGYTSTDH-FLHCLPLHHVhglfnallAPL-------YAGSTVEFMPKFS---- 321
Cdd:PRK08276 155 PKGIKRplPGLDPDeAPGMMLAllGFGMYGGPDSvYLSPAPLYHT--------APLrfgmsalALGGTVVVMEKFDaeea 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 322 VRGIwQRWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTASataarqLRLMMCGssALPLPVMQKWETIT 401
Cdd:PRK08276 227 LALI-ERYR-------------VTHSQLVPTMFVRMLKLPEEVRARYDVSS------LRVAIHA--AAPCPVEVKRAMID 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 --GHVLLERYGMTEFVM-AISNPLKGKRKGGTVGKPLPGVqAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQ 477
Cdd:PRK08276 285 wwGPIIHEYYASSEGGGvTVITSEDWLAHPGSVGKAVLGE-VRILDEDGNeLPPGEIGTVYFEMDGYPFEYHNDPEKTAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 SFIDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNP 557
Cdd:PRK08276 364 ARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 558 EIkrkreeELKPALTlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK08276 443 GA------DAGDALA-AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
219-613 |
4.77e-48 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 176.99 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 219 DHTINGELDGTRCL----QETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAWGYTS------TDHF 288
Cdd:PRK08751 179 EYRINGAIRFREALalgrKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTgkleegCEVV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 289 LHCLPLHHVHGLF-NALLAPLYAG-----STVEFMPKFsVRGIwQRWResypqdqtkaddaVTVFTGVPTMYTRLIQ--G 360
Cdd:PRK08751 258 ITALPLYHIFALTaNGLVFMKIGGcnhliSNPRDMPGF-VKEL-KKTR-------------FTAFTGVNTLFNGLLNtpG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 361 YEAMDPAlqtasataarQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFV-MAISNPLKGKRKGGTVGKPLPGVQ 439
Cdd:PRK08751 323 FDQIDFS----------SLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 440 AKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLS 518
Cdd:PRK08751 393 ACIKDDAGTVLAIgEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKK-DMILVSGFNVY 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 519 ALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikrKREeelkPALTLEELSMWAKEKLAPYKIPNCLLLWES 598
Cdd:PRK08751 472 PNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-------KKD----PALTAEDVKAHARANLTGYKQPRIIEFRKE 540
|
410
....*....|....*
gi 747052525 599 LPRNAMGKVNKKELK 613
Cdd:PRK08751 541 LPKTNVGKILRRELR 555
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
127-616 |
1.11e-47 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 175.76 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 127 HLG---GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTED----HQELMkaIAVKTS 199
Cdd:PLN02860 51 RLGlrnGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswYEELQ--NDRLPS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 200 AQMSLLPSVPSVStKSTELDHTINGELDGTRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDA 279
Cdd:PLN02860 129 LMWQVFLESPSSS-VFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 280 WGYTSTDHFLHCLPLHHVHGLFNALlAPLYAGSTVEFMPKFSVRGIWQRWResypqdqtkaDDAVTVFTGVPTMYTRLIQ 359
Cdd:PLN02860 208 VGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIK----------QHNVTSMITVPAMMADLIS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 360 gyeamdPALQTASATAARQLRLMMCGSSALPLPVMQKW-ETITGHVLLERYGMTE------FvMAISNP----------- 421
Cdd:PLN02860 277 ------LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAkKLFPNAKLFSAYGMTEacssltF-MTLHDPtlespkqtlqt 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 422 ------LKGKRKGGT-VGKPLPGVQAKIIAEDGScdnvEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVD 494
Cdd:PLN02860 350 vnqtksSSVHQPQGVcVGKPAPHVELKIGLDESS----RVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 495 EDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNP----EIKRKREEELKPA 570
Cdd:PLN02860 426 KAGNLWLIGRSNDRI-KTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwSDNEKENAKKNLT 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 747052525 571 LTLEELSMWAKEK-LAPYKIPNCLLLWES-LPRNAMGKVNKKELKKQL 616
Cdd:PLN02860 505 LSSETLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV 552
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
154-620 |
1.34e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 174.50 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 154 GGVAVPLALSYPEAELLHVMNDSDITMILStedHQELMKAIAVKTSAQMSLL--PSVPSVSTK---STELDHTINGELDG 228
Cdd:PRK12406 60 GAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHGLASALPAGVTVLsvPTPPEIAAAyriSPALLTPPAGAIDW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 229 TRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVH---THKGVLAQVQMLTDAWGYTSTDHFLHCLPLHH----VHGLF 301
Cdd:PRK12406 137 EGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 302 NALLaplyaGSTVEFMPKFSvrgiwqrwresyPQD--QTKADDAVTVFTGVPTMYTRLIQGYEAMDPALQTASataarqL 379
Cdd:PRK12406 217 AGRL-----GGVLVLQPRFD------------PEEllQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSS------L 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 380 RLMMCGSSALPLPV---MQKWetiTGHVLLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEV 454
Cdd:PRK12406 274 RHVIHAAAPCPADVkraMIEW---WGPVIYEYYGSTESgAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGrPLPQGEI 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 455 GELCIKSP--SLFKeYWNLPEvtKQSFID-GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPT 531
Cdd:PRK12406 351 GEIYSRIAgnPDFT-YHNKPE--KRAEIDrGGFITSGDVGYLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 532 ISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKE 611
Cdd:PRK12406 427 VHDCAVFGIPDAEFGEALMAVVEPQPGA----------TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRR 496
|
....*....
gi 747052525 612 LKKQLADQV 620
Cdd:PRK12406 497 LRDPYWANA 505
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
89-618 |
1.93e-47 |
|
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: 174.73 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 89 TAHEKSHSYHQLILSAVKISNLLTGADLRsvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL--SYPE 166
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVGKP------------GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptPGRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 167 AE-LLHVMNDSDITMILSTEDHQELMKAIAVKTSAQmsLLPSVPSVSTKsteldhtingELDGTRCLQETEIPHeisgDD 245
Cdd:cd05931 87 AErLAAILADAGPRVVLTTAAALAAVRAFAASRPAA--GTPRLLVVDLL----------PDTSAADWPPPSPDP----DD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 246 PALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFS-VR- 323
Cdd:cd05931 151 IAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAfLRr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 -GIWQRWRESYPQdqtkaddavtVFTGVPTMytrliqgyeAMDPALQTASATAARQL-----RLMMCGSSalplPVmqKW 397
Cdd:cd05931 231 pLRWLRLISRYRA----------TISAAPNF---------AYDLCVRRVRDEDLEGLdlsswRVALNGAE----PV--RP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 ETITG------------HVLLERYGMTE---FV----------------MAISNPLKGKRKGGT-------VGKPLPGVQ 439
Cdd:cd05931 286 ATLRRfaeafapfgfrpEAFRPSYGLAEatlFVsggppgtgpvvlrvdrDALAGRAVAVAADDPaarelvsCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 440 AKIIAEDGS--CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFI------DGGFFKTGDAARVDeDGYYVILGRTnADIMK 511
Cdd:cd05931 366 VRIVDPETGreLPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdEGGWLRTGDLGFLH-DGELYITGRL-KDLII 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 512 VGGYKLSALEIEAVLLE-HPTISE--CCVLGLPDKDYGEAVcaiiIPNPEIKRKREEELKPALTLEELSMWAKEKLAPYK 588
Cdd:cd05931 444 VRGRNHYPQDIEATAEEaHPALRPgcVAAFSVPDDGEERLV----VVAEVERGADPADLAAIAAAIRAAVAREHGVAPAD 519
|
570 580 590
....*....|....*....|....*....|
gi 747052525 589 IpnCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:cd05931 520 V--VLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
83-612 |
3.72e-47 |
|
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: 172.48 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGP-----------GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDItmilstedhqelmkAIAVKTSAQMSLLPSVPSVSTKSTELDHtingeldgtrcLQETEIPHEIS 242
Cdd:cd12116 70 DYPADRLRYILEDAEP--------------ALVLTDDALPDRLPAGLPVLLLALAAAA-----------AAPAAPRTPVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCL-PLHHVHGLfnALLAPLYAGSTVEFMPKFS 321
Cdd:cd12116 125 PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTtYAFDISLL--ELLLPLLAGARVVIAPRET 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 322 VRGiwqrwresyPQD--QTKADDAVTVFTGVPTMYTrliqgyeamdpALQTASATAARQLRLMmCGSSALPlPVMQKWET 399
Cdd:cd12116 203 QRD---------PEAlaRLIEAHSITVMQATPATWR-----------MLLDAGWQGRAGLTAL-CGGEALP-PDLAARLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTE-FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGscDNV---EVGELCIKSPSLFKEYWNLPEVT 475
Cdd:cd12116 261 SRVGSLWNLYGPTEtTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAAL--RPVppgVPGELYIGGDGVAQGYLGRPALT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 476 KQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEA 548
Cdd:cd12116 339 AERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQV-KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 549 VCAIIIPNPeikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd12116 418 VAYVVLKAG-----------AAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
245-609 |
8.38e-47 |
|
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: 167.68 E-value: 8.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRG 324
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IWQRwresypqdqtKADDAVTVFTGVPTMYTRLIQgyeamDPALQTASATAarqLRLMMCGSSALPLPVMQKWETITG-H 403
Cdd:cd17638 81 ILEA----------IERERITVLPGPPTLFQSLLD-----HPGRKKFDLSS---LRAAVTGAATVPVELVRRMRSELGfE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTEFVMA-ISNPLKGKRK-GGTVGKPLPGVQAKIiaedgscdnVEVGELCIKSPSLFKEYWNLPEVTKQSFID 481
Cdd:cd17638 143 TVLTAYGLTEAGVAtMCRPGDDAETvATTCGRACPGFEVRI---------ADDGEVLVRGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkr 561
Cdd:cd17638 214 DGWLHTGDVGELDERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV-- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 747052525 562 kreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNK 609
Cdd:cd17638 291 --------TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
231-576 |
5.43e-46 |
|
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: 170.09 E-value: 5.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 231 CLQETEIPHEI---SGDDPALIIYTSGTTGKPKGVVHTHK----GVLAQVQMLTDAWGytSTDHFLHCLPLHHVHGlFNA 303
Cdd:cd17639 72 SLNETECSAIFtdgKPDDLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLGDRVPELLG--PDDRYLAYLPLAHIFE-LAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 304 LLAPLYAGSTVEFmpkfsvrgiwqrwreSYPQ---DQTKAD---DAV----TVFTGVPTMYTRLIQGYEAMDPALQT--- 370
Cdd:cd17639 149 ENVCLYRGGTIGY---------------GSPRtltDKSKRGckgDLTefkpTLMVGVPAIWDTIRKGVLAKLNPMGGlkr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 371 -------------------------------ASATAARqLRLMMCGSSALPlPVMQKWETITGHVLLERYGMTEFV--MA 417
Cdd:cd17639 214 tlfwtayqsklkalkegpgtplldelvfkkvRAALGGR-LRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETCagGT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 418 ISNPlkGKRKGGTVGKPLPGVQAKI--IAEDG-SCDNVEV-GELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARV 493
Cdd:cd17639 292 VQDP--GDLETGRVGPPLPCCEIKLvdWEEGGySTDKPPPrGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEF 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 494 DEDGYYVILGRTNaDIMKV--GGYklSALE-IEAVLLEHPTISECCVLGLPDKDYgeaVCAIIIPNPE-IKRKREEELKP 569
Cdd:cd17639 370 HPDGTLKIIDRKK-DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEKhLTKLAEKHGVI 443
|
....*..
gi 747052525 570 ALTLEEL 576
Cdd:cd17639 444 NSEWEEL 450
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
126-571 |
6.57e-46 |
|
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: 169.96 E-value: 6.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 126 KHLG---GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLalsYPEA---ELLHVMNDSDI-TMILSTEDHQELMKAIAVKT 198
Cdd:cd05932 24 RALGlepGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTLnpdTIRYVLEHSESkALFVGKLDDWKAMAPGVPEG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 199 SAQMSLLPsvPSVSTKSTELDHTINgeldgTRCLQETEIPHEisGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTD 278
Cdd:cd05932 101 LISISLPP--PSAANCQYQWDDLIA-----QHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 AWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFsvrgiwqrwrESYPQDQTKADDavTVFTGVPTMYTRLI 358
Cdd:cd05932 172 HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESL----------DTFVEDVQRARP--TLFFSVPRLWTKFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 359 QG-YEAMDPA-LQ---------------TASATAARQLRLMMCGSSALPLPVMQkWETITGHVLLERYGMTE-FVMAISN 420
Cdd:cd05932 240 QGvQDKIPQQkLNlllkipvvnslvkrkVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTEnFAYSHLN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 pLKGKRKGGTVGKPLPGVQAKIiAEDGscdnvevgELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYV 500
Cdd:cd05932 319 -YPGRDKIGTVGNAGPGVEVRI-SEDG--------EILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLT 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 501 ILGRTNaDIMKVGGYKLSA-LEIEAVLLEHPTISECCVLG--LPdkdygeAVCAIIIPNPEIKRKREEELKPAL 571
Cdd:cd05932 389 ITGRVK-DIFKTSKGKYVApAPIENKLAEHDRVEMVCVIGsgLP------APLALVVLSEEARLRADAFARAEL 455
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
244-616 |
1.83e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 169.07 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHkGVLAQV--QMLTDAW-GYTSTDHFLHCLPLHH---VHGLFNallapLYAGSTVEFM 317
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTH-GQMAFVitNHLADLMpGTTEQDASLVVAPLSHgagIHQLCQ-----VARGAATVLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 P--KFSVRGIWQ---RWResypqdqtkaddaVTVFTGVPTMYTRLIQgyeamDPALQTASATAarqLRLMMCGSSALPLP 392
Cdd:PRK07470 237 PseRFDPAEVWAlveRHR-------------VTNLFTVPTILKMLVE-----HPAVDRYDHSS---LRYVIYAGAPMYRA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 393 VMQKWETITGHVLLERYGMTEFVMAIS-------NPLKGKRKG-GTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPS 463
Cdd:PRK07470 296 DQKRALAKLGKVLVQYFGLGEVTGNITvlppalhDAEDGPDARiGTCGFERTGMEVQIQDDEGReLPPGETGEICVIGPA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 464 LFKEYWNLPEVTKQSFIDGgFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDK 543
Cdd:PRK07470 376 VFAGYYNNPEANAKAFRDG-WFRTGDLGHLDARGFLYITGRA-SDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 544 DYGEAVCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQL 616
Cdd:PRK07470 454 VWGEVGVAVCVARDGA----------PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
240-613 |
2.03e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 169.46 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVqmLTDAWGYTStdhFLH--------CLPLHHVHGL-FNALLApLYA 310
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYGP---LLHpgkelvvtALPLYHIFALtVNCLLF-IEL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 311 GSTVEFM--PkfsvRGIWQRWRE--SYPqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGS 386
Cdd:PRK08974 276 GGQNLLItnP----RDIPGFVKElkKYP---------FTAITGVNTLFNALLNNEEFQELDFSS--------LKLSVGGG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 387 SALPLPVMQKWETITGHVLLERYGMTEFVMAIS-NPLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSL 464
Cdd:PRK08974 335 MAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDDDGNeVPPGEPGELWVKGPQV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 465 FKEYWNLPEVTKQsFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKD 544
Cdd:PRK08974 415 MLGYWQRPEATDE-VIKDGWLATGDIAVMDEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEV 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 545 YGEAVCAIIIPNpeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK08974 493 SGEAVKIFVVKK-----------DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
83-612 |
2.55e-45 |
|
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: 167.50 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVgIVAKPS-PEFVAGVLGTwFSGGVAVPLA 161
Cdd:cd05920 29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRP-----------GDRV-VVQLPNvAEFVVLFFAL-LRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 L-SYPEAELLHVMNDSDITMILSTE-----DHQELMKaiavktsaqmsllpsvpsvstkstELDHTINgeldgtrclqet 235
Cdd:cd05920 96 LpSHRRSELSAFCAHAEAVAYIVPDrhagfDHRALAR------------------------ELAESIP------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 236 eipheisgdDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHvhglfNALLA-P-----LY 309
Cdd:cd05920 140 ---------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NFPLAcPgvlgtLL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 310 AGSTVEFMPKFSvrgiwqrwresyPQDQTKADDA--VTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSS 387
Cdd:cd05920 206 AGGRVVLAPDPS------------PDAAFPLIERegVTVTALVPALVSLWLDAAASRRADLSS--------LRLLQVGGA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 388 ALPLPVMQKWETITGHVLLERYGMTEFVM---AISNPlkGKRKGGTVGKPL-PGVQAKIIAEDGScdNV---EVGELCIK 460
Cdd:cd05920 266 RLSPALARRVPPVLGCTLQQVFGMAEGLLnytRLDDP--DEVIIHTQGRPMsPDDEIRVVDEEGN--PVppgEEGELLTR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGL 540
Cdd:cd05920 342 GPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 541 PDKDYGEAVCAIIIPNPeikrkreeelkPALTLEELSMWAKEK-LAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd05920 421 PDELLGERSCAFVVLRD-----------PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
83-612 |
3.60e-45 |
|
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: 166.27 E-value: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvKGNGEnkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAA------RGVGP-----ERLVALALPRSAELVVAILAVLKAGAAYLPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEDHqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheis 242
Cdd:cd17652 70 AYPAERIAYMLADARPALLLTTPDN------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 gddPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglFNA----LLAPLYAGSTVEFMP 318
Cdd:cd17652 95 ---LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-----FDAsvweLLMALLAGATLVLAP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KfsvrgiwQRWRESYPQDQTKADDAVTVFTGVPTmytrliqgyeamdpALQTASATAARQLRLMMCGSSALPLPVMQKWE 398
Cdd:cd17652 167 A-------EELLPGEPLADLLREHRITHVTLPPA--------------ALAALPPDDLPDLRTLVVAGEACPAELVDRWA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 TitGHVLLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQAKIIaeDGSCDNV---EVGELCIKSPSLFKEYWNLPEV 474
Cdd:cd17652 226 P--GRRMINAYGPTETtVCATMAGPLPGGGVPPIGRPVPGTRVYVL--DARLRPVppgVPGELYIAGAGLARGYLNRPGL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 475 TKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:cd17652 302 TAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDK 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 548 AVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17652 381 RLVAYVVPAPG----------AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
130-615 |
6.75e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 167.63 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAI--AVKTSAQMSLLPS 207
Cdd:PRK06155 71 GDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdpGDLPLPAVWLLDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 208 VPSVSTkSTELDHTINGELDGTRClqeteiPHEISGDDPALIIYTSGTTGKPKGVVHTHkgvlAQV----QMLTDAWGYT 283
Cdd:PRK06155 151 PASVSV-PAGWSTAPLPPLDAPAP------AAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFywwgRNSAEDLEIG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 284 STDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPKFSVRGIWQRWRESypqdqtkaDDAVTVFTGvptmytrliqgyeA 363
Cdd:PRK06155 220 ADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSASGFWPAVRRH--------GATVTYLLG-------------A 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 364 MDPALQTASATAA-RQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTE--FVMAISNPlkgKRKGGTVGKPLPGVQA 440
Cdd:PRK06155 278 MVSILLSQPARESdRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTEtnFVIAVTHG---SQRPGSMGRLAPGFEA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 441 KIIAEDGS-CDNVEVGELCIKS--PSLFKE-YWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYK 516
Cdd:PRK06155 355 RVVDEHDQeLPDGEPGELLLRAdePFAFATgYFGMPEKTVEAWRN-LWFHTGDRVVRDADGWFRFVDRIK-DAIRRRGEN 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 517 LSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLW 596
Cdd:PRK06155 433 ISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGT----------ALEPVALVRHCEPRLAYFAVPRYVEFV 502
|
490
....*....|....*....
gi 747052525 597 ESLPRNAMGKVNKKELKKQ 615
Cdd:PRK06155 503 AALPKTENGKVQKFVLREQ 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
68-616 |
9.96e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 166.21 E-value: 9.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGV 147
Cdd:PRK06145 1 MFNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQ-----------GDVVALLMKNSAAFLELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDhqelmkaiavktsaqmslLPSVPSVSTKSTELDHtiNGELD 227
Cdd:PRK06145 70 FAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE------------------FDAIVALETPKIVIDA--AAQAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 228 GTRCLQ-ETEIP--HEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNAL 304
Cdd:PRK06145 130 SRRLAQgGLEIPpqAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 305 LAPLYAGSTVEFMPKFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIqgyeamdpALQTASATAARQLRLMMC 384
Cdd:PRK06145 210 IAVLWVGGTLRIHREFDPEAVLA----------AIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLAWCIG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 GSSALP-LPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKR--KGGTVGKPLPGVQAKIIAEDGSC--DNVEvGELCI 459
Cdd:PRK06145 272 GGEKTPeSRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIADGAGRWlpPNMK-GEICM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 460 KSPSLFKEYWNLPEVTKQSFIdGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLG 539
Cdd:PRK06145 351 RGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 540 LPDKDYGEAVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQL 616
Cdd:PRK06145 429 VHDDRWGERITAVVVLNP----------GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
56-607 |
1.69e-43 |
|
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: 164.67 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 56 YRLFSSDTHNSILMELVKAVANRG---SISPESiAVTAHEKSHSYHQLILSAVKISNLLTgaDLRSVKGNgenkhlggaR 132
Cdd:cd17634 44 IKWFEDATLNLAANALDRHLRENGdrtAIIYEG-DDTSQSRTISYRELHREVCRFAGTLL--DLGVKKGD---------R 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQMSLLPSVPSVS 212
Cdd:cd17634 112 VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 T----KSTELDHTINGELD-GTRCLQETEIPHE----ISGDDPALIIYTSGTTGKPKGVVHTHKG-VLAQVQMLTDAWGY 282
Cdd:cd17634 192 HvivlKRTGSDIDWQEGRDlWWRDLIAKASPEHqpeaMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 283 TSTDHFLHCLPLHHVHGLFNALLAPLYAGSTV---EFMPKFSVRG-IWQrwresypqdqTKADDAVTVFTGVPTMytrlI 358
Cdd:cd17634 272 GPGDIYWCTADVGWVTGHSYLLYGPLACGATTllyEGVPNWPTPArMWQ----------VVDKHGVNILYTAPTA----I 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 359 QGYEAMDP-ALQTASATAARQLrlmmcGSSALPL-PvmQKWETITGHVLLER------YGMTEFVMAISNPLKGKR--KG 428
Cdd:cd17634 338 RALMAAGDdAIEGTDRSSLRIL-----GSVGEPInP--EAYEWYWKKIGKEKcpvvdtWWQTETGGFMITPLPGAIelKA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 429 GTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKS--PSLFKEYWNLPEVTKQSFID--GGFFKTGDAARVDEDGYYVILG 503
Cdd:cd17634 411 GSATRPVFGVQPAVVDNEGhPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 504 RTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkrEEELKPALTlEELSMWAKEK 583
Cdd:cd17634 491 RSD-DVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNH------GVEPSPELY-AELRNWVRKE 562
|
570 580
....*....|....*....|....
gi 747052525 584 LAPYKIPNCLLLWESLPRNAMGKV 607
Cdd:cd17634 563 IGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
234-613 |
2.07e-43 |
|
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: 162.16 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 234 ETEIPHEISGDDpalIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDA---WGYTSTDHFLHCLPLHHVHGLFNALLApLYA 310
Cdd:cd05929 118 ETPIEDEAAGWK---MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgFGPGADSVYLSPAPLYHAAPFRWSMTA-LFM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 311 GSTVEFMPKFSVRGIW---QRWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPA-----LQTASATAArqlrlm 382
Cdd:cd05929 194 GGTLVLMEKFDPEEFLrliERYR-------------VTFAQFVPTMFVRLLKLPEAVRNAydlssLKRVIHAAA------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 383 MCgssalPLPVMQKWETITGHVLLERYGMTEF--VMAIS--NPLKGKrkgGTVGKPLPGVqAKIIAEDGS-CDNVEVGEL 457
Cdd:cd05929 255 PC-----PPWVKEQWIDWGGPIIWEYYGGTEGqgLTIINgeEWLTHP---GSVGRAVLGK-VHILDEDGNeVPPGEIGEV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 458 CIKSPSLFkEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCV 537
Cdd:cd05929 326 YFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 538 LGLPDKDYGEAVCAIIIPNPeikrkrEEELKPALTlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05929 404 VGVPDEELGQRVHAVVQPAP------GADAGTALA-EELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
233-614 |
7.78e-43 |
|
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: 162.73 E-value: 7.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 233 QETEIPHE-ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAW--GYTSTDHFLhCLP-----LHHVHGLFnal 304
Cdd:cd05966 219 QSPECEPEwMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAAT-TFKYvfDYHPDDIYW-CTAdigwiTGHSYIVY--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 305 lAPLYAGSTV---EFMPKFSVRGIW----QRWResypqdqtkaddaVTVFTGVPTmytrLIQGYEAMDPALQTASATAar 377
Cdd:cd05966 294 -GPLANGATTvmfEGTPTYPDPGRYwdivEKHK-------------VTIFYTAPT----AIRALMKFGDEWVKKHDLS-- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 378 QLRLMmcGSSALPL-PVMQKW--ETItGH---VLLERYGMTEFVMAISNPLKGKR--KGGTVGKPLPGVQAKIIAEDGS- 448
Cdd:cd05966 354 SLRVL--GSVGEPInPEAWMWyyEVI-GKercPIVDTWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAILDEEGNe 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 449 CDNVEVGELCIKS--PSLFKEYWNLPEVTKQSFI--DGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEA 524
Cdd:cd05966 431 VEGEVEGYLVIKRpwPGMARTIYGDHERYEDTYFskFPGYYFTGDGARRDEDGYYWITGRVD-DVINVSGHRLGTAEVES 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 525 VLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeiKRKREEELKpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAM 604
Cdd:cd05966 510 ALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKD--GEEPSDELR-----KELRKHVRKEIGPIATPDKIQFVPGLPKTRS 582
|
410
....*....|
gi 747052525 605 GKVNKKELKK 614
Cdd:cd05966 583 GKIMRRILRK 592
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
245-619 |
1.51e-42 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 159.39 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALI-IYTSGTTGKPKGVVHTHKGVLAQVQMLTDawgytstdHF----LHC---LPLHHVHGLFNALLAPLYAGstvef 316
Cdd:PRK07445 120 ETGWImIPTGGSSGQIRFAIHTWETLTASVQGFQR--------YFqlqqVNSfcvLPLYHVSGLMQFMRSFLTGG----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 mpKFSVrgiwQRWR--ESYPQDQTKADDAVTVFtgVPTMYTRLIQGYeamdpalqtasATAARQLRLMMCGSSalplPVm 394
Cdd:PRK07445 187 --KLVI----LPYKrlKSGQELPPNPSDFFLSL--VPTQLQRLLQLR-----------PQWLAQFRTILLGGA----PA- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 qkWETitghvLLER-----------YGMTEFVMAISN--P---LKGKRkggTVGKPLPGVQAKIIAEDgscdnveVGELC 458
Cdd:PRK07445 243 --WPS-----LLEQarqlqlrlaptYGMTETASQIATlkPddfLAGNN---SSGQVLPHAQITIPANQ-------TGNIT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKSPSLFKEYWnlPevtkQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIMKvGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:PRK07445 306 IQAQSLALGYY--P----QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 539 GLPDKDYGEAVCAIIIPNPeikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK07445 379 GLPDPHWGEVVTAIYVPKD-----------PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
.
gi 747052525 619 Q 619
Cdd:PRK07445 448 R 448
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
133-612 |
3.59e-42 |
|
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: 158.37 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDsditmilstedhqelmkaiavktsAQMSLLPSVPsvs 212
Cdd:cd17644 53 VGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILED------------------------AQISVLLTQP--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 tksteldhtingeldgtrclqeteipheisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCL 292
Cdd:cd17644 106 -------------------------------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 293 PLHhvhglFNA----LLAPLYAGSTVEFMPKFSVRGIWQRWreSYPQDQTkaddaVTVFTGVPTMYTRLIQgyeamdpAL 368
Cdd:cd17644 155 SIA-----FDVaaeeIYVTLLSGATLVLRPEEMRSSLEDFV--QYIQQWQ-----LTVLSLPPAYWHLLVL-------EL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 369 QTASATAARQLRLMMCGSSALPLPVMQKWETITGHV--LLERYGMTEFVMA-----ISNPLKGKRKGGTVGKPLPGVQAK 441
Cdd:cd17644 216 LLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFiqLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 442 IIAEDGSCDNVEV-GELCIKSPSLFKEYWNLPEVTKQSFIDGGF--------FKTGDAARVDEDGYYVILGRTNADImKV 512
Cdd:cd17644 296 ILDENLQPVPVGVpGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQV-KI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 513 GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPnpeikrKREEELKPaltlEELSMWAKEKLAPYKIPNC 592
Cdd:cd17644 375 RGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP------HYEESPST----VELRQFLKAKLPDYMIPSA 444
|
490 500
....*....|....*....|
gi 747052525 593 LLLWESLPRNAMGKVNKKEL 612
Cdd:cd17644 445 FVVLEELPLTPNGKIDRRAL 464
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
245-607 |
9.60e-42 |
|
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: 153.72 E-value: 9.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLApLYAGSTVEFMPKFSVRG 324
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IWqRWRESYpqdqtkaddAVTVFTGVPTMYTRLIQGYEAMDPalqtasataarqLRLMMCGSSALPLPVMQKWETITGH- 403
Cdd:cd17633 80 WI-RKINQY---------NATVIYLVPTMLQALARTLEPESK------------IKSIFSSGQKLFESTKKKLKNIFPKa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTE--FVMAISNplKGKRKGGTVGKPLPGVQAKIIAEDGScdnvEVGELCIKSPSLFKEYWNLPEVTKqsfid 481
Cdd:cd17633 138 NLIEFYGTSElsFITYNFN--QESRPPNSVGRPFPNVEIEIRNADGG----EIGKIFVKSEMVFSGYVRGGFSNP----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNpeikr 561
Cdd:cd17633 207 DGWMSVGDIGYVDEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD----- 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 747052525 562 kreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKV 607
Cdd:cd17633 281 --------KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
130-617 |
3.12e-41 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 157.06 E-value: 3.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGV---AVPLalsYPEAELLHVMNDSDITMILStedhqelmKAIAVKTSAQMSLLP 206
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGAVtttANPF---YTPAEIAKQAKASGAKLIIT--------QSCYVDKLKGLAEDD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 207 SVPSVstksteldhTINGELDGtrCLQ--------ETEIPH-EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT 277
Cdd:PLN02246 144 GVTVV---------TIDDPPEG--CLHfseltqadENELPEvEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 278 DA----WGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKF---SVRGIWQRWResypqdqtkaddaVTVFTGV 350
Cdd:PLN02246 213 DGenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFeigALLELIQRHK-------------VTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 351 PTMYTrliqgyeamdpALQTASATAARQL---RLMMCGssALPL------PVMQKwetITGHVLLERYGMTEF--VMAIS 419
Cdd:PLN02246 280 PPIVL-----------AIAKSPVVEKYDLssiRMVLSG--AAPLgkeledAFRAK---LPNAVLGQGYGMTEAgpVLAMC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 420 -----NPLkgKRKGGTVGKPLPGVQAKIIAEDGSCD---NVEvGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAA 491
Cdd:PLN02246 344 lafakEPF--PVKSGSCGTVVRNAELKIVDPETGASlprNQP-GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 492 RVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKrkreeelkpaL 571
Cdd:PLN02246 421 YIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSE----------I 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 747052525 572 TLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLA 617
Cdd:PLN02246 490 TEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLA 535
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
244-614 |
4.64e-41 |
|
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: 155.92 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGV-LAQVQMLTdAWGYTSTDHFLHCLPLHHVHGLFNALlAPLYAGSTVEFMPKFSV 322
Cdd:cd12118 133 WDPIALNYTSGTTGRPKGVVYHHRGAyLNALANIL-EWEMKQHPVYLWTLPMFHCNGWCFPW-TVAAVGGTNVCLRKVDA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RGIWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIqgyEAMDPALQTASATAArqlrlMMCGSSALPLPVMQKWETITG 402
Cdd:cd12118 211 KAIYDLIEK----------HKVTHFCGAPTVLNMLA---NAPPSDARPLPHRVH-----VMTAGAPPPAAVLAKMEELGF 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 403 HVLlERYGMTEfvmaISNPlkgkrkgGTVG--KP----LPGV-QAKIIAEDG--------------------SCDNVEVG 455
Cdd:cd12118 273 DVT-HVYGLTE----TYGP-------ATVCawKPewdeLPTEeRARLKARQGvryvgleevdvldpetmkpvPRDGKTIG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 456 ELCIKSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISEC 535
Cdd:cd12118 341 EIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 536 CVLGLPDKDYGEAVCAIIipnpeikrkreeELKPA--LTLEELSMWAKEKLAPYKIPNCLLLWEsLPRNAMGKVNKKELK 613
Cdd:cd12118 419 AVVARPDEKWGEVPCAFV------------ELKEGakVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
.
gi 747052525 614 K 614
Cdd:cd12118 486 D 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-620 |
5.00e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 160.71 E-value: 5.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 71 LVKAVANRGsisPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLrsvkgngenkhLGGARVGIVAKPSPEFVAGVLGT 150
Cdd:PRK12467 517 LIEAQARQH---PERPALVFGEQVLSYAELNRQANRLAHVLIAAGV-----------GPDVLVGIAVERSIEMVVGLLAV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 151 WFSGGVAVPLALSYPEAELLHVMNDSDITMILStedHQELMKAIAVKTSaqmslLPSVPsvstksteldhtINGELDGTR 230
Cdd:PRK12467 583 LKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT---QSHLLAQLPVPAG-----LRSLC------------LDEPADLLC 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 231 CLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhHVHGLFNALLAPLYA 310
Cdd:PRK12467 643 GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALAS 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 311 GSTVEFMPKFSVRGiwqrwresyPQD--QTKADDAVTVFTGVPTMYTRLiqgyeamdpaLQTASATAARQLRLMMCGSSA 388
Cdd:PRK12467 722 GATLHLLPPDCARD---------AEAfaALMADQGVTVLKIVPSHLQAL----------LQASRVALPRPQRALVCGGEA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 389 LPLPVMQKW-ETITGHVLLERYGMTEFVMAISN-PLKGK---RKGGTVGKPLPGVQAKIIaeDGSCDNVEV---GELCIK 460
Cdd:PRK12467 783 LQVDLLARVrALGPGARLINHYGPTETTVGVSTyELSDEerdFGNVPIGQPLANLGLYIL--DHYLNPVPVgvvGELYIG 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFI------DGG-FFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTIS 533
Cdd:PRK12467 861 GAGLARGYHRRPALTAERFVpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVR 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 534 ECCVLGLPDkDYGEAVCAIIIPNPEIkrkreEELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK12467 940 EAVVLAQPG-DAGLQLVAYLVPAAVA-----DGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP 1013
|
....*..
gi 747052525 614 KQLADQV 620
Cdd:PRK12467 1014 KPDASAV 1020
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
75-614 |
9.71e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 159.94 E-value: 9.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 75 VANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLL----TGADlrsvkgngenkhlggARVGIVAKPSPEFVAGVLGT 150
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLialgVGPE---------------VLVGIAVERSLEMVVGLLAI 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 151 WFSGGVAVPLALSYPEAELLHVMNDSDITMILstedhqelmkaiavktsAQMSLLPSVPSVS-TKSTELDHtINGELDGT 229
Cdd:PRK12467 1645 LKAGGAYVPLDPEYPRERLAYMIEDSGIELLL-----------------TQSHLQARLPLPDgLRSLVLDQ-EDDWLEGY 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 230 rclQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLH---HVHGLFnallA 306
Cdd:PRK12467 1707 ---SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAfdvSVWELF----W 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 307 PLYAGSTVEFMPKfsvrGIWQRWRESYpqdQTKADDAVTVFTGVPTMYTRLIQgyeaMDPALqtasaTAARQLRLMMCGS 386
Cdd:PRK12467 1780 PLINGARLVIAPP----GAHRDPEQLI---QLIERQQVTTLHFVPSMLQQLLQ----MDEQV-----EHPLSLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 387 SALPLPVMQKW-ETITGHVLLERYGMTEFVMAIS------NPLKGkRKGGTVGKPLPGVQAKIIaeDGSCDNVEV---GE 456
Cdd:PRK12467 1844 EALEVEALRPWlERLPDTGLFNLYGPTETAVDVThwtcrrKDLEG-RDSVPIGQPIANLSTYIL--DASLNPVPIgvaGE 1920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 457 LCIKSPSLFKEYWNLPEVTKQSFI-------DGGFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEH 529
Cdd:PRK12467 1921 LYLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQV-KIRGFRIELGEIEARLREQ 1999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 530 PTISECCVLGLpDKDYGEAVCAIIIPN-PEIKrkrEEELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVN 608
Cdd:PRK12467 2000 GGVREAVVIAQ-DGANGKQLVAYVVPTdPGLV---DDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLD 2075
|
....*.
gi 747052525 609 KKELKK 614
Cdd:PRK12467 2076 RKALPA 2081
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
245-609 |
1.12e-40 |
|
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: 151.26 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKG-VLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVR 323
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 GIWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIQGYEAmdpALQTAsataaRQLRLMMCGSSALPLPVMQKWETITGH 403
Cdd:cd17635 82 SLFKILTT----------NAVTTTCLVPTLLSKLVSELKS---ANATV-----PSLRLIGYGGSRAIAADVRFIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTEFVMAISNPL-KGKRKGGTVGKPLPGVQAKIIAEDG-SCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFID 481
Cdd:cd17635 144 NTAQVYGLSETGTALCLPTdDDSIEINAVGRPYPGVDVYLAATDGiAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GgFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKR 561
Cdd:cd17635 224 G-WVNTGDLGERREDGFLFITGRS-SESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 747052525 562 KREEELKPALTLEelsmwakekLAPYKIPNCLLLWESLPRNAMGKVNK 609
Cdd:cd17635 302 NAIRALKHTIRRE---------LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
75-614 |
2.32e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 158.97 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 75 VANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvKGNGENkhlggARVGIVAKPSPEFVAGVLGTWFSG 154
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIA------RGVGPE-----VLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 155 GVAVPLALSYPEAELLHVMNDSDITMILStedhqelmkaiavktsaQMSLLPSVPSVS-TKSTELDHTinGELDGtrcLQ 233
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLT-----------------QSHLLQRLPIPDgLASLALDRD--EDWEG---FP 4683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 234 ETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhHVHGLFNALLAPLYAGST 313
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGAS 4762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 314 VEFMPKfsvrGIWQrwRESYPQDQTKADDAVTVFTgvPTMYTRLIQGYE-AMDPAlqtasataarQLRLMMCGSSALPLP 392
Cdd:PRK12316 4763 VVIRDD----SLWD--PERLYAEIHEHRVTVLVFP--PVYLQQLAEHAErDGEPP----------SLRVYCFGGEAVAQA 4824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 393 VMQKWETITGHV-LLERYGMTEfvmAISNPLKGKRKGGT--------VGKPLPGVQAKIIaeDGSCDNVEV---GELCIK 460
Cdd:PRK12316 4825 SYDLAWRALKPVyLFNGYGPTE---TTVTVLLWKARDGDacgaaympIGTPLGNRSGYVL--DGQLNPLPVgvaGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTIS 533
Cdd:PRK12316 4900 GEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQV-KIRGFRIELGEIEARLREHPAVR 4978
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 534 ECCVLGLPDKdYGEAVCAIIIPN-------PEIKRKREEELKPALtleelsmwaKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:PRK12316 4979 EAVVIAQEGA-VGKQLVGYVVPQdpaladaDEAQAELRDELKAAL---------RERLPEYMVPAHLVFLARMPLTPNGK 5048
|
....*...
gi 747052525 607 VNKKELKK 614
Cdd:PRK12316 5049 LDRKALPQ 5056
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
68-612 |
3.21e-40 |
|
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: 153.43 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRgsiSPESIAVTAHEKSH--SYHQLIlsaVKISNLLTGADLRSVKGngenkhlgGARVGIVAKPSPEFVA 145
Cdd:cd05923 3 VFEMLRRAASR---APDACAIADPARGLrlTYSELR---ARIEAVAARLHARGLRP--------GQRVAVVLPNSVEAVI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 146 GVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDhQELMKAIAVKTSAQMSLlpsvpsvstksteldhtinGE 225
Cdd:cd05923 69 ALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD-AQVMDAIFQSGVRVLAL-------------------SD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 226 LDGTR--CLQETEIPHEISG-DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDH--FLHCLPLHHVHGL 300
Cdd:cd05923 129 LVGLGepESAGPLIEDPPREpEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHnvVLGLMPLYHVIGF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 301 FNALLAPLYAGSTvefmpkfsvrgiWQRWRESYPQDQTKADDA--VTVFTGVPTMYTRLIqgyeamdpALQTASATAARQ 378
Cdd:cd05923 209 FAVLVAALALDGT------------YVVVEEFDPADALKLIEQerVTSLFATPTHLDALA--------AAAEFAGLKLSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 379 LRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPlkgKRKGGTVGKPLPGVQAKIIAEDGSCD----NVEV 454
Cdd:cd05923 269 LRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVRIGGSPDealaNGEE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 455 GELCIK--SPSLFKEYWNLPEVTKQSFIDGGFFkTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTI 532
Cdd:cd05923 346 GELIVAaaADAAFTGYLNQPEATAKKLQDGWYR-TGDVGYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 533 SECCVLGLPDKDYGEAVCAIIIPNPeikrkreeelkPALTLEELSMWAKE-KLAPYKIPNCLLLWESLPRNAMGKVNKKE 611
Cdd:cd05923 424 TEVVVIGVADERWGQSVTACVVPRE-----------GTLSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQ 492
|
.
gi 747052525 612 L 612
Cdd:cd05923 493 L 493
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
248-613 |
5.86e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 153.76 E-value: 5.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 248 LIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTV---EFMPKFSVRG 324
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVtrrRFDPEATLDL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IwqrwresypqDQTKAddavTVFTGVPTMYTRLiqgyeaMDPALQTASATAARQLRLMMCGSSALPLPVMQKWETITGHV 404
Cdd:PRK13382 280 I----------DRHRA----TGLAVVPVMFDRI------MDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 405 LLERYGMTEFVM-AISNPLKGKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYwnLPEVTKQsFIDG 482
Cdd:PRK13382 340 IYNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRILDQDFReVPTGEVGTIFVRNDTQFDGY--TSGSTKD-FHDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 483 gFFKTGDAARVDEDGYYVILGRTnaDIMKV-GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkr 561
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRD--DEMIVsGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA-- 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 747052525 562 kreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PRK13382 492 --------SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-620 |
1.86e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 156.27 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLILSAvkisNLLTGAdLRSvKGNGEnkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:PRK12316 524 TPEAPALAFGEETLDYAELNRRA----NRLAHA-LIE-RGVGP-----DVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILStedhqelmkaiavktsaQMSLLPSVP-SVSTKSTELDHtINGELDGtrclQETEIPH- 239
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLS-----------------QSHLGRKLPlAAGVQVLDLDR-PAAWLEG----YSEENPGt 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglFNA----LLAPLYAGSTVE 315
Cdd:PRK12316 651 ELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFS-----FDVsvweFFWPLMSGARLV 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 316 FMPKFSVRGIWQRWresypqdQTKADDAVTVFTGVPTMytrlIQGYeamdpaLQTASATAARQLRLMMCGSSALPLPVMQ 395
Cdd:PRK12316 726 VAAPGDHRDPAKLV-------ELINREGVDTLHFVPSM----LQAF------LQDEDVASCTSLRRIVCSGEALPADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWETI--TGHvLLERYGMTEFVMAISNPLKGKRKGGTV--GKPLPGVQAKIIaeDGSCDNVEV---GELCIKSPSLFKEY 468
Cdd:PRK12316 789 QVFAKlpQAG-LYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYIL--DANLEPVPVgvlGELYLAGRGLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 469 WNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPd 542
Cdd:PRK12316 866 HGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 943
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 543 kdyGEAVCAIIIPnpeikrkreeELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PRK12316 944 ---GKQLVGYVVL----------ESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVA 1008
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
132-614 |
6.66e-39 |
|
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: 150.37 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 132 RVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEdhQELMKAIAVKtsaqmSLLPSVPSV 211
Cdd:cd17642 71 RIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK--KGLQKVLNVQ-----KKLKIIKTI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 212 STKSTELDhtingeLDGTRCLQETEIPHEISG--------------DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT 277
Cdd:cd17642 144 IILDSKED------YKGYQCLYTFITQNLPPGfneydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHAR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 278 D---AWGYTSTDHFLHCLPLHHVHGLFNaLLAPLYAGSTVEFMPKFsvrgiwqrwrESYPQDQTKADDAVTVFTGVPTMY 354
Cdd:cd17642 218 DpifGNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKF----------EEELFLRSLQDYKVQSALLVPTLF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 355 -----TRLIQGYEAMDpalqtasataarqlrLMMCGSSALPLpvmqkwETITGHVLLER---------YGMTEFVMAISN 420
Cdd:cd17642 287 affakSTLVDKYDLSN---------------LHEIASGGAPL------SKEVGEAVAKRfklpgirqgYGLTETTSAILI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 PLKGKRKGGTVGKPLPGVQAKIIAED-GSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGY 498
Cdd:cd17642 346 TPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPnERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGH 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 499 YVILGRTNAdIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIpnpeikrkreEELKPALTLEELSM 578
Cdd:cd17642 426 FFIVDRLKS-LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV----------LEAGKTMTEKEVMD 494
|
490 500 510
....*....|....*....|....*....|....*..
gi 747052525 579 WAKEKLAPYK-IPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd17642 495 YVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
68-612 |
1.03e-38 |
|
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: 148.23 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 68 LMELVKAVANRgsiSPESIAVTAHEKSHSYHQLILSAVKIsnlltGADLRsVKGNGEnkhlgGARVGIVAKPSPEFVAGV 147
Cdd:cd12115 1 LHDLVEAQAAR---TPDAIALVCGDESLTYAELNRRANRL-----AARLR-AAGVGP-----ESRVGVCLERTPDLVVAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 148 LGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeld 227
Cdd:cd12115 67 LAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 228 gtrclqeteipheisGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWG---------YTSTdhflhCLPLHhVH 298
Cdd:cd12115 104 ---------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSaeelagvlaSTSI-----CFDLS-VF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 299 GLFnallAPLYAGSTVefmpkFSVRGIWQRwrESYPqdqtkADDAVTVFTGVPTMYTRLIQgyeamdpalQTASATAARQ 378
Cdd:cd12115 163 ELF----GPLATGGKV-----VLADNVLAL--PDLP-----AAAEVTLINTVPSAAAELLR---------HDALPASVRV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 379 LRLmmcgsSALPLP---VMQKWETITGHVLLERYGMTE-FVMAISNPL-KGKRKGGTVGKPLPGVQAKIIaeDGSCDNV- 452
Cdd:cd12115 218 VNL-----AGEPLPrdlVQRLYARLQVERVVNLYGPSEdTTYSTVAPVpPGASGEVSIGRPLANTQAYVL--DRALQPVp 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 --EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEA 524
Cdd:cd12115 291 lgVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRAD-NQVKVRGFRIELGEIEA 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 525 VLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAM 604
Cdd:cd12115 370 ALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG----------AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPN 439
|
....*...
gi 747052525 605 GKVNKKEL 612
Cdd:cd12115 440 GKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
73-619 |
1.31e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 153.57 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 73 KAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvKGNGEnkhlgGARVGIVAKPSPEFVAGVLGTWF 152
Cdd:PRK12316 2007 QRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA------RGVGP-----EVRVAIAAERSFELVVALLAVLK 2075
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 153 SGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQElmkaiavktsaQMSLLPSVPSvstksteLDHTINGELDGTrcl 232
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE-----------RLPLPAGVAR-------LPLDRDAEWADY--- 2134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 233 QETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhHVHGLFNALLAPLYAGS 312
Cdd:PRK12316 2135 PDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 313 TVEFMPKfsvrGIW---QRWRESYPQdqtkaddAVTVFTGVPTMytrliqgyeamdpaLQTASATAARQ-----LRLMMC 384
Cdd:PRK12316 2214 RVLIRDD----ELWdpeQLYDEMERH-------GVTILDFPPVY--------------LQQLAEHAERDgrppaVRVYCF 2268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 GSSALPLPVMQK-WETITGHVLLERYGMTEfvmAISNPLKGK--------RKGGTVGKPLPGVQAKIIAEDGSCDNVE-V 454
Cdd:PRK12316 2269 GGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLLWKcrpqdpcgAAYVPIGRALGNRRAYILDADLNLLAPGmA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 455 GELCIKSPSLFKEYWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLL 527
Cdd:PRK12316 2346 GELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQV-KIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 528 EHPTISECCVLGLpDKDYGEAVCAIIIPNPEIKrkreeelkpaLTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKV 607
Cdd:PRK12316 2425 AHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAE----------DLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
570
....*....|..
gi 747052525 608 NKKELKKQLADQ 619
Cdd:PRK12316 2494 DRKALPKPDVSQ 2505
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
245-608 |
1.72e-38 |
|
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: 144.75 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVhGLFNALLAPLYAGSTVEFMPKFSVRG 324
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IwqrwresypQDQTKADDAVTVFTGVPTMytrliqgyeamdpaLQTASATAARQLRLmmcgSSALPLPVMQKWE---TIT 401
Cdd:cd17636 80 V---------LELIEAERCTHAFLLPPTI--------------DQIVELNADGLYDL----SSLRSSPAAPEWNdmaTVD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 GHVLLER---YGMTEFV-MAISNPLKGKRKGGTvGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTK 476
Cdd:cd17636 133 TSPWGRKpggYGQTEVMgLATFAALGGGAIGGA-GRPSPLVQVRILDEDGReVPDGEVGEIVARGPTVMAGYWNRPEVNA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 477 QSFIDGGFfKTGDAARVDEDGYYVILGrTNADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPN 556
Cdd:cd17636 212 RRTRGGWH-HTNDLGRREPDGSLSFVG-PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLK 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 747052525 557 PEIkrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVN 608
Cdd:cd17636 290 PGA----------SVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
248-614 |
4.28e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 148.54 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 248 LIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLApLYAGSTVEFMPKF----SVR 323
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFdpeaTLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 GIwqrwresypqDQTKADDAVTVftgvPTMYTRLIQGYEAMDPALQTASataarqLRLMMCGSSALPLPVMQKWETITGH 403
Cdd:PRK07788 290 DI----------AKHKATALVVV----PVMLSRILDLGPEVLAKYDTSS------LKIIFVSGSALSPELATRALEAFGP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGscdNV----EVGELCIKSPSLFKEYWNLPevTKQs 478
Cdd:PRK07788 350 VLYNLYGSTEVaFATIATPEDLAEAPGTVGRPPKGVTVKILDENG---NEvprgVVGRIFVGNGFPFEGYTDGR--DKQ- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 fIDGGFFKTGDAARVDEDGYYVILGRtnADIMKV-GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNP 557
Cdd:PRK07788 424 -IIDGLLSSGDVGYFDEDGLLFVDGR--DDDMIVsGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 558 EikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:PRK07788 501 G----------AALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
96-576 |
1.41e-37 |
|
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: 146.98 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 96 SYHQLILSAVKIsnlltGADLRSVKGNGENKHlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVPLalsY----PEAeLLH 171
Cdd:cd05927 7 SYKEVAERADNI-----GSALRSLGGKPAPAS----FVGIYSINRPEWIISELACYAYSLVTVPL---YdtlgPEA-IEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 172 VMNDSDITMILSTEDhqelmkaiaVKTsaqMSLlpsvpsvstksTELdhtingELDGTRCLQETEIPheiSGDDPALIIY 251
Cdd:cd05927 74 ILNHAEISIVFCDAG---------VKV---YSL-----------EEF------EKLGKKNKVPPPPP---KPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 252 TSGTTGKPKGVVHTHKGVLAQV----QMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLApLYAGSTVefmpkfsvrGIWQ 327
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKI---------GFYS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 328 RwresypQDQTKADDAV----TVFTGVPTMYTRL---IQGYEAMDPALQ-----TASATAARQL---------------- 379
Cdd:cd05927 192 G------DIRLLLDDIKalkpTVFPGVPRVLNRIydkIFNKVQAKGPLKrklfnFALNYKLAELrsgvvraspfwdklvf 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 380 -----------RLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKI--IAED 446
Cdd:cd05927 266 nkikqalggnvRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdVPEM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 447 G--SCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKV--GGYkLSALEI 522
Cdd:cd05927 346 NydAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKK-NIFKLsqGEY-VAPEKI 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 523 EAVLLEHPTISECCVLGLPDKDYgeaVCAIIIPNPE-IKRKREEELKPALTLEEL 576
Cdd:cd05927 424 ENIYARSPFVAQIFVYGDSLKSF---LVAIVVPDPDvLKEWAASKGGGTGSFEEL 475
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-619 |
1.43e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.49 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLILSAVKISNLLTGAdlrsvkGNGENkhlggARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:PRK12316 3070 TPDAVALAFGEQRLSYAELNRRANRLAHRLIER------GVGPD-----VLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILStedhQELMKaiavktsaqmslLPSVPSVSTKSTEldhtingelDGTRCLQETEIPHEI 241
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLS----QSHLR------------LPLAQGVQVLDLD---------RGDENYAEANPAIRT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhHVHGLFNALLAPLYAGSTVefmpkfs 321
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARV------- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 322 VRGIWQRWRESYPQDQTKADDAVTVFTGVPTMYTRLiqgyeamdpaLQTASATAARQLRLMMCGSSALPLPVMQKWetIT 401
Cdd:PRK12316 3266 VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF----------LEEEDAHRCTSLKRIVCGGEALPADLQQQV--FA 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 GHVLLERYGMTEFVMAISNPLKGKRKGGT--VGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVTKQS 478
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVgALGELYLGGEGLARGYHNRPGLTAER 3413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FIDGGF------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGlpdkDYGEAVCAI 552
Cdd:PRK12316 3414 FVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQV-KIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAY 3488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 553 IIPNPEIKRKReEELKPALtleelsmwaKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PRK12316 3489 VVPEDEAGDLR-EALKAHL---------KASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
238-614 |
1.70e-37 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 147.78 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAW--GYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTV- 314
Cdd:TIGR02188 231 PEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAM-TMKYvfDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTv 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 315 --EFMPKFSVRGIWQRWRESYpqdqtkaddAVTVFTGVPTMyTRLIQGYEAMDPALQTASAtaarqLRLMmcGSSALPL- 391
Cdd:TIGR02188 310 mfEGVPTYPDPGRFWEIIEKH---------KVTIFYTAPTA-IRALMRLGDEWVKKHDLSS-----LRLL--GSVGEPIn 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 392 PVMQKW-ETITGH---VLLERYGMTEFVMAISNPLKG--KRKGGTVGKPLPGVQAKIIAEDG-SCDNVEV-GELCIKS-- 461
Cdd:TIGR02188 373 PEAWMWyYKVVGKercPIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVDEEGnPVEGPGEgGYLVIKQpw 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSLFKEYWNLPEvtkqSFIDG------GFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISEC 535
Cdd:TIGR02188 453 PGMLRTIYGDHE----RFVDTyfspfpGYYFTGDGARRDKDGYIWITGRVD-DVINVSGHRLGTAEIESALVSHPAVAEA 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 536 CVLGLPDKDYGEAVCAIIIpnpeIKRKREEELKpalTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:TIGR02188 528 AVVGIPDDIKGQAIYAFVT----LKDGYEPDDE---LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRK 599
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
167-615 |
7.74e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 144.06 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 167 AELLHVMNDSDITMILSTEDHQELMKAiavktsaqmsLLPSVPSVSTkstELDHTINGELDG-------TRCLQETEIPH 239
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARA----------LLKQCPGVRH---RLVLDGDGELEGfvgyaeaVAGLPATPIAD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDpalIIYTSGTTGKPKGV--------VHTHKGVLAQVQMLtdaWGYTSTDHFLHCLPLHHVhglfnallAPLYA- 310
Cdd:PRK13391 153 ESLGTD---MLYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHS--------APQRAv 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 311 ------GSTVEFMPKF----SVRGIwQRWRESYPQdqtkaddavtvftGVPTMYTRLIQGYEAMDPALQTASATAARQlr 380
Cdd:PRK13391 219 mlvirlGGTVIVMEHFdaeqYLALI-EEYGVTHTQ-------------LVPTMFSRMLKLPEEVRDKYDLSSLEVAIH-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 381 lmmcgsSALPLPVMQKWETIT--GHVLLERYGMTE--FVMAISNPLKGKRKGgTVGKPLPGVqAKIIAEDGS-CDNVEVG 455
Cdd:PRK13391 283 ------AAAPCPPQVKEQMIDwwGPIIHEYYAATEglGFTACDSEEWLAHPG-TVGRAMFGD-LHILDDDGAeLPPGEPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 456 ELCIKSPSLFkEYWNLPEVTKQS-FIDGGFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISE 534
Cdd:PRK13391 355 TIWFEGGRPF-EYLNDPAKTAEArHPDGTWSTVGDIGYVDEDGYLYLTDRA-AFMIISGGVNIYPQEAENLLITHPKVAD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 535 CCVLGLPDKDYGEAVCAIIIPNPEIkrkreeELKPALTlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:PRK13391 433 AAVFGVPNEDLGEEVKAVVQPVDGV------DPGPALA-AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
.
gi 747052525 615 Q 615
Cdd:PRK13391 506 R 506
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
240-614 |
1.85e-36 |
|
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: 142.50 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHV------HGLFNALLAPLYagST 313
Cdd:cd17640 84 ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSyersaeYFIFACGCSQAY--TS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 314 VEFMPKfsvrgIWQRWResyPQdqtkaddavtVFTGVPTMYTRLIQGYEAmdpalQTASATAARQ-----------LRLM 382
Cdd:cd17640 162 IRTLKD-----DLKRVK---PH----------YIVSVPRLWESLYSGIQK-----QVSKSSPIKQflflfflsggiFKFG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 383 MCGSSALPLPVMQKWETItGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGScdNV----EVGELC 458
Cdd:cd17640 219 ISGGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGN--VVlppgEKGIVW 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIMKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:cd17640 296 VRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 539 GLPDKDYGeavcAIIIPNpeikrkreeelkpaltLEELSMWAKEKlaPYKIPNCLLLWESlprnamgkvNKKELKK 614
Cdd:cd17640 376 GQDQKRLG----ALIVPN----------------FEELEKWAKES--GVKLANDRSQLLA---------SKKVLKL 420
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
244-619 |
1.91e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 139.80 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTdhFLHCLPLHHVHGLfNALLAPLYAGST---VEFMPKF 320
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQ--WLLALPAHHIAGL-QVLVRSVIAGSEpveLDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 321 SvrgiwqrwresyPQDQTKADDAVtvftGVPTMYTRLIqgyeAM--DPALQTASATAA-RQLRLMMCGSSALPLPVMQKW 397
Cdd:PRK07824 112 D------------PTALPRAVAEL----GGGRRYTSLV----PMqlAKALDDPAATAAlAELDAVLVGGGPAPAPVLDAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 ETItGHVLLERYGMTEfvmaisnplkgkRKGGTV--GKPLPGVQAKIiaEDGscdNVEVGelcikSPSLFKEYWNLPEvt 475
Cdd:PRK07824 172 AAA-GINVVRTYGMSE------------TSGGCVydGVPLDGVRVRV--EDG---RIALG-----GPTLAKGYRNPVD-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 476 KQSFIDGGFFKTGDAARVDeDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIP 555
Cdd:PRK07824 227 PDPFAEPGWFRTDDLGALD-DGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 556 NPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PRK07824 305 DGG----------PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
237-614 |
5.65e-36 |
|
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: 143.22 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 237 IPHE---ISGDDPALIIYTSGTTGKPKGVVHTHKG-VLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGS 312
Cdd:cd05967 220 EPVDcvpVAATDPLYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 313 TVEFMPKFSVR----GIWQRWRESYpqdQTKAddavtVFTgVPTMYtRLIQGYeamDPALQTASATAARQLRLMMCGSSA 388
Cdd:cd05967 300 TTVLYEGKPVGtpdpGAFWRVIEKY---QVNA-----LFT-APTAI-RAIRKE---DPDGKYIKKYDLSSLRTLFLAGER 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 389 LPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKR----KGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIK--- 460
Cdd:cd05967 367 LDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLDEDGEpVGPNELGNIVIKlpl 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFI--DGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:cd05967 447 PPGCLLTLWKNDERFKKLYLskFPGYYDTGDAGYKDEDGYLFIMGRTD-DVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 539 GLPDKDYGEAVCAIIIPNPEIKRKREEELKpaltleELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKITAEELEK------ELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
133-615 |
9.41e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 141.36 E-value: 9.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKaiavktsaqmSLLPSVPSVS 212
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLD----------GLDPGVRVIN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 TKSTELDHTINGELDgtrclqeTEIPH-EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHC 291
Cdd:PRK07867 127 VDSPAWADELAAHRD-------AEPPFrVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 292 LPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWREsYpqdqtkaddAVTVFT--GVPTMYtrLIQGYEAMDPALQ 369
Cdd:PRK07867 200 MPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRR-Y---------GATYANyvGKPLSY--VLATPERPDDADN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 370 TasataarqLRLMMcGSSALPlPVMQKWETITGHVLLERYGMTEFVMAISnplkgkRKGGT----VGKPLPGVQ------ 439
Cdd:PRK07867 268 P--------LRIVY-GNEGAP-GDIARFARRFGCVVVDGFGSTEGGVAIT------RTPDTppgaLGPLPPGVAivdpdt 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 440 ------AKIIAEDGSCDNVEVGELC-IKSPSLFKEYWNLPEVTKQSfIDGGFFKTGDAARVDEDGYYVILGRTnADIMKV 512
Cdd:PRK07867 332 gtecppAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER-MRGGVYWSGDLAYRDADGYAYFAGRL-GDWMRV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 513 GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeELKPALTLEELSmwAKEKLAPYKIPNC 592
Cdd:PRK07867 410 DGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGA------KFDPDAFAEFLA--AQPDLGPKQWPSY 481
|
490 500
....*....|....*....|...
gi 747052525 593 LLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK07867 482 VRVCAELPRTATFKVLKRQLSAE 504
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
251-618 |
1.34e-35 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 141.04 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 251 YTSGTTGKPKGVVHTHKG-VL-AQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVefMPKFSVRG--IW 326
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnVLhALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLV--MPGAKLDGasVY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 327 QRWresypqDQTKaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGHVLl 406
Cdd:PRK06018 262 ELL------DTEK----VTFTAGVPTVWLMLLQYMEKEGLKLPH--------LKMVVCGGSAMPRSMIKAFEDMGVEVR- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 407 ERYGMTEF-----VMAISNP---LKGKRK---GGTVGKPLPGVQAKIIAEDGS---CDNVEVGELCIKSPSLFKEYWnlp 472
Cdd:PRK06018 323 HAWGMTEMsplgtLAALKPPfskLPGDARldvLQKQGYPPFGVEMKITDDAGKelpWDGKTFGRLKVRGPAVAAAYY--- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 473 EVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAI 552
Cdd:PRK06018 400 RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSK-DVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLI 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 553 IIPNPEIKRKREEELKpaltleelsmWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK06018 479 VQLKPGETATREEILK----------YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
83-612 |
1.91e-35 |
|
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: 138.84 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGadlRSVKGNgenkhlggARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRG---KGVKPD--------DQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILStedhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheiS 242
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT----------------------------------------------------------N 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLhclplhhVHGLFNallaplYAGSTVEFMPKFSV 322
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSL-------VYASFS------FDASAWEIFPHLTA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RGIWQRWRESYPQDQTKADD-----AVTVfTGVPTmytRLIQGYEAMDpalqtasataARQLRLMMCGSSALPLPVMQkw 397
Cdd:cd17645 170 GAALHVVPSERRLDLDALNDyfnqeGITI-SFLPT---GAAEQFMQLD----------NQSLRVLLTGGDKLKKIERK-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 etitGHVLLERYGMTE-FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNVEV-GELCIKSPSLFKEYWNLPEVT 475
Cdd:cd17645 234 ----GYKLVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVaGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 476 KQSFIDGGF------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAV 549
Cdd:cd17645 310 AEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQV-KIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 550 CAIIIPnpeikrkrEEELKPaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17645 389 VAYVTA--------PEEIPH----EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
82-612 |
3.49e-35 |
|
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: 138.76 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLilsaVKISNLLTgadlRSVKGNGENKHlggARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:cd17656 1 TPDAVAVVFENQKLTYREL----NERSNQLA----RFLREKGVKKD---SIVAIMMERSAEMIVGILGILKAGGAFVPID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILSTEDHqelmkaiAVKTSAQMSL-LPSVPSVSTKSTEldhtingeldgtrclqetEIPHE 240
Cdd:cd17656 70 PEYPEERRIYIMLDSGVRVVLTQRHL-------KSKLSFNKSTiLLEDPSISQEDTS------------------NIDYI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLH-CLPLHHV--HGLFNALLAplyaGSTVEFM 317
Cdd:cd17656 125 NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQfATCSFDVcyQEIFSTLLS----GGTLYII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 PKFSVRGIWQRWresypqDQTKADDAVTVFtgVPTMYTRLI-QGYEAMDPALQTAS--ATAARQLRLMMcgssalPLPVM 394
Cdd:cd17656 201 REETKRDVEQLF------DLVKRHNIEVVF--LPVAFLKFIfSEREFINRFPTCVKhiITAGEQLVITN------EFKEM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKWETITGHvllERYGMTE---FVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWN 470
Cdd:cd17656 267 LHEHNVHLH---NHYGPSEthvVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQgIVGELYISGASVARGYLN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 471 LPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKD 544
Cdd:cd17656 344 RQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDK 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 545 YGEAVCAIIIPnpeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17656 423 GEKYLCAYFVM------------EQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
239-614 |
4.25e-35 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 141.99 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 239 HEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP 318
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KfsvrgiwqrwresyPQD-----QTKADDAVTVFTGVPT---MYTRLIQgyeaMDPaLQTASataarqLRLMMCGSSALP 390
Cdd:PRK08633 857 D--------------PTDalgiaKLVAKHRATILLGTPTflrLYLRNKK----LHP-LMFAS------LRLVVAGAEKLK 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 391 LPVMQKWETITGHVLLERYGMTEF--VMAISNP---------LKGKRKgGTVGKPLPGVQAKIIAEDgSCDNVEVGE--- 456
Cdd:PRK08633 912 PEVADAFEEKFGIRILEGYGATETspVASVNLPdvlaadfkrQTGSKE-GSVGMPLPGVAVRIVDPE-TFEELPPGEdgl 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 457 LCIKSPSLFKEYWNLPEVTKQSF--IDG-GFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIE---AVLLEHP 530
Cdd:PRK08633 990 ILIGGPQVMKGYLGDPEKTAEVIkdIDGiGWYVTGDKGHLDEDGFLTITDRY-SRFAKIGGEMVPLGAVEeelAKALGGE 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 531 TIsECCVLGLPDKDYGEAVCAIIIPNPEikrkREEELKPALtleelsmwAKEKLAPYKIPNCLLLWESLPRNAMGKVNKK 610
Cdd:PRK08633 1069 EV-VFAVTAVPDEKKGEKLVVLHTCGAE----DVEELKRAI--------KESGLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
....
gi 747052525 611 ELKK 614
Cdd:PRK08633 1136 GLKE 1139
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
71-616 |
1.74e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 137.80 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 71 LVKAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGT 150
Cdd:cd05906 16 LLRAAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRP-----------GDSVILQFDDNEDFIPAFWAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 151 WFSGGVAVPL--ALSYPEAE-----LLHVMNDSDITMILSTEDHQELMKAIAVKTSAQMSLLPSVPSVStksteldhtin 223
Cdd:cd05906 85 VLAGFVPAPLtvPPTYDEPNarlrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELL----------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 224 geldgtRCLQETEIPHEiSGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNA 303
Cdd:cd05906 154 ------DTAADHDLPQS-RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 304 LLAPLYAGS------TVEFM--PKfsvrgIWQRWRESYPQDQTKAddavtvftgvPT-MYTRLIQGYEAMDPalQTASAT 374
Cdd:cd05906 227 HLRAVYLGCqqvhvpTEEILadPL-----RWLDLIDRYRVTITWA----------PNfAFALLNDLLEEIED--GTWDLS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 375 AarqLRLMMCGSSALPLPVMQKwetITGhvLLERY-----------GMTEFVMAI---SNPLKGKRKGGT----VGKPLP 436
Cdd:cd05906 290 S---LRYLVNAGEAVVAKTIRR---LLR--LLEPYglppdairpafGMTETCSGViysRSFPTYDHSQALefvsLGRPIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 437 GVQAKIIAEDGSC-DNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDeDGYYVILGRTnADIMKVGGY 515
Cdd:cd05906 362 GVSMRIVDDEGQLlPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRT-KDTIIVNGV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 516 KLSALEIEAVLLEHP--TISECCVLGLPDKDYGEAVCAIIIpNPEIKRkreeELKPALTLEELSMWAKEK--LAP-YKIP 590
Cdd:cd05906 440 NYYSHEIEAAVEEVPgvEPSFTAAFAVRDPGAETEELAIFF-VPEYDL----QDALSETLRAIRSVVSREvgVSPaYLIP 514
|
570 580
....*....|....*....|....*.
gi 747052525 591 nclLLWESLPRNAMGKVNKKELKKQL 616
Cdd:cd05906 515 ---LPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
91-613 |
1.82e-34 |
|
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: 138.39 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 91 HEKSHSYHQLILSAVKISNLLtgadlrsvkgngenKHLG---GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEA 167
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGL--------------RALGvgkGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 168 ELLHVMNDSDITMILSTE-----DHQELMKAIAVKTSAQMSLLPSVPSVSTKSTELDHTINGELDGTRcLQETEIPH--E 240
Cdd:cd05968 154 AAATRLQDAEAKALITADgftrrGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDE-EKETAGDGaeR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGV-LAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFnALLAPLYAGSTV---EF 316
Cdd:cd05968 233 TESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMvlyDG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 MPKFSVRGiwQRWResypqdqTKADDAVTVFTGVPTMYTRLIQGYEAmdpalqTASATAARQLRLMmcGSSALPL---PV 393
Cdd:cd05968 312 APDHPKAD--RLWR-------MVEDHEITHLGLSPTLIRALKPRGDA------PVNAHDLSSLRVL--GSTGEPWnpePW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETI-TGHVLLERY-GMTEFVMAI--SNPLKgKRKGGTVGKPLPGVQAKIIAEDGSCDNVEVGELCIKSP--SLFKE 467
Cdd:cd05968 375 NWLFETVgKGRNPIINYsGGTEISGGIlgNVLIK-PIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPwpGMTRG 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFID--GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDY 545
Cdd:cd05968 454 FWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSD-DTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVK 532
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 546 GEAVCAIIIPNPEIKRKreEELKpaltlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05968 533 GEAIVCFVVLKPGVTPT--EALA-----EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
82-618 |
2.36e-34 |
|
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: 136.52 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:cd05918 12 QPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGP-----------GVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILStedhqelmkaiavktsaqmsllpSVPsvstksteldhtingeldgtrclqeteiphei 241
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT-----------------------SSP-------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 sgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHclplhhvhglFNA---------LLAPLYAGS 312
Cdd:cd05918 106 --SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ----------FASytfdvsileIFTTLAAGG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 313 TV-------------EFMpkfsvrgiwQRWResypqdqtkaddaVTVFTGVPTMyTRLIqgyeamDPAlQTASataarqL 379
Cdd:cd05918 174 CLcipseedrlndlaGFI---------NRLR-------------VTWAFLTPSV-ARLL------DPE-DVPS------L 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 380 RLMMCGSSALPLPVMQKWetiTGHV-LLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQakIIAEDGSCDNV----E 453
Cdd:cd05918 218 RTLVLGGEALTQSDVDTW---ADRVrLINAYGPAECtIAATVSPVVPSTDPRNIGRPLGATC--WVVDPDNHDRLvpigA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 454 VGELCIKSPSLFKEYWNLPEVTKQSFID-------------GGFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSAL 520
Cdd:cd05918 293 VGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsgrgRRLYRTGDLVRYNPDGSLEYVGRKDTQV-KIRGQRVELG 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 521 EIEAVLLEH-PTISECCVLGLPDKDYGEA--VCAIIIPNPEIKRKREEELKPALTLEE-------LSMWAKEKLAPYKIP 590
Cdd:cd05918 372 EIEHHLRQSlPGAKEVVVEVVKPKDGSSSpqLVAFVVLDGSSSGSGDGDSLFLEPSDEfralvaeLRSKLRQRLPSYMVP 451
|
570 580
....*....|....*....|....*...
gi 747052525 591 NCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:cd05918 452 SVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
228-614 |
3.86e-34 |
|
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: 135.00 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 228 GTRCLQEtEIPHeisGDDPALIIYTSGTTGKPKGVVHTHKGVLAQvQMLTDAW-GYTSTD-HFLHCLPLHHVHGlFNALL 305
Cdd:cd05974 73 AVYAAVD-ENTH---ADDPMLLYFTSGTTSKPKLVEHTHRSYPVG-HLSTMYWiGLKPGDvHWNISSPGWAKHA-WSCFF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 APLYAGSTVEFM--PKFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQgyeamdpalqTASATAARQLRLMM 383
Cdd:cd05974 147 APWNAGATVFLFnyARFDAKRVLA----------ALVRYGVTTLCAPPTVWRMLIQ----------QDLASFDVKLREVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGScdNVEVGELCI---- 459
Cdd:cd05974 207 GAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA--PATEGEVALdlgd 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 460 -KSPSLFKEYWNLPEVTKQSfIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:cd05974 285 tRPVGLMKGYAGDPDKTAHA-MRGGYYRTGDIAMRDEDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVV 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 539 GLPDKDygeavcAIIIPNPEIKRKREEELKPALTLeELSMWAKEKLAPYKIPNCLLLWEsLPRNAMGKVNKKELKK 614
Cdd:cd05974 363 PSPDPV------RLSVPKAFIVLRAGYEPSPETAL-EIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
238-614 |
6.17e-34 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 137.19 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 238 PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMlTDAW--GYTSTDHFL----------HClplHHVHGlfnall 305
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAM-TMKYvfDYKDGDVYWctadvgwvtgHS---YIVYG------ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 aPLYAGSTV---EFMPKFSVRGIWqrWR--ESYpqdqtkaddAVTVFTGVPTMYTRLIQgyEAMDPALQTASATaarqLR 380
Cdd:PRK00174 309 -PLANGATTlmfEGVPNYPDPGRF--WEviDKH---------KVTIFYTAPTAIRALMK--EGDEHPKKYDLSS----LR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 381 LMmcGSSALPL-----------------PVMQK-WETITGHVLlerygmtefvmaISnPLKG--KRKGGTVGKPLPGVQA 440
Cdd:PRK00174 371 LL--GSVGEPInpeawewyykvvggercPIVDTwWQTETGGIM------------IT-PLPGatPLKPGSATRPLPGIQP 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 441 KIIAEDG-SCDNVEVGELCIKS--PSLFKEYWNLPEVTKQSF---IDGGFFkTGDAARVDEDGYYVILGRTNaDIMKVGG 514
Cdd:PRK00174 436 AVVDEEGnPLEGGEGGNLVIKDpwPGMMRTIYGDHERFVKTYfstFKGMYF-TGDGARRDEDGYYWITGRVD-DVLNVSG 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 515 YKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikRKREEELKpaltlEELSMWAKEKLAPYKIPNCLL 594
Cdd:PRK00174 514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGG--EEPSDELR-----KELRNWVRKEIGPIAKPDVIQ 586
|
410 420
....*....|....*....|
gi 747052525 595 LWESLPRNAMGKVNKKELKK 614
Cdd:PRK00174 587 FAPGLPKTRSGKIMRRILRK 606
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
244-619 |
7.06e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 136.03 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGlFNALLAPLYAGSTVEFMPKFsvr 323
Cdd:PRK06164 181 DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAPLVCEPVF--- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 giwqrwrESYPQDQTKADDAVTVFTGVPTMYTRLiqgyeamdpaLQTASATAA-RQLRLMMCGSSALPLPVMQKWETITG 402
Cdd:PRK06164 257 -------DAARTARALRRHRVTHTFGNDEMLRRI----------LDTAGERADfPSARLFGFASFAPALGELAALARARG 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 403 HVLLERYGMTEfVMAI------SNPLKGKRKGGtvGKPL-PGVQAKII-AEDGS-CDNVEVGELCIKSPSLFKEYWNLPE 473
Cdd:PRK06164 320 VPLTGLYGSSE-VQALvalqpaTDPVSVRIEGG--GRPAsPEARVRARdPQDGAlLPDGESGEIEIRAPSLMRGYLDNPD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 474 VTKQSFIDGGFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVcAII 553
Cdd:PRK06164 397 ATARALTDDGYFRTGDLGYTRGDGQFVYQTRM-GDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFV 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 554 IPNPEIkRKREEELKPaltleelsmWAKEKLAPYKIPNCLLLWESLPRNAMG---KVNKKELkKQLADQ 619
Cdd:PRK06164 475 IPTDGA-SPDEAGLMA---------ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL-REMAQA 532
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
87-616 |
1.01e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 135.49 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 87 AVTAheKSHSYHQLILSAVKISNLLTGADLRsvKGngenkhlggaRVGIVAKPS-PEFVAGVLGTWFSGGV---AVPLAL 162
Cdd:PLN02330 50 AVTG--KAVTYGEVVRDTRRFAKALRSLGLR--KG----------QVVVVVLPNvAEYGIVALGIMAAGGVfsgANPTAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 sypEAELLHVMNDSDITMILSTEDHQELMKAIAVktsaqmsllpsvPSVSTKSTELDHTINGE--LDGTRCLQETEIPHE 240
Cdd:PLN02330 116 ---ESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL------------PVIVLGEEKIEGAVNWKelLEAADRAGDTSDNEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQV-----QMLTDAWGYTSTdhfLHCLPLHHVHGLFNALLAPLYAGSTVE 315
Cdd:PLN02330 181 ILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsslfSVGPEMIGQVVT---LGLIPFFHIYGITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 316 FMPKFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQgyeamDPALQTASATAARqLRLMMCGSSALPLPVMQ 395
Cdd:PLN02330 258 VMSRFELRTFLN----------ALITQEVSFAPIVPPIILNLVK-----NPIVEEFDLSKLK-LQAIMTAAAPLAPELLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWET-ITGHVLLERYGMTE---FVMAISNPLKGK--RKGGTVGKPLPGVQAKIIAEDG--SCDNVEVGELCIKSPSLFKE 467
Cdd:PLN02330 322 AFEAkFPGVQVQEAYGLTEhscITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDTgrSLPKNTPGELCVRSQCVMQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:PLN02330 402 YYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 548 AVCAIIIPNPEIKRKREEELKpaltleelsmWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQL 616
Cdd:PLN02330 481 IPAACVVINPKAKESEEDILN----------FVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
130-600 |
1.68e-33 |
|
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: 135.28 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIA--VKTSAQMSLLPS 207
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVleGGTPPRLVVFDH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 208 VPSVSTKSTELD-------------HTINGELDGTRCLQETEIPHEISGDDP-ALIIYTSGTTGKPKGVVHTHkgvlaqv 273
Cdd:cd17632 173 RPEVDAHRAALEsarerlaavgipvTTLTLIAVRGRDLPPAPLFRPEPDDDPlALLIYTSGSTGTPKGAMYTE------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 274 QMLTDAW--------GYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPKFSVRGIWQRWRESYPqdqtkaddavT 345
Cdd:cd17632 246 RLVATFWlkvssiqdIRPPASITLNFMPMSHIAGR-ISLYGTLARGGTAYFAAASDMSTLFDDLALVRP----------T 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 346 VFTGVPTMYTRLIQGYEA-MDPALQ------TASATAARQLR---------LMMCGSSALPlPVMQKW-ETITGHVLLER 408
Cdd:cd17632 315 ELFLVPRVCDMLFQRYQAeLDRRSVagadaeTLAERVKAELRervlggrllAAVCGSAPLS-AEMKAFmESLLDLDLHDG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 409 YGMTEFVMAISNplkgkrkgGTVGKPlPGVQAKIIaedgscDNVEV-----------GELCIKSPSLFKEYWNLPEVTKQ 477
Cdd:cd17632 394 YGSTEAGAVILD--------GVIVRP-PVLDYKLV------DVPELgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 SFIDGGFFKTGDA-ARVDEDgYYVILGRTNADImkvggyKLSALE------IEAVLLEHPTISECCVLGLPDKDYgeaVC 550
Cdd:cd17632 459 VFDEDGFYRTGDVmAELGPD-RLVYVDRRNNVL------KLSQGEfvtvarLEAVFAASPLVRQIFVYGNSERAY---LL 528
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 747052525 551 AIIIPNPEIKRKR-EEELKPALtLEELSMWAKEK-LAPYKIPNCLLLwESLP 600
Cdd:cd17632 529 AVVVPTQDALAGEdTARLRAAL-AESLQRIAREAgLQSYEIPRDFLI-ETEP 578
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
133-615 |
2.52e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 134.38 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAvktsaqmslLPSVPSVS 212
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLD---------LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 TKSTELDHTINGELDgtrclqetEIPH-EISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHC 291
Cdd:PRK13388 126 VDTPAYAELVAAAGA--------LTPHrEVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 292 LPLHHVHGLFnALLAP-LYAGSTVEFMPKFSVRGIWQRWREsYpqdqtkaddAVTVFT--GVPTMYtrLIQGYEAMDpal 368
Cdd:PRK13388 198 MPLFHSNAVM-AGWAPaVASGAAVALPAKFSASGFLDDVRR-Y---------GATYFNyvGKPLAY--ILATPERPD--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 369 qtasaTAARQLRLMMcGSSALPlpvmqkwETIT------GHVLLERYGMTEFVMAISNPLKGKRkgGTVGKPLPGVQ--- 439
Cdd:PRK13388 262 -----DADNPLRVAF-GNEASP-------RDIAefsrrfGCQVEDGYGSSEGAVIVVREPGTPP--GSIGRGAPGVAiyn 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 440 --------AKIIAEDGSCDNVE--VGELCIKS-PSLFKEYWNLPEVTKQSfIDGGFFKTGDAARVDEDGYYVILGRTnAD 508
Cdd:PRK13388 327 petltecaVARFDAHGALLNADeaIGELVNTAgAGFFEGYYNNPEATAER-MRHGMYWSGDLAYRDADGWIYFAGRT-AD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 509 IMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPeikrkrEEELKPALTLEELSmwAKEKLAPYK 588
Cdd:PRK13388 405 WMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD------GATFDPDAFAAFLA--AQPDLGTKA 476
|
490 500
....*....|....*....|....*..
gi 747052525 589 IPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK13388 477 WPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
130-606 |
4.39e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 133.47 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILStedHQELMKAIAvktsaqmSLLPSVP 209
Cdd:PRK07798 53 GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY---EREFAPRVA-------EVLPRLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTINGELDGTRCLQE-------TEIPHEISGDDpALIIYTSGTTGKPKGVVHTH----KGVLAQVQMLTD 278
Cdd:PRK07798 123 KLRTLVVVEDGSGNDLLPGAVDYEDalaagspERDFGERSPDD-LYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 AWGYTSTDH-----------FLHCLPLHHVHGLFNALLApLYAGSTVEFMP--KFSVRGIWQrwresypqdqTKADDAVT 345
Cdd:PRK07798 202 EPIEDEEELakraaagpgmrRFPAPPLMHGAGQWAAFAA-LFSGQTVVLLPdvRFDADEVWR----------TIEREKVN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 346 VFTGVPTMYTR-LIQgyeamdpALQTASATAARQLRLMmcGSSALPL--PVMQKW-ETITGHVLLERYGMTEF-VMAISN 420
Cdd:PRK07798 271 VITIVGDAMARpLLD-------ALEARGPYDLSSLFAI--ASGGALFspSVKEALlELLPNVVLTDSIGSSETgFGGSGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 421 PLKGKRKGG--TVGkplPGVQAKIIAEDGSCdnVEVGELCI----KSPSLFKEYWNLPEVTKQSF--IDGGFFK-TGDAA 491
Cdd:PRK07798 342 VAKGAVHTGgpRFT---IGPRTVVLDEDGNP--VEPGSGEIgwiaRRGHIPLGYYKDPEKTAETFptIDGVRYAiPGDRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 492 RVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelkPAL 571
Cdd:PRK07798 417 RVEADGTITLLGRGSVCI-NTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG----------ARP 485
|
490 500 510
....*....|....*....|....*....|....*
gi 747052525 572 TLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:PRK07798 486 DLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
129-618 |
6.73e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 133.37 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 129 GGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTedhQELMKAIAvktsaqmSLLPSV 208
Cdd:PRK05620 63 GDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD---PRLAEQLG-------EILKEC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 209 PSV-----------STKSTELDHTIN-----GELDGtrclQETEIP-HEISGDDPALIIYTSGTTGKPKGVVHTHKGVLA 271
Cdd:PRK05620 133 PCVravvfigpsdaDSAAAHMPEGIKvysyeALLDG----RSTVYDwPELDETTAAAICYSTGTTGAPKGVVYSHRSLYL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 272 QVQML--TDAWGYTSTDHFLHCLPLHHVHGlFNALLAPLYAGSTVeFMPKFSVrgiwqrwreSYPQ-DQTKADDAVTVFT 348
Cdd:PRK05620 209 QSLSLrtTDSLAVTHGESFLCCVPIYHVLS-WGVPLAAFMSGTPL-VFPGPDL---------SAPTlAKIIATAMPRVAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 349 GVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEfvmaiSNPLkgkrkg 428
Cdd:PRK05620 278 GVPTLWIQLMVHYLKNPPERMS--------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE-----TSPV------ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 429 GTVGKPLPGV-----------QAKI-------IAEDG----SCDNVEvGELCIKSPSLFKEYWNLP-------------- 472
Cdd:PRK05620 339 GTVARPPSGVsgearwayrvsQGRFpasleyrIVNDGqvmeSTDRNE-GEIQVRGNWVTASYYHSPteegggaastfrge 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 473 --EVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVC 550
Cdd:PRK05620 418 dvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPL 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 551 AIIIPNPEIKRKREeelkpalTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK05620 497 AVTVLAPGIEPTRE-------TAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLAD 557
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
83-612 |
1.56e-32 |
|
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: 130.67 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvkgngenkhLGGAR---VGIVAKPSPEFVAGVLGTWFSGGVAVP 159
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRG--------------LGVAPgsvVGVCADRSLDAIVGLLAVLKAGGAYVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 160 LALSYPEAELLHVMNDSDITMILstedhqelmkaiavktsaqmsLLPsvpsvstksteldhtingeldgtrclqeteiph 239
Cdd:cd17650 67 IDPDYPAERLQYMLEDSGAKLLL---------------------TQP--------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 eisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP- 318
Cdd:cd17650 93 ----EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPd 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 --KFSVRGIWQRWRESypqdqtkaddAVTVFTGVPTMYTRLIQ--GYEAMDPAlqtasataarQLRLMMCGSSALPLPvM 394
Cdd:cd17650 169 evKLDPAALYDLILKS----------RITLMESTPALIRPVMAyvYRNGLDLS----------AMRLLIVGSDGCKAQ-D 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKWET---ITGHVLLERYGMTEFVMAIS---NPLKGKRKGGTV--GKPLPGVQAKIIAEDGSCDNVEV-GELCIKSPSLF 465
Cdd:cd17650 228 FKTLAarfGQGMRIINSYGVTEATIDSTyyeEGRDPLGDSANVpiGRPLPNTAMYVLDERLQPQPVGVaGELYIGGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 466 KEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLG 539
Cdd:cd17650 308 RGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGR-VDHQVKIRGFRIELGEIESQLARHPAIDEAVVAV 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 540 LPDKDYGEAVCAIIIPnpeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17650 387 REDKGGEARLCAYVVA------------AATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
241-615 |
2.13e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 132.85 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQ-MLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPk 319
Cdd:PRK06060 142 MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDaMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINS- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGiwqrwrESYPQDQTKADDavTVFTGVPTMYTRLIQGyeamdpalqtASATAARQLRLMMCGSSALPLPVMQKW-E 398
Cdd:PRK06060 221 APVTP------EAAAILSARFGP--SVLYGVPNFFARVIDS----------CSPDSFRSLRCVVSAGEALELGLAERLmE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 TITGHVLLERYGMTEFVMA-ISNPLKGKRKgGTVGKPLPGVQAKIIAEDGSCDNVEV-GELCIKSPSLFKEYWNLPEvtk 476
Cdd:PRK06060 283 FFGGIPILDGIGSTEVGQTfVSNRVDEWRL-GTLGRVLPPYEIRVVAPDGTTAGPGVeGDLWVRGPAIAKGYWNRPD--- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 477 QSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIP- 555
Cdd:PRK06060 359 SPVANEGWLDTRDRVCIDSDGWVTYRCRAD-DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVAt 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 556 -----NPEIKRKREEELkpaLTleelsmwakeKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK06060 438 sgatiDGSVMRDLHRGL---LN----------RLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
251-620 |
5.70e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 130.21 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 251 YTSGTTGKPKGVVHTHKG-VL-AQVQMLTDAWGYTSTDHFLHCLPLHHVH--GLFNAllAPLYAGSTVEFMPKFSVRGIW 326
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStVLhAYGAALPDAMGLSARDAVLPVVPMFHVNawGLPYS--APLTGAKLVLPGPDLDGKSLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 327 qrwrESYPQDQtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVMQKWETITGHVLL 406
Cdd:PRK07008 261 ----ELIEAER------VTFSAGVPTVWLGLLNHMREAGLRFST--------LRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 407 ERYGMTEFV-MAISNPLKGKRKGGTV----------GKPLPGVQAKIIAEDG---SCDNVEVGELCIKSPSLFKEYWNlp 472
Cdd:PRK07008 323 HAWGMTEMSpLGTLCKLKWKHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGrelPWDGKAFGDLQVRGPWVIDRYFR-- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 473 evTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAI 552
Cdd:PRK07008 401 --GDASPLVDGWFPTGDVATIDADGFMQITDRSK-DVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 553 IIPNPEIKRKREEELKpaltleelsmWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PRK07008 478 VVKRPGAEVTREELLA----------FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
130-572 |
4.34e-31 |
|
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: 127.92 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPL-----------ALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKT 198
Cdd:cd17641 36 GDVVAILGDNRPEWVWAELAAQAIGALSLGIyqdsmaeevayLLNYTGARVVIAEDEEQVDKLLEIADRIPSVRYVIYCD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 199 SAQM-----SLLPSVPSVSTKSTELDHTINGELDgtRCLQETeipheiSGDDPALIIYTSGTTGKPKGVVHTHKGVLAQV 273
Cdd:cd17641 116 PRGMrkyddPRLISFEDVVALGRALDRRDPGLYE--REVAAG------KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 274 QMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEF-------MPkfSVRGIWQR--------WRESYPQDQT 338
Cdd:cd17641 188 AAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFpeepetmME--DLREIGPTfvllpprvWEGIAADVRA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 339 KADDAvTVFTGVptMYTRLI-QGYEA---------MDPALQTASATAA-------------RQLRLMMCGSSALPLPVMQ 395
Cdd:cd17641 266 RMMDA-TPFKRF--MFELGMkLGLRAldrgkrgrpVSLWLRLASWLADallfrplrdrlgfSRLRSAATGGAALGPDTFR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWETItGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIaedgscdnvEVGELCIKSPSLFKEYWNLPEVT 475
Cdd:cd17641 343 FFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRID---------EVGEILVRSPGVFVGYYKNPEAT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 476 KQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVG-GYKLSALEIEAVLLEHPTISECCVLGlPDKDYgeaVCAIII 554
Cdd:cd17641 413 AEDFDEDGWLHTGDAGYFKENGHLVVIDRAK-DVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG-AGRPY---LTAFIC 487
|
490
....*....|....*...
gi 747052525 555 PNPEIKRKREEELKPALT 572
Cdd:cd17641 488 IDYAIVGKWAEQRGIAFT 505
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
251-615 |
5.97e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 127.37 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 251 YTSGTTGKPKGVVHTHKG--VLAQVQMLtdAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVeFMPKFSVRGIWQR 328
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNV-CLRKVDPKLIFDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 329 WREsypqdqtkadDAVTVFTGVPTMYTRLIQGYEAMDPALqtasataARQLRLMMCGSsALPLPVMQKWETItGHVLLER 408
Cdd:PRK08162 266 IRE----------HGVTHYCGAPIVLSALINAPAEWRAGI-------DHPVHAMVAGA-APPAAVIAKMEEI-GFDLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 409 YGMTE----------------FVMAISNPLKGKR-------KGGTV-----GKPLPGvqakiiaedgscDNVEVGELCIK 460
Cdd:PRK08162 327 YGLTEtygpatvcawqpewdaLPLDERAQLKARQgvryplqEGVTVldpdtMQPVPA------------DGETIGEIMFR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 461 SPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGL 540
Cdd:PRK08162 395 GNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSK-DIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 541 PDKDYGEAVCAIIipnpeikrkreeELKPALTL--EELSMWAKEKLAPYKIPNCLLLWEsLPRNAMGKVNKKELKKQ 615
Cdd:PRK08162 473 PDPKWGEVPCAFV------------ELKDGASAteEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQ 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
133-614 |
8.94e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.51 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILStedHQELMKAiavktsaqmslLPSVPSVS 212
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT---QAHLLEQ-----------LPAPAGDT 3213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 213 TKSTELDhTINGELDgtRCLQETeipheISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCL 292
Cdd:PRK12467 3214 ALTLDRL-DLNGYSE--NNPSTR-----VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFM 3285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 293 PLHhVHGLFNALLAPLYAGSTVefmpkfSVRGIWQRWRESYPQdQTKADDaVTVFTGVPTMYTRLiqgyeamdpaLQTAS 372
Cdd:PRK12467 3286 SFS-FDGAQERFLWTLICGGCL------VVRDNDLWDPEELWQ-AIHAHR-ISIACFPPAYLQQF----------AEDAG 3346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 373 ATAARQLRLMMCGSSALPLPVMQKWETITGHV-LLERYGMTEfvmAISNPLKGKRKGGTV--------GKPLPGVQAKII 443
Cdd:PRK12467 3347 GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTE---AVVTVTLWKCGGDAVceapyapiGRPVAGRSIYVL 3423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 444 aeDGSCDNVEVG---ELCIKSPSLFKEYWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVG 513
Cdd:PRK12467 3424 --DGQLNPVPVGvagELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQV-KIR 3500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 514 GYKLSALEIEAVLLEHPTISECCVLGLpDKDYGEAVCAIIIPNPEikrkrEEELKpaltlEELSMWAKEKLAPYKIPNCL 593
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADP-----QGDWR-----ETLRDHLAASLPDYMVPAQL 3569
|
490 500
....*....|....*....|.
gi 747052525 594 LLWESLPRNAMGKVNKKELKK 614
Cdd:PRK12467 3570 LVLAAMPLGPNGKVDRKALPD 3590
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-612 |
1.22e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 128.75 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLILSAVKISNLLTGadlrsvKGNGENkhlggARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:PRK05691 1144 TPERIALVWDGGSLDYAELHAQANRLAHYLRD------KGVGPD-----VCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILSTedhqelmkaiavktSAQMSLLPSVPSVSTKSTELDHtingeLDGtrclQETEIPH-E 240
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQ--------------SHLLERLPQAEGVSAIALDSLH-----LDS----WPSQAPGlH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLaPLYAGStvefmpKF 320
Cdd:PRK05691 1270 LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFW-PLITGC------RL 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 321 SVRGIWQRwRESYPQDQTKADDAVTVFTGVPTMYTRLIQgyeamDPAlqtasATAARQLRLMMCGSSALPLP----VMQK 396
Cdd:PRK05691 1343 VLAGPGEH-RDPQRIAELVQQYGVTTLHFVPPLLQLFID-----EPL-----AAACTSLRRLFSGGEALPAElrnrVLQR 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 397 WETITGHvllERYGMTEFVMAISN----PLKGKRKggTVGKPLPGVQAKIIaeDGSCDNVE---VGELCIKSPSLFKEYW 469
Cdd:PRK05691 1412 LPQVQLH---NRYGPTETAINVTHwqcqAEDGERS--PIGRPLGNVLCRVL--DAELNLLPpgvAGELCIGGAGLARGYL 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 470 NLPEVTKQSFI------DGG-FFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLGLPD 542
Cdd:PRK05691 1485 GRPALTAERFVpdplgeDGArLYRTGDRARWNADGALEYLGRLDQQV-KLRGFRVEPEEIQARLLAQPGVAQAAVLVREG 1563
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 543 kdygeAVCAIIIPNPEIKRKREEE---LKPALtleelsmwaKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:PRK05691 1564 -----AAGAQLVGYYTGEAGQEAEaerLKAAL---------AAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
133-539 |
1.32e-30 |
|
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: 126.70 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGVAVP-LALSYPEAeLLHVMNDSDITmILSTEDHQELMKAIAVKTSaqmslLPSVPSV 211
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGiYTTNSPEA-CQYVAETSEAN-ILVVENQKQLQKILQIQDK-----LPHLKAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 212 STKSTEL-DHTIN-----GELDGTRCLQETEIPHEISGDDP---ALIIYTSGTTGKPKGVVHTHKGVL----AQVQMLTD 278
Cdd:cd05933 109 IQYKEPLkEKEPNlyswdEFMELGRSIPDEQLDAIISSQKPnqcCTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 AWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRG-IWQRWRESYPqdqtkaddavTVFTGVPTMYTRL 357
Cdd:cd05933 189 RPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGtLVKTLREVRP----------TAFMGVPRVWEKI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 358 ---IQGYEAMDPALQTASATAAR------QLRLMMcGSSALPLP-------VMQKWETITG----HVLL----------- 406
Cdd:cd05933 259 qekMKAVGAKSGTLKRKIASWAKgvgletNLKLMG-GESPSPLFyrlakklVFKKVRKALGldrcQKFFtgaapisretl 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 407 -----------ERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDgsCDNVevGELCIKSPSLFKEYWNLPEVT 475
Cdd:cd05933 338 efflslnipimELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD--ADGI--GEICFWGRHVFMGYLNMEDKT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 747052525 476 KQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIMKVGGYKLSALEIE-AVLLEHPTISECCVLG 539
Cdd:cd05933 414 EEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEdAVKKELPIISNAMLIG 478
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
130-620 |
1.15e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 124.70 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLH----------VMNDSDITMILStedhqeLMKAIAVKtS 199
Cdd:PTZ00216 146 GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYalreteckaiVCNGKNVPNLLR------LMKSGGMP-N 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 200 AQMSLLPSVP-SVSTKSTELDHTINGELDGTRCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHTH----KGVLAQVQ 274
Cdd:PTZ00216 219 TTIIYLDSLPaSVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHgsltAGILALED 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 275 MLTDAWG-YTSTDHFLHCLPLHHV--HGLFNALLA---------P-----LYA---GSTVEFMPKFsvrgiwqrwresyp 334
Cdd:PTZ00216 299 RLNDLIGpPEEDETYCSYLPLAHImeFGVTNIFLArgaligfgsPrtltdTFArphGDLTEFRPVF-------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 335 qdqtkaddavtvFTGVPTMYTRLIQGYEAMDP-------------------ALQTASAT---------AARQ-----LRL 381
Cdd:PTZ00216 365 ------------LIGVPRIFDTIKKAVEAKLPpvgslkrrvfdhayqsrlrALKEGKDTpywnekvfsAPRAvlggrVRA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 382 MMCGSSalPL-PVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDG--SCDNVEV-GEL 457
Cdd:PTZ00216 433 MLSGGG--PLsAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEykHTDTPEPrGEI 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 458 CIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNADIMKVGGYKLsALE-IEAVLLEHPTISE-- 534
Cdd:PTZ00216 511 LLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYI-ALEaLEALYGQNELVVPng 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 535 CCVLGLPDKDYgeaVCAIIIPN-----------------PEIKRKREEELKPALTLEELSMWAKEKlaPYKIPN--CLLL 595
Cdd:PTZ00216 590 VCVLVHPARSY---ICALVLTDeakamafakehgiegeyPAILKDPEFQKKATESLQETARAAGRK--SFEIVRhvRVLS 664
|
570 580
....*....|....*....|....*....
gi 747052525 596 WESLPRN----AMGKVNKKELKKQLADQV 620
Cdd:PTZ00216 665 DEWTPENgvltAAMKLKRRVIDERYADLI 693
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
185-576 |
2.28e-29 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 123.06 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 185 EDHQELMKAIAvktsaqMSLLPSVPSVSTKSTELDHTIN--GELDGTRCLQETEIPHE-ISGDDPALIIYTSGTTGKPKG 261
Cdd:PRK08180 153 DDGAAFARALA------AVVPADVEVVAVRGAVPGRAATpfAALLATPPTAAVDAAHAaVGPDTIAKFLFTSGSTGLPKA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 262 VVHTHKGVLAQVQMLTDAWGYTSTDH--FLHCLPLHHVHG---LFNALLA---PLY--AGS-TVEFMPKfSVRGIwqrwR 330
Cdd:PRK08180 227 VINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGgnhNLGIVLYnggTLYidDGKpTPGGFDE-TLRNL----R 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 331 ESYPqdqtkaddavTVFTGVPTmytrliqGYEAMDPALQTASATAAR---QLRLMMCGSSALPLPVMQKWETITGHVLLE 407
Cdd:PRK08180 302 EISP----------TVYFNVPK-------GWEMLVPALERDAALRRRffsRLKLLFYAGAALSQDVWDRLDRVAEATCGE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 408 R------YGMTE---FVMAISNPLKgkrKGGTVGKPLPGVQAKIIAEDGSCdnvevgELCIKSPSLFKEYWNLPEVTKQS 478
Cdd:PRK08180 365 RirmmtgLGMTEtapSATFTTGPLS---RAGNIGLPAPGCEVKLVPVGGKL------EVRVKGPNVTPGYWRAPELTAEA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FIDGGFFKTGDAAR-VDED----GyYVILGRTNADimkvggYKLS--------ALEIEAVLLEHPTISECCVLGlPDKDY 545
Cdd:PRK08180 436 FDEEGYYRSGDAVRfVDPAdperG-LMFDGRIAED------FKLSsgtwvsvgPLRARAVSAGAPLVQDVVITG-HDRDE 507
|
410 420 430
....*....|....*....|....*....|.
gi 747052525 546 geaVCAIIIPNPEIKRkREEELKPALTLEEL 576
Cdd:PRK08180 508 ---IGLLVFPNLDACR-RLAGLLADASLAEV 534
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-614 |
2.80e-29 |
|
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: 120.88 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLtgADLRSVKGngenkhlggARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:cd17653 11 PDAVAVESLGGSLTYGELDAASNALANRL--LQLGVVPG---------DVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEdhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheiS 242
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTD--------------------------------------------------------S 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 GDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglFNA----LLAPLYAGSTVEFmp 318
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIA-----FDAcigeIFSTLCNGGTLVL-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 kfsvrgiwqrwRESypqDQTKADDA--VTVFTGVPTmytrliqgyeamdpALQTASATAARQLRLMMCGSSALPLPVMQK 396
Cdd:cd17653 177 -----------ADP---SDPFAHVArtVDALMSTPS--------------ILSTLSPQDFPNLKTIFLGGEAVPPSLLDR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 397 WETitGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIKSPSLFKEYWNLPEVT 475
Cdd:cd17653 229 WSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEgVVGEICISGVQVARGYLGNPALT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 476 KQSFIDGGF------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEA-VLLEHPTISECCVLglpdkDYGEA 548
Cdd:cd17653 307 ASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQV-KVRGFRINLEEIEEvVLQSQPEVTQAAAI-----VVNGR 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 549 VCAIIIPNPEIKRKREEELKpaltleelsmwakEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKK 614
Cdd:cd17653 381 LVAFVTPETVDVDGLRSELA-------------KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
61-616 |
4.32e-29 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 121.65 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 61 SDTHNSILMELVKAVANRgsisPESIAVTAHEKSH--SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAK 138
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQQ----PEAIALRRCDGTSalRYRELVAEVGGLAADLRAQSVSR-----------GSRVLVISD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 139 PSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQelmkaiaVKTSAQMSLLPSVPSVSTKSTEL 218
Cdd:PRK05857 75 NGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSK-------MASSAVPEALHSIPVIAVDIAAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 219 DHTINGELDGTRCLQETEIpheiSGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTD---AW-GYTSTDHFLHCLPL 294
Cdd:PRK05857 148 TRESEHSLDAASLAGNADQ----GSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKeglNWvTWVVGETTYSPLPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 295 HHVHGLFNALLAPLYAGSTVefmpkfsvrgiwQRWRESYPQDQTKADDAVTVFTGVPTMYTRLIqgYEamdpaLQTAsAT 374
Cdd:PRK05857 224 THIGGLWWILTCLMHGGLCV------------TGGENTTSLLEILTTNAVATTCLVPTLLSKLV--SE-----LKSA-NA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 375 AARQLRLMMCGSS---ALPLPVMQKWETITGHVL-LERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCD 450
Cdd:PRK05857 284 TVPSLRLVGYGGSraiAADVRFIEATGVRTAQVYgLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 451 NV-------EVGELCIKSPSLFKEYWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNADIMKvGGYKLSALEIE 523
Cdd:PRK05857 364 TApgagpsaSFGTLWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 524 AVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKREEELKPALTleelSMWAKEKLAPYKiPNCLLLWESLPRNA 603
Cdd:PRK05857 442 RIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIA----ARFRRESEPMAR-PSTIVIVTDIPRTQ 516
|
570
....*....|...
gi 747052525 604 MGKVNKKELKKQL 616
Cdd:PRK05857 517 SGKVMRASLAAAA 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
251-613 |
4.96e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.88 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 251 YTSGTTGKPKGVVHTHKGvlAQVQMLTDA--WGYTSTDHFLHCLPLHHVHG-LFNALLAPLyAGSTVeFMPKFSVRGIWQ 327
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNAliWGMNEGAVYLWTLPMFHCNGwCFTWTLAAL-CGTNI-CLRQVTAKAIYS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 328 rwresypqdqTKADDAVTVFTGVPTMYTRLIQGyeamdPALQTAsATAARQLRLMMCGssALPLPVMQKWETITGHVLLE 407
Cdd:PLN02479 278 ----------AIANYGVTHFCAAPVVLNTIVNA-----PKSETI-LPLPRVVHVMTAG--AAPPPSVLFAMSEKGFRVTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 408 RYGMTE-------------------FVMAISNPLKGKRKGGTVG---------KPLPGvqakiiaedgscDNVEVGELCI 459
Cdd:PLN02479 340 TYGLSEtygpstvcawkpewdslppEEQARLNARQGVRYIGLEGldvvdtktmKPVPA------------DGKTMGEIVM 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 460 KSPSLFKEYWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRtNADIMKVGGYKLSALEIEAVLLEHPTISECCVLG 539
Cdd:PLN02479 408 RGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR-SKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 540 LPDKDYGEAVCAIIIPNPEIKRKREEELKpaltlEELSMWAKEKLAPYKIPNClLLWESLPRNAMGKVNKKELK 613
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPGVDKSDEAALA-----EDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVLR 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
76-612 |
1.35e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 122.58 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 76 ANRGSISPESIAVTAHEKSHSYHQLILSAvkisNLLTGAdLRSvKGNGENkhlggARVGIVAKPSPEFVAGVLGTWFSGG 155
Cdd:PRK05691 2195 AAQAARTPQAPALTFAGQTLSYAELDARA----NRLARA-LRE-RGVGPQ-----VRVGLALERSLEMVVGLLAILKAGG 2263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 156 VAVPLALSYPEAELLHVMNDSDITMILStedHQELMKAiavktsaqMSLLPSvpSVSTKSTE-----LDHTINGELDGTR 230
Cdd:PRK05691 2264 AYVPLDPEYPLERLHYMIEDSGIGLLLS---DRALFEA--------LGELPA--GVARWCLEddaaaLAAYSDAPLPFLS 2330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 231 CLQeteipHEisgddpALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglFNA----LLA 306
Cdd:PRK05691 2331 LPQ-----HQ------AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN-----FDAaserLLV 2394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 307 PLYAGSTVEFMP--KFSVRGIWQRWREsypqdqtkadDAVTVFTGVPTMYTRLIQGYeamdpalqtasATAARQLRLMMC 384
Cdd:PRK05691 2395 PLLCGARVVLRAqgQWGAEEICQLIRE----------QQVSILGFTPSYGSQLAQWL-----------AGQGEQLPVRMC 2453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 --GSSALPLPVMQKW-ETITGHVLLERYGMTE-FVMAISNPLKGKRKGGTVGKPLPGV----QAKIIAED------GScd 450
Cdd:PRK05691 2454 itGGEALTGEHLQRIrQAFAPQLFFNAYGPTEtVVMPLACLAPEQLEEGAASVPIGRVvgarVAYILDADlalvpqGA-- 2531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 451 nveVGELCIKSPSLFKEYWNLPEVTKQSFI------DGG-FFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIE 523
Cdd:PRK05691 2532 ---TGELYVGGAGLAQGYHDRPGLTAERFVadpfaaDGGrLYRTGDLVRLRADGLVEYVGRIDHQV-KIRGFRIELGEIE 2607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 524 AVLLEHPTISECCVLGLpDKDYGEAVCAIIIPNpeiKRKREEELKPALTlEELSMWAKEKLAPYKIPNCLLLWESLPRNA 603
Cdd:PRK05691 2608 SRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSA---VAGQDDEAQAALR-EALKAHLKQQLPDYMVPAHLILLDSLPLTA 2682
|
....*....
gi 747052525 604 MGKVNKKEL 612
Cdd:PRK05691 2683 NGKLDRRAL 2691
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
244-619 |
2.39e-28 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 120.59 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVeFMpkfsvr 323
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEV-FL------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 giwqrwresYPQ-------DQTKADDAVTVFTGVPTM---YTRLIQGYEamdpalqtasatAARqLRLMMCGSSALPLPV 393
Cdd:PRK08043 438 ---------YPSplhyrivPELVYDRNCTVLFGTSTFlgnYARFANPYD------------FAR-LRYVVAGAEKLQEST 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEF--VMAISNPLKGKRkgGTVGKPLPGVQAKIIA----EDGscdnvevGELCIKSPSLFKE 467
Cdd:PRK08043 496 KQLWQDKFGLRILEGYGVTECapVVSINVPMAAKP--GTVGRILPGMDARLLSvpgiEQG-------GRLQLKGPNIMNG 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNL--PEVTK-------QSFIDGGFFKTGDAARVDEDGYYVILGRTNAdIMKVGGYKLSALEIEAVLLEHPTISECCVL 538
Cdd:PRK08043 567 YLRVekPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGRAKR-FAKIAGEMVSLEMVEQLALGVSPDKQHATA 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 539 GLPDKDYGEAVcAIIIPNPEIKRkreeelkpaltlEELSMWAKEKLAP-YKIPNCLLLWESLPRNAMGKVNKKELkKQLA 617
Cdd:PRK08043 646 IKSDASKGEAL-VLFTTDSELTR------------EKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTL-KSMV 711
|
..
gi 747052525 618 DQ 619
Cdd:PRK08043 712 DE 713
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
83-612 |
2.97e-28 |
|
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: 118.27 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTG-ADLRSVKgngenkhlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSvAEIRPDD-----------LVGLVLDKSELMIIAILAVWKAGAAYVPID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPeaellhvmnDSDITMILStedhqelmkaiavKTSAQMsllpsvpsVSTKSTELdhtingeldgtrclqeteiphei 241
Cdd:cd17648 70 PSYP---------DERIQFILE-------------DTGARV--------VITNSTDL----------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 sgddpALIIYTSGTTGKPKGVVHTHKGVlaqVQMLTDAWG-YTSTDHFLHCLPL-------HHVHGLFNALLAplyaGST 313
Cdd:cd17648 97 -----AYAIYTSGTTGKPKGVLVEHGSV---VNLRTSLSErYFGRDNGDEAVLFfsnyvfdFFVEQMTLALLN----GQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 314 VeFMPKFSVRGIWQRWREsYPQDQtkaddAVTVFTGVPTmytrLIQGYEamdpalqTASATaarQLRLMMCGSSALPLPV 393
Cdd:cd17648 165 L-VVPPDEMRFDPDRFYA-YINRE-----KVTYLSGTPS----VLQQYD-------LARLP---HLKRVDAAGEEFTAPV 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEF-VMAISNPLKG-KRKGGTVGKPLPGVQAKIIAED------GScdnveVGELCIKSPSLF 465
Cdd:cd17648 224 FEKLRSRFAGLIINAYGPTETtVTNHKRFFPGdQRFDKSLGRPVRNTKCYVLNDAmkrvpvGA-----VGELYLGGDGVA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 466 KEYWNLPEVTKQSFIDGGF--------------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPT 531
Cdd:cd17648 299 RGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQV-KIRGQRIEPGEVEAALASYPG 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 532 ISECCVLGLPDKDYGEAV-----CAIIIPNPEikrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:cd17648 378 VRECAVVAKEDASQAQSRiqkylVGYYLPEPG-----------HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGK 446
|
....*.
gi 747052525 607 VNKKEL 612
Cdd:cd17648 447 LDVRAL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
92-619 |
7.71e-28 |
|
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: 117.15 E-value: 7.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 92 EKSHSYHQLILSAVKISNLLTGAdlRSVKGngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGgvAVPLALSY--PEAEL 169
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDD--LGVQA--------GDFVAIDLTNSPEFVFLWLGLWSIG--AAPAFINYnlSGDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 170 LHVMNDSDITMILSTEDhqelmkaiavktsaqmsllpsvpsvstksteldhtingeldgtrclqeteipheisgdDPALI 249
Cdd:cd05937 71 IHCLKLSGSRFVIVDPD----------------------------------------------------------DPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 250 IYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRW 329
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 330 RESypqdqtkaDDAVTVFTGvptmytrliqgyEAMDPALQTASATAARQLRLMMCGSSALPLPVMQKW-ETITGHVLLER 408
Cdd:cd05937 173 RDS--------GATIIQYVG------------ELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFrERFNVPEIGEF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 409 YGMTEFVMAISNPLKGKRKGGTVGK-------PLPGVQA--KIIAEDGS---------CDNVEVGE-------LCIKSPS 463
Cdd:cd05937 233 YAATEGVFALTNHNVGDFGAGAIGHhglirrwKFENQVVlvKMDPETDDpirdpktgfCVRAPVGEpgemlgrVPFKNRE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 464 LFKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISECCV 537
Cdd:cd05937 313 AFQGYLHNEDATESKLVRDVFrkgdiyFRTGDLLRQDADGRWYFLDRL-GDTFRWKSENVSTTEVADVLGAHPDIAEANV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 538 LG--LPDKDyGEAVCAIiipnpeIKRKREEELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLprnaMGKVNKKELKKQ 615
Cdd:cd05937 392 YGvkVPGHD-GRAGCAA------ITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEV----ATTDNHKQQKGV 460
|
....
gi 747052525 616 LADQ 619
Cdd:cd05937 461 LRDE 464
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
245-613 |
5.57e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 115.50 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVefmpkfSVRG 324
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSV------CMRH 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IwqrwreSYPQDQTKAD-DAVTVFTGVPTMYTRLIQGyEAMDPALQTASATaarqlrlMMCGSSALPLPVMQKWETITGH 403
Cdd:PLN03102 261 V------TAPEIYKNIEmHNVTHMCCVPTVFNILLKG-NSLDLSPRSGPVH-------VLTGGSPPPAALVKKVQRLGFQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 404 VLlERYGMTEFVMAI----------------SNPLKGKRKGGTVGKPLPGVQAKIIAEDGSCDNVEVGELCIKSPSLFKE 467
Cdd:PLN03102 327 VM-HAYGLTEATGPVlfcewqdewnrlpenqQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFiDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGE 547
Cdd:PLN03102 406 YLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSK-DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 548 AVCAIIIPNPEIKRKREEELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:PLN03102 484 TPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
82-619 |
1.56e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 113.04 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 82 SPESIAVTAHEKSHSYHQLilsAVKISNLLTGADLRSVKGngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLA 161
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQL---CARIDQLAAGFAQQGVVE--------GSGVALRGKNSPETLLAYLALLQCGARVLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 162 LSYPEAELLHVMNDSDITMILSTEDHqelmKAIAVKTSAQMSLLPSVPSVStksteldhtingeldgtrclqeteipheI 241
Cdd:PRK09029 85 PQLPQPLLEELLPSLTLDFALVLEGE----NTFSALTSLHLQLVEGAHAVA----------------------------W 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLfnallaplyagstvefmpkfs 321
Cdd:PRK09029 133 QPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQ--------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 322 vrGIWQRW---------RESYPQDQtkADDAVTVFTGVPTMYTRLIQgyeamdpalQTASATAARQLRLmmcGSSALPLP 392
Cdd:PRK09029 192 --GIVWRWlyagatlvvRDKQPLEQ--ALAGCTHASLVPTQLWRLLD---------NRSEPLSLKAVLL---GGAAIPVE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 393 VMQKWE-----TITGhvllerYGMTEF---VMAisnplkgKRKGGT--VGKPLPGVQAKIIAedgscdnvevGELCIKSP 462
Cdd:PRK09029 256 LTEQAEqqgirCWCG------YGLTEMastVCA-------KRADGLagVGSPLPGREVKLVD----------GEIWLRGA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 463 SLFKEYWN----LPEVTKQsfidgGFFKTGDAARVDeDGYYVILGRtnADIMKV-GGYKLSALEIEAVLLEHPTISECCV 537
Cdd:PRK09029 313 SLALGYWRqgqlVPLVNDE-----GWFATRDRGEWQ-NGELTILGR--LDNLFFsGGEGIQPEEIERVINQHPLVQQVFV 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 538 LGLPDKDYGEAVCAIIipnpeikrkreeELKPALTLEELSMWAKEKLAPYKIP-NCLLLWESLPRNAMgKVNKKELKKQL 616
Cdd:PRK09029 385 VPVADAEFGQRPVAVV------------ESDSEAAVVNLAEWLQDKLARFQQPvAYYLLPPELKNGGI-KISRQALKEWV 451
|
...
gi 747052525 617 ADQ 619
Cdd:PRK09029 452 AQQ 454
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
242-620 |
2.06e-26 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 115.06 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDPALIIYTSGTTGKPKGVVHTHKGVLA---QVQMLTDawgYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP 318
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLAnraQVAARID---FSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 K-FSVRGIwqrwresyPQ--DQTKAddavTVFTGVPTMYTrliqGYEamdpalQTASATAARQLRLMMCGSSALPLPVMQ 395
Cdd:PRK06814 868 SpLHYRII--------PEliYDTNA----TILFGTDTFLN----GYA------RYAHPYDFRSLRYVFAGAEKVKEETRQ 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 396 KWETITGHVLLERYGMTEF--VMAISNPLKGKrkGGTVGKPLPGVQAKIiaedgscDNV----EVGELCIKSPSLFKEYW 469
Cdd:PRK06814 926 TWMEKFGIRILEGYGVTETapVIALNTPMHNK--AGTVGRLLPGIEYRL-------EPVpgidEGGRLFVRGPNVMLGYL 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 470 NL--PEVTKQSfiDGGFFKTGDAARVDEDGYYVILGRTNAdIMKVGGYKLSALEIEAVllehptISECcvlglpDKDYGE 547
Cdd:PRK06814 997 RAenPGVLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKR-FAKIAGEMISLAAVEEL------AAEL------WPDALH 1061
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 747052525 548 AVCAiiIPNPeikrKREEEL-----KPALTLEELSMWAKEKLAP-YKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PRK06814 1062 AAVS--IPDA----RKGERIillttASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAA 1134
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
244-587 |
6.08e-26 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 112.89 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLApLYAGSTVEFmpkfsvr 323
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAVGF------- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 324 giwqrwresYPQDQTKADDAV-----TVFTGVPTMYTRLiqgYEAMDPALQT----------ASATAARQ---------- 378
Cdd:PLN02736 293 ---------YQGDNLKLMDDLaalrpTIFCSVPRLYNRI---YDGITNAVKEsgglkerlfnAAYNAKKQalengknpsp 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 379 -----------------LRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAK 441
Cdd:PLN02736 361 mwdrlvfnkikaklggrVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVK 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 442 IIaedgscDNVEV-----------GELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIM 510
Cdd:PLN02736 441 LV------DVPEMnytsedqpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKK-NIF 513
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 511 KVGGYKLSALE-IEAVLLEHPTISECCVLGlpdKDYGEAVCAIIIPNPEIkrkreeeLKPaltleelsmWAKEKLAPY 587
Cdd:PLN02736 514 KLAQGEYIAPEkIENVYAKCKFVAQCFVYG---DSLNSSLVAVVVVDPEV-------LKA---------WAASEGIKY 572
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
241-562 |
8.66e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 112.06 E-value: 8.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHK---GVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHG---LFNALLaplYAGSTV 314
Cdd:PRK12582 217 ITPDTVAKYLFTSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnaNFNGLL---WGGGTL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 315 EFMPKFSVRGIW----QRWRESYPqdqtkaddavTVFTGVPTMYTRLIqgyEAM--DPALQtasATAARQLRLMMCGSSA 388
Cdd:PRK12582 294 YIDDGKPLPGMFeetiRNLREISP----------TVYGNVPAGYAMLA---EAMekDDALR---RSFFKNLRLMAYGGAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 389 LPLPVMQKWE----TITGH--VLLERYGMTEFVMAISNPLKGKRKGGTVGKPLPGVQAKIiaedgscdnVEVG---ELCI 459
Cdd:PRK12582 358 LSDDLYERMQalavRTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL---------APVGdkyEVRV 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 460 KSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAAR-VDED----GyYVILGRTNADimkvggYKLS--------ALEIEAVL 526
Cdd:PRK12582 429 KGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAED------FKLStgtwvsvgTLRPDAVA 501
|
330 340 350
....*....|....*....|....*....|....*.
gi 747052525 527 LEHPTISECCVLGLpDKDYgeaVCAIIIPNPEIKRK 562
Cdd:PRK12582 502 ACSPVIHDAVVAGQ-DRAF---IGLLAWPNPAACRQ 533
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
136-620 |
1.27e-25 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 112.83 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 136 VAKP-SPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQMSLLPSVPSVSTK 214
Cdd:PRK10252 513 VALPrSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 215 STELdhtingeldgtrclqeteiPHeisgdDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPL 294
Cdd:PRK10252 593 QLSQ-------------------PH-----HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPC 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 295 H---HVHGLFnallAPLYAGSTVEFMPKFSVRGiwqrwresyPQDQTK--ADDAVTVFTGVPTMYTRLIQgyeamdpALQ 369
Cdd:PRK10252 649 SfdvSVWEFF----WPFIAGAKLVMAEPEAHRD---------PLAMQQffAEYGVTTTHFVPSMLAAFVA-------SLT 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 370 TASATAA-RQLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTEFVMAISN-PLKGKRKGGTVGKPLP------GVQAK 441
Cdd:PRK10252 709 PEGARQScASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWyPAFGEELAAVRGSSVPigypvwNTGLR 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 442 IIaeDGSCDNVEV---GELCIKSPSLFKEYWNLPEVTKQSFIDGGF------FKTGDAARVDEDGYYVILGRTNaDIMKV 512
Cdd:PRK10252 789 IL--DARMRPVPPgvaGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSD-DQLKI 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 513 GGYKLSALEIEAVLLEHPTISEC----CVLGLPDKDYGEA--VCAIIIPNPEIkrkreeelkpALTLEELSMWAKEKLAP 586
Cdd:PRK10252 866 RGQRIELGEIDRAMQALPDVEQAvthaCVINQAAATGGDArqLVGYLVSQSGL----------PLDTSALQAQLRERLPP 935
|
490 500 510
....*....|....*....|....*....|....*
gi 747052525 587 YKIPNCLLLWESLPRNAMGKVNKKEL-KKQLADQV 620
Cdd:PRK10252 936 HMVPVVLLQLDQLPLSANGKLDRKALpLPELKAQV 970
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
81-613 |
1.56e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 110.48 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 81 ISPESIAVTAHEKSH--SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSG--GV 156
Cdd:PRK13390 9 IAPDRPAVIVAETGEqvSYRQLDDDSAALARVLYDAGLRT-----------GDVVALLSDNSPEALVVLWAALRSGlyIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 157 AVPLALSYPEAEllHVMNDSDITMILSTEdhqeLMKAIAVKTSAQMsllpsvpsvstkstELDHTINGELDGTRCLQETe 236
Cdd:PRK13390 78 AINHHLTAPEAD--YIVGDSGARVLVASA----ALDGLAAKVGADL--------------PLRLSFGGEIDGFGSFEAA- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 237 ipheISGDDP--------ALIIYTSGTTGKPKGVVHTHKGVLAQ------VQMLTDAWGYTSTDHFLHCLPLHHVH---- 298
Cdd:PRK13390 137 ----LAGAGPrlteqpcgAVMLYSSGTTGFPKGIQPDLPGRDVDapgdpiVAIARAFYDISESDIYYSSAPIYHAAplrw 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 299 -GLFNALlaplyaGSTVEFMPKFSVR---GIWQRWResypqdqtkaddaVTVFTGVPTMYTRLIQgyeaMDPALQTASAT 374
Cdd:PRK13390 213 cSMVHAL------GGTVVLAKRFDAQatlGHVERYR-------------ITVTQMVPTMFVRLLK----LDADVRTRYDV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 375 AArqLRLMMCGSSALPLPVMQKWETITGHVLLERYGMTE-FVMAISNPLKGKRKGGTVGKPLPGvQAKIIAEDGS-CDNV 452
Cdd:PRK13390 270 SS--LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEaHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNeLPAG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKT--GDAARVDEDGYYVILGRTNADIMKvGGYKLSALEIEAVLLEHP 530
Cdd:PRK13390 347 RIGTVYFERDRLPFRYLNDPEKTAAAQHPAHPFWTtvGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQETENALTMHP 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 531 TISECCVLGLPDKDYGEAVCAIIipnpeikrKREEELKPALTL-EELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNK 609
Cdd:PRK13390 426 AVHDVAVIGVPDPEMGEQVKAVI--------QLVEGIRGSDELaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVK 497
|
....
gi 747052525 610 KELK 613
Cdd:PRK13390 498 GLLR 501
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
244-568 |
4.29e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 109.60 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhhvHGLFNALLAplyAGSTVEFM------ 317
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL---FALFGPALG---MTSVIPDMdptrpa 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 318 ---PKFSVRGIwQRWresypqdqtkaddAVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqLRLMMCGSSALPLPVM 394
Cdd:PRK09274 248 tvdPAKLFAAI-ERY-------------GVTNLFGSPALLERLGRYGEANGIKLPS--------LRRVISAGAPVPIAVI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKWETITGHV--LLERYGMTEfVMAISN-----PLKGKRK-----GGT-VGKPLPGVQAKIIA----------EDGSCDN 451
Cdd:PRK09274 306 ERFRAMLPPDaeILTPYGATE-ALPISSiesreILFATRAatdngAGIcVGRPVDGVEVRIIAisdapipewdDALRLAT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 452 VEVGELCIKSPSLFKEYWNLPEVTKQSFI---DGGFF-KTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLL 527
Cdd:PRK09274 385 GEIGEIVVAGPMVTRSYYNRPEATRLAKIpdgQGDVWhRMGDLGYLDAQGRLWFCGRK-AHRVETAGGTLYTIPCERIFN 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 747052525 528 EHPTISECCVLGLPDKdyGEAVCAIII-PNPEIKRKR---EEELK 568
Cdd:PRK09274 464 THPGVKRSALVGVGVP--GAQRPVLCVeLEPGVACSKsalYQELR 506
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
69-614 |
2.28e-24 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 106.90 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 69 MELVKAVANRGSISPESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVL 148
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPD-----------KSPIIVFGHMSPEMLATFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 149 GTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQmsllpsVPSVSTKSTELDHTingeldg 228
Cdd:PRK04813 71 GAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDE------LKDIFATGNPYDFD------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 229 trclqeteipHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQ-MLTDawgYTSTDH--FLHCLPLH---HVHGLFN 302
Cdd:PRK04813 138 ----------HAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNwMLED---FALPEGpqFLNQAPYSfdlSVMDLYP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 303 ALLAplyaGSTVEFMPKFSVRGIWQRWrESYPQDQtkaddaVTVFTGVPTMytrliqgyeaMDPALQTASATAARQLRL- 381
Cdd:PRK04813 205 TLAS----GGTLVALPKDMTANFKQLF-ETLPQLP------INVWVSTPSF----------ADMCLLDPSFNEEHLPNLt 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 382 --MMCGSsALPLPVMQKwetitghvLLER---------YGMTEFVMAIS------------NPLKgkrkggtVGKPLPGV 438
Cdd:PRK04813 264 hfLFCGE-ELPHKTAKK--------LLERfpsatiyntYGPTEATVAVTsieitdemldqyKRLP-------IGYAKPDS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 439 QAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSF--IDG-GFFKTGDAARVDeDGYYVILGRTNADImKVGG 514
Cdd:PRK04813 328 PLLIIDEEGTkLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGqPAYHTGDAGYLE-DGLLFYQGRIDFQI-KLNG 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 515 YKLSALEIEAVLLEHPTISECCVLglP-DKDYG-EAVCAIIIPNPEiKRKREEELKPALTlEELsmwaKEKLAPYKIPNC 592
Cdd:PRK04813 406 YRIELEEIEQNLRQSSYVESAVVV--PyNKDHKvQYLIAYVVPKEE-DFEREFELTKAIK-KEL----KERLMEYMIPRK 477
|
570 580
....*....|....*....|..
gi 747052525 593 LLLWESLPRNAMGKVNKKELKK 614
Cdd:PRK04813 478 FIYRDSLPLTPNGKIDRKALIE 499
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
83-612 |
6.20e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 105.85 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 83 PESIAVTAHEKSHSYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLAL 162
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAP-----------GRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 163 SYPEAELLHVMNDSDITMILSTEdhqELMKAIAVKTSAQMSLLPSvpsvstksteldhTINGELDGTRclQETEIPHEIs 242
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADN---EFAERIAGADDAVAVIDPA-------------TAGAEESGGR--PAVAAPGRI- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 243 gddpalIIYTSGTTGKPKGVVHTHK---GVLAQVQMLTDAWGYTSTDHFLhCLPLHHVHGlFNALLAPLYAGSTVEFMPK 319
Cdd:PRK13383 179 ------VLLTSGTTGKPKGVPRAPQlrsAVGVWVTILDRTRLRTGSRISV-AMPMFHGLG-LGMLMLTIALGGTVLTHRH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGiwqrwreSYPQDQTKADDAvtvFTGVPTMYTRLiqgyeaMDPALQTASATAARQLRLMMCGSSALPLPVMQKWET 399
Cdd:PRK13383 251 FDAEA-------ALAQASLHRADA---FTAVPVVLARI------LELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 ITGHVLLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQAKIIAEDGScdnvEVGelcikspslfkeywnlPEVTKQS 478
Cdd:PRK13383 315 TYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNR----PVG----------------PRVTGRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 479 FIDG-----------------GFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLP 541
Cdd:PRK13383 375 FVGGelagtrytdgggkavvdGMTSTGDMGYLDNAGRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747052525 542 DKDYGEAVCAIIIPNPeikrkreeelKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:PRK13383 454 DERFGHRLAAFVVLHP----------GSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
230-568 |
7.70e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 104.85 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 230 RCLQETEiPHEISG----DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLhhvHGLFNALL 305
Cdd:cd05910 68 QCLQEAE-PDAFIGipkaDEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPL---FALFGPAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 306 APLYAGSTVEFM------PKFSVRGIwQRWResypqdqtkaddaVTVFTGVPTMYTRLIQGYEAMDPALQTasataarqL 379
Cdd:cd05910 144 GLTSVIPDMDPTrparadPQKLVGAI-RQYG-------------VSIVFGSPALLERVARYCAQHGITLPS--------L 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 380 RLMMCGSSALPLPVMQKWETIT--GHVLLERYGMTEF----------VMAISNPLKGKRKGGTVGKPLPGVQAKIIA--- 444
Cdd:cd05910 202 RRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEAlpvssigsreLLATTTAATSGGAGTCVGRPIPGVRVRIIEidd 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 445 -------EDGSCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFI---DGGFF-KTGDAARVDEDGYYVILGRTNADIMKVG 513
Cdd:cd05910 282 epiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIddnSEGFWhRMGDLGYLDDEGRLWFCGRKAHRVITTG 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 514 GyKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAV-CAIIIPNPEIKRKR-EEELK 568
Cdd:cd05910 362 G-TLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVlCVEPLPGTITPRARlEQELR 417
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
244-588 |
1.45e-23 |
|
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: 104.82 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTD--HFLHCLPLHHVHGLFNALLAPLYAGSTVEF----- 316
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 MP-KF--SVRGIwqrwRESYPqdqtkaddavTVFTGVPtmytrliQGYEAMDPALQTASATAAR---QLRLMMCGSSALP 390
Cdd:cd05921 245 MPgGFeeTLRNL----REISP----------TVYFNVP-------AGWEMLVAALEKDEALRRRffkRLKLMFYAGAGLS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 391 LPVmqkWETI-------TGH--VLLERYGMTE---FVMAISNPLKgkrKGGTVGKPLPGVQAKIIAEDGSCdnvevgELC 458
Cdd:cd05921 304 QDV---WDRLqalavatVGEriPMMAGLGATEtapTATFTHWPTE---RSGLIGLPAPGTELKLVPSGGKY------EVR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAAR-VDED----GYYvILGRTNADimkvggYKLS--------ALEIEAV 525
Cdd:cd05921 372 VKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKlADPDdpakGLV-FDGRVAED------FKLAsgtwvsvgPLRARAV 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 526 LLEHPTISECCVLGlPDKDYgeaVCAIIIPNP----EIKRKREEELKPALTLEELSMWAKEKLAPYK 588
Cdd:cd05921 445 AACAPLVHDAVVAG-EDRAE---VGALVFPDLlacrRLVGLQEASDAEVLRHAKVRAAFRDRLAALN 507
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
241-620 |
1.79e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 105.36 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDPALIIYTSGTTGKPKGVVHTHKGVLA-QVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTV---EF 316
Cdd:PLN02654 272 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVyTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVlvfEG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 317 MPKFSVRG-IWQrwresyPQDQTKaddaVTVFTGVPTMYTRLiqgyeaMDPALQTASATAARQLRLMmcGSSALPL-PVM 394
Cdd:PLN02654 352 APNYPDSGrCWD------IVDKYK----VTIFYTAPTLVRSL------MRDGDEYVTRHSRKSLRVL--GSVGEPInPSA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKW-ETITGHV---LLERYGMTEFVMAISNPLKGK--RKGGTVGKPLPGVQAKIIAE-----DGSCDnvevGELCIKS-- 461
Cdd:PLN02654 414 WRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEkgkeiEGECS----GYLCVKKsw 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSLFKEYWNLPEVTKQSFID--GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLG 539
Cdd:PLN02654 490 PGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEAAVVG 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 540 LPDKDYGEAVCAIIIPNPEIkrKREEELKPALTleelsMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PLN02654 569 IEHEVKGQGIYAFVTLVEGV--PYSEELRKSLI-----LTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ 641
|
.
gi 747052525 620 V 620
Cdd:PLN02654 642 L 642
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
130-539 |
2.00e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 104.92 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQMSLLPSVP 209
Cdd:PLN02861 102 GDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTEldhtiNGELDGTRCL----------QETEIPHEiSGDDPALIIYTSGTTGKPKGVVHTHKGVLAQV----QM 275
Cdd:PLN02861 182 DVSSEQKE-----EAEELGVSCFsweefslmgsLDCELPPK-QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstdHL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 276 L--TDAwGYTSTDHFLHCLPLHHVhglFNALLAP--LYAGSTVEFMpKFSVRGIWQRWRESYPqdqtkaddavTVFTGVP 351
Cdd:PLN02861 256 LkvTDR-VATEEDSYFSYLPLAHV---YDQVIETycISKGASIGFW-QGDIRYLMEDVQALKP----------TIFCGVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 352 TMYTRLIQGYEA-----------------------MDPALQTASA--------------TAARQLRLMMCGSSALPLPVM 394
Cdd:PLN02861 321 RVYDRIYTGIMQkissggmlrkklfdfaynyklgnLRKGLKQEEAsprldrlvfdkikeGLGGRVRLLLSGAAPLPRHVE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKWETITGHVLLERYGMTEF----VMAISNPLKgkrKGGTVGKPLPGVQAKI--IAEDG--SCDNVEVGELCIKSPSLFK 466
Cdd:PLN02861 401 EFLRVTSCSVLSQGYGLTEScggcFTSIANVFS---MVGTVGVPMTTIEARLesVPEMGydALSDVPRGEICLRGNTLFS 477
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 467 EYWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALE-IEAVLLEHPTISECCVLG 539
Cdd:PLN02861 478 GYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKK-NIFKLSQGEYVAVEnLENTYSRCPLIASIWVYG 549
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-613 |
2.28e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 102.81 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 211 VSTKSTELdhtINGELDGTRCLQETEIPHEisgddPALIIYTSGTTGKPKGV----------VHTHKGVLAQVQMLTDaw 280
Cdd:PRK08308 76 KRAGCHGL---LYGESDFTKLEAVNYLAEE-----PSLLQYSSGTTGEPKLIrrswteidreIEAYNEALNCEQDETP-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 281 gytstdhFLHClPLHHVHGLFNALLAPLYAGSTVEFM----PKFsvrgIWQRWREsYPQDqtkaddavtVFTGVPTMY-- 354
Cdd:PRK08308 146 -------IVAC-PVTHSYGLICGVLAALTRGSKPVIItnknPKF----ALNILRN-TPQH---------ILYAVPLMLhi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 355 -TRLIQGYEAMDpalqtasataarqlRLMMCGSsALPLPVMQKWETITGHvLLERYGMTEF-VMAISNPLkgkRKGGTVG 432
Cdd:PRK08308 204 lGRLLPGTFQFH--------------AVMTSGT-PLPEAWFYKLRERTTY-MMQQYGCSEAgCVSICPDM---KSHLDLG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 433 KPLPGVQAKIiaedGSCDNvEVGELCIKspslfkeywnlpevtkqsfIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKV 512
Cdd:PRK08308 265 NPLPHVSVSA----GSDEN-APEEIVVK-------------------MGDKEIFTKDLGYKSERGTLHFMGRMD-DVINV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 513 GGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIkrkreeelkpalTLEELSMWAKEKLAPYKIPNC 592
Cdd:PRK08308 320 SGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI------------DPVQLREWCIQHLAPYQVPHE 387
|
410 420
....*....|....*....|.
gi 747052525 593 LLLWESLPRNAMGKVNKKELK 613
Cdd:PRK08308 388 IESVTEIPKNANGKVSRKLLE 408
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
242-608 |
2.60e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 102.08 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 242 SGDDpALIIYTSGTTGKPKGVVHTHKGV---------LAQVQMLTDAW------GYTSTDHFLHClPLHHVHGLFNALLA 306
Cdd:cd05924 2 SADD-LYILYTGGTTGMPKGVMWRQEDIfrmlmggadFGTGEFTPSEDahkaaaAAAGTVMFPAP-PLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 307 PLYAGSTVEFMPKFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTR-LIQgyeamdpALQTASATAARQLRLMMCG 385
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWR----------TIEKHKVTSMTIVGDAMARpLID-------ALRDAGPYDLSSLFAISSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 386 SSALPLPVMQKWETITGH-VLLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVQakIIAEDGScdNVEVGE----LCI 459
Cdd:cd05924 143 GALLSPEVKQGLLELVPNiTLVDAFGSSETgFTGSGHSAGSGPETGPFTRANPDTV--VLDDDGR--VVPPGSggvgWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 460 KSPSLFKEYWNLPEVTKQSF--IDGGFFK-TGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECC 536
Cdd:cd05924 219 RRGHIPLGYYGDEAKTAETFpeVDGVRYAvPGDRATVEADGTVTLLGRGSVCI-NTGGEKVFPEEVEEALKSHPAVYDVL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 537 VLGLPDKDYGEAVCAIIipnpeikrkreeELKPA--LTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVN 608
Cdd:cd05924 298 VVGRPDERWGQEVVAVV------------QLREGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
40-615 |
1.07e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 102.65 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 40 SLSVFSLKVPSFRSF---------QYRLFSSDTHNSILMELVKAVANRgsisPESIAVTAHEKSHSYHQLILSAVKISNL 110
Cdd:PRK08279 3 TLMDLAARLPRRLPDlpgilrglkRTALITPDSKRSLGDVFEEAAARH----PDRPALLFEDQSISYAELNARANRYAHW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 111 LtgadlrsvKGNGENKhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDHQEL 190
Cdd:PRK08279 79 A--------AARGVGK---GDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 191 MKAIAVKTSAQMSLLpSVPSVSTKSTELDHTINGELDG--TRCLQETEiphEISGDDPALIIYTSGTTGKPKGVVHTHKG 268
Cdd:PRK08279 148 FEEARADLARPPRLW-VAGGDTLDDPEGYEDLAAAAAGapTTNPASRS---GVTAKDTAFYIYTSGTTGLPKAAVMSHMR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 269 VLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIW---QRWResypqdqtkaddaVT 345
Cdd:PRK08279 224 WLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWddvRRYR-------------AT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 346 VFTGVPTMYTRLIQgyeamdpalQTASAT-AARQLRLmMCGSSALPlPVMQKWETITG--HVlLERYGMTEFVMAISNpL 422
Cdd:PRK08279 291 AFQYIGELCRYLLN---------QPPKPTdRDHRLRL-MIGNGLRP-DIWDEFQQRFGipRI-LEFYAASEGNVGFIN-V 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 423 KGKRkgGTVGKpLPGVQAKIIA--------------EDGSCDNVEVGE--LCI-----KSPslFKEYwNLPEVTKQSFID 481
Cdd:PRK08279 358 FNFD--GTVGR-VPLWLAHPYAivkydvdtgepvrdADGRCIKVKPGEvgLLIgritdRGP--FDGY-TDPEASEKKILR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 482 GGF------FKTGDAARVDEDGYYVILGRtnadimkVG------GYKLSALEIEAVLLEHPTISECCVLG--LPDKDyGE 547
Cdd:PRK08279 432 DVFkkgdawFNTGDLMRDDGFGHAQFVDR-------LGdtfrwkGENVATTEVENALSGFPGVEEAVVYGveVPGTD-GR 503
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 548 AVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQ 615
Cdd:PRK08279 504 AGMAAIVLADG----------AEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKE 561
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
430-620 |
1.87e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 101.22 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 430 TVGKPL-PGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNA 507
Cdd:PRK10946 354 TQGRPMsPDDEVWVADADGNpLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 508 DIMKvGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNpeikrkreEELKPAltleELSMWAKEK-LAP 586
Cdd:PRK10946 434 QINR-GGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK--------EPLKAV----QLRRFLREQgIAE 500
|
170 180 190
....*....|....*....|....*....|....
gi 747052525 587 YKIPNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PRK10946 501 FKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
80-612 |
4.32e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.78 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 80 SISPESIAVTAHEKSHSYHQLILSAVKISNLLTGAdlrsvkGNGENKhlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVP 159
Cdd:PRK05691 3731 AAHPQRIAASCLDQQWSYAELNRAANRLGHALRAA------GVGVDQ-----PVALLAERGLDLLGMIVGSFKAGAGYLP 3799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 160 LALSYPEAELLHVMNDSDITMILST----EDHQELMKAIAVKTSAQMSLLPSVPSvstkSTELDHTingeldgtrclqet 235
Cdd:PRK05691 3800 LDPGLPAQRLQRIIELSRTPVLVCSaacrEQARALLDELGCANRPRLLVWEEVQA----GEVASHN-------------- 3861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 236 eiPHEISG-DDPALIIYTSGTTGKPKGVVHTHKGVL----AQVQMLT----DAWGYTSTDHFlhclplhhVHGLFNALLA 306
Cdd:PRK05691 3862 --PGIYSGpDNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlSKVPYLAlseaDVIAQTASQSF--------DISVWQFLAA 3931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 307 PLYaGSTVEFMPKFSVRGiwqrwresyPQ---DQTKADdAVTVFTGVPTmytrLIQGYEAMDPAlqtasatAARQLRLMM 383
Cdd:PRK05691 3932 PLF-GARVEIVPNAIAHD---------PQgllAHVQAQ-GITVLESVPS----LIQGMLAEDRQ-------ALDGLRWML 3989
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPLPVMQKWetitghvlLERYGMTEFVMA-----ISNPLKGKR--KGGTVGKPLP-GVQA---KIIAEDGSCDNV 452
Cdd:PRK05691 3990 PTGEAMPPELARQW--------LQRYPQIGLVNAygpaeCSDDVAFFRvdLASTRGSYLPiGSPTdnnRLYLLDEALELV 4061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 ---EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF-------FKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEI 522
Cdd:PRK05691 4062 plgAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQV-KIRGYRIELGEI 4140
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 523 EAVLLEHPTISECCVlGLPDKDYGEAVCAIIIPnpeikrkREEELKPALTLEELSMWAKEKLAPYKIPNCLLLWESLPRN 602
Cdd:PRK05691 4141 EARLHEQAEVREAAV-AVQEGVNGKHLVGYLVP-------HQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLN 4212
|
570
....*....|
gi 747052525 603 AMGKVNKKEL 612
Cdd:PRK05691 4213 ANGKLDRKAL 4222
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
245-567 |
6.16e-21 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 96.94 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHthkgvlaqvqmltDAWGY-----TSTDHFLHCLP---------LHHVHGLFNALLAPLYA 310
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGVQR-------------DTGGYavalaTSMDTIFGGKAgetffcasdIGWVVGHSYIVYAPLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 311 GSTV---EFMPKFSVRGIWQRWRESYpqdqtkaddAVTVFTGVPTMyTRLIQGYeamDPALQTASATAArqLR-LMMCG- 385
Cdd:PRK10524 301 GMATimyEGLPTRPDAGIWWRIVEKY---------KVNRMFSAPTA-IRVLKKQ---DPALLRKHDLSS--LRaLFLAGe 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 386 ----------SSALPLPVMQK-WETITGHVllerygmtefVMAISNPLKGK-RKGGTVGKPLPGVQAKIIAE-DGS-CDN 451
Cdd:PRK10524 366 pldeptaswiSEALGVPVIDNyWQTETGWP----------ILAIARGVEDRpTRLGSPGVPMYGYNVKLLNEvTGEpCGP 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 452 VEVGELCIKSP--------------SLFKEYWnlpevtkqSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKL 517
Cdd:PRK10524 436 NEKGVLVIEGPlppgcmqtvwgdddRFVKTYW--------SLFGRQVYSTFDWGIRDADGYYFILGRTD-DVINVAGHRL 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 518 SALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIP-------NPEIKRKREEEL 567
Cdd:PRK10524 507 GTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPkdsdslaDREARLALEKEI 563
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
130-614 |
2.73e-20 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 94.69 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYP----EA--ELLHVM-NDSDITMILSTEDHQELMKAIAVktsaqm 202
Cdd:PRK09192 74 GDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggrESyiAQLRGMlASAQPAAIITPDELLPWVNEATH------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 203 sllpsvpsvstkSTELDHTINGELDGTRCLQETEIPhEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLT-DAWG 281
Cdd:PRK09192 148 ------------GNPLLHVLSHAWFKALPEADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 282 YTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMP--KFSVRgiwqrwresypqdqtkaddavtvftgvPTMYTRLIQ 359
Cdd:PRK09192 215 VRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFARR---------------------------PLQWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 360 ------------GYEAMdpALQTASAT-AARQL---RLMMCGSSALPLPVMQKWETITGHV------LLERYGMTEFVMA 417
Cdd:PRK09192 268 rnrgtisysppfGYELC--ARRVNSKDlAELDLscwRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 418 ISNPLKGK-------------RKGGTV---------------GKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEY 468
Cdd:PRK09192 346 VSFSPLGSgivveevdrdrleYQGKAVapgaetrrvrtfvncGKALPGHEIEIRNEAGMpLPERVVGHICVRGPSLMSGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 469 WNLPEVTKQSFIDgGFFKTGDAARVdEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTI--SECCVLGLPDkDYG 546
Cdd:PRK09192 426 FRDEESQDVLAAD-GWLDTGDLGYL-LDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQ-ENG 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747052525 547 EAVCAII---IPNPEIKRKREEELKpALTLEELSMWAKEKLAPykiPNclllweSLPRNAMGKVNKKELKK 614
Cdd:PRK09192 502 EKIVLLVqcrISDEERRGQLIHALA-ALVRSEFGVEAAVELVP---PH------SLPRTSSGKLSRAKAKK 562
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
244-560 |
8.14e-20 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 93.34 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEF-----MP 318
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFaynplYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 319 KFSVRGIwqrwresypqDQTKaddaVTVFTGVPTMYtrliqgyeamDPALQTA--SATAARQLRLMMCGSSALPLPVMQK 396
Cdd:PRK06334 263 KKIVEMI----------DEAK----VTFLGSTPVFF----------DYILKTAkkQESCLPSLRFVVIGGDAFKDSLYQE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 397 WETITGHVLLER-YGMTEFVMAIS-NPLKGKRKGGTVGKPLPGVQAKIIAEDG--SCDNVEVGELCIKSPSLFKEYwnLP 472
Cdd:PRK06334 319 ALKTFPHIQLRQgYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETkvPVSSGETGLVLTRGTSLFSGY--LG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 473 EVTKQSFIDGG---FFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHptiseccvLGLPDKDYGEAV 549
Cdd:PRK06334 397 EDFGQGFVELGgetWYVTGDLGYVDRHGELFLKGRL-SRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGPL 467
|
330
....*....|.
gi 747052525 550 CAIIIPNPEIK 560
Cdd:PRK06334 468 VVCGLPGEKVR 478
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
245-615 |
1.01e-19 |
|
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: 92.42 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRG 324
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IWqrwresypqDQTKADDAvTVFtgvptMYTRLIQGYEAMDPALQTASataARQLRlMMCGSSALPlpvmQKWETIT--- 401
Cdd:cd05940 162 FW---------DDIRKYQA-TIF-----QYIGELCRYLLNQPPKPTER---KHKVR-MIFGNGLRP----DIWEEFKerf 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 --GHVlLERYGMTEFVMAISNpLKGKRkgGTVGKpLPGVQAKIIA----------------EDGSCDNV---EVGELC-- 458
Cdd:cd05940 219 gvPRI-AEFYAATEGNSGFIN-FFGKP--GAIGR-NPSLLRKVAPlalvkydlesgepirdAEGRCIKVprgEPGLLIsr 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKSPSLFKEYWNLPEVTKQ----SFIDG-GFFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTIS 533
Cdd:cd05940 294 INPLEPFDGYTDPAATEKKilrdVFKKGdAWFNTGDLMRLDGEGFWYFVDRL-GDTFRWKGENVSTTEVAAVLGAFPGVE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 534 ECCVLG--LPDKDyGEAVCA-IIIPNPEikrkreeelkpALTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKK 610
Cdd:cd05940 373 EANVYGvqVPGTD-GRAGMAaIVLQPNE-----------EFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKV 440
|
....*
gi 747052525 611 ELKKQ 615
Cdd:cd05940 441 DLRNE 445
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
130-523 |
4.11e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.83 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDsditmilsTEDHQELMKAIAVKTSAqmSLLPSVP 209
Cdd:PRK07768 54 GDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAED--------TLRVIGMIGAKAVVVGE--PFLAAAP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 210 SVSTKSTELDHTinGELDGTrclQETEIPhEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYT-STDHF 288
Cdd:PRK07768 124 VLEEKGIRVLTV--ADLLAA---DPIDPV-ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 289 LHCLPLHHVHGLFNALLAPLYAGSTVEFMpkfsvrgiwqrwresypqdqTKADdavtvFTGVPTMYTRLIQGYEA-MDPA 367
Cdd:PRK07768 198 VSWLPLFHDMGMVGFLTVPMYFGAELVKV--------------------TPMD-----FLRDPLLWAELISKYRGtMTAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 368 LQTASATAARQL--------------RLMMCGSSALPLPVMQKWETITG------HVLLERYGMTEFVMAIS-----NPL 422
Cdd:PRK07768 253 PNFAYALLARRLrrqakpgafdlsslRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSfspcgAGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 423 K---------------------GKRKGGTVGKPLPGVQAKIIAEDGS-CDNVEVGELCIKSPSLFKEYwnlpeVTKQSFI 480
Cdd:PRK07768 333 VvdevdadllaalrravpatkgNTRRLATLGPPLPGLEVRVVDEDGQvLPPRGVGVIELRGESVTPGY-----LTMDGFI 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 747052525 481 ----DGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIE 523
Cdd:PRK07768 408 paqdADGWLDTGDLGYLTEEGEVVVCGRVK-DVIIMAGRNIYPTDIE 453
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
245-614 |
1.01e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 86.33 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 DPALIIYTSGTTGKPKGVVHTHKGVL--AQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSV 322
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 323 RGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQGYEAMDPA----LQTASATAAR-----------QLRLMMC--- 384
Cdd:cd05915 234 ASLVE----------LFDGEGVTFTAGVPTVWLALADYLESTGHRlktlRRLVVGGSAAprsliarfermGVEVRQGygl 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 ------GSSALPLPvmqKWETITGHVLLE---RYGMTEFVMAIS--NPLkgkrkggTVGKPLPGVQAKIIAEDGScdnve 453
Cdd:cd05915 304 tetspvVVQNFVKS---HLESLSEEEKLTlkaKTGLPIPLVRLRvaDEE-------GRPVPKDGKALGEVQLKGP----- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 454 vgelcikspSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTIS 533
Cdd:cd05915 369 ---------WITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLK-DLIKSGGEWISSVDLENALMGHPKVK 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 534 ECCVLGLPDKDYGEAVCAIIipnpeikRKREEELKPaltlEELSMWAKEKLAPYK-IPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd05915 439 EAAVVAIPHPKWQERPLAVV-------VPRGEKPTP----EELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRAL 507
|
..
gi 747052525 613 KK 614
Cdd:cd05915 508 RE 509
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
246-618 |
1.55e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 86.33 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 246 PALIIYTSGTTGKPKGVVHTHKGVLAQVQMLtdaWGYTSTDHFLHCLPLHH------VHGLFNALLA-----PLYAGSTV 314
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYY---WRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLSlgntfVMFEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 315 EfmPKFSVRGIWQrwresypqdqTKADDAVTVFTGVPTMYTRLIQgyeaMDP-ALQTASATAARQLRLMMCGSSALPLPV 393
Cdd:PTZ00237 333 K--NKHIEDDLWN----------TIEKHKVTHTLTLPKTIRYLIK----TDPeATIIRSKYDLSNLKEIWCGGEVIEESI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 394 MQKWETITGHVLLERYGMTEFVMA-------ISNPLKgkrkggTVGKPLPGVQAKIIAEDGSCDNV-EVGELCIK---SP 462
Cdd:PTZ00237 397 PEYIENKLKIKSSRGYGQTEIGITylycyghINIPYN------ATGVPSIFIKPSILSEDGKELNVnEIGEVAFKlpmPP 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 463 SLFKEYWNLPEVTKQSFID-GGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLP 541
Cdd:PTZ00237 471 SFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLVLECCSIGIY 549
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 542 DKDYGEAVCAIIIpnpeIKRKREEELKPALTLE-ELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLAD 618
Cdd:PTZ00237 550 DPDCYNVPIGLLV----LKQDQSNQSIDLNKLKnEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLND 623
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
521-606 |
8.42e-17 |
|
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: 75.27 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 521 EIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrkreeelkPALTLEELSMWAKEKLAPYKIPNCLLLWESLP 600
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG----------VELLEEELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 747052525 601 RNAMGK 606
Cdd:pfam13193 71 KTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
71-618 |
8.56e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.83 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 71 LVKAVANRGSISPESIAVT--AHEKSH----SYHQLILSAVKISnlltgADLRSVKGNGENkhlggarvGIVAKPS-PEF 143
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRflADDPGEgvvlSYRDLDLRARTIA-----AALQARASFGDR--------AVLLFPSgPDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 144 VAGVLGTWFSGGVAVPlalSYP--------EAELLHVMNDSDITMILSTEDHQELMKAIAVKTSAQmslLPSVPSVSTks 215
Cdd:PRK05691 78 VAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAAN---APELLCVDT-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 216 teLDHTINGELDGTrclqeteiphEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWG--YTSTDHFLHCLP 293
Cdd:PRK05691 150 --LDPALAEAWQEP----------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 294 LHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWRESYPQDQtkaddavTVFTGVPTMYTRLIQgyeamdpalQTASA 373
Cdd:PRK05691 218 LYHDMGLIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG-------GTISGGPDFAYRLCS---------ERVSE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 374 TAARQL-----RLMMCGSSALPLPVMQKWET------ITGHVLLERYGMTEFVMAISNPLKGKR---------------- 426
Cdd:PRK05691 282 SALERLdlsrwRVAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGipaleldaealarnra 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 427 ---KGGTV---GKPLPGvQAKIIAE----DGSCDNVeVGELCIKSPSLFKEYWNLPEVTKQSFI--DG-GFFKTGDAARV 493
Cdd:PRK05691 362 epgTGSVLmscGRSQPG-HAVLIVDpqslEVLGDNR-VGEIWASGPSIAHGYWRNPEASAKTFVehDGrTWLRTGDLGFL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 494 dEDGYYVILGRTNaDIMKVGGYKLSALEIEAVL-LEHPTISECCVLGLPDKDYGEAVCAIIIpnpEIKRKREEELKPALT 572
Cdd:PRK05691 440 -RDGELFVTGRLK-DMLIVRGHNLYPQDIEKTVeREVEVVRKGRVAAFAVNHQGEEGIGIAA---EISRSVQKILPPQAL 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 747052525 573 LEELSMWAKEklAPYKIPNCLLLWE--SLPRNAMGKVNKKELKKQLAD 618
Cdd:PRK05691 515 IKSIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQRSACRLRLAD 560
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
85-612 |
1.88e-16 |
|
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: 82.13 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 85 SIAVTAHEKSHSYHQLilsAVKISNLLtgADLRsvkgngENKHLGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSY 164
Cdd:cd17654 7 IIDQTTSDTTVSYADL---AEKISNLS--NFLR------KKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 165 PEAELLHVMNDSDITMILsTEDHQELMKAIAVKTSAQMSLLpsvpsvstksteLDHtingeldgtrCLqeteipheisgd 244
Cdd:cd17654 76 PEQRSLTVMKKCHVSYLL-QNKELDNAPLSFTPEHRHFNIR------------TDE----------CL------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 245 dpALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHhvhglfnallaplYAGSTVEFMPKFSVRG 324
Cdd:cd17654 121 --AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLT-------------FDPSVVEIFLSLSSGA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 325 IWQRWRESYPQDQTKADDA------VTVFTGVPTmytrLIQGYEAMDPALQTASATAArqLRLMMCGSSALP-LPVMQKW 397
Cdd:cd17654 186 TLLIVPTSVKVLPSKLADIlfkrhrITVLQATPT----LFRRFGSQSIKSTVLSATSS--LRVLALGGEPFPsLVILSSW 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 398 --ETITGHVlLERYGMTEF-VMAISNPLKGKRKGGTVGKPLPGVqaKIIAEDgSCDNVEVGELCIKSPS---LFKEYWNL 471
Cdd:cd17654 260 rgKGNRTRI-FNIYGITEVsCWALAYKVPEEDSPVQLGSPLLGT--VIEVRD-QNGSEGTGQVFLGGLNrvcILDDEVTV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 472 PEVTkqsfidggFFKTGDAARVdEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTISECCVLgLPDKDygEAVCA 551
Cdd:cd17654 336 PKGT--------MRATGDFVTV-KDGELFFLGRKDSQI-KRRGKRINLDLIQQVIESCLGVESCAVT-LSDQQ--RLIAF 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 747052525 552 IIipnpeikrkreEELKPALTLEELSmwaKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17654 403 IV-----------GESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
244-606 |
2.78e-16 |
|
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: 82.32 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQmltdawgytsTDHFLHClPLHHVHGLF----------NALLAPLYAGST 313
Cdd:cd05943 249 DHPLYILYSSGTTGLPKCIVHGAGGTLLQHL----------KEHILHC-DLRPGDRLFyyttcgwmmwNWLVSGLAVGAT 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 314 V------EFMPKFSVRgiwqrWRESypqDQTKaddaVTVFTGVPTMYTRLIQGYeaMDPA----LQTasataarqLRLMM 383
Cdd:cd05943 318 IvlydgsPFYPDTNAL-----WDLA---DEEG----ITVFGTSAKYLDALEKAG--LKPAethdLSS--------LRTIL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 384 CGSSALPlPVMQKW--ETITGHVLLERY-GMTEFV--MAISNPLKGKRKGGTVGKPLpGVQAKIIAEDGSCDNVEVGELC 458
Cdd:cd05943 376 STGSPLK-PESFDYvyDHIKPDVLLASIsGGTDIIscFVGGNPLLPVYRGEIQCRGL-GMAVEAFDEEGKPVWGEKGELV 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 459 IKS--PSLFKEYWNLPEVTK--QSFID--GGFFKTGDAARVDEDGYYVILGRTNADImKVGGYKLSALEIEAVLLEHPTI 532
Cdd:cd05943 454 CTKpfPSMPVGFWNDPDGSRyrAAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTL-NPGGVRIGTAEIYRVVEKIPEV 532
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 747052525 533 SECCVLGLPDKDYGEAVcaIIIpnpeIKRKREEELKPALtLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGK 606
Cdd:cd05943 533 EDSLVVGQEWKDGDERV--ILF----VKLREGVELDDEL-RKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
241-539 |
3.04e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 82.46 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 241 ISGDDP---ALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDaWG----YTSTDHFLHcLPLHHVHGLFNALLApLYAGST 313
Cdd:PTZ00342 298 IQNEDPdfiTSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK-HSifkkYNPKTHLSY-LPISHIYERVIAYLS-FMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 314 VEfmpkfsvrgIWQRWRESYPQD--QTKADdavtVFTGVPTMYTRL---IQGYEAMDPALQTASATAARQLRL-MMCG-- 385
Cdd:PTZ00342 375 IN---------IWSKDINYFSKDiyNSKGN----ILAGVPKVFNRIytnIMTEINNLPPLKRFLVKKILSLRKsNNNGgf 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 386 ----------SSALPLPVMQKWETI-TG------------HVLL-----ERYGMTEfvmaISNPLKGKRKGGT----VGK 433
Cdd:PTZ00342 442 skflegithiSSKIKDKVNPNLEVIlNGggklspkiaeelSVLLnvnyyQGYGLTE----TTGPIFVQHADDNntesIGG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 434 PL-PGVQAKIIAED--GSCDNVEVGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVDEDGYYVILGRTNadim 510
Cdd:PTZ00342 518 PIsPNTKYKVRTWEtyKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK---- 593
|
330 340 350
....*....|....*....|....*....|....*
gi 747052525 511 kvGGYKLSALE-IEAVLL-----EHPTISECCVLG 539
Cdd:PTZ00342 594 --GLVKLSQGEyIETDMLnnlysQISFINFCVVYG 626
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
236-576 |
1.85e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 79.86 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 236 EIPHEISGDDP---ALIIYTSGTTGKPKGVVHTHKGVLAQV------------QMLTDawgytstDHFLHCLPLHHV--- 297
Cdd:PLN02430 209 ENPSETNPPKPldiCTIMYTSGTSGDPKGVVLTHEAVATFVrgvdlfmeqfedKMTHD-------DVYLSFLPLAHIldr 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 298 ----------------HGLFNALLAPLyagstVEFMPkfsvrgiwqrwresypqdqtkaddavTVFTGVPTMYTRLiqgY 361
Cdd:PLN02430 282 mieeyffrkgasvgyyHGDLNALRDDL-----MELKP--------------------------TLLAGVPRVFERI---H 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 362 EAMDPALQ----------------------------TASATA---------AR---QLRLMMCGSSALPLPVMQKWETIT 401
Cdd:PLN02430 328 EGIQKALQelnprrrlifnalykyklawmnrgyshkKASPMAdflafrkvkAKlggRLRLLISGGAPLSTEIEEFLRVTS 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 402 GHVLLERYGMTEfvmaisnPLKGKRKG--------GTVGkpLPGVQAKIIAEDGS------CDNVEVGELCIKSPSLFKE 467
Cdd:PLN02430 408 CAFVVQGYGLTE-------TLGPTTLGfpdemcmlGTVG--APAVYNELRLEEVPemgydpLGEPPRGEICVRGKCLFSG 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 468 YWNLPEVTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALE-IEAVLLEHPTISECCVLGlpdKDYG 546
Cdd:PLN02430 479 YYKNPELTEEVMKD-GWFHTGDIGEILPNGVLKIIDRKK-NLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG---DSFK 553
|
410 420 430
....*....|....*....|....*....|
gi 747052525 547 EAVCAIIIPNPEIKRKREEELKPALTLEEL 576
Cdd:PLN02430 554 SMLVAVVVPNEENTNKWAKDNGFTGSFEEL 583
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
244-615 |
1.01e-14 |
|
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: 77.14 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPK--FS 321
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTrlFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 322 VRGI-WQRWRESYPQDQTKADD----------AVTVFTGVPTMYTRLI-QGYEAMDPAL-----QTASATAARQLRLMMC 384
Cdd:cd05908 186 RRPIlWLKKASEHKATIVSSPNfgykyflktlKPEKANDWDLSSIRMIlNGAEPIDYELcheflDHMSKYGLKRNAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 385 -----GSSALPLPVMQKWETItghVLLERYGMT--EFVMAISnplKGKRKGGT---VGKPLPGVQAKIIAEDGS-CDNVE 453
Cdd:cd05908 266 yglaeASVGASLPKAQSPFKT---ITLGRRHVThgEPEPEVD---KKDSECLTfveVGKPIDETDIRICDEDNKiLPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 454 VGELCIKSPSLFKEYWNLPEVTKQSFIDGGFFKTGDAARVdEDGYYVILGRTNaDIMKVGGYKLSALEIE--AVLLEHPT 531
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREK-DIIFVNGQNVYPHDIEriAEELEGVE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 532 ISECCVLGLPDKDYG--EAVCAIiipnpeIKRKREEELKPALT-----LEELSMWAKEKLAPYKIpnclllwesLPRNAM 604
Cdd:cd05908 418 LGRVVACGVNNSNTRneEIFCFI------EHRKSEDDFYPLGKkikkhLNKRGGWQINEVLPIRR---------IPKTTS 482
|
410
....*....|.
gi 747052525 605 GKVNKKELKKQ 615
Cdd:cd05908 483 GKVKRYELAQR 493
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
130-351 |
2.34e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 73.22 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPL-ALSYP-EAELLH-VMNDSDITMILSTEDHQELMKAIAVKTSAQMSllP 206
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPgHVGRLHaVLDDCTPSAILTTTDSAEGVRKFFRARPAKER--P 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 207 SVPSVSTKSTELDhtingeldgtrclqETEIPHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYTSTD 286
Cdd:PRK07769 157 RVIAVDAVPDEVG--------------ATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGD 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 747052525 287 HFLHCLPLHHVHGLFNALLAPLyAGSTVEFM-PKFSVR--GIWQRwresypQDQTKADDAVTVFTGVP 351
Cdd:PRK07769 223 RGVSWLPFFHDMGLITVLLPAL-LGHYITFMsPAAFVRrpGRWIR------ELARKPGGTGGTFSAAP 283
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
130-537 |
3.01e-13 |
|
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: 72.77 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTE-DHQELMKAI-AVKT---SAQMSL 204
Cdd:cd05905 40 GDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVEaCLKGLPKKLlKSKTaaeIAKKKG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 205 LPSVPSVSTKSTEldhtingeldgTRCLQETEIPHEI-SGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGYT 283
Cdd:cd05905 120 WPKILDFVKIPKS-----------KRSKLKKWGPHPPtRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 284 STDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIWQRWRESYPQDQTKaddavTVFTGVPTMYTRLiqgyea 363
Cdd:cd05905 189 ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVR-----DAYVKLRTLHWCL------ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 364 mdpaLQTASATAARQLR------LMMCGSSALPLP---VMQKW-ETITGHVLLERYGMTEFvMAISNPLKGKRKGGT--- 430
Cdd:cd05905 258 ----KDLSSTLASLKNRdvnlssLRMCMVPCENRPrisSCDSFlKLFQTLGLSPRAVSTEF-GTRVNPFICWQGTSGpep 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 431 ------------------------------VGKPLPGVQAKIIAEDGS--CDNVEVGELCIKSPSLFKEYWNLPEVTKQ- 477
Cdd:cd05905 333 srvyldmralrhgvvrlderdkpnslplqdSGKVLPGAQVAIVNPETKglCKDGEIGEIWVNSPANASGYFLLDGETNDt 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 478 ---------SFIDGG--FFKTGD----------AARVDEDGYYVILGRTNaDIMKVGGYKLSALEIEA-VLLEHPTISEC 535
Cdd:cd05905 413 fkvfpstrlSTGITNnsYARTGLlgflrptkctDLNVEEHDLLFVVGSID-ETLEVRGLRHHPSDIEAtVMRVHPYRGRC 491
|
..
gi 747052525 536 CV 537
Cdd:cd05905 492 AV 493
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
127-556 |
3.56e-13 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 72.46 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 127 HLGGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSteDHQELMKAIAVktSAQMSLLP 206
Cdd:PLN02387 128 HNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC--DSKQLKKLIDI--SSQLETVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 207 SVPSVSTKSTELDHTINGELDGT--------RCLQETEI-PHEISGDDPALIIYTSGTTGKPKGVVHTHKGVLAQVQ-ML 276
Cdd:PLN02387 204 RVIYMDDEGVDSDSSLSGSSNWTvssfseveKLGKENPVdPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgVM 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 277 TDAWGYTSTDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPKFSVRGIWQRWRESypqdqTKADDAV---TVFTGVPTM 353
Cdd:PLN02387 284 TVVPKLGKNDVYLAYLPLAHILEL-AAESVMAAVGAAIGYGSPLTLTDTSNKIKKG-----TKGDASAlkpTLMTAVPAI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 354 --------------------------YTRLIQ----------GYEAM---DPALQTASATAARQLRLMMCGSSALPlPVM 394
Cdd:PLN02387 358 ldrvrdgvrkkvdakgglakklfdiaYKRRLAaiegswfgawGLEKLlwdALVFKKIRAVLGGRIRFMLSGGAPLS-GDT 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 395 QKWETIT-GHVLLERYGMTEFVM--AISNPlkGKRKGGTVGKPLPGVQAKIIA-EDG----SCDNVEVGELCIKSPSLFK 466
Cdd:PLN02387 437 QRFINIClGAPIGQGYGLTETCAgaTFSEW--DDTSVGRVGPPLPCCYVKLVSwEEGgyliSDKPMPRGEIVIGGPSVTL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 467 EYWNLPEVTKQSF-IDGG---FFKTGDAARVDEDGYYVILGRTNaDIMKV--GGYkLSALEIEAVLLEHPTISECCVLGL 540
Cdd:PLN02387 515 GYFKNQEKTDEVYkVDERgmrWFYTGDIGQFHPDGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHAD 592
|
490
....*....|....*..
gi 747052525 541 PDKDYgeavC-AIIIPN 556
Cdd:PLN02387 593 PFHSY----CvALVVPS 605
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
240-599 |
7.99e-13 |
|
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: 71.17 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 240 EISGDDPALIIYTSGTTGKPKGVVHTHKGVLaQVQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPK 319
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 320 FSVRGIWQRWRESypqdqtkaddAVTVFtgvptMYTRLIQGYEAMDPalQTASATAARqLRLMMcGSSALPlpvmQKWET 399
Cdd:cd05938 219 FSASQFWDDCRKH----------NVTVI-----QYIGELLRYLCNQP--QSPNDRDHK-VRLAI-GNGLRA----DVWRE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 400 IT---GHV-LLERYGMTEFVMAISNpLKGKRkgGTVGK---------PLPGVQAKIIAE------DGSCDNVEVGE---- 456
Cdd:cd05938 276 FLrrfGPIrIREFYGSTEGNIGFFN-YTGKI--GAVGRvsylykllfPFELIKFDVEKEepvrdaQGFCIPVAKGEpgll 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 457 LC-IKSPSLFKEYWNLPEVTKQS-----FIDGG-FFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEH 529
Cdd:cd05938 353 VAkITQQSPFLGYAGDKEQTEKKllrdvFKKGDvYFNTGDLLVQDQQNFLYFHDRV-GDTFRWKGENVATTEVADVLGLL 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 747052525 530 PTISECCVLGLPDKDY-GEAVCAIIIpnpeikrkreeeLKP--ALTLEELSMWAKEKLAPYKIPNCLLLWESL 599
Cdd:cd05938 432 DFLQEVNVYGVTVPGHeGRIGMAAVK------------LKPghEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
133-540 |
3.03e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 69.41 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 133 VGIVAKPSPEFVAGVLGTWFSGGvAVPL---------ALSYPEAELLHVMNdSDITMILSTEDHQELMKAIavktsaqms 203
Cdd:PRK05851 57 VGLVGEPTVELVAAIQGAWLAGA-AVSIlpgpvrgadDGRWADATLTRFAG-IGVRTVLSHGSHLERLRAV--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 204 llpsVPSVSTKS-TELDHTingeldgTRCLQETEIPHEisgdDPALIIYTSGTTGKPKGVVHTHKGVLAQVQMLTDAWGY 282
Cdd:PRK05851 126 ----DSSVTVHDlATAAHT-------NRSASLTPPDSG----GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 283 TS-TDHFLHCLPLHHVHGLfNALLAPLYAGSTVEFMPK--FSVRGI-WQRWresypqdqtkADDAVTVFTGVPTM----- 353
Cdd:PRK05851 191 DAaTDVGCSWLPLYHDMGL-AFLLTAALAGAPLWLAPTtaFSASPFrWLSW----------LSDSRATLTAAPNFaynli 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 354 --YTRLIQGYE--AMDPALQTAsataarqlRLMMCGSSALPLPVMQKWETITGhVLLERYGMTEFVMAISNPLKG----- 424
Cdd:PRK05851 260 gkYARRVSDVDlgALRVALNGG--------EPVDCDGFERFATAMAPFGFDAG-AAAPSYGLAESTCAVTVPVPGiglrv 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 425 ----------KRKGGTVGKPLPGVQAKIIAEDGSCDNV--EVGELCIKSPSLFKEYwnlpeVTKQSFIDGGFFKTGDAAR 492
Cdd:PRK05851 331 devttddgsgARRHAVLGNPIPGMEVRISPGDGAAGVAgrEIGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGY 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 747052525 493 VDEDGyYVILGRTNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGL 540
Cdd:PRK05851 406 LVDGG-LVVCGRAK-ELITVAGRNIFPTEIERVAAQVRGVREGAVVAV 451
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
130-317 |
7.68e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 68.05 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLalSYPEAELLH-----VMNDSDITMILSTEdhqelmkAIA--VKTSAQM 202
Cdd:PRK05850 59 GDRAVILAPQGLEYIVAFLGALQAGLIAVPL--SVPQGGAHDervsaVLRDTSPSVVLTTS-------AVVddVTEYVAP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 203 SLLPSVPSVstksTELDhTINgeLDGTRCLQETEIPHeisgDDPALIIYTSGTTGKPKGVVHTHKGVLAQV-QMLTDAWG 281
Cdd:PRK05850 130 QPGQSAPPV----IEVD-LLD--LDSPRGSDARPRDL----PSTAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 747052525 282 YT-----STDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFM 317
Cdd:PRK05850 199 DTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLT 239
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
130-559 |
2.62e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 66.58 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 130 GARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDITMILSTEDH-QELMKAIAvKTSAQMSLLPSV 208
Cdd:PLN02614 104 EAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKiSELFKTCP-NSTEYMKTVVSF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 209 PSVSTKSTELDHTIN------GELDGTRCLQETEIPHEiSGDDPALIIYTSGTTGKPKGVVHTHKGVL----AQVQMLTD 278
Cdd:PLN02614 183 GGVSREQKEEAETFGlviyawDEFLKLGEGKQYDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVtliaGVIRLLKS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 279 A-WGYTSTDHFLHCLPLHHVhglFNALLAPLY--AGSTVEFMpKFSVRGIWQRWRESYPqdqtkaddavTVFTGVPTMYT 355
Cdd:PLN02614 262 AnAALTVKDVYLSYLPLAHI---FDRVIEECFiqHGAAIGFW-RGDVKLLIEDLGELKP----------TIFCAVPRVLD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 356 RLIQGYE--------------------------------AMDPALQTASATAARQ-----LRLMMCGSSALPLPVMQKWE 398
Cdd:PLN02614 328 RVYSGLQkklsdggflkkfvfdsafsykfgnmkkgqshvEASPLCDKLVFNKVKQglggnVRIILSGAAPLASHVESFLR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 399 TITGHVLLERYGMTEFVMAISNPLKGKRKG-GTVGKPLPGVQAKIIA----EDGSCDNVEVGELCIKSPSLFKEYWNLPE 473
Cdd:PLN02614 408 VVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESvpemEYDALASTPRGEICIRGKTLFSGYYKRED 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 474 VTKQSFIDgGFFKTGDAARVDEDGYYVILGRTNaDIMKVGGYKLSALE-IEAVLLEHPTISECCVLGlpdKDYGEAVCAI 552
Cdd:PLN02614 488 LTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKK-NIFKLSQGEYVAVEnIENIYGEVQAVDSVWVYG---NSFESFLVAI 562
|
....*..
gi 747052525 553 IIPNPEI 559
Cdd:PLN02614 563 ANPNQQI 569
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
113-524 |
7.24e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.15 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 113 GADLRSVKGNGEnkhlggaRVGIVAKPSPEFVAGVLGTWFSGGVAVPL-ALSYP-EAELLH-VMNDSDITMILST----E 185
Cdd:PRK12476 82 GARLQQVAGPGD-------RVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPgHAERLDtALRDAEPTVVLTTtaaaE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 186 DHQELMKAIAVKTSAQMSLLPSVPSvstksteldhtingeldgtrCLQETEIPHEISGDDPALIIYTSGTTGKPKGVVHT 265
Cdd:PRK12476 155 AVEGFLRNLPRLRRPRVIAIDAIPD--------------------SAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEIT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 266 HKGVLAQ-VQMLTDAWGYTSTDHFLHCLPLHHVHGLFNALLAPLYAGSTVEFMPKFSVRGIwQRWRESYpqdqTKADDAV 344
Cdd:PRK12476 215 HRAVGTNlVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRP-QRWIKAL----SEGSRTG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 345 TVFTGVPTMytrliqgyeAMDPALQTASATAARQLRL----MMCGSSALPLPVMQKWETITGHVLLER------YGMTE- 413
Cdd:PRK12476 290 RVVTAAPNF---------AYEWAAQRGLPAEGDDIDLsnvvLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEa 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 414 --FVMAISNPLKGK-----RKGGTV-------------------GKPLPGVQAKIIAEDGSCD--NVEVGELCIKSPSLF 465
Cdd:PRK12476 361 tlFVATIAPDAEPSvvyldREQLGAgravrvaadapnavahvscGQVARSQWAVIVDPDTGAElpDGEVGEIWLHGDNIG 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 747052525 466 KEYWNLPEVTKQSF------------------IDGGFFKTGDAArVDEDGYYVILGRTnADIMKVGGYKLSALEIEA 524
Cdd:PRK12476 441 RGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLG-VYLDGELYITGRI-ADLIVIDGRNHYPQDIEA 515
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
96-615 |
3.48e-10 |
|
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: 62.44 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 96 SYHQLILSAVKISNLLTGADLRSvkgngenkhlgGARVGIVAKPSPEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMND 175
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRS-----------GDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 176 SditmilstedhqelmKAIAVKTSAQMSLLpsvpsvSTKSTELDHTINGELDgtrclqeteipheisgdDPALIIYTSGT 255
Cdd:cd05939 74 S---------------KAKALIFNLLDPLL------TQSSTEPPSQDDVNFR-----------------DKLFYIYTSGT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 256 TGKPKGVVHTHKGVLAQVQMLTDAWGYTSTDHFLHCLPLHH----VHGLFNALLaplyAGSTVEFMPKFSVRGIWqrwre 331
Cdd:cd05939 116 TGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNFW----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 332 sypQDQTKADDAVTVFTGVPTMYTrliqgyeamdpaLQTASATAARQLRL-MMCGSSALPlpvmQKWETITGHV----LL 406
Cdd:cd05939 187 ---DDCVKYNCTIVQYIGEICRYL------------LAQPPSEEEQKHNVrLAVGNGLRP----QIWEQFVRRFgipqIG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 407 ERYGMTEFVMAISNplkgkrKGGTVGK------------PLPGVQAK------IIAEDGSC-------DNVEVGELCIKS 461
Cdd:cd05939 248 EFYGATEGNSSLVN------IDNHVGAcgfnsrilpsvyPIRLIKVDedtgelIRDSDGLCipcqpgePGLLVGKIIQND 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 462 PSL-FKEYWNLPEVTKQ----SFIDGG-FFKTGDAARVDEDGYYVILGRTnADIMKVGGYKLSALEIEAVLLEHPTISEC 535
Cdd:cd05939 322 PLRrFDGYVNEGATNKKiardVFKKGDsAFLSGDVLVMDELGYLYFKDRT-GDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 536 CVLG--LPDKDyGEAVCAIIIpNPEIKrkreeelkpaLTLEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK 613
Cdd:cd05939 401 VVYGveVPGVE-GRAGMAAIV-DPERK----------VDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
..
gi 747052525 614 KQ 615
Cdd:cd05939 469 KE 470
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
453-612 |
6.19e-10 |
|
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: 61.76 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF----------------------------FKTGDAARVDEDGYYVILGR 504
Cdd:cd17647 314 EVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 505 TNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIP--NPEIKRKREEELKPALTLEE------- 575
Cdd:cd17647 394 AD-DQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPrfDKPDDESFAQEDVPKEVSTDpivkgli 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 747052525 576 --------LSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKEL 612
Cdd:cd17647 473 gyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
244-545 |
5.25e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 52.88 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 244 DDPALIIYTSGTTGKPKGVVHTHKGVLAQvqmltdawgytstdHflhcLPLHHVHG-------LF----------NALLA 306
Cdd:PRK03584 263 DHPLWILYSSGTTGLPKCIVHGHGGILLE--------------H----LKELGLHCdlgpgdrFFwyttcgwmmwNWLVS 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 307 PLYAGSTV------EFMPKFSVrgIWQRwresypqdqtkADDA-VTVFTGVPTMYTrliqgyeamdpALQTASATAARQ- 378
Cdd:PRK03584 325 GLLVGATLvlydgsPFYPDPNV--LWDL-----------AAEEgVTVFGTSAKYLD-----------ACEKAGLVPGETh 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 379 ----LRLMMCGSSALPlPVMQKW--ETITGHVLLERY-GMTEFV--MAISNPLKGKRKGGTVGKPLpGVQAKIIAEDGSC 449
Cdd:PRK03584 381 dlsaLRTIGSTGSPLP-PEGFDWvyEHVKADVWLASIsGGTDICscFVGGNPLLPVYRGEIQCRGL-GMAVEAWDEDGRP 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 450 DNVEVGEL-CIKS-PS--LFkeYWNLPEVTK--QSFIDG--GFFKTGDAARVDEDGYYVILGRTNADIMKvGGYKLSALE 521
Cdd:PRK03584 459 VVGEVGELvCTKPfPSmpLG--FWNDPDGSRyrDAYFDTfpGVWRHGDWIEITEHGGVVIYGRSDATLNR-GGVRIGTAE 535
|
330 340
....*....|....*....|....*.
gi 747052525 522 IEAVLLEHPTISECCVLGL--PDKDY 545
Cdd:PRK03584 536 IYRQVEALPEVLDSLVIGQewPDGDV 561
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
453-617 |
1.10e-06 |
|
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: 51.99 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 453 EVGELCIKSPSLFKEYWNLPEVTKQSFIDGGF----------------------------FKTGDAARVDEDGYYVILGR 504
Cdd:TIGR03443 620 EVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlYRTGDLGRYLPDGNVECCGR 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 505 TNaDIMKVGGYKLSALEIEAVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEikrKRE-EELKPALTLEE-------- 575
Cdd:TIGR03443 700 AD-DQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDK---SDElEEFKSEVDDEEssdpvvkg 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 747052525 576 ----------LSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELK----KQLA 617
Cdd:TIGR03443 776 likyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdtAQLA 831
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
488-619 |
1.11e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 48.27 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 488 GDAARVDEDGYYVILGRTNaDIMKVGGYKLSALEIE-AVLLEHPTISECCVLGLPDKDYGEAVCAIIIPNPEIKRKREEE 566
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRAD-DTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQA 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 747052525 567 LKPALTlEELSMWAKEKLAPYKIPNCLLLWESLPRNAMGKVNKKELKKQLADQ 619
Cdd:PLN03051 441 RPEALQ-KKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKE 492
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
496-620 |
2.71e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 47.38 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 747052525 496 DGYYVILGRTNaDIMKVGGYKLSALEIEAVL-LEHPTISECCVLGLPDKDYG--EAVCAIIIPNPEIKRKREEELKPALT 572
Cdd:PLN03052 602 GGYYRAHGRAD-DTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFN 680
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 747052525 573 LEelsmwAKEKLAP-YKIpNCLLLWESLPRNAMGKVNKKELKKQLADQV 620
Cdd:PLN03052 681 SA-----IQKKLNPlFKV-SAVVIVPSFPRTASNKVMRRVLRQQLAQEL 723
|
|
| |
