|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1-653 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 1028.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 1 MNAIATEADVLRIENQGPPA-DLPASTYEMIGRGAAIDPSAPALSFFLRADDHRKPLRWTYAALLRDITRAANMFSRLGI 79
Cdd:PRK07529 1 MPAFATLADIEAIEAVPLAArDLPASTYELLSRAAARHPDAPALSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 80 DRHAVVAYVLPNLPETHFVIWGGEAAGIVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSEVPSLQS 159
Cdd:PRK07529 81 GPGDVVAFLLPNLPETHFALWGGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAALPELRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 160 LVLIDLAERVQGWRRIAARAMQRreckrlhgragvrgavPRHVAIHDFDSAMSRESGDSLLIPRRFEADDISSYFCTGGT 239
Cdd:PRK07529 161 VVEVDLARYLPGPKRLAVPLIRR----------------KAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 240 TGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGYRGDGVVKRFWE 319
Cdd:PRK07529 225 TGMPKLAQHTHGNEVANAWLGALLLGLG--PGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVIANFWK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 320 IVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGE 399
Cdd:PRK07529 303 IVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 400 RRLGSIGLRIPGQMMKAVILDDAGRYVRDCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDlgdgRQWLNTGDLARRDAQ 479
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLE----DGWLNTGDLGRIDAD 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 480 GYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGER 559
Cdd:PRK07529 459 GYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAER 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 560 AAIPKRIHIVDAMPLTAVGKIFKPELKRWETFDALVSALKDAGVEGARVSMVDDPSRGLTLHVALSDHAQTAKANTVMGR 639
Cdd:PRK07529 539 AAVPKHVRILDALPKTAVGKIFKPALRRDAIRRVLRAALRDAGVEAEVVDVVEDGRRGLVAQVALRGAEDREAVAAVLGR 618
|
650
....*....|....
gi 1142773712 640 FPFAFSTSVEPEHH 653
Cdd:PRK07529 619 YAFPWEISTADPHA 632
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-587 |
1.76e-165 |
|
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: 477.74 E-value: 1.76e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQG 307
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALN--SLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 308 YRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDgRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEG 387
Cdd:cd05944 80 YRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVN-ADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 388 ACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDDAGRYVRDCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqW 467
Cdd:cd05944 159 TCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADG----W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 468 LNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETE 547
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1142773712 548 LDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05944 315 LLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
27-588 |
1.36e-118 |
|
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: 361.05 E-value: 1.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFGGR--------RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 -IVCAINPLLEGPAIASLLKAANAKVLVTLApfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrrec 185
Cdd:COG0318 74 aVVVPLNPRLTAEELAYILEDSGARALVTAL------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 186 krlhgragvrgavprhvaihdfdsamsresgdslliprrfeaddissYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVG 265
Cdd:COG0318 105 -----------------------------------------------ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 266 agMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVP-V 344
Cdd:COG0318 138 --LTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL------LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPeF 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 DGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPP-GGERRLGSIGLRIPGQMMKavILDDAG 423
Cdd:COG0318 210 ARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEdPGERRPGSVGRPLPGVEVR--IVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 424 RyvrDCVENEVGVLTISGPNVFAGYLQ-EDQNKSLwldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPA 502
Cdd:COG0318 288 R---ELPPGEVGEIVVRGPNVMKGYWNdPEATAEA---FRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPA 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 503 TIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFK 582
Cdd:COG0318 360 EVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLA-RYKVPRRVEFVDELPRTASGKIDR 438
|
....*.
gi 1142773712 583 PELKRW 588
Cdd:COG0318 439 RALRER 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
27-586 |
5.72e-114 |
|
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: 349.94 E-value: 5.72e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMGR--------KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 -IVCAINPLLEGPAIASLLKAANAKVLVTLAPFpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreC 185
Cdd:cd05936 74 aVVVPLNPLYTPRELEHILNDSGAKALIVAVSF----------------------------------------------T 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 186 KRLHGRAGVRGAVPRHvaihdfdsamsresgdslliprrfeADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVG 265
Cdd:cd05936 108 DLLAAGAPLGERVALT-------------------------PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 266 AGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgTPQgYRGDGVVKrfweIVEHHRINFFSAVPTLYSALLDVP-V 344
Cdd:cd05936 163 DLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVL-IPR-FRPIGVLK----EIRKHRVTIFPGVPTMYIALLNAPeF 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 DGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGR 424
Cdd:cd05936 237 KKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPG--TEVKIVDDDGE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 425 YVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLWLDlgDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATI 504
Cdd:cd05936 315 ELPP---GEVGELWVRGPQVMKGYWNRPEETAEAFV--DG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREV 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 505 EEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIF 581
Cdd:cd05936 388 EEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCR----EQLAgykVPRQVEFRDELPKSAVGKIL 463
|
....*
gi 1142773712 582 KPELK 586
Cdd:cd05936 464 RRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
229-580 |
6.54e-92 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 288.03 E-value: 6.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 229 DISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVnAVLATGLVPFSRGAHVVLgtpqgy 308
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 309 RGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTE- 386
Cdd:cd04433 72 LPKFDPEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 GACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLwlDLGDGrq 466
Cdd:cd04433 152 GGTVATGPPDDDARKPGSVGRPVPG--VEVRIVDPDGGELPP---GEIGELVVRGPSVMKGYWNNPEATAA--VDEDG-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:cd04433 223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 1142773712 547 ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd04433 303 ELRAHVRERLA-PYKVPRRVVFVDALPRTASGKI 335
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
27-603 |
3.67e-91 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 293.56 E-value: 3.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSFflrADDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIW---EGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 -IVCAINPLLEGPAIASLLKAANAKVLVT----LAPFPGSDIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramq 181
Cdd:COG0365 89 aVHSPVFPGFGAEALADRIEDAEAKVLITadggLRGGKVIDLKEKVDEALEELPSLEHVIVVG----------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 182 rreckRLHGRAGVRGAvprhvaiHDFDSAMSRESGDslLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVG 261
Cdd:COG0365 152 -----RTGADVPMEGD-------LDWDELLAAASAE--FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 262 QVVgAGMGPGKTVFCGLPLF----HVNAVLAtglvPFSRGAHVVL--GTPqGYRGDGvvkRFWEIVEHHRINFFSAVPTL 335
Cdd:COG0365 218 KYV-LDLKPGDVFWCTADIGwatgHSYIVYG----PLLNGATVVLyeGRP-DFPDPG---RLWELIEKYGVTVFFTAPTA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 336 YSALL---DVPVDGRNIDSLEygLCGAA--PMPVEVFRTFQDRTGVRILEGYGLTE-GACVSSvNPPGGERRLGSIGLRI 409
Cdd:COG0365 289 IRALMkagDEPLKKYDLSSLR--LLGSAgePLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFIS-NLPGLPVKPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 410 PGqmMKAVILDDAGryvRDCVENEVGVLTISG--PNVFAGYLQEDQ-NKSLWLDLGDGrqWLNTGDLARRDAQGYFWLTG 486
Cdd:COG0365 366 PG--YDVAVVDEDG---NPVPPGEEGELVIKGpwPGMFRGYWNDPErYRETYFGRFPG--WYRTGDGARRDEDGYFWILG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 487 RRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET---ELDTFIRGMIGERAAiP 563
Cdd:COG0365 439 RSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAY-P 517
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1142773712 564 KRIHIVDAMPLTAVGKIFKPELKRWETFDAL--VSALKDAGV 603
Cdd:COG0365 518 REIEFVDELPKTRSGKIMRRLLRKIAEGRPLgdTSTLEDPEA 559
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
21-587 |
4.93e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 286.70 E-value: 4.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 21 DLPASTYEMIGRGAAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEtHFVIW 100
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGR--------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHE-YLEAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 101 -GGEAAGIVCA-INPLLEGPAIASLLKAANAKVLVTlapfpGSDIWSKIQPVLSEVPSLQSLVLIdlaervqgwrriaar 178
Cdd:PRK06187 74 fAVPKIGAVLHpINIRLKPEEIAYILNDAEDRVVLV-----DSEFVPLLAAILPQLPTVRTVIVE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 179 amqrreckrlhgraGVRGAVPRHVAIHDFDSAMSRESGDSLLIPrrFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAW 258
Cdd:PRK06187 134 --------------GDGPAAPLAPEVGEYEELLAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 259 SVGQvvGAGMGPGKTVFCGLPLFHVNAvLATGLVPFSRGAHVVLgtpqgyrgdgvVKRF-----WEIVEHHRINFFSAVP 333
Cdd:PRK06187 198 AVCA--WLKLSRDDVYLVIVPMFHVHA-WGLPYLALMAGAKQVI-----------PRRFdpenlLDLIETERVTFFFAVP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 334 TLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPP-----GGERRLGSIGL 407
Cdd:PRK06187 264 TIWQMLLKAPrAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpGQWTKRRSAGR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 408 RIPGqmMKAVILDDAGRYV-RDcvENEVGVLTISGPNVFAGYL-QEDQNKSLWLDlgdGrqWLNTGDLARRDAQGYFWLT 485
Cdd:PRK06187 344 PLPG--VEARIVDDDGDELpPD--GGEVGEIIVRGPWLMQGYWnRPEATAETIDG---G--WLHTGDVGYIDEDGYLYIT 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 486 GRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKR 565
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLA-KFKLPKR 493
|
570 580
....*....|....*....|..
gi 1142773712 566 IHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK06187 494 IAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
32-582 |
1.04e-88 |
|
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: 282.96 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALSFflradDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-CA 110
Cdd:cd17631 3 RRARRHPDRTALVF-----GGR---SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVfVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 111 INPLLEGPAIASLLKAANAKVLVtlapfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhg 190
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 191 ragvrgavprhvaihdfdsamsresgdslliprrfeaDDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGP 270
Cdd:cd17631 98 -------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA--VNALAALDLGP 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 271 GKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtPQGYRGDgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNI 349
Cdd:cd17631 139 DDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI--LRKFDPE----TVLDLIERHRVTSFFLVPTMIQALLQHPRfATTDL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 350 DSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGYGLTEGACVSSVNPPGG-ERRLGSIGLRIPGqmMKAVILDDAGRYVRD 428
Cdd:cd17631 213 SSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDhRRKLGSAGRPVFF--VEVRIVDPDGREVPP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 429 cveNEVGVLTISGPNVFAGYL-QEDQNKSLwldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEP 507
Cdd:cd17631 290 ---GEVGEIVVRGPHVMAGYWnRPEATAAA---FRDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDV 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 508 LHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFK 582
Cdd:cd17631 362 LYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLA-RYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-586 |
6.21e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 278.33 E-value: 6.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 23 PASTYEMIGRGAAIDPSAPALSFflraddhrKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPetHFVI--W 100
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVF--------GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSP--HWVIaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 101 GGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGSDiwskiQPVLSEVPSLQSLVLIDlaervqgwrriaara 179
Cdd:PRK07656 74 GALKAGaVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVD-----YSATTRLPALEHVVICE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 180 mqrreckrlhgragVRGAVPRHVAIHDFDSAMSResGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWS 259
Cdd:PRK07656 134 --------------TEEDDPHTEKMKTFTDFLAA--GDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAAD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 260 VGQVvgAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVlgtpqgyrgdgVVKRF-----WEIVEHHRINFFSAVPT 334
Cdd:PRK07656 198 WAEY--LGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATIL-----------PLPVFdpdevFRLIETERITVLPGPPT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 335 LYSALLDVPvDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVR-ILEGYGLTEGACVSSVNPPGGERRL--GSIGLRI 409
Cdd:PRK07656 265 MYNSLLQHP-DRSAEDlsSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDDRKTvaGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 410 PGQMMKavILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRK 489
Cdd:PRK07656 344 AGVENK--IVNELGEEVPV---GEVGELLVRGPNVMKGYYDDPEATAAAID-ADG--WLHTGDLGRLDEEGYLYIVDRKK 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 490 ELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmigERAA---IPKRI 566
Cdd:PRK07656 416 DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCR----EHLAkykVPRSI 491
|
570 580
....*....|....*....|
gi 1142773712 567 HIVDAMPLTAVGKIFKPELK 586
Cdd:PRK07656 492 EFLDELPKNATGKVLKRALR 511
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-580 |
1.37e-82 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 268.80 E-value: 1.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 38 PSAPALSfflrADDHRKplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCA-INPLLE 116
Cdd:cd05926 1 PDAPALV----VPGSTP--ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVApLNPAYK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 117 GPAIASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSevpslqslvLIDLAERVQGwrriaaramqrrecKRLHGRAGVrg 196
Cdd:cd05926 75 KAEFEFYLADLGSKLVLTPKGELGPASRAASKLGLA---------ILELALDVGV--------------LIRAPSAES-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 197 avprhVAIHDFDSAMSRESGDSLliprrfeADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFC 276
Cdd:cd05926 130 -----LSNLLADKKNAKSEGVPL-------PDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK--LTPDDRTLV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 277 GLPLFHVNAVLATGLVPFSRGAHVVLgtPQGYRGdgvvKRFWEIVEHHRINFFSAVPTLYSALLDVPV--DGRNIDSLEY 354
Cdd:cd05926 196 VMPLFHVHGLVASLLSTLAAGGSVVL--PPRFSA----STFWPDVRDYNATWYTAVPTIHQILLNRPEpnPESPPPKLRF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 355 GLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNP-PGGERRLGSIGlriPGQMMKAVILDDAGRYVRDCVENE 433
Cdd:cd05926 270 IRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPlPPGPRKPGSVG---KPVGVEVRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 434 VgvlTISGPNVFAGYLQ-EDQNKSLWLdlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHP 512
Cdd:cd05926 347 I---CLRGPNVTRGYLNnPEANAEAAF--KDG--WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHP 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 513 AVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKI 580
Cdd:cd05926 420 AVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR----KHLAafkVPKKVYFVDELPKTATGKI 486
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
58-580 |
2.29e-77 |
|
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: 254.83 E-value: 2.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVC-AINPLLEGPAIASLLKAANAKVLVTLA 136
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFsAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 137 pfpgsDIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramqrreckrlhgragvrGAVPRHVAIHDFDSAMSRESG 216
Cdd:cd05911 91 -----DGLEKVKEAAKELGPKDKIIVLD-------------------------------DKPDGVLSIEDLLSPTLGEED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 217 DSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFsR 296
Cdd:cd05911 135 EDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-N 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 297 GAHVVLgTPQGYrgdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQ-DRT 374
Cdd:cd05911 214 GATVII-MPKFD-----SELFLDLIEKYKITFLYLVPPIAAALAKSPlLDKYDLSSLRVILSGGAPLSKELQELLAkRFP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 GVRILEGYGLTEGACVSSVNPpGGERRLGSIGLRIPGQMMKavILDDAGRyvRDCVENEVGVLTISGPNVFAGYLQ-EDQ 453
Cdd:cd05911 288 NATIKQGYGMTETGGILTVNP-DGDDKPGSVGRLLPNVEAK--IVDDDGK--DSLGPNEPGEICVRGPQVMKGYYNnPEA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 454 NKSLWLDlgDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVA 533
Cdd:cd05911 363 TKETFDE--DG--WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRA 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1142773712 534 YVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05911 439 YVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVDEIPKSASGKI 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-586 |
6.40e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 253.77 E-value: 6.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 1 MNAIATEAdVLRIENQGPPADLP---ASTYEMIGRGAAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRL 77
Cdd:PRK05605 7 MSAFADKP-WLQSYAPWTPHDLDygdTTLVDLYDNAVARFGDRPALDFFGA--------TTTYAELGKQVRRAAAGLRAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 78 GIDRHAVVAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVtlapfpgsdIWSKIQPVLSEVP- 155
Cdd:PRK05605 78 GVRPGDRVAIVLPNCPQHIVAFYAVLRLGaVVVEHNPLYTAHELEHPFEDHGARVAI---------VWDKVAPTVERLRr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 156 --SLQSLVLIDLAERVQGWRRIAAR-----AMQRREckRLHGRAgvRGAVPrhvaihdFDSAMSRESGDSLLI--PRRFE 226
Cdd:PRK05605 149 ttPLETIVSVNMIAAMPLLQRLALRlpipaLRKARA--ALTGPA--PGTVP-------WETLVDAAIGGDGSDvsHPRPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDISSYFCTGGTTGLPKIAIRRHGNEVAN-----AWsvgqVVGAGMGPgKTVFCGLPLFHVNAVLATG-LVPFSRGAHV 300
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANaaqgkAW----VPGLGDGP-ERVLAALPMFHAYGLTLCLtLAVSIGGELV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 301 VLGTPQgyrgdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRIL 379
Cdd:PRK05605 293 LLPAPD-------IDLILDAMKKHPPTWLPGVPPLYEKIAEAAEeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 380 EGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYL-QEDQNKSLW 458
Cdd:PRK05605 366 EGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPD---GEEGELLVRGPQVFKGYWnRPEETAKSF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 459 LDlgdgrQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLK 538
Cdd:PRK05605 443 LD-----GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLE 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1142773712 539 AGATATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK05605 518 PGAALDPEGLRAYCREHL-TRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-495 |
1.42e-71 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 237.60 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 34 AAIDPSAPALSFflraDDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEtHFVIWGG--EAAGIVCAI 111
Cdd:pfam00501 5 AARTPDKTALEV----GEGR---RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPE-WVVAFLAclKAGAVYVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 112 NPLLEGPAIASLLKAANAKVLVTLAPFpgsdIWSKIQPVLSEVPSLQSLVLIDLAERVQGWRriaaramqrreckrLHGR 191
Cdd:pfam00501 77 NPRLPAEELAYILEDSGAKVLITDDAL----KLEELLEALGKLEVVKLVLVLDRDPVLKEEP--------------LPEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 192 AGVRGAVPRhvaihdfdsamsresgdsllIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQV--VGAGMG 269
Cdd:pfam00501 139 AKPADVPPP--------------------PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrpRGFGLG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 270 PGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgTPQGYRGDgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNI 349
Cdd:pfam00501 199 PDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVL-PPGFPALD--PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 350 -DSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGER--RLGSIGLRIPGQMMKavILDDA-GRY 425
Cdd:pfam00501 276 lSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrSLGSVGRPLPGTEVK--IVDDEtGEP 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 426 VRDcveNEVGVLTISGPNVFAGYL-QEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRG 495
Cdd:pfam00501 354 VPP---GEPGELCVRGPGVMKGYLnDPELTAEAFDEDG----WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-587 |
3.77e-64 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 221.47 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 38 PSAPALSFFlrADDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEthFVIWGGEAAGIVCAINPLLeg 117
Cdd:PRK13295 38 PDKTAVTAV--RLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWE--FTVLYLACSRIGAVLNPLM-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 118 P-----AIASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramqrreckrlhgrA 192
Cdd:PRK13295 112 PifrerELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELPALRHVVVVG---------------------------G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 193 GVRGAVPRHVAIHDFDSAmsrESGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGK 272
Cdd:PRK13295 165 DGADSFEALLITPAWEQE---PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG--LGADD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 273 TVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDS 351
Cdd:PRK13295 240 VILMASPMAHQTGFMYGLMMPVMLGATAVL------QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVkESGRPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 352 LEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLG-SIGLRIPGQMMKAVILDDAgryvrDCV 430
Cdd:PRK13295 314 LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERAStTDGCPLPGVEVRVVDADGA-----PLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 431 ENEVGVLTISGPNVFAGYLQEDQnksLWLDLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHR 510
Cdd:PRK13295 389 AGQIGRLQVRGCSNFGGYLKRPQ---LNGTDADG--WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 511 HPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK13295 464 HPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-585 |
1.76e-62 |
|
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: 215.95 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 18 PPADLPASTYEMIGRGAaiDPSAPALsffLRADDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHF 97
Cdd:cd05904 1 LPTDLPLDSVSFLFASA--HPSRPAL---IDAATGR---ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 98 VIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLAPfpgsdiwskiqpVLSEVPSLQSLVLidlaervqgwrria 176
Cdd:cd05904 73 AFLAVLSLGaVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE------------LAEKLASLALPVV-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 177 aramqrreckrLHGRAGVRGAvprhvaihDFDSAMSRESGDSLLIPRrFEADDISSYFCTGGTTGLPKIAIRRHGNEVAN 256
Cdd:cd05904 127 -----------LLDSAEFDSL--------SFSDLLFEADEAEPPVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 257 AWSVGQVVGAGMGPGKTVFCGLPLFHVN--AVLATGLVpfSRGAHVVlgtpqgyrgdgVVKRF-----WEIVEHHRINFF 329
Cdd:cd05904 187 VAQFVAGEGSNSDSEDVFLCVLPMFHIYglSSFALGLL--RLGATVV-----------VMPRFdleelLAAIERYKVTHL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 330 SAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDR-TGVRILEGYGLTEGACVSSVNPPGGE--RRLGSI 405
Cdd:cd05904 254 PVVPPIVLALVKSPiVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTGVVAMCFAPEKdrAKYGSV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 406 GLRIPGqmMKAVILD-DAGRyvrDCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWL 484
Cdd:cd05904 334 GRLVPN--VEAKIVDpETGE---SLPPNQTGELWIRGPSIMKGYLNNPEATAATID-KEG--WLHTGDLCYIDEDGYLFI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 485 TGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETEldtfIRGMIGERAAIPK 564
Cdd:cd05904 406 VDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDE----IMDFVAKQVAPYK 481
|
570 580
....*....|....*....|....
gi 1142773712 565 RIH---IVDAMPLTAVGKIFKPEL 585
Cdd:cd05904 482 KVRkvaFVDAIPKSPSGKILRKEL 505
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
236-586 |
1.33e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 205.97 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPqGYRGDGVVk 315
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGYFIGER--LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP-SFDPLAVL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 rfwEIVEHHRINFFSAVPTLYSALLDVPVDGR-NIDSLEYGLCGAAPMPVEVFRTFQDRTGVR-ILEGYGLTEGACVSSV 393
Cdd:cd05917 86 ---EAIEKEKCTALHGVPTMFIAELEHPDFDKfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 394 NPPGG--ERRLGSIGLRIPGQMMKavILDDAGRYVrdCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTG 471
Cdd:cd05917 163 TRTDDsiEKRVNTVGRIMPHTEAK--IVDPEGGIV--PPVGVPGELCIRGYSVMKGYWNDPEKTAEAID-GDG--WLHTG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 472 DLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTF 551
Cdd:cd05917 236 DLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAY 315
|
330 340 350
....*....|....*....|....*....|....*
gi 1142773712 552 IRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05917 316 CKGKIA-HYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
59-585 |
1.80e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 211.82 E-value: 1.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGE-AAGIVCAINPLLEGPAIASLLKAANAKVLVTLap 137
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLlAGGIVVQTNPLYTERELEYQLHDSGAKVILCL-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 138 fpgSDIWSKIQPVLSEVpSLQSLVLIDLAERVQGWRRIAARAMQRReckrlhgRAGVRGAVPRHVAIHDFDSaMSRESGD 217
Cdd:PRK06710 129 ---DLVFPRVTNVQSAT-KIEHVIVTRIADFLPFPKNLLYPFVQKK-------QSNLVVKVSESETIHLWNS-VEKEVNT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 218 SLLIPRRFEaDDISSYFCTGGTTGLPKIAIRRHGNEVANA-----WSVGQVVGAgmgpgKTVFCGLPLFHVNAVLATGLV 292
Cdd:PRK06710 197 GVEVPCDPE-NDLALLQYTGGTTGFPKGVMLTHKNLVSNTlmgvqWLYNCKEGE-----EVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVLgTPQGYrgdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNIDSLEYGLCGAAPMPVEVFRTFQ 371
Cdd:PRK06710 271 SIMQGYKMVL-IPKFD-----MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDdAGRYVRdcvENEVGVLTISGPNVFAGYLQE 451
Cdd:PRK06710 345 TVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLE-TGEALP---PGEIGEIVVKGPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 452 DQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELP 531
Cdd:PRK06710 421 PEETAAVLQDG----WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 532 VAYVQLKAGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:PRK06710 497 KAFVVLKEGTECSEEELNQFARKYLAAY-KVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
38-580 |
2.33e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 210.97 E-value: 2.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 38 PSAPALSFFLRAddhrkplrWTYAALLRDITR-AANMFSRLGIDRHAVVAYVLPNLPE---THFVIWGGEAagIVCAINP 113
Cdd:PRK08314 24 PDKTAIVFYGRA--------ISYRELLEEAERlAGYLQQECGVRKGDRVLLYMQNSPQfviAYYAILRANA--VVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 114 LLEGPAIASLLKAANAKVLVTlapfpGSDIWSKIQPVLSEVPsLQSLVLIDLAERVQGWRRIAARAMQRRECKRlhgrag 193
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVGNLR-LRHVIVAQYSDYLPAEPEIAVPAWLRAEPPL------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 194 vrgAVPRHVAIHDFDSAMsresgDSLLIPRRFEA--DDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPG 271
Cdd:PRK08314 162 ---QALAPGGVVAWKEAL-----AAGLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 272 KTVFCGLPLFHVnavlaTGLV-----PFSRGAHVVLGTpqgyRGDGVVKRfwEIVEHHRINFFSAVPTLYSALLDVP-VD 345
Cdd:PRK08314 232 SVVLAVLPLFHV-----TGMVhsmnaPIYAGATVVLMP----RWDREAAA--RLIERYRVTHWTNIPTMVVDFLASPgLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 346 GRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERR--LGsiglrIPGQMMKAVILD-DA 422
Cdd:PRK08314 301 ERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLqcLG-----IPTFGVDARVIDpET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 423 GRYVRDcveNEVGVLTISGPNVFAGYLQ-EDQNKSLWLDLgDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDP 501
Cdd:PRK08314 376 LEELPP---GEVGEIVVHGPQVFKGYWNrPEATAEAFIEI-DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 502 ATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDtfIRGMIGERAA---IPKRIHIVDAMPLTAVG 578
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEE--IIAWAREHMAaykYPRIVEFVDSLPKSGSG 529
|
..
gi 1142773712 579 KI 580
Cdd:PRK08314 530 KI 531
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
59-580 |
2.04e-59 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 205.41 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPE---THFVIWggEAAGIVCAINPLLEGPAIASLLKAANAKVLVTL 135
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQyviAYFAIW--RANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 136 Apfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhgragvrgavprhvaihdfdsamsres 215
Cdd:cd05935 81 S------------------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 216 gdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFS 295
Cdd:cd05935 82 ----------ELDDLALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVY 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 296 RGAHVVLGTpqgyRGDGVVKRfwEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRT 374
Cdd:cd05935 150 VGGTYVLMA----RWDRETAL--ELIEKYKVTFWTNIPTMLVDLLATPeFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 GVRILEGYGLTEGACVSSVNPPGgerRLGSIGLRIPGQMMKAVILD-DAGRYVRDcveNEVGVLTISGPNVFAGYLQ-ED 452
Cdd:cd05935 224 GLRFVEGYGLTETMSQTHTNPPL---RPKLQCLGIP*FGVDARVIDiETGRELPP---NEVGEIVVRGPQIFKGYWNrPE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 453 QNKSLWLDLgDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPV 532
Cdd:cd05935 298 ETEESFIEI-KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVK 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1142773712 533 AYVQLKAG--ATATETELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKI 580
Cdd:cd05935 377 AFIVLRPEyrGKVTEEDIIEWAREQMAAYKY-PREVEFVDELPRSASGKI 425
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
28-586 |
3.92e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 208.09 E-value: 3.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 28 EMIGRGAAIDPSAPALSFflraddHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPE---THFVIwgGEA 104
Cdd:PRK12583 22 DAFDATVARFPDREALVV------RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEwllTQFAT--ARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 105 AGIVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSEVPSLQSLVLIdlAERVQGWRRIAARAMQrre 184
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALA--CERLPELRGVVSLAPA--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 185 ckrlhgragvrgAVPRHVAIHDFDSAMSRESGDSLL-IPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQV 263
Cdd:PRK12583 169 ------------PPPGFLAWHELQARGETVSREALAeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 264 VGagMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtPQGYRGDGVVKRfweIVEHHRINFFSAVPTLYSALLDVP 343
Cdd:PRK12583 237 LG--LTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY--PNEAFDPLATLQ---AVEEERCTALYGVPTMFIAELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 344 VDGR-NIDSLEYGLCGAAPMPVEVFRTFQDRTGV-RILEGYGLTEGACVSSVNPPGG--ERRLGSIGLRIPGQMMKavIL 419
Cdd:PRK12583 310 QRGNfDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlERRVETVGRTQPHLEVK--VV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 420 DDAGRYVrdcVENEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNI 499
Cdd:PRK12583 388 DPDGATV---PRGEIGELCTRGYSVMKGYWNNPEATAESID-EDG--WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 500 DPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGK 579
Cdd:PRK12583 462 YPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAH-FKVPRYFRFVDEFPMTVTGK 540
|
....*..
gi 1142773712 580 IFKPELK 586
Cdd:PRK12583 541 VQKFRMR 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
236-587 |
4.74e-59 |
|
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: 204.83 E-value: 4.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVAN------AWsvgqvvgaGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtpqgyR 309
Cdd:cd05941 97 TSGTTGRPKGVVLTHANLAANvralvdAW--------RWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEF------L 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 310 GDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVP--VDGRNIDSLEYGL-------CGAAPMPVEVFRTFQDRTGVRILE 380
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYeaHFTDPQFARAAAAerlrlmvSGSAALPVPTLEEWEAITGHTLLE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 381 GYGLTEGACVSSvNPPGGERRLGSIGLRIPGQMMKavILDDAGRYVRDcvENEVGVLTISGPNVFAGYLQEDQNKSLWLD 460
Cdd:cd05941 243 RYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQAR--IVDEETGEPLP--RGEVGEIQVRGPSVFKEYWNKPEATKEEFT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 lGDGrqWLNTGDLARRDAQGYFWLTGRRKELII-RGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKA 539
Cdd:cd05941 318 -DDG--WFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1142773712 540 GATA-TETELDTFIRgMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05941 395 GAAAlSLEELKEWAK-QRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-580 |
6.12e-59 |
|
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: 206.45 E-value: 6.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 50 DDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-CAINPLLEGPAIASLLKAAN 128
Cdd:cd05959 25 DDAG---SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVpVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 129 AKVLVTlapfpGSDIWSKIQPVLSEV-PSLQSLVlidlaerVQGWRRIAARAMQRREckrlhgragvrgaVPRHvaihdf 207
Cdd:cd05959 102 ARVVVV-----SGELAPVLAAALTKSeHTLVVLI-------VSGGAGPEAGALLLAE-------------LVAA------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 208 dsamsrESGDslLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGaGMGPGKTVFCGLPLFHvnavl 287
Cdd:cd05959 151 ------EAEQ--LKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVL-GIREDDVCFSAAKLFF----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 288 ATGL-----VPFSRGAHVVLgtpqgYRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDG-RNIDSLEYGLCGAAP 361
Cdd:cd05959 217 AYGLgnsltFPLSVGATTVL-----MPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPsRDLSSLRLCVSAGEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 362 MPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGgERRLGSIGLRIPGQMMKAVilDDAGRYVRDcveNEVGVLTISG 441
Cdd:cd05959 292 LPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPG-RVRYGTTGKPVPGYEVELR--DEDGGDVAD---GEPGELYVRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 442 PNVFAGYL-QEDQNKSLWLDlgdgrQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAI 520
Cdd:cd05959 366 PSSATMYWnNRDKTRDTFQG-----EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVV 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 521 GRPDVHAGELPVAYVQLKAGATATE---TELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05959 441 GVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPY-KYPRWIVFVDELPKTATGKI 502
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
58-586 |
1.10e-58 |
|
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: 203.34 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTla 136
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGaVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 137 pfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhgragvrgavprhvaihdfdsamsresg 216
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 217 dslliprrfEADDISSYFCTGGTTGLPKIAIRRHgnevanAWSVGQVVGA----GMGPGKTVFCGLPLFHVNAVLATGLV 292
Cdd:cd05972 79 ---------DAEDPALIYFTSGTTGLPKGVLHTH------SYPLGHIPTAaywlGLRPDDIHWNIADPGWAKGAWSSFFG 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVLgtpqgYRGDGVV-KRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQ 371
Cdd:cd05972 144 PWLLGATVFV-----YEGPRFDaERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTE-GACVSsvNPPGGERRLGSIGLRIPGqmMKAVILDDAGRyvrDCVENEVGVLTI--SGPNVFAGY 448
Cdd:cd05972 219 AATGLPIRDGYGQTEtGLTVG--NFPDMPVKPGSMGRPTPG--YDVAIIDDDGR---ELPPGEEGDIAIklPPPGLFLGY 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 449 LQ-EDQNKSLWLDlgdgrQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHA 527
Cdd:cd05972 292 VGdPEKTEASIRG-----DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVR 366
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773712 528 GELPVAYVQLKAGATATET---ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05972 367 GEVVKAFVVLTSGYEPSEElaeELQGHVKKVLA-PYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-586 |
4.15e-57 |
|
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: 199.05 E-value: 4.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-CAINPLLEGPAIASLLKAANAKVLVTl 135
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVlVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 136 apfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhgragvrgavprhvaihdfdsamsres 215
Cdd:cd05934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 216 gdslliprrfeadDISSYFCTGGTTGLPKIAIRRHGNevANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFS 295
Cdd:cd05934 82 -------------DPASILYTSGTTGPPKGVVITHAN--LTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALS 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 296 RGAHVVLGTPQGYRgdgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLeYGLCGAAPMPVEVFRTFQDRTG 375
Cdd:cd05934 147 VGATLVLLPRFSAS------RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHR-LRAAYGAPNPPELHEEFEERFG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 376 VRILEGYGLTEGaCVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDCVENEVGVLTISGPNVFAGYL-QEDQN 454
Cdd:cd05934 220 VRLLEGYGMTET-IVGVIGPRDEPRRPGSIGRPAPG--YEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYnMPEAT 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 455 KSLWLDLgdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAY 534
Cdd:cd05934 297 AEAMRNG-----WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAV 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1142773712 535 VQLKAGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05934 372 VVLRPGETLDPEELFAFCEGQLAYF-KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
23-596 |
1.01e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 200.60 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 23 PASTYEMIGRGAAIDPSAPALSFflraDDhrkpLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGG 102
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPALVL----GD----TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 103 EAAGI-VCAINPLlegpaiASL------LKAANAKVL-VTLAPFPGsdiwsKIQPVLSEVPSLQSLVLIDlaeRVQGWRR 174
Cdd:PRK06188 83 QLAGLrRTALHPL------GSLddhayvLEDAGISTLiVDPAPFVE-----RALALLARVPSLKHVLTLG---PVPDGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 175 IAARAMQrreckrlhgrAGVRGAVPRHVAihdfdsamsresgdslliprrfeaDDISSYFCTGGTTGLPKIAIRRHGNEV 254
Cdd:PRK06188 149 LLAAAAK----------FGPAPLVAAALP------------------------PDIAGLAYTGGTTGKPKGVMGTHRSIA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 255 ANAwsVGQVVGAGMGPGKTVFCGLPLFHVNAVLatgLVP-FSRGAHVVLgtPQGYRGDgvvkRFWEIVEHHRINFFSAVP 333
Cdd:PRK06188 195 TMA--QIQLAEWEWPADPRFLMCTPLSHAGGAF---FLPtLLRGGTVIV--LAKFDPA----EVLRAIEEQRITATFLVP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 334 TLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSV-----NPPGGERRLGSIGL 407
Cdd:PRK06188 264 TMIYALLDHPdLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYlrkrdHDPDDPKRLTSCGR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 408 RIPGqmMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYL-QEDQNKSLwldLGDGrqWLNTGDLARRDAQGYFWLTG 486
Cdd:PRK06188 344 PTPG--LRVALLDEDGREVA---QGEVGEICVRGPLVMDGYWnRPEETAEA---FRDG--WLHTGDVAREDEDGFYYIVD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 487 RRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGERAAiPKRI 566
Cdd:PRK06188 414 RKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHA-PKQV 492
|
570 580 590
....*....|....*....|....*....|..
gi 1142773712 567 HIVDAMPLTAVGKIFKPELKR--WETFDALVS 596
Cdd:PRK06188 493 DFVDSLPLTALGKPDKKALRAryWEGRGRAVG 524
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
57-585 |
1.08e-54 |
|
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: 194.77 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGI---DRHAVVAYvlpNLPEtHFVIW-GGEAAGIVC-AINPLLEGPAIASLLKAANAKV 131
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVkpgDRVATLAW---NTHR-HLELYyAVPGMGAVLhTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 132 LV---TLAPfpgsdiwsKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramqrreckrlhgrAGVRGAVPRHVAIHDFD 208
Cdd:cd12119 101 VFvdrDFLP--------LLEAIAPRLPTVEHVVVMT---------------------------DDAAMPEPAGVGVLAYE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 209 SAMSRESGDSLLipRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAvla 288
Cdd:cd12119 146 ELLAAESPEYDW--PDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNA--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 289 TGLvPFsrgAHVVLGTPQGYRG---DGvvKRFWEIVEHHRINFFSAVPTLYSALLD-VPVDGRNIDSLEYGLCGAAPMPV 364
Cdd:cd12119 221 WGL-PY---AAAMVGAKLVLPGpylDP--ASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAVPR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 365 EVFRTFQDRtGVRILEGYGLTEGACVSSVN-PPGGERRLG---------SIGLRIPGQMMKavILDDAGRYV-RDcvENE 433
Cdd:cd12119 295 SLIEAFEER-GVRVIHAWGMTETSPLGTVArPPSEHSNLSedeqlalraKQGRPVPGVELR--IVDDDGRELpWD--GKA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 434 VGVLTISGPNVFAGYLQEDQNKSLWLDlgDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPA 513
Cdd:cd12119 370 VGELQVRGPWVTKSYYKNDEESEALTE--DG--WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773712 514 VQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:cd12119 446 VAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVA-KWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-588 |
8.59e-54 |
|
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: 192.67 E-value: 8.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSfflraDDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:COG1021 28 GDLLRRRAERHPDRIAVV-----DGER---RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 IVcainPLLEGPA-----IASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSEVPSLQSLVLIDLAERVQGWRRIAARAMQ 181
Cdd:COG1021 100 AI----PVFALPAhrraeISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGDAGEFTSLDALLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 182 RREckrlhgragvRGAVPRHVAIhdfdsamsresgdsLLIprrfeaddissyfcTGGTTGLPKIAIRRHGNEVANAWSVG 261
Cdd:COG1021 176 LSE----------PRPDPDDVAF--------------FQL--------------SGGTTGLPKLIPRTHDDYLYSVRASA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 262 QVvgAGMGPGKTVFCGLPLFHvNAVLATG--LVPFSRGAHVVLGTpqgyrgDGVVKRFWEIVEHHRINFFSAVPTLYSAL 339
Cdd:COG1021 218 EI--CGLDADTVYLAALPAAH-NFPLSSPgvLGVLYAGGTVVLAP------DPSPDTAFPLIERERVTVTALVPPLALLW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 340 LD-VPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGacvsSVN------PPggERRLGSIGLRI-PG 411
Cdd:COG1021 289 LDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG----LVNytrlddPE--EVILTTQGRPIsPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 412 QMMKavILDDAGRYVRDCvenEVGVLTISGPNVFAGYLQ-EDQNKSLWLDlgDGrqWLNTGDLARRDAQGYFWLTGRRKE 490
Cdd:COG1021 363 DEVR--IVDEDGNPVPPG---EVGELLTRGPYTIRGYYRaPEHNARAFTP--DG--FYRTGDLVRRTPDGYLVVEGRAKD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 491 LIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKaGATATETELDTFIRgmigER--AA--IPKRI 566
Cdd:COG1021 434 QINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLR----ERglAAfkLPDRL 508
|
570 580
....*....|....*....|..
gi 1142773712 567 HIVDAMPLTAVGKIFKPELKRW 588
Cdd:COG1021 509 EFVDALPLTAVGKIDKKALRAA 530
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-586 |
1.92e-53 |
|
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: 189.51 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCA-INPLLEGPAIASLLKAANAKVLVtl 135
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNpILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 136 apfpgsdiwskiqpvlseVPSLqslvlidlaervqgWRRIaaramqrreckrlhgragvrgavpRHVAihdfdsamsres 215
Cdd:cd05903 79 ------------------VPER--------------FRQF------------------------DPAA------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 216 gdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFs 295
Cdd:cd05903 91 ----------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASI--RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPL- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 296 rgahvVLGTPQgyrgdgVVKRFW------EIVEHHRINFFSAVPTLYSALLDVPVD-GRNIDSLEYGLCGAAPMPVEVFR 368
Cdd:cd05903 158 -----LLGAPV------VLQDIWdpdkalALMREHGVTFMMGATPFLTDLLNAVEEaGEPLSRLRTFVCGGATVPRSLAR 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 369 TFQDRTGVRILEGYGLTE-GACVSSVNPPGGERRLGSIGLRIPGQMMKavILDDAGRYVrdcVENEVGVLTISGPNVFAG 447
Cdd:cd05903 227 RAAELLGAKVCSAYGSTEcPGAVTSITPAPEDRRLYTDGRPLPGVEIK--VVDDTGATL---APGVEGELLSRGPSVFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 448 YLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHA 527
Cdd:cd05903 302 YLDRPDLTADAAPEG----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERL 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773712 528 GELPVAYVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05903 378 GERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
28-586 |
2.37e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 191.30 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 28 EMIGRGAAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGI---DRHAVVAYvlpNlpETHFVI-WGGE 103
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGDR--------SWTYAELDAAVNRVAAALLDLGLkkgDRVAALGH---N--SDAYALlWLAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 104 A-AGIV-CAINPLLEGPAIASLLKAANAKVLVTlapfpGSDIWSKIQPVLSEVPSLQSLVL--IDLAERVQGWRriaara 179
Cdd:PRK08316 82 ArAGAVhVPVNFMLTGEELAYILDHSGARAFLV-----DPALAPTAEAALALLPVDTLILSlvLGGREAPGGWL------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 180 mqrreckrlhgragvrgavprhvaihDFDSAMSRESGDSLLIPRRfeADDISSYFCTGGTTGLPKIAIRRHGNEVANawS 259
Cdd:PRK08316 151 --------------------------DFADWAEAGSVAEPDVELA--DDDLAQILYTSGTESLPKGAMLTHRALIAE--Y 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 260 VGQVVGAGMGPGKTVFCGLPLFHvnavlatglvpfSRGAHVVLGtPQGYRGDGVV-------KRFWEIVEHHRINFFSAV 332
Cdd:PRK08316 201 VSCIVAGDMSADDIPLHALPLYH------------CAQLDVFLG-PYLYVGATNVildapdpELILRTIEAERITSFFAP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 333 PTLYSALLDVPV-DGRNIDSLEYGLCGAAPMPVEVFRTFQDR-TGVRILEGYGLTEGACVSSV-NPPGGERRLGSIGLri 409
Cdd:PRK08316 268 PTVWISLLRHPDfDTRDLSSLRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQTEIAPLATVlGPEEHLRRPGSAGR-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 410 PGQMMKAVILDDAGRyvrDCVENEVGVLTISGPNVFAGYL-QEDQNKSLWLDlgdgrQWLNTGDLARRDAQGYFWLTGRR 488
Cdd:PRK08316 346 PVLNVETRVVDDDGN---DVAPGEVGEIVHRSPQLMLGYWdDPEKTAEAFRG-----GWFHSGDLGVMDEEGYITVVDRK 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 489 KELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmigERAA---IPKR 565
Cdd:PRK08316 418 KDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCR----ARLAgfkVPKR 493
|
570 580
....*....|....*....|.
gi 1142773712 566 IHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08316 494 VIFVDELPRNPSGKILKRELR 514
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
85-586 |
5.53e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 191.19 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 85 VAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLAPFPgsdiwSKIQPVL--SEVPSLQSLV 161
Cdd:PRK12492 78 IAVQMPNVLQYPIAVFGALRAGlIVVNTNPLYTAREMRHQFKDSGARALVYLNMFG-----KLVQEVLpdTGIEYLIEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 162 LIDLAERVQGWRRIAARAMQRRECKRLHgragvrgaVPRHVAihdFDSAMsRESGDSLLIPRRFEADDISSYFCTGGTTG 241
Cdd:PRK12492 153 MGDLLPAAKGWLVNTVVDKVKKMVPAYH--------LPQAVP---FKQAL-RQGRGLSLKPVPVGLDDIAVLQYTGGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 242 LPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVF--------CGLPLFHVNAVLATGLVPFSRGAHVVLGT-PQGYRGdg 312
Cdd:PRK12492 221 LAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMkegqevmiAPLPLYHIYAFTANCMCMMVSGNHNVLITnPRDIPG-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 313 vvkrFWEIVEHHRINFFSAVPTLYSALLDVPvDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACV 390
Cdd:PRK12492 299 ----FIKELGKWRFSALLGLNTLFVALMDHP-GFKDLDfsALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 391 SSVNPPGGERRLGSIGLRIPGQMMKavILDDAGryvrdcVE---NEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqW 467
Cdd:PRK12492 374 ASTNPYGELARLGTVGIPVPGTALK--VIDDDG------NElplGERGELCIKGPQVMKGYWQQPEATAEALD-AEG--W 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 468 LNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATEtE 547
Cdd:PRK12492 443 FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE-E 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1142773712 548 LDTFIR-GMIGERaaIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK12492 522 LKAYCKeNFTGYK--VPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
171-587 |
9.95e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 188.92 E-value: 9.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 171 GWRRIAARAMQRRECKRLHGRAGVRgavpRHVAIHDFDSAMSRESGDslLIPRRFEADDISSYfcTGGTTGLPKIAIRRH 250
Cdd:PRK06839 100 GTTVLFVEKTFQNMALSMQKVSYVQ----RVISITSLKEIEDRKIDN--FVEKNESASFIICY--TSGTTGKPKGAVLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 251 GNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtPQGYRGDGVVKrfweIVEHHRINFFS 330
Cdd:PRK06839 172 ENMFWNA--LNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV--PRKFEPTKALS----MIEKHKVTVVM 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 331 AVPTLYSALLDVPV-DGRNIDSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGYGLTEGA-CVSSVNPPGGERRLGSIGLr 408
Cdd:PRK06839 244 GVPTIHQALINCSKfETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSpTVFMLSEEDARRKVGSIGK- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 409 iPGQMMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRR 488
Cdd:PRK06839 322 -PVLFCDYELIDENKNKVE---VGEVGELLIRGPNVMKEYWNRPDATEETIQDG----WLCTGDLARVDEDGFVYIVGRK 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 489 KELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHI 568
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLA-KYKIPKEIVF 472
|
410
....*....|....*....
gi 1142773712 569 VDAMPLTAVGKIFKPELKR 587
Cdd:PRK06839 473 LKELPKNATGKIQKAQLVN 491
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
80-586 |
6.34e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 188.43 E-value: 6.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 80 DRHAVVayvLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLApfpgsDIWSKIQPVLSEVpSLQ 158
Cdd:PRK05677 76 DRIAVQ---LPNVLQYPVAVFGAMRAGlIVVNTNPLYTAREMEHQFNDSGAKALVCLA-----NMAHLAEKVLPKT-GVK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 159 SLVLIDLAERVQGWRRIAARAMQRReCKRLHGRAGVRGAVPrhvaihdFDSAMSRESGDSLLiPRRFEADDISSYFCTGG 238
Cdd:PRK05677 147 HVIVTEVADMLPPLKRLLINAVVKH-VKKMVPAYHLPQAVK-------FNDALAKGAGQPVT-EANPQADDVAVLQYTGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 239 TTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGK-TVFCGLPLFHVNAVLATGLVPFSRGAHVVLGT-PQGYrgDGVVK- 315
Cdd:PRK05677 218 TTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCeILIAPLPLYHIYAFTFHCMAMMLIGNHNILISnPRDL--PAMVKe 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 -RFWeivehhRINFFSAVPTLYSALLDVPvDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSS 392
Cdd:PRK05677 296 lGKW------KFSGFVGLNTLFVALCNNE-AFRKLDfsALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 393 VNPPGGeRRLGSIGLRIPGQMMKavILDDAGRyvrDCVENEVGVLTISGPNVFAGYLQ--EDQNKSLwldlgDGRQWLNT 470
Cdd:PRK05677 369 VNPSQA-IQVGTIGIPVPSTLCK--VIDDDGN---ELPLGEVGELCVKGPQVMKGYWQrpEATDEIL-----DSDGWLKT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 471 GDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDT 550
Cdd:PRK05677 438 GDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME 517
|
490 500 510
....*....|....*....|....*....|....*..
gi 1142773712 551 FIRG-MIGERaaIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK05677 518 HMRAnLTGYK--VPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
50-587 |
1.73e-50 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 184.18 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 50 DDHRKplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVcaINPLLEGPAIASLLKAAN- 128
Cdd:PRK06087 44 DNHGA--SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV--SVPLLPSWREAELVWVLNk 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 129 --AKVLVTLAPFPGSDIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramqrreckrlhgragvrGAVPRHVAIhd 206
Cdd:PRK06087 120 cqAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVD-------------------------------KLAPATSSL-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 207 fdsAMSR--ESGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVgqVVGAGMGPGKTVFCGLPLFHVN 284
Cdd:PRK06087 167 ---SLSQiiADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAY--CARLNLTWQDVFMMPAPLGHAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 285 AVLATGLVPFSRGAHVVLgtPQGYRGDGVVkrfwEIVEHHRINF-FSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMP 363
Cdd:PRK06087 242 GFLHGVTAPFLIGARSVL--LDIFTPDACL----ALLEQQRCTCmLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 364 VEVFRTFQDRtGVRILEGYGLTEgACVSSVNPPGG--ERRLGSIGLRIPGQMMKAVilDDAGRYVRDCVENEvgvlTIS- 440
Cdd:PRK06087 316 KKVARECQQR-GIKLLSVYGSTE-SSPHAVVNLDDplSRFMHTDGYAAAGVEIKVV--DEARKTLPPGCEGE----EASr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 441 GPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAI 520
Cdd:PRK06087 388 GPNVFMGYLDEPELTARALD-EEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 521 GRPDVHAGELPVAYVQLKAG-ATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPhHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
70-586 |
4.48e-50 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 183.15 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 70 AANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGI-VCAINPLLEGPAIASLLKAANAKVLVTLAPFPgsdiwSKIQ 148
Cdd:PRK08751 64 AAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLtVVNVNPLYTPRELKHQLIDSGASVLVVIDNFG-----TTVQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 149 PVLSEVPsLQSLVLIDLAERVqGWRRIAARAMQRRECKRLHGRAGVRGAVprhvaihDFDSAMSRESGDSLlIPRRFEAD 228
Cdd:PRK08751 139 QVIADTP-VKQVITTGLGDML-GFPKAALVNFVVKYVKKLVPEYRINGAI-------RFREALALGRKHSM-PTLQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 229 DISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQ-VVGAG-MGPGK-TVFCGLPLFHVNAVLATGLVpFSR--GAHVVLG 303
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwLAGTGkLEEGCeVVITALPLYHIFALTANGLV-FMKigGCNHLIS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 304 TPQGYRGdgvvkrFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGY 382
Cdd:PRK08751 288 NPRDMPG------FVKELKKTRFTAFTGVNTLFNGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVrdcVENEVGVLTISGPNVFAGYLQEDQNKSLWLDlG 462
Cdd:PRK08751 362 GLTETSPAACINPLTLKEYNGSIGLPIPS--TDACIKDDAGTVL---AIGEIGELCIKGPQVMKGYWKRPEETAKVMD-A 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 463 DGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELpVAYVQLKAGAT 542
Cdd:PRK08751 436 DG--WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKKDPA 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1142773712 543 ATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08751 513 LTAEDVKAHARANL-TGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
223-589 |
6.65e-50 |
|
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: 180.01 E-value: 6.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 223 RRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVL 302
Cdd:cd05969 84 ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD--LHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 303 gtpqgYRGDGVVKRFWEIVEHHRINFFSAVPTLYSALL---DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRIL 379
Cdd:cd05969 162 -----YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMkegDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 380 EGYGLTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDcveNEVGVLTISG--PNVFAGYLQEDQNKSL 457
Cdd:cd05969 237 DTWWQTETGSIMIANYPCMPIKPGSMGKPLPG--VKAAVVDENGNELPP---GTKGILALKPgwPSMFRGIWNDEERYKN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 458 WLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQL 537
Cdd:cd05969 312 SFIDG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISL 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 538 KAGATATE---TELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKIFKPELKRWE 589
Cdd:cd05969 388 KEGFEPSDelkEEIINFVRQKLGAHVA-PREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
228-587 |
8.68e-50 |
|
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: 178.69 E-value: 8.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVnavlaTGLVPFSRGahVVLGTPQG 307
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSA--IGSALNLGLTEDDNWLCALPLFHI-----SGLSILMRS--VIYGMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 308 yrgdgVVKRF-----WEIVEHHRINFFSAVPTLYSALLDVPVDGRNiDSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGY 382
Cdd:cd05912 148 -----LVDKFdaeqvLHLINSGKVTIISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEGAC-VSSVNPPGGERRLGSIGLRIPGQMMKavILDDAGRyvrdcvENEVGVLTISGPNVFAGYL-QEDQNKSLWLD 460
Cdd:cd05912 221 GMTETCSqIVTLSPEDALNKIGSAGKPLFPVELK--IEDDGQP------PYEVGEILLKGPNVTKGYLnRPDATEESFEN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 lgdgrQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqlKAG 540
Cdd:cd05912 293 -----GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV--VSE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1142773712 541 ATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05912 366 RPISEEELIAYCS----EKLAkykVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-586 |
4.73e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 180.01 E-value: 4.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALSFFlraddHRKpLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEthfviW------GGEAA 105
Cdd:PRK08315 24 RTAARYPDREALVYR-----DQG-LRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPE-----WvltqfaTAKIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 106 GIVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGSDIWSKIQPVLSE-------------VPSLQSLVLIDlAERVQG- 171
Cdd:PRK08315 93 AILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPElatcepgqlqsarLPELRRVIFLG-DEKHPGm 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 172 --WRRIAARAmqrreckrlhgragvrgavpRHVAIHDFDSAMSRESGDslliprrfeaDDISSYFcTGGTTGLPKIAIRR 249
Cdd:PRK08315 172 lnFDELLALG--------------------RAVDDAELAARQATLDPD----------DPINIQY-TSGTTGFPKGATLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 250 HGNEVANAWSVGQVVGagMGPGKTVFCGLPLFH----VNAVLATglvpFSRGAHVVlgtpqgYRGDGvvkrF-----WEI 320
Cdd:PRK08315 221 HRNILNNGYFIGEAMK--LTEEDRLCIPVPLYHcfgmVLGNLAC----VTHGATMV------YPGEG----FdplatLAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 321 VEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVR-ILEGYGLTE---GACVSSVNP 395
Cdd:PRK08315 285 VEEERCTALYGVPTMFIAELDHPdFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSeVTIAYGMTEtspVSTQTRTDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 396 PGgERRLGSIGLRIPGQMMKavILD-DAGRYVRdcvENEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLA 474
Cdd:PRK08315 365 PL-EKRVTTVGRALPHLEVK--IVDpETGETVP---RGEQGELCTRGYSVMKGYWNDPEKTAEAID-ADG--WMHTGDLA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 475 RRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRG 554
Cdd:PRK08315 436 VMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRG 515
|
570 580 590
....*....|....*....|....*....|..
gi 1142773712 555 MIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08315 516 KIA-HYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
177-586 |
7.36e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 179.08 E-value: 7.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 177 ARAMQRRECKRLHGRAgVRGAVP--RHV-------AIHDFDSAMSRESGDSLLiPRRFEADDISSYFCTGGTTGLPKIAI 247
Cdd:PRK07470 105 ARAMICHADFPEHAAA-VRAASPdlTHVvaiggarAGLDYEALVARHLGARVA-NAAVDHDDPCWFFFTSGTTGRPKAAV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 248 RRHGnevanawSVGQVVG---AGMGPGKTVF-CGL---PLFHVNAVLAtgLVPFSRGAHVVLgtPQGYRGDgvVKRFWEI 320
Cdd:PRK07470 183 LTHG-------QMAFVITnhlADLMPGTTEQdASLvvaPLSHGAGIHQ--LCQVARGAATVL--LPSERFD--PAEVWAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 321 VEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMpvevFRTFQDRT----GVRILEGYGLTEGACVSSVNP 395
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVEHPaVDRYDHSSLRYVIYAGAPM----YRADQKRAlaklGKVLVQYFGLGEVTGNITVLP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 396 P-------GGERRLGSIGLRIPGqmMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYL--QEDQNKSLwldlGDGrq 466
Cdd:PRK07470 326 PalhdaedGPDARIGTCGFERTG--MEVQIQDDEGRELP---PGETGEICVIGPAVFAGYYnnPEANAKAF----RDG-- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:PRK07470 395 WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA 474
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1142773712 547 ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK07470 475 ELLAWLDGKVA-RYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
221-594 |
6.97e-48 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 175.83 E-value: 6.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 221 IPRrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANA------WsvgqvvgaGMGPGKTVFCGLPLFHVNAV-LATGLVP 293
Cdd:PRK07514 151 VPR--GADDLAAILYTSGTTGRSKGAMLSHGNLLSNAltlvdyW--------RFTPDDVLIHALPIFHTHGLfVATNVAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 294 FSRGAHVVLgtpQGYRGDGVVKRFweivehHRINFFSAVPTLYSALLDVPVDGRNIDS-LEYGLCGAAPMPVEVFRTFQD 372
Cdd:PRK07514 221 LAGASMIFL---PKFDPDAVLALM------PRATVMMGVPTFYTRLLQEPRLTREAAAhMRLFISGSAPLLAETHREFQE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 373 RTGVRILEGYGLTEGACVSSvNPPGGERRLGSIGLRIPGQMMKAVILDDAgryvRDCVENEVGVLTISGPNVFAGYLQ-- 450
Cdd:PRK07514 292 RTGHAILERYGMTETNMNTS-NPYDGERRAGTVGFPLPGVSLRVTDPETG----AELPPGEIGMIEVKGPNVFKGYWRmp 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 451 EDQNKSLwldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGEL 530
Cdd:PRK07514 367 EKTAEEF---RADG--FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEG 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 531 PVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKrwETFDAL 594
Cdd:PRK07514 442 VTAVVVPKPGAALDEAAILAALKGRLA-RFKQPKRVFFVDELPRNTMGKVQKNLLR--EQYADL 502
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
19-585 |
1.23e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 176.38 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 19 PADLPASTYEMIGRGAAID---------PSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVL 89
Cdd:PRK06178 19 PAGIPREPEYPHGERPLTEylrawarerPQRPAIIFYGH--------VITYAELDELSDRFAALLRQRGVGAGDRVAVFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 90 PNLPETHFVIWGGEAAGIVCA-INPLLEGPAIASLLKAANAKVLVTLAPFpgsdiWSKIQPVLSEVpSLQSLVLIDLAER 168
Cdd:PRK06178 91 PNCPQFHIVFFGILKLGAVHVpVSPLFREHELSYELNDAGAEVLLALDQL-----APVVEQVRAET-SLRHVIVTSLADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 169 VQGWRRIAARAMqrreckrlhgragVRGAVPRHVAIHDFDSAMSRESGDSLLIPRrfEADDISSYFCTGGTTGLPKIAIR 248
Cdd:PRK06178 165 LPAEPTLPLPDS-------------LRAPRLAAAGAIDLLPALRACTAPVPLPPP--ALDALAALNYTGGTTGMPKGCEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 249 RHGNEV---ANAWSVGQVVGAGmgpgkTVFCG-LPLFHVNAVLATGLVPFSRGAHVVLGTpqgyRGDGVVkrFWEIVEHH 324
Cdd:PRK06178 230 TQRDMVytaAAAYAVAVVGGED-----SVFLSfLPEFWIAGENFGLLFPLFSGATLVLLA----RWDAVA--FMAAVERY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 325 RINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGA--APMPVEVFRTFQDRTGVRILEG-YGLTEGACVSSVNP--PGG 398
Cdd:PRK06178 299 RVTRTVMLVDNAVELMDHPrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAgfQDD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 399 ERRLGS----IGLRIPGQMMKavILD-DAGRYVRDCVENEVGVLTisgPNVFAGYLQE-DQNKSLwldLGDGrqWLNTGD 472
Cdd:PRK06178 379 DFDLLSqpvfVGLPVPGTEFK--ICDfETGELLPLGAEGEIVVRT---PSLLKGYWNKpEATAEA---LRDG--WLHTGD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 473 LARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFI 552
Cdd:PRK06178 449 IGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWC 528
|
570 580 590
....*....|....*....|....*....|....*
gi 1142773712 553 RgmigERAAIPK--RIHIVDAMPLTAVGKIFKPEL 585
Cdd:PRK06178 529 R----ENMAVYKvpEIRIVDALPMTATGKVRKQDL 559
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
23-588 |
1.29e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 175.91 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 23 PASTYEMIGRGAAIDPSAPALSFflraddhrKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLP---ETHFvi 99
Cdd:PRK08162 17 PLTPLSFLERAAEVYPDRPAVIH--------GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPamvEAHF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 100 wGGEAAGIVC-AINPLLEGPAIASLLKAANAKVLVTLAPFpgSDIwskIQPVLSEVPSLQSLVLIDLAERVQGWRRIAAR 178
Cdd:PRK08162 87 -GVPMAGAVLnTLNTRLDAASIAFMLRHGEAKVLIVDTEF--AEV---AREALALLPGPKPLVIDVDDPEYPGGRFIGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 179 amqrreckrlhgragvrgavprhvaihDFDSAMSRESGDSLLIPRRFEADDIS-SYfcTGGTTGLPKIAIRRHGNEVANA 257
Cdd:PRK08162 161 ---------------------------DYEAFLASGDPDFAWTLPADEWDAIAlNY--TSGTTGNPKGVVYHHRGAYLNA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 258 wsVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQgyrgdgvVKRFWEIVEHHRINFFSAVPTLYS 337
Cdd:PRK08162 212 --LSNILAWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNVCLRKVD-------PKLIFDLIREHGVTHYCGAPIVLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 338 ALLDVPVDGR-NIDSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGYGLTEGACVSSVNP--------PGGER--RLGSIG 406
Cdd:PRK08162 283 ALINAPAEWRaGIDHPVHAMVAGAAPPAAVIAKMEEI-GFDLTHVYGLTETYGPATVCAwqpewdalPLDERaqLKARQG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 407 LRIPGQMMKAVILDDAGRYV-RDcvENEVGVLTISGPNVFAGYLQEDqnKSLWLDLGDGrqWLNTGDLARRDAQGYFWLT 485
Cdd:PRK08162 362 VRYPLQEGVTVLDPDTMQPVpAD--GETIGEIMFRGNIVMKGYLKNP--KATEEAFAGG--WFHTGDLAVLHPDGYIKIK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 486 GRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKR 565
Cdd:PRK08162 436 DRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLA-GFKVPKA 514
|
570 580
....*....|....*....|...
gi 1142773712 566 IhIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK08162 515 V-VFGELPKTSTGKIQKFVLREQ 536
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
225-590 |
1.38e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 174.38 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 225 FEADDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVnavlaTGLVPFSRGahVVLGT 304
Cdd:PRK03640 138 FDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSA--VGSALNLGLTEDDCWLAAVPIFHI-----SGLSILMRS--VIYGM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 305 PqgyrgdgVV-------KRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRtGVR 377
Cdd:PRK03640 209 R-------VVlvekfdaEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK-GIP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 378 ILEGYGLTEGAC-VSSVNPPGGERRLGSIGLriPGQMMKAVILDDAgryvRDCVENEVGVLTISGPNVFAGYL-QEDQNK 455
Cdd:PRK03640 281 VYQSYGMTETASqIVTLSPEDALTKLGSAGK--PLFPCELKIEKDG----VVVPPFEEGEIVVKGPNVTKGYLnREDATR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 456 SlwlDLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYV 535
Cdd:PRK03640 355 E---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 536 qlKAGATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIFKPELKRWET 590
Cdd:PRK03640 430 --VKSGEVTEEELRHFCE----EKLAkykVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
32-586 |
3.79e-47 |
|
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: 173.25 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALsfflraddHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLP---ETHFviwGGEAAGIV 108
Cdd:cd12118 12 RAAAVYPDRTSI--------VYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPamyELHF---GVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 109 -CAINPLLEGPAIASLLKAANAKVLVTLAPFpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckr 187
Cdd:cd12118 81 lNALNTRLDAEEIAFILRHSEAKVLFVDREF------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 188 lhgragvrgavprhvaihDFDSAMSRESGDSLLIPRRFEADDISSYFcTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAG 267
Cdd:cd12118 112 ------------------EYEDLLAEGDPDFEWIPPADEWDPIALNY-TSGTTGRPKGVVYHHRGAYLNA--LANILEWE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 268 MGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGyrgdgvvKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDG 346
Cdd:cd12118 171 MKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDA-------KAIYDLIEKHKVTHFCGAPTVLNMLANAPpSDA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 347 RNIDSLEYGLCGAAPMPVEVFRTFQdRTGVRILEGYGLTEGACVSSVNP--------PGGER-RLGS-IGLRIPGQMMKA 416
Cdd:cd12118 244 RPLPHRVHVMTAGAPPPAAVLAKME-ELGFDVTHVYGLTETYGPATVCAwkpewdelPTEERaRLKArQGVRYVGLEEVD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 417 VILDDAGRYV-RDCVEneVGVLTISGPNVFAGYLQ-EDQNKSLwldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIR 494
Cdd:cd12118 323 VLDPETMKPVpRDGKT--IGEIVFRGNIVMKGYLKnPEATAEA---FRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIIS 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 495 GGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmigERAA---IPKRIhIVDA 571
Cdd:cd12118 396 GGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCR----EHLAgfmVPKTV-VFGE 470
|
570
....*....|....*
gi 1142773712 572 MPLTAVGKIFKPELK 586
Cdd:cd12118 471 LPKTSTGKIQKFVLR 485
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
226-586 |
1.68e-46 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 172.93 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKT-VFCGLPLFHVNAVLATGLVPFSRGAHVVLGT 304
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKElVVTALPLYHIFALTVNCLLFIELGGQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 305 -PQGYrgDGVVKRfweiVEHHRINFFSAVPTLYSALLDVPvDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVRILEG 381
Cdd:PRK08974 284 nPRDI--PGFVKE----LKKYPFTAITGVNTLFNALLNNE-EFQELDfsSLKLSVGGGMAVQQAVAERWVKLTGQYLLEG 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMKavILDDAGRyvrDCVENEVGVLTISGPNVFAGYLQE-DQNKSLwld 460
Cdd:PRK08974 357 YGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIK--LVDDDGN---EVPPGEPGELWVKGPQVMLGYWQRpEATDEV--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 LGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqLKAG 540
Cdd:PRK08974 429 IKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKD 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1142773712 541 ATATETELDTFIRG-MIGERaaIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08974 506 PSLTEEELITHCRRhLTGYK--VPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
58-589 |
2.75e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 171.24 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-CAINPLLEGPAIASLLKAANAKVLVTLA 136
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYyTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 137 pfpgsdiwskiqpvlsevpslqslvliDLAERVQGWRRIAARAMQRReckrlhgrAGVRGAVPRHvaiHDFDSAMSRESG 216
Cdd:PRK08276 92 ---------------------------ALADTAAELAAELPAGVPLL--------LVVAGPVPGF---RSYEEALAAQPD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 217 DSllIPRRFEADDISsYfcTGGTTGLPKiAIRR-----HGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVnAVLAtgl 291
Cdd:PRK08276 134 TP--IADETAGADML-Y--SSGTTGRPK-GIKRplpglDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLR--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 292 vpFSRGAHVVLGTpqgyrgdgVV-------KRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRN---IDSLEYGLCGAAP 361
Cdd:PRK08276 204 --FGMSALALGGT--------VVvmekfdaEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRArydVSSLRVAIHAAAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 362 MPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMkavILDDAGRyvrDCVENEVGVLTISG 441
Cdd:PRK08276 274 CPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLGEVR---ILDEDGN---ELPPGEIGTVYFEM 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 442 PNVFAGYLQ-EDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAI 520
Cdd:PRK08276 348 DGYPFEYHNdPEKTAAARNPHG----WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVF 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 521 GRPDVHAGELPVAYVQLKAGATATE---TELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKR--WE 589
Cdd:PRK08276 424 GVPDEEMGERVKAVVQPADGADAGDalaAELIAWLRGRLA-HYKCPRSIDFEDELPRTPTGKLYKRRLRDryWE 496
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
17-586 |
3.02e-46 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 172.13 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 17 GPPADLPASTYemigrgaaidPSAPAL---SFFLRADdhRKPL-----RWTYAALLRDITRAANMFSRLGIDRHAVVAYV 88
Cdd:PRK07059 12 GVPAEIDASQY----------PSLADLleeSFRQYAD--RPAFicmgkAITYGELDELSRALAAWLQSRGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 89 LPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLAPFPgsdiwSKIQPVLSEVPSlqslvlidlae 167
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGyVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFA-----TTVQQVLAKTAV----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 168 rvqgwRRIAARAMqrrecKRLHGRAG------VRG--------AVPRHVAihdFDSAMSRESGDSLLiPRRFEADDISSY 233
Cdd:PRK07059 144 -----KHVVVASM-----GDLLGFKGhivnfvVRRvkkmvpawSLPGHVR---FNDALAEGARQTFK-PVKLGPDDVAFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 234 FCTGGTTGLPKIAIRRHGNEVAN-----AWsVGQVVGAGMGPGKTVF-CGLPLFHVNAVLATGLVPFSRGAHVVLgTPQG 307
Cdd:PRK07059 210 QYTGGTTGVSKGATLLHRNIVANvlqmeAW-LQPAFEKKPRPDQLNFvCALPLYHIFALTVCGLLGMRTGGRNIL-IPNP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 308 YRGDGVVKRFweivEHHRINFFSAVPTLYSALLDVPvDGRNIDSLEYGLCGAAPMPVE--VFRTFQDRTGVRILEGYGLT 385
Cdd:PRK07059 288 RDIPGFIKEL----KKYQVHIFPAVNTLYNALLNNP-DFDKLDFSKLIVANGGGMAVQrpVAERWLEMTGCPITEGYGLS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 386 EGACVSSVNPPGGERRLGSIGLRIPGQMMkaVILDDAGRyvrDCVENEVGVLTISGPNVFAGYLQ--EDQNKSLwldLGD 463
Cdd:PRK07059 363 ETSPVATCNPVDATEFSGTIGLPLPSTEV--SIRDDDGN---DLPLGEPGEICIRGPQVMAGYWNrpDETAKVM---TAD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 464 GrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqLKAGATA 543
Cdd:PRK07059 435 G--FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPAL 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1142773712 544 TETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK07059 512 TEEDVKAFCK----ERLTnykRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-586 |
1.17e-45 |
|
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: 168.39 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 223 RRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPlFHVNAVLATGLVPFSRGAHVVL 302
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG--ITADDRALTVLP-LSYDYGLSVLNTHLLRGATLVL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 303 gTPQGYRGDGvvkrFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDR-TGVRILEG 381
Cdd:cd05922 189 -TNDGVLDDA----FWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELlPGAQVYVM 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTEGACVSSVNPPGGE-RRLGSIGLRIPGQmmKAVILDDAGRyvrDCVENEVGVLTISGPNVFAGYLQEDQNKslwLD 460
Cdd:cd05922 264 YGQTEATRRMTYLPPERIlEKPGSIGLAIPGG--EFEILDDDGT---PTPPGEPGEIVHRGPNVMKGYWNDPPYR---RK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDvHAGELPVAYVQLKAg 540
Cdd:cd05922 336 EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPD- 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1142773712 541 atatETELDTFIRGM--IGERAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05922 414 ----KIDPKDVLRSLaeRLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
57-586 |
1.39e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 169.48 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFViWGGEA--AGIVCAINPLLEGPAIASLLKAANAKVLVT 134
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFC-WFGLAkiGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 135 LAPFPGsdIWSKIQPVLSEvpSLQSLVLIDLAErvqgwrriaaramqrreckrlhgragvrgavPRHVAIHDFDSAMSRE 214
Cdd:PRK08008 116 SAQFYP--MYRQIQQEDAT--PLRHICLTRVAL-------------------------------PADDGVSSFTQLKAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 215 SGdSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGN-EVANAWSVGQVvgaGMGPGKTVFCGLPLFHVNAVLATGLVP 293
Cdd:PRK08008 161 PA-TLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNlRFAGYYSAWQC---ALRDDDVYLTVMPAFHIDCQCTAAMAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 294 FSRGAHVVLGTPQGYRgdgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPV--DGRN--IDSLEYGLcgaaPMPVEVFRT 369
Cdd:PRK08008 237 FSAGATFVLLEKYSAR------AFWGQVCKYRATITECIPMMIRTLMVQPPsaNDRQhcLREVMFYL----NLSDQEKDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 370 FQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGlRiPGQMMKAVILDDAGRYVRDCVENEVGVLTISGPNVFAGYL 449
Cdd:PRK08008 307 FEERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIG-R-PGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 450 QEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGE 529
Cdd:PRK08008 385 LDPKATAKVLE-ADG--WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 530 LPVAYVQLKAGATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08008 462 AIKAFVVLNEGETLSEEEFFAFCE----QNMAkfkVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
236-588 |
6.60e-44 |
|
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: 160.19 E-value: 6.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVnavlaTGLVPFSR----GAHVVLGTPqgyRGD 311
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAGLHSRLG--FGGGDSWLLSLPLYHV-----GGLAILVRsllaGAELVLLER---NQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 312 GVVKRfweivEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGYGLTEGACVS 391
Cdd:cd17630 78 LAEDL-----APPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 392 SVNPPGGERRlGSIGLRIPGqmmkavilddagryVRDCVENEvGVLTISGPNVFAGYLqedqnKSLWLDLGDGRQWLNTG 471
Cdd:cd17630 152 ATKRPDGFGR-GGVGVLLPG--------------RELRIVED-GEIWVGGASLAMGYL-----RGQLVPEFNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 472 DLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqlKAGATATETELDTF 551
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADPAELRAW 288
|
330 340 350
....*....|....*....|....*....|....*..
gi 1142773712 552 IRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:cd17630 289 LKDKLA-RFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
15-523 |
1.02e-42 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 162.96 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 15 NQGPPADLPASTYEMIGRGAAIDPSAPALSFflRADDHRKPlrWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPE 94
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALRE--KEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 95 THFV---IWGgeAAGIVCAINPLLEGPAIASLLKAANAKVLVTLapfpGSDIWSKIQPVLSEVPSLQSLVLIDlaervqg 171
Cdd:COG1022 78 WVIAdlaILA--AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVE----DQEQLDKLLEVRDELPSLRHIVVLD------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 172 wrriaaramqrreckrlhgragvRGAVPRHVAIHDFDSAMsrESGDSLLIPRRFEA-------DDISSYFCTGGTTGLPK 244
Cdd:COG1022 145 -----------------------PRGLRDDPRLLSLDELL--ALGREVADPAELEArraavkpDDLATIIYTSGTTGRPK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 245 IAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHV------NAVLATGL-VPFSRGA------------HVVLGTP 305
Cdd:COG1022 200 GVMLTHRNLLSNARALLERLP--LGPGDRTLSFLPLAHVfertvsYYALAAGAtVAFAESPdtlaedlrevkpTFMLAVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 qgyrgdgvvkRFWEIVeHHRIN-------------FFSAVPT----------------------------LYSALLDVpV 344
Cdd:COG1022 278 ----------RVWEKV-YAGIQakaeeagglkrklFRWALAVgrryararlagkspslllrlkhaladklVFSKLREA-L 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 DGRnidsLEYGLCGAAPMPVEVFRTFQDrTGVRILEGYGLTEGACVSSVNPPGgERRLGSIGLRIPGqmMKAVILDDagr 424
Cdd:COG1022 346 GGR----LRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPG-DNRIGTVGPPLPG--VEVKIAED--- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 425 yvrdcvenevGVLTISGPNVFAGYLQ-EDQNKSLWLDlgDGrqWLNTGDLARRDAQGYFWLTGRRKELII-RGGHNIDPA 502
Cdd:COG1022 415 ----------GEILVRGPNVMKGYYKnPEATAEAFDA--DG--WLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQ 480
|
570 580
....*....|....*....|...
gi 1142773712 503 TIEEPLHRHPAVQIAAAIG--RP 523
Cdd:COG1022 481 PIENALKASPLIEQAVVVGdgRP 503
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
56-588 |
1.16e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 160.74 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 56 LRWTYAALLRDITRAANMFSRLGI---DRHAVVAYVLPNLPETHFVIwgGEAAGIVCAINPLLEGPAIASLLKAANAKVL 132
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCvdgERLAVLARNSVWLVALHFAC--ARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 133 VtlapfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhGRAGVRGAVPRHVAIHDF-DSAM 211
Cdd:PRK09088 99 L--------------------------------------------------------GDDAVAAGRTDVEDLAAFiASAD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 212 SRESGDSLLIPRrfeaDDISSYFCTGGTTGLPKIAI--RRHGNEVANAWSVGQVVGAgmgpgKTVF-CGLPLFHVnavla 288
Cdd:PRK09088 123 ALEPADTPSIPP----ERVSLILFTSGTSGQPKGVMlsERNLQQTAHNFGVLGRVDA-----HSSFlCDAPMFHI----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 289 TGLVPFSRGAHVVLGTPQ---GYRGDGVVKRFWEI---VEHhrinfFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAP 361
Cdd:PRK09088 189 IGLITSVRPVLAVGGSILvsnGFEPKRTLGRLGDPalgITH-----YFCVPQMAQAFRAQPgFDAAALRHLTALFTGGAP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 362 MPVEVFRTFQDRtGVRILEGYGLTEGACV--SSVNPPGGERRLGSIGLRIPGQMMKAVilDDAGRyvrDCVENEVGVLTI 439
Cdd:PRK09088 264 HAAEDILGWLDD-GIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVV--DDQGN---DCPAGVPGELLL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 440 SGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAA 519
Cdd:PRK09088 338 RGPNLSPGYWRRPQATARAFT-GDG--WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAV 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773712 520 IGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK09088 415 VGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLA-KYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
211-586 |
2.28e-42 |
|
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: 158.78 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 211 MSRESGDSLLIprrFEADDISSYFCTGGTTGLPKIAIRRHGNEV--ANAWSVGQVvgaGMGPGKTVFCGLPLFHVNAVLA 288
Cdd:cd05919 77 IARDCEARLVV---TSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAREAL---GLTPGDRVFSSAKMFFGYGLGN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 289 TGLVPFSRGAHVVLGTpqgyrGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNID-SLEYGLCGAAPMPVEVF 367
Cdd:cd05919 151 SLWFPLAVGASAVLNP-----GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALrSLRLCVSAGEALPRGLG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 368 RTFQDRTGVRILEGYGLTEGACVSSVNPPGgERRLGSIGLRIPGQMMKavILDDAGRYVRDcveNEVGVLTISGPNVFAG 447
Cdd:cd05919 226 ERWMEHFGGPILDGIGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIR--LVDEEGHTIPP---GEEGDLLVRGPSAAVG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 448 Y--LQEDQNKSLwldlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDV 525
Cdd:cd05919 300 YwnNPEKSRATF----NGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPES 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 526 HAGELPVAYVQLKAGATATET---ELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05919 374 TGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAH-KVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
229-582 |
2.88e-42 |
|
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: 155.74 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 229 DISSYFCTGGTTGLPK--IAIRRHGNEVANAWS-VGQVVGagmgpGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVlgtP 305
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTLRAAAAWAdCADLTE-----DDRYLIINPFFHTFGYKAGIVACLLTGATVV---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QG-YRGDGVVKRfweiVEHHRINFFSAVPTLYSALLDVPvDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVR-ILEG 381
Cdd:cd17638 73 VAvFDVDAILEA----IERERITVLPGPPTLFQSLLDHP-GRKKFDlsSLRAAVTGAATVPVELVRRMRSELGFEtVLTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTEGACVSSVNPPGGERRLGS-IGLRIPGqmMKAVILDDAGRYVRdcvenevgvltisGPNVFAGYLQEDQNKSLWLD 460
Cdd:cd17638 148 YGLTEAGVATMCRPGDDAETVATtCGRACPG--FEVRIADDGEVLVR-------------GYNVMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 lGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAG 540
Cdd:cd17638 213 -ADG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1142773712 541 ATATETELDTFIRgmigERAA---IPKRIHIVDAMPLTAVGKIFK 582
Cdd:cd17638 290 VTLTEEDVIAWCR----ERLAnykVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
225-588 |
5.63e-42 |
|
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: 159.03 E-value: 5.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 225 FEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLG- 303
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN--PEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHp 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 304 TPQGYRGDGvvkrfwEIVEHHRINFFSAVPTLYSALLdvpvdgRNID-----SLEYGLCGAAPMPVEVFRTFQDRTGVRI 378
Cdd:cd05909 222 NPLDYKKIP------ELIYDKKATILLGTPTFLRGYA------RAAHpedfsSLRLVVAGAEKLKDTLRQEFQEKFGIRI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 379 LEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDcvENEVGVLTISGPNVFAGYLQEDQNKSLW 458
Cdd:cd05909 290 LEGYGTTECSPVISVNTPQSPNKEGTVGRPLPG--MEVKIVSVETHEEVP--IGEGGLLLVRGPNVMLGYLNEPELTSFA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 459 LdlgdGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQ-IAAAIGRPDVHAGELPVAYVql 537
Cdd:cd05909 366 F----GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLT-- 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 538 kagaTATETELDTFIRGM--IG-ERAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:cd05909 440 ----TTTDTDPSSLNDILknAGiSNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
32-580 |
2.38e-41 |
|
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: 158.89 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALSFFLRADDHRKPL-----------RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPET----- 95
Cdd:cd17634 48 EDATLNLAANALDRHLRENGDRTAIiyegddtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAavaml 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 96 --------HFVIWGGEAAGivcainpllegpAIASLLKAANAKVLVTLAPF--PGSDIwsKIQPVLSE-----VPSLQSL 160
Cdd:cd17634 128 acarigavHSVIFGGFAPE------------AVAGRIIDSSSRLLITADGGvrAGRSV--PLKKNVDDalnpnVTSVEHV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 161 VLIDLAERVQGWRriaaramqrrECKRLHGRAGVRGAVPRHVaihdfdsamsresgdslliPRRFEADDISSYFCTGGTT 240
Cdd:cd17634 194 IVLKRTGSDIDWQ----------EGRDLWWRDLIAKASPEHQ-------------------PEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 241 GLPKIAIRRHGN-EVANAWSVGQVVGagMGPGKTVFCGLPLFHV--NAVLATGlvPFSRGAHVVL--GTPQGYRGDgvvk 315
Cdd:cd17634 245 GKPKGVLHTTGGyLVYAATTMKYVFD--YGPGDIYWCTADVGWVtgHSYLLYG--PLACGATTLLyeGVPNWPTPA---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RFWEIVEHHRINFFSAVPTLYSALL---DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVR---ILEGYGLTE--G 387
Cdd:cd17634 317 RMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTEtgG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 388 ACVSSVnPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDCVENEVgVLTISGP-NVFAGYLQEDQNKSLWLDLGDGrQ 466
Cdd:cd17634 397 FMITPL-PGAIELKAGSATRPVFG--VQPAVVDNEGHPQPGGTEGNL-VITDPWPgQTRTLFGDHERFEQTYFSTFKG-M 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLnTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:cd17634 472 YF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPE 550
|
570 580 590
....*....|....*....|....*....|....*..
gi 1142773712 547 ---ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17634 551 lyaELRNWVRKEIG-PLATPDVVHWVDSLPKTRSGKI 586
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
227-580 |
1.22e-40 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 154.17 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDISSYFCTGGTTGLPKIAIRRHGN--EVANAWSVgQVVGAgmgPGKTVFCGLP-LFHVNAVLATGLVPFSRGAHVVL- 302
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDplASADRYAV-NVLRL---REDDRFVGSPpLAFTFGLGGVLLFPFGVGASGVLl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 303 --GTPQgyrgdgvvkRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRIL 379
Cdd:cd05958 172 eeATPD---------LLLSAIARYKPTVLFTAPTAYRAMLAHPdAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 380 EGYGLTEGACVSSVNPPGgERRLGSIGLRIPGqmMKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLwl 459
Cdd:cd05958 243 DGIGSTEMFHIFISARPG-DARPGATGKPVPG--YEAKVVDDEGNPVPD---GTIGRLAVRGPTGCRYLADKRQRTYV-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 460 dlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKA 539
Cdd:cd05958 315 --QGG--WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRP 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1142773712 540 GATATET---ELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05958 391 GVIPGPVlarELQDHAKAHIAPY-KYPRAIEFVTELPRTATGKL 433
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
59-580 |
1.49e-40 |
|
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: 155.76 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCAinPLLEGPAIASLLKAAN-AKVLVTLAP 137
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVA--PTNDIYNERELDHSLNiSKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 138 FPGSDiwsKIQPVLSEVPSLQSLVLIDLAERVQGWRRIAARAMQRreckrlhgragvrgaVPRHVAIHDFdsamsresgd 217
Cdd:cd17642 124 KKGLQ---KVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQN---------------LPPGFNEYDF---------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 218 sllIPRRFEAD-DISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQ-VVGAGMGPGKTVFCGLPLFHVNAVLATgLVPFS 295
Cdd:cd17642 176 ---KPPSFDRDeQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAILTVIPFHHGFGMFTT-LGYLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 296 RGAHVVLGtpqgYRGDGvvKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRT 374
Cdd:cd17642 252 CGFRVVLM----YKFEE--ELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGAPLSKEVGEAVAKRF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 GVR-ILEGYGLTEGACVSSVNPPGGERRlGSIGLRIPGQMMKAVILDdAGRYVRdcvENEVGVLTISGPNVFAGYLQEDQ 453
Cdd:cd17642 326 KLPgIRQGYGLTETTSAILITPEGDDKP-GAVGKVVPFFYAKVVDLD-TGKTLG---PNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 454 NKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVA 533
Cdd:cd17642 401 ATKALID-KDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAA 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1142773712 534 YVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17642 478 VVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKI 524
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
226-521 |
1.53e-40 |
|
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: 153.91 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTP 305
Cdd:cd05907 85 DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPAT--EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QGYRGDG----------VVKRFWEivEHHRINFFSAVPTLYSALLDVPVDGRnidsLEYGLCGAAPMPVEVFRTFQdRTG 375
Cdd:cd05907 163 AETLLDDlsevrptvflAVPRVWE--KVYAAIKVKAVPGLKRKLFDLAVGGR----LRFAASGGAPLPAELLHFFR-ALG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 376 VRILEGYGLTEGACVSSVNPPGGERrLGSIGLRIPGqmMKAVILDDagryvrdcvenevGVLTISGPNVFAGYLQEDQNK 455
Cdd:cd05907 236 IPVYEGYGLTETSAVVTLNPPGDNR-IGTVGKPLPG--VEVRIADD-------------GEILVRGPNVMLGYYKNPEAT 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 456 SLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELII-RGGHNIDPATIEEPLHRHPAVQIAAAIG 521
Cdd:cd05907 300 AEALD-ADG--WLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
18-586 |
4.22e-40 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 154.53 E-value: 4.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 18 PPAD--LPAstyeMIGRGAAIDPSAPalsfFLRADDhrkpLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPET 95
Cdd:PRK06155 17 PPSErtLPA----MLARQAERYPDRP----LLVFGG----TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 96 HFVIWG-GEAAGIVCAINPLLEGPAIASLLKAANAKVLVTLAPFpgsdiWSKIQPVLSEVPSLQSLVLIDlaervqgwrr 174
Cdd:PRK06155 85 LDVFLGcAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-----LAALEAADPGDLPLPAVWLLD---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 175 iaaramqrreckrlhgrAGVRGAVPRHVaihdfdSAMSRESGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEV 254
Cdd:PRK06155 150 -----------------APASVSVPAGW------STAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 255 AnaWSVGQVVGAGMGPGKTVFCGLPLFHVNAvLATGLVPFSRGAHVVLGTPQGyrgdgvVKRFWEIVEHHRINFFSAVPT 334
Cdd:PRK06155 207 W--WGRNSAEDLEIGADDVLYTTLPLFHTNA-LNAFFQALLAGATYVLEPRFS------ASGFWPAVRRHGATVTYLLGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 335 LYSALLDVPVDGRNIDS-LEYGLCGAapMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPggERRLGSIGLRIPGqm 413
Cdd:PRK06155 278 MVSILLSQPARESDRAHrVRVALGPG--VPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHG--SQRPGSMGRLAPG-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 414 MKAVILDDAGRYVRDCVENEVgVLTISGPNVFA-GYLqEDQNKSL--WLDLgdgrqWLNTGDLARRDAQGYFWLTGRRKE 490
Cdd:PRK06155 352 FEARVVDEHDQELPDGEPGEL-LLRADEPFAFAtGYF-GMPEKTVeaWRNL-----WFHTGDRVVRDADGWFRFVDRIKD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 491 LIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVD 570
Cdd:PRK06155 425 AIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLA-YFAVPRYVEFVA 503
|
570
....*....|....*.
gi 1142773712 571 AMPLTAVGKIFKPELK 586
Cdd:PRK06155 504 ALPKTENGKVQKFVLR 519
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
59-586 |
5.20e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 153.98 E-value: 5.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLAP 137
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGaVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 138 FPGsdiwsKIQPvLSEVPSLQsLVLIDlaERVQGWRRIAArAMQRREckrlhgragvrgAVPRHVAIHDfdsamsresgd 217
Cdd:PLN02246 132 YVD-----KLKG-LAEDDGVT-VVTID--DPPEGCLHFSE-LTQADE------------NELPEVEISP----------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 218 slliprrfeaDDISSYFCTGGTTGLPKIAIRRHGNEVAnawSVGQVVGA-----GMGPGKTVFCGLPLFHV---NAVLAT 289
Cdd:PLN02246 179 ----------DDVVALPYSSGTTGLPKGVMLTHKGLVT---SVAQQVDGenpnlYFHSDDVILCVLPMFHIyslNSVLLC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 290 GLvpfsR-GAHVVlgtpqgyrgdgVVKRF-----WEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPM 362
Cdd:PLN02246 246 GL----RvGAAIL-----------IMPKFeigalLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 363 PVEVFRTFQDR-TGVRILEGYGLTEGACVSSVNPPGG----ERRLGSIGLRIPGQMMKavILD-DAGRYVRdcvENEVGV 436
Cdd:PLN02246 311 GKELEDAFRAKlPNAVLGQGYGMTEAGPVLAMCLAFAkepfPVKSGSCGTVVRNAELK--IVDpETGASLP---RNQPGE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 437 LTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQI 516
Cdd:PLN02246 386 ICIRGPQIMKGYLNDPEATANTID-KDG--WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 517 AAAIGRPDVHAGELPVAYVQLKAGATATETEldtfIRGMIGERAAIPKRIH---IVDAMPLTAVGKIFKPELK 586
Cdd:PLN02246 463 AAVVPMKDEVAGEVPVAFVVRSNGSEITEDE----IKQFVAKQVVFYKRIHkvfFVDSIPKAPSGKILRKDLR 531
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
27-589 |
6.46e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 154.28 E-value: 6.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAiDPSAPALSF-FLRADDHRKplrWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAA 105
Cdd:PRK04319 46 YEAIDRHAD-GGRKDKVALrYLDASRKEK---YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 106 G-IVCainPLLE--GP-AIASLLKAANAKVLVTLApfpgsDIWSKIqpVLSEVPSLQSLVLIDlaervqgwrriaaramq 181
Cdd:PRK04319 122 GaIVG---PLFEafMEeAVRDRLEDSEAKVLITTP-----ALLERK--PADDLPSLKHVLLVG----------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 182 rreckrlhgraGVRGAVPRHVaihDFDSAMsRESGDSLLIPRrFEADDISSYFCTGGTTGLPKIAIRRHgNEVANAWSVG 261
Cdd:PRK04319 175 -----------EDVEEGPGTL---DFNALM-EQASDEFDIEW-TDREDGAILHYTSGSTGKPKGVLHVH-NAMLQHYQTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 262 QVVgAGMGPGKTVFCglplfhvNA----VLAT--GLV-PFSRGAHVVLgtpqgYRGDGVVKRFWEIVEHHRINFFSAVPT 334
Cdd:PRK04319 238 KYV-LDLHEDDVYWC-------TAdpgwVTGTsyGIFaPWLNGATNVI-----DGGRFSPERWYRILEDYKVTVWYTAPT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 335 LYSALL---DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPG 411
Cdd:PRK04319 305 AIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 412 qmMKAVILDDAGryvrDCVE-NEVGVLTI-SG-PNVFAGYLQEDQ--NKSLWLDlgdgrqWLNTGDLARRDAQGYFWLTG 486
Cdd:PRK04319 385 --IEAAIVDDQG----NELPpNRMGNLAIkKGwPSMMRGIWNNPEkyESYFAGD------WYVSGDSAYMDEDGYFWFQG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 487 RRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATEtELDTFIRGMIGER---AAIP 563
Cdd:PRK04319 453 RVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE-ELKEEIRGFVKKGlgaHAAP 531
|
570 580
....*....|....*....|....*.
gi 1142773712 564 KRIHIVDAMPLTAVGKIFKPELKRWE 589
Cdd:PRK04319 532 REIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
27-586 |
7.49e-40 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 153.80 E-value: 7.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALsffLRADDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:cd05970 20 YDVVDAMAKEYPDKLAL---VWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 -IVCAINPLLEGPAIASLLKAANAKVLVTLApfpGSDIWSKIQPVLSEVPSLQSLVLIDLAERvQGWRriaaramqrrec 185
Cdd:cd05970 97 aIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIEKAAPECPSKPKLVWVGDPVP-EGWI------------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 186 krlhgragvrgavprhvaihDFDSAMSRESGDsllIPRR-----FEADDISSYFCTGGTTGLPKIAirrhgnEVANAWSV 260
Cdd:cd05970 161 --------------------DFRKLIKNASPD---FERPtansyPCGEDILLVYFSSGTTGMPKMV------EHDFTYPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 261 GQVVGA----GMGPGktvfcGLPLfhvnAVLATGLvpfsrgAHVVLGT--PQGYRGDGVV----KRF-----WEIVEHHR 325
Cdd:cd05970 212 GHIVTAkywqNVREG-----GLHL----TVADTGW------GKAVWGKiyGQWIAGAAVFvydyDKFdpkalLEKLSKYG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 326 INFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEgACVSSVNPPGGERRLGSI 405
Cdd:cd05970 277 VTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTE-TTLTIATFPWMEPKPGSM 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 406 GLRIPGqmMKAVILDDAGRYVRDCVENEVGVLTISGPNV--FAGYLQ-EDQNKSLWLDlgdgrQWLNTGDLARRDAQGYF 482
Cdd:cd05970 356 GKPAPG--YEIDLIDREGRSCEAGEEGEIVIRTSKGKPVglFGGYYKdAEKTAEVWHD-----GYYHTGDAAWMDEDGYL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 483 WLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET---ELDTFIRGMIGER 559
Cdd:cd05970 429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTAPY 508
|
570 580
....*....|....*....|....*..
gi 1142773712 560 AAiPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05970 509 KY-PRIVEFVDELPKTISGKIRRVEIR 534
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
236-580 |
1.28e-39 |
|
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: 148.57 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWsvgQVVGA-GMGPGKTVFCGLPLFHVNAvLATGLVPFSRGAHVVlgtpqgyrgdgVV 314
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIAANL---QLIHAmGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANV-----------VM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 315 KRF-----WEIVEHHRINFFSAVPTLYSALLD-VPVDGRNIDSLEYGLCGAAPmpvEVFRTFQDRTGVRILEGYGLTEGA 388
Cdd:cd17637 73 EKFdpaeaLELIEEEKVTLMGSFPPILSNLLDaAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 389 CVSSVNPpgGERRLGSIGLriPGQMMKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWL 468
Cdd:cd17637 150 GLVTLSP--YRERPGSAGR--PGPLVRVRIVDDNDRPVPA---GETGEIVVRGPLVFQGYWNLPELTAYTFRNG----WH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 469 NTGDLARRDAQGYFWLTGRR--KELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTAD 298
|
330 340 350
....*....|....*....|....*....|....
gi 1142773712 547 ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17637 299 ELIEFVGSRIA-RYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
30-586 |
1.99e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 152.62 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 30 IGRGAAIDPSAPALSFFLRADdhrkplrwTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG-IV 108
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTT--------TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGaIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 109 CAINPLLEGPAIASLLKAANAKVLVTLAPfpgsdiwskIQPVLSEV----PSLQSLVLI--DLAERVQGWRRIAARAmqr 182
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVSDCGAHVVVTEAA---------LAPVATAVrdivPLLSTVVVAggSSDDSVLGYEDLLAEA--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 183 reckrlhgragvrGAVPRHVAIHDfdsamsresgdslliprrfeaDDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQ 262
Cdd:PRK07786 163 -------------GPAHAPVDIPN---------------------DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 263 VVGAGMGpGKTVFCGLPLFHVNAV--LATGLVpfsRGAHVVLgTPQGYRGDGvvkRFWEIVEHHRINFFSAVPTLYSALL 340
Cdd:PRK07786 209 TNGADIN-SDVGFVGVPLFHIAGIgsMLPGLL---LGAPTVI-YPLGAFDPG---QLLDVLEAEKVTGIFLVPAQWQAVC 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 341 DVP-VDGRNIdSLEYGLCGAAPMPVEVFRTFQDR-TGVRILEGYGLTEGACVSSVnpPGGE---RRLGSIGLRIPgqMMK 415
Cdd:PRK07786 281 AEQqARPRDL-ALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEMSPVTCM--LLGEdaiRKLGSVGKVIP--TVA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 416 AVILDDAgryVRDCVENEVGVLTISGPNVFAGYLQedqNKSLWLDLGDGrQWLNTGDLARRDAQGYFWLTGRRKELIIRG 495
Cdd:PRK07786 356 ARVVDEN---MNDVPVGEVGEIVYRAPTLMSGYWN---NPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 496 GHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE-TELDTFIRGMIGeRAAIPKRIHIVDAMPL 574
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTlEDLAEFLTDRLA-RYKHPKALEIVDALPR 507
|
570
....*....|..
gi 1142773712 575 TAVGKIFKPELK 586
Cdd:PRK07786 508 NPAGKVLKTELR 519
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
236-589 |
2.21e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 151.30 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPK-IAIRRHG-----NEVANAWsvgqvvgaGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGA---HVVLGTPQ 306
Cdd:PRK07787 136 TSGTTGPPKgVVLSRRAiaadlDALAEAW--------QWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNrfvHTGRPTPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 307 GY----RGDGVVkrfweivehhrinFFsAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGY 382
Cdd:PRK07787 208 AYaqalSEGGTL-------------YF-GVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEGACVSSVNPpGGERRLGSIGLRIPGQMMKAVilDDAGRYVRDCVEnEVGVLTISGPNVFAGYL-QEDQNKSLWLDl 461
Cdd:PRK07787 274 GMTETLITLSTRA-DGERRPGWVGLPLAGVETRLV--DEDGGPVPHDGE-TVGELQVRGPTLFDGYLnRPDATAAAFTA- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 462 gDGrqWLNTGDLARRDAQGYFWLTGRRK-ELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQlkAG 540
Cdd:PRK07787 349 -DG--WFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GA 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1142773712 541 ATATETELDTFirgmIGERAAIPKR---IHIVDAMPLTAVGKIFKPELKRWE 589
Cdd:PRK07787 424 DDVAADELIDF----VAQQLSVHKRpreVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
236-586 |
4.02e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 151.00 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKiAIRRHGNEVANAWSVGQVVGAGMG--PGKTVFCGLPLFHvNAVLATGLVPFSRGAHVVLgTPqgyRGDGv 313
Cdd:PRK12406 160 TSGTTGHPK-GVRRAAPTPEQAAAAEQMRALIYGlkPGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVL-QP---RFDP- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 314 vKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRN---IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACV 390
Cdd:PRK12406 233 -EELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAkydVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 391 SSVNPPGGERRLGSIGLRIPGQMMKavILDDAGRYVRDcveNEVG--VLTISGPNVFAGYLQEDQNKSLwldlgDGRQWL 468
Cdd:PRK12406 312 TFATSEDALSHPGTVGKAAPGAELR--FVDEDGRPLPQ---GEIGeiYSRIAGNPDFTYHNKPEKRAEI-----DRGGFI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 469 NTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETEL 548
Cdd:PRK12406 382 TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADI 461
|
330 340 350
....*....|....*....|....*....|....*...
gi 1142773712 549 DTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK12406 462 RAQLKARLA-GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
57-591 |
8.36e-39 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 150.67 E-value: 8.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGI---DRHAVVAYvlpNlPETHFVIW-GGEAAGIVC-AINPLLEGPAIASLLKAANAKV 131
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIklgDRVATIAW---N-TWRHLEAWyGIMGIGAIChTVNPRLFPEQIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 132 LVTLAPF-PgsdIWSKIQPVLsevPSLQS-LVLIDLAERVQgwrriaaramqrreckrlhgrAGVRGAVPrhvaihdFDS 209
Cdd:PRK06018 115 VITDLTFvP---ILEKIADKL---PSVERyVVLTDAAHMPQ---------------------TTLKNAVA-------YEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 210 AMSRESGDSLLipRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLAT 289
Cdd:PRK06018 161 WIAEADGDFAW--KTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 290 GLVPfSRGAHVVLgtpQGYRGDGVvkRFWEIVEHHRINFFSAVPTLYSALLD-VPVDGRNIDSLEYGLCGAAPMPVEVFR 368
Cdd:PRK06018 239 FSAP-SMGTKLVM---PGAKLDGA--SVYELLDTEKVTFTAGVPTVWLMLLQyMEKEGLKLPHLKMVVCGGSAMPRSMIK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 369 TFQDrTGVRILEGYGLTEGACVSSV--------NPPGGER--RLGSIGLRIPGQMMKavILDDAGRYV-RDcvENEVGVL 437
Cdd:PRK06018 313 AFED-MGVEVRHAWGMTEMSPLGTLaalkppfsKLPGDARldVLQKQGYPPFGVEMK--ITDDAGKELpWD--GKTFGRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 438 TISGPNVFAGYLQEDQNkslwldLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIA 517
Cdd:PRK06018 388 KVRGPAVAAAYYRVDGE------ILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 518 AAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKrwETF 591
Cdd:PRK06018 462 AVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIA-KWWMPDDVAFVDAIPHTATGKILKTALR--EQF 532
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
58-586 |
9.82e-39 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 150.51 E-value: 9.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLVTLA 136
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGgVFSGANPTALESEIKKQAEAAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 137 PFPGsdiwskiqpvlsEVPSLQSLVLIDLAERVQGwrriaarAMQRRECKRLHGRAGVRGAvprHVAIHDfdsamsresg 216
Cdd:PLN02330 136 TNYG------------KVKGLGLPVIVLGEEKIEG-------AVNWKELLEAADRAGDTSD---NEEILQ---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 217 dslliprrfeaDDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMgPGKTVFCGL-PLFHVNAVLATGLVPF- 294
Cdd:PLN02330 184 -----------TDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEM-IGQVVTLGLiPFFHIYGITGICCATLr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 295 SRGAHVVLGtpqgyRGDgvVKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYG--LCGAAPMPVEVFRTFQ 371
Cdd:PLN02330 252 NKGKVVVMS-----RFE--LRTFLNALITQEVSFAPIVPPIILNLVKNPiVEEFDLSKLKLQaiMTAAAPLAPELLTAFE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DR-TGVRILEGYGLTEGACVSSV--NPPGGE--RRLGSIGLRIPGQMMKaVILDDAGRYVRdcvENEVGVLTISGPNVFA 446
Cdd:PLN02330 325 AKfPGVQVQEAYGLTEHSCITLThgDPEKGHgiAKKNSVGFILPNLEVK-FIDPDTGRSLP---KNTPGELCVRSQCVMQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 447 GYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVH 526
Cdd:PLN02330 401 GYYNNKEETDRTID-EDG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 527 AGELPVAYVQLKAGATATETELDTFIRGMIGERAAIpKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PLN02330 478 AGEIPAACVVINPKAKESEEDILNFVAANVAHYKKV-RVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
31-586 |
8.73e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 147.15 E-value: 8.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 31 GRGAAIDPSAPAlsfFLRADDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-C 109
Cdd:PRK13391 4 GIHAQTTPDKPA---VIMASTGE---VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYyT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 110 AINPLLEGPAIASLLKAANAKVLVTlapfpgSDIWSKIQPVLSE-VPSLQSLVLIDLAERVQGWRRIAAramqrreckrl 188
Cdd:PRK13391 78 CVNSHLTPAEAAYIVDDSGARALIT------SAAKLDVARALLKqCPGVRHRLVLDGDGELEGFVGYAE----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 189 hgragVRGAVPrhvaihdfDSAMSRES-GDSLLIprrfeaddiSSyfctgGTTGLPKiAIRRHGNEV------------A 255
Cdd:PRK13391 141 -----AVAGLP--------ATPIADESlGTDMLY---------SS-----GTTGRPK-GIKRPLPEQppdtplpltaflQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 256 NAWsvgqvvgaGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGtpqgyRGDGvvKRFWEIVEHHRINFFSAVPTL 335
Cdd:PRK13391 193 RLW--------GFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME-----HFDA--EQYLALIEEYGVTHTQLVPTM 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 336 YSALLDVPVDGRN---IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGq 412
Cdd:PRK13391 258 FSRMLKLPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 413 mmKAVILDDAGRyvrDCVENEVGVLTISGPNVFAgYLQeDQNKSLWLDLGDGrQWLNTGDLARRDAQGYFWLTGRRKELI 492
Cdd:PRK13391 337 --DLHILDDDGA---ELPPGEPGTIWFEGGRPFE-YLN-DPAKTAEARHPDG-TWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 493 IRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE---TELDTFIRGMIGeRAAIPKRIHIV 569
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLS-RQKCPRSIDFE 487
|
570
....*....|....*..
gi 1142773712 570 DAMPLTAVGKIFKPELK 586
Cdd:PRK13391 488 DELPRLPTGKLYKRLLR 504
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
57-586 |
1.10e-37 |
|
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: 148.62 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGI---DRhaVVAYvLPNLPETHF-------------VIWGGEAAgivcainpllegPAI 120
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVvkgDR--VIIY-MPMIPEAAIamlacarigaihsVVFGGFAA------------KEL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 121 ASLLKAANAKVLVTlAPF---PGsdiwsKIQPVLSevpslqslvLIDLAERVQGWRRIAARAMQRRECKrlhgraGVRGA 197
Cdd:cd05967 147 ASRIDDAKPKLIVT-ASCgiePG-----KVVPYKP---------LLDKALELSGHKPHHVLVLNRPQVP------ADLTK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 198 VPRHVaihDFDSAMS-RESGDSLLIprrfEADDISSYFCTGGTTGLPKIAIRRHGNE-VANAWSVGQVVGagMGPGKTVF 275
Cdd:cd05967 206 PGRDL---DWSELLAkAEPVDCVPV----AATDPLYILYTSGTTGKPKGVVRDNGGHaVALNWSMRNIYG--IKPGDVWW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 276 C----GLPLFHVNAVLAtglvPFSRGAHVVL--GTPQGYRGDGVvkrFWEIVEHHRIN-FFSAvPTLYSALLDVPVDGR- 347
Cdd:cd05967 277 AasdvGWVVGHSYIVYG----PLLHGATTVLyeGKPVGTPDPGA---FWRVIEKYQVNaLFTA-PTAIRAIRKEDPDGKy 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 348 ----NIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTE-GACVSSvNPPGGER---RLGSIGLRIPGQMMKavIL 419
Cdd:cd05967 349 ikkyDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTEtGWPITA-NPVGLEPlpiKAGSPGKPVPGYQVQ--VL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 420 DDAGRYVRdcvENEVGVLTISGPnVFAGYLQedqnkSLWLD--------LGDGRQWLNTGDLARRDAQGYFWLTGRRKEL 491
Cdd:cd05967 426 DEDGEPVG---PNELGNIVIKLP-LPPGCLL-----TLWKNderfkklyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDV 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 492 IIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATAT----ETELDTFIRGMIGERAAiPKRIH 567
Cdd:cd05967 497 INVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAA-FRLVI 575
|
570
....*....|....*....
gi 1142773712 568 IVDAMPLTAVGKIFKPELK 586
Cdd:cd05967 576 FVKRLPKTRSGKILRRTLR 594
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
12-585 |
1.87e-37 |
|
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: 145.93 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 12 RIENQGPPADLPASTYemIGRGAAIDPSAPALsfflRADDHRkplrWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPN 91
Cdd:cd05920 5 RYRAAGYWQDEPLGDL--LARSAARHPDRIAV----VDGDRR----LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 92 LPEthFVIwggeaagivcainpllegpAIASLLKAAnakvlvtlapfpgsdiwskIQPVLSeVPSLQSLVLIDLAERVQg 171
Cdd:cd05920 75 VAE--FVV-------------------LFFALLRLG-------------------AVPVLA-LPSHRRSELSAFCAHAE- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 172 wrriaARAMqrreckrlhgragvrgAVPRhvAIHDFDS-AMSRESGDSllIPrrfeadDISSYFCTGGTTGLPKIAIRRH 250
Cdd:cd05920 113 -----AVAY----------------IVPD--RHAGFDHrALARELAES--IP------EVALFLLSGGTTGTPKLIPRTH 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 251 GNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHvNAVLAT--GLVPFSRGAHVVLGTpqgyrgDGVVKRFWEIVEHHRINF 328
Cdd:cd05920 162 NDYAYNVRASAEV--CGLDQDTVYLAVLPAAH-NFPLACpgVLGTLLAGGRVVLAP------DPSPDAAFPLIEREGVTV 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 329 FSAVPTLYSALLD-VPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEG-ACVSSVNPPGgERRLGSIG 406
Cdd:cd05920 233 TALVPALVSLWLDaAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGlLNYTRLDDPD-EVIIHTQG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 407 LRI-PGQMMKavILDDAGRYVRdcvENEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLT 485
Cdd:cd05920 312 RPMsPDDEIR--VVDEEGNPVP---PGEEGELLTRGPYTIRGYYRAPEHNARAFT-PDG--FYRTGDLVRRTPDGYLVVE 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 486 GRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATEtELDTFIRGMIGERAAIPKR 565
Cdd:cd05920 384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAA-QLRRFLRERGLAAYKLPDR 462
|
570 580
....*....|....*....|
gi 1142773712 566 IHIVDAMPLTAVGKIFKPEL 585
Cdd:cd05920 463 IEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
57-586 |
2.38e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 146.39 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGI---DRHAVVAYVLPNLPETHFVIWGgeaAGIVC-AINPLLEGPAIASLLKAANAKVL 132
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVepgDRVGTLAWNGYRHLEAYYGVSG---SGAVChTINPRLFPEQIAYIVNHAEDRYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 133 ---VTLAPFpgsdiwskIQPVLSEVPSlqslvlidlaerVQGWRriaarAMqrreCKRLHGRAGvrgAVPrhvaIHDFDS 209
Cdd:PRK07008 116 lfdLTFLPL--------VDALAPQCPN------------VKGWV-----AM----TDAAHLPAG---STP----LLCYET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 210 AMSRESGDSLLiPRrFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAvlaT 289
Cdd:PRK07008 160 LVGAQDGDYDW-PR-FDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNA---W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 290 GLvPFS---RGAHVVLGTPQGyrgDGvvKRFWEIVEHHRINFFSAVPTLYSALLD-VPVDGRNIDSLEYGLCGAAPMPVE 365
Cdd:PRK07008 235 GL-PYSaplTGAKLVLPGPDL---DG--KSLYELIEAERVTFSAGVPTVWLGLLNhMREAGLRFSTLRRTVIGGSACPPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 366 VFRTFQDRTGVRILEGYGLTEGACVSSV--------NPPGGERR--LGSIGLRIPGQMMKavILDDAGRYVR-DCVEneV 434
Cdd:PRK07008 309 MIRTFEDEYGVEVIHAWGMTEMSPLGTLcklkwkhsQLPLDEQRklLEKQGRVIYGVDMK--IVGDDGRELPwDGKA--F 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 435 GVLTISGPNVFAGYLQEDQNKslwldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAV 514
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASP-----LVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1142773712 515 QIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK07008 458 AEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVA-KWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
173-582 |
5.71e-37 |
|
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: 144.06 E-value: 5.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 173 RRIAARAMQRRECKRLHGRAGVRGAvprHVAIHDFDSAmsRESGDSLLIPRRFEADDISSyfcTGGTTGLPKiAIRRH-- 250
Cdd:cd05929 78 RAEACAIIEIKAAALVCGLFTGGGA---LDGLEDYEAA--EGGSPETPIEDEAAGWKMLY---SGGTTGRPK-GIKRGlp 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 251 GNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHvNAVLATGLVPFSRGAHVVLgtpqgyrgdgVVK----RFWEIVEHHRI 326
Cdd:cd05929 149 GGPPDNDTLMAAALGFGPGADSVYLSPAPLYH-AAPFRWSMTALFMGGTLVL----------MEKfdpeEFLRLIERYRV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 327 NFFSAVPTLYSALLDVPVDGRN---IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNppgGERRL- 402
Cdd:cd05929 218 TFAQFVPTMFVRLLKLPEAVRNaydLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN---GEEWLt 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 403 --GSIGLRIPGQMMkavILDDAGRYVRDCVENEVGVLTISGPNVFAGYLQEDQNKslwldlgDGRQWLNTGDLARRDAQG 480
Cdd:cd05929 295 hpGSVGRAVLGKVH---ILDEDGNEVPPGEIGEVYFANGPGFEYTNDPEKTAAAR-------NEGGWSTLGDVGYLDEDG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 481 YFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGA---TATETELDTFIRGMIg 557
Cdd:cd05929 365 YLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLRDRL- 443
|
410 420
....*....|....*....|....*
gi 1142773712 558 ERAAIPKRIHIVDAMPLTAVGKIFK 582
Cdd:cd05929 444 SRYKCPRSIEFVAELPRDDTGKLYR 468
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
27-585 |
2.04e-36 |
|
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: 143.03 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSfflradDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG 106
Cdd:cd05923 4 FEMLRRAASRAPDACAIA------DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 107 IVCA-INPLLEGPAIASLLKAANAKvlvtlapfpgsdiwskiqpvlsevpslqSLVLIDLAERVQGwrriaaramqrrec 185
Cdd:cd05923 78 AVPAlINPRLKAAELAELIERGEMT----------------------------AAVIAVDAQVMDA-------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 186 krlhgragVRGAVPRHVAIHDFDSAMSRESGDSLLIPRRFEADDISSYFCTGGTTGLPKIAI--RRHGNEVANAWSvgQV 263
Cdd:cd05923 116 --------IFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVipQRAAESRVLFMS--TQ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 264 VGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtPQGYRGDGVVKrfweIVEHHRINFFSAVPTLYSALL-DV 342
Cdd:cd05923 186 AGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV--VEEFDPADALK----LIEQERVTSLFATPTHLDALAaAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 343 PVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEgACVSSVNPpggERRLGSiGLRiPG--QMMKAV-IL 419
Cdd:cd05923 260 EFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE-AMNSLYMR---DARTGT-EMR-PGffSEVRIVrIG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 420 DDAGRYVRDCVENEVgVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNI 499
Cdd:cd05923 334 GSPDEALANGEEGEL-IVAAAADAAFTGYLNQPEATAKKLQDG----WYRTGDVGYVDPSGDVRILGRVDDMIISGGENI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 500 DPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGaTATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGK 579
Cdd:cd05923 409 HPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNK 487
|
....*.
gi 1142773712 580 IFKPEL 585
Cdd:cd05923 488 VLRRQL 493
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
209-580 |
2.22e-36 |
|
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: 141.90 E-value: 2.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 209 SAMSRESGDSLLIPrrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVNAVLA 288
Cdd:cd05930 77 AYILEDSGAKLVLT---DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP--LTPGDRVLQFTSFSFDVSVWE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 289 TgLVPFSRGAHVVLgTPQGYRGDGVvkRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNiDSLEYGLCGAAPMPVEVFR 368
Cdd:cd05930 152 I-FGALLAGATLVV-LPEEVRKDPE--ALADLLAEEGITVLHLTPSLLRLLLQELELAAL-PSLRLVLVGGEALPPDLVR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 369 TFQDR-TGVRILEGYGLTEGACVSS---VNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRDcveNEVGVLTISGPNV 444
Cdd:cd05930 227 RWRELlPGARLVNLYGPTEATVDATyyrVPPDDEEDGRVPIGRPIPN--TRVYVLDENLRPVPP---GVPGELYIGGAGL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 445 FAGYL-QEDQNKSLWL-DLGDGRQWL-NTGDLARRDAQGYFWLTGRRKELI-IRGgHNIDPATIEEPLHRHPAVQIAAAI 520
Cdd:cd05930 302 ARGYLnRPELTAERFVpNPFGPGERMyRTGDLVRWLPDGNLEFLGRIDDQVkIRG-YRIELGEIEAALLAHPGVREAAVV 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 521 GRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05930 381 AREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPD-YMVPSAFVVLDALPLTPNGKV 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
38-590 |
4.84e-36 |
|
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: 142.60 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 38 PSAPALSFflrADDHRKPLRWTYAALLRDITRAANMFSRL-GIDRHAVVAYVLPNLPETHFVIWGGEAAGIVcaINP--- 113
Cdd:cd05928 25 PPNPALWW---VNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--FIPgti 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 114 LLEGPAIASLLKAANAKVLVT---LAPfpgsdiwsKIQPVLSEVPSLQSLVLIDlAERVQGWrriaaramqrreckrLHG 190
Cdd:cd05928 100 QLTAKDILYRLQASKAKCIVTsdeLAP--------EVDSVASECPSLKTKLLVS-EKSRDGW---------------LNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 191 RAGVRGAVPRHVAIhdfdsamsrESGDSlliprrfeadDISSYFCTGGTTGLPKIAIRRHGnevanAWSVGQVVGA---- 266
Cdd:cd05928 156 KELLNEASTEHHCV---------ETGSQ----------EPMAIYFTSGTTGSPKMAEHSHS-----SLGLGLKVNGrywl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 267 GMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGYRGDGVVKrfweIVEHHRINFFSAVPTLYSALLDVPVDG 346
Cdd:cd05928 212 DLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILK----TLSSYPITTFCGAPTVYRMLVQQDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 347 RNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSvNPPGGERRLGSIGLRIPGQMMKavILDDAGRYV 426
Cdd:cd05928 288 YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICA-NFKGMKIKPGSMGKASPPYDVQ--IIDDNGNVL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 427 RDCVENEVGVLTisGPN----VFAGYLqEDQNKSLWLDLGDgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPA 502
Cdd:cd05928 365 PPGTEGDIGIRV--KPIrpfgLFSGYV-DNPEKTAATIRGD---FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 503 TIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE-----TELDTFIRGmIGERAAIPKRIHIVDAMPLTAV 577
Cdd:cd05928 439 EVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDpeqltKELQQHVKS-VTAPYKYPRKVEFVQELPKTVT 517
|
570
....*....|...
gi 1142773712 578 GKIFKPELKRWET 590
Cdd:cd05928 518 GKIQRNELRDKEW 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
59-586 |
1.41e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 140.79 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPE-THFVIWGGEAAGIVCAINPLLEGPAIASLLKAANAKVLVtlap 137
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAfLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 138 fpgsdiwskIQPVLSEVPSLQSLVLIDLAERVQGWRRIAARAMqrrECKRLHGRAgvrgavprhvaihdfdsamsresgd 217
Cdd:PRK06145 105 ---------VDEEFDAIVALETPKIVIDAAAQADSRRLAQGGL---EIPPQAAVA------------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 218 slliprrfeADDISSYFCTGGTTGLPKIAIRRHGNEvanAW-SVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSR 296
Cdd:PRK06145 148 ---------PTDLVRLMYTSGTTDRPKGVMHSYGNL---HWkSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 297 GAhvVLGTPQGYRGDGVVkrfwEIVEHHRINFFSAVPTLYSALLDVPVDGR-NIDSLEYGLCGAAPMPVEVFRTFQDR-T 374
Cdd:PRK06145 216 GG--TLRIHREFDPEAVL----AAIERHRLTCAWMAPVMLSRVLTVPDRDRfDLDSLAWCIGGGEKTPESRIRDFTRVfT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 GVRILEGYGLTEGACVSSVNPPGGE-RRLGSIGLRIPgqMMKAVILDDAGRYVrdcVENEVGVLTISGPNVFAGYLQeDQ 453
Cdd:PRK06145 290 RARYIDAYGLTETCSGDTLMEAGREiEKIGSTGRALA--HVEIRIADGAGRWL---PPNMKGEICMRGPKVTKGYWK-DP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 454 NKSLWLDLGDgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVA 533
Cdd:PRK06145 364 EKTAEAFYGD---WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 534 YVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK06145 441 VVVLNPGATLTLEALDRHCRQRLAS-FKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
10-580 |
1.60e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 141.18 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 10 VLRIENQGPPADLPASTYEMIGRGAAIDPSAPALSFflraDDHRKPLrwTYAALLRDITRAANMFSRLGIDRHAVVAYVL 89
Cdd:PRK05852 2 RFMGGAAPMASDFGPRIADLVEVAATRLPEAPALVV----TADRIAI--SYRDLARLVDDLAGQLTRSGLLPGDRVALRM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 90 PNLPEthFVIW---GGEAAGIVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGsdiwskiqpvlsevpslqslvliDLA 166
Cdd:PRK05852 76 GSNAE--FVVAllaASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPH-----------------------DRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 167 ERVQGWRRIAARAmqrreckrlhgrAGVRGAVPRHVAIHDFDSAmsrESGDSLLIPRRFEADDISSYFcTGGTTGLPKIA 246
Cdd:PRK05852 131 EPTTRWWPLTVNV------------GGDSGPSGGTLSVHLDAAT---EPTPATSTPEGLRPDDAMIMF-TGGTTGLPKMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 247 IRRHGNEVANAWSVgqVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTpqgyRGDGVVKRFWEIVEHHRI 326
Cdd:PRK05852 195 PWTHANIASSVRAI--ITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPA----RGRFSAHTFWDDIKAVGA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 327 NFFSAVPTLYSALLDVP---VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGA-CVSSVNPPG---GE 399
Cdd:PRK05852 269 TWYTAVPTIHQILLERAatePSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThQVTTTQIEGigqTE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 400 RRLGSIGL--RIPGQMMKAVILDDagryvRDCVENEVGVLTISGPNVFAGYLQEDQNKSLwlDLGDGrqWLNTGDLARRD 477
Cdd:PRK05852 349 NPVVSTGLvgRSTGAQIRIVGSDG-----LPLPAGAVGEVWLRGTTVVRGYLGDPTITAA--NFTDG--WLRTGDLGSLS 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 478 AQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRgmig 557
Cdd:PRK05852 420 AAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCR---- 495
|
570 580
....*....|....*....|....*.
gi 1142773712 558 ERAA---IPKRIHIVDAMPLTAVGKI 580
Cdd:PRK05852 496 ERLAafeIPASFQEASGLPHTAKGSL 521
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
236-587 |
1.97e-35 |
|
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: 139.19 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIrrHGNEVANAWSVGQVVGAGMGPGKTVFCGlplfhVNAVLATGLVpFSRGAHVVLGTPQG-YRGDGVV 314
Cdd:cd05973 96 TSGTTGLPKGVP--VPLRALAAFGAYLRDAVDLRPEDSFWNA-----ADPGWAYGLY-YAITGPLALGHPTIlLEGGFSV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 315 KRFWEIVEHHRINFFSAVPTLYSALL--DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTE-GACVS 391
Cdd:cd05973 168 ESTWRVIERLGVTNLAGSPTAYRLLMaaGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGMVLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 392 SVNPPGGERRLGSIGLRIPGQmmKAVILDDAGRYVrdcVENEVGVLTISGPNV----FAGYLQEDQNKSlwldlgDGRqW 467
Cdd:cd05973 248 NHHALEHPVHAGSAGRAMPGW--RVAVLDDDGDEL---GPGEPGRLAIDIANSplmwFRGYQLPDTPAI------DGG-Y 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 468 LNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAG---ATAT 544
Cdd:cd05973 316 YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhegTPAL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1142773712 545 ETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05973 396 ADELQLHVKKRLSAH-AYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-592 |
4.57e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 139.82 E-value: 4.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 38 PSAPALSFFL--RADDHRKPL-----RWTYAALLRD-ITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVC 109
Cdd:PRK07867 2 SSAPTVAELLlpLAEDDDRGLyfedsFTSWREHIRGsAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 110 A-INPLLEGPAIASLLKAANAKVLVTLAPFPgsdiwskiqPVLSEVPSLQSLVLIDLAErvqgWRRIAAramqrreckrl 188
Cdd:PRK07867 82 VgLNPTRRGAALARDIAHADCQLVLTESAHA---------ELLDGLDPGVRVINVDSPA----WADELA----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 189 hgraGVRGAVPRhvaihdfdsamsresgdslliPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagM 268
Cdd:PRK07867 138 ----AHRDAEPP---------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFG--L 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 269 GPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALL---DVPVD 345
Cdd:PRK07867 191 GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIAL------RRKFSASGFLPDVRRYGATYANYVGKPLSYVLatpERPDD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 346 GRNIDSLEYGLCGAAPmpveVFRTFQDRTGVRILEGYGLTEGAcVSSVNPPGGerRLGSIGLRIP---------GQMMKA 416
Cdd:PRK07867 265 ADNPLRIVYGNEGAPG----DIARFARRFGCVVVDGFGSTEGG-VAITRTPDT--PPGALGPLPPgvaivdpdtGTECPP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 417 VILDDAGRYVRDCVENEVgvLTISGPNVFAGYLQEDQNKSLwlDLGDGRQWlnTGDLARRDAQGYFWLTGRRKELIIRGG 496
Cdd:PRK07867 338 AEDADGRLLNADEAIGEL--VNTAGPGGFEGYYNDPEADAE--RMRGGVYW--SGDLAYRDADGYAYFAGRLGDWMRVDG 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 497 HNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGM--IGERAAiPKRIHIVDAMPL 574
Cdd:PRK07867 412 ENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQW-PSYVRVCAELPR 490
|
570 580
....*....|....*....|
gi 1142773712 575 TAVGKIFKPELK--RWETFD 592
Cdd:PRK07867 491 TATFKVLKRQLSaeGVDCAD 510
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
226-587 |
4.61e-35 |
|
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: 137.95 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIrrHGNEVAnawsVGQVVGAGMgpgktVFCGLP----LFHVNA------VLATGLVPFS 295
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGAL--HAHRVL----LGHLPGVQF-----PFNLFPrdgdLYWTPAdwawigGLLDVLLPSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 296 -RGAHVVLGTPQGYRGdgvvKRFWEIVEHHRINFFSAVPTLYSALLDVPVD-GRNIDSLEYGLCGAAPMPVEVFRTFQDR 373
Cdd:cd05971 155 yFGVPVLAHRMTKFDP----KAALDLMSRYGVTTAFLPPTALKMMRQQGEQlKHAQVKLRAIATGGESLGEELLGWAREQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 374 TGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMKavILDDAGRYVRDCVENEVGVLTiSGPNVFAGYLQEDQ 453
Cdd:cd05971 231 FGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVA--IVDDNGTPLPPGEVGEIAVEL-PDPVAFLGYWNNPS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 454 NKSLWLdLGDgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVA 533
Cdd:cd05971 308 ATEKKM-AGD---WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKA 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 534 YVQLKAGATATET---ELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05971 384 FVVLNPGETPSDAlarEIQELVKTRLAAHEY-PREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
46-592 |
1.33e-33 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 136.16 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 46 FLRADDHRkplrWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEThFVIWGGEA-AGIVCA-INPLLEGPAIASL 123
Cdd:PRK08279 55 ALLFEDQS----ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEY-LAAWLGLAkLGAVVAlLNTQQRGAVLAHS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 124 LKAANAKVLVTlapfpGSDIWSKIQPVLSEVPSLQSLVLIDLAERVQ--GWRRIAARAMQRRECKRlhgraGVRGAVPrh 201
Cdd:PRK08279 130 LNLVDAKHLIV-----GEELVEAFEEARADLARPPRLWVAGGDTLDDpeGYEDLAAAAAGAPTTNP-----ASRSGVT-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 202 vaihdfdsamsresgdslliprrfeADDISSYFCTGGTTGLPKIAIRRHGNevANAWSVGQVVGAGMGPGKTVFCGLPLF 281
Cdd:PRK08279 198 -------------------------AKDTAFYIYTSGTTGLPKAAVMSHMR--WLKAMGGFGGLLRLTPDDVLYCCLPLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 282 HVNAVL-ATGLVpFSRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPV---DGRNidSLEYgLC 357
Cdd:PRK08279 251 HNTGGTvAWSSV-LAAGATLAL------RRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPkptDRDH--RLRL-MI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 358 GAAPMPvEVFRTFQDRTGV-RILEGYGLTEGAcVSSVNPPGgerRLGSIGlRIPGQMMK------------AVILDDAGR 424
Cdd:PRK08279 321 GNGLRP-DIWDEFQQRFGIpRILEFYAASEGN-VGFINVFN---FDGTVG-RVPLWLAHpyaivkydvdtgEPVRDADGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 425 YVRdCVENEVGVLT--ISGPNVFAGYL-QEDQNKSLWLD-LGDGRQWLNTGDLARRDAQGYFWL------TGRRKeliir 494
Cdd:PRK08279 395 CIK-VKPGEVGLLIgrITDRGPFDGYTdPEASEKKILRDvFKKGDAWFNTGDLMRDDGFGHAQFvdrlgdTFRWK----- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 495 gGHNIDPATIEEPLHRHPA--------VQIAAAIGRpdvhAGelpVAYVQLKAGAtatETELDTFIRGMIGE--RAAIPK 564
Cdd:PRK08279 469 -GENVATTEVENALSGFPGveeavvygVEVPGTDGR----AG---MAAIVLADGA---EFDLAALAAHLYERlpAYAVPL 537
|
570 580
....*....|....*....|....*...
gi 1142773712 565 RIHIVDAMPLTAVGKIFKPELKRwETFD 592
Cdd:PRK08279 538 FVRLVPELETTGTFKYRKVDLRK-EGFD 564
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
26-580 |
1.84e-32 |
|
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: 132.68 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 26 TYEMIGRGAAIDPSAPALSFflRADDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPET---------- 95
Cdd:cd05966 55 SYNCLDRHLKERGDKVAIIW--EGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELviamlacari 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 96 ---HFVIWGGEAAgivcainpllegPAIASLLKAANAKVLVTL-------APFPGSDIwskIQPVLSEVPSLQS-LVLID 164
Cdd:cd05966 133 gavHSVVFAGFSA------------ESLADRINDAQCKLVITAdggyrggKVIPLKEI---VDEALEKCPSVEKvLVVKR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 165 LAERVqgwrriaarAMQRreckrlhGRAgvrgavprhvaiHDFDSAMSRESGDSLliPRRFEADDISSYFCTGGTTGLPK 244
Cdd:cd05966 198 TGGEV---------PMTE-------GRD------------LWWHDLMAKQSPECE--PEWMDSEDPLFILYTSGSTGKPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 245 IAIRRHGnevanawsvGQVVGAGMgPGKTVF-------------CGLPLFHVNAVLAtglvPFSRGAHVVL--GTPQgYR 309
Cdd:cd05966 248 GVVHTTG---------GYLLYAAT-TFKYVFdyhpddiywctadIGWITGHSYIVYG----PLANGATTVMfeGTPT-YP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 310 GDGvvkRFWEIVEHHRINFFSAVPTLYSALL---DVPVDGRNIDSLEygLCGAA--PMPVEVFRTFQDRTG---VRILEG 381
Cdd:cd05966 313 DPG---RYWDIVEKHKVTIFYTAPTAIRALMkfgDEWVKKHDLSSLR--VLGSVgePINPEAWMWYYEVIGkerCPIVDT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTE--GACVSSVnPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVrdcvENEV-GVLTISGPnvFAGYLQedqnkSLW 458
Cdd:cd05966 388 WWQTEtgGIMITPL-PGATPLKPGSATRPFFG--IEPAILDEEGNEV----EGEVeGYLVIKRP--WPGMAR-----TIY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 459 ldlGDGRQWLNT-----------GDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHA 527
Cdd:cd05966 454 ---GDHERYEDTyfskfpgyyftGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 528 GELPVAYVQLKAGATAT---ETELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKI 580
Cdd:cd05966 531 GEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIAT-PDKIQFVPGLPKTRSGKI 585
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
228-587 |
2.68e-32 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 131.89 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVAnawSVGQVVG------AGMGPGKTVFCGLPLFHVN--AVLATGLVpfSRGAH 299
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIA---MVELFVRfeasqyEYPGSDNVYLAALPMFHIYglSLFVVGLL--SLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 300 VVlgtpqgyrgdgVVKRF-----WEIVEHHRINFFSAVPTLYSALLDV--PVDGRNIDSLEYGLCGAAPMPVEVFRTF-Q 371
Cdd:PLN02574 273 IV-----------VMRRFdasdmVKVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQ 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTEGACVSS--VNPPGgERRLGSIGLRIPGqmMKAVILD-DAGRYVRdcvENEVGVLTISGPNVFAGY 448
Cdd:PLN02574 342 TLPHVDFIQGYGMTESTAVGTrgFNTEK-LSKYSSVGLLAPN--MQAKVVDwSTGCLLP---PGNCGELWIQGPGVMKGY 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 449 LQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAG 528
Cdd:PLN02574 416 LNNPKATQSTID-KDG--WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773712 529 ELPVAYVQLKAGATATETELDTFIRGMIGERAAIPKRIhIVDAMPLTAVGKIFKPELKR 587
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVV-FVQSIPKSPAGKILRRELKR 550
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
236-580 |
4.78e-32 |
|
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: 126.75 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHgnevaNAWSVGQVvgagmgpgktvfCGLPLFHV---NAVLATGLVPFS---RGAHVVLGTPQGYR 309
Cdd:cd17633 8 TSGTTGLPKAYYRSE-----RSWIESFV------------CNEDLFNIsgeDAILAPGPLSHSlflYGAISALYLGGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 310 GDG--VVKRFWEIVEHHRINFFSAVPTLYSALLDVpvdGRNIDSLEYGLCGAAPMPVEVFRTFQDRT-GVRILEGYGLTE 386
Cdd:cd17633 71 GQRkfNPKSWIRKINQYNATVIYLVPTMLQALART---LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 GACVSsVNPPGGERRLGSIGLRIPGQMMkavilddagrYVRDCVENEVGVLTISGPNVFAGYLQEDQNKSlwldlgDGrq 466
Cdd:cd17633 148 LSFIT-YNFNQESRPPNSVGRPFPNVEI----------EIRNADGGEIGKIFVKSEMVFSGYVRGGFSNP------DG-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQlkaGATATET 546
Cdd:cd17633 209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYK 285
|
330 340 350
....*....|....*....|....*....|....
gi 1142773712 547 ELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17633 286 QLKRFLKQKL-SRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
59-586 |
6.06e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 130.13 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGI-VCAINPLLEGPAIASLLKAANAKVLVTLAP 137
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLyITAINHHLTAPEADYIVGDSGARVLVASAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 138 FPGsdiwskiqpVLSEVPSlqslvliDLAERVQGWRRIAARAmqrreckrlhgragvrgavprhvaihDFDSAMSRESgd 217
Cdd:PRK13390 106 LDG---------LAAKVGA-------DLPLRLSFGGEIDGFG--------------------------SFEAALAGAG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 218 slliPRRFEADDISSYFCTGGTTGLPK-IAIRRHGNEV-ANAWSVGQVVGA--GMGPGKTVFCGLPLFHVNAVLATGLVp 293
Cdd:PRK13390 142 ----PRLTEQPCGAVMLYSSGTTGFPKgIQPDLPGRDVdAPGDPIVAIARAfyDISESDIYYSSAPIYHAAPLRWCSMV- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 294 FSRGAHVVLGtpqgyrgdgvvKRF-----WEIVEHHRINFFSAVPTLYSALLDVPVDGR---NIDSLEYGLCGAAPMPVE 365
Cdd:PRK13390 217 HALGGTVVLA-----------KRFdaqatLGHVERYRITVTQMVPTMFVRLLKLDADVRtryDVSSLRAVIHAAAPCPVD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 366 VFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMkavILDDAGRyvrDCVENEVGVLTISGPNVF 445
Cdd:PRK13390 286 VKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGDLH---ICDDDGN---ELPAGRIGTVYFERDRLP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 446 AGYLQeDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDV 525
Cdd:PRK13390 360 FRYLN-DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 526 HAGELPVAYVQLKAGATATET---ELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK13390 439 EMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKA-PRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-582 |
6.28e-32 |
|
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: 131.07 E-value: 6.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALSFFLRADDHRKPLRW----------TYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWG 101
Cdd:cd05968 56 VGGRMNIVEQLLDKWLADTRTRPALRWegedgtsrtlTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 102 GEAAGIVcaINPLLEG---PAIASLLKAANAKVLVTLAPFPGSDiwskiqpvlsevpslqslVLIDLAERVqgwrRIAAR 178
Cdd:cd05968 136 VARIGGI--VVPIFSGfgkEAAATRLQDAEAKALITADGFTRRG------------------REVNLKEEA----DKACA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 179 AMQRRECKRLHGRAGVrgAVPRHVAiHDFDSAMSRESGDSLLipRRFEADDISSYFCTGGTTGLPKIAIRRHGN------ 252
Cdd:cd05968 192 QCPTVEKVVVVRHLGN--DFTPAKG-RDLSYDEEKETAGDGA--ERTESEDPLMIIYTSGTTGKPKGTVHVHAGfplkaa 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 253 -EVANAWSVGQV--------VGAGMGPGkTVFCGLPLfhvnavlatglvpfsrGAHVVLgtPQGYRGDGVVKRFWEIVEH 323
Cdd:cd05968 267 qDMYFQFDLKPGdlltwftdLGWMMGPW-LIFGGLIL----------------GATMVL--YDGAPDHPKADRLWRMVED 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 324 HRINFFSAVPTLYSALL---DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTG---VRILEGYGLTEGACVSSVNPPG 397
Cdd:cd05968 328 HEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGkgrNPIINYSGGTEISGGILGNVLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 398 GERRLGSIGLRIPGqmMKAVILDDAGRYVRDcvenEVGVLTISGPNVfagylqeDQNKSLWldlGDGRQWLNT------- 470
Cdd:cd05968 408 KPIKPSSFNGPVPG--MKADVLDESGKPARP----EVGELVLLAPWP-------GMTRGFW---RDEDRYLETywsrfdn 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 471 ----GDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:cd05968 472 vwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 1142773712 547 ---ELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFK 582
Cdd:cd05968 552 laeELMERVADELG-KPLSPERILFVKDLPKTRNAKVMR 589
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
70-602 |
1.17e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 130.14 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 70 AANMFSrLGIDRHAVVAYVLPNLP---ETHFVIwgGEAAGIVCAINPLLEGPAIASLLKAANAKVLvtlapFPGSDIWSK 146
Cdd:PLN03102 53 AASLIS-LNITKNDVVSVLAPNTPamyEMHFAV--PMAGAVLNPINTRLDATSIAAILRHAKPKIL-----FVDRSFEPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 147 IQPVLSEVPSLQSlvlidlaervqgwrriaaramqrreckRLHgragvrgavPRHVAIHDFDSAMSRESGDS-------- 218
Cdd:PLN03102 125 AREVLHLLSSEDS---------------------------NLN---------LPVIFIHEIDFPKRPSSEELdyecliqr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 219 -----LLIPRRF----EADDISSYFcTGGTTGLPKIAIRRHGNEVANAWSVgqVVGAGMGPGKTVFCGLPLFHVNAVLAT 289
Cdd:PLN03102 169 geptpSLVARMFriqdEHDPISLNY-TSGTTADPKGVVISHRGAYLSTLSA--IIGWEMGTCPVYLWTLPMFHCNGWTFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 290 GLVPFSRGAHVVL---GTPQGYRGdgvvkrfweiVEHHRINFFSAVPTLYSALLDvpvdGRNID-SLEYG----LCGAAP 361
Cdd:PLN03102 246 WGTAARGGTSVCMrhvTAPEIYKN----------IEMHNVTHMCCVPTVFNILLK----GNSLDlSPRSGpvhvLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 362 MPVEVFRTFQdRTGVRILEGYGLTEGA-----CVSSVN----PPGGERRLGS-IGLRIPGQMMKAVILDDAGRYV-RDcv 430
Cdd:PLN03102 312 PPAALVKKVQ-RLGFQVMHAYGLTEATgpvlfCEWQDEwnrlPENQQMELKArQGVSILGLADVDVKNKETQESVpRD-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 431 ENEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHR 510
Cdd:PLN03102 389 GKTMGEIVIKGSSIMKGYLKNPKATSEAFKHG----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 511 HPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIrgmIGERAAI------------PKRIHIVDAMPLTAVG 578
Cdd:PLN03102 465 YPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLV---TRERDLIeycrenlphfmcPRKVVFLQELPKNGNG 541
|
570 580
....*....|....*....|....
gi 1142773712 579 KIFKPELKrwETFDALVSALKDAG 602
Cdd:PLN03102 542 KILKPKLR--DIAKGLVVEDEDNV 563
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
376-588 |
1.79e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 125.28 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 376 VRILEGYGLTEGACVSSVNPPGGERRLGSIGLriPGQMMKAVILDDAGRyvrDCVENEVGVLTISGPNVFAGYLqedqNK 455
Cdd:PRK07638 280 AKLYEFYGASELSFVTALVDEESERRPNSVGR--PFHNVQVRICNEAGE---EVQKGEIGTVYVKSPQFFMGYI----IG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 456 SLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYV 535
Cdd:PRK07638 351 GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 536 QlkagATATETELDTFIRGMIgerAA--IPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK07638 431 K----GSATKQQLKSFCLQRL---SSfkIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
226-516 |
3.36e-30 |
|
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: 124.09 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGT- 304
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG--KGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDk 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 305 --------PQGYRGD--GVVKRFWEIvEHHRINffSAVPTLYSA----LLDVPVDGRNIDSL-------------EYGLC 357
Cdd:cd05914 165 ipsakiiaLAFAQVTptLGVPVPLVI-EKIFKM--DIIPKLTLKkfkfKLAKKINNRKIRKLafkkvheafggniKEFVI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 358 GAAPMPVEVFRTFQdRTGVRILEGYGLTEGACVSSVNPPGgERRLGSIGLRIPGqmMKAVILDDAGryvrdcvENEVGVL 437
Cdd:cd05914 242 GGAKINPDVEEFLR-TIGFPYTIGYGMTETAPIISYSPPN-RIRLGSAGKVIDG--VEVRIDSPDP-------ATGEGEI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 438 TISGPNVFAGYLQEDQNKSLWLDLgDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRG-GHNIDPATIEEPLHRHPAVQI 516
Cdd:cd05914 311 IVRGPNVMKGYYKNPEATAEAFDK-DG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLE 387
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
48-617 |
3.53e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 125.14 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 48 RADDHRKPLR-----WTYAALLRD-ITRAANMFSRLGIDRHAVVAYVLPNLPEthFVIWGGEAA---GIVCAINPLLEGP 118
Cdd:PRK13388 12 RAGDDTIAVRygdrtWTWREVLAEaAARAAALIALADPDRPLHVGVLLGNTPE--MLFWLAAAAlggYVLVGLNTTRRGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 119 AIASLLKAANAKVLVT----LAPFPGSDiwskiqpvLSEVPslqsLVLIDLAErvqgWRRIAARAmqrreckrlhgragv 194
Cdd:PRK13388 90 ALAADIRRADCQLLVTdaehRPLLDGLD--------LPGVR----VLDVDTPA----YAELVAAA--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 195 rGAVPRHVAIhdfdsamsresgdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSvgQVVGAGMGPGKTV 274
Cdd:PRK13388 139 -GALTPHREV---------------------DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA--LTERFGLTRDDVC 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 275 FCGLPLFHVNAVLATGLVPFSRGAHVVLG---TPQGYRGDgvVKRFweivehhRINFFSAVPTLYSALL---DVPVDGRN 348
Cdd:PRK13388 195 YVSMPLFHSNAVMAGWAPAVASGAAVALPakfSASGFLDD--VRRY-------GATYFNYVGKPLAYILatpERPDDADN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 349 IDSLEYGlCGAAPmpvEVFRTFQDRTGVRILEGYGLTEGAcVSSVNPPGGERrlGSIGLRIPG---------QMMKAVIL 419
Cdd:PRK13388 266 PLRVAFG-NEASP---RDIAEFSRRFGCQVEDGYGSSEGA-VIVVREPGTPP--GSIGRGAPGvaiynpetlTECAVARF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 420 DDAGRYVRdcVENEVGVLT-ISGPNVFAGYLQEDQNKSlwLDLGDGRQWlnTGDLARRDAQGYFWLTGRRKELIIRGGHN 498
Cdd:PRK13388 339 DAHGALLN--ADEAIGELVnTAGAGFFEGYYNNPEATA--ERMRHGMYW--SGDLAYRDADGWIYFAGRTADWMRVDGEN 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 499 IDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGM--IGERAAiPKRIHIVDAMPLTA 576
Cdd:PRK13388 413 LSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAW-PRYVRIAADLPSTA 491
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1142773712 577 VGKIFKPEL--KRWETFDALVSAlkdAGVEGARVSMVDDPSRG 617
Cdd:PRK13388 492 TNKVLKRELiaQGWATGDPVTLW---VRRGGPAYRLMSEPAKA 531
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
228-521 |
4.04e-30 |
|
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: 124.01 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVpFSRGAHVVLGTPQG 307
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ--PGDRFLSILPIWHSYERSAEYFI-FACGCSQAYTSIRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 308 YRGD---------GVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIdslEYGLCGAAPMPVEVfRTFQDRTGVRI 378
Cdd:cd17640 165 LKDDlkrvkphyiVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIF---KFGISGGGALPPHV-DTFFEAIGIEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 379 LEGYGLTEGACVSSVNPPGGERRlGSIGLRIPGQMMKavILDDAGRYVRDcvENEVGVLTISGPNVFAGYLQEDQNKSLW 458
Cdd:cd17640 241 LNGYGLTETSPVVSARRLKCNVR-GSVGRPLPGTEIK--IVDPEGNVVLP--PGEKGIVWVRGPQVMKGYYKNPEATSKV 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 459 LDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELII-RGGHNIDPATIEEPLHRHPAVQIAAAIG 521
Cdd:cd17640 316 LD-SDG--WFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
53-554 |
1.08e-29 |
|
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: 123.35 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 53 RKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPE---THFVIWggEAAGIVCAINPLLEGPAIASLLKAANA 129
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEwfiTDLAIW--MAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 130 KVLvtlapFPGS-DIWSKIQPVLSEVPSLQSLVLIDLAERVQGWRRIAARAmqrreckrlhgrAGVRGAVPRhvaihdfd 208
Cdd:cd05932 80 KAL-----FVGKlDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQH------------PPLEERPTR-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 209 samsresgdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGNevaNAWSVGQVVGA-GMGPGKTVFCGLPLFHVNAVL 287
Cdd:cd05932 135 -----------------FPEQLATLIYTSGTTGQPKGVMLTFGS---FAWAAQAGIEHiGTEENDRMLSYLPLAHVTERV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 288 ATGLVPFSRGahVVLGTPQGyrgdgvVKRFWEIVEHHRINFFSAVPTLYSA----------------LLDVPV------- 344
Cdd:cd05932 195 FVEGGSLYGG--VLVAFAES------LDTFVEDVQRARPTLFFSVPRLWTKfqqgvqdkipqqklnlLLKIPVvnslvkr 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 ---DGRNIDSLEYGLCGAAPMPVEVFRTFQdRTGVRILEGYGLTEGACVSSVNPPGgERRLGSIGLRIPGQMMKavILDD 421
Cdd:cd05932 267 kvlKGLGLDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPG-RDKIGTVGNAGPGVEVR--ISED 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 422 agryvrdcvenevGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKELI-IRGGHNID 500
Cdd:cd05932 343 -------------GEILVRSPALMMGYYKDPEATAEAFT-ADG--FLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVA 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 501 PATIEEPLHRHPAVQIAAAIGRPDVHagelPVAYVQLKAGATAtetELDTFIRG 554
Cdd:cd05932 407 PAPIENKLAEHDRVEMVCVIGSGLPA----PLALVVLSEEARL---RADAFARA 453
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
236-587 |
2.32e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 122.73 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVAnawSVGQVVGA-GMGPGKTVFCGLPLFH----VNAVLATGLvpfsrGAHVVLgtpqgyrg 310
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLA---PLAGLLSRvPFRAGETTLLPAPMFHatgwAHLTLAMAL-----GSTVVL-------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 311 dgvVKRF-----WEIVEHHRINFFSAVPTLYSALLDVPVDGRN---IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGY 382
Cdd:PRK07788 279 ---RRRFdpeatLEDIAKHKATALVVVPVMLSRILDLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAFGPVLYNLY 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYLqedqnkslwldlg 462
Cdd:PRK07788 356 GSTEVAFATIATPEDLAEAPGTVGRPPKG--VTVKILDENGNEVP---RGVVGRIFVGNGFPFEGYT------------- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 463 DGRQ------WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQ 536
Cdd:PRK07788 418 DGRDkqiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 537 LKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK07788 498 KAPGAALDEDAIKDYVRDNLA-RYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
236-580 |
1.08e-28 |
|
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: 119.70 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKT-VFCGLPLFHVnAVLATgLVPFSRGAHVVLGTPQGYRGDGVV 314
Cdd:cd12116 134 TSGSTGRPKGVVVSHRNLVNFLHSMRERLG--LGPGDRlLAVTTYAFDI-SLLEL-LLPLLAGARVVIAPRETQRDPEAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 315 KRFweiVEHHRINFFSAVPTLYSALLDVpvDGRNIDSLEyGLCGAAPMPVEVFRTFQDRTGvRILEGYGLTEGACVSSVN 394
Cdd:cd12116 210 ARL---IEAHSITVMQATPATWRMLLDA--GWQGRAGLT-ALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIWSTAA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 395 PPGGERRLGSIGLRIPGqmMKAVILDDAGRYVrdcVENEVGVLTISGPNVFAGYLQEDQ--NKSLWLD--LGDGRQWLNT 470
Cdd:cd12116 283 RVTAAAGPIPIGRPLAN--TQVYVLDAALRPV---PPGVPGELYIGGDGVAQGYLGRPAltAERFVPDpfAGPGSRLYRT 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 471 GDLARRDAQGYFWLTGRRKELI-IRgGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELpVAYVQLKAGATATETELD 549
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALR 435
|
330 340 350
....*....|....*....|....*....|.
gi 1142773712 550 TFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd12116 436 AHLRATLPA-YMVPSAFVRLDALPLTANGKL 465
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
229-580 |
4.33e-28 |
|
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: 115.82 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 229 DISSYFCTGGTTGLPKIAIRRHGNEVAnAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGY 308
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFA-VPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 309 rgdgvvKRFWEIVEHHRINFFSAVPTLYSALLDVPVDG----RNIDSLEYGlcGAAPMPVEVfRTFQDRTGVRILEGYGL 384
Cdd:cd17635 81 ------KSLFKILTTNAVTTTCLVPTLLSKLVSELKSAnatvPSLRLIGYG--GSRAIAADV-RFIEATGLTNTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 385 TEGACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDDAgryvrDCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdg 464
Cdd:cd17635 152 SETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGI-----AGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 465 rqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqlkagaTAT 544
Cdd:cd17635 225 --WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV------VAS 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1142773712 545 ETELDTFIRGMI------GERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17635 297 AELDENAIRALKhtirreLEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
236-580 |
7.17e-28 |
|
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: 117.76 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPK-IAIRRHGneVAN--AWSVGQVvgaGMGPGKTVFCGLPL-FHVNavLATGLVPFSRGAHVVLGTPQGYRGD 311
Cdd:cd17646 146 TSGSTGRPKgVMVTHAG--IVNrlLWMQDEY---PLGPGDRVLQKTPLsFDVS--VWELFWPLVAGARLVVARPGGHRDP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 312 GVVKRFweiVEHHRINFFSAVPTLYSALLDVPVDGRnIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGAC-V 390
Cdd:cd17646 219 AYLAAL---IREHGVTTCHFVPSMLRVFLAEPAAGS-CASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 391 SS--VNPPGGERRLgSIGLRIPGqmMKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYL-QEDQNKSLWLD--LGDGR 465
Cdd:cd17646 295 THwpVRGPAETPSV-PIGRPVPN--TRLYVLDDALRPVPVGV---PGELYLGGVQLARGYLgRPALTAERFVPdpFGPGS 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 466 QWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE 545
Cdd:cd17646 369 RMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD 448
|
330 340 350
....*....|....*....|....*....|....*.
gi 1142773712 546 T-ELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17646 449 TaALRAHLAERLPE-YMVPAAFVVLDALPLTANGKL 483
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
319-587 |
7.27e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 118.32 E-value: 7.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 319 EIVEHHRINFFSAVPTLYSALLDVPVDGRN---IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNP 395
Cdd:PRK13382 278 DLIDRHRATGLAVVPVMFDRIMDLPAEVRNrysGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 396 PGGERRLGSIGLRIPGQMMKavILDDAGRyvrDCVENEVGVLTISGPNVFAGYlQEDQNKslwlDLGDGrqWLNTGDLAR 475
Cdd:PRK13382 358 ADLRAAPDTAGRPAEGTEIR--ILDQDFR---EVPTGEVGTIFVRNDTQFDGY-TSGSTK----DFHDG--FMASGDVGY 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 476 RDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGM 555
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN 505
|
250 260 270
....*....|....*....|....*....|..
gi 1142773712 556 IGeRAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK13382 506 LA-NYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
55-586 |
9.52e-28 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 118.02 E-value: 9.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 55 PLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLP---ETHFviwGGEAAG-IVCAINPLLEGPAIASLLKAANAK 130
Cdd:PLN02479 43 SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPamyEAHF---GVPMAGaVVNCVNIRLNAPTIAFLLEHSKSE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 131 VL-VTLAPFPGSD----IWSKiqpvlSEVPSLQSLVLIdlaerVQGWRRIAARAMQRreckrlhgrAGVRGAVprhvaih 205
Cdd:PLN02479 120 VVmVDQEFFTLAEealkILAE-----KKKSSFKPPLLI-----VIGDPTCDPKSLQY---------ALGKGAI------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 206 DFDSAMsrESGDSLLI--PRRFEADDISSYFcTGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHV 283
Cdd:PLN02479 174 EYEKFL--ETGDPEFAwkPPADEWQSIALGY-TSGTTASPKGVVLHHRGAYLMALSNALI--WGMNEGAVYLWTLPMFHC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 284 NAVLatglvpFSRGAHVVLGTPQGYRgDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNI---DSLEYGLCGAA 360
Cdd:PLN02479 249 NGWC------FTWTLAALCGTNICLR-QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILplpRVVHVMTAGAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 361 PMPVEVFRTFQdrTGVRILEGYGLTEGACVSSVN---------PPGGERRLGS------IGLR----IPGQMMKAVILDD 421
Cdd:PLN02479 322 PPPSVLFAMSE--KGFRVTHTYGLSETYGPSTVCawkpewdslPPEEQARLNArqgvryIGLEgldvVDTKTMKPVPADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 422 AgryvrdcvenEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDP 501
Cdd:PLN02479 400 K----------TMGEIVMRGNMVMKGYLKNPKANEEAFANG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 502 ATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGA-----TATETELDTFIRgmigERAA---IPKRIhIVDAMP 573
Cdd:PLN02479 466 LEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVdksdeAALAEDIMKFCR----ERLPaywVPKSV-VFGPLP 540
|
570
....*....|...
gi 1142773712 574 LTAVGKIFKPELK 586
Cdd:PLN02479 541 KTATGKIQKHVLR 553
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
236-580 |
3.35e-27 |
|
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: 115.04 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPK-IAIRrHGNEVA-NAWSVGQvvgAGMGPGKtVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGYRGdgv 313
Cdd:cd05945 105 TSGSTGRPKgVQIS-HDNLVSfTNWMLSD---FPLGPGD-VFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATAD--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 314 VKRFWEIVEHHRINFFSAVPTLYS-ALLDVPVDGRNIDSLEYGL-CGAaPMPVEVFRTFQDRT-GVRILEGYGLTE--GA 388
Cdd:cd05945 177 PKQLFRFLAEHGITVWVSTPSFAAmCLLSPTFTPESLPSLRHFLfCGE-VLPHKTARALQQRFpDARIYNTYGPTEatVA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 389 CVSSV---NPPGGERRLgSIGLRIPGqmMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYL--QEDQNKSLWLDlgD 463
Cdd:cd05945 256 VTYIEvtpEVLDGYDRL-PIGYAKPG--AKLVILDEDGRPVP---PGEKGELVISGPSVSKGYLnnPEKTAAAFFPD--E 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 464 GRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATA 543
Cdd:cd05945 328 GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA 407
|
330 340 350
....*....|....*....|....*....|....*...
gi 1142773712 544 TET-ELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05945 408 GLTkAIKAELAERLPP-YMIPRRFVYLDELPLNANGKI 444
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
225-580 |
4.48e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 117.72 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 225 FEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMgpgKTVFCG-LPLFHVNAVLATGLVPFSRGAHVVLg 303
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRN---DDVILSsLPFFHSFGLTVTLWLPLLEGIKVVY- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 304 TPQGYRGDGVVKrfweIVEHHRINFFSAVPTLYSALLDVP-VDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGY 382
Cdd:PRK08633 855 HPDPTDALGIAK----LVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEGACVSSVNPPGGER---------RLGSIGLRIPGQMMKavILD-DAGryvRDCVENEVGVLTISGPNVFAGYL-QE 451
Cdd:PRK08633 931 GATETSPVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVR--IVDpETF---EELPPGEDGLILIGGPQVMKGYLgDP 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 452 DQNKSLWLDLgDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHR--HPAVQIAAAIGRPDVHAGE 529
Cdd:PRK08633 1006 EKTAEVIKDI-DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE 1084
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 530 LPVAYVQLKAGATATeteldtfIRGMIGE----RAAIPKRIHIVDAMPLTAVGKI 580
Cdd:PRK08633 1085 KLVVLHTCGAEDVEE-------LKRAIKEsglpNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
227-588 |
5.70e-27 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 117.37 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVL-GTP 305
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFS--PEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLyPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QGYRgdgvvkrfweivehhrinffsAVPTL------------------YSALLDvPVDGRnidSLEYGLCGAAPMPVEVF 367
Cdd:PRK06814 870 LHYR---------------------IIPELiydtnatilfgtdtflngYARYAH-PYDFR---SLRYVFAGAEKVKEETR 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 368 RTFQDRTGVRILEGYGLTEGACVSSVNPPgGERRLGSIGLRIPGqmMKAVILDDAGRyvrdcveNEVGVLTISGPNVFAG 447
Cdd:PRK06814 925 QTWMEKFGIRILEGYGVTETAPVIALNTP-MHNKAGTVGRLLPG--IEYRLEPVPGI-------DEGGRLFVRGPNVMLG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 448 YLQEDQNKSLwLDLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHA 527
Cdd:PRK06814 995 YLRAENPGVL-EPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARK 1071
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 528 GElpvAYVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK06814 1072 GE---RIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
227-579 |
8.78e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 112.48 E-value: 8.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDIssY-FCTGGTTGLPKIAIRRHGN------------EVANAWSVGQVVGAGMGPGKTVFCGLPLFHvNAVLATGLVP 293
Cdd:cd05924 3 ADDL--YiLYTGGTTGMPKGVMWRQEDifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMH-GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 294 FSRGAHVVLGTPqGYRGDGVvkrfWEIVEHHRINFFSAVPTLYSA-LLDVPVDGRNID--SLEYGLCGAAPMPVEVFRTF 370
Cdd:cd05924 80 LLGGQTVVLPDD-RFDPEEV----WRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDlsSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 371 QDRT-GVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGqmmkAVILDDAGRYVRDCVEnEVGVLTISGpNVFAGYL 449
Cdd:cd05924 155 LELVpNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPD----TVVLDDDGRVVPPGSG-GVGWIARRG-HIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 450 QEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGE 529
Cdd:cd05924 229 GDEAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1142773712 530 LPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGK 579
Cdd:cd05924 309 EVVAVVQLREGAGVDLEELREHCRTRIA-RYKLPKQVVFVDEIERSPAGK 357
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
21-588 |
1.21e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 114.32 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 21 DLPAStyEMIGRGAaiDPSAPALsfflrADDHRkplRWTYAALLRDITRAANMFSRLGIDRH--AVVAyvLPNLPETHFV 98
Cdd:PRK10946 24 DLPLT--DILTRHA--ASDAIAV-----ICGER---QFSYRELNQASDNLACSLRRQGIKPGdtALVQ--LGNVAEFYIT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 99 IWGGEAAGIVcAINPL-----LEGPAIA-----SLLKAANAKVLvtlapFPGSDIwskIQPVLSEVPSLQSLVLidlaer 168
Cdd:PRK10946 90 FFALLKLGVA-PVNALfshqrSELNAYAsqiepALLIADRQHAL-----FSDDDF---LNTLVAEHSSLRVVLL------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 169 vqgwrriaaramqrreckrlHGRAGvrgavprhvaIHDFDSAMSRESGDSLLIPRRfeADDISSYFCTGGTTGLPKIAIR 248
Cdd:PRK10946 155 --------------------LNDDG----------EHSLDDAINHPAEDFTATPSP--ADEVAFFQLSGGSTGTPKLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 249 RHGNEVanaWSV-GQVVGAGMGPGKTVFCGLPLFHVNAVLATG-LVPFSRGAHVVLGTpqgyrgDGVVKRFWEIVEHHRI 326
Cdd:PRK10946 203 THNDYY---YSVrRSVEICGFTPQTRYLCALPAAHNYPMSSPGaLGVFLAGGTVVLAP------DPSATLCFPLIEKHQV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 327 NFFSAVP---TLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGAcvssVN------PPg 397
Cdd:PRK10946 274 NVTALVPpavSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL----VNytrlddSD- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 398 gERRLGSIGLRI-PGQMMKavILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGDLARR 476
Cdd:PRK10946 349 -ERIFTTQGRPMsPDDEVW--VADADGNPLPQ---GEVGRLMTRGPYTFRGYYKSPQHNASAFD-ANG--FYCSGDLVSI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 477 DAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATAteTELDTFIRGMI 556
Cdd:PRK10946 420 DPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA--VQLRRFLREQG 497
|
570 580 590
....*....|....*....|....*....|..
gi 1142773712 557 GERAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK10946 498 IAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
57-579 |
1.48e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 114.21 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGI---DRHAVVAYVLPNLPETHFVIWGGEAAGIvcAINPLLEGPAIASLLKAANAKVLV 133
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLgpgDHVGIYARNRIEYVEAMLGAFKARAVPV--NVNYRYVEDELRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 134 ---TLAPfpgsdiwsKIQPVLSEVPSLQSLVLIDLAErvqgwrriaaramqrreckrlhGRAGVRGAVprhvaihDFDSA 210
Cdd:PRK07798 106 yerEFAP--------RVAEVLPRLPKLRTLVVVEDGS----------------------GNDLLPGAV-------DYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 211 MSRESGDSLLIPRrfEADDIssYF-CTGGTTGLPKIAIRRH---------------GNEVANAWSVGQVVGAGMGPgkTV 274
Cdd:PRK07798 149 LAAGSPERDFGER--SPDDL--YLlYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGM--RR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 275 FCGLPLFHVNAVLATGLVPFSrGAHVVLGTPQGYRGDGVvkrfWEIVEHHRINFFSAVPTLYSA-LLDVPVDGRNID--S 351
Cdd:PRK07798 223 FPAPPLMHGAGQWAAFAALFS-GQTVVLLPDVRFDADEV----WRTIEREKVNVITIVGDAMARpLLDALEARGPYDlsS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 352 LEYGLCGAAPMPVEVFRTFQDR-TGVRILEGYGLTE-GACVSSVNPPGGERRLGS---IGLRipgqmmkAVILDDAGRYV 426
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSEtGFGGSGTVAKGAVHTGGPrftIGPR-------TVVLDEDGNPV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 427 RDCvENEVGVLTISGPnVFAGYLQEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEE 506
Cdd:PRK07798 371 EPG-SGEIGWIARRGH-IPLGYYKDPEKTAETFPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 507 PLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGK 579
Cdd:PRK07798 449 ALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLA-GYKVPRAIWFVDEVQRSPAGK 520
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
59-519 |
1.67e-26 |
|
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: 112.36 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 59 TYAALLRDITR-AANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIV-CAINPllEGPA--IASLLKAANAKVLVT 134
Cdd:TIGR01733 1 TYRELDERANRlARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAyVPLDP--AYPAerLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 135 LAPFpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhgRAGVRGAVPRHVAIHDFDSAMSRE 214
Cdd:TIGR01733 79 DSAL----------------------------------------------------ASRLAGLVLPVILLDPLELAALDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 215 SGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHVNAVLATgLVPF 294
Cdd:TIGR01733 107 APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR--YGLDPDDRVLQFASLSFDASVEEI-FGAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 295 SRGAHVVLGTPQGYRGDGVVKRFWeiVEHHRINFFSAVPTLYSALLdvPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRT 374
Cdd:TIGR01733 184 LAGATLVVPPEDEERDDAALLAAL--IAEHPVTVLNLTPSLLALLA--AALPPALASLRLVILGGEALTPALVDRWRARG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 G-VRILEGYGLTEGACVSSVN--PPGGERRLGS--IGLRIPGqmMKAVILDDAGRyvrDCVENEVGVLTISGPNVFAGYL 449
Cdd:TIGR01733 260 PgARLINLYGPTETTVWSTATlvDPDDAPRESPvpIGRPLAN--TRLYVLDDDLR---PVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 450 -QEDQNK----SLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAA 519
Cdd:TIGR01733 335 nRPELTAerfvPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
226-529 |
2.73e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 113.55 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWsvGQVVGAGMGPGKTVFCG-LPLFHVNAVLATGLVPFSRGAHVVLGT 304
Cdd:PRK07768 150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAE--AMFVAAEFDVETDVMVSwLPLFHDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 305 PQGYRGDGVVkrfW-EIVEHHRINFFSAVPTLYSAL---LDVPVDGRNID--SLEYGLCGAAPMPVEVFRTFQD---RTG 375
Cdd:PRK07768 228 PMDFLRDPLL---WaELISKYRGTMTAAPNFAYALLarrLRRQAKPGAFDlsSLRFALNGAEPIDPADVEDLLDagaRFG 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 376 VR---ILEGYGLTE------------GACVSSVNP-------------PGGERRLGSIGLRIPGqmMKAVILDDAGRYvr 427
Cdd:PRK07768 305 LRpeaILPAYGMAEatlavsfspcgaGLVVDEVDAdllaalrravpatKGNTRRLATLGPPLPG--LEVRVVDEDGQV-- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 428 dCVENEVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEP 507
Cdd:PRK07768 381 -LPPRGVGVIELRGESVTPGYLTMDGFIPAQDADG----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
330 340
....*....|....*....|....
gi 1142773712 508 LHRHPAVQI--AAAIGRPDVHAGE 529
Cdd:PRK07768 456 AARVEGVRPgnAVAVRLDAGHSRE 479
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
27-580 |
5.87e-26 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 113.12 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 27 YEMIGRGAAIDPSAPALSFFLRADDHRKplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHF--------- 97
Cdd:PRK10524 56 HNAVDRHLAKRPEQLALIAVSTETDEER--TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFamlacarig 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 98 ----VIWGGEAAGivcainpllegpAIASLLKAANAKVLVTlapfpgSDIWSKIQPVLSEVPSLQSLvlIDLAErvqgwr 173
Cdd:PRK10524 134 aihsVVFGGFASH------------SLAARIDDAKPVLIVS------ADAGSRGGKVVPYKPLLDEA--IALAQ------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 174 riaaramqrreckrlHGRAGV----RGAVP-RHVAIHDFDSAMSRE-SGDSLLIPRRFEADDISSYFCTGGTTGLPKiAI 247
Cdd:PRK10524 188 ---------------HKPRHVllvdRGLAPmARVAGRDVDYATLRAqHLGARVPVEWLESNEPSYILYTSGTTGKPK-GV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 248 RRH--GNEVANAWSVGQVVGAGmgPGKTVFC----GLPLFHVNAVLAtglvPFSRGAHVVL--GTPqgYRGDGVVkrFWE 319
Cdd:PRK10524 252 QRDtgGYAVALATSMDTIFGGK--AGETFFCasdiGWVVGHSYIVYA----PLLAGMATIMyeGLP--TRPDAGI--WWR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 320 IVEHHRIN-FFSAvPTLYSALLDVPVD---GRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNP 395
Cdd:PRK10524 322 IVEKYKVNrMFSA-PTAIRVLKKQDPAllrKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 396 PGGER---RLGSIGLRIPGQMMKavILDDA-GRyvrDCVENEVGVLTISGPnVFAGYLQ----EDQN--KSLWLDLGdgR 465
Cdd:PRK10524 401 RGVEDrptRLGSPGVPMYGYNVK--LLNEVtGE---PCGPNEKGVLVIEGP-LPPGCMQtvwgDDDRfvKTYWSLFG--R 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 466 QWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE 545
Cdd:PRK10524 473 QVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAD 552
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1142773712 546 TE----LDTFIRGMIGER---AAIPKRIHIVDAMPLTAVGKI 580
Cdd:PRK10524 553 REarlaLEKEIMALVDSQlgaVARPARVWFVSALPKTRSGKL 594
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
56-587 |
8.71e-26 |
|
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: 111.75 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 56 LRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAG-IVCAINPLLEGPAIASLLKAANAKVLvt 134
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGaVLHTANPRLSPKEIAYILNHAEDKVL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 135 lapFPGSDIWSkiqpVLSEVPSLQSLVLIDLAERvqgwrriaaramqrreckrlhgragvrgavPRHVAIHDFDSamsre 214
Cdd:cd05915 101 ---LFDPNLLP----LVEAIRGELKTVQHFVVMD------------------------------EKAPEGYLAYE----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 215 SGDSLLIPRR--FEADDISSYFcTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLV 292
Cdd:cd05915 139 EALGEEADPVrvPERAACGMAY-TTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVLgtpQGYRGDGVVkrFWEIVEHHRINFFSAVPtlysaLLDVPVDGRniDSLEYG------LCGAAPMPVEV 366
Cdd:cd05915 218 TLVGAKQVLP---GPRLDPASL--VELFDGEGVTFTAGVPT-----VWLALADYL--ESTGHRlktlrrLVVGGSAAPRS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 367 FRTFQDRTGVRILEGYGLTE--GACVSSVNPPGGERRLGSIGLRIPGQ-----MMKAVILDDAGRYVRDCVENEVGVLTI 439
Cdd:cd05915 286 LIARFERMGVEVRQGYGLTEtsPVVVQNFVKSHLESLSEEEKLTLKAKtglpiPLVRLRVADEEGRPVPKDGKALGEVQL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 440 SGPNVFAGYLQEDQNKSLWLDLGDgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAA 519
Cdd:cd05915 366 KGPWITGGYYGNEEATRSALTPDG---FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAV 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 520 IGRPDVHAGELPVAYVQLKAgATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:cd05915 443 VAIPHPKWQERPLAVVVPRG-EKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
192-580 |
2.10e-25 |
|
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: 110.79 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 192 AGVRGAVPRHVAIHDFDSAMSRESGDSLLI-------PRRFEADDIS--SYfcTGGTTGLPKIAIRRHGNEVANAWSVgq 262
Cdd:cd05931 106 AAALAAVRAFAASRPAAGTPRLLVVDLLPDtsaadwpPPSPDPDDIAylQY--TSGSTGTPKGVVVTHRNLLANVRQI-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 263 VVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQGYrgdgvVKR--FW-EIVEHHRINFfSAVPTLYSAL 339
Cdd:cd05931 182 RRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAF-----LRRplRWlRLISRYRATI-SAAPNFAYDL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 340 L---DVPVDGRNID--SLEYGLCGAAPMPVEVFRTFQDR---TGVR---ILEGYGLTEGACVSSVNPPGGE--------- 399
Cdd:cd05931 256 CvrrVRDEDLEGLDlsSWRVALNGAEPVRPATLRRFAEAfapFGFRpeaFRPSYGLAEATLFVSGGPPGTGpvvlrvdrd 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 400 ----------------RRLGSIGLRIPGqmMKAVILDDAGRyvRDCVENEVGVLTISGPNVFAGYLQ---EDQNKSLWLD 460
Cdd:cd05931 336 alagravavaaddpaaRELVSCGRPLPD--QEVRIVDPETG--RELPDGEVGEIWVRGPSVASGYWGrpeATAETFGALA 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 461 LGDGRQWLNTGDLARRdAQGYFWLTGRRKELIIRGGHNIDPATIEEPL-HRHPAVQI--AAAIGRPDVHAGELpVAYVQL 537
Cdd:cd05931 412 ATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAeEAHPALRPgcVAAFSVPDDGEERL-VVVAEV 489
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1142773712 538 KAGATATET-ELDTFIRGMIGERAAI-PKRIHIV--DAMPLTAVGKI 580
Cdd:cd05931 490 ERGADPADLaAIAAAIRAAVAREHGVaPADVVLVrpGSIPRTSSGKI 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
209-580 |
4.14e-25 |
|
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: 108.93 E-value: 4.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 209 SAMSRESGDSLLIPrrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTvfcglpLFHVNA--- 285
Cdd:cd17643 77 AFILADSGPSLLLT---DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT------LFHSYAfdf 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 286 -------VLATG----LVPfsrgaHVVLGTPQgyrgdgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNIDSLE 353
Cdd:cd17643 148 svweiwgALLHGgrlvVVP-----YEVARSPE---------DFARLLRDEGVTVLNQTPSAFYQLVEAADrDGRDPLALR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 354 YGLCGAAPMPVEVFRTFQDRTGV---RILEGYGLTEgACVSS----VNPPGGERRLGS-IGLRIPGQmmKAVILDDAGRY 425
Cdd:cd17643 214 YVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITE-TTVHVtfrpLDAADLPAAAASpIGRPLPGL--RVYVLDADGRP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 426 VRDcveNEVGVLTISGPNVFAGYL-QEDQNKSLWLDL---GDGRQWLNTGDLARRDAQGYFWLTGRRKELI-IRgGHNID 500
Cdd:cd17643 291 VPP---GVVGELYVSGAGVARGYLgRPELTAERFVANpfgGPGSRMYRTGDLARRLPDGELEYLGRADEQVkIR-GFRIE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 501 PATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17643 367 LGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELL-PDYMVPARYVPLDALPLTVNGKL 445
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
236-580 |
3.48e-24 |
|
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: 105.91 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKtvfCGLPL--FHVNAVLATGLVPFSRGAHVVLGTPQGYRGdgv 313
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPLAAHCQATAERYG--LTPGD---RELQFasFNFDGAHEQLLPPLICGACVVLRPDELWAS--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 314 VKRFWEIVEHHRINFFSAVPTLYSALLDVPVDG--RNIDSLEYGLCGAAPMPVEVFRTFQdRTGVRILEGYGLTEGACVS 391
Cdd:cd17649 174 ADELAEMVRELGVTVLDLPPAYLQQLAEEADRTgdGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEATVTP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 392 SV-NPPGGERRLGS---IGLRIPGQmmKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQE-DQNKSLWL---DLGD 463
Cdd:cd17649 253 LVwKCEAGAARAGAsmpIGRPLGGR--SAYILDADLNPVPV---GVTGELYIGGEGLARGYLGRpELTAERFVpdpFGAP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 464 GRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELpVAYVQLKAGATA 543
Cdd:cd17649 328 GSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQ 406
|
330 340 350
....*....|....*....|....*....|....*....
gi 1142773712 544 TET--ELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17649 407 PELraQLRTALRASLPD-YMVPAHLVFLARLPLTPNGKL 444
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
18-588 |
4.05e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 106.75 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 18 PPADLPASTYEMIGRGAAIDPSAPALSfflradDHRKPLrwTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEthF 97
Cdd:PRK06164 4 DAAPRADTLASLLDAHARARPDAVALI------DEDRPL--SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIE--W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 98 VIWGGEAA---GIVCAINPLLEGPAIASLLKAANAKVLVTLAPFPGSD---IWSKIQPvlSEVPSLQSLVLIDLAERVqg 171
Cdd:PRK06164 74 VVLFLACArlgATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDfaaILAAVPP--DALPPLRAIAVVDDAADA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 172 wrrIAARA-MQRRECKRLHGRAGVRGAvprhvaihdfdsamsresgdsllIPRRFEADDISSYFCTGGTTGLPKIAIRRH 250
Cdd:PRK06164 150 ---TPAPApGARVQLFALPDPAPPAAA-----------------------GERAADPDAGALLFTTSGTTSGPKLVLHRQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 251 GNEVANAWSVGQVVGagMGPGKTVFCGLPL---FHVNAVLATglvpFSRGAHVVL----GTPQGYRgdgvvkrfweIVEH 323
Cdd:PRK06164 204 ATLLRHARAIARAYG--YDPGAVLLAALPFcgvFGFSTLLGA----LAGGAPLVCepvfDAARTAR----------ALRR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 324 HRINFFSAVPTLYSALLDVPVDGRNIDSLEY-GLCGAAPMPVEVFRTFQDRtGVRILEGYGLTE-GACVS--SVNPPGGE 399
Cdd:PRK06164 268 HRVTHTFGNDEMLRRILDTAGERADFPSARLfGFASFAPALGELAALARAR-GVPLTGLYGSSEvQALVAlqPATDPVSV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 400 RRLGSIGLRIPGQMMKAVILDDAGRyvrdCVENEVGVLTISGPNVFAGYLqEDQNKSLWLDLGDGrqWLNTGDLARRDAQ 479
Cdd:PRK06164 347 RIEGGGRPASPEARVRARDPQDGAL----LPDGESGEIEIRAPSLMRGYL-DNPDATARALTDDG--YFRTGDLGYTRGD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 480 GYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpdVHAGE-LPVAYVQLKAGATATETELdtfiRGMIGE 558
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAGL----MAACRE 493
|
570 580 590
....*....|....*....|....*....|....*.
gi 1142773712 559 RAA---IPKRIHIVDAMPLTAVG---KIFKPELKRW 588
Cdd:PRK06164 494 ALAgfkVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
236-578 |
8.93e-23 |
|
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: 99.68 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGqvVGAGMGPGKTVFCGLPLFHVnAVLATGLVPFSRGAHVVlgtpqgyrgdgVVK 315
Cdd:cd17636 8 TAAFSGRPNGALLSHQALLAQALVLA--VLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNV-----------FVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RF-----WEIVEHHRINFFSAVPTLYSALLDVPVDGR-NIDSLEYGlcgAAPMPVEVFRTFQDRTGVRILEGYGLTEGAC 389
Cdd:cd17636 74 RVdaeevLELIEAERCTHAFLLPPTIDQIVELNADGLyDLSSLRSS---PAAPEWNDMATVDTSPWGRKPGGYGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 390 VSSVNPPGGERrLGSIGLriPGQMMKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDqnkslwlDLGDGRQ--- 466
Cdd:cd17636 151 LATFAALGGGA-IGGAGR--PSPLVQVRILDEDGREVPD---GEVGEIVARGPTVMAGYWNRP-------EVNARRTrgg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATET 546
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEA 297
|
330 340 350
....*....|....*....|....*....|..
gi 1142773712 547 ELDTFIRGMIGERAAiPKRIHIVDAMPLTAVG 578
Cdd:cd17636 298 ELIEHCRARIASYKK-PKSVEFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
57-593 |
2.48e-22 |
|
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: 100.51 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCA-INPLLEGPAIASLLKAANAKVLVtl 135
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAAlINYNLRGESLAHCLNVSSAKHLV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 136 apfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlhgragvrgavprhvaihdFDSAMsres 215
Cdd:cd05940 81 -----------------------------------------------------------------------VDAAL---- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 216 gdslliprrfeaddissYFCTGGTTGLPKIAIRRHGnevaNAWSVGQVVG--AGMGPGKTVFCGLPLFHVNAVL---ATG 290
Cdd:cd05940 86 -----------------YIYTSGTTGLPKAAIISHR----RAWRGGAFFAgsGGALPSDVLYTCLPLYHSTALIvgwSAC 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 291 LVpfsRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPvdgRNIDSLEYGL---CGAAPMPvEVF 367
Cdd:cd05940 145 LA---SGATLVI------RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQP---PKPTERKHKVrmiFGNGLRP-DIW 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 368 RTFQDRTGV-RILEGYGLTEGACvSSVNPPGGERRLGSIGLRIPGQMMKAVI-LD-DAGRYVRD----CVE---NEVGVL 437
Cdd:cd05940 212 EEFKERFGVpRIAEFYAATEGNS-GFINFFGKPGAIGRNPSLLRKVAPLALVkYDlESGEPIRDaegrCIKvprGEPGLL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 438 T--ISGPNVFAGYL-QEDQNKSLWLD-LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPA 513
Cdd:cd05940 291 IsrINPLEPFDGYTdPAATEKKILRDvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPG 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 514 VQIAAAIGR--PDvHAGELPVAYVQLKAGataTETELDTFIRGMIGE--RAAIPKRIHIVDAMPLTAVGKIFKPELKRwE 589
Cdd:cd05940 371 VEEANVYGVqvPG-TDGRAGMAAIVLQPN---EEFDLSALAAHLEKNlpGYARPLFLRLQPEMEITGTFKQQKVDLRN-E 445
|
....
gi 1142773712 590 TFDA 593
Cdd:cd05940 446 GFDP 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
316-580 |
2.68e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 101.76 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RFWEIVEHHRINFFSAVPTLYSALL---DVPVDGRNIDSLEygLCGAAPMPV--EVFRTFQDRTG---VRILEGYGLTE- 386
Cdd:PRK00174 330 RFWEVIDKHKVTIFYTAPTAIRALMkegDEHPKKYDLSSLR--LLGSVGEPInpEAWEWYYKVVGgerCPIVDTWWQTEt 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 GACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRyvrDCVENEVGVLTISGPnvFAGylqedQNKSLWldlGDGRQ 466
Cdd:PRK00174 408 GGIMITPLPGATPLKPGSATRPLPG--IQPAVVDEEGN---PLEGGEGGNLVIKDP--WPG-----MMRTIY---GDHER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNT-----------GDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYV 535
Cdd:PRK00174 473 FVKTyfstfkgmyftGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFV 552
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1142773712 536 QLKAGATATE---TELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKI 580
Cdd:PRK00174 553 TLKGGEEPSDelrKELRNWVRKEIGP-IAKPDVIQFAPGLPKTRSGKI 599
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
181-585 |
6.66e-22 |
|
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: 99.27 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 181 QRREckRLHGRAGVRGAVPRHV----------AIHDFDSAmsrESGDSLLIPRRFEADDISSYFCTGGTTGLPKiairrh 250
Cdd:cd12114 74 ARRE--AILADAGARLVLTDGPdaqldvavfdVLILDLDA---LAAPAPPPPVDVAPDDLAYVIFTSGSTGTPK------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 251 GNEVANAwsvgqvvgagmGPGKTVFCGLPLFHVNA---VLA-TGLV----------PFSRGAHVVLgTPQGYRGDgvVKR 316
Cdd:cd12114 143 GVMISHR-----------AALNTILDINRRFAVGPddrVLAlSSLSfdlsvydifgALSAGATLVL-PDEARRRD--PAH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 317 FWEIVEHHRINFFSAVPTLYSALLDVPVD-GRNIDSLEYGLCGAAPMPVEVFRTFQDRT-GVRILEGYGLTEGACVSSVN 394
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLEMLLDVLEAaQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYH 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 395 PPG-GERRLGSI--GLRIPGQMMKavILDDAGRYVRDCVeneVGVLTISGPNVFAGYLQeDQNKSL--WLDLGDGRQWLN 469
Cdd:cd12114 289 PIDeVPPDWRSIpyGRPLANQRYR--VLDPRGRDCPDWV---PGELWIGGRGVALGYLG-DPELTAarFVTHPDGERLYR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 470 TGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELD 549
Cdd:cd12114 363 TGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALR 442
|
410 420 430
....*....|....*....|....*....|....*.
gi 1142773712 550 TFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:cd12114 443 AFLAQTLP-AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
227-589 |
3.11e-21 |
|
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: 96.87 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDISSYFCTGGTTGLPKIAIRRHgnevaNAWSVGQVVG---AGMGPGKTvfcglplfHVNaVLATG---------LVPF 294
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTH-----RSYPVGHLSTmywIGLKPGDV--------HWN-ISSPGwakhawscfFAPW 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 295 SRGAHVVLGTPQGYRGdgvvKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEygLCGAA-PMPVEVFRTFQDR 373
Cdd:cd05974 150 NAGATVFLFNYARFDA----KRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLRE--VVGAGePLNPEVIEQVRRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 374 TGVRILEGYGLTEGACVSSvNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVRdcvENEVG-VLTISGP-NVFAGYLQE 451
Cdd:cd05974 224 WGLTIRDGYGQTETTALVG-NSPGQPVKAGSMGRPLPG--YRVALLDPDGAPAT---EGEVAlDLGDTRPvGLMKGYAGD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 452 DQNKSLWLDLGDGRqwlnTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELP 531
Cdd:cd05974 298 PDKTAHAMRGGYYR----TGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVP 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 532 VAYVQLKAGATAT-ETELDTFirGMIGERAAIPKRIHIVD--AMPLTAVGKIFKPELKRWE 589
Cdd:cd05974 374 KAFIVLRAGYEPSpETALEIF--RFSRERLAPYKRIRRLEfaELPKTISGKIRRVELRRRE 432
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
32-580 |
6.02e-21 |
|
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: 96.64 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 32 RGAAIDPSAPALsfflrADDHRkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCA- 110
Cdd:cd17651 3 RQAARTPDAPAL-----VAEGR---RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 111 INPLLEGPAIASLLKAANAKVLVTlapfpgsdiwskiqpvlsevpslqslvlidlaervqgwrriaaramqrreckrlHG 190
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLT------------------------------------------------------HP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 191 RAGVRGAVPRHVAIHDFDSAMSRESGDSLLIPRrfEADDISSYFCTGGTTGLPKIAIRRHGNeVAN--AWsvgQVVGAGM 268
Cdd:cd17651 101 ALAGELAVELVAVTLLDQPGAAAGADAEPDPAL--DADDLAYVIYTSGSTGRPKGVVMPHRS-LANlvAW---QARASSL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 269 GPGKTV--FCGLPL-FHVNAVLATGLVpfsrGAHVVLGTPQgYRGDgvVKRFWEIVEHHRIN-FFSAVPTLYSALLDVPV 344
Cdd:cd17651 175 GPGARTlqFAGLGFdVSVQEIFSTLCA----GATLVLPPEE-VRTD--PPALAAWLDEQRISrVFLPTVALRALAEHGRP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 DGRNIDSLEYGLCGAAPMPVE--VFRTFQDRTGVRILEGYGLTEGACVSSV---NPPGGERRLGSIGLRIPGqmMKAVIL 419
Cdd:cd17651 248 LGVRLAALRYLLTGGEQLVLTedLREFCAGLPGLRLHNHYGPTETHVVTALslpGDPAAWPAPPPIGRPIDN--TRVYVL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 420 DDAGRYVRDCVeneVGVLTISGPNVFAGYLQE-DQNKSLWLD---LGDGRQWLnTGDLARRDAQGYFWLTGRRKELI-IR 494
Cdd:cd17651 326 DAALRPVPPGV---PGELYIGGAGLARGYLNRpELTAERFVPdpfVPGARMYR-TGDLARWLPDGELEFLGRADDQVkIR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 495 GgHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPL 574
Cdd:cd17651 402 G-FRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPE-YMVPSAFVLLDALPL 479
|
....*.
gi 1142773712 575 TAVGKI 580
Cdd:cd17651 480 TPNGKL 485
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
20-585 |
9.82e-21 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 96.23 E-value: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 20 ADLPASTYEMIGRGAAIDPSAPALsfflRADDHRKPLRwtYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVI 99
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQQPEAIAL----RRCDGTSALR--YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 100 WGGEAAGivcAINPLLEG--PAiASLLKAANAKVLVTLAPFPGSDIWSKIQP-VLSEVPSLQSLVLIDLAErvqgwrria 176
Cdd:PRK05857 84 LACAKLG---AIAVMADGnlPI-AAIERFCQITDPAAALVAPGSKMASSAVPeALHSIPVIAVDIAAVTRE--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 177 aramqrreckrlhgragvrgavprhvAIHDFDSAMSRESGDSlliprrfEADDISSYFCTGGTTGLPK---------IAI 247
Cdd:PRK05857 151 --------------------------SEHSLDAASLAGNADQ-------GSEDPLAMIFTSGTTGEPKavllanrtfFAV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 248 RRHGNEVANAWsVGQVVGagmgpgKTVFCGLPLFHVNAV--LATGLVpfsRGAHVVLGTPQGyrgdgvvKRFWEIVEHHR 325
Cdd:PRK05857 198 PDILQKEGLNW-VTWVVG------ETTYSPLPATHIGGLwwILTCLM---HGGLCVTGGENT-------TSLLEILTTNA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 326 INFFSAVPTLYSALL-DVPVDGRNIDSLEY-GLCGAAPMPVEVfrTFQDRTGVRILEGYGLTEGACVSSVNPPGGER--- 400
Cdd:PRK05857 261 VATTCLVPTLLSKLVsELKSANATVPSLRLvGYGGSRAIAADV--RFIEATGVRTAQVYGLSETGCTALCLPTDDGSivk 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 401 -RLGSIGLRIPGQMMKAVILDDAGRYVRDCVEN-EVGVLTISGPNVFAGYLQEDQNKSLWLDLGdgrqWLNTGDLARRDA 478
Cdd:PRK05857 339 iEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSaSFGTLWIKSPANMLGYWNNPERTAEVLIDG----WVNTGDLLERRE 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 479 QGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGEL----PVAYVQLKAGATAtetELDTFIRG 554
Cdd:PRK05857 415 DGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALvglaVVASAELDESAAR---ALKHTIAA 491
|
570 580 590
....*....|....*....|....*....|....
gi 1142773712 555 MI---GERAAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:PRK05857 492 RFrreSEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
46-587 |
1.36e-20 |
|
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: 95.81 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 46 FLRADDHrkPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVcainPLLEGPAIASLLK 125
Cdd:cd05906 30 YIDADGS--EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV----PAPLTVPPTYDEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 126 AANAKVLvtlapfpgSDIWSKI-QPVLsevpslqsLVLIDLAERVQGWRRIAARAMQRreckrlhgragvrgavprhvaI 204
Cdd:cd05906 104 NARLRKL--------RHIWQLLgSPVV--------LTDAELVAEFAGLETLSGLPGIR---------------------V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 205 HDFDSAMSRESGDSLLIPRrfeADDISSYFCTGGTTGLPKIAIRRHGNEVANawSVGQVVGAGMGPGKTVFCGLPLFHVN 284
Cdd:cd05906 147 LSIEELLDTAADHDLPQSR---PDDLALLMLTSGSTGFPKAVPLTHRNILAR--SAGKIQHNGLTPQDVFLNWVPLDHVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 285 AVLATGLVPFSRGA---HV----VLGTPqgyrgdgvvKRFWEIVEHHRI------NFFSAvptLYSALLDVPVDGR-NID 350
Cdd:cd05906 222 GLVELHLRAVYLGCqqvHVpteeILADP---------LRWLDLIDRYRVtitwapNFAFA---LLNDLLEEIEDGTwDLS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 351 SLEYGLCGAAPMPVEVFRTFQ---DRTGVR---ILEGYGLTE---GACVSSV---NPPGGERRLGSIGLRIPGQMMKavI 418
Cdd:cd05906 290 SLRYLVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAFGMTEtcsGVIYSRSfptYDHSQALEFVSLGRPIPGVSMR--I 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 419 LDDAGryvrDCV-ENEVGVLTISGPNVFAGYLQ-EDQNKSLWLDlgDGrqWLNTGDLARRDAqGYFWLTGRRKELIIRGG 496
Cdd:cd05906 368 VDDEG----QLLpEGEVGRLQVRGPVVTKGYYNnPEANAEAFTE--DG--WFRTGDLGFLDN-GNLTITGRTKDTIIVNG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 497 HNIDPATIEEPLHRHPAVQI----AAAIGRPDVHAGELPVAYV-----QLKAGATATEteldtfIRGMIGERAAIpKRIH 567
Cdd:cd05906 439 VNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVpeydlQDALSETLRA------IRSVVSREVGV-SPAY 511
|
570 580
....*....|....*....|....
gi 1142773712 568 IV----DAMPLTAVGKIFKPELKR 587
Cdd:cd05906 512 LIplpkEEIPKTSLGKIQRSKLKA 535
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
236-587 |
1.44e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 96.02 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANawSVGQVVGAGMGPGKTVFCGLPLFHV---NAVLATGLVPfsrGAHVVLgtPQgYRGDG 312
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALIVQ--SLAKIAIVGYGEDDVYLHTAPLCHIgglSSALAMLMVG---ACHVLL--PK-FDAKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 313 VVkrfwEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYG---LCGAAPMPVEVFR-TFQDRTGVRILEGYGLTEgA 388
Cdd:PLN02860 252 AL----QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVrkiLNGGGSLSSRLLPdAKKLFPNAKLFSAYGMTE-A 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 389 CVSsvnppggerrLGSIGLRIPGQMMKAVILDDAGRYVRDCVENEVGV----------LTIS-------------GPNVF 445
Cdd:PLN02860 327 CSS----------LTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVcvgkpaphveLKIGldessrvgriltrGPHVM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 446 AGYLqeDQNKSLWLDL-GDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPD 524
Cdd:PLN02860 397 LGYW--GQNSETASVLsNDG--WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPD 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 525 VHAGELPVAYVQLKAGATATETELDTFIRGMIG--------------ERAAIPKRIHI-VDAMPLTAVGKIFKPELKR 587
Cdd:PLN02860 473 SRLTEMVVACVRLRDGWIWSDNEKENAKKNLTLssetlrhhcreknlSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
219-588 |
1.66e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 96.32 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 219 LLIPRRF----EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPLFHVNAVLATGLVPF 294
Cdd:PRK08043 352 LLMPRLAqvkqQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI--ADFTPNDRFMSALPLFHSFGLTVGLFTPL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 295 SRGAHVVL-GTPQGYRgdgVVKrfwEIVEHHRINFFSAVPTLYS--ALLDVPVDgrnIDSLEYGLCGAAPMPVEVFRTFQ 371
Cdd:PRK08043 430 LTGAEVFLyPSPLHYR---IVP---ELVYDRNCTVLFGTSTFLGnyARFANPYD---FARLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTEGACVSSVNPPGGErRLGSIGLRIPGqmMKAVILDDAGryvrdcVENEvGVLTISGPNVFAGYLQE 451
Cdd:PRK08043 501 DKFGLRILEGYGVTECAPVVSINVPMAA-KPGTVGRILPG--MDARLLSVPG------IEQG-GRLQLKGPNIMNGYLRV 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 452 DQNKSLWLDLGDGRQ------WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEE-PLHRHPAVQIAAAIgRPD 524
Cdd:PRK08043 571 EKPGVLEVPTAENARgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSD 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 525 VHAGElpvAYVQLKAGATATETELDTFIRGMIGERAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK08043 650 ASKGE---ALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
226-492 |
4.63e-20 |
|
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: 93.82 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATgLVPFSRGAHVVLGTP 305
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAE-NVCLYRGGTIGYGSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 Q--------GYRGDGV---------VKRFWEIVEHHRINFFSAVPTL--------YSA------------LLDVPV---- 344
Cdd:cd17639 165 RtltdkskrGCKGDLTefkptlmvgVPAIWDTIRKGVLAKLNPMGGLkrtlfwtaYQSklkalkegpgtpLLDELVfkkv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 345 ----DGRnidsLEYGLCGAAPMPVEVFRtFQDRTGVRILEGYGLTEGACVSSVNPPgGERRLGSIGLRIPGQMMKAVILD 420
Cdd:cd17639 245 raalGGR----LRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTETCAGGTVQDP-GDLETGRVGPPLPCCEIKLVDWE 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 421 DAGrYVRDCVENEvGVLTISGPNVFAGYL-QEDQNKSLWldLGDGrqWLNTGDLARRDAQGYFWLTGRRKELI 492
Cdd:cd17639 319 EGG-YSTDKPPPR-GEILIRGPNVFKGYYkNPEKTKEAF--DGDG--WFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
58-521 |
1.26e-19 |
|
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: 93.19 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHF-----VIWGGEAAGIVCAINPllegPAIASLLKAANAKVL 132
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIaavgaIFAGGIAVGIYTTNSP----EACQYVAETSEANIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 133 VT-----LApfpgsdiwsKIQPVLSEVPSLQSLVLI--DLAER---VQGWRRIaaraMQrreckrlhgragvrgaVPRHV 202
Cdd:cd05933 85 VVenqkqLQ---------KILQIQDKLPHLKAIIQYkePLKEKepnLYSWDEF----ME----------------LGRSI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 203 AIHDFDSAMSRESGDS--LLIprrfeaddissYfcTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGK--TVFCGL 278
Cdd:cd05933 136 PDEQLDAIISSQKPNQccTLI-----------Y--TSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGqeSVVSYL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 279 PLFHVNAVLATGLVPFSRGAHVVLGTPQGYRGDGV-------------VKRFWE-IVEHHRINFFSAVP----------- 333
Cdd:cd05933 203 PLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVktlrevrptafmgVPRVWEkIQEKMKAVGAKSGTlkrkiaswakg 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 334 -------TLYSALLDVPVDGRNIDSLEY-------GL--C-----GAAPMPVEVFRTFQDrTGVRILEGYGLTEGACVSS 392
Cdd:cd05933 283 vgletnlKLMGGESPSPLFYRLAKKLVFkkvrkalGLdrCqkfftGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 393 VNPPGGeRRLGSIGLRIPGQMMKAVILDDAGryvrdcveneVGVLTISGPNVFAGYLQEDQNKSLWLDlGDGrqWLNTGD 472
Cdd:cd05933 362 ISNPQA-YRLLSCGKALPGCKTKIHNPDADG----------IGEICFWGRHVFMGYLNMEDKTEEAID-EDG--WLHSGD 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 473 LARRDAQGYFWLTGRRKELIIR-GGHNIDPATIEEPLH-RHPAVQIAAAIG 521
Cdd:cd05933 428 LGKLDEDGFLYITGRIKELIITaGGENVPPVPIEDAVKkELPIISNAMLIG 478
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
57-592 |
1.86e-19 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 91.72 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEtHFVIWGGEAA-GIVCA-INPLLEGPAIASLLKAANAKVLVT 134
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLE-FVALWLGLAKiGVETAlINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 135 lapfpgsdiwSKIQPVLS----EVPSLQSLvlidlaervqgwrriaaramqrreckrlhgragvrgavprhvaihdfdsa 210
Cdd:cd05939 82 ----------NLLDPLLTqsstEPPSQDDV-------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 211 msresgdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFHVnavlATG 290
Cdd:cd05939 102 ---------------NFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIA--AGAYYAFGMRPEDVVYDCLPLYHS----AGG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 291 LVPFsrGAHVVLGTPQGYRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPV---DGRNIDSLEYGlCGAAPmpvEVF 367
Cdd:cd05939 161 IMGV--GQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPseeEQKHNVRLAVG-NGLRP---QIW 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 368 RTFQDRTGV-RILEGYGLTEGACvSSVNPPGgerRLGSIGL--RIPGQMMKAVIL---DDAGRYVRD-------CVENEV 434
Cdd:cd05939 235 EQFVRRFGIpQIGEFYGATEGNS-SLVNIDN---HVGACGFnsRILPSVYPIRLIkvdEDTGELIRDsdglcipCQPGEP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 435 GVL--TISGPNV---FAGYLQE-DQNKSLWLD-LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEP 507
Cdd:cd05939 311 GLLvgKIIQNDPlrrFDGYVNEgATNKKIARDvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 508 LHRhpavqiaaAIGRPDVHAGELPVAYVQLKAGATA-----TETELDTFIRGMIGERA--AIPKRIHIVDAMPLTAVGKI 580
Cdd:cd05939 391 LSN--------VLGLEDVVVYGVEVPGVEGRAGMAAivdpeRKVDLDRFSAVLAKSLPpyARPQFIRLLPEVDKTGTFKL 462
|
570
....*....|..
gi 1142773712 581 FKPELKRwETFD 592
Cdd:cd05939 463 QKTDLQK-EGYD 473
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
69-587 |
3.91e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.38 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 69 RAANM----FSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVcaINPL---LEGPAIASLLKAANAKVLVT---LAPf 138
Cdd:PRK05620 47 RAAALahalHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAV--FNPLnkqLMNDQIVHIINHAEDEVIVAdprLAE- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 139 pgsdiwsKIQPVLSEVPSLQSLVLIdlaervqGWRRIAARAMQrreckrlhgragvrgaVPRHVAIHDFDSAMSRESGDs 218
Cdd:PRK05620 124 -------QLGEILKECPCVRAVVFI-------GPSDADSAAAH----------------MPEGIKVYSYEALLDGRSTV- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 219 LLIPRRFEADDISSYFCTGgTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVnavLATGlVPFsrgA 298
Cdd:PRK05620 173 YDWPELDETTAAAICYSTG-TTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGESFLCCVPIYHV---LSWG-VPL---A 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 299 HVVLGTPQGYRG-DGVVKRFWEIVEHHRINFFSAVPTLYSAL----LDVPVDGRnidSLEYGLCGAAPMPVEVFRTFQDR 373
Cdd:PRK05620 245 AFMSGTPLVFPGpDLSAPTLAKIIATAMPRVAHGVPTLWIQLmvhyLKNPPERM---SLQEIYVGGSAVPPILIKAWEER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 374 TGVRILEGYGLTEGACVSSV-NPPGG---ERRLG---SIGlRIPGQMMKAVILDdaGRYVRDCVENEvGVLTISGPNVFA 446
Cdd:PRK05620 322 YGVDVVHVWGMTETSPVGTVaRPPSGvsgEARWAyrvSQG-RFPASLEYRIVND--GQVMESTDRNE-GEIQVRGNWVTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 447 GYLQEDQNKSLWL-------DLGDGRQ------WLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPA 513
Cdd:PRK05620 398 SYYHSPTEEGGGAastfrgeDVEDANDrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 514 VQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGERAA--IPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK05620 478 VVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNwmLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
236-585 |
4.47e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 90.83 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHvNAVLATGLVPFSRGAHVVlgTPQGYRGDGVVK 315
Cdd:PRK13383 182 TSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFH-GLGLGMLMLTIALGGTVL--THRHFDAEAALA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RfweiVEHHRINFFSAVPTLYSALLDVP--VDGRN-IDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSS 392
Cdd:PRK13383 259 Q----ASLHRADAFTAVPVVLARILELPprVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGAL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 393 VNPPGGERRLGSIGLRIPGQMMKavILDDAGRYVRDCVENEVGVltisgpnvfAGYLQEDQNKSlwldlGDGRQWLN--- 469
Cdd:PRK13383 335 ATPADLRDAPETVGKPVAGCPVR--ILDRNNRPVGPRVTGRIFV---------GGELAGTRYTD-----GGGKAVVDgmt 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 470 -TGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETEL 548
Cdd:PRK13383 399 sTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQL 478
|
330 340 350
....*....|....*....|....*....|....*..
gi 1142773712 549 DTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:PRK13383 479 RDYLKDRV-SRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
210-580 |
5.24e-19 |
|
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: 90.06 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 210 AMSRESGDSLLIPRRfEADDISSYFCTGGTTGLPKIAIRRHGNeVANAWSVGqvvGAGM--GPGKTV--FCGlPLFHVNA 285
Cdd:cd17653 88 AILRTSGATLLLTTD-SPDDLAYIIFTSGSTGIPKGVMVPHRG-VLNYVSQP---PARLdvGPGSRVaqVLS-IAFDACI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 286 --VLATglvpFSRGAHVVLGTPQGYRGDgvVKRfweivehhRINFFSAVPTLYSALldvpvDGRNIDSLEYGLCGAAPMP 363
Cdd:cd17653 162 geIFST----LCNGGTLVLADPSDPFAH--VAR--------TVDALMSTPSILSTL-----SPQDFPNLKTIFLGGEAVP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 364 VEVFRTFqdRTGVRILEGYGLTEGACVSSVNPPGGERRLgSIGLRIPGQMMkaVILDDAGRYVrdcVENEVGVLTISGPN 443
Cdd:cd17653 223 PSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTC--YILDADLQPV---PEGVVGEICISGVQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 444 VFAGYLQEDQ---NKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHR-HPAVQIAAA 519
Cdd:cd17653 295 VARGYLGNPAltaSKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAA 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 520 IgrpdVHAGELpVAYVqlkAGATATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17653 375 I----VVNGRL-VAFV---TPETVDVDGLRSELAKHL-PSYAVPDRIIALDSFPLTANGKV 426
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
236-597 |
6.72e-19 |
|
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: 91.46 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPK-IAIRrHGNeVAN--AWSVGQVvgaGMGPGKTVfcglPLFH-VNAVLATG--LVPFSRGAHVVLGTPQGyR 309
Cdd:COG1020 625 TSGSTGRPKgVMVE-HRA-LVNllAWMQRRY---GLGPGDRV----LQFAsLSFDASVWeiFGALLSGATLVLAPPEA-R 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 310 GDGVvkRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRniDSLEYGLCGAAPMPVEVFRTFQDRT-GVRILEGYGLTE-- 386
Cdd:COG1020 695 RDPA--ALAELLARHRVTVLNLTPSLLRALLDAAPEAL--PSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTEtt 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 -GACVSSVNPPGGERRLGSIGLRIPGQmmKAVILDDAGryvRDCVENEVGVLTISGPNVFAGYLQEDqnkslwlDL---- 461
Cdd:COG1020 771 vDSTYYEVTPPDADGGSVPIGRPIANT--RVYVLDAHL---QPVPVGVPGELYIGGAGLARGYLNRP-------ELtaer 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 462 -------GDGRQWLNTGDLARRDAQG---YFwltGRR----KeliIRgGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHA 527
Cdd:COG1020 839 fvadpfgFPGARLYRTGDLARWLPDGnleFL---GRAddqvK---IR-GFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 528 GELPVAYVQLKAGATATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPELKRWETFDALVSA 597
Cdd:COG1020 912 DKRLVAYVVPEAGAAAAAALLRLALALLL-PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
211-580 |
6.72e-18 |
|
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: 86.75 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 211 MSRESGDSLLIprrFEADDISSYFCTGGTTGLPKIAIRRHGN--EVANAWsvgqvvgagmgpgKTVFcGLPLFHVNAVLA 288
Cdd:cd17650 79 MLEDSGAKLLL---TQPEDLAYVIYTSGTTGKPKGVMVEHRNvaHAAHAW-------------RREY-ELDSFPVRLLQM 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 289 TGL---VPFSRGAHVVL--GT----PQGYRGDGVvkRFWEIVEHHRINFFSAVPTLYSALLD-VPVDGRNIDSLEYGLCG 358
Cdd:cd17650 142 ASFsfdVFAGDFARSLLngGTlvicPDEVKLDPA--ALYDLILKSRITLMESTPALIRPVMAyVYRNGLDLSAMRLLIVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 359 AAPMPVEVFRTFQDRTG--VRILEGYGLTEgACVSSVNPPGGERRLGS-----IGLRIPGQMMkaVILDDAGRYVRDCVe 431
Cdd:cd17650 220 SDGCKAQDFKTLAARFGqgMRIINSYGVTE-ATIDSTYYEEGRDPLGDsanvpIGRPLPNTAM--YVLDERLQPQPVGV- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 432 neVGVLTISGPNVFAGYL-QEDQNKSLWLD--LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPL 508
Cdd:cd17650 296 --AGELYIGGAGVARGYLnRPELTAERFVEnpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQL 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142773712 509 HRHPAVQIAAAIGRPDVHAGELPVAYVQlkAGATATETELdtfiRGMIGER---AAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17650 374 ARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAEL----RAFLAKElpsYMIPSYYVQLDALPLTPNGKV 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
504-579 |
1.57e-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: 77.20 E-value: 1.57e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 504 IEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGK 579
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGP-YAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-580 |
1.64e-17 |
|
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: 85.72 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 34 AAIDPSAPALSFFLRaddhrkplRWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGivCAINP 113
Cdd:cd12117 7 AARTPDAVAVVYGDR--------SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG--AAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 114 L-LEGPA--IASLLKAANAKVLVTLAPFPGSdiwskiqpvlseVPSLQSLVLIDLAERVQGwrriaaramqrreckrlhg 190
Cdd:cd12117 77 LdPELPAerLAFMLADAGAKVLLTDRSLAGR------------AGGLEVAVVIDEALDAGP------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 191 ragvrGAVPRHVAihdfdsamsresgdslliprrfEADDISSYFCTGGTTGLPKIAIRRHGN---EVANAWsvgqvvGAG 267
Cdd:cd12117 126 -----AGNPAVPV----------------------SPDDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTN------YVT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 268 MGPGKTVFCGLPLfhvnAVLATGL---VPFSRGAHVVLgTPQGYRGDGvvKRFWEIVEHHRIN--FFSAvpTLYSALLDV 342
Cdd:cd12117 173 LGPDDRVLQTSPL----AFDASTFeiwGALLNGARLVL-APKGTLLDP--DALGALIAEEGVTvlWLTA--ALFNQLADE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 343 PVDGrnIDSLEYGLCGAAPMPVEVFRTFQDRT-GVRILEGYGLTEG---ACVSSVNPPGGERRLGSIGLRIPGqmMKAVI 418
Cdd:cd12117 244 DPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENttfTTSHVVTELDEVAGSIPIGRPIAN--TRVYV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 419 LDDAGRYVRdcvENEVGVLTISGPNVFAGYL---QEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRR-KELIIR 494
Cdd:cd12117 320 LDEDGRPVP---PGVPGELYVGGDGLALGYLnrpALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIdDQVKIR 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 495 GgHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATEteldtfIRGMIGERA---AIPKRIHIVDA 571
Cdd:cd12117 397 G-FRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAE------LRAFLRERLpayMVPAAFVVLDE 469
|
....*....
gi 1142773712 572 MPLTAVGKI 580
Cdd:cd12117 470 LPLTANGKV 478
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
226-491 |
1.99e-17 |
|
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: 85.73 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAG--MGPGKTVFCGLPLFH------VNAVLATGL-VPFSR 296
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILnkINPTDVYISYLPLAHifervvEALFLYHGAkIGFYS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 297 G-------------AHVVLGTP-----------QGYRGDGVVKR--FWEIVEHHRINFFSAVPTlYSALLDVPVD----- 345
Cdd:cd05927 192 GdirlllddikalkPTVFPGVPrvlnriydkifNKVQAKGPLKRklFNFALNYKLAELRSGVVR-ASPFWDKLVFnkikq 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 346 --GRNIDSLeygLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPgGERRLGSIGLRIPGQMMKAVILDDAG 423
Cdd:cd05927 271 alGGNVRLM---LTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLP-GDTSVGHVGGPLPCAEVKLVDVPEMN 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773712 424 RYVRDCveNEVGVLTISGPNVFAGYLQ-EDQNKSLwLDLgDGrqWLNTGDLARRDAQGYFWLTGRRKEL 491
Cdd:cd05927 347 YDAKDP--NPRGEVCIRGPNVFSGYYKdPEKTAEA-LDE-DG--WLHTGDIGEWLPNGTLKIIDRKKNI 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
222-601 |
5.04e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.98 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 222 PRRFEADDISSYFCTGGTTGLPKIAIRRHGN-----EVANAWSvgqvvgaGMGPGKTVFcglpLFHVNAVLATGLV---P 293
Cdd:PRK12467 650 EVALDPDNLAYVIYTSGSTGQPKGVAISHGAlanyvCVIAERL-------QLAADDSML----MVSTFAFDLGVTElfgA 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 294 FSRGAHVVLGTPQGYRgDGvvKRFWEIVEHHRINFFSAVPTLYSALLDVP-VDGrnIDSLEYGLCGAAPMPVE-VFRTFQ 371
Cdd:PRK12467 719 LASGATLHLLPPDCAR-DA--EAFAALMADQGVTVLKIVPSHLQALLQASrVAL--PRPQRALVCGGEALQVDlLARVRA 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTEGACVSSVNPPGGERRLGS---IGLRIPGQMMKavILDdagRYVRDCVENEVGVLTISGPNVFAGY 448
Cdd:PRK12467 794 LGPGARLINHYGPTETTVGVSTYELSDEERDFGnvpIGQPLANLGLY--ILD---HYLNPVPVGVVGELYIGGAGLARGY 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 449 LQE---DQNKSLWLDLG-DGRQWLNTGDLARRDAQGYFWLTGRRKELI-IRgGHNIDPATIEEPLHRHPAVQIAAAIGRP 523
Cdd:PRK12467 869 HRRpalTAERFVPDPFGaDGGRLYRTGDLARYRADGVIEYLGRMDHQVkIR-GFRIELGEIEARLLAQPGVREAVVLAQP 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 524 DVHAGELpVAYVQLKAGATATE-----TELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIfkpELKRWETFDAlvSAL 598
Cdd:PRK12467 948 GDAGLQL-VAYLVPAAVADGAEhqatrDELKAQLRQVLPDY-MVPAHLLLLDSLPLTPNGKL---DRKALPKPDA--SAV 1020
|
...
gi 1142773712 599 KDA 601
Cdd:PRK12467 1021 QAT 1023
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
332-580 |
5.30e-17 |
|
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: 83.91 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 332 VPTLYSALLD---VPVDGRNIDsleygLCGAaPMPVEVFRTFQDR-TGVRILEGYGLTEGACVSSVNP-PGGERRLGSIG 406
Cdd:cd12115 198 VPSAAAELLRhdaLPASVRVVN-----LAGE-PLPRDLVQRLYARlQVERVVNLYGPSEDTTYSTVAPvPPGASGEVSIG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 407 LRIPGQmmKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYLQEDQ---NKSLWLDLGDGRQWLNTGDLARRDAQGYFW 483
Cdd:cd12115 272 RPLANT--QAYVLDRALQPVPLGV---PGELYIGGAGVARGYLGRPGltaERFLPDPFGPGARLYRTGDLVRWRPDGLLE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 484 LTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGErAAIP 563
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPA-YMVP 425
|
250
....*....|....*..
gi 1142773712 564 KRIHIVDAMPLTAVGKI 580
Cdd:cd12115 426 SRFVRLDALPLTPNGKI 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
236-580 |
8.94e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPG---KTVFCglplFHVNavLATGLVPFSRGAHVVLGTPQGYRGdg 312
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTvlqKTPFS----FDVS--VWEFFWPLMSGARLVVAAPGDHRD-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 313 vVKRFWEIVEHHRINFFSAVPTLYSALLDVPvDGRNIDSLEYGLCGAAPMPVE-VFRTFQDRTGVRILEGYGLTEGA--- 388
Cdd:PRK12316 735 -PAKLVELINREGVDTLHFVPSMLQAFLQDE-DVASCTSLRRIVCSGEALPADaQEQVFAKLPQAGLYNLYGPTEAAidv 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 389 -CVSSVNPPGGERrlgSIGLRIPGqmMKAVILDDAGRYVRDCVENEvgvLTISGPNVFAGYLQE---DQNKSLWLDLGDG 464
Cdd:PRK12316 813 tHWTCVEEGGDSV---PIGRPIAN--LACYILDANLEPVPVGVLGE---LYLAGRGLARGYHGRpglTAERFVPSPFVAG 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 465 RQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIgrpdVHAGELPVAYVQLKAGATAT 544
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLESEGGDW 960
|
330 340 350
....*....|....*....|....*....|....*.
gi 1142773712 545 ETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKI 580
Cdd:PRK12316 961 REALKAHLAASLPEY-MVPAQWLALERLPLTPNGKL 995
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
236-588 |
1.48e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 82.73 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIrrHGNEVANA--------WSVGQVVGagmgpgktvFCGLPLFHVnavlaTGLVPFSR-----GAHVVL 302
Cdd:PRK07445 128 TGGSSGQIRFAI--HTWETLTAsvqgfqryFQLQQVNS---------FCVLPLYHV-----SGLMQFMRsfltgGKLVIL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 303 GtpqgyrgdgvvkrfWEIVEHHRIN-------FFSAVPTLYSALLDVPVDG-RNIDSLEYGlcGAAPMP--VEVFRTFQd 372
Cdd:PRK07445 192 P--------------YKRLKSGQELppnpsdfFLSLVPTQLQRLLQLRPQWlAQFRTILLG--GAPAWPslLEQARQLQ- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 373 rtgVRILEGYGLTEGAC-VSSVNPpgGERRLGSIGLripGQMMKAVILDdagryvrdCVENEVGVLTISGPNVFAGYlqe 451
Cdd:PRK07445 255 ---LRLAPTYGMTETASqIATLKP--DDFLAGNNSS---GQVLPHAQIT--------IPANQTGNITIQAQSLALGY--- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 452 dqnkslWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELP 531
Cdd:PRK07445 316 ------YPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 532 VAYVQLKAGATATEtELDTFIRGMIGeRAAIPKRIHIVDAMPLTAVGKIFKPELKRW 588
Cdd:PRK07445 390 TAIYVPKDPSISLE-ELKTAIKDQLS-PFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
228-587 |
1.55e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 81.63 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagmGPGKTVFcGLPLFH-------VNAVLAtGLVPfsrgahV 300
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG---GPGQWLL-ALPAHHiaglqvlVRSVIA-GSEP------V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 301 VLGTPQGYRGDGVVKRFWEIVEHHRinFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDrTGVRILE 380
Cdd:PRK07824 104 ELDVSAGFDPTALPRAVAELGGGRR--YTSLVPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA-AGINVVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 381 GYGLTE--GACVSSVNPpggerrLGSIGLRIPGqmmkavilddagryvrdcvenevGVLTISGPNVFAGYLQEDQNKSlW 458
Cdd:PRK07824 181 TYGMSEtsGGCVYDGVP------LDGVRVRVED-----------------------GRIALGGPTLAKGYRNPVDPDP-F 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 459 LDLGdgrqWLNTGDLARRDAqGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLK 538
Cdd:PRK07824 231 AEPG----WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1142773712 539 AGATATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK07824 306 GGPAPTLEALRAHVARTL-DRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
261-615 |
2.89e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 82.84 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 261 GQVVGAGMGPGKTVFCGLPLFHVNAVLAtglvpfSRGAHVVLGT----PQGYRGDgvvkRFWEIVEHHRINFFSAVPTLY 336
Cdd:PRK07868 636 GTASAAALDRRDTVYCLTPLHHESGLLV------SLGGAVVGGSrialSRGLDPD----RFVQEVRQYGVTVVSYTWAML 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 337 SALLDVP---VDGRNIDSLEYGlcgaAPMPVEVFRTFQDR-TGVRILEGYGLTEGACVSSvNPPGGerRLGSIGLRIPG- 411
Cdd:PRK07868 706 REVVDDPafvLHGNHPVRLFIG----SGMPTGLWERVVEAfAPAHVVEFFATTDGQAVLA-NVSGA--KIGSKGRPLPGa 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 412 --------QMMKAVILDDAGRYVRDCVENEVGVL-TISGPNVfagylqeDQNKSLWLDL-GDGRQWLNTGDLARRDAQGY 481
Cdd:PRK07868 779 grvelaayDPEHDLILEDDRGFVRRAEVNEVGVLlARARGPI-------DPTASVKRGVfAPADTWISTEYLFRRDDDGD 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 482 FWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpDVHAGELPVAYVQLKAGATATETELDTFIRGM-IGERa 560
Cdd:PRK07868 852 YWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGV-EVGGRQLAVAAVTLRPGAAITAADLTEALASLpVGLG- 929
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 561 aiPKRIHIVDAMPLTAvgkifkpelkrweTFDALVSALKDAGV--EGARVSMVDDPS 615
Cdd:PRK07868 930 --PDIVHVVPEIPLSA-------------TYRPTVSALRAAGIpkPGRQAWYFDPET 971
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
236-580 |
3.03e-16 |
|
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: 81.68 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGaGMGPGKTVFcglpLFHVNAVLAtglvPFSR-------GAHVVLGTPQGY 308
Cdd:cd17648 102 TSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDEAV----LFFSNYVFD----FFVEqmtlallNGQKLVVPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 309 RGDGvvKRFWEIVEHHRINFFSAVPTLYSAlldvpVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGA 388
Cdd:cd17648 173 RFDP--DRFYAYINREKVTYLSGTPSVLQQ-----YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 389 CVSSVNP-PGGERRLGSIGLRIPGqmMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYL---------------QED 452
Cdd:cd17648 246 VTNHKRFfPGDQRFDKSLGRPVRN--TKCYVLNDAMKRVP---VGAVGELYLGGDGVARGYLnrpeltaerflpnpfQTE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 453 QNKSlwldLGDGRQWLNTGDLARRDAQGYFWLTGRRK-ELIIRgGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELP 531
Cdd:cd17648 321 QERA----RGRNARLYKTGDLVRWLPSGELEYLGRNDfQVKIR-GQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSR 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 532 -----VAYVQLKAGaTATETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17648 396 iqkylVGYYLPEPG-HVPESDLLSFLRAKL-PRYMVPARLVRLEGIPVTINGKL 447
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
293-612 |
3.97e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 82.25 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVL--GTPQgYRGDGvvkRFWEIVEHHRINFFSAVPTLYSALL---DVPVDGRNIDSLEYGLCGAAPMPVEVF 367
Cdd:PLN02654 339 PMLNGATVLVfeGAPN-YPDSG---RCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPINPSAW 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 368 RTFQDRTG---VRILEGYGLTE-GACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAGRYVrdcvENEV-GVLTI--S 440
Cdd:PLN02654 415 RWFFNVVGdsrCPISDTWWQTEtGGFMITPLPGAWPQKPGSATFPFFG--VQPVIVDEKGKEI----EGECsGYLCVkkS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 441 GPNVFAG-YLQEDQNKSLWLDLGDGrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAA 519
Cdd:PLN02654 489 WPGAFRTlYGDHERYETTYFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 520 IGRPDVHAGELPVAYVQLKAGATATE---TELDTFIRGMIGERAAiPKRIHIVDAMPLTAVGKIFKPELKRWET--FDAL 594
Cdd:PLN02654 567 VGIEHEVKGQGIYAFVTLVEGVPYSEelrKSLILTVRNQIGAFAA-PDKIHWAPGLPKTRSGKIMRRILRKIASrqLDEL 645
|
330 340
....*....|....*....|
gi 1142773712 595 --VSALKDAGVEGARVSMVD 612
Cdd:PLN02654 646 gdTSTLADPGVVDQLIALAD 665
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-514 |
9.95e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.75 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTP 305
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QGYRGDGVvkRFWEIVEHHRiNFFSAVPTLYSALLDVPVDGRNIDSLEY-----GLCGAAPMPVEVFRTFQDR------T 374
Cdd:PRK05691 244 AYFLERPL--RWLEAISEYG-GTISGGPDFAYRLCSERVSESALERLDLsrwrvAYSGSEPIRQDSLERFAEKfaacgfD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 375 GVRILEGYGLTEGACVSSvnppGGERRLGSIGLRIPGQMMKA-VILDDAGRYVRDC--------------------VENE 433
Cdd:PRK05691 321 PDSFFASYGLAEATLFVS----GGRRGQGIPALELDAEALARnRAEPGTGSVLMSCgrsqpghavlivdpqslevlGDNR 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 434 VGVLTISGPNVFAGYLQEDQNKSLWLDLGDGRQWLNTGDLA-RRDaqGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHP 512
Cdd:PRK05691 397 VGEIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGfLRD--GELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474
|
..
gi 1142773712 513 AV 514
Cdd:PRK05691 475 EV 476
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
222-505 |
1.91e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 79.76 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 222 PRRFEA---DDISSYFCTGGTTGLPKIAIRRHGNEVANAwsVGQVVGAGMGPGKTVFCGLPLFH----VNAVLAtglvpf 294
Cdd:PLN02736 212 PQPFRPpkpEDVATICYTSGTTGTPKGVVLTHGNLIANV--AGSSLSTKFYPSDVHISYLPLAHiyerVNQIVM------ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 295 srgahVVLGTPQG-YRGDgvVKRFWEIVEHHRINFFSAVPTLYSALLD--------------------------VPVDGR 347
Cdd:PLN02736 284 -----LHYGVAVGfYQGD--NLKLMDDLAALRPTIFCSVPRLYNRIYDgitnavkesgglkerlfnaaynakkqALENGK 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 348 NI----DSL-------------EYGLCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACV-SSVNPpgGERRLGSIGLRI 409
Cdd:PLN02736 357 NPspmwDRLvfnkikaklggrvRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCViSGMDE--GDNLSGHVGSPN 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 410 PGQMMKAVILDDAGrYVRDCVENEVGVLTISGPNVFAGYLQ-EDQNKslwlDLGDGRQWLNTGDLArrdaqgyFWLTGRR 488
Cdd:PLN02736 435 PACEVKLVDVPEMN-YTSEDQPYPRGEICVRGPIIFKGYYKdEVQTR----EVIDEDGWLHTGDIG-------LWLPGGR 502
|
330 340
....*....|....*....|....*
gi 1142773712 489 KELIIRG--------GHNIDPATIE 505
Cdd:PLN02736 503 LKIIDRKknifklaqGEYIAPEKIE 527
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
228-586 |
3.14e-15 |
|
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: 78.63 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQvvGAGMGPGKTVFCGLPLFHVNAVLATGLVPFSRGAHVVLGTPQG 307
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSH--DLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 308 yrgdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPV---DGRNIDSLEYGlCGAAPmpvEVFRTFQDRTGVRIL-EGYG 383
Cdd:cd05937 165 ------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPspyDRDHKVRVAWG-NGLRP---DIWERFRERFNVPEIgEFYA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 384 LTEGAcVSSVNPPGGERRLGSIGLR------------IPGQM---MKAVILDDAGRYVRDCVENEVG--VLTISGPNV-- 444
Cdd:cd05937 235 ATEGV-FALTNHNVGDFGAGAIGHHglirrwkfenqvVLVKMdpeTDDPIRDPKTGFCVRAPVGEPGemLGRVPFKNRea 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 445 FAGYLQ-EDQNKSLWLD--LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIG 521
Cdd:cd05937 314 FQGYLHnEDATESKLVRdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 522 --RPDvHAGELPVAYVQLKAGATA----TETELDTFIRGMIgERAAIPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:cd05937 394 vkVPG-HDGRAGCAAITLEESSAVptefTKSLLASLARKNL-PSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
324-580 |
5.80e-15 |
|
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: 77.68 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 324 HRINFFSAVPtlySALLDVPVDGRnIDSLEYGLCGAAPMPVEVFRTFQDRtgvRILEGYGLTEG-ACVSSVNPPGGERRL 402
Cdd:cd17652 183 HRITHVTLPP---AALAALPPDDL-PDLRTLVVAGEACPAELVDRWAPGR---RMINAYGPTETtVCATMAGPLPGGGVP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 403 gSIGLRIPGQmmKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYL-QEDQNKSLWLD---LGDGRQWLNTGDLARRDA 478
Cdd:cd17652 256 -PIGRPVPGT--RVYVLDARLRPVPPGV---PGELYIAGAGLARGYLnRPGLTAERFVAdpfGAPGSRMYRTGDLARWRA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 479 QGYFWLTGRRKELI-IRGgHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIg 557
Cdd:cd17652 330 DGQLEFLGRADDQVkIRG-FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERL- 407
|
250 260
....*....|....*....|...
gi 1142773712 558 ERAAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17652 408 PGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
209-588 |
9.55e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 209 SAMSRESGDSLLIPRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHV-NAVL 287
Cdd:PRK09274 155 ATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYG--IEPGEIDLPTFPLFALfGPAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 288 -ATGLVP---FSRGAHVvlgTPQgyrgdgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNIDSLEYGLCGAAPM 362
Cdd:PRK09274 233 gMTSVIPdmdPTRPATV---DPA---------KLFAAIERYGVTNLFGSPALLERLGRYGEaNGIKLPSLRRVISAGAPV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 363 PVEVFRTFQD--RTGVRILEGYGLTEGACVSSVnppGGERRLGS------------IGLRIPGQMMKAVILDDAG----R 424
Cdd:PRK09274 301 PIAVIERFRAmlPPDAEILTPYGATEALPISSI---ESREILFAtraatdngagicVGRPVDGVEVRIIAISDAPipewD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 425 YVRDCVENEVGVLTISGPNVFAGYLQEDQ----NKslwLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNID 500
Cdd:PRK09274 378 DALRLATGEIGEIVVAGPMVTRSYYNRPEatrlAK---IPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLY 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 501 PATIEEPLHRHPAVQIAAAIGRPdVHAGELPVAYVQLKAGAT----ATETELDTfirgmIGERAAIPKRIHIVDAMPLTA 576
Cdd:PRK09274 455 TIPCERIFNTHPGVKRSALVGVG-VPGAQRPVLCVELEPGVAcsksALYQELRA-----LAAAHPHTAGIERFLIHPSFP 528
|
410
....*....|....*..
gi 1142773712 577 V-----GKIFKPELKRW 588
Cdd:PRK09274 529 VdirhnAKIFREKLAVW 545
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
58-527 |
1.11e-14 |
|
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: 77.46 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 58 WTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPEthfVIWGGEAAGIVCAIN-PLLE---GPAIASLLKAANAKVLV 133
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPE---WVWAELAAQAIGALSlGIYQdsmAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 134 TlapfPGSDIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaARAMQRRECKRLHGRAGVRGAVPRHVAIHDfdsamsr 213
Cdd:cd17641 89 A----EDEEQVDKLLEIADRIPSVRYVIYCD------------PRGMRKYDDPRLISFEDVVALGRALDRRDP------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 214 ESGDSLLipRRFEADDISSYFCTGGTTGLPKIAIRRHGNeVANAWSVGQVVGaGMGPGKTVFCGLPL-------FHVNAV 286
Cdd:cd17641 146 GLYEREV--AAGKGEDVAVLCTTSGTTGKPKLAMLSHGN-FLGHCAAYLAAD-PLGPGDEYVSVLPLpwigeqmYSVGQA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 287 LATG-LVPFSR------------GAHVVLGTP------------------------------QGYRGDGVVKRFWEIVEH 323
Cdd:cd17641 222 LVCGfIVNFPEepetmmedlreiGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGKRGRPVSLW 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 324 HRINFFSAVPTLYSALLDVpvdgRNIDSLEYGLCGAAPMPVEVFRTFQdRTGVRILEGYGLTEgACVSSVNPPGGERRLG 403
Cdd:cd17641 302 LRLASWLADALLFRPLRDR----LGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTE-LAGAYTVHRDGDVDPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 404 SIGLRIPGQMMKAvilddagryvrdcveNEVGVLTISGPNVFAGYLQeDQNKSLWLDLGDGrqWLNTGDLARRDAQGYFW 483
Cdd:cd17641 376 TVGVPFPGTEVRI---------------DEVGEILVRSPGVFVGYYK-NPEATAEDFDEDG--WLHTGDAGYFKENGHLV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1142773712 484 LTGRRKEL-IIRGGHNIDPATIEEPLHRHPAVQIAAAIG--RPDVHA 527
Cdd:cd17641 438 VIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGagRPYLTA 484
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
317-583 |
1.90e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 76.70 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 317 FWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSlEYGL-------CGAAPMPVEVFRTFQDRTGVRILEGYGLTEGAC 389
Cdd:PTZ00237 341 LWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRS-KYDLsnlkeiwCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGI 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 390 VSSVNPPGGERRLGSIGlrIPGQMMKAVILDDAGRYVRdcvENEVG--VLTISGPNVFAG--YLQEDQNKSLWLDLgdgR 465
Cdd:PTZ00237 420 TYLYCYGHINIPYNATG--VPSIFIKPSILSEDGKELN---VNEIGevAFKLPMPPSFATtfYKNDEKFKQLFSKF---P 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 466 QWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE 545
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQS 571
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1142773712 546 TELDTF---IRGMIG---ERAAIPKRIHIVDAMPLTAVGKIFKP 583
Cdd:PTZ00237 572 IDLNKLkneINNIITqdiESLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
57-592 |
2.14e-14 |
|
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: 76.18 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 57 RWTYAALLRDITRAANMFSRLGIDRH-AVVAYVLPNLPEthFV-IWGGEA-AGIVCA-INPLLEGPAIASLLKAANAKVL 132
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHAGLRPgDTVALLLGNEPA--FLwIWLGLAkLGCPVAfLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 133 VTlapfpGSDIWSKIQPVLsevPSLQslvlidlAERVQGWrriaaraMQRRECKrlhgragvrgavprHVAIHDFDSAMS 212
Cdd:cd05938 83 VV-----APELQEAVEEVL---PALR-------ADGVSVW-------YLSHTSN--------------TEGVISLLDKVD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 213 RESGDSllIPRRFEAD----DISSYFCTGGTTGLPKIAIRRHgnevANAWSVGQVVGA-GMGPGKTVFCGLPLFHVNAVL 287
Cdd:cd05938 127 AASDEP--VPASLRAHvtikSPALYIYTSGTTGLPKAARISH----LRVLQCSGFLSLcGVTADDVIYITLPLYHSSGFL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 288 ATGLVPFSRGAHVVLgtpqgyRGDGVVKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNID-----SLEYGLCGaapm 362
Cdd:cd05938 201 LGIGGCIELGATCVL------KPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDhkvrlAIGNGLRA---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 363 pvEVFRTFQDRTG-VRILEGYGLTEGAcVSSVNPPGgerRLGSIG-------LRIPGQMMKAVIldDAGRYVRD----CV 430
Cdd:cd05938 271 --DVWREFLRRFGpIRIREFYGSTEGN-IGFFNYTG---KIGAVGrvsylykLLFPFELIKFDV--EKEEPVRDaqgfCI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 431 E---NEVGVLT--ISGPNVFAGYL--QEDQNKSLWLDL---GDgrQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNID 500
Cdd:cd05938 343 PvakGEPGLLVakITQQSPFLGYAgdKEQTEKKLLRDVfkkGD--VYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 501 PATIEEPLHRHPAVQIAAAIGRPdV--HAGELPVAYVQLKAGatateTELDtfirgmiGERA-----------AIPKRIH 567
Cdd:cd05938 421 TTEVADVLGLLDFLQEVNVYGVT-VpgHEGRIGMAAVKLKPG-----HEFD-------GKKLyqhvreylpayARPRFLR 487
|
570 580
....*....|....*....|....*
gi 1142773712 568 IVDAMPLTAVGKIFKPELKRwETFD 592
Cdd:cd05938 488 IQDSLEITGTFKQQKVRLVE-EGFN 511
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
372-579 |
2.46e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 76.20 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLtegacvsSVNPPGGERRLGSI---GLRIPGQMMKavILDDAGRYVRdcvENEVGVLTISGPNVFAGY 448
Cdd:PRK09192 358 EEVDRDRLEYQGK-------AVAPGAETRRVRTFvncGKALPGHEIE--IRNEAGMPLP---ERVVGHICVRGPSLMSGY 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 449 L-QEDQNKSLwldLGDGrqWLNTGDLARRdAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQI--AAAIGRPDv 525
Cdd:PRK09192 426 FrDEESQDVL---AADG--WLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQ- 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 526 HAGELPVAYVQLKAGATATETELdtfirgmIGERAAIPKRIHIVDAM---------PLTAVGK 579
Cdd:PRK09192 499 ENGEKIVLLVQCRISDEERRGQL-------IHALAALVRSEFGVEAAvelvpphslPRTSSGK 554
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
222-587 |
5.99e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 5.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 222 PRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFCGlplFHVNAVLATGLVPFSRGAHVV 301
Cdd:PRK12316 3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT---FSFDVFVEELFWPLMSGARVV 3266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 302 LGTPQGYRGdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPvDGRNIDSLEYGLCGAAPMPVEVFRtfQDRTGVRILEG 381
Cdd:PRK12316 3267 LAGPEDWRD---PALLVELINSEGVDVLHAYPSMLQAFLEEE-DAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNL 3340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTEgACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYLQE---DQNKSLW 458
Cdd:PRK12316 3341 YGPTE-ATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGA---LGELYLGGEGLARGYHNRpglTAERFVP 3416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 459 LDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpdvhAGELPVAYVQLK 538
Cdd:PRK12316 3417 DPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPE 3492
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1142773712 539 AGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPELKR 587
Cdd:PRK12316 3493 DEAGDLREALKAHLKASLPEY-MVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
236-586 |
2.30e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.53 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVvGAGMGPGKTVFCGLPLFHV----NAV---LATGlvpfsrGAHVVLGTPQGY 308
Cdd:PRK06060 153 TSGTTGPPKAAIHRHADPLTFVDAMCRK-ALRLTPEDTGLCSARMYFAyglgNSVwfpLATG------GSAVINSAPVTP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 309 RGDGVVK-RFWEIVEHHRINFFSAV-----PTLYSALLDVPVDGrniDSLEYGLcgaAPMPVEVFrtfqdrTGVRILEGY 382
Cdd:PRK06060 226 EAAAILSaRFGPSVLYGVPNFFARVidscsPDSFRSLRCVVSAG---EALELGL---AERLMEFF------GGIPILDGI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 383 GLTEgACVSSVNPPGGERRLGSIGLRIPGQMMKAVILDdaGRYVRDCVEnevGVLTISGPNVFAGYLqeDQNKSLWLDLG 462
Cdd:PRK06060 294 GSTE-VGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPD--GTTAGPGVE---GDLWVRGPAIAKGYW--NRPDSPVANEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 463 dgrqWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGAT 542
Cdd:PRK06060 366 ----WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAT 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1142773712 543 ATETELDTFIRGMIGERAA--IPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK06060 442 IDGSVMRDLHRGLLNRLSAfkVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-536 |
3.81e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.11 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 225 FEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHV-NAVLA-TGLVP---FSRGAH 299
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG--IRPGEVDLATFPLFALfGPALGlTSVIPdmdPTRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 300 VvlgTPQgyrgdgvvkRFWEIVEHHRINFFSAVPtlysALLDV-----PVDGRNIDSLEYGLCGAAPMPVEVFRTFQD-- 372
Cdd:cd05910 160 A---DPQ---------KLVGAIRQYGVSIVFGSP----ALLERvarycAQHGITLPSLRRVLSAGAPVPIALAARLRKml 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 373 RTGVRILEGYGLTEGACVSSVN---------PPGGERRLGSIGLRIPGQMMKAVILDDAG----RYVRDCVENEVGVLTI 439
Cdd:cd05910 224 SDEAEILTPYGATEALPVSSIGsrellatttAATSGGAGTCVGRPIPGVRVRIIEIDDEPiaewDDTLELPRGEIGEITV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 440 SGPNVFAGYL-QEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAA 518
Cdd:cd05910 304 TGPTVTPTYVnRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
330 340
....*....|....*....|
gi 1142773712 519 --AIGRPdvhAGELPVAYVQ 536
Cdd:cd05910 384 lvGVGKP---GCQLPVLCVE 400
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
226-511 |
5.87e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.77 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 226 EADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKTVFcgLPLFHVNAVLATGLVPFSRGAHVVLGTP 305
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSF--LPPFHAYGFNSCTLFPLLSGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QGYrgdgvVKRFWEIVEHHRINFFSAVPTLYSALLDVPV-DGRNIDSLEYGLCGAAPMPVEVF-RTFQDRTGVRILEGYG 383
Cdd:PRK06334 259 PLY-----PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKkQESCLPSLRFVVIGGDAFKDSLYqEALKTFPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 384 LTEGACVSSVNPPGGERRLGSIGLRIPGqmMKAVILDDAgRYVrDCVENEVGVLTISGPNVFAGYLQEDQNKSlWLDLGd 463
Cdd:PRK06334 334 TTECSPVITINTVNSPKHESCVGMPIRG--MDVLIVSEE-TKV-PVSSGETGLVLTRGTSLFSGYLGEDFGQG-FVELG- 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1142773712 464 GRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRH 511
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
224-627 |
6.75e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.68 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 224 RFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVvgAGMGPGKTVFCGLPlFHVNAVLATGLVPFSRGAHVVLg 303
Cdd:PRK12316 2142 QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER--YELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLI- 2217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 304 tpqgyRGDGV--VKRFWEIVEHHRINFFSAVPTLYSALLDV-PVDGRNIDSLEYgLCGAAPMPVEVFRTFQDRT-GVRIL 379
Cdd:PRK12316 2218 -----RDDELwdPEQLYDEMERHGVTILDFPPVYLQQLAEHaERDGRPPAVRVY-CFGGEAVPAASLRLAWEALrPVYLF 2291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 380 EGYGLTEGACVSSVNPPGGERRLGS----IGLRIPGQmmKAVILDDAgryVRDCVENEVGVLTISGPNVFAGYLQED-QN 454
Cdd:PRK12316 2292 NGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNR--RAYILDAD---LNLLAPGMAGELYLGGEGLARGYLNRPgLT 2366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 455 KSLWLD---LGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpDVHAGELP 531
Cdd:PRK12316 2367 AERFVPdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQL 2445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 532 VAYVQLKAGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIFKPELKRWETFDALVSALKDAGVEGARVSMV 611
Cdd:PRK12316 2446 VAYVVPDDAAEDLLAELRAWLAARLPAY-MVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAI 2524
|
410
....*....|....*.
gi 1142773712 612 DDPSRGLTlHVALSDH 627
Cdd:PRK12316 2525 WQAVLKVE-QVGLDDH 2539
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
236-588 |
8.56e-13 |
|
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: 71.03 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFC------GLPLFHVNAVLATG---LVPfSRgahvvlgtpq 306
Cdd:cd05918 114 TSGSTGKPKGVVIEHRALSTSALAHGRALG--LTSESRVLQfasytfDVSILEIFTTLAAGgclCIP-SE---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 307 gyrgDGVVKRFWEIVEHHRINFFSAVPTLySALLDvPVDgrnIDSLEYGLCGAAPMPVEVFRTFQDRtgVRILEGYGLTE 386
Cdd:cd05918 181 ----EDRLNDLAGFINRLRVTWAFLTPSV-ARLLD-PED---VPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 GACVSSVNPPGGERRLGSIGLRIPGQmmkAVILdDAGRYVRDCVENEVGVLTISGPNVFAGYL-QEDQNKS--------- 456
Cdd:cd05918 250 CTIAATVSPVVPSTDPRNIGRPLGAT---CWVV-DPDNHDRLVPIGAVGELLIEGPILARGYLnDPEKTAAafiedpawl 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 457 LWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELI-IRgGHNIDPATIEEPLHRHPAVQ---IAAAIGRPDVHAGELPV 532
Cdd:cd05918 326 KQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVkIR-GQRVELGEIEHHLRQSLPGAkevVVEVVKPKDGSSSPQLV 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1142773712 533 AYVQLkAGATATETELDTFIRGMIGERAAIPKRIH-----------------IVDAMPLTAVGKIFKPELKRW 588
Cdd:cd05918 405 AFVVL-DGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
203-580 |
1.75e-12 |
|
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: 70.05 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 203 AIHDFDSAMSRESGDSLLIPRRfeADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGmgpGKTVFCGLPLFH 282
Cdd:cd17655 114 IDLLDEDTIYHEESENLEPVSK--SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQG---EHLRVALFASIS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 283 VNAVLATGLVPFSRGAHVVLGtPQGYRGDGVVkrFWEIVEHHRINFFSAVPTLYSALldVPVDGRNIDSLEYGLCGAAPM 362
Cdd:cd17655 189 FDASVTEIFASLLSGNTLYIV-RKETVLDGQA--LTQYIRQNRITIIDLTPAHLKLL--DAADDSEGLSLKHLIVGGEAL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 363 PVEVFRTF--QDRTGVRILEGYGLTEgACV--SSVNPPGGERRLGSIGLRIPGQMMKAVILDDAGRYVRdcvENEVGVLT 438
Cdd:cd17655 264 STELAKKIieLFGTNPTITNAYGPTE-TTVdaSIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQP---VGVAGELY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 439 ISGPNVFAGYL-QEDQNKSLWLD--LGDGRQWLNTGDLARRDAQGYFWLTGR-RKELIIRGgHNIDPATIEEPLHRHPAV 514
Cdd:cd17655 340 IGGEGVARGYLnRPELTAEKFVDdpFVPGERMYRTGDLARWLPDGNIEFLGRiDHQVKIRG-YRIELGEIEARLLQHPDI 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142773712 515 QIAAAIGRPDvHAGELPV-AYVqlkagatATETELDTfirGMIGERAA-------IPKRIHIVDAMPLTAVGKI 580
Cdd:cd17655 419 KEAVVIARKD-EQGQNYLcAYI-------VSEKELPV---AQLREFLArelpdymIPSYFIKLDEIPLTPNGKV 481
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
222-492 |
2.12e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.15 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 222 PRRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVgAGMGPGKTVFCGLPLFHVnAVLATGLVPFSRGAHVV 301
Cdd:PLN02387 244 PDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVV-PKLGKNDVYLAYLPLAHI-LELAAESVMAAVGAAIG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 302 LGTP-----------QGYRGD-------------------------------GVVKRFWEIVEHHRI-----NFFSAVpT 334
Cdd:PLN02387 322 YGSPltltdtsnkikKGTKGDasalkptlmtavpaildrvrdgvrkkvdakgGLAKKLFDIAYKRRLaaiegSWFGAW-G 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 335 LYSALLDVPVdGRNIDSLEYG-----LCGAAPMPVEVFRTFQDRTGVRILEGYGLTE---GACVSSVNPPGgerrLGSIG 406
Cdd:PLN02387 401 LEKLLWDALV-FKKIRAVLGGrirfmLSGGAPLSGDTQRFINICLGAPIGQGYGLTEtcaGATFSEWDDTS----VGRVG 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 407 LRIPGQMMKAVILDDAGRYVRDCVENEvGVLTISGPNVFAGYL--QEDQNKSLWLDlGDGRQWLNTGDLARRDAQGYFWL 484
Cdd:PLN02387 476 PPLPCCYVKLVSWEEGGYLISDKPMPR-GEIVIGGPSVTLGYFknQEKTDEVYKVD-ERGMRWFYTGDIGQFHPDGCLEI 553
|
....*...
gi 1142773712 485 TGRRKELI 492
Cdd:PLN02387 554 IDRKKDIV 561
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
236-598 |
5.35e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.42 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGnEVANAWSVGQVVgAGMGPGKTVFCGLPlFHVNAVLATGLVPFSRGAHVVLGTPQGYRGDgvvk 315
Cdd:PRK12467 3245 TSGSTGKPKGVGVRHG-ALANHLCWIAEA-YELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNDLWDPE---- 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RFWEIVEHHRINFFSAVPTLYSALLDVPvDGRNIDSLEYGLCGAAPMPVEVF-RTFQDRTGVRILEGYGLTEGACVSSVN 394
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPAYLQQFAEDA-GGADCASLDIYVFGGEAVPPAAFeQVKRKLKPRGLTNGYGPTEAVVTVTLW 3396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 395 PPGGERRLGS----IGLRIPGqmMKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYLQEdqnKSLWLD-------LGD 463
Cdd:PRK12467 3397 KCGGDAVCEApyapIGRPVAG--RSIYVLDGQLNPVPVGV---AGELYIGGVGLARGYHQR---PSLTAErfvadpfSGS 3468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 464 GRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpDVHAGELPVAYVQLKAGATA 543
Cdd:PRK12467 3469 GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGD 3547
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 544 TETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKIF-----KPELKRWETFDALVSAL 598
Cdd:PRK12467 3548 WRETLRDHLAASLPDY-MVPAQLLVLAAMPLGPNGKVDrkalpDPDAKGSREYVAPRSEV 3606
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
223-603 |
1.12e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.45 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 223 RRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPlFHVNAVLATGLVPFSRGAHVVL 302
Cdd:PRK12316 4689 VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE--LTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVI 4765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 303 GTPQGYRGDgvvkRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFR-TFQDRTGVRILEG 381
Cdd:PRK12316 4766 RDDSLWDPE----RLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDlAWRALKPVYLFNG 4841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 382 YGLTEGACVSSVNPPGGERRLGS----IGLRIPGqmMKAVILDDAGRYVRDCVeneVGVLTISGPNVFAGYLQE---DQN 454
Cdd:PRK12316 4842 YGPTETTVTVLLWKARDGDACGAaympIGTPLGN--RSGYVLDGQLNPLPVGV---AGELYLGGEGVARGYLERpalTAE 4916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 455 KSLWLDLGD-GRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELpVA 533
Cdd:PRK12316 4917 RFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQL-VG 4995
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 534 YVQLKAGATATETELDTFIRGMIGE--RAAIPKRI---HIV--DAMPLTAVGKIfkpELKRWETFDAlvSALKDAGV 603
Cdd:PRK12316 4996 YVVPQDPALADADEAQAELRDELKAalRERLPEYMvpaHLVflARMPLTPNGKL---DRKALPQPDA--SLLQQAYV 5067
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
29-580 |
1.22e-11 |
|
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: 67.68 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 29 MIGRGAAIDPSApalsffLRADDHRKPLRWTYAALLRDITRAANMFSRLGI---DRhaVVAYvLPNLPEThfVIWGGEAA 105
Cdd:cd05943 76 LLRHADADDPAA------IYAAEDGERTEVTWAELRRRVARLAAALRALGVkpgDR--VAGY-LPNIPEA--VVAMLATA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 106 ---GIVCAINPLLEGPAIASLLKAANAKVLVT--LAPFPGS--DIWSKIQPVLSEVPSLQSLVLIDlaeRVQGWRRIAAR 178
Cdd:cd05943 145 sigAIWSSCSPDFGVPGVLDRFGQIEPKVLFAvdAYTYNGKrhDVREKVAELVKGLPSLLAVVVVP---YTVAAGQPDLS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 179 AMQRReckrlhgragvrgavprhvaiHDFDSAMSRESGDSLLiPRRFEADD-----ISSyfctgGTTGLPKIAIRRHGNE 253
Cdd:cd05943 222 KIAKA---------------------LTLEDFLATGAAGELE-FEPLPFDHplyilYSS-----GTTGLPKCIVHGAGGT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 254 VANAWSvGQVVGAGMGPGKTVF----CGLPLFHvnaVLATGLvpfSRGAHVVL--GTPqGYRGDGVvkrFWEIVEHHRIN 327
Cdd:cd05943 275 LLQHLK-EHILHCDLRPGDRLFyyttCGWMMWN---WLVSGL---AVGATIVLydGSP-FYPDTNA---LWDLADEEGIT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 328 FFSAVPTLYSALLD---VPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRILEGY--GLTE-GACVSSVNPPGGERR 401
Cdd:cd05943 344 VFGTSAKYLDALEKaglKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKPDVLLASisGGTDiISCFVGGNPLLPVYR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 402 lGSIGLRIPGqmMKAVILDDAGRYVRDcvenEVGVLTI-----SGPNVF----------AGYLqeDQNKSLWldlgdgrq 466
Cdd:cd05943 424 -GEIQCRGLG--MAVEAFDEEGKPVWG----EKGELVCtkpfpSMPVGFwndpdgsryrAAYF--AKYPGVW-------- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 wlNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATEt 546
Cdd:cd05943 487 --AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDD- 563
|
570 580 590
....*....|....*....|....*....|....*..
gi 1142773712 547 ELDTFIRGMIGERAA---IPKRIHIVDAMPLTAVGKI 580
Cdd:cd05943 564 ELRKRIRSTIRSALSprhVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
34-545 |
2.48e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 66.43 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 34 AAIDPSAPALsfflRADDHRkplrWTYAALLRDITRAANMFSRLGIDRHAVVAYVLPNLPETHFVIWGGEAAGIVCA-IN 112
Cdd:PRK09029 13 AQVRPQAIAL----RLNDEV----LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLpLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 113 PLLEGPAIASLLKAANAKVLVTLAPFPgsdiwskiqpvlsEVPSLQSLVLIDLAERVQGwrriaaramqrreckrlhgra 192
Cdd:PRK09029 85 PQLPQPLLEELLPSLTLDFALVLEGEN-------------TFSALTSLHLQLVEGAHAV--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 193 gvrgavprhvaihdfdsamsresgdslliprRFEADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVvgagM--GP 270
Cdd:PRK09029 131 -------------------------------AWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSL----MpfTA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 271 GKTVFCGLPLFHVNAVlatGLVP--FSRGAHVVLGTPQGyrgdgvvkrFWEIVEH--HRinffSAVPTLYSALLDvpvDG 346
Cdd:PRK09029 176 QDSWLLSLPLFHVSGQ---GIVWrwLYAGATLVVRDKQP---------LEQALAGctHA----SLVPTQLWRLLD---NR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 347 RNIDSLEYGLCGAAPMPVEVFRTFQDRtGVRILEGYGLTEGAcvSSVNPPGGERRLGsIGLRIPGqmmkavilddagRYV 426
Cdd:PRK09029 237 SEPLSLKAVLLGGAAIPVELTEQAEQQ-GIRCWCGYGLTEMA--STVCAKRADGLAG-VGSPLPG------------REV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 427 RdCVENEVgvlTISGPNVFAGYLQEDQnkslWLDLGDGRQWLNTGDLARRDaQGYFWLTGRRKELIIRGGHNIDPATIEE 506
Cdd:PRK09029 301 K-LVDGEI---WLRGASLALGYWRQGQ----LVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIER 371
|
490 500 510
....*....|....*....|....*....|....*....
gi 1142773712 507 PLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATE 545
Cdd:PRK09029 372 VINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN 410
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
236-586 |
1.17e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.90 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIaIRRHGNEVA---NAWSVGQVVGAGMGPgkTVFCglPLFHVNAVLATGLVPFSRGAHVVLGTPQGYRGdg 312
Cdd:PRK08308 109 SSGTTGEPKL-IRRSWTEIDreiEAYNEALNCEQDETP--IVAC--PVTHSYGLICGVLAALTRGSKPVIITNKNPKF-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 313 VVKRFWEIVEHhrinFFSAVPTLYSALLDVPVDGRNIDSLeygLCGAAPMPVEVFRTFQDRTgVRILEGYGLTEGACVSs 392
Cdd:PRK08308 182 ALNILRNTPQH----ILYAVPLMLHILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAGCVS- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 393 VNPPggerrlgsigLRIPGQMMKAVilddagRYVRdcvenevgvltisgpnVFAGylqEDQNKSLWLDLGDGRQWLNTGD 472
Cdd:PRK08308 253 ICPD----------MKSHLDLGNPL------PHVS----------------VSAG---SDENAPEEIVVKMGDKEIFTKD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 473 LARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVqlkagatATETELDTF- 551
Cdd:PRK08308 298 LGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV-------ISHEEIDPVq 370
|
330 340 350
....*....|....*....|....*....|....*...
gi 1142773712 552 IRGMIGERAA---IPKRIHIVDAMPLTAVGKIFKPELK 586
Cdd:PRK08308 371 LREWCIQHLApyqVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
236-505 |
1.89e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCG-LPLFHvNAVLATGLVPFSRGAHVVLGTPQGYRGDGVv 314
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVG--LDAATDVGCSwLPLYH-DMGLAFLLTAALAGAPLWLAPTTAFSASPF- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 315 kRFWEIVEHHRINFFSAVPTLYSAL--LDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQD---RTGVR---ILEGYGLTE 386
Cdd:PRK05851 236 -RWLSWLSDSRATLTAAPNFAYNLIgkYARRVSDVDLGALRVALNGGEPVDCDGFERFATamaPFGFDagaAAPSYGLAE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 387 GACVSSVNPPG--------------GERRLGSIGLRIPGqmMKAVILDDAGRyvRDCVENEVGVLTISGPNVFAGYLQED 452
Cdd:PRK05851 315 STCAVTVPVPGiglrvdevttddgsGARRHAVLGNPIPG--MEVRISPGDGA--AGVAGREIGEIEIRGASMMSGYLGQA 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 453 QnkslwldlGDGRQWLNTGDLarrdaqGYFW-----LTGRRKELIIRGGHNIDPATIE 505
Cdd:PRK05851 391 P--------IDPDDWFPTGDL------GYLVdgglvVCGRAKELITVAGRNIFPTEIE 434
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
37-580 |
2.35e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 63.66 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 37 DPSAPALSFflrADDHRKPLRWTYAALLRDITRAANMFSRLGI---DRhaVVAYvLPNLPEThfVIWGGEAAGI-----V 108
Cdd:PRK03584 97 RDDRPAIIF---RGEDGPRRELSWAELRRQVAALAAALRALGVgpgDR--VAAY-LPNIPET--VVAMLATASLgaiwsS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 109 CAinPLLEGPAIASLLKAANAKVLVTLA--PFPGS--DIWSKIQPVLSEVPSLQSLVLIDlaervqgwrriaaramqrre 184
Cdd:PRK03584 169 CS--PDFGVQGVLDRFGQIEPKVLIAVDgyRYGGKafDRRAKVAELRAALPSLEHVVVVP-------------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 185 ckrlhgRAGVRGAVPRHVAIHDFDSAMSRESGDSLliprRFEA---DD---I--SSyfctgGTTGLPKIAIRRHGNEVAN 256
Cdd:PRK03584 227 ------YLGPAAAAAALPGALLWEDFLAPAEAAEL----EFEPvpfDHplwIlySS-----GTTGLPKCIVHGHGGILLE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 257 AWSVGQvVGAGMGPGKTVF----CGLPL--FHVnAVLATglvpfsrGAHVVL--GTPqGYRGDGVvkrFWEIVEHHRINF 328
Cdd:PRK03584 292 HLKELG-LHCDLGPGDRFFwyttCGWMMwnWLV-SGLLV-------GATLVLydGSP-FYPDPNV---LWDLAAEEGVTV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 329 FSAVPTLYSALLD---VPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTGVRIlegygltegaCVSSVNppGGERRLGS- 404
Cdd:PRK03584 359 FGTSAKYLDACEKaglVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKADV----------WLASIS--GGTDICSCf 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 405 -IGLRI----PGQM------MKAVILDDAGRYVRDcvenEVG--VLTISGPN--VFagylqedqnksLWLDlGDGRQWLN 469
Cdd:PRK03584 427 vGGNPLlpvyRGEIqcrglgMAVEAWDEDGRPVVG----EVGelVCTKPFPSmpLG-----------FWND-PDGSRYRD 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 470 T-----------GDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLK 538
Cdd:PRK03584 491 AyfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA 570
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1142773712 539 AGATATEtELDTFIRGMIGERAA---IPKRIHIVDAMPLTAVGKI 580
Cdd:PRK03584 571 EGVTLDD-ALRARIRTTIRTNLSprhVPDKIIAVPDIPRTLSGKK 614
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
211-585 |
1.43e-09 |
|
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: 60.65 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 211 MSRESGDSLLIPrrfEADDISSYFCTGGTTGLPKIAIRRHGNEV------ANAWSVGQ----VVGAGMGPGKTVFCGLPL 280
Cdd:cd17645 90 MLADSSAKILLT---NPDDLAYVIYTSGSTGLPKGVMIEHHNLVnlcewhRPYFGVTPadksLVYASFSFDASAWEIFPH 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 281 FHVNAVLatglvpfsrgaHVVlgtPQGYRGDgvVKRFWEIVEHHRINFfSAVPTLYSALLdVPVDGRnidSLEYGLCGAA 360
Cdd:cd17645 167 LTAGAAL-----------HVV---PSERRLD--LDALNDYFNQEGITI-SFLPTGAAEQF-MQLDNQ---SLRVLLTGGD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 361 PMPVEVfrtfqdRTGVRILEGYGLTEGACVSSVNPPGGERrlGSIGLRIPGQMMKAVILDDAGRYvrdCVENEVGVLTIS 440
Cdd:cd17645 226 KLKKIE------RKGYKLVNNYGPTENTVVATSFEIDKPY--ANIPIGKPIDNTRVYILDEALQL---QPIGVAGELCIA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 441 GPNVFAGYL---QEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIA 517
Cdd:cd17645 295 GEGLARGYLnrpELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELA 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142773712 518 AAIGRPDVHAGELPVAYVQLKAGATATEteldtfIRGMIGERAA---IPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:cd17645 375 AVLAKEDADGRKYLVAYVTAPEEIPHEE------LREWLKNDLPdymIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
227-505 |
4.64e-09 |
|
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: 59.04 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 227 ADDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVNAVLATGLVPFSRGA-HVVLGTP 305
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE--WKTKDRILSWMPLTHDMGLIAFHLAPLIAGMnQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 306 QgyrgdgVVKR--FW-EIVEHHRINFFSAVPTLYSALLDV--PVDGRNID--SLEYGLCGAAPMPVEVFRTFQDRTGVR- 377
Cdd:cd05908 183 L------FIRRpiLWlKKASEHKATIVSSPNFGYKYFLKTlkPEKANDWDlsSIRMILNGAEPIDYELCHEFLDHMSKYg 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 378 -----ILEGYGLTE---GACVSSVN----PPGGERRLGSIGLRIPGQMMK---AVILDDAGRYVRDC----VENE----- 433
Cdd:cd05908 257 lkrnaILPVYGLAEasvGASLPKAQspfkTITLGRRHVTHGEPEPEVDKKdseCLTFVEVGKPIDETdiriCDEDnkilp 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 434 ---VGVLTISGPNVFAGYL--QEDQNKSLwldLGDGrqWLNTGDLA-RRDaqGYFWLTGRRKELIIRGGHNIDPATIE 505
Cdd:cd05908 337 dgyIGHIQIRGKNVTPGYYnnPEATAKVF---TDDG--WLKTGDLGfIRN--GRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
236-587 |
4.86e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.79 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLP---------LFHvnavlatglvPFSRGAHVVLGTPQ 306
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVNRLCATQEAYQ--LSAADVVLQFTSfafdvsvweLFW----------PLINGARLVIAPPG 1793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 307 GYRGDGvvkRFWEIVEHHRINFFSAVPTLYSALLDVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQDRTG-VRILEGYGLT 385
Cdd:PRK12467 1794 AHRDPE---QLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPT 1870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 386 EGAC------VSSVNPPGgeRRLGSIGLRIPgqmmkavildDAGRYVRDCVENEV-----GVLTISGPNVFAGYLQEDQN 454
Cdd:PRK12467 1871 ETAVdvthwtCRRKDLEG--RDSVPIGQPIA----------NLSTYILDASLNPVpigvaGELYLGGVGLARGYLNRPAL 1938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 455 KSLWL-----DLGDGRQWlNTGDLARRDAQGYFWLTGR-RKELIIRgGHNIDPATIEEPLHRHPAVQIAAAIGRpDVHAG 528
Cdd:PRK12467 1939 TAERFvadpfGTVGSRLY-RTGDLARYRADGVIEYLGRiDHQVKIR-GFRIELGEIEARLREQGGVREAVVIAQ-DGANG 2015
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 529 ELPVAYVQLKAGATATETELDTFIRGMIGE--RAAIPKRI---HIV--DAMPLTAVGKIFKPELKR 587
Cdd:PRK12467 2016 KQLVAYVVPTDPGLVDDDEAQVALRAILKNhlKASLPEYMvpaHLVflARMPLTPNGKLDRKALPA 2081
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
236-585 |
3.66e-08 |
|
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: 56.33 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGagMGPGKTVFCGLPLFHVNAVLATgLVPFSRGAhVVLGTPQGYRGdgVVK 315
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIQHFRSLFN--ITSEDILFLTSPLTFDPSVVEI-FLSLSSGA-TLLIVPTSVKV--LPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 316 RFWEIV-EHHRINFFSAVPTLYSALLDVPVDGRNI---DSLEYGLCGAAPMP----VEVFRTFQDRTgvRILEGYGLTEG 387
Cdd:cd17654 200 KLADILfKRHRITVLQATPTLFRRFGSQSIKSTVLsatSSLRVLALGGEPFPslviLSSWRGKGNRT--RIFNIYGITEV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 388 ACVSSVNPPGGERRLGSIGLRIPGQMMkavilddagrYVRDCVENEV-GVLTISGPNVfAGYLQEDQNKSLwldlgdgRQ 466
Cdd:cd17654 278 SCWALAYKVPEEDSPVQLGSPLLGTVI----------EVRDQNGSEGtGQVFLGGLNR-VCILDDEVTVPK-------GT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 467 WLNTGDLARRDAQGYFWLtGRRKELIIRGGHNIDPATIEEPLHRH-PAVQIAAAIgrpdvHAGELPVAYVQLKAGATATE 545
Cdd:cd17654 340 MRATGDFVTVKDGELFFL-GRKDSQIKRRGKRINLDLIQQVIESClGVESCAVTL-----SDQQRLIAFIVGESSSSRIH 413
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1142773712 546 TELDTFIRgmigERAAIPKRIHIVDAMPLTAVGKIFKPEL 585
Cdd:cd17654 414 KELQLTLL----SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
367-580 |
5.44e-08 |
|
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: 55.56 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 367 FRTFQDRTGVRILEGYGLTEGACVS--SVNPPGGERRLGSIGLriPGQMMKAVILDDAGRYVRDCVeneVGVLTISGPNV 444
Cdd:cd17656 263 FKEMLHEHNVHLHNHYGPSETHVVTtyTINPEAEIPELPPIGK--PISNTWIYILDQEQQLQPQGI---VGELYISGASV 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 445 FAGYLQEDQ--NKSLWLDLGDGRQWL-NTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIG 521
Cdd:cd17656 338 ARGYLNRQEltAEKFFPDPFDPNERMyRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLD 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142773712 522 RPDVHAGELPVAYVQlkAGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKI 580
Cdd:cd17656 418 KADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEY-MIPSFFVPLDQLPLTPNGKV 473
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
293-587 |
6.04e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.21 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVLGTPQGYRGDGVVKRFweiVEHHRINFFSAVPTLYSAL---LDVPVDGRNIDSLEYGLCGAAPMPVEVFRT 369
Cdd:PRK10252 660 PFIAGAKLVMAEPEAHRDPLAMQQF---FAEYGVTTTHFVPSMLAAFvasLTPEGARQSCASLRQVFCSGEALPADLCRE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 370 FQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIP-------GQMMkavILDDAGRYVRDCVeneVGVLTISGP 442
Cdd:PRK10252 737 WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPigypvwnTGLR---ILDARMRPVPPGV---AGDLYLTGI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 443 NVFAGYL-QEDQNKSLWLD--LGDGRQWLNTGDLARRDAQGYFWLTGRRKELI-IRgGHNIDPATIEEPLHRHPAVQIAA 518
Cdd:PRK10252 811 QLAQGYLgRPDLTASRFIAdpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLkIR-GQRIELGEIDRAMQALPDVEQAV 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 519 AIGRPDVHAGELP------VAYVQLKAGATATETELDTFIRGMIGErAAIPKRIHIVDAMPLTAVGKIF-----KPELKR 587
Cdd:PRK10252 890 THACVINQAAATGgdarqlVGYLVSQSGLPLDTSALQAQLRERLPP-HMVPVVLLQLDQLPLSANGKLDrkalpLPELKA 968
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
236-491 |
2.92e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.83 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGMGPGKT--VFCG-LPLFHVNAvLATGLVPFSRGAHVVLGTPQGY---- 308
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEdeTYCSyLPLAHIME-FGVTNIFLARGALIGFGSPRTLtdtf 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 309 ---RGDgvvkrfweiVEHHRINFFSAVP------------------TL--------YSALL-------DVP--------- 343
Cdd:PTZ00216 351 arpHGD---------LTEFRPVFLIGVPrifdtikkaveaklppvgSLkrrvfdhaYQSRLralkegkDTPywnekvfsa 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 344 ---VDGRNIDSLeygLCGAAPMPVEVfrtfQDRTGV---RILEGYGLTEGACVssvnppGGERRLGSIGLRIPGQMMKAV 417
Cdd:PTZ00216 422 praVLGGRVRAM---LSGGGPLSAAT----QEFVNVvfgMVIQGWGLTETVCC------GGIQRTGDLEPNAVGQLLKGV 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 418 ---ILDDAGRYVRDCVENEvGVLTISGPNVFAGYL-QEDQNKSLwLDlGDGrqWLNTGDLARRDAQGYFWLTGRRKEL 491
Cdd:PTZ00216 489 emkLLDTEEYKHTDTPEPR-GEILLRGPFLFKGYYkQEELTREV-LD-EDG--WFHTGDVGSIAANGTLRIIGRVKAL 561
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
192-449 |
8.23e-07 |
|
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: 52.05 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 192 AGVRGAVPRHVAIHdFDSAMSRESGDSLliPRRFEA---DDISSYFCTGGTTGLPKIAIRRHGNEVANAWSVGQVVGAGM 268
Cdd:cd05921 129 VVSRNAVAGRGAIS-FAELAATPPTAAV--DAAFAAvgpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 269 GPGKTVFCGLPLFHV---NAVLatGLVPFSRGA-HVVLGTPQGYRGDGVVKRFWEIVEhhriNFFSAVPTLYSALL---- 340
Cdd:cd05921 206 EEPPVLVDWLPWNHTfggNHNF--NLVLYNGGTlYIDDGKPMPGGFEETLRNLREISP----TVYFNVPAGWEMLVaale 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 341 -DVPVDGRNIDSLEYGLCGAAPMPVEVFRTFQD----RTGVRI--LEGYGLTEGA--CVSSVNPpggERRLGSIGLRIPG 411
Cdd:cd05921 280 kDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAptATFTHWP---TERSGLIGLPAPG 356
|
250 260 270
....*....|....*....|....*....|....*...
gi 1142773712 412 QMMKAVILDdaGRYvrdcvenEVGVltiSGPNVFAGYL 449
Cdd:cd05921 357 TELKLVPSG--GKY-------EVRV---KGPNVTPGYW 382
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
293-580 |
2.87e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 293 PFSRGAHVVLGTPQGYRGDgvvKRFWEIVEHHRINFFSAVPTLYSALLDVPVDGrNIDSLEYGLCGAAPMPVEVF-RTFQ 371
Cdd:PRK05691 1335 PLITGCRLVLAGPGEHRDP---QRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRnRVLQ 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 372 DRTGVRILEGYGLTEGAcvssVNPPGGERRlGSIGLRIP-GQMMKAV---ILDDAGRYVRDCVeneVGVLTISGPNVFAG 447
Cdd:PRK05691 1411 RLPQVQLHNRYGPTETA----INVTHWQCQ-AEDGERSPiGRPLGNVlcrVLDAELNLLPPGV---AGELCIGGAGLARG 1482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 448 YL----QEDQNKSLWLDLGDGRQWLNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRP 523
Cdd:PRK05691 1483 YLgrpaLTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVRE 1562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1142773712 524 DVHAGELpVAYVQLKAGATATETELDTFIRGMIGERaAIPKRIHIVDAMPLTAVGKI 580
Cdd:PRK05691 1563 GAAGAQL-VGYYTGEAGQEAEAERLKAALAAELPEY-MVPAQLIRLDQMPLGPSGKL 1617
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
356-491 |
4.64e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 49.63 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 356 LCGAAPMPVEVFRTFQDRTGVRILEGYGLTEGACVSSVNPPGGERRLGSIGLRIPGQMMKaviLDDAGRYVRDCVENEV- 434
Cdd:PLN02614 392 LSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIR---LESVPEMEYDALASTPr 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142773712 435 GVLTISGPNVFAGYLQ-EDQNKSLWLDlgdgrQWLNTGDLARRDAQGYFWLTGRRKEL 491
Cdd:PLN02614 469 GEICIRGKTLFSGYYKrEDLTKEVLID-----GWLHTGDVGEWQPNGSMKIIDRKKNI 521
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
321-580 |
5.18e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 321 VEHHRINFFSAVPTLYSALLDVPVDGrnIDSLEYGLCGAAPMPVEVFRTFQDR-TGVRILEGYGLTEgaC--------VS 391
Cdd:PRK05691 3956 VQAQGITVLESVPSLIQGMLAEDRQA--LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAE--CsddvaffrVD 4031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 392 SVNPPGGERRLGSiglriPGQMMKAVILDDAGRYVRdcvENEVGVLTISGPNVFAGYLQEDQNKSLWLDL----GDGRQW 467
Cdd:PRK05691 4032 LASTRGSYLPIGS-----PTDNNRLYLLDEALELVP---LGAVGELCVAGTGVGRGYVGDPLRTALAFVPhpfgAPGERL 4103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 468 LNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQiAAAIGRPDVHAGELPVAYVQLKAGATATETE 547
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVR-EAAVAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
250 260 270
....*....|....*....|....*....|....*...
gi 1142773712 548 LDTFIRGMigeRAAIPKRI---H--IVDAMPLTAVGKI 580
Cdd:PRK05691 4183 LERIKQRL---RAELPDYMvplHwlWLDRLPLNANGKL 4217
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
278-580 |
1.42e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.11 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 278 LPLFHvNAVLATGLVPFSRGAHVVLGTPQGY-RGDGVVKRFWEIVEHHRINFFSAVPTL---YSALLDVPVDGR------ 347
Cdd:PRK07769 228 LPFFH-DMGLITVLLPALLGHYITFMSPAAFvRRPGRWIRELARKPGGTGGTFSAAPNFafeHAAARGLPKDGEppldls 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 348 NIDSLeygLCGAAPMPVEVFRTFQDRTG------VRILEGYGLTEGACVSSVNPPGGERRLGSIG---------LRIP-- 410
Cdd:PRK07769 307 NVKGL---LNGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVSTTPMDEEPTVIYVDrdelnagrfVEVPad 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 411 ----------GQMMK---AVILD-DAGRYVRDcveNEVGVLTISGPNVFAGY--------------LQEDQNKSLWLDLG 462
Cdd:PRK07769 384 apnavaqvsaGKVGVsewAVIVDpETASELPD---GQIGEIWLHGNNIGTGYwgkpeetaatfqniLKSRLSESHAEGAP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 463 DGRQWLNTGDLARRdAQGYFWLTGRRKELIIRGGHNIDPATIE------EPLHRH--------PAVQIAAAIgRPDVHAG 528
Cdd:PRK07769 461 DDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEytaqeaTKALRTgyvaafsvPANQLPQVV-FDDSHAG 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 529 ---------ELPVAYVQLKAGATATETE--LDTfIRGMIGERAAIPKR-IHIVDA--MPLTAVGKI 580
Cdd:PRK07769 539 lkfdpedtsEQLVIVAERAPGAHKLDPQpiADD-IRAAIAVRHGVTVRdVLLVPAgsIPRTSSGKI 603
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
10-449 |
1.50e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 41.79 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 10 VLRIENQGPPADLPASTYEMIGRGAAidpSAPALSFFLRADDHRKPLRWTYAALLRDITRAANMFSRLGIDRHAVVAYVL 89
Cdd:PRK08180 25 TIYLRSAEPLGDYPRRLTDRLVHWAQ---EAPDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 90 PNLPETHFVIWGGEAAGI-VCAINPllegpaiasllkaANAKVlvtlapfpgSDIWSKIQPVLSEVPSlqSLVLIDLAER 168
Cdd:PRK08180 102 GNSIEHALLALAAMYAGVpYAPVSP-------------AYSLV---------SQDFGKLRHVLELLTP--GLVFADDGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 169 VQgwRRIAARAMQRRECKRLHGRAGVRGAVPrhvaihdFDSAMSRESGDSllIPRRFEA---DDISSYFCTGGTTGLPKI 245
Cdd:PRK08180 158 FA--RALAAVVPADVEVVAVRGAVPGRAATP-------FAALLATPPTAA--VDAAHAAvgpDTIAKFLFTSGSTGLPKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 246 AIRRHGNEVANAWSVGQVVGAgMGPGKTVFCG-LPLFHV---NAVLatGLVPFSRGAHvvlgtpqgYRGDG--VVKRFWE 319
Cdd:PRK08180 227 VINTHRMLCANQQMLAQTFPF-LAEEPPVLVDwLPWNHTfggNHNL--GIVLYNGGTL--------YIDDGkpTPGGFDE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 320 IVEHHR-IN---FFSaVPTLYSALLDV----PVDGRNIDS-LEYGLCGAAPMPVEVF----RTFQDRTG--VRILEGYGL 384
Cdd:PRK08180 296 TLRNLReISptvYFN-VPKGWEMLVPAlerdAALRRRFFSrLKLLFYAGAALSQDVWdrldRVAEATCGerIRMMTGLGM 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1142773712 385 TEGA-CVSSVNPPGGerRLGSIGLRIPGQMMKAVILDdaGRYvrdcvenEVGVltiSGPNVFAGYL 449
Cdd:PRK08180 375 TETApSATFTTGPLS--RAGNIGLPAPGCEVKLVPVG--GKL-------EVRV---KGPNVTPGYW 426
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
414-580 |
1.56e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.42 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 414 MKAVILDDAGRYVRDcveNEVGVLTISGPNVFAGYLQEDQ--NKSLWLDlgDGRQWLNTGDLARRDaQGYFWLTGRRKEL 491
Cdd:PRK04813 327 SPLLIIDEEGTKLPD---GEQGEIVISGPSVSKGYLNNPEktAEAFFTF--DGQPAYHTGDAGYLE-DGLLFYQGRIDFQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 492 IIRGGHNIDPATIEEPLHRHPAVQIAAAIGRPDVHAGELPVAYVQLKAGATATETELDTFIRGMIGERAA---IPKRIHI 568
Cdd:PRK04813 401 IKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMeymIPRKFIY 480
|
170
....*....|..
gi 1142773712 569 VDAMPLTAVGKI 580
Cdd:PRK04813 481 RDSLPLTPNGKI 492
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
228-386 |
3.52e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 40.13 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 228 DDISSYFCTGGTTGLPKIaIRRHGNEVAN-AWSVGQV-VGAGMGPGKTVFC--GLPLFhvnavlaTGLVPFSRGAH---- 299
Cdd:COG1541 83 EEIVRIHASSGTTGKPTV-VGYTRKDLDRwAELFARSlRAAGVRPGDRVQNafGYGLF-------TGGLGLHYGAErlga 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 300 -VVLGTPqgyrgdGVVKRFWEIVEHHRINFFSAVPTLYSALLDVpVDGRNID----SLEYGLCGAAPMPVEVFRTFQDRT 374
Cdd:COG1541 155 tVIPAGG------GNTERQLRLMQDFGPTVLVGTPSYLLYLAEV-AEEEGIDprdlSLKKGIFGGEPWSEEMRKEIEERW 227
|
170
....*....|..
gi 1142773712 375 GVRILEGYGLTE 386
Cdd:COG1541 228 GIKAYDIYGLTE 239
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
236-580 |
5.54e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.15 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 236 TGGTTGLPKIAIRRHGNEVANAWSVgqVVGAGMGPGKtvfCGLPLFHVNAVLATG--LVPFSRGAHVVLgTPQGYRGdgv 313
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAV--IERFGMRADD---CELHFYSINFDAASErlLVPLLCGARVVL-RAQGQWG--- 2411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 314 VKRFWEIVEHHRINFFSAVPTlYSALLDVPVDGRNiDSLEYGLC---GAAPMPVEVFRTFQDRTGVRILEGYGLTEG--- 387
Cdd:PRK05691 2412 AEEICQLIREQQVSILGFTPS-YGSQLAQWLAGQG-EQLPVRMCitgGEALTGEHLQRIRQAFAPQLFFNAYGPTETvvm 2489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 388 --ACVSSVNPPGGERRL--GS-IGLRIpgqmmkAVILDDAGRYVRdcvENEVGVLTISGPNVFAGY-----LQEDQNKSL 457
Cdd:PRK05691 2490 plACLAPEQLEEGAASVpiGRvVGARV------AYILDADLALVP---QGATGELYVGGAGLAQGYhdrpgLTAERFVAD 2560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142773712 458 WLDLGDGRQWlNTGDLARRDAQGYFWLTGRRKELIIRGGHNIDPATIEEPLHRHPAVQIAAAIGRpDVHAGELPVAYVqL 537
Cdd:PRK05691 2561 PFAADGGRLY-RTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYL-V 2637
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1142773712 538 KAGATATETELDTFIRGMIGERAA------IPKRIHIVDAMPLTAVGKI 580
Cdd:PRK05691 2638 SAVAGQDDEAQAALREALKAHLKQqlpdymVPAHLILLDSLPLTANGKL 2686
|
|
| |
