|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1-451 |
0e+00 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 804.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 1 MIFSDWPWRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVL 80
Cdd:PRK09029 2 MIFSDWPWRHWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 81 PVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHL 160
Cdd:PRK09029 82 PLNPQLPQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 161 ASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAGCTHASLVPTQLWRLLVNRS-SVS 239
Cdd:PRK09029 162 ASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDKQPLEQALAGCTHASLVPTQLWRLLDNRSePLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 240 LKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADVGSPLPGREVKIVNNEVWLRAASMAEGYWRN 319
Cdd:PRK09029 242 LKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRADGLAGVGSPLPGREVKLVDGEIWLRGASLALGYWRQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 320 GQLVSLVNDEGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVME 399
Cdd:PRK09029 322 GQLVPLVNDEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 727407383 400 YDHESV--DLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALKEWVQRQQ 451
Cdd:PRK09029 402 SDSEAAvvNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKEWVAQQL 455
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
135-447 |
1.41e-144 |
|
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: 415.58 E-value: 1.41e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK-QPLEQ 213
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERnQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 214 MLA--GCTHASLVPTQLWRLLVNR----SSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADG-- 285
Cdd:cd17630 81 DLAppGVTHVSLVPTQLQRLLDSGqgpaALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGfg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 LADVGSPLPGREVKIVNN-EVWLRAASMAEGYWRnGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:cd17630 161 RGGVGVLLPGRELRIVEDgEIWVGGASLAMGYLR-GQLVPEFNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 364 PEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYD--HESVDLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQ 441
Cdd:cd17630 240 PEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRgpADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
....*.
gi 727407383 442 ALKEWV 447
Cdd:cd17630 320 ALRAWL 325
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
30-443 |
9.81e-121 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 359.07 E-value: 9.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 30 WRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPDgE 109
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 110 NTFPALTSLHIQRVEGAHAAA------WQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:TIGR01923 81 LEEKDFQADSLDRIEAAGRYEtslsasFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 184 LFHVSGQGIMWRWLYAGARMTVRDKQP-LEQMLAG--CTHASLVPTQLWRLLVNRSS-VSLKAVLLGGAAIPIELTEQAR 259
Cdd:TIGR01923 161 LYHISGLSILFRWLIEGATLRIVDKFNqLLEMIANerVTHISLVPTQLNRLLDEGGHnENLRKILLGGSAIPAPLIEEAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 260 EQGIRCFCGYGLTEFASTVCAKEADGLA---DVGSPLPGREVKIVN------NEVWLRAASMAEGYWRNGQLVSLVNDEG 330
Cdd:TIGR01923 241 QYGLPIYLSYGMTETCSQVTTATPEMLHarpDVGRPLAGREIKIKVdnkeghGEIMVKGANLMKGYLYQGELTPAFEQQG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 331 WYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM--EYDHESVDL 407
Cdd:TIGR01923 321 WFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIvsESDISQAKL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 727407383 408 SEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQAL 443
Cdd:TIGR01923 401 IAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-451 |
7.07e-92 |
|
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: 285.55 E-value: 7.07e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpq 88
Cdd:COG0318 6 RRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 plleellpnltlqfalvpdgentfPALTSLHIQRVEgAHAAAwqptRL---CSMTLTSGSTGLPKAAVHTYQAHLASAEG 165
Cdd:COG0318 81 ------------------------PRLTAEELAYIL-EDSGA----RAlvtALILYTSGTTGRPKGVMLTHRNLLANAAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 166 VLSLIPFGDHDDWLLSLPLFHVSGQGI-MWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLL--VNRSS 237
Cdd:COG0318 132 IAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPERVLEliereRVTVLFGVPTMLARLLrhPEFAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 238 V---SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD----VGSPLPGREVKIVNN------ 303
Cdd:COG0318 212 YdlsSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGERrpgsVGRPLPGVEVRIVDEdgrelp 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -----EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAV 377
Cdd:COG0318 292 pgevgEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLdEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 378 LQVFIVPVADKEFGHRPVAVMEY-DHESVD---LSEWVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKEWVQRQ 450
Cdd:COG0318 372 AEAAVVGVPDEKWGERVVAFVVLrPGAELDaeeLRAFLRERLARYKVPRRVEfvdELP---RTASGKIDRRALRERYAAG 448
|
.
gi 727407383 451 Q 451
Cdd:COG0318 449 A 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
135-438 |
1.94e-89 |
|
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: 275.32 E-value: 1.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQM 214
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LA-----GCTHASLVPTQLWRLLVNRSSV-----SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEA 283
Cdd:cd04433 81 LEliereKVTILLGVPTLLARLLKAPESAgydlsSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 284 DGLA----DVGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTI 347
Cdd:cd04433 161 DDDArkpgSVGRPVPGVEVRIVDPdggelppgeigELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDeDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEY----DHESVDLSEWVKDKLARFQQPVR 423
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpgaDLDAEELRAHVRERLAPYKVPRR 320
|
330
....*....|....*
gi 727407383 424 WLTLPPELKNGGIKI 438
Cdd:cd04433 321 VVFVDALPRTASGKI 335
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
32-445 |
7.10e-62 |
|
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: 206.43 E-value: 7.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfalvpdgent 111
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR-------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 112 fpaLTslhiqrvegAHAAAWQ-------PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEG-VLSLiPFGDHDDWLLSLP 183
Cdd:cd05912 60 ---LT---------PNELAFQlkdsdvkLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGsALNL-GLTEDDNWLCALP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 184 LFHVSGQGIMWRWLYAGARMTVRDKQPLEQML-----AGCTHASLVPTQLWRLLV---NRSSVSLKAVLLGGAAIPIELT 255
Cdd:cd05912 127 LFHISGLSILMRSVIYGMTVYLVDKFDAEQVLhlinsGKVTIISVVPTMLQRLLEilgEGYPNNLRCILLGGGPAPKPLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 256 EQAREQGIRCFCGYGLTEFASTVCA-KEADGLADVGS---PLPGREVKIVNN--------EVWLRAASMAEGYWRNGQLV 323
Cdd:cd05912 207 EQCKEKGIPVYQSYGMTETCSQIVTlSPEDALNKIGSagkPLFPVELKIEDDgqppyevgEILLKGPNVTKGYLNRPDAT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 324 SLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEY 400
Cdd:cd05912 287 EESFENGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAfvVSER 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 727407383 401 DHESVDLSEWVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKE 445
Cdd:cd05912 367 PISEEELIAYCSEKLAKYKVPKKIYfvdELP---RTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
13-450 |
1.19e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 199.80 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 13 QVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:PRK03640 13 FLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 93 ELLPNLTLQF---------ALVPDGENTFPALTSLHIQRVEgaHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASA 163
Cdd:PRK03640 93 WQLDDAEVKClitdddfeaKLIPGISVKFAELMNGPKEEAE--IQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 164 EG-VLSLipfG--DHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLLV-- 233
Cdd:PRK03640 171 VGsALNL---GltEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKllqtgGVTIISVVSTMLQRLLErl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 234 --NRSSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCA-KEADGLADVGS---PLPGREVKIVNN---- 303
Cdd:PRK03640 248 geGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVTlSPEDALTKLGSagkPLFPCELKIEKDgvvv 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 ------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPA 376
Cdd:PRK03640 328 ppfeegEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPG 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 377 VLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKEWVQRQ 450
Cdd:PRK03640 408 VAEAGVVGVPDDKWGQVPVAfvVKSGEVTEEELRHFCEEKLAKYKVPKRFYfveELP---RNASGKLLRHELKQLVEEM 483
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
9-438 |
2.29e-55 |
|
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: 189.74 E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpq 88
Cdd:cd17631 2 RRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 plleellpnltlqFALVPDgENTFPALTSlhiqrveGAHAAAWQPTRLCsmtLTSGSTGLPKAAVHTYQAHLASAEGVLS 168
Cdd:cd17631 77 -------------FRLTPP-EVAYILADS-------GAKVLFDDLALLM---YTSGTTGRPKGAMLTHRNLLWNAVNALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 169 LIPFGDHDDWLLSLPLFHVSGQGIMW-RWLYAGARMTVRDKQPLEQMLAGC-----THASLVPTQLWRLL--VNRSSV-- 238
Cdd:cd17631 133 ALDLGPDDVLLVVAPLFHIGGLGVFTlPTLLRGGTVVILRKFDPETVLDLIerhrvTSFFLVPTMIQALLqhPRFATTdl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 -SLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADG----LADVGSPLPGREVKIVNN---------- 303
Cdd:cd17631 213 sSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDhrrkLGSAGRPVFFVEVRIVDPdgrevppgev 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVF 381
Cdd:cd17631 293 gEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 382 IVPVADKEFGHRPVAVM------EYDHEsvDLSEWVKDKLARFQQPVR---WLTLPpelKNGGIKI 438
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVvprpgaELDED--ELIAHCRERLARYKIPKSvefVDALP---RNATGKI 433
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-445 |
1.55e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 186.93 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQ 88
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 PlleellpnltlQFA----------------LVPDGENTFPALTSL-HIQRVEGAHAA----------AW---QPTR--- 135
Cdd:PRK06187 93 E-----------EIAyilndaedrvvlvdseFVPLLAAILPQLPTVrTVIVEGDGPAAplapevgeyeELlaaASDTfdf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 136 -------LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK 208
Cdd:PRK06187 162 pdidendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 -QP---LEQMLA-GCTHASLVPTqLWRLLVNRSSV------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:PRK06187 242 fDPenlLDLIETeRVTFFFAVPT-IWQMLLKAPRAyfvdfsSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 277 TV-CAKEADGLAD-------VGSPLPGREVKIVNN-------------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATR 335
Cdd:PRK06187 321 VVsVLPPEDQLPGqwtkrrsAGRPLPGVEARIVDDdgdelppdggevgEIIVRGPWLMQGYWNRPEATAETIDGGWLHTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 336 DRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHE--SVDLSEW 410
Cdd:PRK06187 401 DVGYIDeDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAvvVLKPGATldAKELRAF 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 727407383 411 VKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKE 445
Cdd:PRK06187 481 LRGRLAKFKLPKRIAfvdELP---RTSVGKILKRVLRE 515
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-355 |
4.06e-53 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 183.67 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 8 WRHWRQVRGETIALRLND-EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN--- 83
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNprl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ---------------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAH---AAAWQPTRLCSM 139
Cdd:pfam00501 81 paeelayiledsgakvlitddALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPpppPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 140 TLTSGSTGLPKAAVHTYQAHLASAEGVLSLIP----FGDHDDWLLSLPLFHVSGQG-IMWRWLYAGARMTVRDKQPLEQM 214
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LA--------GCTHASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPIELTEQAREQGIRCF-CGYGLTEfASTVC 279
Cdd:pfam00501 241 AAllelieryKVTVLYGVPT-LLNMLLEagapkrALLSSLRLVLSGGAPLPPELARRFRELFGGALvNGYGLTE-TTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 280 AKEADGLAD------VGSPLPGREVKIVNN------------EVWLRAASMAEGYWRNGQL-VSLVNDEGWYATRDRGEM 340
Cdd:pfam00501 319 TTPLPLDEDlrslgsVGRPLPGTEVKIVDDetgepvppgepgELCVRGPGVMKGYLNDPELtAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*.
gi 727407383 341 H-NGKLTIVGRLDNLF 355
Cdd:pfam00501 399 DeDGYLEIVGRKKDQI 414
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
142-443 |
2.08e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 174.85 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIpfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD----------KQPL 211
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRL--GGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsagfdptalPRAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 212 EQMLAGCTHASLVPTQLWRLLVNRSSV----SLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEfastvcakEADGLA 287
Cdd:PRK07824 121 AELGGGRRYTSLVPMQLAKALDDPAATaalaELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSE--------TSGGCV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 DVGSPLPGREVKIVNNEVWLRAASMAEGYwRNGQLVSLVNDEGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:PRK07824 193 YDGVPLDGVRVRVEDGRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV----DLSEWVKDKLARFQQPvRWLTLPPELKNGGI-KISRQA 442
Cdd:PRK07824 272 EAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAptleALRAHVARTLDRTAAP-RELHVVDELPRRGIgKVDRRA 350
|
.
gi 727407383 443 L 443
Cdd:PRK07824 351 L 351
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-444 |
1.17e-48 |
|
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: 172.75 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 15 RGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEEL 94
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 95 LPNLTLQFALVPDGENTFpaltslhiqrVEGAHAAAWQPTR----LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLI 170
Cdd:cd05936 92 LNDSGAKALIVAVSFTDL----------LAAGAPLGERVALtpedVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 171 PF-GDHDDWLL-SLPLFHVSGQGI-MWRWLYAGARM----TVRDKQPLEQMLA-GCTHASLVPTqLWRLLVNRSSV---- 238
Cdd:cd05936 162 EDlLEGDDVVLaALPLFHVFGLTVaLLLPLALGATIvlipRFRPIGVLKEIRKhRVTIFPGVPT-MYIALLNAPEFkkrd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 --SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLADVGS---PLPGREVKIVN---------- 302
Cdd:cd05936 241 fsSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSigiPLPGTEVKIVDddgeelppge 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 -NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:cd05936 321 vGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 381 FIVPVADKEFGHRPVA-VMEYDHESV---DLSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05936 401 AVVGVPDPYSGEAVKAfVVLKEGASLteeEIIAFCREQLAGYKVP-RQVEFRDELpKSAVGKILRRELR 468
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
142-451 |
8.87e-48 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 170.17 E-value: 8.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGvlslipFGDHDDW-----LLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQ--- 213
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQG------FQRYFQLqqvnsFCVLPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSgqe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 214 MLAGCTHA--SLVPTQLWRLLVNRSS--VSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCA-KEADGLA- 287
Cdd:PRK07445 202 LPPNPSDFflSLVPTQLQRLLQLRPQwlAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATlKPDDFLAg 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 --DVGSPLPGREVKIVNN---EVWLRAASMAEGYWRNgqlvsLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEG 361
Cdd:PRK07445 282 nnSSGQVLPHAQITIPANqtgNITIQAQSLALGYYPQ-----ILDSQGIFETDDLGYLdAQGYLHILGRNSQKIITGGEN 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 362 IQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSE---WVKDKLARFQQPVRWLTLPPELKNGGIKI 438
Cdd:PRK07445 357 VYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEElktAIKDQLSPFKQPKHWIPVPQLPRNPQGKI 436
|
330
....*....|...
gi 727407383 439 SRQALKEWVQRQQ 451
Cdd:PRK07445 437 NRQQLQQIAVQRL 449
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
27-431 |
2.11e-47 |
|
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: 168.93 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 27 QLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVnpqlpqplleellpnltlqFAlvp 106
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI-------------------YP--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 107 dgenTFPALTSLHIQRVEGAHAA-AWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLF 185
Cdd:cd05907 63 ----TSSAEQIAYILNDSEAKALfVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 186 HVSGQgIMWRWLYAGARMTVRDKQPLEQMLAGCTHASlvPTQL------WRLLVNRSSV-----------------SLKA 242
Cdd:cd05907 139 HVFER-RAGLYVPLLAGARIYFASSAETLLDDLSEVR--PTVFlavprvWEKVYAAIKVkavpglkrklfdlavggRLRF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 243 VLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIV-NNEVWLRAASMAEGYWRN 319
Cdd:cd05907 216 AASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDnrIGTVGKPLPGVEVRIAdDGEILVRGPNVMLGYYKN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 320 GQLVSLVNDE-GWYATRDRGEMH-NGKLTIVGRLDNLFF-SGGEGIQPEEVERVIAAHPAVLQV------------FIVP 384
Cdd:cd05907 296 PEATAEALDAdGWLHTGDLGEIDeDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAvvigdgrpflvaLIVP 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 385 VAD------KEFGHRPVAVME-YDHESV--DLSEWVKD---KLARFQQPVRWLTLPPEL 431
Cdd:cd05907 376 DPEaleawaEEHGIAYTDVAElAANPAVraEIEAAVEAanaRLSRYEQIKKFLLLPEPF 434
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-444 |
1.97e-41 |
|
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: 152.45 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleellpnltlqfAL 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT------------------AL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 105 VPDgentfpALTslHIQRVEGAHAAAwqpTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL 184
Cdd:cd05934 63 RGD------ELA--YIIDHSGAQLVV---VDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 185 FHVSGQGIMW-RWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLLVNRSSVSLKAVLL---GGAAIPIELT 255
Cdd:cd05934 132 FHINAQAVSVlAALSVGATLVLLPRFSASRFWSdvrryGATVTNYLGAMLSYLLAQPPSPDDRAHRLraaYGAPNPPELH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 256 EQAREQ-GIRCFCGYGLTE----FASTVCAKEADGLAdvGSPLPGREVKIVNN-----------EVWLRAA---SMAEGY 316
Cdd:cd05934 212 EEFEERfGVRLLEGYGMTEtivgVIGPRDEPRRPGSI--GRPAPGYEVRIVDDdgqelpagepgELVIRGLrgwGFFKGY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 317 WRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADkEFGHRPV 395
Cdd:cd05934 290 YNMPEATAEAMRNGWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPD-EVGEDEV 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 396 AVMEYDHES-----VDLSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05934 369 KAVVVLRPGetldpEELFAFCEGQLAYFKVP-RYIRFVDDLpKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
19-445 |
7.47e-38 |
|
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: 142.81 E-value: 7.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVV-EGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleellpn 97
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNP------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 98 ltlqfalvpdgenTFPALTSLHIqrVEGAHAAAWqpTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDD 177
Cdd:cd05941 70 -------------SYPLAELEYV--ITDSEPSLV--LDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 178 WLLSLPLFHVSG--QGIMWRwLYAGARMTVRDKQPLEQMLAGCTHASL-----VPTQLWRLL----------VNRSSVSL 240
Cdd:cd05941 133 LLHVLPLHHVHGlvNALLCP-LFAGASVEFLPKFDPKEVAISRLMPSItvfmgVPTIYTRLLqyyeahftdpQFARAAAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 241 KAVLL---GGAAIPIELTEQARE-QGIRCFCGYGLTEFA-STVCAKEADGLA-DVGSPLPGREVKIVNN----------- 303
Cdd:cd05941 212 ERLRLmvsGSAALPVPTLEEWEAiTGHTLLERYGMTEIGmALSNPLDGERRPgTVGMPLPGVQARIVDEetgeplprgev 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYWRNGQ-LVSLVNDEGWYATRDRGEM-HNGKLTIVGRL-DNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:cd05941 292 gEIQVRGPSVFKEYWNKPEaTKEEFTDDGWFKTGDLGVVdEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSE 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727407383 380 VFIVPVADKEFGHRPVAVMEYDHESV-----DLSEWVKDKLARFQQPVRwLTLPPEL-KNGGIKISRQALKE 445
Cdd:cd05941 372 CAVIGVPDPDWGERVVAVVVLRAGAAalsleELKEWAKQRLAPYKRPRR-LILVDELpRNAMGKVNKKELRK 442
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
24-420 |
2.51e-37 |
|
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: 142.35 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 24 NDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFA 103
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 104 LV-PDG-ENTFPALTSLHIQ--------RVEGAH------------AAAWQPTR-----------LCSmtltSGSTGLPK 150
Cdd:cd05911 87 FTdPDGlEKVKEAAKELGPKdkiivlddKPDGVLsiedllsptlgeEDEDLPPPlkdgkddtaaiLYS----SGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 151 AAVHTYQAHLASAEGVLSLIP--FGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAGC-----THASL 223
Cdd:cd05911 163 GVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIekykiTFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 224 VPTQLwRLLVNRSSV------SLKAVLLGGAAIPIELTEQAREQGIRCFC--GYGLTE--FASTVCAKEADGLADVGSPL 293
Cdd:cd05911 243 VPPIA-AALAKSPLLdkydlsSLRVILSGGAPLSKELQELLAKRFPNATIkqGYGMTEtgGILTVNPDGDDKPGSVGRLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 294 PGREVKIVNN------------EVWLRAASMAEGYWRNGQ-LVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGG 359
Cdd:cd05911 322 PNVEAKIVDDdgkdslgpnepgEICVRGPQVMKGYYNNPEaTKETFDEDGWLHTGDIGYFdEDGYLYIVDRKKELIKYKG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 360 EGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VMEYDHESV---DLSEWVKDKLARFQQ 420
Cdd:cd05911 402 FQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAyVVRKPGEKLtekEVKDYVAKKVASYKQ 466
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-443 |
8.72e-37 |
|
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: 139.97 E-value: 8.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellpnl 98
Cdd:cd05930 4 VAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLD--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 tlqfalvPDgentFPA--LTSLhiqrVEGAHAAAW--QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGD 174
Cdd:cd05930 69 -------PS----YPAerLAYI----LEDSGAKLVltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 175 HDDWL-LSLPLFHVSGQGIMWrWLYAGA------RMTVRDKQPLEQMLA--GCTHASLVPTqLWRLLVN----RSSVSLK 241
Cdd:cd05930 134 GDRVLqFTSFSFDVSVWEIFG-ALLAGAtlvvlpEEVRKDPEALADLLAeeGITVLHLTPS-LLRLLLQelelAALPSLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 242 AVLLGGAAIPIELTEQAREQGIRC--FCGYGLTE--FAST--VCAKEADGLADV--GSPLPGREVKIVNN---------- 303
Cdd:cd05930 212 LVLVGGEALPPDLVRRWRELLPGArlVNLYGPTEatVDATyyRVPPDDEEDGRVpiGRPIPNTRVYVLDEnlrpvppgvp 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYWRNGQLV--SLVND--EGW---YATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:cd05930 292 gELYIGGAGLARGYLNRPELTaeRFVPNpfGPGermYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAH 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 375 PAVLQVFIVPVADKEFGHRPVA--VMEYDHE--SVDLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05930 372 PGVREAAVVAREDGDGEKRLVAyvVPDEGGEldEEELRAHLAERLPDYMVPSAFVVLDalPLTPNG--KVDRKAL 444
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-398 |
4.24e-36 |
|
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: 137.90 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPd 107
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 108 gentfpaltslhiqRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV 187
Cdd:cd05903 81 --------------ERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 188 SGQ-GIMWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLL-----VNRSSVSLKAVLLGGAAIPIELTE 256
Cdd:cd05903 147 TGFvYGFTLPLLLGAPVVLQDIWDPDKALAlmrehGVTFMMGATPFLTDLLnaveeAGEPLSRLRTFVCGGATVPRSLAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 257 QAREQGIRCFCG-YGLTEFASTVCAKEaDGLADV-----GSPLPGREVKIVNN-----------EVWLRAASMAEGYWRN 319
Cdd:cd05903 227 RAAELLGAKVCSaYGSTECPGAVTSIT-PAPEDRrlytdGRPLPGVEIKVVDDtgatlapgvegELLSRGPSVFLGYLDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 320 GQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM 398
Cdd:cd05903 306 PDLTADAAPEGWFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVV 385
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
137-445 |
6.52e-36 |
|
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: 138.92 E-value: 6.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 137 CSMTLTSGSTGLPKAAV--------HTYQAHLASAegvlslIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTV--R 206
Cdd:cd12119 166 AAICYTSGTTGNPKGVVyshrslvlHAMAALLTDG------LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLpgP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 207 DKQP--LEQMLA--GCTHASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEF-- 274
Cdd:cd12119 240 YLDPasLAELIEreGVTFAAGVPT-VWQGLLDhleangRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsp 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 275 ---ASTVCAKEADGLADV--------GSPLPGREVKIVNN-------------EVWLRAASMAEGYWRNGQLVSLVNDEG 330
Cdd:cd12119 319 lgtVARPPSEHSNLSEDEqlalrakqGRPVPGVELRIVDDdgrelpwdgkavgELQVRGPWVTKSYYKNDEESEALTEDG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 331 WYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VMEYDHESVD-- 406
Cdd:cd12119 399 WLRTGDVATIDeDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAvVVLKEGATVTae 478
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 727407383 407 -LSEWVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKE 445
Cdd:cd12119 479 eLLEFLADKVAKWWLPDDVVfvdEIP---KTSTGKIDKKALRE 518
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
16-445 |
1.65e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 137.73 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 16 GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN------------ 83
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNtrytadeaayil 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRV-----EGAHAAAWQPTRLCSMTLTSGST 146
Cdd:PRK07656 99 argdakalfvlgLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFlaagdPAERAPEVDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 147 GLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRW-LYAGARM-------------TVRDKQPle 212
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNApLMRGATIlplpvfdpdevfrLIETERI-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 213 QMLAGcthaslVPTQLWRLL--VNRSSV---SLKAVLLGGAAIPIELTEQAREQ-GIRCFC-GYGLTEFASTVCAKEADG 285
Cdd:PRK07656 257 TVLPG------PPTMYNSLLqhPDRSAEdlsSLRLAVTGAASMPVALLERFESElGVDIVLtGYGLSEASGVTTFNRLDD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 LAD-----VGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRGEM-HNGKLTI 347
Cdd:PRK07656 331 DRKtvagtIGTAIAGVENKIVNElgeevpvgevgELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGRLdEEGYLYI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--------RPVAVMEYDhesvDLSEWVKDKLARFQ 419
Cdd:PRK07656 411 VDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEvgkayvvlKPGAELTEE----ELIAYCREHLAKYK 486
|
490 500
....*....|....*....|....*....
gi 727407383 420 QP--VRWL-TLPpelKNGGIKISRQALKE 445
Cdd:PRK07656 487 VPrsIEFLdELP---KNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-421 |
8.15e-34 |
|
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: 131.45 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 27 QLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLeellpnltlQFALVP 106
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL---------EYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 107 DGENTFPALTSLHiqrvegahaaawqptRLCSMTLTSGSTGLPKAAVHTYQAHLASAegVLSLIPFG-DHDDWLL-SLPL 184
Cdd:cd05935 72 SGAKVAVVGSELD---------------DLALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGlTPSDVILaCLPL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 185 FHVSG-QGIMWRWLYAGAR---MTVRDKQPLEQMLA--GCTHASLVPTQLWRLLVN-----RSSVSLKAVLLGGAAIPIE 253
Cdd:cd05935 135 FHVTGfVGSLNTAVYVGGTyvlMARWDRETALELIEkyKVTFWTNIPTMLVDLLATpefktRDLSSLKVLTGGGAPMPPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 254 LTEQAREQ-GIRCFCGYGLTEFAS--TVCAKEADGLADVGSPLPGREVKIVN------------NEVWLRAASMAEGYWR 318
Cdd:cd05935 215 VAEKLLKLtGLRFVEGYGLTETMSqtHTNPPLRPKLQCLGIP*FGVDARVIDietgrelppnevGEIVVRGPQIFKGYWN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 319 NGQLV--SLVNDEG--WYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR 393
Cdd:cd05935 295 RPEETeeSFIEIKGrrFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEE 374
|
410 420 430
....*....|....*....|....*....|....
gi 727407383 394 PVAVMEYDHE------SVDLSEWVKDKLARFQQP 421
Cdd:cd05935 375 VKAFIVLRPEyrgkvtEEDIIEWAREQMAAYKYP 408
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
14-445 |
3.57e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 130.75 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 14 VRGETIALRLNDEQLNWRELCARVDELASGFAAQ-GVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:PRK06839 14 LHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 93 ELLPNLTLQFALVpdgENTFPAlTSLHIQRVEGAHAAAW---------------------QPTRLCsmtLTSGSTGLPKA 151
Cdd:PRK06839 94 FQLKDSGTTVLFV---EKTFQN-MALSMQKVSYVQRVISitslkeiedrkidnfveknesASFIIC---YTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 152 AVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIM-WRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVP 225
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFEPTKALSmiekhKVTVVMGVP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 226 TQLWRLL--VNRSSVSLKAVLL---GGAAIPIELTEQAREQGIRCFCGYGLTEFASTV--CAKE--ADGLADVGSPLPGR 296
Cdd:PRK06839 247 TIHQALIncSKFETTNLQSVRWfynGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfmLSEEdaRRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 297 EVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQP 364
Cdd:PRK06839 327 DYELIDEnknkvevgevgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVdEDGFVYIVGRKKEMIISGGENIYP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 365 EEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV----DLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISR 440
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVliekDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
....*
gi 727407383 441 QALKE 445
Cdd:PRK06839 487 AQLVN 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
19-421 |
6.73e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 127.74 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNL 98
Cdd:PRK07788 66 AALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAARE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 TLQfALVPDGENT------FPALTSLHIQRV----EGAHAAAWQ----------------PTRLCSMT-LTSGSTGLPKA 151
Cdd:PRK07788 146 GVK-ALVYDDEFTdllsalPPDLGRLRAWGGnpddDEPSGSTDEtlddliagsstaplpkPPKPGGIViLTSGTTGTPKG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 152 AVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAG-----CTHASLVPT 226
Cdd:PRK07788 225 APRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDiakhkATALVVVPV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 227 QLWRLL-------VNRSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD---VGSPLPG 295
Cdd:PRK07788 305 MLSRILdlgpevlAKYDTSSLKIIFVSGSALSPELATRALEAfGPVLYNLYGSTEVAFATIATPEDLAEApgtVGRPPKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 REVKIV---NNEV--------WLRAASMAEGYW--RNGQLVslvndEGWYATRDRGemH---NGKLTIVGRLDNLFFSGG 359
Cdd:PRK07788 385 VTVKILdenGNEVprgvvgriFVGNGFPFEGYTdgRDKQII-----DGLLSSGDVG--YfdeDGLLFVDGRDDDMIVSGG 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 360 EGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR-PVAVMEYDHESVD---LSEWVKDKLARFQQP 421
Cdd:PRK07788 458 ENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRlRAFVVKAPGAALDedaIKDYVRDNLARYKVP 523
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
8-383 |
2.39e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 126.75 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 8 WRHWRQVRGETIALRLND----EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV- 82
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 -----------------------NPQLPQPLLEELLPNLTLQFALV--PDGENTFPALTSL-----------HIQRVEgA 126
Cdd:COG1022 97 ptssaeevayilndsgakvlfveDQEQLDKLLEVRDELPSLRHIVVldPRGLRDDPRLLSLdellalgrevaDPAELE-A 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 127 HAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV----SGQGIMWR------- 195
Cdd:COG1022 176 RRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVfertVSYYALAAgatvafa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 196 ------------------------W--LYAGARMTVRDKQPLEQML----------------AGCTHASL--VPTQLWRL 231
Cdd:COG1022 256 espdtlaedlrevkptfmlavprvWekVYAGIQAKAEEAGGLKRKLfrwalavgrryararlAGKSPSLLlrLKHALADK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 232 LVnRSSV------SLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKI-VN 302
Cdd:COG1022 336 LV-FSKLrealggRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDnrIGTVGPPLPGVEVKIaED 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 NEVWLRAASMAEGYWRNGQLV-SLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFF-SGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:COG1022 415 GEILVRGPNVMKGYYKNPEATaEAFDADGWLHTGDIGELdEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQ 494
|
....
gi 727407383 380 VFIV 383
Cdd:COG1022 495 AVVV 498
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-437 |
2.43e-31 |
|
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: 123.16 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ--GIMWRWLYaGARMTVRDKQ- 209
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvlGVLACLTH-GATMVFPSPSf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 210 -PLEQMLA----GCTHASLVPTQLWRLL-----VNRSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCF-CGYGLTEfAST 277
Cdd:cd05917 80 dPLAVLEAiekeKCTALHGVPTMFIAELehpdfDKFDLSSLRTGIMAGAPCPPELMKRVIEVmNMKDVtIAYGMTE-TSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 278 VC-AKEADGLAD-----VGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRG 338
Cdd:cd05917 159 VStQTRTDDSIEkrvntVGRIMPHTEAKIVDpeggivppvgvpGELCIRGYSVMKGYWNDPEKTAEAIDgDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 339 EMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VMEYDHESV---DLSEWVKD 413
Cdd:cd05917 239 VMDeDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAwIRLKEGAELteeDIKAYCKG 318
|
330 340
....*....|....*....|....*.
gi 727407383 414 KLARFQQP--VRWLTLPPELKNGGIK 437
Cdd:cd05917 319 KIAHYKVPryVFFVDEFPLTVSGKIQ 344
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
24-445 |
4.32e-31 |
|
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: 124.73 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 24 NDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFA 103
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 104 LVPDGENT--FPALTSLHIQRVEGAHAAAWQPTRLCSMTL--------------------------TSGSTGLPKAAVHT 155
Cdd:cd05926 91 LTPKGELGpaSRAASKLGLAILELALDVGVLIRAPSAESLsnlladkknaksegvplpddlalilhTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 156 YQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-GIMWRWLYAGARMTVRDK-------QPLEQmlAGCTHASLVPTq 227
Cdd:cd05926 171 HRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRfsastfwPDVRD--YNATWYTAVPT- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 228 LWRLLVNRSS-------VSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD----VGSPLpG 295
Cdd:cd05926 248 IHQILLNRPEpnpesppPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGPRkpgsVGKPV-G 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 REVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGI 362
Cdd:cd05926 327 VEVRILDEdgeilppgvvgEICLRGPNVTRGYLNNPEANAEAAFkDGWFRTGDLGYLdADGYLFLTGRIKELINRGGEKI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 363 QPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHE--SVDLSEWVKDKLARFQQPVR-WLT--LPpelKNGG 435
Cdd:cd05926 407 SPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAavVLREGASvtEEELRAFCRKHLAAFKVPKKvYFVdeLP---KTAT 483
|
490
....*....|
gi 727407383 436 IKISRQALKE 445
Cdd:cd05926 484 GKIQRRKVAE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3-444 |
1.30e-30 |
|
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: 123.63 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 3 FSDWPWRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV 82
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 NPQ------------------------LPQPLLEELLPNLTLQFALVPDG---ENTFPALTSLHIQRVEGAHAAAWQPTR 135
Cdd:cd05959 85 NTLltpddyayyledsrarvvvvsgelAPVLAAALTKSEHTLVVLIVSGGagpEAGALLLAELVAAEAEQLKPAATHADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 136 LCSMTLTSGSTGLPKAAVHTYQAHLASAE----GVLSLIPfgdhDDWLLSLP-LFHVSGQG-IMWRWLYAGARMTVRDKQ 209
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAElyarNVLGIRE----DDVCFSAAkLFFAYGLGnSLTFPLSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 210 P-----LEQMLAGctHASL---VPTQLWRLLVN-----RSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFA 275
Cdd:cd05959 241 PtpaavFKRIRRY--RPTVffgVPTLYAAMLAApnlpsRDLSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEML 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 276 STVCAKEADGL--ADVGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRD---RGE 339
Cdd:cd05959 319 HIFLSNRPGRVryGTTGKPVPGYEVELRDEdggdvadgepgELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDkyvRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 340 mhNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM----EYDHESV---DLSEWVK 412
Cdd:cd05959 399 --DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpGYEDSEAleeELKEFVK 476
|
490 500 510
....*....|....*....|....*....|...
gi 727407383 413 DKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05959 477 DRLAPYKYP-RWIVFVDELpKTATGKIQRFKLR 508
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-396 |
1.47e-30 |
|
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: 123.50 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVpDGENt 111
Cdd:cd05904 37 ELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT-TAEL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 112 FPALTSLHIQ-------RVEGAH--------------AAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLI 170
Cdd:cd05904 115 AEKLASLALPvvlldsaEFDSLSfsdllfeadeaeppVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 171 PFGDHDD--WLLSLPLFHVSG-QGIMWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLlVNRSSV---- 238
Cdd:cd05904 195 GSNSDSEdvFLCVLPMFHIYGlSSFALGLLRLGATVVVMPRFDLEELLAaieryKVTHLPVVPPIVLAL-VKSPIVdkyd 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 --SLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEF--ASTVCAKEADGLADVGSP---LPGREVKIVN------- 302
Cdd:cd05904 274 lsSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTEStgVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDpetgesl 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 -----NEVWLRAASMAEGYWRNGQLVSL-VNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHP 375
Cdd:cd05904 354 ppnqtGELWIRGPSIMKGYLNNPEATAAtIDKEGWLHTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHP 433
|
410 420
....*....|....*....|.
gi 727407383 376 AVLQVFIVPVADKEFGHRPVA 396
Cdd:cd05904 434 EILDAAVIPYPDEEAGEVPMA 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
25-444 |
1.83e-29 |
|
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: 119.49 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfaL 104
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPL------------------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 105 VPDGEntfpALTSLHIQ-RVEGAHAAAwqptrLCSMTLTSGSTGLPKAAVHTYQAHLASAEG----VLSLIPfgdhDDWL 179
Cdd:cd05919 70 HPDDY----AYIARDCEaRLVVTSADD-----IAYLLYSSGTTGPPKGVMHAHRDPLLFADAmareALGLTP----GDRV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 180 LSLP-LFHVSGQG-IMWRWLYAGARMTVRDKQPL-EQMLAgcTHASLVPTQLW-------RLLVN-----RSSVSLKAVL 244
Cdd:cd05919 137 FSSAkMFFGYGLGnSLWFPLAVGASAVLNPGWPTaERVLA--TLARFRPTVLYgvptfyaNLLDScagspDALRSLRLCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 245 LGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVNNE-----------VWLRAA 310
Cdd:cd05919 215 SAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRPGAwrLGSTGRPVPGYEIRLVDEEghtippgeegdLLVRGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 311 SMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKE 389
Cdd:cd05919 295 SAAVGYWNNPEKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEST 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727407383 390 FGHRPVAVMEYDHESV-------DLSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05919 375 GLSRLTAFVVLKSPAApqeslarDIHRHLLERLSAHKVP-RRIAFVDELpRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
13-421 |
2.63e-29 |
|
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: 119.71 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 13 QVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:cd12118 15 AVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 93 ELLPNLTLQFALVpDGENTFPALTSlhiqrvEGAHAAAWQPTR----LCSMTLTSGSTGLPKAAVHTYQ-AHLASAEGVL 167
Cdd:cd12118 95 FILRHSEAKVLFV-DREFEYEDLLA------EGDPDFEWIPPAdewdPIALNYTSGTTGRPKGVVYHHRgAYLNALANIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 168 SLiPFGDHDDWLLSLPLFHVSGQGIMWR-WLYAGARMTVRDKQPLE--QMLA--GCTHASLVPTQLWRLLVNRSSVSLKA 242
Cdd:cd12118 168 EW-EMKQHPVYLWTLPMFHCNGWCFPWTvAAVGGTNVCLRKVDAKAiyDLIEkhKVTHFCGAPTVLNMLANAPPSDARPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 243 -----VLLGGAAIPIELTEQAREQGIRCFCGYGLTEFA--STVCAK--EADGLA---------------------DVGSP 292
Cdd:cd12118 247 phrvhVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWkpEWDELPteerarlkarqgvryvgleevDVLDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 293 LPGREV----KIVNnEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd12118 327 ETMKPVprdgKTIG-EIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEV 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 727407383 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEY-DHESV---DLSEWVKDKLARFQQP 421
Cdd:cd12118 406 EGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELkEGAKVteeEIIAFCREHLAGFMVP 463
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
9-443 |
2.78e-29 |
|
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: 119.35 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARvlPVNPQLPQ 88
Cdd:cd05920 22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 PLLEELLPNLTLQFAL--VPDGENTFPALTSLHIQRVEGAHAAAWQptrlcsmtLTSGSTGLPKAAVHTYQAHLASAEGV 166
Cdd:cd05920 100 RRSELSAFCAHAEAVAyiVPDRHAGFDHRALARELAESIPEVALFL--------LSGGTTGTPKLIPRTHNDYAYNVRAS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 167 LSLIPFGDHDDWLLSLPLFH---VSGQGIMWRwLYAGARMTV-RDKQPLEQMLA----GCTHASLVPT--QLWRLLVNRS 236
Cdd:cd05920 172 AEVCGLDQDTVYLAVLPAAHnfpLACPGVLGT-LLAGGRVVLaPDPSPDAAFPLiereGVTVTALVPAlvSLWLDAAASR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 237 S---VSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEfaSTVCAKEADGLADV-----GSPL-PGREVKIVN---- 302
Cdd:cd05920 251 RadlSSLRLLQVGGARLSPALARRVPPVlGCTLQQVFGMAE--GLLNYTRLDDPDEViihtqGRPMsPDDEIRVVDeegn 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 -------NEVWLRAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAA 373
Cdd:cd05920 329 pvppgeeGELLTRGPYTIRGYYRAPEHNARAfTPDGFYRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVENLLLR 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 374 HPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEwVKDKL-----ARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05920 409 HPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQ-LRRFLrerglAAYKLPDRIEFVDslPLTAVG--KIDKKAL 482
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
9-421 |
3.03e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 119.88 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHwRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN----- 83
Cdd:PRK07786 25 RH-ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNfrltp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ------------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEG-AHAAAWQPTRLCSMTL-TS 143
Cdd:PRK07786 104 peiaflvsdcgahvvvteAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGpAHAPVDIPNDSPALIMyTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 144 GSTGLPKAAVHTyqaHLASAEGVLSLI----PFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVR-----DKQPLEQM 214
Cdd:PRK07786 184 GTTGRPKGAVLT---HANLTGQAMTCLrtngADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYplgafDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LAG--CTHASLVPTQlWRLL-----VNRSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTVCAKEADG 285
Cdd:PRK07786 261 LEAekVTGIFLVPAQ-WQAVcaeqqARPRDLALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 ----LADVGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVG 349
Cdd:PRK07786 340 airkLGSVGKVIPTVAARVVDEnmndvpvgevgEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQdEEGYVWVVD 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 350 RLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV-----DLSEWVKDKLARFQQP 421
Cdd:PRK07786 420 RKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaltleDLAEFLTDRLARYKHP 496
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
19-443 |
6.66e-29 |
|
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: 118.77 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN--------------- 83
Cdd:cd05923 20 IADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINprlkaaelaelierg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ---------PQLPQPLLEELLPNLTLQFALVPDGENTfpALTSLHIQRVEGAHAAAWqptrlcsMTLTSGSTGLPKAAVh 154
Cdd:cd05923 100 emtaaviavDAQVMDAIFQSGVRVLALSDLVGLGEPE--SAGPLIEDPPREPEQPAF-------VFYTSGTTGLPKGAV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 155 tyQAHLASAEGVLSLIP-----FGDHDDWLLSLPLFHVSGqgimWRWLYAGAR------MTVRDKQP------LEQMLAG 217
Cdd:cd05923 170 --IPQRAAESRVLFMSTqaglrHGRHNVVLGLMPLYHVIG----FFAVLVAALaldgtyVVVEEFDPadalklIEQERVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 CTHAslVPTQLWRLL-----VNRSSVSLKAVLLGGAAIPIELTEQAREqgirCFCG-----YGLTEFASTVCAKEADgla 287
Cdd:cd05923 244 SLFA--TPTHLDALAaaaefAGLKLSSLRHVTFAGATMPDAVLERVNQ----HLPGekvniYGTTEAMNSLYMRDAR--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 dVGSPL-PG--REVKIV--------------NNEVWLRAASMA--EGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTI 347
Cdd:cd05923 315 -TGTEMrPGffSEVRIVriggspdealangeEGELIVAAAADAafTGYLNQPEATAKKLQDGWYRTGDVGYVDpSGDVRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEW----VKDKLARFQQPVR 423
Cdd:cd05923 394 LGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELdqfcRASELADFKRPRR 473
|
490 500
....*....|....*....|
gi 727407383 424 WLTLPPELKNGGIKISRQAL 443
Cdd:cd05923 474 YFFLDELPKNAMNKVLRRQL 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3-449 |
2.57e-28 |
|
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: 117.17 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 3 FSDWpWRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvLPV 82
Cdd:COG1021 27 LGDL-LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 npqlpqplleellpnltlqFAL---------------------VPD---------------------------GE-NTFP 113
Cdd:COG1021 104 -------------------FALpahrraeishfaeqseavayiIPDrhrgfdyralarelqaevpslrhvlvvGDaGEFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 114 ALTSLHIQRVEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHT-----YQAhLASAE--GVlslipfgDHDD-WLLSLPLF 185
Cdd:COG1021 165 SLDALLAAPADLSEPRP-DPDDVAFFQLSGGTTGLPKLIPRThddylYSV-RASAEicGL-------DADTvYLAALPAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 186 H---VSGQGIMWRwLYAGARMTV-RDKQPlEQMLA-----GCTHASLVPTQLWRLL--VNRSSV---SLKAVLLGGAAIP 251
Cdd:COG1021 236 HnfpLSSPGVLGV-LYAGGTVVLaPDPSP-DTAFPliereRVTVTALVPPLALLWLdaAERSRYdlsSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 252 IELTEQAREQ-GircfCG----YGLtefastvcakeADGL---------ADV-----GSPL-PGREVKIVN---NEV--- 305
Cdd:COG1021 314 PELARRVRPAlG----CTlqqvFGM-----------AEGLvnytrlddpEEVilttqGRPIsPDDEVRIVDedgNPVppg 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 306 -----WLRAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVL 378
Cdd:COG1021 379 evgelLTRGPYTIRGYYRAPEHNARAfTPDGFYRTGDLVRRTpDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVH 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 379 QVFIVPVADKEFGHRPVAVMEYDHESVDLSE---WVKDK-LARFQQPVRwLTLPPELKNGGI-KISRQALKEWVQR 449
Cdd:COG1021 459 DAAVVAMPDEYLGERSCAFVVPRGEPLTLAElrrFLRERgLAAFKLPDR-LEFVDALPLTAVgKIDKKALRAALAA 533
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
17-421 |
7.69e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.03 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12583 35 EALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQF-----------------ALVP------------------------DGENTfPALTSLH--IQRVEG-------A 126
Cdd:PRK12583 115 QSGVRWvicadafktsdyhamlqELLPglaegqpgalacerlpelrgvvslAPAPP-PGFLAWHelQARGETvsrealaE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 127 HAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-----GIMwrwlYAGA 201
Cdd:PRK12583 194 RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMvlanlGCM----TVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 202 RMTVRDK--QPLEQMLA----GCTHASLVPTQLWRLLVN--RSSV---SLKAVLLGGAAIPIELTEQAREQgIRC---FC 267
Cdd:PRK12583 270 CLVYPNEafDPLATLQAveeeRCTALYGVPTMFIAELDHpqRGNFdlsSLRTGIMAGAPCPIEVMRRVMDE-MHMaevQI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 268 GYGLTEfASTVCAKE--ADGL----ADVGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDE- 329
Cdd:PRK12583 349 AYGMTE-TSPVSLQTtaADDLerrvETVGRTQPHLEVKVVDPdgatvprgeigELCTRGYSVMKGYWNNPEATAESIDEd 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 330 GWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHE--S 404
Cdd:PRK12583 428 GWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAwvRLHPGHAasE 507
|
490
....*....|....*..
gi 727407383 405 VDLSEWVKDKLARFQQP 421
Cdd:PRK12583 508 EELREFCKARIAHFKVP 524
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
135-440 |
1.27e-27 |
|
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: 112.11 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH-VSGQGIMWRwLYAGARMTVRDK-QPLE 212
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISA-LYLGGTFIGQRKfNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 213 QMLAGCTHAS----LVPTQLWRLL-VNRSSVSLKAVLLGGAAIPIELTEQAREQ----GIRCFCGYGLTEFASTVCAKEA 283
Cdd:cd17633 80 WIRKINQYNAtviyLVPTMLQALArTLEPESKIKSIFSSGQKLFESTKKKLKNIfpkaNLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 284 DGLADVGSPLPGREVKIVNNE------VWLRAASMAEGYWRNGQlvslVNDEGWYATRDRG-EMHNGKLTIVGRLDNLFF 356
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADggeigkIFVKSEMVFSGYVRGGF----SNPDGWMSVGDIGyVDEEGYLYLVGRESDMII 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 357 SGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDH-ESVDLSEWVKDKLARFQQPVRWLTLP--PELKN 433
Cdd:cd17633 236 IGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKlTYKQLKRFLKQKLSRYEIPKKIIFVDslPYTSS 315
|
....*..
gi 727407383 434 GgiKISR 440
Cdd:cd17633 316 G--KIAR 320
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
32-446 |
1.95e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.13 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQF--------A 103
Cdd:PRK09088 27 ELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLllgddavaA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 104 LVPDGENtFPALTSlHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:PRK09088 107 GRTDVED-LAAFIA-SADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 184 LFHVSGQGIMWR-WLYAGARMTVRDKQPLEQMLA-------GCTHASLVPtQLWRLLVNRSSV------SLKAVLLGGAA 249
Cdd:PRK09088 185 MFHIIGLITSVRpVLAVGGSILVSNGFEPKRTLGrlgdpalGITHYFCVP-QMAQAFRAQPGFdaaalrHLTALFTGGAP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 250 IPIELTEQAREQGIRCFCGYGLTEfASTV------CAKEADGLADVGSPLPGREVKIVNN-----------EVWLRAASM 312
Cdd:PRK09088 264 HAAEDILGWLDDGIPMVDGFGMSE-AGTVfgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDqgndcpagvpgELLLRGPNL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 313 AEGYWRNGQLVSLVND-EGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEF 390
Cdd:PRK09088 343 SPGYWRRPQATARAFTgDGWFRTGDIARRDaDGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQW 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727407383 391 GHRPVAVM----EYDHESVDLSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALKEW 446
Cdd:PRK09088 423 GEVGYLAIvpadGAPLDLERIRSHLSTRLAKYKVP-KHLRLVDALpRTASGKLQKARLRDA 482
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-443 |
7.21e-27 |
|
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: 112.38 E-value: 7.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 16 GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELL 95
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 96 PNLTLQFALV-PDGENTFPA---LTSLHIQRVEGAHAAAW---QPTRLCSMTLTSGSTGLPKAAVHTYQA---HLASAEG 165
Cdd:cd12116 81 EDAEPALVLTdDALPDRLPAglpVLLLALAAAAAAPAAPRtpvSPDDLAYVIYTSGSTGRPKGVVVSHRNlvnFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 166 VLSLIPfgdhDDWLLSL--PLFHVSGQGIMWRwLYAGARM------TVRDKQPLEQMLA--GCTHASLVPTqLWRLLV-- 233
Cdd:cd12116 161 RLGLGP----GDRLLAVttYAFDISLLELLLP-LLAGARVviapreTQRDPEALARLIEahSITVMQATPA-TWRMLLda 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 234 ---NRSSVSLkavLLGGAAIPIELTEQAREQGIRCFCGYGLTEFA--STVCA-KEADGLADVGSPLPGREVKIVNN---- 303
Cdd:cd12116 235 gwqGRAGLTA---LCGGEALPPDLAARLLSRVGSLWNLYGPTETTiwSTAARvTAAAGPIPIGRPLANTQVYVLDAalrp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -------EVWLRAASMAEGYWRNGQLVS--LVND------EGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd12116 312 vppgvpgELYIGGDGVAQGYLGRPALTAerFVPDpfagpgSRLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHRIELGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 368 ERVIAAHPAVLQVfIVPVADKEFGHRPVAVMEYDH-ESVDLSEW---VKDKLARFQQPVRWLTLP--PELKNGgiKISRQ 441
Cdd:cd12116 392 EAALAAHPGVAQA-AVVVREDGGDRRLVAYVVLKAgAAPDAAALrahLRATLPAYMVPSAFVRLDalPLTANG--KLDRK 468
|
..
gi 727407383 442 AL 443
Cdd:cd12116 469 AL 470
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
16-445 |
8.16e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.83 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 16 GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTL------------------------LAWLA 71
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFesmfaafrlgavwvptnfrqtpdeVAYLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 72 LlQCGARVLPVNPQLPQPLLEELLPNLTLQFALV---PDGENTFPALTSLHI-QRVEGAHAAAWQPtrlCSMTLTSGSTG 147
Cdd:PRK07470 101 E-ASGARAMICHADFPEHAAAVRAASPDLTHVVAiggARAGLDYEALVARHLgARVANAAVDHDDP---CWFFFTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 148 LPKAAVHTY-------QAHLASaegvlsLIP-FGDHDDWLLSLPLFHvsGQGIMWRWLYAGARMTV---RDKQPLEQMLA 216
Cdd:PRK07470 177 RPKAAVLTHgqmafviTNHLAD------LMPgTTEQDASLVVAPLSH--GAGIHQLCQVARGAATVllpSERFDPAEVWA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 -----GCTHASLVPTQLwRLLVNRSSV------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTV-----C 279
Cdd:PRK07470 249 lverhRVTNLFTVPTIL-KMLVEHPAVdrydhsSLRYVIYAGAPMYRADQKRALAKlGKVLVQYFGLGEVTGNItvlppA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 280 AKEADGLADV-----GSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQlvslVNDE----GWYATRDRGE 339
Cdd:PRK07470 328 LHDAEDGPDArigtcGFERTGMEVQIQDDegrelppgetgEICVIGPAVFAGYYNNPE----ANAKafrdGWFRTGDLGH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 340 MH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAV-MEYDHESVD---LSEWVKDK 414
Cdd:PRK07470 404 LDaRGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVcVARDGAPVDeaeLLAWLDGK 483
|
490 500 510
....*....|....*....|....*....|....
gi 727407383 415 LARFQQPVR---WLTLPpelKNGGIKISRQALKE 445
Cdd:PRK07470 484 VARYKLPKRfffWDALP---KSGYGKITKKMVRE 514
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
142-438 |
2.78e-26 |
|
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: 108.89 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLplFHVSGQGIMWRWL----YAGARMTVRDKQPLEQMLA- 216
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLP--LPATHIGGLWWILtcliHGGLCVTGGENTTYKSLFKi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 ----GCTHASLVPTqLWRLLVN------RSSVSLKAVLLGGAaIPIELTEQARE--QGIRCFCGYGLTEFASTVCAKEAD 284
Cdd:cd17635 87 lttnAVTTTCLVPT-LLSKLVSelksanATVPSLRLIGYGGS-RAIAADVRFIEatGLTNTAQVYGLSETGTALCLPTDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 GLAD---VGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVG 349
Cdd:cd17635 165 DSIEinaVGRPYPGVDVYLAATdgiagpsasfgTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERrEDGFLFITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 350 RLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAvmeydheSVDLSEWVKDKLARFQQPVRWLTLPP 429
Cdd:cd17635 245 RSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGL-------AVVASAELDENAIRALKHTIRRELEP 317
|
....*....
gi 727407383 430 ELKNGGIKI 438
Cdd:cd17635 318 YARPSTIVI 326
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
141-445 |
3.02e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 111.39 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 141 LTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA---- 216
Cdd:PRK13382 203 LTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDlidr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 -GCTHASLVPTQLWRLL------VNR-SSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLA 287
Cdd:PRK13382 283 hRATGLAVVPVMFDRIMdlpaevRNRySGRSLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATEAGMIATATPADLRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 ---DVGSPLPGREVKIVNNE-----------VWLRAASMAEGYwRNGQLVSLVndEGWYATRDRGEMH-NGKLTIVGRLD 352
Cdd:PRK13382 363 apdTAGRPAEGTEIRILDQDfrevptgevgtIFVRNDTQFDGY-TSGSTKDFH--DGFMASGDVGYLDeNGRLFVVGRDD 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESV--DLSEWVKDKLARFQQPvRWLTLP 428
Cdd:PRK13382 440 EMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAfvVLKPGASATpeTLKQHVRDNLANYKVP-RDIVVL 518
|
330
....*....|....*...
gi 727407383 429 PELKNGGI-KISRQALKE 445
Cdd:PRK13382 519 DELPRGATgKILRRELQA 536
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
6-421 |
3.08e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 111.24 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 6 WPWRhwrqvrgetIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCGARVLPVN 83
Cdd:PRK13383 48 WPGR---------TAIIDDDGALSYRELQRATESLARRLTRDGVAPGRavGVMCR--NGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 PQLPQPLLEELLPNLTLQFALVPD---------GENTFPALTSLHIQRVEGAHAAAWQPTRLcsMTLTSGSTGLPKAAVH 154
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNefaeriagaDDAVAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGVPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 155 TYQahLASAEGV----LSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAGCT-HA----SLVP 225
Cdd:PRK13383 195 APQ--LRSAVGVwvtiLDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASlHRadafTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 226 TQLWRLLVNRSSV-------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADgLAD----VGSPL 293
Cdd:PRK13383 273 VVLARILELPPRVrarnplpQLRVVMSSGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPAD-LRDapetVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 294 PGREVKI-----------VNNEVWLRAASMAEGYWRNGQLVSLvndEGWYATRDRGEMHN-GKLTIVGRLDNLFFSGGEG 361
Cdd:PRK13383 352 AGCPVRIldrnnrpvgprVTGRIFVGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNaGRLFIVGREDDMIISGGEN 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727407383 362 IQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VMEYDHESVD---LSEWVKDKLARFQQP 421
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAfVVLHPGSGVDaaqLRDYLKDRVSRFEQP 492
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
19-443 |
3.44e-26 |
|
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: 110.03 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellpnl 98
Cdd:cd17652 4 PAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLD--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 tlqfalvPDgentFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAV--HTYQAHLASAEGvlSLIPFGDHD 176
Cdd:cd17652 69 -------PA----YPAERIAYMLADARPALLLTTPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQI--AAFDVGPGS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 177 DWL-LSLPLFHVSgqgiMWRW---LYAGARMTVRDK------QPLEQMLA--GCTHASLVPTQLwRLLVNRSSVSLKAVL 244
Cdd:cd17652 136 RVLqFASPSFDAS----VWELlmaLLAGATLVLAPAeellpgEPLADLLRehRITHVTLPPAAL-AALPPDDLPDLRTLV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 245 LGGAAIPIELTEQ-AReqGIRCFCGYGLTEfaSTVCAKEADGLAD-----VGSPLPGREVKI-----------VNNEVWL 307
Cdd:cd17652 211 VAGEACPAELVDRwAP--GRRMINAYGPTE--TTVCATMAGPLPGggvppIGRPVPGTRVYVldarlrpvppgVPGELYI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 308 RAASMAEGYWRNGQL--VSLVND------EGWYATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVL 378
Cdd:cd17652 287 AGAGLARGYLNRPGLtaERFVADpfgapgSRMYRTGDLARWRAdGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727407383 379 QVFIVPVADKEFGHRPVA-VMEYDHESVD---LSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17652 367 EAVVVVRDDRPGDKRLVAyVVPAPGAAPTaaeLRAHLAERLPGYMVPAAFVVLDalPLTPNG--KLDRRAL 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
11-448 |
5.69e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 110.59 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 11 WRQVRGETIALR-----LNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALL------------ 73
Cdd:COG0365 18 HAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACArigavhspvfpg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 74 -----------QCGARVL----------PVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAWQ 132
Cdd:COG0365 98 fgaealadrieDAEAKVLitadgglrggKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCS-----MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIpFGDHDD----------WllslplfhvsgqgIMWRW- 196
Cdd:COG0365 178 PEPTDAddplfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV-LDLKPGdvfwctadigW-------------ATGHSy 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 197 -----LYAGARMTVRDKQP-------LEQMLA--GCTHASLVPTqLWRLLVN--------RSSVSLKAVLLGGAAIPIEL 254
Cdd:COG0365 244 ivygpLLNGATVVLYEGRPdfpdpgrLWELIEkyGVTVFFTAPT-AIRALMKagdeplkkYDLSSLRLLGSAGEPLNPEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 255 TEQAREQ-GIRCFCGYGLTEFASTVCAkeADGLADV--GS---PLPGREVKIVNN-----------EVWLRAA--SMAEG 315
Cdd:COG0365 323 WEWWYEAvGVPIVDGWGQTETGGIFIS--NLPGLPVkpGSmgkPVPGYDVAVVDEdgnpvppgeegELVIKGPwpGMFRG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 316 YWRNgqlvslvnDE-----------GWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIV 383
Cdd:COG0365 401 YWND--------PEryretyfgrfpGWYRTGDGARRDeDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 384 PVADKEFGHRPVA--VMEYDHESVD-----LSEWVKDKLARFQQP--VRWLtlpPEL---KNGgiKISRQALKEWVQ 448
Cdd:COG0365 473 GVPDEIRGQVVKAfvVLKPGVEPSDelakeLQAHVREELGPYAYPreIEFV---DELpktRSG--KIMRRLLRKIAE 544
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
20-421 |
8.90e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 110.05 E-value: 8.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELAsGFAAQ--GVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN-------------- 83
Cdd:PRK08314 28 AIVFYGRAISYRELLEEAERLA-GYLQQecGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNpmnreeelahyvtd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 --------------PQLPQPLLEELLPNLTLQF--ALVPDGENTFPAL--TSLHIQRVEGAHAAAWQ------------- 132
Cdd:PRK08314 107 sgarvaivgselapKVAPAVGNLRLRHVIVAQYsdYLPAEPEIAVPAWlrAEPPLQALAPGGVVAWKealaaglapppht 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 --PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAegVLSLIPFGDHDD--WLLSLPLFHVSG-QGIMWRWLYAGAR---MT 204
Cdd:PRK08314 187 agPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPEsvVLAVLPLFHVTGmVHSMNAPIYAGATvvlMP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 205 VRDKQPLEQMLA--GCTHASLVPTQLWRLLVN-----RSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:PRK08314 265 RWDREAAARLIEryRVTHWTNIPTMVVDFLASpglaeRDLSSLRYIGGGGAAMPEAVAERLKELtGLDYVEGYGLTETMA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 277 TVCAKEAD-------GLA-----------DVGSPLPGREVkivnNEVWLRAASMAEGYWRNGQLV--SLVNDEG--WYAT 334
Cdd:PRK08314 345 QTHSNPPDrpklqclGIPtfgvdarvidpETLEELPPGEV----GEIVVHGPQVFKGYWNRPEATaeAFIEIDGkrFFRT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 335 RDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV------DL 407
Cdd:PRK08314 421 GDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgktteeEI 500
|
490
....*....|....
gi 727407383 408 SEWVKDKLARFQQP 421
Cdd:PRK08314 501 IAWAREHMAAYKYP 514
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-443 |
1.10e-25 |
|
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: 108.87 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfalvpdgeNTFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd05945 73 -------------ASSPAERIREILDAAKPALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 177 DWLLSLPL-FHVSGQGIMWRWLYAGA-----RMTVRDKQPLEQMLA--GCTHASLVPTqLWRLLV-----NRSSV-SLKA 242
Cdd:cd05945 140 VFLNQAPFsFDLSVMDLYPALASGATlvpvpRDATADPKQLFRFLAehGITVWVSTPS-FAAMCLlsptfTPESLpSLRH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 243 VLLGGAAIPIELTE--QAREQGIRCFCGYGLTE--FASTVCAKEADGLAD-----VGSPLPGREVKIVNN---------- 303
Cdd:cd05945 219 FLFCGEVLPHKTARalQQRFPDARIYNTYGPTEatVAVTYIEVTPEVLDGydrlpIGYAKPGAKLVILDEdgrpvppgek 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYWRNGQLV--SLVNDEG--WYATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAV 377
Cdd:cd05945 299 gELVISGPSVSKGYLNNPEKTaaAFFPDEGqrAYRTGDLVRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727407383 378 LQVFIVPVADKEFGHRPVAVMEYDH--ESVDLSEW---VKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05945 379 KEAVVVPKYKGEKVTELIAFVVPKPgaEAGLTKAIkaeLAERLPPYMIPRRFVYLDelPLNANG--KIDRKAL 449
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-443 |
1.21e-25 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 108.90 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQVR--GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:cd17646 6 EQAArtPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 90 LLEELLPNLTLQF-----ALVPDGENTFPALTSLHIQRVEGAHAAAWQPTR---LCSMTLTSGSTGLPKAAVHTyqaHLA 161
Cdd:cd17646 86 RLAYMLADAGPAVvlttaDLAARLPAGGDVALLGDEALAAPPATPPLVPPRpdnLAYVIYTSGSTGRPKGVMVT---HAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 162 SAEGVLSL---IPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLEQMLA--GCTHASLVPTQLw 229
Cdd:cd17646 163 IVNRLLWMqdeYPLGPGDRVLQKTPLsFDVSVWELFWP-LVAGARLVVarpgghRDPAYLAALIRehGVTTCHFVPSML- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 230 RLLVN----RSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD-----VGSPLPGREVK 299
Cdd:cd17646 241 RVFLAepaaGSCASLRRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPVRGPAEtpsvpIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 300 I-----------VNNEVWLRAASMAEGYWRNGQLV--SLVND-----EGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGE 360
Cdd:cd17646 321 VlddalrpvpvgVPGELYLGGVQLARGYLGRPALTaeRFVPDpfgpgSRMYRTGDLARWrPDGALEFLGRSDDQVKIRGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 361 GIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVD---LSEWVKDKLARFQQPVRWLTLP--PELKN 433
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGyvVPAAGAAGPDtaaLRAHLAERLPEYMVPAAFVVLDalPLTAN 480
|
490
....*....|
gi 727407383 434 GgiKISRQAL 443
Cdd:cd17646 481 G--KLDRAAL 488
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
17-443 |
1.61e-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: 108.16 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleellp 96
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfalvpdgenTFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd17643 70 --------------AYPVERIAFILADSGPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 177 DWLLslplFHVSGQGI----MWRWLYAGARMTV------RDKQPLEQML--AGCTHASLVPTQLWRLL-----VNRSSVS 239
Cdd:cd17643 136 VWTL----FHSYAFDFsvweIWGALLHGGRLVVvpyevaRSPEDFARLLrdEGVTVLNQTPSAFYQLVeaadrDGRDPLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 240 LKAVLLGGAAIPIELTEQARE----QGIRCFCGYGLTEfaSTV-------CAKEADGLAD--VGSPLPGREVKIVNN--- 303
Cdd:cd17643 212 LRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITE--TTVhvtfrplDAADLPAAAAspIGRPLPGLRVYVLDAdgr 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 --------EVWLRAASMAEGY-----------------------WRNGQLVSLVNDegwyatrdrgemhnGKLTIVGRLD 352
Cdd:cd17643 290 pvppgvvgELYVSGAGVARGYlgrpeltaerfvanpfggpgsrmYRTGDLARRLPD--------------GELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV----DLSEWVKDKLARFQQPVRWLTLP 428
Cdd:cd17643 356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAadiaELRALLKELLPDYMVPARYVPLD 435
|
490
....*....|....*..
gi 727407383 429 --PELKNGgiKISRQAL 443
Cdd:cd17643 436 alPLTVNG--KLDRAAL 450
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
139-450 |
2.08e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 108.33 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH-------VSGqgimwrwLYAGARMTVRDKQPL 211
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHslflygaIST-------LYVGQTVHLMRKFIP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 212 EQMLAGCTHASL-----VPTQLWRLL-VNRSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTE--FASTVCAK 281
Cdd:PRK07638 221 NQVLDKLETENIsvmytVPTMLESLYkENRVIENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASElsFVTALVDE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 282 EADGLAD-VGSPLPGREVKIVN--------NE---VWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRG-EMHNGKLTIV 348
Cdd:PRK07638 301 ESERRPNsVGRPFHNVQVRICNeageevqkGEigtVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGyEDEEGFIYIV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLARFQQPVRWLTLP 428
Cdd:PRK07638 381 GREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVD 460
|
330 340
....*....|....*....|....
gi 727407383 429 --PELKNGgiKISRQALKEWVQRQ 450
Cdd:PRK07638 461 eiPYTNSG--KIARMEAKSWIENQ 482
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
142-436 |
3.44e-25 |
|
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: 105.43 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK----QPLEQMLAg 217
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKfdpaEALELIEE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 cTHASLV---PTQLWRLL--VNRSSV---SLKAVLLGGAAIPIELTEqaREQGIRCFCGYGLTE---FASTVCAKEADGL 286
Cdd:cd17637 87 -EKVTLMgsfPPILSNLLdaAEKSGVdlsSLRHVLGLDAPETIQRFE--ETTGATFWSLYGQTEtsgLVTLSPYRERPGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 AdvGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRL--D 352
Cdd:cd17637 164 A--GRPGPLVRVRIVDDndrpvpagetgEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFdEDGYLWYAGRKpeK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV----DLSEWVKDKLARFQQP--VRWLT 426
Cdd:cd17637 242 ELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATltadELIEFVGSRIARYKKPryVVFVE 321
|
330
....*....|
gi 727407383 427 LPPELKNGGI 436
Cdd:cd17637 322 ALPKTADGSI 331
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
142-389 |
3.54e-25 |
|
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: 107.53 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-QGIMWRWLYAGARMTVRDKQP----LEQMLA 216
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFLDKIPsakiIALAFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 GCTHASLVPTQL--------------------WRL---LVNRSSVSL-------------KAVLLGGAAIPIELTEQARE 260
Cdd:cd05914 177 QVTPTLGVPVPLviekifkmdiipkltlkkfkFKLakkINNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFLRT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 261 QGIrCFC-GYGLTEFASTVC--AKEADGLADVGSPLPGREVKI-------VNNEVWLRAASMAEGYWRNGQL-VSLVNDE 329
Cdd:cd05914 257 IGF-PYTiGYGMTETAPIISysPPNRIRLGSAGKVIDGVEVRIdspdpatGEGEIIVRGPNVMKGYYKNPEAtAEAFDKD 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727407383 330 GWYATRDRGEM-HNGKLTIVGRLDNLFFSG-GEGIQPEEVERVIAAHPAVLQVFIVPVADKE 389
Cdd:cd05914 336 GWFHTGDLGKIdAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
26-397 |
3.86e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.83 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALV 105
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 106 PD----------GENTFPALTSL-HIQRVEGAHA---------AAWQ---------------PTRLCSMTLTSGSTGLPK 150
Cdd:PRK13295 134 PKtfrgfdhaamARRLRPELPALrHVVVVGGDGAdsfeallitPAWEqepdapailarlrpgPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 151 AAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG--QGIMWRwLYAGARMTVRDKQPLEQMLA-----GCTHaSL 223
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfmYGLMMP-VMLGATAVLQDIWDPARAAElirteGVTF-TM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 224 VPTQLWRLLVN------RSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTE--FASTVCAKEADGLADV--GSP 292
Cdd:PRK13295 292 ASTPFLTDLTRavkesgRPVSSLRTFLCAGAPIPGALVERARAAlGAKIVSAWGMTEngAVTLTKLDDPDERASTtdGCP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 293 LPGREVKIVNNE-----------VWLRAASMAEGYWRNGQLvSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGE 360
Cdd:PRK13295 372 LPGVEVRVVDADgaplpagqigrLQVRGCSNFGGYLKRPQL-NGTDADGWFDTGDLARIDaDGYIRISGRSKDVIIRGGE 450
|
410 420 430
....*....|....*....|....*....|....*..
gi 727407383 361 GIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAV 397
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAF 487
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
11-445 |
5.16e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 107.28 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 11 WRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPL 90
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 91 LEELLPNLTLQFALVPDGENTFPALTslHIQRVEGAHA-----------------AAWQPTRLCSMTLTSGSTGLPKAAV 153
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAIVALE--TPKIVIDAAAqadsrrlaqggleippqAAVAPTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 154 HTY-QAHLASAEGVLSLIPFGDhDDWLLSLPLFHVS-----GQGIMWrwlYAGARMTVRDKQPlEQMLAGC-----THAS 222
Cdd:PRK06145 169 HSYgNLHWKSIDHVIALGLTAS-ERLLVVGPLYHVGafdlpGIAVLW---VGGTLRIHREFDP-EAVLAAIerhrlTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 223 LVPTQLWRLLV----NRSSVSLKAVLLGGAaipieltEQAREQGIRCFC----------GYGLTEFAS----TVCAKEAD 284
Cdd:PRK06145 244 MAPVMLSRVLTvpdrDRFDLDSLAWCIGGG-------EKTPESRIRDFTrvftraryidAYGLTETCSgdtlMEAGREIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 GLADVGSPLPGREVKI-----------VNNEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLD 352
Cdd:PRK06145 317 KIGSTGRALAHVEIRIadgagrwlppnMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLdEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDH----ESVDLSEWVKDKLARFQQPvRWLTLP 428
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgatlTLEALDRHCRQRLASFKVP-RQLKVR 475
|
490
....*....|....*...
gi 727407383 429 PEL-KNGGIKISRQALKE 445
Cdd:PRK06145 476 DELpRNPSGKVLKRVLRD 493
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
13-391 |
1.13e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 106.63 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 13 QVRGETIALRLND--EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPL 90
Cdd:PRK05857 25 RQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 91 LEELLPNLTLQFALV-----------PDGENTFPALTslhIQRVEGAHAAAWQPTR-------------LCSMTLTSGST 146
Cdd:PRK05857 105 IERFCQITDPAAALVapgskmassavPEALHSIPVIA---VDIAAVTRESEHSLDAaslagnadqgsedPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 147 GLPKAAVHTYQAHLA-----SAEGvLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQ--PLEQMLAG-- 217
Cdd:PRK05857 182 GEPKAVLLANRTFFAvpdilQKEG-LNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENttSLLEILTTna 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 CTHASLVPTQLWRLLVNRSSV-----SLKAVLLGGA---AIPIELTEQAreqGIRCFCGYGLTEFAST-VCAKEADG--- 285
Cdd:PRK05857 261 VATTCLVPTLLSKLVSELKSAnatvpSLRLVGYGGSraiAADVRFIEAT---GVRTAQVYGLSETGCTaLCLPTDDGsiv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 ---LADVGSPLPGREVKIVNNE-----------------VWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGK 344
Cdd:PRK05857 338 kieAGAVGRPYPGVDVYLAATDgigptapgagpsasfgtLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERReDGF 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 727407383 345 LTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFG 391
Cdd:PRK05857 418 FYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-444 |
2.50e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 103.71 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG---QGIMWrwLYAGARMTV---- 205
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGsvvTLLTP--LASGAHVVLagpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 206 --RDKQPLEQMLA-----GCTHASLVPTQLWRLL---VNRSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEF 274
Cdd:cd05944 79 gyRNPGLFDNFWKlveryRITSLSTVPTVYAALLqvpVNADISSLRFAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 275 ASTVCAKEADG---LADVGSPLPGREVKIVN----------------NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATR 335
Cdd:cd05944 159 TCLVAVNPPDGpkrPGSVGLRLPYARVRIKVldgvgrllrdcapdevGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 336 DRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDH----ESVDLSEW 410
Cdd:cd05944 239 DLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPgavvEEEELLAW 318
|
330 340 350
....*....|....*....|....*....|....*
gi 727407383 411 VKDKLA-RFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:cd05944 319 ARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
133-396 |
3.88e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 105.42 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAeGVLSLIPFGDHDDWLLS-LPLFHV------------SGQGIMWrwlya 199
Cdd:PRK07529 212 PDDVAAYFHTGGTTGMPKLAQHTHGNEVANA-WLGALLLGLGPGDTVFCgLPLFHVnallvtglaplaRGAHVVL----- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 200 GARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLL---VNRSSV-SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGY 269
Cdd:PRK07529 286 ATPQGYRGPGVIANFWKiveryRINFLSGVPTVYAALLqvpVDGHDIsSLRYALCGAAPLPVEVFRRFEAAtGVRIVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 270 GLTEFASTVCAKEADGLADVGS---PLPGREVKIV---NNEVWLRAASMAE-------------GYWRNGQLVSLVNDEG 330
Cdd:PRK07529 366 GLTEATCVSSVNPPDGERRIGSvglRLPYQRVRVVildDAGRYLRDCAVDEvgvlciagpnvfsGYLEAAHNKGLWLEDG 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 331 WYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA 396
Cdd:PRK07529 446 WLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
31-377 |
8.11e-24 |
|
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: 102.73 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 31 RELCARVDELASGFAAQGVVE-GSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQ-----------LPQPLLEELLPNL 98
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGpGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAypaerlafileDAGARLLLTDSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 TLQFALVPDGENTFPALTSLHIQR--VEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:TIGR01733 83 ASRLAGLVLPVILLDPLELAALDDapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 177 DWLLSLPL-FHVSGQGImWRWLYAGARMTVRDKQP-------LEQMLA--GCTHASLVPT--QLWRLLVNRSSVSLKAVL 244
Cdd:TIGR01733 163 RVLQFASLsFDASVEEI-FGALLAGATLVVPPEDEerddaalLAALIAehPVTVLNLTPSllALLAAALPPALASLRLVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 245 LGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTVCAKEADG-------LADVGSPLPGREVKIVNN-----------E 304
Cdd:TIGR01733 242 LGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPddapresPVPIGRPLANTRLYVLDDdlrpvpvgvvgE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 305 VWLRAASMAEGYWRNGQLVS--LVNDEG-------WYATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:TIGR01733 322 LYIGGPGVARGYLNRPELTAerFVPDPFaggdgarLYRTGDLVrYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH 401
|
...
gi 727407383 375 PAV 377
Cdd:TIGR01733 402 PGV 404
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
138-445 |
8.22e-24 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 104.33 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 138 SMTLTSGSTGLPKAAVHTYQAHLASAegvLSLI---PFGDHDDWLLSLPLFHVSGQGIMWR-WLYAGARMTVRDKQPLEQ 213
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYLST---LSAIigwEMGTCPVYLWTLPMFHCNGWTFTWGtAARGGTSVCMRHVTAPEI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 214 M----LAGCTHASLVPTqLWRLLV--NRSSVSLKA----VLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTV--CAK 281
Cdd:PLN03102 267 YknieMHNVTHMCCVPT-VFNILLkgNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlfCEW 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 282 EAD---------------------GLADV---------GSPLPGREVkivnNEVWLRAASMAEGYWRNGQLVSLVNDEGW 331
Cdd:PLN03102 346 QDEwnrlpenqqmelkarqgvsilGLADVdvknketqeSVPRDGKTM----GEIVIKGSSIMKGYLKNPKATSEAFKHGW 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 332 YATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESV--- 405
Cdd:PLN03102 422 LNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAfvVLEKGETTKedr 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 727407383 406 ---------DLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALKE 445
Cdd:PLN03102 502 vdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
28-445 |
8.74e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 103.81 E-value: 8.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPD 107
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 108 ---GENTFPAL----TSLHIQRVEGAHAAAWQPTRLCS-------------------MTLTSGSTGLPKAAVHTYQAHLA 161
Cdd:PRK05852 124 dgpHDRAEPTTrwwpLTVNVGGDSGPSGGTLSVHLDAAteptpatstpeglrpddamIMFTGGTTGLPKMVPWTHANIAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 162 SAEGVLSLIPFGDHDDWLLSLPLFHvsGQGIMWRWLY-----------AGARMTVRDKQPlEQMLAGCTHASLVPTqLWR 230
Cdd:PRK05852 204 SVRAIITGYRLSPRDATVAVMPLYH--GHGLIAALLAtlasggavllpARGRFSAHTFWD-DIKAVGATWYTAVPT-IHQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 231 LLVNRSSV--------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLADVGSP-----LPGR 296
Cdd:PRK05852 280 ILLERAATepsgrkpaALRFIRSCSAPLTAETAQALQTEfAAPVVCAFGMTEATHQVTTTQIEGIGQTENPvvstgLVGR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 297 ----EVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGE 360
Cdd:PRK05852 360 stgaQIRIVGSdglplpagavgEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSaAGDLSIRGRIKELINRGGE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 361 GIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM---EYDHESVD-LSEWVKDKLARFQQPVRW---LTLPPELKN 433
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIvprESAPPTAEeLVQFCRERLAAFEIPASFqeaSGLPHTAKG 519
|
490
....*....|..
gi 727407383 434 GgikISRQALKE 445
Cdd:PRK05852 520 S---LDRRAVAE 528
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
12-443 |
1.09e-23 |
|
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: 103.05 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQVR--GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV------- 82
Cdd:cd12117 5 EQAArtPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLdpelpae 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 ---------NPQLPQPLLEELLPNLTLQFALVPDGENTfpaltslhiQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAV 153
Cdd:cd12117 85 rlafmladaGAKVLLTDRSLAGRAGGLEVAVVIDEALD---------AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 154 HTYQAHLASAEGVlSLIPFGDHDDWLLSLPL-FHVSGQGImWRWLYAGARMTVRDKQPLEQMLA--------GCThASLV 224
Cdd:cd12117 156 VTHRGVVRLVKNT-NYVTLGPDDRVLQTSPLaFDASTFEI-WGALLNGARLVLAPKGTLLDPDAlgaliaeeGVT-VLWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 225 PTQLWRLLVN---RSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTE---FASTVCAKEADGLAD---VGSPL 293
Cdd:cd12117 233 TAALFNQLADedpECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEnttFTTSHVVTELDEVAGsipIGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 294 PGREVKIVNN-----------EVWLRAASMAEGYWRNGQL-----VSLVNDEG--WYATRDRGEMH-NGKLTIVGRLDNL 354
Cdd:cd12117 313 ANTRVYVLDEdgrpvppgvpgELYVGGDGLALGYLNRPALtaerfVADPFGPGerLYRTGDLARWLpDGRLEFLGRIDDQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDKLARFQQPVRWLTLP--PE 430
Cdd:cd12117 393 VKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAyvVAEGALDAAELRAFLRERLPAYMVPAAFVVLDelPL 472
|
490
....*....|...
gi 727407383 431 LKNGgiKISRQAL 443
Cdd:cd12117 473 TANG--KVDRRAL 483
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
17-444 |
1.19e-23 |
|
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: 102.83 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfalvPDgentFPALTSLHIQRVEGAHAAAWQ-PTRLCSMTLTSGSTGLPKAAVHTYQA---HLASAEGVLSLIPf 172
Cdd:cd17649 69 ---------PE----YPAERLRYMLEDSGAGLLLTHhPRQLAYVIYTSGSTGTPKGVAVSHGPlaaHCQATAERYGLTP- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 173 GDHDdwllsLPLFHVSGQGIMWRW---LYAGARMTVRDKQPL--EQMLA------GCTHASLvPTQLWRLLV-------N 234
Cdd:cd17649 135 GDRE-----LQFASFNFDGAHEQLlppLICGACVVLRPDELWasADELAemvrelGVTVLDL-PPAYLQQLAeeadrtgD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 235 RSSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTE--FASTVCAKEAD-----GLADVGSPLPGREVKIVNN---- 303
Cdd:cd17649 209 GRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEatVTPLVWKCEAGaaragASMPIGRPLGGRSAYILDAdlnp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -------EVWLRAASMAEGYWRNGQLVS--LVND----EG--WYATRD--RGeMHNGKLTIVGRLDNLFFSGGEGIQPEE 366
Cdd:cd17649 289 vpvgvtgELYIGGEGLARGYLGRPELTAerFVPDpfgaPGsrLYRTGDlaRW-RDDGVIEYLGRVDHQVKIRGFRIELGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 367 VERVIAAHPAVLQVFIVPVaDKEFGHRPVA--VMEYDHESVDLSE----WVKDKLARFQQPVRWLTLP--PELKNGgiKI 438
Cdd:cd17649 368 IEAALLEHPGVREAAVVAL-DGAGGKQLVAyvVLRAAAAQPELRAqlrtALRASLPDYMVPAHLVFLArlPLTPNG--KL 444
|
....*.
gi 727407383 439 SRQALK 444
Cdd:cd17649 445 DRKALP 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
142-428 |
1.65e-23 |
|
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: 100.65 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMW-RWLYAGAR---MTVRDKQPLEQMLAg 217
Cdd:cd17638 8 TSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIvACLLTGATvvpVAVFDVDAILEAIE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 cTHASLV----PTQLWRLLV-----NRSSVSLKAVLLGGAAIPIELTEQAREQ-GIR-CFCGYGLTEFASTVCAKEADGL 286
Cdd:cd17638 87 -RERITVlpgpPTLFQSLLDhpgrkKFDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTEAGVATMCRPGDDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 ADV----GSPLPGREVKIVNN-EVWLRAASMAEGYWRNGQLVS-LVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGG 359
Cdd:cd17638 166 ETVattcGRACPGFEVRIADDgEVLVRGYNVMQGYLDDPEATAeAIDADGWLHTGDVGELdERGYLRITDRLKDMYIVGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 360 EGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--------RPVAVMEYDhesvDLSEWVKDKLARFQQP--VRWL-TLP 428
Cdd:cd17638 246 FNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEvgkafvvaRPGVTLTEE----DVIAWCRERLANYKVPrfVRFLdELP 321
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
19-391 |
9.35e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 100.83 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNL 98
Cdd:PRK06188 29 PALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 TLQfALVPDGeNTFPALTSLHIQRVEG-----------------AHAAAWQPTRL---------CSMTLTSGSTGLPKAA 152
Cdd:PRK06188 109 GIS-TLIVDP-APFVERALALLARVPSlkhvltlgpvpdgvdllAAAAKFGPAPLvaaalppdiAGLAYTGGTTGKPKGV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 153 VHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGI---MWRwlyaGARMTVRDKQPLEQMLA-----GCTHASLV 224
Cdd:PRK06188 187 MGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFlptLLR----GGTVIVLAKFDPAEVLRaieeqRITATFLV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 225 PTQLWRLL-----VNRSSVSLKAVLLGGAAI-PIELTEQAREQGIRCFCGYGLTEFASTVC--------AKEADGLADVG 290
Cdd:PRK06188 263 PTMIYALLdhpdlRTRDLSSLETVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEAPMVITylrkrdhdPDDPKRLTSCG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 291 SPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSG 358
Cdd:PRK06188 343 RPTPGLRVALLDEdgrevaqgevgEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREdEDGFYYIVDRKKDMIVTG 422
|
410 420 430
....*....|....*....|....*....|...
gi 727407383 359 GEGIQPEEVERVIAAHPAVLQVFIVPVADKEFG 391
Cdd:PRK06188 423 GFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWG 455
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
26-383 |
1.30e-22 |
|
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: 99.74 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpVNpqlpqplleellpnltlqfalV 105
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA----VD---------------------V 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 106 PDGeNTFPALTSLHIQRVEGAHAAAWQ--PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:cd17640 59 VRG-SDSSVEELLYILNHSESVALVVEndSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 184 LFH---------VSGQGI---------------------------MWRWLYAGARMTVRDKQPLEQMLAGCThaslvptq 227
Cdd:cd17640 138 IWHsyersaeyfIFACGCsqaytsirtlkddlkrvkphyivsvprLWESLYSGIQKQVSKSSPIKQFLFLFF-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 228 lwrLLVNRssvsLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVNNE- 304
Cdd:cd17640 210 ---LSGGI----FKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCnvRGSVGRPLPGTEIKIVDPEg 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 305 -----------VWLRAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEM-HNGKLTIVGRL-DNLFFSGGEGIQPEEVERV 370
Cdd:cd17640 283 nvvlppgekgiVWVRGPQVMKGYYKNPEATSKVlDSDGWFNTGDLGWLtCGGELVLTGRAkDTIVLSNGENVEPQPIEEA 362
|
410
....*....|...
gi 727407383 371 IAAHPAVLQVFIV 383
Cdd:cd17640 363 LMRSPFIEQIMVV 375
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
130-450 |
1.88e-22 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.87 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 130 AWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK- 208
Cdd:PLN02860 168 AWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKf 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 ------QPLEQMlaGCTHASLVPTQLWRLL-VNRSSV------SLKAVLLGGAAIPIELTEQARE--QGIRCFCGYGLTE 273
Cdd:PLN02860 248 dakaalQAIKQH--NVTSMITVPAMMADLIsLTRKSMtwkvfpSVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 274 FASTV---------CAKEADGLAD----------------VGSPLPGREVKIVNNE------VWLRAASMAEGYWrnGQL 322
Cdd:PLN02860 326 ACSSLtfmtlhdptLESPKQTLQTvnqtksssvhqpqgvcVGKPAPHVELKIGLDEssrvgrILTRGPHVMLGYW--GQN 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 323 VSLVND---EGWYATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM 398
Cdd:PLN02860 404 SETASVlsnDGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 727407383 399 eydhesvdlsewvkdklaRFQQPVRWLTLPPELKNGGIKISRQALKEWVQRQ 450
Cdd:PLN02860 484 ------------------RLRDGWIWSDNEKENAKKNLTLSSETLRHHCREK 517
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
140-444 |
2.17e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 100.11 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 140 TLTSGSTGLPKAAVHTYQAHLASAEGV----LSLIPfgdHDDWLLSLPLFHVSGQG-IMWRWLYAGARMTVrDKQPLEQM 214
Cdd:PRK06060 151 TYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTP---EDTGLCSARMYFAYGLGnSVWFPLATGGSAVI-NSAPVTPE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LAGCTHASLVPTQLWRL------LVNRSSV----SLKAVLLGGAAIPIELTEQARE--QGIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK06060 227 AAAILSARFGPSVLYGVpnffarVIDSCSPdsfrSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTEVGQTFVSNR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 283 ADG--LADVGSPLPGREVKIV-----------NNEVWLRAASMAEGYWRNGQlvSLVNDEGWYATRDRGEMH-NGKLTIV 348
Cdd:PRK06060 307 VDEwrLGTLGRVLPPYEIRVVapdgttagpgvEGDLWVRGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDsDGWVTYR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVadKEFGHRPV-------AVMEYDHESV--DLSEWVKDKLARFQ 419
Cdd:PRK06060 385 CRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTlqaflvaTSGATIDGSVmrDLHRGLLNRLSAFK 462
|
330 340
....*....|....*....|....*..
gi 727407383 420 QPVRWLTLP--PELKNGgiKISRQALK 444
Cdd:PRK06060 463 VPHRFAVVDrlPRTPNG--KLVRGALR 487
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-445 |
4.62e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 98.47 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN--------------- 83
Cdd:PRK08316 28 TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNfmltgeelayildhs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ----------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAwqpTRLCSMTLTSGSTG 147
Cdd:PRK08316 108 garaflvdpalaptaeAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELAD---DDLAQILYTSGTES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 148 LPKAAVHTYQAHLAsaEGVLSLIP--FGDHDDWLLSLPLFHvSGQ--GIMWRWLYAGARMTVRDKQPLEQMLA-----GC 218
Cdd:PRK08316 185 LPKGAMLTHRALIA--EYVSCIVAgdMSADDIPLHALPLYH-CAQldVFLGPYLYVGATNVILDAPDPELILRtieaeRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 219 THASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFA--STVC-AKEADGLA 287
Cdd:PRK08316 262 TSFFAPPT-VWISLLRhpdfdtRDLSSLRKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAplATVLgPEEHLRRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 D-VGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNL 354
Cdd:PRK08316 341 GsAGRPVLNVETRVVDDdgndvapgevgEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMdEEGYITVVDRKKDM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAV------MEYDHEsvDLSEWVKDKLARFQQPVRWL--- 425
Cdd:PRK08316 421 IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVvvpkagATVTED--ELIAHCRARLAGFKVPKRVIfvd 498
|
490 500
....*....|....*....|
gi 727407383 426 TLPpelKNGGIKISRQALKE 445
Cdd:PRK08316 499 ELP---RNPSGKILKRELRE 515
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
15-423 |
6.09e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 98.02 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 15 RGETIALRLNDEQ-LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN---------- 83
Cdd:PRK07514 15 DRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNtaytlaeldy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 --------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSlhiQRVEGAHAAAWQPTRLCSMTLTSGSTGLP 149
Cdd:PRK07514 95 figdaepalvvcdpANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAA---AAPDDFETVPRGADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 150 KAAVHTYQAHLASAEGVLSLIPFGDhDDWLL-SLPLFHVSG-----QGImwrwLYAGARMTVRDKQPLEQMLAGCTHASL 223
Cdd:PRK07514 172 KGAMLSHGNLLSNALTLVDYWRFTP-DDVLIhALPIFHTHGlfvatNVA----LLAGASMIFLPKFDPDAVLALMPRATV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 224 ---VPTQLWRLL----VNRSSVSLKAVLLGGAAiPIeLTEQARE----QGIRCFCGYGLTE---FASTVCAKEADGlADV 289
Cdd:PRK07514 247 mmgVPTFYTRLLqeprLTREAAAHMRLFISGSA-PL-LAETHREfqerTGHAILERYGMTEtnmNTSNPYDGERRA-GTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 290 GSPLPGREVKIVNNE------------VWLRAASMAEGYWRN-GQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLF 355
Cdd:PRK07514 324 GFPLPGVSLRVTDPEtgaelppgeigmIEVKGPNVFKGYWRMpEKTAEEFRADGFFITGDLGKIdERGYVHIVGRGKDLI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 356 FSGGEGIQPEEVERVIAAHPAVLQ--VFIVPVADkeFGHRPVAV------MEYDHESVdLSEwVKDKLARFQQPVR 423
Cdd:PRK07514 404 ISGGYNVYPKEVEGEIDELPGVVEsaVIGVPHPD--FGEGVTAVvvpkpgAALDEAAI-LAA-LKGRLARFKQPKR 475
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
17-443 |
1.39e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 96.62 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpvnpqlpqplleellp 96
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfALVPDGENTFPALTSLHIQRVEGAHAAAwQPTRLCSMTLTSGSTGLPK---------AAVHTYQAHLASAE--- 164
Cdd:cd12115 75 ------AYVPLDPAYPPERLRFILEDAQARLVLT-DPDDLAYVIYTSGSTGRPKgvaiehrnaAAFLQWAAAAFSAEela 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 165 GVLSLIPFGdhddwlLSLPLFHVSGQgimwrwLYAGARMTVRDKQ---PLEQMLAGCTHASLVPTQLWRLL-VNRSSVSL 240
Cdd:cd12115 148 GVLASTSIC------FDLSVFELFGP------LATGGKVVLADNVlalPDLPAAAEVTLINTVPSAAAELLrHDALPASV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 241 KAVLLGGAAIPIELTE--QAREQGIRCFCGYGLTEFA--STVCA--KEADGLADVGSPLPGREVKIVNN----------- 303
Cdd:cd12115 216 RVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTtySTVAPvpPGASGEVSIGRPLANTQAYVLDRalqpvplgvpg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 EVWLRAASMAEGYWRNGQLVS---LVNDEG----WYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHP 375
Cdd:cd12115 296 ELYIGGAGVARGYLGRPGLTAerfLPDPFGpgarLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIP 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727407383 376 AVLQVFIVPVADKEFGHRPVA--VMEYDHESV--DLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd12115 376 GVREAVVVAIGDAAGERRLVAyiVAEPGAAGLveDLRRHLGTRLPAYMVPSRFVRLDalPLTPNG--KIDRSAL 447
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
20-444 |
1.40e-21 |
|
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: 96.39 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELASGFAAQGV-VEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellpnl 98
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATM--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 tlqfALVPDGENTFPaltslhIQRVEGAHA-AAWQPTR---LCSMTLTSGSTGLPKAAVHTYQAHLASAEG----VLSLI 170
Cdd:cd05958 68 ----PLLRPKELAYI------LDKARITVAlCAHALTAsddICILAFTSGTTGAPKATMHFHRDPLASADRyavnVLRLR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 171 PfgdhDDWLLSLP-LFHVSGQGIMWRW-LYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQLWRLL-----VNRSSV 238
Cdd:cd05958 138 E----DDRFVGSPpLAFTFGLGGVLLFpFGVGASGVLLEEATPDLLLSaiaryKPTVLFTAPTAYRAMLahpdaAGPDLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTE-FASTVCAKEADG-LADVGSPLPGREVKIVNN--------EVWL 307
Cdd:cd05958 214 SLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEmFHIFISARPGDArPGATGKPVPGYEAKVVDDegnpvpdgTIGR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 308 RAASMAEGYWRNGQLVSLVN-DEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPV 385
Cdd:cd05958 294 LAVRGPTGCRYLADKRQRTYvQGGWNITGDTYSRDpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGH 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 386 ADKEFGHRPVA--VMEYDHESV-----DLSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05958 374 PDESRGVVVKAfvVLRPGVIPGpvlarELQDHAKAHIAPYKYP-RAIEFVTELpRTATGKLQRFALR 439
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-444 |
1.60e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 96.35 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfALV 105
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS-ALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 106 PDGENTfPALtslhiqrvegahaaawqptrlcsMTLTSGSTGLPKAAVHTYQ---AHLASAEGVLSLIP-----FGDHDD 177
Cdd:cd05971 84 TDGSDD-PAL-----------------------IIYTSGTTGPPKGALHAHRvllGHLPGVQFPFNLFPrdgdlYWTPAD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 178 WLLSLPLFhvsgqGIMWRWLYAGA-----RMTVRDKQPLEQMLA--GCTHASLVPTQLwRLL------VNRSSVSLKAVL 244
Cdd:cd05971 140 WAWIGGLL-----DVLLPSLYFGVpvlahRMTKFDPKAALDLMSryGVTTAFLPPTAL-KMMrqqgeqLKHAQVKLRAIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 245 LGGAAIPIELTEQAREQ-GIRCFCGYGLTE--FASTVCAKEADGL-ADVGSPLPGREVKIVNNE-------------VWL 307
Cdd:cd05971 214 TGGESLGEELLGWAREQfGVEVNEFYGQTEcnLVIGNCSALFPIKpGSMGKPIPGHRVAIVDDNgtplppgevgeiaVEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 308 RAASMAEGYWRNGQLVSLVNDEGWYATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVA 386
Cdd:cd05971 294 PDPVAFLGYWNNPSATEKKMAGDWLLTGDLGrKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727407383 387 D-------KEFGHRPVAVMEYDHESVDLSEWVKDKLARFQQPvRWLTLPPEL---KNGgiKISRQALK 444
Cdd:cd05971 374 DpirgeivKAFVVLNPGETPSDALAREIQELVKTRLAAHEYP-REIEFVNELprtATG--KIRRRELR 438
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
142-449 |
1.87e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 96.74 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG--QGIMWRWLyAGARMTVRD----KQPLEQM- 214
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGflHGVTAPFL-IGARSVLLDiftpDACLALLe 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LAGCTHASLVPTQLWRLLVNRSS-----VSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADGL--- 286
Cdd:PRK06087 274 QQRCTCMLGATPFIYDLLNLLEKqpadlSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLsrf 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 -ADVGSPLPGREVKIVN---NEVWL--------RAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEM-HNGKLTIVGRLD 352
Cdd:PRK06087 354 mHTDGYAAAGVEIKVVDearKTLPPgcegeeasRGPNVFMGYLDEPELTARAlDEEGWYYSGDLCRMdEAGYIKITGRKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWV----KDKLARFQQPVRWLT 426
Cdd:PRK06087 434 DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAyvVLKAPHHSLTLEEVVaffsRKRVAKYKYPEHIVV 513
|
330 340
....*....|....*....|....*
gi 727407383 427 LP--PELKNGGIKISRQAlKEWVQR 449
Cdd:PRK06087 514 IDklPRTASGKIQKFLLR-KDIMRR 537
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
134-445 |
2.08e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.97 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 134 TRLCSMTLTSGSTGLPKAAVHTYQ---AHLASA------EGVLSLIPFGdhddwllSLPLFHVSG-QGIMWRWLYAGARM 203
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRnlvANLCSSlfsvgpEMIGQVVTLG-------LIPFFHIYGiTGICCATLRNKGKV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 204 TVRDKQPLEQMLAG-----CTHASLVPTQLWRLLVNR-------SSVSLKAVLLGGAAIPIELTE--QAREQGIRCFCGY 269
Cdd:PLN02330 257 VVMSRFELRTFLNAlitqeVSFAPIVPPIILNLVKNPiveefdlSKLKLQAIMTAAAPLAPELLTafEAKFPGVQVQEAY 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 270 GLTEFaSTVCAKEAD-----GLA---DVGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQLVS-LVND 328
Cdd:PLN02330 337 GLTEH-SCITLTHGDpekghGIAkknSVGFILPNLEVKFIDpdtgrslpkntpGELCVRSQCVMQGYYNNKEETDrTIDE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 329 EGWYATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV-- 405
Cdd:PLN02330 416 DGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKes 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 727407383 406 --DLSEWVKDKLARFQQ--PVRWLTLPPELKNGgiKISRQALKE 445
Cdd:PLN02330 496 eeDILNFVAANVAHYKKvrVVQFVDSIPKSLSG--KIMRRLLKE 537
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
13-448 |
2.11e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 96.55 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 13 QVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLA--------------------- 71
Cdd:PRK08162 29 EVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGvpmagavlntlntrldaasia 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 72 --LLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAA-----AWQPTR----LCSMT 140
Cdd:PRK08162 109 fmLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASgdpdfAWTLPAdewdAIALN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 141 LTSGSTGLPKAAV-HTYQAHLASAEGVLSLiPFGDHDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVR--DKQPLEQMLA 216
Cdd:PRK08162 189 YTSGTTGNPKGVVyHHRGAYLNALSNILAW-GMPKHPVYLWTLPMFHCNGWCFPWTVaARAGTNVCLRkvDPKLIFDLIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 --GCTHASLVPTQLwRLLVN-----RSSVSLK-AVLLGGAAIPIELTEQAREQGIRCFCGYGLTEF--ASTVCAKEA--D 284
Cdd:PRK08162 268 ehGVTHYCGAPIVL-SALINapaewRAGIDHPvHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETygPATVCAWQPewD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 GLAD---------------------VGSPLPGREVKIVNN---EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM 340
Cdd:PRK08162 347 ALPLderaqlkarqgvryplqegvtVLDPDTMQPVPADGEtigEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 341 H-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEY-DHESV---DLSEWVKDKL 415
Cdd:PRK08162 427 HpDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELkDGASAteeEIIAHCREHL 506
|
490 500 510
....*....|....*....|....*....|....*
gi 727407383 416 ARFQQP--VRWLTLPpelKNGGIKISRQALKEWVQ 448
Cdd:PRK08162 507 AGFKVPkaVVFGELP---KTSTGKIQKFVLREQAK 538
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
9-445 |
3.79e-21 |
|
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: 95.52 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGeTIALRLNDEQLNWRElcaRVdelasgFAAQGVVEGSGVMLRAWN---TPQTLLAWLALLQCGARVLPVNPQ 85
Cdd:cd05929 9 AQVFHQRR-LLLLDVYSIALNRNA---RA------AAAEGVWIADGVYIYLINsilTVFAAAAAWKCGACPAYKSSRAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 86 LPQPLLEELLPNLTLqfALVPDGENTFPALTSLhiqrvegAHAAAWQPTRLCS-------MTLTSGSTGLPKA------A 152
Cdd:cd05929 79 AEACAIIEIKAAALV--CGLFTGGGALDGLEDY-------EAAEGGSPETPIEdeaagwkMLYSGGTTGRPKGikrglpG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 153 VHTYQAHLASAEGvlsLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVPTQ 227
Cdd:cd05929 150 GPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRlieryRVTFAQFVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 228 LWRLL------VNRSSV-SLKAVLLGGAAIPIELTEQARE-QGIRCFCGYGLTE-FASTVCAKEaDGLA---DVGSPLPG 295
Cdd:cd05929 227 FVRLLklpeavRNAYDLsSLKRVIHAAAPCPPWVKEQWIDwGGPIIWEYYGGTEgQGLTIINGE-EWLThpgSVGRAVLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 rEVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:cd05929 306 -KVHILDEdgnevppgeigEVYFANGPGFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 364 PEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV-------DLSEWVKDKLARFQQP--VRWLTLPPELKNG 434
Cdd:cd05929 385 PQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADagtalaeELIAFLRDRLSRYKCPrsIEFVAELPRDDTG 464
|
490
....*....|.
gi 727407383 435 giKISRQALKE 445
Cdd:cd05929 465 --KLYRRLLRD 473
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
133-383 |
5.81e-21 |
|
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: 95.23 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-GIMWRWLYAG----------- 200
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERvFVEGGSLYGGvlvafaesldt 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 201 -------ARMTVRDKQP-LEQMLAGCTHASLVPTQLWRLL----VNR-------SSVSLKAV--LLGGAA-IPIELTEQA 258
Cdd:cd05932 216 fvedvqrARPTLFFSVPrLWTKFQQGVQDKIPQQKLNLLLkipvVNSlvkrkvlKGLGLDQCrlAGCGSApVPPALLEWY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 259 REQGIRCFCGYGLTE-FA-STVCAKEADGLADVGSPLPGREVKIVNN-EVWLRAASMAEGYWRNG-QLVSLVNDEGWYAT 334
Cdd:cd05932 296 RSLGLNILEAYGMTEnFAySHLNYPGRDKIGTVGNAGPGVEVRISEDgEILVRSPALMMGYYKDPeATAEAFTADGFLRT 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 727407383 335 RDRGEM-HNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAHPAVLQVFIV 383
Cdd:cd05932 376 GDKGELdADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-409 |
8.28e-21 |
|
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: 94.71 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-QGIMWRWLYAGARM--------------TVR 206
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKVvfhpnpldykkipeLIY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 207 DKqpleqmlaGCTHASLVPTQLwRLLVNRSS----VSLKAVLLGGAAIPIELTEQARE-QGIRCFCGYGLTEfASTVCA- 280
Cdd:cd05909 235 DK--------KATILLGTPTFL-RGYARAAHpedfSSLRLVVAGAEKLKDTLRQEFQEkFGIRILEGYGTTE-CSPVISv 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 281 --KEADGLAD-VGSPLPGREVKIVNNE------------VWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGK 344
Cdd:cd05909 305 ntPQSPNKEGtVGRPLPGMEVKIVSVEtheevpigegglLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIdGEGF 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 345 LTIVGRLDNLFFSGGEGIQPEEVERVIAAH-PAVLQVFIVPVADKEFGHRPVAVmeYDHESVDLSE 409
Cdd:cd05909 385 LTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL--TTTTDTDPSS 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-443 |
8.90e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 8 WRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLP 87
Cdd:PRK12316 517 FEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 88 QPLLEELLPNLTLQFALVPDGENTFPALtSLHIQRVEGAHAAAWQP--------TRLCSMTL-----TSGSTGLPKAAVH 154
Cdd:PRK12316 597 AERLAYMLEDSGVQLLLSQSHLGRKLPL-AAGVQVLDLDRPAAWLEgyseenpgTELNPENLayviyTSGSTGKPKGAGN 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 155 TYQA---HLASAEGVLSLipfGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLEQMLA--GCTHAS 222
Cdd:PRK12316 676 RHRAlsnRLCWMQQAYGL---GVGDTVLQKTPFsFDVSVWEFFWP-LMSGARLVVaapgdhRDPAKLVELINreGVDTLH 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 223 LVPTQLWRLLVN---RSSVSLKAVLLGGAAIPIELTEQ--AREQGIRCFCGYGLTEFASTV----CAKEADGLADVGSPL 293
Cdd:PRK12316 752 FVPSMLQAFLQDedvASCTSLRRIVCSGEALPADAQEQvfAKLPQAGLYNLYGPTEAAIDVthwtCVEEGGDSVPIGRPI 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 294 PGREVKI-----------VNNEVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGEMH-NGKLTIVGRLDNL 354
Cdd:PRK12316 832 ANLACYIldanlepvpvgVLGELYLAGRGLARGYHGRPGLTAerfvpspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLARFQQPVRWLTLP--PELK 432
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALErlPLTP 991
|
490
....*....|.
gi 727407383 433 NGgiKISRQAL 443
Cdd:PRK12316 992 NG--KLDRKAL 1000
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-444 |
1.29e-20 |
|
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: 93.56 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVnpqlpqplleellpnltlqfalvpd 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 108 gentFPALTSLHI-QRVE--GAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQ---AHLASAEGVLSLIPFGDHddWLLS 181
Cdd:cd05972 56 ----TTLLGPKDIeYRLEaaGAKAIVTDAEDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIH--WNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 182 LP--LFHVSGqGIMWRWLyAGARMTVRDKQPL--EQMLA-----GCTHASLVPTqLWRLLV-----NRSSVSLKAVLLGG 247
Cdd:cd05972 130 DPgwAKGAWS-SFFGPWL-LGATVFVYEGPRFdaERILElleryGVTSFCGPPT-AYRMLIkqdlsSYKFSHLRLVVSAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 248 AAIPIELTEQAREQ-GIRCFCGYGLTEFASTV----CAKEADGlaDVGSPLPGREVKIVNNE-------------VWLRA 309
Cdd:cd05972 207 EPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVgnfpDMPVKPG--SMGRPTPGYDVAIIDDDgrelppgeegdiaIKLPP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 310 ASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADK 388
Cdd:cd05972 285 PGLFLGYVGDPEKTEASIRGDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727407383 389 EFGHRPVA--VMEYDHESVD-----LSEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05972 365 VRGEVVKAfvVLTSGYEPSEelaeeLQGHVKKVLAPYKYP-REIEFVEELpKTISGKIRRVELR 427
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
142-423 |
1.50e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 94.30 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLS-LPLFHVSGQGI-MWRWLYAGARM----TVRDKQPLEQM 214
Cdd:PRK05605 227 TSGTTGKPKGAQLTHRNLFANAAQGKAWVPgLGDGPERVLAaLPMFHAYGLTLcLTLAVSIGGELvllpAPDIDLILDAM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 -------LAGcthaslVPTQLWRLLV--NRSSVSLKAV---LLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAK 281
Cdd:PRK05605 307 kkhpptwLPG------VPPLYEKIAEaaEERGVDLSGVrnaFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGN 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 282 ---EADGLADVGSPLPGREVKIVN-------------NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGK 344
Cdd:PRK05605 381 pmsDDRRPGYVGVPFPDTEVRIVDpedpdetmpdgeeGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEeDGF 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 345 LTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VMEYDHESVD---LSEWVKDKLARFQQ 420
Cdd:PRK05605 461 IRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAaVVLEPGAALDpegLRAYCREHLTRYKV 540
|
...
gi 727407383 421 PVR 423
Cdd:PRK05605 541 PRR 543
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
133-414 |
2.90e-20 |
|
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: 93.43 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTLTSGSTGLPKAAVHTyQAHLASAEGVLSLIPFG----DHDDWLLS-LPLFHVSGQGIMWRWLYAGARM---- 203
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLT-HGNIVSNVAGVFKILEIlnkiNPTDVYISyLPLAHIFERVVEALFLYHGAKIgfys 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 204 ----------------------------------TVRDKQPLEQML---------AGCTHASLVPTQLWRLLV-NRSSVS 239
Cdd:cd05927 192 gdirlllddikalkptvfpgvprvlnriydkifnKVQAKGPLKRKLfnfalnyklAELRSGVVRASPFWDKLVfNKIKQA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 240 L----KAVLLGGAAIPIELTEQAREqgirCFC-----GYGLTE-FASTVCAKEADGLA-DVGSPLPGREVKIV------- 301
Cdd:cd05927 272 LggnvRLMLTGSAPLSPEVLEFLRV----ALGcpvleGYGQTEcTAGATLTLPGDTSVgHVGGPLPCAEVKLVdvpemny 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 302 ----NN---EVWLRAASMAEGYWRNGQLVSLVNDE-GWYATRDRGE-MHNGKLTIVGRLDNLF-FSGGEGIQPEEVERVI 371
Cdd:cd05927 348 dakdPNprgEVCIRGPNVFSGYYKDPEKTAEALDEdGWLHTGDIGEwLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIY 427
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 727407383 372 AAHPAVLQVFIVPVADKEFghrPVAVMEYDHESVDlsEWVKDK 414
Cdd:cd05927 428 ARSPFVAQIFVYGDSLKSF---LVAIVVPDPDVLK--EWAASK 465
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
9-422 |
5.35e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 92.41 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQ 88
Cdd:PRK06178 40 RAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFRE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 PLLEELLPNLTLQFALVPD----------------------------GENTFPALTSLHIQR--VEGAH------AAAWQ 132
Cdd:PRK06178 120 HELSYELNDAGAEVLLALDqlapvveqvraetslrhvivtsladvlpAEPTLPLPDSLRAPRlaAAGAIdllpalRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTL--------TSGSTGLPKAAVHTyQAHL---ASAEGVLSLIpfGDHDDWLLS-LPLFHVSGQ--GIMWRwLY 198
Cdd:PRK06178 200 PVPLPPPALdalaalnyTGGTTGMPKGCEHT-QRDMvytAAAAYAVAVV--GGEDSVFLSfLPEFWIAGEnfGLLFP-LF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 199 AGARMTVRDK-QPLEQMLA----GCTHASLVPTQLWRLLvNRSSV------SLKAVllGGAAIPIELTEQAREQ------ 261
Cdd:PRK06178 276 SGATLVLLARwDAVAFMAAveryRVTRTVMLVDNAVELM-DHPRFaeydlsSLRQV--RVVSFVKKLNPDYRQRwraltg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 262 GIRCFCGYGLTEF--ASTVCAKEADGLAD-------VGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNG 320
Cdd:PRK06178 353 SVLAEAAWGMTEThtCDTFTAGFQDDDFDllsqpvfVGLPVPGTEFKICDfetgellplgaeGEIVVRTPSLLKGYWNKP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 321 QLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VM 398
Cdd:PRK06178 433 EATAEALRDGWLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAfVQ 512
|
490 500
....*....|....*....|....*..
gi 727407383 399 ---EYDHESVDLSEWVKDKLARFQQPV 422
Cdd:PRK06178 513 lkpGADLTAAALQAWCRENMAVYKVPE 539
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
17-443 |
1.31e-19 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 90.96 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPvnpqlpqplleellp 96
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfaLVPDgentFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd17644 80 -------LDPN----YPQERLTYILEDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 177 DWLLSLPL-FHVSGQGIMWRWlYAGARMTVRDKQ---PLEQMLAGCTHASL----VPTQLWRLLVNRSSVS-------LK 241
Cdd:cd17644 149 RVLQFASIaFDVAAEEIYVTL-LSGATLVLRPEEmrsSLEDFVQYIQQWQLtvlsLPPAYWHLLVLELLLStidlpssLR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 242 AVLLGGAAIPIELTEQARE---QGIRCFCGYGLTE--FASTVCAKEADGLAD-----VGSPLPGREVKI----------- 300
Cdd:cd17644 228 LVIVGGEAVQPELVRQWQKnvgNFIQLINVYGPTEatIAATVCRLTQLTERNitsvpIGRPIANTQVYIldenlqpvpvg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 VNNEVWLRAASMAEGYWRNGQLVS--LVND-------EGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVERV 370
Cdd:cd17644 308 VPGELHIGGVGLARGYLNRPELTAekFISHpfnssesERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 371 IAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHE--SVDLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17644 388 LSQHNDVKTAVVIVREDQPGNKRLVAyiVPHYEESpsTVELRQFLKAKLPDYMIPSAFVVLEelPLTPNG--KIDRRAL 464
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
12-445 |
3.80e-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: 90.69 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQVR--GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqp 89
Cdd:COG1020 484 AQAArtPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD------ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 90 lleellpnltlqfalvPD--------------------GENTFPALTSLHIQRVE------GAHAAAWQPTRLCSMTL-- 141
Cdd:COG1020 558 ----------------PAypaerlaymledagarlvltQSALAARLPELGVPVLAldalalAAEPATNPPVPVTPDDLay 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 ---TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGImWRWLYAGARM------TVRDKQPL 211
Cdd:COG1020 622 viyTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsFDASVWEI-FGALLSGATLvlappeARRDPAAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 212 EQMLA--GCTHASLVPTqLWRLLVN---RSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTVCAKEAD 284
Cdd:COG1020 701 AELLArhRVTVLNLTPS-LLRALLDaapEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETTVDSTYYEVT 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 GLAD------VGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVS--------LVNDEGWYATRDRGE 339
Cdd:COG1020 780 PPDAdggsvpIGRPIANTRVYVLDAhlqpvpvgvpgELYIGGAGLARGYLNRPELTAerfvadpfGFPGARLYRTGDLAR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 340 MH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLAR- 417
Cdd:COG1020 860 WLpDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALl 939
|
490 500 510
....*....|....*....|....*....|.
gi 727407383 418 ---FQQPVRWLTLPPELKNGGIKISRQALKE 445
Cdd:COG1020 940 lppYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-396 |
1.15e-18 |
|
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: 88.04 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLS-LPLFHV---SGQGIMwrwLYAGARM------TVRDK-- 208
Cdd:cd17639 96 TSGSTGNPKGVMLTHGNLVAGIAGLGDRVPeLLGPDDRYLAyLPLAHIfelAAENVC---LYRGGTIgygsprTLTDKsk 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 ----------QP---------------------------------------LEQMLAGCThaslvpTQLWRLLV------ 233
Cdd:cd17639 173 rgckgdltefKPtlmvgvpaiwdtirkgvlaklnpmgglkrtlfwtayqskLKALKEGPG------TPLLDELVfkkvra 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 234 ---NRssvsLKAVLLGGAAipieLTEQAREQGIRCFC----GYGLTEfasTVCAKEADGLAD-----VGSPLPGREVKIV 301
Cdd:cd17639 247 algGR----LRYMLSGGAP----LSADTQEFLNIVLCpviqGYGLTE---TCAGGTVQDPGDletgrVGPPLPCCEIKLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 302 N--------------NEVWLRAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQP 364
Cdd:cd17639 316 DweeggystdkppprGEILIRGPNVFKGYYKNPEKTKEAfDGDGWFHTGDIGEFHpDGTLKIIDRKKDLVkLQNGEYIAL 395
|
330 340 350
....*....|....*....|....*....|..
gi 727407383 365 EEVERVIAAHPAVLQVFIVPVADKEFghrPVA 396
Cdd:cd17639 396 EKLESIYRSNPLVNNICVYADPDKSY---PVA 424
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
12-445 |
2.40e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.51 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQVR--GETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQL--- 86
Cdd:PRK06155 29 RQAEryPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALrgp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 87 --PQPLLEELLPNLTLQFALVPDGENTFPALTSL-HIQRVEGAHAAAW---------------------QPTRLCSMTLT 142
Cdd:PRK06155 109 qlEHILRNSGARLLVVEAALLAALEAADPGDLPLpAVWLLDAPASVSVpagwstaplppldapapaaavQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 143 SGSTGL------PKAAVHTYQAHLASAEGVlslipfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA 216
Cdd:PRK06155 189 SGTTGPskgvccPHAQFYWWGRNSAEDLEI------GADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 -----GCTHASLVPTQLWRLLVNRSSVSLKA----VLLGGaAIPIELTEQAREQ-GIRCFCGYGLTEfASTVCA--KEAD 284
Cdd:PRK06155 263 avrrhGATVTYLLGAMVSILLSQPARESDRAhrvrVALGP-GVPAALHAAFRERfGVDLLDGYGSTE-TNFVIAvtHGSQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 GLADVGSPLPGREVKIVNN-----------EVWLRAA---SMAEGY----------WRNgqlvslvndeGWYATRDRGEM 340
Cdd:PRK06155 341 RPGSMGRLAPGFEARVVDEhdqelpdgepgELLLRADepfAFATGYfgmpektveaWRN----------LWFHTGDRVVR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAdKEFGHRPV--AVMEYDHES---VDLSEWVKDK 414
Cdd:PRK06155 411 dADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVmaAVVLRDGTAlepVALVRHCEPR 489
|
490 500 510
....*....|....*....|....*....|...
gi 727407383 415 LARFQQP--VRWLTLPPELKNGgiKISRQALKE 445
Cdd:PRK06155 490 LAYFAVPryVEFVAALPKTENG--KVQKFVLRE 520
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
132-412 |
6.71e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 86.31 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV-------------------SG--Q 190
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIyervnqivmlhygvavgfyQGdnL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 191 GIM-----------------WRWLYAGARMTVRDKQPLEQMLAGCTHAS--------LVPTQLW-RLLVNRssvsLKAVL 244
Cdd:PLN02736 299 KLMddlaalrptifcsvprlYNRIYDGITNAVKESGGLKERLFNAAYNAkkqalengKNPSPMWdRLVFNK----IKAKL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 245 LG-------GAAiPI--ELTEQAREQ-GIRCFCGYGLTEFASTVCA-KEADGL-ADVGSPLPGREVKIVN---------- 302
Cdd:PLN02736 375 GGrvrfmssGAS-PLspDVMEFLRICfGGRVLEGYGMTETSCVISGmDEGDNLsGHVGSPNPACEVKLVDvpemnytsed 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 -----NEVWLRAASMAEGYWRNG-QLVSLVNDEGWYATRDRGE-MHNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAH 374
Cdd:PLN02736 454 qpyprGEICVRGPIIFKGYYKDEvQTREVIDEDGWLHTGDIGLwLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKC 533
|
330 340 350
....*....|....*....|....*....|....*...
gi 727407383 375 PAVLQVFIvpvADKEFGHRPVAVMEYDHESvdLSEWVK 412
Cdd:PLN02736 534 KFVAQCFV---YGDSLNSSLVAVVVVDPEV--LKAWAA 566
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
24-445 |
7.62e-18 |
|
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: 86.01 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 24 NDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfA 103
Cdd:cd05970 44 EERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIK-M 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 104 LVPDGENTFPaltslhiQRVEGAHAAAWQPTRL---------------------------------------CSMTLTSG 144
Cdd:cd05970 123 IVAIAEDNIP-------EEIEKAAPECPSKPKLvwvgdpvpegwidfrkliknaspdferptansypcgediLLVYFSSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 145 STGLPK--AAVHTYQ-AHLASAEGVLSLIPFGDHddwllslplFHVSGQG---IMWRWLY----AGARMTVRD------K 208
Cdd:cd05970 196 TTGMPKmvEHDFTYPlGHIVTAKYWQNVREGGLH---------LTVADTGwgkAVWGKIYgqwiAGAAVFVYDydkfdpK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 QPLEQMLAGCTHASLVPTQLWRLLVnRSSVS------LKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTV--- 278
Cdd:cd05970 267 ALLEKLSKYGVTTFCAPPTIYRFLI-REDLSrydlssLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTETTLTIatf 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 279 -CAKEADGlaDVGSPLPGREVKIVNN-----------EVWLRAAS-----MAEGYWRNGQLVSLVNDEGWYATRDRGEM- 340
Cdd:cd05970 346 pWMEPKPG--SMGKPAPGYEIDLIDRegrsceageegEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMd 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 341 HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--RPVAVMEYDHESVD-----LSEWVKD 413
Cdd:cd05970 424 EDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQvvKATIVLAKGYEPSEelkkeLQDHVKK 503
|
490 500 510
....*....|....*....|....*....|...
gi 727407383 414 KLARFQQPvRWLTLPPEL-KNGGIKISRQALKE 445
Cdd:cd05970 504 VTAPYKYP-RIVEFVDELpKTISGKIRRVEIRE 535
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
17-443 |
8.30e-18 |
|
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: 85.47 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN---------PQLP 87
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDpaypaerlaFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 88 QPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAV--HTYQAHLASAEG 165
Cdd:cd17651 90 DAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 166 VLSLIPFGDHDDwLLSLPLFHVSGQGImWRWLYAGARMTVRD---KQPLEQMLAGC----THASLVPTQLWRLLVN---- 234
Cdd:cd17651 170 RASSLGPGARTL-QFAGLGFDVSVQEI-FSTLCAGATLVLPPeevRTDPPALAAWLdeqrISRVFLPTVALRALAEhgrp 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 235 --RSSVSLKAVLLGGAAIPIELTEQ---AREQGIRCFCGYGLTEfASTVCAKEADGLAD-------VGSPLPGREVKI-- 300
Cdd:cd17651 248 lgVRLAALRYLLTGGEQLVLTEDLRefcAGLPGLRLHNHYGPTE-THVVTALSLPGDPAawpapppIGRPIDNTRVYVld 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 ---------VNNEVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:cd17651 327 aalrpvppgVPGELYIGGAGLARGYLNRPELTAerfvpdpFVPGARMYRTGDLARwLPDGELEFLGRADDQVKIRGFRIE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 364 PEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLAR----FQQPVRWLTLP--PELKNGgiK 437
Cdd:cd17651 407 LGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALAThlpeYMVPSAFVLLDalPLTPNG--K 484
|
....*.
gi 727407383 438 ISRQAL 443
Cdd:cd17651 485 LDRRAL 490
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
142-446 |
3.93e-17 |
|
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: 83.32 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQA---HLASAEGVLSLIPfgdhDD--WLLSLPLFhVSGQ--GIMWRWLYaGARMTVRDKQ----- 209
Cdd:cd05969 97 TSGTTGTPKGVLHVHDAmifYYFTGKYVLDLHP----DDiyWCTADPGW-VTGTvyGIWAPWLN-GVTNVVYEGRfdaes 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 210 ---PLEQMlaGCTHASLVPTQLWRLLvnRSSV---------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:cd05969 171 wygIIERV--KVTVWYTAPTAIRMLM--KEGDelarkydlsSLRFIHSVGEPLNPEAIRWGMEVfGVPIHDTWWQTETGS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 277 TVCAKEADGLADVGS---PLPGREVKIVNNE-----------VWLRAA--SMAEGYWRNGQLVSLVNDEGWYATRDRGEM 340
Cdd:cd05969 247 IMIANYPCMPIKPGSmgkPLPGVKAAVVDENgnelppgtkgiLALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVD-----LSEWVK 412
Cdd:cd05969 327 dEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAfiSLKEGFEPSDelkeeIINFVR 406
|
330 340 350
....*....|....*....|....*....|....*.
gi 727407383 413 DKLARFQQP--VRWLTLPPELKNGgiKISRQALKEW 446
Cdd:cd05969 407 QKLGAHVAPreIEFVDNLPKTRSG--KIMRRVLKAK 440
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-445 |
4.21e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 8 WRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLP 87
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 88 QPLLEELLPNLTLQFAL----------VPDGENTFP--ALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHT 155
Cdd:PRK12467 598 QDRLAYMLDDSGVRLLLtqshllaqlpVPAGLRSLCldEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 156 YQAHLASAEGVLSLIPFGDHDDWLL-SLPLFHVSGQGIMWRwLYAGARMTVRDKQPL---EQMLA-----GCTHASLVPT 226
Cdd:PRK12467 678 HGALANYVCVIAERLQLAADDSMLMvSTFAFDLGVTELFGA-LASGATLHLLPPDCArdaEAFAAlmadqGVTVLKIVPS 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 227 QlWRLLVNRSSV----SLKAVLLGGAAIPIELTEQARE--QGIRCFCGYGLTEFASTV----CAKEA--DGLADVGSPLP 294
Cdd:PRK12467 757 H-LQALLQASRValprPQRALVCGGEALQVDLLARVRAlgPGARLINHYGPTETTVGVstyeLSDEErdFGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 295 GREVKIVNN-----------EVWLRAASMAEGYWRNGQLVS--LVND------EGWYATRDRGEMH-NGKLTIVGRLDNL 354
Cdd:PRK12467 836 NLGLYILDHylnpvpvgvvgELYIGGAGLARGYHRRPALTAerFVPDpfgadgGRLYRTGDLARYRaDGVIEYLGRMDHQ 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVpVADKEFGHRPVA-----VMEYDHESVDLSEWVKDKLAR----FQQPVRWL 425
Cdd:PRK12467 916 VKIRGFRIELGEIEARLLAQPGVREAVVL-AQPGDAGLQLVAylvpaAVADGAEHQATRDELKAQLRQvlpdYMVPAHLL 994
|
490 500
....*....|....*....|..
gi 727407383 426 TLP--PELKNGgiKISRQALKE 445
Cdd:PRK12467 995 LLDslPLTPNG--KLDRKALPK 1014
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
20-447 |
4.32e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.12 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCArvdelASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLT 99
Cdd:PRK07787 18 AVRIGGRVLSRSDLAG-----AATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 100 LQFALV--PDGENTFPALT-SLHiqrVEGAHAAAWQPTRLCSMTL-TSGSTGLPKAAVHTYQA------HLASAEGVLSl 169
Cdd:PRK07787 93 AQAWLGpaPDDPAGLPHVPvRLH---ARSWHRYPEPDPDAPALIVyTSGTTGPPKGVVLSRRAiaadldALAEAWQWTA- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 170 ipfgdhDDWLL-SLPLFHVSGQ--GIMWRwLYAGARM--TVRDKqPLEQMLAGCTHASL---VPTQLWRLLVNRSSV-SL 240
Cdd:PRK07787 169 ------DDVLVhGLPLFHVHGLvlGVLGP-LRIGNRFvhTGRPT-PEAYAQALSEGGTLyfgVPTVWSRIAADPEAArAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 241 K-AVLL--GGAAIPIELTEQ-AREQGIRCFCGYGLTEFASTVCAKeADG---LADVGSPLPGREVKIVNN---------- 303
Cdd:PRK07787 241 RgARLLvsGSAALPVPVFDRlAALTGHRPVERYGMTETLITLSTR-ADGerrPGWVGLPLAGVETRLVDEdggpvphdge 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 ---EVWLRAASMAEGYW-RNGQLVSLVNDEGWY-----ATRDRGEMHNgkltIVGRLD-NLFFSGGEGIQPEEVERVIAA 373
Cdd:PRK07787 320 tvgELQVRGPTLFDGYLnRPDATAAAFTADGWFrtgdvAVVDPDGMHR----IVGREStDLIKSGGYRIGAGEIETALLG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 374 HPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDKLARFQQP--VRWL-TLPpelKNGGIKISRQALKEWV 447
Cdd:PRK07787 396 HPGVREAAVVGVPDDDLGQRIVAyvVGADDVAADELIDFVAQQLSVHKRPreVRFVdALP---RNAMGKVLKKQLLSEG 471
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
118-432 |
4.52e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 83.71 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 118 LHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGV-LSLIPFGD---HDDWLLS-LPLFHVSGQGI 192
Cdd:PLN02430 204 LHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdLFMEQFEDkmtHDDVYLSfLPLAHILDRMI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 193 MWRWLYAGARM--------TVRD-------------------------------------------KQPLEQMLAGCTHA 221
Cdd:PLN02430 284 EEYFFRKGASVgyyhgdlnALRDdlmelkptllagvprvferihegiqkalqelnprrrlifnalyKYKLAWMNRGYSHK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 222 SLVPTQ---LWRLLVNRSSVSLKAVLLGGAAIPIELTEQAReqgIRCFC----GYGLTE--------FASTVCAKEADGL 286
Cdd:PLN02430 364 KASPMAdflAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLR---VTSCAfvvqGYGLTEtlgpttlgFPDEMCMLGTVGA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 ADVGSPLPGREVKIVN---------NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLF- 355
Cdd:PLN02430 441 PAVYNELRLEEVPEMGydplgepprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILpNGVLKIIDRKKNLIk 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 356 FSGGEGIQPEEVERVIAAHPAVLQVFivpVADKEFGHRPVAVMEYDHESVdlSEWVKDKlaRFQQPVRWLTLPPELK 432
Cdd:PLN02430 521 LSQGEYVALEYLENVYGQNPIVEDIW---VYGDSFKSMLVAVVVPNEENT--NKWAKDN--GFTGSFEELCSLPELK 590
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-443 |
5.12e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFAL----------VPDGENTFPALTSLHIQ-RVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQA---HLAS 162
Cdd:PRK12316 2098 DSGAALLLtqrhllerlpLPAGVARLPLDRDAEWAdYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGAlvaHCQA 2177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 163 AEGVLSLIPfGDHDDWLLSLPlFHVSGQGIMWRwLYAGARMTVRD------KQPLEQMLA-GCTHASLVPTQLWRLL--- 232
Cdd:PRK12316 2178 AGERYELSP-ADCELQFMSFS-FDGAHEQWFHP-LLNGARVLIRDdelwdpEQLYDEMERhGVTILDFPPVYLQQLAeha 2254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 233 -VNRSSVSLKAVLLGGAAIPIELTEQARE--QGIRCFCGYGLTEFASTV-----CAKEADGLADV--GSPLPGREVKIVN 302
Cdd:PRK12316 2255 eRDGRPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVVTPllwkcRPQDPCGAAYVpiGRALGNRRAYILD 2334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 -----------NEVWLRAASMAEGYWRNGQLVS--LVND------EGWYATRD--RGEMhNGKLTIVGRLDNLFFSGGEG 361
Cdd:PRK12316 2335 adlnllapgmaGELYLGGEGLARGYLNRPGLTAerFVPDpfsasgERLYRTGDlaRYRA-DGVVEYLGRIDHQVKIRGFR 2413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 362 IQPEEVERVIAAHPAVLQVFIVPVaDKEFGHR------PVAVMEYDHEsvDLSEWVKDKLARFQQPVRWLTLPPELKNGG 435
Cdd:PRK12316 2414 IELGEIEARLQAHPAVREAVVVAQ-DGASGKQlvayvvPDDAAEDLLA--ELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
....*...
gi 727407383 436 IKISRQAL 443
Cdd:PRK12316 2491 GKLDRKAL 2498
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
17-445 |
1.00e-16 |
|
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: 81.97 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd17653 12 DAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFALVPDGENtfpaltslhiqrvEGAHAAAwqptrlcsmtlTSGSTGLPKAAVHTYQA--HLASAEGVLSLIPFGD 174
Cdd:cd17653 92 TSGATLLLTTDSPD-------------DLAYIIF-----------TSGSTGIPKGVMVPHRGvlNYVSQPPARLDVGPGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 175 HDDWLLSlPLFHVSgQGIMWRWLYAGARMTVRD-KQPLEQMLAGCTHASLVPTQLWRLLVNRSSvSLKAVLLGGAAIPIE 253
Cdd:cd17653 148 RVAQVLS-IAFDAC-IGEIFSTLCNGGTLVLADpSDPFAHVARTVDALMSTPSILSTLSPQDFP-NLKTIFLGGEAVPPS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 254 LTEQAREqGIRCFCGYGLTEfaSTVCAKEADGLADV----GSPLPG----------REVKI-VNNEVWLRAASMAEGYWR 318
Cdd:cd17653 225 LLDRWSP-GRRLYNAYGPTE--CTISSTMTELLPGQpvtiGKPIPNstcyildadlQPVPEgVVGEICISGVQVARGYLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 319 NGQL--VSLVNDEGW-----YATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVI-AAHPAVLQVFIVPVADke 389
Cdd:cd17653 302 NPALtaSKFVPDPFWpgsrmYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNG-- 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727407383 390 fghrpVAVMEYDHESVDLSEwVKDKLAR----FQQPVRWLTLP--PELKNGgiKISRQALKE 445
Cdd:cd17653 380 -----RLVAFVTPETVDVDG-LRSELAKhlpsYAVPDRIIALDsfPLTANG--KVDRKALRE 433
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-399 |
1.02e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.49 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 29 NWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGA-------RVLPVNPQLPQPLLEELLPNLTLQ 101
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAichtvnpRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 102 FalVPDGENTFPALTSL----------HIQR------------VEGAHA-AAWQ---PTRLCSMTLTSGSTGLPKAAVHT 155
Cdd:PRK06018 121 F--VPILEKIADKLPSVeryvvltdaaHMPQttlknavayeewIAEADGdFAWKtfdENTAAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 156 Y-----QAHLASAEGVLSLipfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTV----RDKQPLEQMLAG--CTHASLV 224
Cdd:PRK06018 199 HrsnvlHALMANNGDALGT---SAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakLDGASVYELLDTekVTFTAGV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 225 PTqLWRLLV------NRSSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFA--STVCA-----------KEADG 285
Cdd:PRK06018 276 PT-VWLMLLqymekeGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplGTLAAlkppfsklpgdARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 LADVGSPLPGREVKIVNNE-------------VWLRAASMAEGYWRNGQlvSLVNDEGWYATRDRGEM-HNGKLTIVGRL 351
Cdd:PRK06018 355 LQKQGYPPFGVEMKITDDAgkelpwdgktfgrLKVRGPAVAAAYYRVDG--EILDDDGFFDTGDVATIdAYGYMRITDRS 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 727407383 352 DNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVME 399
Cdd:PRK06018 433 KDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ 480
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
17-443 |
2.26e-16 |
|
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: 80.97 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPID------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 nltlqfalvPDgentFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQ--AHLASA---EGVLSLIP 171
Cdd:cd17650 69 ---------PD----YPAERLQYMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRnvAHAAHAwrrEYELDSFP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 172 FGdhddwLLSLPLFHVS-GQGIMWRWLYAGARM------TVRDKQPLEQML--AGCTHASLVPTQLWRLL--VNRSSV-- 238
Cdd:cd17650 136 VR-----LLQMASFSFDvFAGDFARSLLNGGTLvicpdeVKLDPAALYDLIlkSRITLMESTPALIRPVMayVYRNGLdl 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 -SLKAVLLGGAAIPIE--LTEQAR-EQGIRCFCGYGLTEFA--STVCAKEADGLAD-----VGSPLPGREVKI------- 300
Cdd:cd17650 211 sAMRLLIVGSDGCKAQdfKTLAARfGQGMRIINSYGVTEATidSTYYEEGRDPLGDsanvpIGRPLPNTAMYVlderlqp 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 ----VNNEVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVE 368
Cdd:cd17650 291 qpvgVAGELYIGGAGVARGYLNRPELTAerfvenpFAPGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 369 RVIAAHPAVLQVFIVPVADKEfGHRPVAVMEYDHESVD---LSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17650 371 SQLARHPAIDEAVVAVREDKG-GEARLCAYVVAAATLNtaeLRAFLAKELPSYMIPSYYVQLDalPLTPNG--KVDRRAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
19-443 |
2.37e-16 |
|
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: 80.68 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellpnl 98
Cdd:cd17645 15 VAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 99 tlqfalvPDgentFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDw 178
Cdd:cd17645 80 -------PD----YPGERIAYMLADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 179 llSLPLFHVSGQGIMWR---WLYAGARMTVRD---KQPLEQMLAGC-THA---SLVPTQLWRLLVNRSSVSLKAVLLGGa 248
Cdd:cd17645 148 --SLVYASFSFDASAWEifpHLTAGAALHVVPserRLDLDALNDYFnQEGitiSFLPTGAAEQFMQLDNQSLRVLLTGG- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 249 aipiELTEQAREQGIRCFCGYGLTEFASTVCAKEAD---GLADVGSPLPGREVKIVNN-----------EVWLRAASMAE 314
Cdd:cd17645 225 ----DKLKKIERKGYKLVNNYGPTENTVVATSFEIDkpyANIPIGKPIDNTRVYILDEalqlqpigvagELCIAGEGLAR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 315 GYWRNGQLVS-------LVNDEGWYATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVA 386
Cdd:cd17645 301 GYLNRPELTAekfivhpFVPGERMYRTGDLAKFLPdGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 387 DKefGHRP------VAVMEYDHESvdLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17645 381 DA--DGRKylvayvTAPEEIPHEE--LREWLKNDLPDYMIPTYFVHLKalPLTANG--KVDRKAL 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
126-445 |
4.53e-16 |
|
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: 80.40 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 126 AHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIM-WRWLYAGARMT 204
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 205 vrdKQPLEQMLAGcthaslvPTQLWRL-----------------LVNRSS----------VSLKAVLLGG----AAIPIE 253
Cdd:cd05906 239 ---HVPTEEILAD-------PLRWLDLidryrvtitwapnfafaLLNDLLeeiedgtwdlSSLRYLVNAGeavvAKTIRR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 254 LTEQAREQGIRCFC---GYGLTEFAS-----TVCAKE----ADGLADVGSPLPGREVKIVNNE-----------VWLRAA 310
Cdd:cd05906 309 LLRLLEPYGLPPDAirpAFGMTETCSgviysRSFPTYdhsqALEFVSLGRPIPGVSMRIVDDEgqllpegevgrLQVRGP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 311 SMAEGYWRNGQLV--SLVNDeGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAdk 388
Cdd:cd05906 389 VVTKGYYNNPEANaeAFTED-GWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFA-- 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727407383 389 efgHRP-------VAVM---EYDHES--VDLSEWVKDKLARFQ--QPVRWLTLPPEL--KNGGIKISRQALKE 445
Cdd:cd05906 466 ---VRDpgaeteeLAIFfvpEYDLQDalSETLRAIRSVVSREVgvSPAYLIPLPKEEipKTSLGKIQRSKLKA 535
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
110-389 |
4.69e-16 |
|
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: 80.36 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 110 NTFPALTSLHIQRVEGAHAAAWQPTRLCSMTL-----TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL 184
Cdd:cd05931 120 PAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIaylqyTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 185 FH----VSGQGIMwrwLYAGAR---MTVRD--KQPLE--QMLA--GCTHaSLVPTQLWRLLVNRSSV---------SLKA 242
Cdd:cd05931 200 YHdmglIGGLLTP---LYSGGPsvlMSPAAflRRPLRwlRLISryRATI-SAAPNFAYDLCVRRVRDedlegldlsSWRV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 243 VLLGGaaipieltEQAREQGIRCF---------------CGYGLTE-----------------------FASTVCAKEAD 284
Cdd:cd05931 276 ALNGA--------EPVRPATLRRFaeafapfgfrpeafrPSYGLAEatlfvsggppgtgpvvlrvdrdaLAGRAVAVAAD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 285 G-----LADVGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQLVSLVN-------DEGWYATRDRGEM 340
Cdd:cd05931 348 DpaareLVSCGRPLPDQEVRIVDpetgrelpdgevGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 727407383 341 HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ-----VFIVPVADKE 389
Cdd:cd05931 428 HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcvaAFSVPDDGEE 481
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
124-396 |
5.28e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 80.27 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 124 EGAHAAAWQPT----RLCSMTLTSGSTGLPKAAV-HTYQAHLASAEGVLsLIPFGDHDDWLLSLPLFHVSGQGIMWRW-L 197
Cdd:PLN02479 181 TGDPEFAWKPPadewQSIALGYTSGTTASPKGVVlHHRGAYLMALSNAL-IWGMNEGAVYLWTLPMFHCNGWCFTWTLaA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 198 YAGARMTVRD--KQPLEQMLA--GCTHASLVPTQLwRLLVNrSSVSLKA--------VLLGGAAIPIELTEQAREQGIRC 265
Cdd:PLN02479 260 LCGTNICLRQvtAKAIYSAIAnyGVTHFCAAPVVL-NTIVN-APKSETIlplprvvhVMTAGAAPPPSVLFAMSEKGFRV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 266 FCGYGLTEF--ASTVCA--KEADGLA---------------------DV-----GSPLPGREVKIvnNEVWLRAASMAEG 315
Cdd:PLN02479 338 THTYGLSETygPSTVCAwkPEWDSLPpeeqarlnarqgvryigleglDVvdtktMKPVPADGKTM--GEIVMRGNMVMKG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 316 YWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRP 394
Cdd:PLN02479 416 YLKNPKANEEAFANGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESP 495
|
..
gi 727407383 395 VA 396
Cdd:PLN02479 496 CA 497
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-443 |
1.03e-15 |
|
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: 78.85 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd12114 4 TAVICGDGTLTYGELAERARRVAGALKAAGVRPGDlvAVTLP--KGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFALVpDGENTFPALTSLHIQRVEGAHAAAW--------QPTRLCSMTLTSGSTGLPKAAVHTYQA---------- 158
Cdd:cd12114 82 DAGARLVLT-DGPDAQLDVAVFDVLILDLDALAAPappppvdvAPDDLAYVIFTSGSTGTPKGVMISHRAalntildinr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 159 --HLASAEGVLSLIPFgDHDdwllsLPLFHVSGQgimwrwLYAGARMTV----RDKQPLEQMLAGCTHA----SLVPTQL 228
Cdd:cd12114 161 rfAVGPDDRVLALSSL-SFD-----LSVYDIFGA------LSAGATLVLpdeaRRRDPAHWAELIERHGvtlwNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 229 WRLL-----VNRSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFA--STVC--AKEADGLADV--GSPLPG 295
Cdd:cd12114 229 EMLLdvleaAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASiwSIYHpiDEVPPDWRSIpyGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 REVKIVNN-----------EVWLRAASMAEGYWRNGQL-----VSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSG 358
Cdd:cd12114 309 QRYRVLDPrgrdcpdwvpgELWIGGRGVALGYLGDPELtaarfVTHPDGERLYRTGDLGRYrPDGTLEFLGRRDGQVKVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 359 GEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLA----RFQQPVRWLTLP--PELK 432
Cdd:cd12114 389 GYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAqtlpAYMIPSRVIALEalPLTA 468
|
490
....*....|.
gi 727407383 433 NGgiKISRQAL 443
Cdd:cd12114 469 NG--KVDRAAL 477
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
142-445 |
1.27e-15 |
|
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: 79.11 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIpFGDH---DDWLLS-LPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAG 217
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNIVARFSHARDPI-FGNQiipDTAILTvIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 -----CTHASLVPTQLWRL----LVNRSSVS-LKAVLLGGAAIPIELTEQAREQ----GIRcfCGYGLTEFASTVCA--K 281
Cdd:cd17642 271 lqdykVQSALLVPTLFAFFakstLVDKYDLSnLHEIASGGAPLSKEVGEAVAKRfklpGIR--QGYGLTETTSAILItpE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 282 EADGLADVGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQLVS-LVNDEGWYATRDRGEMHN-GKLTI 347
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDldtgktlgpnerGELCVKGPMIMKGYVNNPEATKaLIDKDGWLHSGDIAYYDEdGHFFI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHeSVDLSE-----WVKDKLA---RFQ 419
Cdd:cd17642 429 VDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEA-GKTMTEkevmdYVASQVStakRLR 507
|
330 340
....*....|....*....|....*.
gi 727407383 420 QPVRWLTLPPelKNGGIKISRQALKE 445
Cdd:cd17642 508 GGVKFVDEVP--KGLTGKIDRRKIRE 531
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-451 |
1.29e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 78.92 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 136 LCSMTLTSGSTGLPKAAVHTYQAHLASA-EGVLSLIPFGDHDDWLLS-LPLFHVSGQ-GIMWRWLYAGARMTVRDKQPLE 212
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNLVSNTlMGVQWLYNCKEGEEVVLGvLPFFHVYGMtAVMNLSIMQGYKMVLIPKFDMK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 213 QMLAGCTH--ASLVP--TQLWRLLVNRSSV------SLKAVLLGGAAIPIELTEQ-AREQGIRCFCGYGLTEFASTVCAK 281
Cdd:PRK06710 288 MVFEAIKKhkVTLFPgaPTIYIALLNSPLLkeydisSIRACISGSAPLPVEVQEKfETVTGGKLVEGYGLTESSPVTHSN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 282 ---EADGLADVGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKL 345
Cdd:PRK06710 368 flwEKRVPGSIGVPWPDTEAMIMSletgealppgeiGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMdEDGFF 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 346 TIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--RPVAVMEYDHESV--DLSEWVKDKLARFQQP 421
Cdd:PRK06710 448 YVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGEtvKAFVVLKEGTECSeeELNQFARKYLAAYKVP 527
|
330 340 350
....*....|....*....|....*....|.
gi 727407383 422 vRWLTLPPELKNGGI-KISRQALKEWVQRQQ 451
Cdd:PRK06710 528 -KVYEFRDELPKTTVgKILRRVLIEEEKRKN 557
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
142-444 |
1.62e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 78.73 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVL----SLIPFGDHDD-WLLSLPLFHVSGQGIMWRWLYA-GARMTVRDKQPLEQML 215
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNvYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASDMV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 216 A-----GCTHASLVPTQLWRLLVNRSSV------SLKAVLLGGAAipieLTEQAREQGIRCFC------GYGLTEFAST- 277
Cdd:PLN02574 286 KvidrfKVTHFPVVPPILMALTKKAKGVcgevlkSLKQVSCGAAP----LSGKFIQDFVQTLPhvdfiqGYGMTESTAVg 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 278 ---VCAKEADGLADVGSPLPGREVKIVN------------NEVWLRAASMAEGYWRNGQ-LVSLVNDEGWYATRDRGEM- 340
Cdd:PLN02574 362 trgFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgncGELWIQGPGVMKGYLNNPKaTQSTIDKDGWLRTGDIAYFd 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 341 HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESV----DLSEWVKDKLA 416
Cdd:PLN02574 442 EDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTlsqeAVINYVAKQVA 521
|
330 340
....*....|....*....|....*...
gi 727407383 417 RFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:PLN02574 522 PYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
106-336 |
5.80e-15 |
|
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: 77.09 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 106 PDGENTFPALTSLH---IQRVEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD-----D 177
Cdd:cd05921 135 VAGRGAISFAELAAtppTAAVDAAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 178 WLlslPLFHVSGQGIMWRW-LYAGARMTVRDKQPLEQMLAGC---------THASLVPTQlWRLLVN----------RSS 237
Cdd:cd05921 214 WL---PWNHTFGGNHNFNLvLYNGGTLYIDDGKPMPGGFEETlrnlreispTVYFNVPAG-WEMLVAalekdealrrRFF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 238 VSLKAVLLGGAAIP-------IELTEQAREQGIRCFCGYGLTEFA--STVCAKEADGLADVGSPLPGREVKIVNN----E 304
Cdd:cd05921 290 KRLKLMFYAGAGLSqdvwdrlQALAVATVGERIPMMAGLGATETAptATFTHWPTERSGLIGLPAPGTELKLVPSggkyE 369
|
250 260 270
....*....|....*....|....*....|...
gi 727407383 305 VWLRAASMAEGYWRNGQLVSLVNDE-GWYATRD 336
Cdd:cd05921 370 VRVKGPNVTPGYWRQPELTAQAFDEeGFYCLGD 402
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-445 |
7.66e-15 |
|
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: 76.07 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfaLVPD 107
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTL------------------LTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 108 GENTfpaltslHIQRVEGAHAAAWQPTRLCSMTL---TSGSTGLPKAAVHTYQA----HLASAEGVlSLIPFGDHddWLL 180
Cdd:cd05974 63 DLRD-------RVDRGGAVYAAVDENTHADDPMLlyfTSGTTSKPKLVEHTHRSypvgHLSTMYWI-GLKPGDVH--WNI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 181 SLPLFHVSGQGIMWRWLYAGARMTVR-----DKQPLEQMLAGCTHASL-VPTQLWRLLVN----RSSVSLKAVLLGGAAI 250
Cdd:cd05974 133 SSPGWAKHAWSCFFAPWNAGATVFLFnyarfDAKRVLAALVRYGVTTLcAPPTVWRMLIQqdlaSFDVKLREVVGAGEPL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 251 PIELTEQAREQ-GIRCFCGYGLTEfaSTVCAKEADG----LADVGSPLPGREVKIVN--------NEVWL-----RAASM 312
Cdd:cd05974 213 NPEVIEQVRRAwGLTIRDGYGQTE--TTALVGNSPGqpvkAGSMGRPLPGYRVALLDpdgapateGEVALdlgdtRPVGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 313 AEGYWRNGQLVSLVNDEGWYATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFG 391
Cdd:cd05974 291 MKGYAGDPDKTAHAMRGGYYRTGDIAmRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727407383 392 HRPVAVM-------EYDHESVDLSEWVKDKLARFQQpVRWLTLPPELKNGGIKISRQALKE 445
Cdd:cd05974 371 SVPKAFIvlragyePSPETALEIFRFSRERLAPYKR-IRRLEFAELPKTISGKIRRVELRR 430
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
239-421 |
7.67e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 76.73 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIPIELTEQARE-QGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVNN-----------E 304
Cdd:PRK05677 327 ALKLTLSGGMALQLATAERWKEvTGCAICEGYGMTETSPVVSVNPSQAiqVGTIGIPVPSTLCKVIDDdgnelplgevgE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 305 VWLRAASMAEGYW-RNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFI 382
Cdd:PRK05677 407 LCVKGPQVMKGYWqRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727407383 383 VPVADKEFG-HRPVAVMEYDHESVD---LSEWVKDKLARFQQP 421
Cdd:PRK05677 487 IGVPDEKSGeAIKVFVVVKPGETLTkeqVMEHMRANLTGYKVP 529
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
28-421 |
1.32e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 76.00 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN------------------------ 83
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINpayrlseleyalnqsgckaliaad 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ---------PQLPQPLLEELLPNLTLQFALVPD-------------GENTFPALTSL--HIQRVE-GAHAAAWQPTRLCS 138
Cdd:PRK08315 124 gfkdsdyvaMLYELAPELATCEPGQLQSARLPElrrviflgdekhpGMLNFDELLALgrAVDDAElAARQATLDPDDPIN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ--GIMwRWLYAGARMTVrdkqPLE---- 212
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMvlGNL-ACVTHGATMVY----PGEgfdp 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 213 -QMLA-----GCThaSL--VPT----QLWRLLVNRSSVS-LKAVLLGGAAIPIELTEQ------AREQGIrcfcGYGLTE 273
Cdd:PRK08315 279 lATLAaveeeRCT--ALygVPTmfiaELDHPDFARFDLSsLRTGIMAGSPCPIEVMKRvidkmhMSEVTI----AYGMTE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 274 fASTV-CAKEADGLAD-----VGSPLPGREVKIVNN------------EVWLRAASMAEGYWRNGQLVSLVND-EGWYAT 334
Cdd:PRK08315 353 -TSPVsTQTRTDDPLEkrvttVGRALPHLEVKIVDPetgetvprgeqgELCTRGYSVMKGYWNDPEKTAEAIDaDGWMHT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 335 RDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHE--SVDLSE 409
Cdd:PRK08315 432 GDLAVMdEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAwiILRPGATltEEDVRD 511
|
490
....*....|..
gi 727407383 410 WVKDKLARFQQP 421
Cdd:PRK08315 512 FCRGKIAHYKIP 523
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
137-421 |
1.83e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.51 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 137 CSMTLTSGSTGLPKAAV--------HTYQAHLASAEGVLSLipfgdhDDWLLSLPLFHVSGQGIMWRWLYAGARMTVR-- 206
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALyshrstvlHAYGAALPDAMGLSAR------DAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 207 --DKQPLEQMLA--GCTHASLVPTqLWRLLVN-------RSSvSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEF 274
Cdd:PRK07008 253 dlDGKSLYELIEaeRVTFSAGVPT-VWLGLLNhmreaglRFS-TLRRTVIGGSACPPAMIRTFEDEyGVEVIHAWGMTEM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 275 A--STVCAKEADGLADV-----------GSPLPGREVKIVNN-------------EVWLRAASMAEGYWRNGQlVSLVNd 328
Cdd:PRK07008 331 SplGTLCKLKWKHSQLPldeqrkllekqGRVIYGVDMKIVGDdgrelpwdgkafgDLQVRGPWVIDRYFRGDA-SPLVD- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 329 eGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRP-VAVMEYDHESV- 405
Cdd:PRK07008 409 -GWFPTGDVATIdADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPlLVVVKRPGAEVt 487
|
330
....*....|....*...
gi 727407383 406 --DLSEWVKDKLARFQQP 421
Cdd:PRK07008 488 reELLAFYEGKVAKWWIP 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
25-451 |
3.62e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.17 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQ-----------------------CGARVLP 81
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRsglyytpinwhltaaeiayivddSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 82 VNP--QLPQPLLEELLPNLTLQFALV---PDGENTFPALTSLH-----IQRVEGAHaaawqptrlcsMTLTSGSTGLPK- 150
Cdd:PRK08276 89 VSAalADTAAELAAELPAGVPLLLVVagpVPGFRSYEEALAAQpdtpiADETAGAD-----------MLYSSGTTGRPKg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 151 ---AAVHTYQAHLASAEGVLSLIPFGDHDD--WLLSLPLFHVS-GQGIMWRwLYAGARMTVRDKQPLEQMLAG-----CT 219
Cdd:PRK08276 158 ikrPLPGLDPDEAPGMMLALLGFGMYGGPDsvYLSPAPLYHTApLRFGMSA-LALGGTVVVMEKFDAEEALALieryrVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 220 HASLVPTQLWRLLV------NRSSVS-LKAVLLGGAAIPIELTEQAREqgircFCG------YGLTEFASTVCAKEADGL 286
Cdd:PRK08276 237 HSQLVPTMFVRMLKlpeevrARYDVSsLRVAIHAAAPCPVEVKRAMID-----WWGpiiheyYASSEGGGVTVITSEDWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 A---DVGSPLPGrEVKIVN---NEvwLRAASMAEGYW-RNGQLVSLVNDE----------GWYATRDRGEM-HNGKLTIV 348
Cdd:PRK08276 312 AhpgSVGKAVLG-EVRILDedgNE--LPPGEIGTVYFeMDGYPFEYHNDPektaaarnphGWVTVGDVGYLdEDGYLYLT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEyDHESVDLSE--------WVKDKLARFQQ 420
Cdd:PRK08276 389 DRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQ-PADGADAGDalaaeliaWLRGRLAHYKC 467
|
490 500 510
....*....|....*....|....*....|....*.
gi 727407383 421 PvRWLTLPPEL---KNGgiKISRQALKE--WVQRQQ 451
Cdd:PRK08276 468 P-RSIDFEDELprtPTG--KLYKRRLRDryWEGRQR 500
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
142-444 |
4.34e-14 |
|
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: 74.01 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQML------ 215
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFwedlre 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 216 AGCTHASLVPT---QLWRLLVNRSSV-SLKAVLLGGAAIPIELTEQARE--QGIRCFCGYGLTE-FA--STVCA-KEADG 285
Cdd:cd05922 205 HGATGLAGVPStyaMLTRLGFDPAKLpSLRYLTQAGGRLPQETIARLREllPGAQVYVMYGQTEaTRrmTYLPPeRILEK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 286 LADVGSPLPGREVKIVNNEVWL-----------RAASMAEGYWRNGQ-LVSLVNDEGWYATRDRG-EMHNGKLTIVGRLD 352
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTPtppgepgeivhRGPNVMKGYWNDPPyRRKEGRGGGVLHTGDLArRDEDGFLFIVGRRD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADkEFGHRPVAVMEYDHESV--DLSEWVKDKLARFQQP--VRWLTLP 428
Cdd:cd05922 365 RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDpkDVLRSLAERLPPYKVPatVRVVDEL 443
|
330
....*....|....*.
gi 727407383 429 PELKNGgiKISRQALK 444
Cdd:cd05922 444 PLTASG--KVDYAALR 457
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
17-445 |
4.59e-14 |
|
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: 73.90 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN------------- 83
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDpdypeeriqyile 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 ---PQLPQPLLEELLPNLTLQFALVPDGENTFpaltslhIQRVEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHL 160
Cdd:cd17655 92 dsgADILLTQSHLQPPIAFIGLIDLLDEDTIY-------HEESENLEPVS-KSDDLAYVIYTSGSTGKPKGVMIEHRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 161 ASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGImWRWLYAGARM------TVRDKQPLEQML--AGCTHASLVPTQLWRL 231
Cdd:cd17655 164 NLVEWANKVIYQGEHLRVALFASIsFDASVTEI-FASLLSGNTLyivrkeTVLDGQALTQYIrqNRITIIDLTPAHLKLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 232 LVNRSS--VSLKAVLLGGAAIPIELTEQAREQ---GIRCFCGYGLTEfaSTVCA------KEADGLADV--GSPLPGREV 298
Cdd:cd17655 243 DAADDSegLSLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTE--TTVDAsiyqyePETDQQVSVpiGKPLGNTRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 299 KIVNN-----------EVWLRAASMAEGYWRNGQLVS--LVND-----EGWYATRDRGE-MHNGKLTIVGRLDNLFFSGG 359
Cdd:cd17655 321 YILDQygrpqpvgvagELYIGGEGVARGYLNRPELTAekFVDDpfvpgERMYRTGDLARwLPDGNIEFLGRIDHQVKIRG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 360 EGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDKLARFQQPVRWLTLP--PELKNGg 435
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAyiVSEKELPVAQLREFLARELPDYMIPSYFIKLDeiPLTPNG- 479
|
490
....*....|
gi 727407383 436 iKISRQALKE 445
Cdd:cd17655 480 -KVDRKALPE 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-443 |
5.20e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.81 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQV--RGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:PRK12467 3103 AQVarTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 90 LLEELLPNLTLQFALVPDG-ENTFPALTSLHIQRVEGAH---------AAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAH 159
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLTQAHlLEQLPAPAGDTALTLDRLDlngysennpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGAL 3262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 160 LASAEGVLSLIPFGDHDDWLLSLPLfhvSGQGIMWRW---LYAGARMTVR-----DKQPLEQML--AGCTHASLVPTQLW 229
Cdd:PRK12467 3263 ANHLCWIAEAYELDANDRVLLFMSF---SFDGAQERFlwtLICGGCLVVRdndlwDPEELWQAIhaHRISIACFPPAYLQ 3339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 230 RLLVN---RSSVSLKAVLLGGAAIP---IELTEQAREQgiRCFC-GYGLTEFASTV----CAKEADGLAD---VGSPLPG 295
Cdd:PRK12467 3340 QFAEDaggADCASLDIYVFGGEAVPpaaFEQVKRKLKP--RGLTnGYGPTEAVVTVtlwkCGGDAVCEAPyapIGRPVAG 3417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 REVKIVNN-----------EVWLRAASMAEGYWRNGQLVS--------LVNDEGWYATRDRGEMH-NGKLTIVGRLDNLF 355
Cdd:PRK12467 3418 RSIYVLDGqlnpvpvgvagELYIGGVGLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRaDGVIEYLGRIDHQV 3497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 356 FSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVAVMEYDHESVDLSEWVKDKLAR----FQQPVRWLTLP--P 429
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAAslpdYMVPAQLLVLAamP 3576
|
490
....*....|....
gi 727407383 430 ELKNGgiKISRQAL 443
Cdd:PRK12467 3577 LGPNG--KVDRKAL 3588
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
142-421 |
5.67e-14 |
|
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: 72.72 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGAR--MTVR-DKQPLEQMLA-- 216
Cdd:cd17636 8 TAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTnvFVRRvDAEEVLELIEae 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 GCTHASLV-PTQLWRLLVNRSSV----SLKAVL---LGGAAIPIELTEQAREQGircfcGYGLTEFA--STVCAKEADGL 286
Cdd:cd17636 88 RCTHAFLLpPTIDQIVELNADGLydlsSLRSSPaapEWNDMATVDTSPWGRKPG-----GYGQTEVMglATFAALGGGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 ADVGSPLPGREVKIVNN-----------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNL 354
Cdd:cd17636 163 GGAGRPSPLVQVRILDEdgrevpdgevgEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREpDGSLSFVGPKTRM 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--RPVAVMEYDHESV--DLSEWVKDKLARFQQP 421
Cdd:cd17636 243 IKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQsvKAIVVLKPGASVTeaELIEHCRARIASYKKP 313
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
15-449 |
6.54e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 73.62 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 15 RGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNP---------- 84
Cdd:PRK06164 23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTryrshevahi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 85 --------------------QLPQPLLEELLPNLTLQFALVPDGENTFPA--------LTSLHIQR-VEGAHAAAWQPTR 135
Cdd:PRK06164 103 lgrgrarwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADATPApapgarvqLFALPDPApPAAAGERAADPDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 136 LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD----KQPL 211
Cdd:PRK06164 183 GALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPvfdaARTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 212 EQML-AGCTHASLVPTQLWRLL----VNRSSVSLK----AVLLGGAAipiELTEQAREQGIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK06164 263 RALRrHRVTHTFGNDEMLRRILdtagERADFPSARlfgfASFAPALG---ELAALARARGVPLTGLYGSSEVQALVALQP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 283 ADGLADV-----GSPL-PGREVKIVN------------NEVWLRAASMAEGYWRNGQLVS-LVNDEGWYATRDRGEM-HN 342
Cdd:PRK06164 340 ATDPVSVrieggGRPAsPEARVRARDpqdgallpdgesGEIEIRAPSLMRGYLDNPDATArALTDDGYFRTGDLGYTrGD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 343 GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPvADKEFGHRPVA-VMEYDHESVDLSEWV---KDKLARF 418
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATRDGKTVPVAfVIPTDGASPDEAGLMaacREALAGF 498
|
490 500 510
....*....|....*....|....*....|....
gi 727407383 419 QQPVRWLTL---PPELKNGGIKISRQALKEWVQR 449
Cdd:PRK06164 499 KVPARVQVVeafPVTESANGAKIQKHRLREMAQA 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-443 |
7.49e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE 3151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFALvpdgenTFPALTSLHIQRV---------EGAHAAAWQ----PTRLCSMTLTSGSTGLPKAAVHTYQAHLASA 163
Cdd:PRK12316 3152 DSGAQLLL------SQSHLRLPLAQGVqvldldrgdENYAEANPAirtmPENLAYVIYTSGSTGKPKGVGIRHSALSNHL 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 164 EGVLSLIPFGDhDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVR------DKQPLEQML--AGCTHASLVPTQLWRLLVN 234
Cdd:PRK12316 3226 CWMQQAYGLGV-GDRVLQFTTFSFDVFVEELFWpLMSGARVVLAgpedwrDPALLVELInsEGVDVLHAYPSMLQAFLEE 3304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 235 ---RSSVSLKAVLLGGAAIPIELTEQAREQGiRCFCGYGLTEFASTV----CAKEADGLADVGSPLPGREVKIVNN---- 303
Cdd:PRK12316 3305 edaHRCTSLKRIVCGGEALPADLQQQVFAGL-PLYNLYGPTEATITVthwqCVEEGKDAVPIGRPIANRACYILDGslep 3383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -------EVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVE 368
Cdd:PRK12316 3384 vpvgalgELYLGGEGLARGYHNRPGLTAerfvpdpFVPGERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIE 3463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 369 RVIAAHPAVLQVFIVPVAdkefGHRPVAVMEYDHESVDLSEWVKDKLAR----FQQPVRWLTLP--PELKNGgiKISRQA 442
Cdd:PRK12316 3464 ARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKAslpeYMVPAHLLFLErmPLTPNG--KLDRKA 3537
|
.
gi 727407383 443 L 443
Cdd:PRK12316 3538 L 3538
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
239-391 |
8.51e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIPIELTEQARE-QGIRCFCGYGLTEFASTVCA-----KEADGlaDVGSPLPGREVKIVNN--------- 303
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKlTGQYLLEGYGLTECSPLVSVnpydlDYYSG--SIGLPVPSTEIKLVDDdgnevppge 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 --EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK08974 404 pgELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
170
....*....|.
gi 727407383 381 FIVPVADKEFG 391
Cdd:PRK08974 484 AAVGVPSEVSG 494
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
239-445 |
8.57e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 73.37 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIPIELTEQARE-QGIRCFCGYGLTEFASTVCA-----KEADGlaDVGSPLPGREVKIVNN--------- 303
Cdd:PRK08751 330 SLKMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACInpltlKEYNG--SIGLPIPSTDACIKDDagtvlaige 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 --EVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:PRK08751 408 igELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 380 VFIVPVADKEFGHR-PVAVMEYDHE--SVDLSEWVKDKLARFQQPvRWLTLPPELKNGGI-KISRQALKE 445
Cdd:PRK08751 488 VAAVGVPDEKSGEIvKVVIVKKDPAltAEDVKAHARANLTGYKQP-RIIEFRKELPKTNVgKILRRELRD 556
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
142-416 |
8.67e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-QGIMWRWLYAGARMtVRDKQPLEqmlaGCTH 220
Cdd:PRK08633 790 SSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGlTVTLWLPLLEGIKV-VYHPDPTD----ALGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 221 ASLV-----------PTQLwRLLVNRSSV------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK08633 865 AKLVakhratillgtPTFL-RLYLRNKKLhplmfaSLRLVVAGAEKLKPEVADAFEEKfGIRILEGYGATETSPVASVNL 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 283 ADGLAD------------VGSPLPGREVKIVNNE------------VWLRAASMAEGYWRNGQLVSLV----NDEGWYAT 334
Cdd:PRK08633 944 PDVLAAdfkrqtgskegsVGMPLPGVAVRIVDPEtfeelppgedglILIGGPQVMKGYLGDPEKTAEVikdiDGIGWYVT 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 335 RDRGEM-HNGKLTIVGRLDNlfFS--GGEGIQPEEVE-RVIAAHPAVLQVFIVP-VADKEFGHRPVAVmeYDHESVDLSE 409
Cdd:PRK08633 1024 GDKGHLdEDGFLTITDRYSR--FAkiGGEMVPLGAVEeELAKALGGEEVVFAVTaVPDEKKGEKLVVL--HTCGAEDVEE 1099
|
....*..
gi 727407383 410 wVKDKLA 416
Cdd:PRK08633 1100 -LKRAIK 1105
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
139-377 |
1.03e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 73.11 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLS-LPLFHVSGqgiMWRWLyagarmTVrdkqpleQMLAG 217
Cdd:PRK07768 157 MQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMG---MVGFL------TV-------PMYFG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 CTHASLVPTQ------LWRLLVNR----------SSVSLKAVLLGGAAI-----------------PIE------LTEQA 258
Cdd:PRK07768 221 AELVKVTPMDflrdplLWAELISKyrgtmtaapnFAYALLARRLRRQAKpgafdlsslrfalngaePIDpadvedLLDAG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 259 REQGIR---CFCGYGLTE----------------------------FASTVCAKEADGLADVGSPLPGREVKIVNN---- 303
Cdd:PRK07768 301 ARFGLRpeaILPAYGMAEatlavsfspcgaglvvdevdadllaalrRAVPATKGNTRRLATLGPPLPGLEVRVVDEdgqv 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -------EVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHP 375
Cdd:PRK07768 381 lpprgvgVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYlTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVE 460
|
..
gi 727407383 376 AV 377
Cdd:PRK07768 461 GV 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-445 |
4.39e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 4566 DAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFAL----------VPDGentfpaLTSLHIQRVE-----GAHAAA--WQPTRLCSMTLTSGSTGLPKAAVHTYQ-- 157
Cdd:PRK12316 4646 DSGAALLLtqshllqrlpIPDG------LASLALDRDEdwegfPAHDPAvrLHPDNLAYVIYTSGSTGRPKGVAVSHGsl 4719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 158 -AHLASAEGVLSLIPfgdhDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVRD------KQPLEQML-AGCTHASLVPTQL 228
Cdd:PRK12316 4720 vNHLHATGERYELTP----DDRVLQFMSFSFDGSHEGLYHpLINGASVVIRDdslwdpERLYAEIHeHRVTVLVFPPVYL 4795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 229 WRLL----VNRSSVSLKAVLLGGAAIPIELTEQA--REQGIRCFCGYGLTEFASTV-CAKEADGLAD------VGSPLPG 295
Cdd:PRK12316 4796 QQLAehaeRDGEPPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTETTVTVlLWKARDGDACgaaympIGTPLGN 4875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 296 REVKIVNN-----------EVWLRAASMAEGYWRNGQLV------SLVNDEG--WYATRD--RGEMhNGKLTIVGRLDNL 354
Cdd:PRK12316 4876 RSGYVLDGqlnplpvgvagELYLGGEGVARGYLERPALTaerfvpDPFGAPGgrLYRTGDlaRYRA-DGVIDYLGRVDHQ 4954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVA-VMEYDHESVD-----------LSEWVKDKLARFQQPV 422
Cdd:PRK12316 4955 VKIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGyVVPQDPALADadeaqaelrdeLKAALRERLPEYMVPA 5033
|
490 500
....*....|....*....|....*
gi 727407383 423 RWLTLP--PELKNGgiKISRQALKE 445
Cdd:PRK12316 5034 HLVFLArmPLTPNG--KLDRKALPQ 5056
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
30-414 |
5.56e-13 |
|
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: 70.91 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 30 WRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPDGE 109
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 110 ----------------------------------NTFP-------ALTSLHIQRVEGAHAAAwQPTRLCSMTLTSGSTGL 148
Cdd:cd17641 94 qvdklleiadripsvryviycdprgmrkyddprlISFEdvvalgrALDRRDPGLYEREVAAG-KGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 149 PKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL------FHVSGQGI------------------------------ 192
Cdd:cd17641 173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqMYSVGQALvcgfivnfpeepetmmedlreigptfvllp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 193 --MWRWLYAGARMTVRDKQPLEQML----------AGCTHASLVPTQLW-------------RLLVNRSSVS-LKAVLLG 246
Cdd:cd17641 253 prVWEGIAADVRARMMDATPFKRFMfelgmklglrALDRGKRGRPVSLWlrlaswladallfRPLRDRLGFSrLRSAATG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 247 GAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAkEADGLAD---VGSPLPGREVKIVNN-EVWLRAASMAEGYWRNGQ- 321
Cdd:cd17641 333 GAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTV-HRDGDVDpdtVGVPFPGTEVRIDEVgEILVRSPGVFVGYYKNPEa 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 322 LVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAHPAVLQVFIvpvadkeFGH-RP--VA 396
Cdd:cd17641 412 TAEDFDEDGWLHTGDAGYFkENGHLVVIDRAKDVGtTSDGTRFSPQFIENKLKFSPYIAEAVV-------LGAgRPylTA 484
|
490
....*....|....*...
gi 727407383 397 VMEYDHESVdlSEWVKDK 414
Cdd:cd17641 485 FICIDYAIV--GKWAEQR 500
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
122-336 |
8.30e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 70.29 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 122 RVEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD-----DWLlslPLFHVSGQ----GI 192
Cdd:PRK08180 198 AVDAAHAAV-GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppvlvDWL---PWNHTFGGnhnlGI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 193 MwrwLYAGARMTVRDKQPLEQMLAGcTHASL----------VPTqLWRLLVN---------RSSVS-LKAVLLGGAAIPI 252
Cdd:PRK08180 274 V---LYNGGTLYIDDGKPTPGGFDE-TLRNLreisptvyfnVPK-GWEMLVPalerdaalrRRFFSrLKLLFYAGAALSQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 253 -------ELTEQAREQGIRCFCGYGLTEFA--STVCAKEADGLADVGSPLPGREVKIVNN----EVWLRAASMAEGYWRN 319
Cdd:PRK08180 349 dvwdrldRVAEATCGERIRMMTGLGMTETApsATFTTGPLSRAGNIGLPAPGCEVKLVPVggklEVRVKGPNVTPGYWRA 428
|
250
....*....|....*...
gi 727407383 320 GQLVSLV-NDEGWYATRD 336
Cdd:PRK08180 429 PELTAEAfDEEGYYRSGD 446
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
20-445 |
9.03e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.11 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN------------PQLP 87
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNwhfkpeeiayilEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 88 QPLLEELLPNLTLQFALVPDGENTFPALTSLHIQ---RVEGAHAAA---------W-------------QPTrlcSMTLT 142
Cdd:PRK12406 84 ARVLIAHADLLHGLASALPAGVTVLSVPTPPEIAaayRISPALLTPpagaidwegWlaqqepydgppvpQPQ---SMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 143 SGSTGLPK----AAVHTYQAhlASAEGVLSLIpFGDHDDW--LLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA 216
Cdd:PRK12406 161 SGTTGHPKgvrrAAPTPEQA--AAAEQMRALI-YGLKPGIraLLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 -----GCTHASLVPTQLWRLLVNRSSV-------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEA 283
Cdd:PRK12406 238 lierhRITHMHMVPTMFIRLLKLPEEVrakydvsSLRHVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTESGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 284 DGLA---DVGSPLPGREVKIVNN-----------EVWLRAASMAE-GYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTI 347
Cdd:PRK12406 318 DALShpgTVGKAAPGAELRFVDEdgrplpqgeigEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDaDGYLFL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEyDHESVDLSE-----WVKDKLARFQQPV 422
Cdd:PRK12406 398 CDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVE-PQPGATLDEadiraQLKARLAGYKVPK 476
|
490 500
....*....|....*....|....*.
gi 727407383 423 RWL---TLPPElkNGGiKISRQALKE 445
Cdd:PRK12406 477 HIEimaELPRE--DSG-KIFKRRLRD 499
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
18-399 |
1.25e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 69.67 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 18 TIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS---GVMLRawNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEEL 94
Cdd:PRK13388 17 TIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlhvGVLLG--NTPEMLFWLAAAALGGYVLVGLNTTRRGAALAAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 95 LPNLTLQFaLVPDGEN-------TFPALTSL------HIQRVEGAHAA----AWQPTRLCSMTLTSGSTGLPKaAVHTYQ 157
Cdd:PRK13388 95 IRRADCQL-LVTDAEHrplldglDLPGVRVLdvdtpaYAELVAAAGALtphrEVDAMDPFMLIFTSGTTGAPK-AVRCSH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 158 AHLASAEGVL----SLIPfgdHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVRDK---------------------- 208
Cdd:PRK13388 173 GRLAFAGRALterfGLTR---DDVCYVSMPLFH--SNAVMAGWapaVASGAAVALPAKfsasgflddvrrygatyfnyvg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 QPLEQMLAGCTHASLVPTQLwrllvnrssvslkAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLAD 288
Cdd:PRK13388 248 KPLAYILATPERPDDADNPL-------------RVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 289 VGSPLPGreVKIVNNE--------------------------VWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH- 341
Cdd:PRK13388 315 IGRGAPG--VAIYNPEtltecavarfdahgallnadeaigelVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDa 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 727407383 342 NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVME 399
Cdd:PRK13388 393 DGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALV 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
142-449 |
2.20e-12 |
|
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: 68.72 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWL-LSLPLFHVSGQGIMWRWLYAGarmTV---RDKQPLEQmLAG 217
Cdd:cd05918 114 TSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqFASYTFDVSILEIFTTLAAGG---CLcipSEEDRLND-LAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 C------THASLVPTqLWRLLVNRSSVSLKAVLLGGAAIPIELTEQArEQGIRCFCGYGLTEfaSTVCA--KEADGLAD- 288
Cdd:cd05918 190 FinrlrvTWAFLTPS-VARLLDPEDVPSLRTLVLGGEALTQSDVDTW-ADRVRLINAYGPAE--CTIAAtvSPVVPSTDp 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 289 --VGSPLPGReVKIVNN-------------EVWLRAASMAEGYWRNGQLVSL--VNDEGWYATRDRGE------------ 339
Cdd:cd05918 266 rnIGRPLGAT-CWVVDPdnhdrlvpigavgELLIEGPILARGYLNDPEKTAAafIEDPAWLKQEGSGRgrrlyrtgdlvr 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 340 -MHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH-PAVLQVFIVPVADKEFGHRP--VAVMEYDHESV---------- 405
Cdd:cd05918 345 yNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPqlVAFVVLDGSSSgsgdgdslfl 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 727407383 406 -----------DLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQALKEWVQR 449
Cdd:cd05918 425 epsdefralvaELRSKLRQRLPSYMVPSVFLPLShlPLTASG--KIDRRALRELAES 479
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-435 |
2.26e-12 |
|
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: 68.53 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVlpvnpqlpqplleellpnltlqfAL 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVA-----------------------AL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 105 VpdgeNTFPALTSL-HIQRVEGAHAAAWQPtrlCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:cd05940 58 I----NYNLRGESLaHCLNVSSAKHLVVDA---ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 184 LFHVSGQGIMW-RWLYAGARMTVRDKQPLEQMLAGCTH--ASLVP--TQLWRLLVNRssvslkavllggaaiPIELTEqa 258
Cdd:cd05940 131 LYHSTALIVGWsACLASGATLVIRKKFSASNFWDDIRKyqATIFQyiGELCRYLLNQ---------------PPKPTE-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 259 REQGIRCFCGYGL-----------------TEF-ASTVCA------KEADGLADVGSPL-----PGREVKI-VNNEVWLR 308
Cdd:cd05940 194 RKHKVRMIFGNGLrpdiweefkerfgvpriAEFyAATEGNsgfinfFGKPGAIGRNPSLlrkvaPLALVKYdLESGEPIR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 309 AasmAEGYWRN------GQLVSLVND-------------------------EGWYATRDRGEMH-NGKLTIVGRLDNLFF 356
Cdd:cd05940 274 D---AEGRCIKvprgepGLLISRINPlepfdgytdpaatekkilrdvfkkgDAWFNTGDLMRLDgEGFWYFVDRLGDTFR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 357 SGGEGIQPEEVERVIAAHPAVLQ--VFIVPVADKEfGHRPVAVM----EYDHESVDLSEWVKDKLARFQQPVrWLTLPPE 430
Cdd:cd05940 351 WKGENVSTTEVAAVLGAFPGVEEanVYGVQVPGTD-GRAGMAAIvlqpNEEFDLSALAAHLEKNLPGYARPL-FLRLQPE 428
|
....*
gi 727407383 431 LKNGG 435
Cdd:cd05940 429 MEITG 433
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
17-443 |
4.62e-12 |
|
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: 67.88 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFALVPDGENTFPALTSLH-------IQRVEGAH-AAAWQPTRLCSMTLTSGSTGLPKAAV--HTYQAHLASAEGV 166
Cdd:cd17656 83 DSGVRVVLTQRHLKSKLSFNKSTilledpsISQEDTSNiDYINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLLHFERE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 167 LSLIPFGDhDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD--KQPLEQMLAGC----THASLVPTQLWRLL------VN 234
Cdd:cd17656 163 KTNINFSD-KVLQFATCSFDVCYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVkrhnIEVVFLPVAFLKFIfserefIN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 235 RSSVSLKAVLLGGAAIPI--ELTEQAREQGIRCFCGYGLTEfASTVCA------KEADGLADVGSPLPGREVKIVNN--- 303
Cdd:cd17656 242 RFPTCVKHIITAGEQLVItnEFKEMLHEHNVHLHNHYGPSE-THVVTTytinpeAEIPELPPIGKPISNTWIYILDQeqq 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 --------EVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd17656 321 lqpqgivgELYISGASVARGYLNRQELTAekffpdpFDPNERMYRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17656 401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAyfVMEQELNISQLREYLAKQLPEYMIPSFFVPLDqlPLTPNG--KVDRKAL 478
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
142-338 |
4.76e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.15 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQ---AHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWR-WLYAGARMTVRDKQPLEQMLAG 217
Cdd:PRK12582 228 TSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNgLLWGGGTLYIDDGKPLPGMFEE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 218 cTHASL----------VPTQLWRLL-------VNRSSV--SLKAVLLGGAAIPIELTE--QA---REQGIRC--FCGYGL 271
Cdd:PRK12582 308 -TIRNLreisptvygnVPAGYAMLAeamekddALRRSFfkNLRLMAYGGATLSDDLYErmQAlavRTTGHRIpfYTGYGA 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727407383 272 TEFASTVC----AKEADGLadVGSPLPGREVKIVNN----EVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRG 338
Cdd:PRK12582 387 TETAPTTTgthwDTERVGL--IGLPLPGVELKLAPVgdkyEVRVKGPNVTPGYHKDPELTAAAFDeEGFYRLGDAA 460
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
239-391 |
5.61e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 67.54 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIpIELTEQAREQ--GIRCFCGYGLTEFASTVCAK---EADGLADVGSPLPGREVKIVNN---------- 303
Cdd:PRK12492 334 ALKLTNSGGTAL-VKATAERWEQltGCTIVEGYGLTETSPVASTNpygELARLGTVGIPVPGTALKVIDDdgnelplger 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYWRNGQLVSLVND-EGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK12492 413 gELCIKGPQVMKGYWQQPEATAEALDaEGWFKTGDIAVIDpDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
|
170
....*....|.
gi 727407383 381 FIVPVADKEFG 391
Cdd:PRK12492 493 AAIGVPDERSG 503
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
8-387 |
7.56e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 67.01 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 8 WRHWRQVRGETIALRLND-----EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV 82
Cdd:PRK08008 13 WDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 NPQLPQ-------PLLEELLPNLTLQF-----ALVPDGENTFPA--LTSLHIQRVEGAH----AAAWQPTRLCSMT---- 140
Cdd:PRK08008 93 NARLLReesawilQNSQASLLVTSAQFypmyrQIQQEDATPLRHicLTRVALPADDGVSsftqLKAQQPATLCYAPplst 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 141 -------LTSGSTGLPKAAVHT-----YQAHLASAEGVLSlipfgDHDDWLLSLPLFHVSGQ--GIMwRWLYAGARMTVR 206
Cdd:PRK08008 173 ddtaeilFTSGTTSRPKGVVIThynlrFAGYYSAWQCALR-----DDDVYLTVMPAFHIDCQctAAM-AAFSAGATFVLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 207 DK-------QPLEQMLAGCTHAslVPTQLWRLLVNRSSVSLKAVLLGGAAIPIELTEQAREQ-----GIRCFCGYGLTEf 274
Cdd:PRK08008 247 EKysarafwGQVCKYRATITEC--IPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAfeerfGVRLLTSYGMTE- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 275 asTVCAKEADGLAD------VGSPLPGREVKIVNN-----------EVWLRAA---SMAEGYWRNGQLVSLV-NDEGWYA 333
Cdd:PRK08008 324 --TIVGIIGDRPGDkrrwpsIGRPGFCYEAEIRDDhnrplpageigEICIKGVpgkTIFKEYYLDPKATAKVlEADGWLH 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 334 TRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAD 387
Cdd:PRK08008 402 TGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-421 |
8.08e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 66.25 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 MTLTSGSTGLPKAAV-HTYQAHLASAEGvlslIPFGDHDD-----------------WLLSLPLFHVSGqgiMWRWLYA- 199
Cdd:cd05924 8 ILYTGGTTGMPKGVMwRQEDIFRMLMGG----ADFGTGEFtpsedahkaaaaaagtvMFPAPPLMHGTG---SWTAFGGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 200 ---GARMTVRDKQPLEQML-----AGCTHASLVPTQLWRLLV-------NRSSVSLKAVLLGGAAipieLTEQAREQGIR 264
Cdd:cd05924 81 lggQTVVLPDDRFDPEEVWrtiekHKVTSMTIVGDAMARPLIdalrdagPYDLSSLFAISSGGAL----LSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 265 C------FCGYGLTEFASTVCAKEADGLADVGS---PLP--------GREVKIVNNEV-WL-RAASMAEGYWR------- 318
Cdd:cd05924 157 LvpnitlVDAFGSSETGFTGSGHSAGSGPETGPftrANPdtvvldddGRVVPPGSGGVgWIaRRGHIPLGYYGdeaktae 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 319 -----NGQLVSLVNDegwYATRDRGemhnGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR 393
Cdd:cd05924 237 tfpevDGVRYAVPGD---RATVEAD----GTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350
....*....|....*....|....*....|..
gi 727407383 394 PVAVMEYDH----ESVDLSEWVKDKLARFQQP 421
Cdd:cd05924 310 VVAVVQLREgagvDLEELREHCRTRIARYKLP 341
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
132-418 |
1.24e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 66.63 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAVHTyQAHLASAeGVLSLIPFG--DHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVR 206
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCT-HRKVASA-GVMLAQRFGlgPDDVCYVSMPLFH--SNAVMAGWavaLAAGASIALR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 207 DKQPLEQMLA-----GCTHASLVPTQLWRLLV-----NRSSVSLKAVLlGGAAIPIELTEQAREQGIRCFCGYGLTEFAS 276
Cdd:PRK07867 226 RKFSASGFLPdvrryGATYANYVGKPLSYVLAtperpDDADNPLRIVY-GNEGAPGDIARFARRFGCVVVDGFGSTEGGV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 277 TVcAKEADGLADVGSPLPGrEVKIVNNE-------------------------VWLRAASMAEGYWRNGQLVSLVNDEGW 331
Cdd:PRK07867 305 AI-TRTPDTPPGALGPLPP-GVAIVDPDtgtecppaedadgrllnadeaigelVNTAGPGGFEGYYNDPEADAERMRGGV 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 332 YATRD---RGEmhNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDhesvDLS 408
Cdd:PRK07867 383 YWSGDlayRDA--DGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA----PGA 456
|
330
....*....|
gi 727407383 409 EWVKDKLARF 418
Cdd:PRK07867 457 KFDPDAFAEF 466
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-396 |
1.60e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.16 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLAS-AEGVLSLIP---FGDHDDWLLSLPLFHV-SGQGIMWRWLYAGARMTVRDKQPLEQMLA 216
Cdd:PLN02246 187 SSGTTGLPKGVMLTHKGLVTSvAQQVDGENPnlyFHSDDVILCVLPMFHIySLNSVLLCGLRVGAAILIMPKFEIGALLE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 -----GCTHASLVPTQLwrLLVNRSSV-------SLKAVLLGGAAIPIELTE--QAREQGIRCFCGYGLTEfASTVCAKe 282
Cdd:PLN02246 267 liqrhKVTIAPFVPPIV--LAIAKSPVvekydlsSIRMVLSGAAPLGKELEDafRAKLPNAVLGQGYGMTE-AGPVLAM- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 283 adGLADVGSPLPGR-----------EVKIVN------------NEVWLRAASMAEGYWRNGQLVSL-VNDEGWYATRDRG 338
Cdd:PLN02246 343 --CLAFAKEPFPVKsgscgtvvrnaELKIVDpetgaslprnqpGEICIRGPQIMKGYLNDPEATANtIDKDGWLHTGDIG 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 339 EM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA 396
Cdd:PLN02246 421 YIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVA 479
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-419 |
2.24e-11 |
|
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: 65.53 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 138 SMTLTSGSTGLPKAAVHTYQ-AHL-ASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWR-WLYAGARMTVRDKQPLEQM 214
Cdd:cd05915 157 GMAYTTGTTGLPKGVVYSHRaLVLhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAaTLVGAKQVLPGPRLDPASL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 215 LAGCTHASLV-----PTQLWRLLVNRSSVSLK-----AVLLGGAAIPIELTEQAREQGIRCFCGYGLTEF--ASTVCA-- 280
Cdd:cd05915 237 VELFDGEGVTftagvPTVWLALADYLESTGHRlktlrRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETspVVVQNFvk 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 281 --------------KEADGL------ADVGSP----LP--GREVKIVNnevwLRAASMAEGYWRNGQLV-SLVNDEGWYA 333
Cdd:cd05915 317 shleslseeekltlKAKTGLpiplvrLRVADEegrpVPkdGKALGEVQ----LKGPWITGGYYGNEEATrSALTPDGFFR 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 334 TRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVM---EYDHESVDLSE 409
Cdd:cd05915 393 TGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvprGEKPTPEELNE 472
|
330
....*....|
gi 727407383 410 WVKDKLARFQ 419
Cdd:cd05915 473 HLLKAGFAKW 482
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
36-379 |
2.47e-11 |
|
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: 65.19 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 36 RVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFaLVPDGENTFPAL 115
Cdd:cd17654 25 KISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSY-LLQNKELDNAPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 116 TSLHIQRvegaHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGIMW 194
Cdd:cd17654 104 SFTPEHR----HFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLtFDPSVVEIFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 195 RWLYAGARMTVRDKQPLEQM--------LAGCTHASLVPTQLWRLLV--NRSSV-----SLKAVLLGGAAIPIELTEQAR 259
Cdd:cd17654 180 SLSSGATLLIVPTSVKVLPSkladilfkRHRITVLQATPTLFRRFGSqsIKSTVlsatsSLRVLALGGEPFPSLVILSSW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 260 EQ---GIRCFCGYGLTE---FASTVCAKEADGLADVGSPLPGREVKIVNNEvwlraASMAEGYWRNGQL--VSLVNDE-- 329
Cdd:cd17654 260 RGkgnRTRIFNIYGITEvscWALAYKVPEEDSPVQLGSPLLGTVIEVRDQN-----GSEGTGQVFLGGLnrVCILDDEvt 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 727407383 330 ----GWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:cd17654 335 vpkgTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVES 388
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
11-208 |
2.73e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 65.67 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 11 WRQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCG------------ 76
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDvvALLME--NRPEYLAAWLGLAKLGavvallntqqrg 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 77 -----------ARVLPVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAWQPTRlCSMTL---- 141
Cdd:PRK08279 124 avlahslnlvdAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASR-SGVTAkdta 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727407383 142 ----TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVRDK 208
Cdd:PRK08279 203 fyiyTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYH--NTGGTVAWssvLAAGATLALRRK 274
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
142-446 |
4.97e-11 |
|
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: 64.41 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLasaegvlslIPFGDHDDWLLSLplfhvSGQGIMWR-----------------WLyAGA--- 201
Cdd:cd05928 182 TSGTTGSPKMAEHSHSSLG---------LGLKVNGRYWLDL-----TASDIMWNtsdtgwiksawsslfepWI-QGAcvf 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 202 --RMTVRDKQPLEQMLAG--CTHASLVPTqLWRLLV--NRSSV---SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGL 271
Cdd:cd05928 247 vhHLPRFDPLVILKTLSSypITTFCGAPT-VYRMLVqqDLSSYkfpSLQHCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 272 TEfASTVCA-----KEADGlaDVGSPLPGREVKIVNN-----------EVWLRAA-----SMAEGYWRNGQLVSLVNDEG 330
Cdd:cd05928 326 TE-TGLICAnfkgmKIKPG--SMGKASPPYDVQIIDDngnvlppgtegDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 331 WYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAD-------KEFGHRPVAVMEYDH 402
Cdd:cd05928 403 FYLTGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDpirgevvKAFVVLAPQFLSHDP 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 727407383 403 ESV--DLSEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQAL--KEW 446
Cdd:cd05928 483 EQLtkELQQHVKSVTAPYKYPrkVEFVQELPKTVTG--KIQRNELrdKEW 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
25-431 |
6.82e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.94 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTL-LAWLA----------------------LLQCGARVLP 81
Cdd:PRK13391 22 GEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLeVCWAAersglyytcvnshltpaeaayiVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 82 VNPQLPQPLLEELLPNLTLQFALVPDGENTFPAltslhIQRVEGAhAAAWQPTRLCS------MTLTSGSTGLPKAAV-- 153
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLDGDGELEG-----FVGYAEA-VAGLPATPIADeslgtdMLYSSGTTGRPKGIKrp 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 154 --HTYQAHLASAEGVL-SLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLA-----GCTHASLVP 225
Cdd:PRK13391 176 lpEQPPDTPLPLTAFLqRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLAlieeyGVTHTQLVP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 226 TQLWRLLV------NRSSVS-LKAVLLGGAAIPIelteQAREQGIRcFCG------YGLTEFA-STVCAKEaDGLA---- 287
Cdd:PRK13391 256 TMFSRMLKlpeevrDKYDLSsLEVAIHAAAPCPP----QVKEQMID-WWGpiiheyYAATEGLgFTACDSE-EWLAhpgt 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 -------------DVGSPLP-----------GREVKIVNNEVWLRAASMAEGYWRNGQLVSLVNDEGWyatrdrgemhng 343
Cdd:PRK13391 330 vgramfgdlhildDDGAELPpgepgtiwfegGRPFEYLNDPAKTAEARHPDGTWSTVGDIGYVDEDGY------------ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 344 kLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVME-------YDHESVDLSEWVKDKLA 416
Cdd:PRK13391 398 -LYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpvdgvdpGPALAAELIAFCRQRLS 476
|
490
....*....|....*
gi 727407383 417 RFQQPvRWLTLPPEL 431
Cdd:PRK13391 477 RQKCP-RSIDFEDEL 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
20-443 |
1.17e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 63.91 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVmlrAWNTPQTL---LAWLALLQCGARVLPVN--------PQLPQ 88
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRERGVKPGDSV---AVALPRSVfltLALHAIVEAGAAWLPLDtgypddrlKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 89 PLLEELLPNLTLQFALVPDGENTFPALTSLHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLS 168
Cdd:PRK10252 553 DARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQN 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 169 LIPFGDHDDWLLSLPL-FHVSGQGIMWRWLyAGARMTV------RDKQPLEQMLA--GCTHASLVPTQLWRLL------- 232
Cdd:PRK10252 633 HYPLTADDVVLQKTPCsFDVSVWEFFWPFI-AGAKLVMaepeahRDPLAMQQFFAeyGVTTTHFVPSMLAAFVasltpeg 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 233 VNRSSVSLKAVLLGGAAIPIELT-EQAREQGIRCFCGYGLTEFASTVCA--KEADGLADV-GSPLP-GREV-----KI-- 300
Cdd:PRK10252 712 ARQSCASLRQVFCSGEALPADLCrEWQQLTGAPLHNLYGPTEAAVDVSWypAFGEELAAVrGSSVPiGYPVwntglRIld 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 ---------VNNEVWLRAASMAEGYWRNGQLVS-------LVNDEGWYATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:PRK10252 792 armrpvppgVAGDLYLTGIQLAQGYLGRPDLTAsrfiadpFAPGERMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQRIE 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 364 PEEVERVIAAHPAVLQVFIVPV----ADKEFG--HRPVA-VMEYDHESVD---LSEWVKDKLARFQQPVRWLTLP--PEL 431
Cdd:PRK10252 872 LGEIDRAMQALPDVEQAVTHACvinqAAATGGdaRQLVGyLVSQSGLPLDtsaLQAQLRERLPPHMVPVVLLQLDqlPLS 951
|
490
....*....|..
gi 727407383 432 KNGgiKISRQAL 443
Cdd:PRK10252 952 ANG--KLDRKAL 961
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
139-444 |
1.71e-10 |
|
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: 62.54 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 MTLTSGSTGLPKAAVH------TYQAHLASAEGVLSLIPFGDHDD--WLLSLpLFHVSGQGIMW--RWLYAGARMTVRDK 208
Cdd:cd05973 93 MMFTSGTTGLPKGVPVplralaAFGAYLRDAVDLRPEDSFWNAADpgWAYGL-YYAITGPLALGhpTILLEGGFSVESTW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 209 QPLEQMlaGCTHASLVPTqLWRLLV-------NRSSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCA 280
Cdd:cd05973 172 RVIERL--GVTNLAGSPT-AYRLLMaagaevpARPKGRLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLAN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 281 KEADG----LADVGSPLPGREVKIVNNE---------------------VWLRaasmaeGYWRNGQLVSlvnDEGWYATR 335
Cdd:cd05973 249 HHALEhpvhAGSAGRAMPGWRVAVLDDDgdelgpgepgrlaidiansplMWFR------GYQLPDTPAI---DGGYYLTG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 336 DRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--RPVAVMEYDHESV-----DL 407
Cdd:cd05973 320 DTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEvvKAFVVLRGGHEGTpaladEL 399
|
330 340 350
....*....|....*....|....*....|....*....
gi 727407383 408 SEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQALK 444
Cdd:cd05973 400 QLHVKKRLSAHAYPrtIHFVDELPKTPSG--KIQRFLLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
9-436 |
1.86e-10 |
|
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: 62.98 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQvRGETIALRLNDEQ------LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV 82
Cdd:cd17634 61 RHLRE-NGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 83 NPQLPQPLLEELLPNLTLQFALVPDG---------------ENTFPALTSLH---IQRVEGA------------------ 126
Cdd:cd17634 140 FGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplkknvdDALNPNVTSVEhviVLKRTGSdidwqegrdlwwrdliak 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 127 HAAAWQPTRL-----CSMTLTSGSTGLPKAAVHTYQAH-LASAEGVLSLIPFGDHDDWLLSLPLFHVSGQG-IMWRWLYA 199
Cdd:cd17634 220 ASPEHQPEAMnaedpLFILYTSGTTGKPKGVLHTTGGYlVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSyLLYGPLAC 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 200 GARMTVRDKQP-------LEQMLA--GCTHASLVPTQL---------WRLLVNRSSVSlkavLLGGAAIPIE------LT 255
Cdd:cd17634 300 GATTLLYEGVPnwptparMWQVVDkhGVNILYTAPTAIralmaagddAIEGTDRSSLR----ILGSVGEPINpeayewYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 256 EQAREQGIRCFCGYGLTEFASTVCA----KEADGLADVGSPLPGREVKIVNNE-------------VWLRAASMAEGYWR 318
Cdd:cd17634 376 KKIGKEKCPVVDTWWQTETGGFMITplpgAIELKAGSATRPVFGVQPAVVDNEghpqpggtegnlvITDPWPGQTRTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 319 NGQ--LVS-LVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRP 394
Cdd:cd17634 456 DHErfEQTyFSTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAP 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 727407383 395 VAVMEYDHESVD-------LSEWVKDKLARFQQP--VRWLTLPPELKNGGI 436
Cdd:cd17634 536 YAYVVLNHGVEPspelyaeLRNWVRKEIGPLATPdvVHWVDSLPKTRSGKI 586
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-450 |
2.08e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK05691 1146 ERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 97 NLTLQFALVPDGE-NTFPALTSLHIQRVEGAHAAAWQPT---------RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGV 166
Cdd:PRK05691 1226 DSGVELLLTQSHLlERLPQAEGVSAIALDSLHLDSWPSQapglhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 167 LSLIPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLEQMLA--GCTHASLVPTqLWRLLVNRSS 237
Cdd:PRK05691 1306 QATYALDDSDVLMQKAPIsFDVSVWECFWP-LITGCRLVLagpgehRDPQRIAELVQqyGVTTLHFVPP-LLQLFIDEPL 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 238 V----SLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTV----CAKEADGLADVGSPLPGREVKI------- 300
Cdd:PRK05691 1384 AaactSLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAINVthwqCQAEDGERSPIGRPLGNVLCRVldaelnl 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 ----VNNEVWLRAASMAEGYWRNGQLVS--LVND------EGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:PRK05691 1464 lppgVAGELCIGGAGLARGYLGRPALTAerFVPDplgedgARLYRTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEEI 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 368 ERVIAAHPAVLQVfIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLAR----FQQPVRWLTLP--PELKNGgiKISRQ 441
Cdd:PRK05691 1544 QARLLAQPGVAQA-AVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAelpeYMVPAQLIRLDqmPLGPSG--KLDRR 1620
|
490
....*....|.
gi 727407383 442 ALKE--WVQRQ 450
Cdd:PRK05691 1621 ALPEpvWQQRE 1631
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
20-421 |
2.92e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.21 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQcgARVLPVNPqlpqplleellpnlt 99
Cdd:PRK07798 21 ALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK--ARAVPVNV--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 100 lQF-----------------ALVPDGE------NTFPALTSL-HIQRVE---------GAH-----AAAWQPTRLCS--- 138
Cdd:PRK07798 84 -NYryvedelryllddsdavALVYEREfaprvaEVLPRLPKLrTLVVVEdgsgndllpGAVdyedaLAAGSPERDFGers 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 139 -----MTLTSGSTGLPK----------------------AAVHTYQAHLASAEGVLSLIpfgdhddWLLSLPLFHVSGQG 191
Cdd:PRK07798 163 pddlyLLYTGGTTGMPKgvmwrqedifrvllggrdfatgEPIEDEEELAKRAAAGPGMR-------RFPAPPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 192 IMWRWLYAGARMTVRDKQpleqmlagcthaSLVPTQLWRLL----VNRSSV----------------------SLKAVLL 245
Cdd:PRK07798 236 AAFAALFSGQTVVLLPDV------------RFDADEVWRTIerekVNVITIvgdamarplldaleargpydlsSLFAIAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 246 GGAAipieLTEQAREQGIRCFC------GYGLTE--FASTVCAkeADGLADVGSPL--PGREVKIV---NNEV------- 305
Cdd:PRK07798 304 GGAL----FSPSVKEALLELLPnvvltdSIGSSEtgFGGSGTV--AKGAVHTGGPRftIGPRTVVLdedGNPVepgsgei 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 306 -WL-RAASMAEGYW------------RNGQLVSLVNDegwYATRDRGemhnGKLTIVGRLDNLFFSGGEGIQPEEVERVI 371
Cdd:PRK07798 378 gWIaRRGHIPLGYYkdpektaetfptIDGVRYAIPGD---RARVEAD----GTITLLGRGSVCINTGGEKVFPEEVEEAL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 727407383 372 AAHPAVLQVFIVPVADKEFGHRPVAVMEY----DHESVDLSEWVKDKLARFQQP 421
Cdd:PRK07798 451 KAHPDVADALVVGVPDERWGQEVVAVVQLregaRPDLAELRAHCRSSLAGYKVP 504
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
224-444 |
3.61e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 224 VPTQLW---RLLvnRSSVSLKAVLLGGAAIPIELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADVGSPLPGREVKI 300
Cdd:PRK08308 197 VPLMLHilgRLL--PGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKSHLDLGNPLPHVSVSA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 VNNEVwlraasmaegywRNGQLVSLVNDEGWYaTRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:PRK08308 275 GSDEN------------APEEIVVKMGDKEIF-TKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 380 VFIVPVADKEFGHRPVAVMEYDHE--SVDLSEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQALK 444
Cdd:PRK08308 342 AVVYRGKDPVAGERVKAKVISHEEidPVQLREWCIQHLAPYQVPHEIESVTeiPKNANG--KVSRKLLE 408
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-451 |
3.91e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 61.93 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 12 RQVRGETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGarVLPVNP------- 84
Cdd:PRK10946 33 RHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNAlfshqrs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 85 --QLPQPLLEELLPNLTLQFALVPDGE--NTF----PALTSLHIQRVEGAHA-AAW----------QPTR---LCSMTLT 142
Cdd:PRK10946 111 elNAYASQIEPALLIADRQHALFSDDDflNTLvaehSSLRVVLLLNDDGEHSlDDAinhpaedftaTPSPadeVAFFQLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 143 SGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH---VSGQGIMWRWLYAGARMTVRDKQPLeqmlaGC- 218
Cdd:PRK10946 191 GGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypMSSPGALGVFLAGGTVVLAPDPSAT-----LCf 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 219 --------THASLVP--TQLWRLLVNRSS-----VSLKAVLLGGAA--------IPIELTEQAREQgircfcgYGLTEfa 275
Cdd:PRK10946 266 pliekhqvNVTALVPpaVSLWLQAIAEGGsraqlASLKLLQVGGARlsetlarrIPAELGCQLQQV-------FGMAE-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 276 STVCAKEADGLADV-----GSPL-PGREVKIVNNE-----------VWLRAASMAEGYWRNGQLVSLVND-EGWYATRDR 337
Cdd:PRK10946 337 GLVNYTRLDDSDERifttqGRPMsPDDEVWVADADgnplpqgevgrLMTRGPYTFRGYYKSPQHNASAFDaNGFYCSGDL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 338 GEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESVDLSEWVKDK 414
Cdd:PRK10946 417 VSIdPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAflVVKEPLKAVQLRRFLREQ 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 727407383 415 -LARFQQPVRWLTLP--PELKNGgiKISRQALKEWVQRQQ 451
Cdd:PRK10946 497 gIAEFKLPDRVECVDslPLTAVG--KVDKKQLRQWLASRA 534
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
132-382 |
4.53e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 61.96 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLI-----PFGDHDDWLLSLPLFHVSGQGI------------MW 194
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLSYLPLAHIFDRVIeecfiqhgaaigFW 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 195 RW--------------------------LYAGARMTVRDKQPLEQ-------------MLAGCTHASLVPTqLWRLLVNR 235
Cdd:PLN02614 301 RGdvklliedlgelkptifcavprvldrVYSGLQKKLSDGGFLKKfvfdsafsykfgnMKKGQSHVEASPL-CDKLVFNK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 236 SSVSLKA---VLLGGAAiPIELTEQAREQGIRC---FCGYGLTEFASTVCAK---EADGLADVGSPLPGREVKI------ 300
Cdd:PLN02614 380 VKQGLGGnvrIILSGAA-PLASHVESFLRVVACchvLQGYGLTESCAGTFVSlpdELDMLGTVGPPVPNVDIRLesvpem 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 301 --------VNNEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQPEEVERV 370
Cdd:PLN02614 459 eydalastPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQpNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
330
....*....|..
gi 727407383 371 IAAHPAVLQVFI 382
Cdd:PLN02614 539 YGEVQAVDSVWV 550
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
132-382 |
5.42e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 61.40 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGD-----HDDWLLSLPLFHVSGQGIMWRWLYAGA----- 201
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDrvateEDSYFSYLPLAHVYDQVIETYCISKGAsigfw 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 202 ----RMTVRDKQPLE------------------------------------------QMLAGCTHASLVPtQLWRLLVNR 235
Cdd:PLN02861 298 qgdiRYLMEDVQALKptifcgvprvydriytgimqkissggmlrkklfdfaynyklgNLRKGLKQEEASP-RLDRLVFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 236 SSVSLKA---VLLGGAA-IPIELTEQAREQGIRCFC-GYGLTEFAS---TVCAKEADGLADVGSPLPGREVKIVN----- 302
Cdd:PLN02861 377 IKEGLGGrvrLLLSGAApLPRHVEEFLRVTSCSVLSqGYGLTESCGgcfTSIANVFSMVGTVGVPMTTIEARLESvpemg 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 303 ---------NEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQPEEVERVI 371
Cdd:PLN02861 457 ydalsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQpNGAMKIIDRKKNIFkLSQGEYVAVENLENTY 536
|
330
....*....|.
gi 727407383 372 AAHPAVLQVFI 382
Cdd:PLN02861 537 SRCPLIASIWV 547
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
239-391 |
7.41e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 60.80 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 239 SLKAVLLGGAAIPIELTEQAREQgIRCFC--GYGLTEFASTVCAKEADGLA---DVGSPLPGREVKIVNN---------- 303
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEM-TGCPIteGYGLSETSPVATCNPVDATEfsgTIGLPLPSTEVSIRDDdgndlplgep 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 -EVWLRAASMAEGYW-RNGQLVSLVNDEGWYATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK07059 407 gEICIRGPQVMAGYWnRPDETAKVMTADGFFRTGDVGVMDeRGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEV 486
|
170
....*....|.
gi 727407383 381 FIVPVADKEFG 391
Cdd:PRK07059 487 AAVGVPDEHSG 497
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-443 |
1.93e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.17 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 17 ETIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQ----------- 85
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEyprerlaymie 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 86 -------LPQPLLEELLPNLTLQFALVPDGENTFPALTSlhiqrvEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQA 158
Cdd:PRK12467 1669 dsgiellLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYS------DSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGA 1742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 159 HLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLEQMLA--GCTHASLVPTQLW 229
Cdd:PRK12467 1743 LVNRLCATQEAYQLSAADVVLQFTSFaFDVSVWELFWP-LINGARLVIappgahRDPEQLIQLIErqQVTTLHFVPSMLQ 1821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 230 RLLVNRSSV----SLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTV----CAK---EADGLADVGSPLPGR 296
Cdd:PRK12467 1822 QLLQMDEQVehplSLRRVVCGGEALEVEALRPWLERlpDTGLFNLYGPTETAVDVthwtCRRkdlEGRDSVPIGQPIANL 1901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 297 EVKIVNN-----------EVWLRAASMAEGYWRNGQLVS--LVND------EGWYATRD--RGEMhNGKLTIVGRLDNLF 355
Cdd:PRK12467 1902 STYILDAslnpvpigvagELYLGGVGLARGYLNRPALTAerFVADpfgtvgSRLYRTGDlaRYRA-DGVIEYLGRIDHQV 1980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 356 FSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVA-VMEYDHESVD-----------LSEWVKDKLARFQQPVR 423
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAyVVPTDPGLVDddeaqvalraiLKNHLKASLPEYMVPAH 2059
|
490 500
....*....|....*....|..
gi 727407383 424 WLTLP--PELKNGgiKISRQAL 443
Cdd:PRK12467 2060 LVFLArmPLTPNG--KLDRKAL 2079
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
132-370 |
2.05e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.72 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGI-MWRWLYAGARMTVRdKQP 210
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLY-PSP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 211 LeqmlagctHASLVPtqlwRLLVNRSSVSL--KAVLLG-------------------GAAipiELTEQAREQ-----GIR 264
Cdd:PRK08043 442 L--------HYRIVP----ELVYDRNCTVLfgTSTFLGnyarfanpydfarlryvvaGAE---KLQESTKQLwqdkfGLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 265 CFCGYGLTEFASTVC--AKEADGLADVGSPLPGREVKIVN-------NEVWLRAASMAEGYWR---NGQLV--SLVNDEG 330
Cdd:PRK08043 507 ILEGYGVTECAPVVSinVPMAAKPGTVGRILPGMDARLLSvpgieqgGRLQLKGPNIMNGYLRvekPGVLEvpTAENARG 586
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 727407383 331 -----WYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERV 370
Cdd:PRK08043 587 emergWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL 632
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
281-406 |
2.77e-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: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 281 KEADGLADVGSPLPGREVKIVNNE-----------VWLRAASMAEGYWRNGQLVSLV-NDEGWYATRDRGEMHNGKLTIV 348
Cdd:cd05908 308 SECLTFVEVGKPIDETDIRICDEDnkilpdgyighIQIRGKNVTPGYYNNPEATAKVfTDDGWLKTGDLGFIRNGRLVIT 387
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVL--QVFIVPVADKEFGHRPVAVMEYDHESVD 406
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNEEIFCFIEHRKSED 447
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
142-394 |
3.10e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.01 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLS-LPLFHVSGQGIMWRWLYAGARM-----TVRDKQP----- 210
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSwLPLYHDMGLAFLLTAALAGAPLwlaptTAFSASPfrwls 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 211 -LEQMLAGCTHAslvPTQLWRLlVNRSSVSLKAVLLGGAAIPIELTEQAREQGIRCFC---------------GYGLTEF 274
Cdd:PRK05851 240 wLSDSRATLTAA---PNFAYNL-IGKYARRVSDVDLGALRVALNGGEPVDCDGFERFAtamapfgfdagaaapSYGLAES 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 275 ASTVCAKE-ADGL----------------ADVGSPLPGREVKI--------VNN----EVWLRAASMAEGYWrnGQlvSL 325
Cdd:PRK05851 316 TCAVTVPVpGIGLrvdevttddgsgarrhAVLGNPIPGMEVRIspgdgaagVAGreigEIEIRGASMMSGYL--GQ--AP 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727407383 326 VNDEGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRP 394
Cdd:PRK05851 392 IDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARP 460
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-444 |
4.65e-09 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 58.66 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 9 RHWRQVRGETIALRLNDEQ-----LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN 83
Cdd:cd05968 68 DKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 84 PQLPQPLLEELLPNLTLQFALVPDG---------------------------------ENTFPALTSLHIQRVE-----G 125
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALITADGftrrgrevnlkeeadkacaqcptvekvvvvrhlGNDFTPAKGRDLSYDEeketaG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 126 AHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAH-LASAEGVLSLIPFGDHDDwllslpLFHVSGQG-IMWRWLY----- 198
Cdd:cd05968 228 DGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDL------LTWFTDLGwMMGPWLIfggli 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 199 AGARMTVRDKQP-------LEQMLA--GCTHASLVPTqLWRLL-------VNRSSVSlKAVLLGGAAIPIEL-------- 254
Cdd:cd05968 302 LGATMVLYDGAPdhpkadrLWRMVEdhEITHLGLSPT-LIRALkprgdapVNAHDLS-SLRVLGSTGEPWNPepwnwlfe 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 255 ---------------TEQAreQGIrcFCGYGLTE-----FASTVCAKEADGLADVGSPLPGREVKIVNNEVWLraaSMAE 314
Cdd:cd05968 380 tvgkgrnpiinysggTEIS--GGI--LGNVLIKPikpssFNGPVPGMKADVLDESGKPARPEVGELVLLAPWP---GMTR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 315 GYWRN------------------GQLVSLVNDEGWYatrdrgemhngkltIVGRLDNLFFSGGEGIQPEEVERVIAAHPA 376
Cdd:cd05968 453 GFWRDedryletywsrfdnvwvhGDFAYYDEEGYFY--------------ILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727407383 377 VLQVFIVPVADKEFGHRPV--AVMEYDHESV-----DLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVcfVVLKPGVTPTealaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
132-383 |
5.40e-09 |
|
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: 58.14 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 132 QPTRLCSMTLTSGSTGLPKAAV--H---TYQAHLASAEgvLSLIPFGDHDDWLLS-LPLFHVSGQGI-MWRWLYAGARM- 203
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMlsHdniTWTAKAASQH--MDLRPATVGQESVVSyLPLSHIAAQILdIWLPIKVGGQVy 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 204 -------------TVRDKQPL---------EQMLAGCTHASLVPTQLWRLLVNRS-SVSLKA------------------ 242
Cdd:cd05933 226 faqpdalkgtlvkTLREVRPTafmgvprvwEKIQEKMKAVGAKSGTLKRKIASWAkGVGLETnlklmggespsplfyrla 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 243 -------------------VLLGGAAIPIELTEQAREQGIRCFCGYGLTEFAS--TVCAKEADGLADVGSPLPGREVKIV 301
Cdd:cd05933 306 kklvfkkvrkalgldrcqkFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGphTISNPQAYRLLSCGKALPGCKTKIH 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 302 N------NEVWLRAASMAEGYWRNGQLVS-LVNDEGWYATRDRGEM-HNGKLTIVGRLDNLFF-SGGEGIQPEEVE-RVI 371
Cdd:cd05933 386 NpdadgiGEICFWGRHVFMGYLNMEDKTEeAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIItAGGENVPPVPIEdAVK 465
|
330
....*....|..
gi 727407383 372 AAHPAVLQVFIV 383
Cdd:cd05933 466 KELPIISNAMLI 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
133-424 |
1.63e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 56.71 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 133 PTRLCSMTltsGSTGLPKAAVHTYQAHLASAEGVLSLIPFG-DHDD-WLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQP 210
Cdd:PRK05620 183 AAAICYST---GTTGAPKGVVYSHRSLYLQSLSLRTTDSLAvTHGEsFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 211 LEQMLAGCTHASL------VPTqLW-RLLVNR-----SSVSLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEfAST 277
Cdd:PRK05620 260 SAPTLAKIIATAMprvahgVPT-LWiQLMVHYlknppERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTE-TSP 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 278 V--CAKEADGLA---------DVGSPLPGREVKIVNN------------EVWLRAASMAEGYW-----RNGQLVSLVNDE 329
Cdd:PRK05620 338 VgtVARPPSGVSgearwayrvSQGRFPASLEYRIVNDgqvmestdrnegEIQVRGNWVTASYYhspteEGGGAASTFRGE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 330 ------------GWYATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA 396
Cdd:PRK05620 418 dvedandrftadGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
330 340 350
....*....|....*....|....*....|....*
gi 727407383 397 V------MEYDHESV-DLSEWVKDKLARFQQPVRW 424
Cdd:PRK05620 498 VtvlapgIEPTRETAeRLRDQLRDRLPNWMLPEYW 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
118-379 |
1.64e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.10 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 118 LHIQRVEGAHAAAWQ-----PTRLCSMTLTSGSTGLPKAaVHTYQAHLASAEGVLSL---IPFGDhDDWLLS-LPLFHVS 188
Cdd:PRK05691 145 LCVDTLDPALAEAWQepalqPDDIAFLQYTSGSTALPKG-VQVSHGNLVANEQLIRHgfgIDLNP-DDVIVSwLPLYHDM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 189 GQ-GIMWRWLYAGARMTVRDKQ-----PLEQMLAGCTHASLV---PTQLWRLLVNR-SSVSLKAVLLGGAAIPIELTEQA 258
Cdd:PRK05691 223 GLiGGLLQPIFSGVPCVLMSPAyflerPLRWLEAISEYGGTIsggPDFAYRLCSERvSESALERLDLSRWRVAYSGSEPI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 259 REQGIRCF------CG---------YGLTE-----------------------FASTVcAKEADG--LADVGSPLPGREV 298
Cdd:PRK05691 303 RQDSLERFaekfaaCGfdpdsffasYGLAEatlfvsggrrgqgipaleldaeaLARNR-AEPGTGsvLMSCGRSQPGHAV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 299 KIVN------------NEVWLRAASMAEGYWRNGQLVS--LVNDEG--WYATRDRGEMHNGKLTIVGRLDNLFFSGGEGI 362
Cdd:PRK05691 382 LIVDpqslevlgdnrvGEIWASGPSIAHGYWRNPEASAktFVEHDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNL 461
|
330
....*....|....*..
gi 727407383 363 QPEEVERVIAAHPAVLQ 379
Cdd:PRK05691 462 YPQDIEKTVEREVEVVR 478
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
26-421 |
1.76e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.56 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfALV 105
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR-VLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 106 P----DG---ENTFPALTSLHIQ-RVEG------AHAAAWQP--TRLCS--MTLTSGSTGLPKAAVHTYQAHLASAEG-- 165
Cdd:PRK13390 102 AsaalDGlaaKVGADLPLRLSFGgEIDGfgsfeaALAGAGPRltEQPCGavMLYSSGTTGFPKGIQPDLPGRDVDAPGdp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 166 ----VLSLIPFGDHDDWLLSLPLFHVSGqgimWRW---LYAGARMTVRDKQPLEQMLAG------CTHASLVPTQLWRLL 232
Cdd:PRK13390 182 ivaiARAFYDISESDIYYSSAPIYHAAP----LRWcsmVHALGGTVVLAKRFDAQATLGhveryrITVTQMVPTMFVRLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 233 VNRSSV-------SLKAVLLGGAAIPIELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLA----------------- 287
Cdd:PRK13390 258 KLDADVrtrydvsSLRAVIHAAAPCPVDVKHAMIDWlGPIVYEYYSSTEAHGMTFIDSPDWLAhpgsvgrsvlgdlhicd 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 288 DVGSPLPGREVKIV-------------NNEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMhngkltivgrldnL 354
Cdd:PRK13390 338 DDGNELPAGRIGTVyferdrlpfrylnDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSF-------------M 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727407383 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEY-------DHESVDLSEWVKDKLARFQQP 421
Cdd:PRK13390 405 IISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLvegirgsDELARELIDYTRSRIAHYKAP 478
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
290-399 |
6.39e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.54 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 290 GSPLPGREVKIVNNE-----------VWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMHNGKLTIVGRLDNLFFSG 358
Cdd:PRK09192 388 GKALPGHEIEIRNEAgmplpervvghICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIIN 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 727407383 359 GEGIQPEEVERVIAAHPAVLQ----VFIVpvaDKEFGHRPVAVME 399
Cdd:PRK09192 468 GRNIWPQDIEWIAEQEPELRSgdaaAFSI---AQENGEKIVLLVQ 509
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
142-373 |
7.81e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.50 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGqgimwrwLYAGARMTvrdkqpleqMLAGctha 221
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFG-------LTGGLVLP---------LLSG---- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 222 slVPTQLWRLLVNRSSV--------------------------------SLKAVLLGGAAIPiELTEQ--AREQGIRCFC 267
Cdd:PRK06814 861 --VKVFLYPSPLHYRIIpeliydtnatilfgtdtflngyaryahpydfrSLRYVFAGAEKVK-EETRQtwMEKFGIRILE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 268 GYGLTEfASTVCAKE---ADGLADVGSPLPGREVKIVNNE-------VWLRAASMAEGYWR---NGQLVSLVndEGWYAT 334
Cdd:PRK06814 938 GYGVTE-TAPVIALNtpmHNKAGTVGRLLPGIEYRLEPVPgideggrLFVRGPNVMLGYLRaenPGVLEPPA--DGWYDT 1014
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727407383 335 RDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAA 373
Cdd:PRK06814 1015 GDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
20-301 |
1.33e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 50.67 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 20 ALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALL-------------------QCGARVL 80
Cdd:PRK09274 34 DGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFkagavpvlvdpgmgiknlkQCLAEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 81 P---VNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSL-HIQRVEGAHA---AAWQPTRLCSMTLTSGSTGLPKAAV 153
Cdd:PRK09274 114 PdafIGIPKAHLARRLFGWGKPSVRRLVTVGGRLLWGGTTLaTLLRDGAAAPfpmADLAPDDMAAILFTSGSTGTPKGVV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 154 HTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGqgimwrwLYAGARMTVRDKQPL-------EQMLA-----GCTHA 221
Cdd:PRK09274 194 YTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFG-------PALGMTSVIPDMDPTrpatvdpAKLFAaieryGVTNL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 222 SLVPTqLWRLL----VNRSSV--SLKAVLLGGAAIPIELTEQARE---QGIRCFCGYGLTE------------FASTVCA 280
Cdd:PRK09274 267 FGSPA-LLERLgrygEANGIKlpSLRRVISAGAPVPIAVIERFRAmlpPDAEILTPYGATEalpissiesreiLFATRAA 345
|
330 340
....*....|....*....|.
gi 727407383 281 KEADGLADVGSPLPGREVKIV 301
Cdd:PRK09274 346 TDNGAGICVGRPVDGVEVRII 366
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
366-421 |
1.82e-06 |
|
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: 45.61 E-value: 1.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 366 EVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VMEYDHESV--DLSEWVKDKLARFQQP 421
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAfvVLKPGVELLeeELVAHVREELGPYAVP 60
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
142-374 |
2.08e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.81 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRW-LYAGARMtVRDKQPLEQM----LA 216
Cdd:PRK06334 191 TSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFpLLSGVPV-VFAYNPLYPKkiveMI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 217 GCTHASLV---PTQLWRLLV-----NRSSVSLKAVLLGGAAIPIELTEQAREQ--GIRCFCGYGLTEFASTVCAKEADGL 286
Cdd:PRK06334 270 DEAKVTFLgstPVFFDYILKtakkqESCLPSLRFVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTECSPVITINTVNSP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 287 AD---VGSPLPGREVKIVNNE------------VWLRAASMAEGYWRN--GQLVSLVNDEGWYATRDRGEM-HNGKLTIV 348
Cdd:PRK06334 350 KHescVGMPIRGMDVLIVSEEtkvpvssgetglVLTRGTSLFSGYLGEdfGQGFVELGGETWYVTGDLGYVdRHGELFLK 429
|
250 260
....*....|....*....|....*.
gi 727407383 349 GRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:PRK06334 430 GRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
290-377 |
7.00e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 48.35 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 290 GSPLPGREVKIVNN-----------EVWLRAA--SMAEGYWRNGQLVSLVNDEGWYATRDRGEM-HNGKLTIVGRLDNLF 355
Cdd:PRK04319 379 GKPLPGIEAAIVDDqgnelppnrmgNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMdEDGYFWFQGRVDDVI 458
|
90 100
....*....|....*....|..
gi 727407383 356 FSGGEGIQPEEVERVIAAHPAV 377
Cdd:PRK04319 459 KTSGERVGPFEVESKLMEHPAV 480
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
142-192 |
1.07e-05 |
|
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: 47.67 E-value: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAeGVLSLIPFGDHDDWLLSLPLFHVSGQGI 192
Cdd:cd05938 152 TSGTTGLPKAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLL 201
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
142-377 |
1.89e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLSLPLFHV---SGQGIMwrwLYAGAR--------------- 202
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPLAHIlelAAESVM---AAVGAAigygspltltdtsnk 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 203 ----------------MT--------VRD---------------------KQPLEQMLAGCTHASLVPTQLWRLLVNRS- 236
Cdd:PLN02387 335 ikkgtkgdasalkptlMTavpaildrVRDgvrkkvdakgglakklfdiayKRRLAAIEGSWFGAWGLEKLLWDALVFKKi 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 237 ----SVSLKAVLLGGAaiPIELTEQaREQGIrCFC-----GYGLTEfastVCA----KEAD--GLADVGSPLPGREVKIV 301
Cdd:PLN02387 415 ravlGGRIRFMLSGGA--PLSGDTQ-RFINI-CLGapigqGYGLTE----TCAgatfSEWDdtSVGRVGPPLPCCYVKLV 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 302 N---------------NEVWLRAASMAEGYWRNGQL---VSLVNDEG--WYATRDRGEMH-NGKLTIVGRL-DNLFFSGG 359
Cdd:PLN02387 487 SweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKtdeVYKVDERGmrWFYTGDIGQFHpDGCLEIIDRKkDIVKLQHG 566
|
330
....*....|....*...
gi 727407383 360 EGIQPEEVERVIAAHPAV 377
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYV 584
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
25-193 |
2.21e-05 |
|
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: 46.65 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfAL 104
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAK-AL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 105 VPDGENTFPALTSLHIQRVEGAHAAawqpTRLCSMtLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL 184
Cdd:cd05939 80 IFNLLDPLLTQSSTEPPSQDDVNFR----DKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPL 154
|
....*....
gi 727407383 185 FHVSGqGIM 193
Cdd:cd05939 155 YHSAG-GIM 162
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
30-189 |
2.71e-05 |
|
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: 46.27 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 30 WRELCARVDELASGF-AAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpvnpqlpqplleellpnltlqfalVPDG 108
Cdd:cd05937 8 YSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGA---------------------------APAF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 109 ENTfpALTS---LHIQRVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLF 185
Cdd:cd05937 61 INY--NLSGdplIHCLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLY 138
|
....
gi 727407383 186 HVSG 189
Cdd:cd05937 139 HGTA 142
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
290-397 |
2.91e-05 |
|
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: 46.54 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 290 GSPLPGREVKIVN---NEVWLRAASM-----------AEGYWRNGQLVS---LVNDEGWYATRDRGEM-HNGKLTIVGRL 351
Cdd:cd05967 414 GKPVPGYQVQVLDedgEPVGPNELGNiviklplppgcLLTLWKNDERFKklyLSKFPGYYDTGDAGYKdEDGYLFIMGRT 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 727407383 352 DNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAV 397
Cdd:cd05967 494 DDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGL 539
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
304-416 |
1.82e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.78 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 304 EVWLRAASMAEGYWRNGQLV------SLVN-----DEG-WYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVE--- 368
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETertfgaTLVDpspgtPEGpWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEati 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 727407383 369 ------RVIAahpavlqvFIVPVADKEfghRPVAVMEYDHESvDLSEWVKDKLA 416
Cdd:PRK05850 479 qeitggRVAA--------ISVPDDGTE---KLVAIIELKKRG-DSDEEAMDRLR 520
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
12-71 |
8.20e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.70 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727407383 12 RQVRGETIALRLNDE-----QLNWRELCARVDELASGFAAQGVVEG---SGVMLrawNTPQTLLAWLA 71
Cdd:PRK03584 94 RHRRDDRPAIIFRGEdgprrELSWAELRRQVAALAAALRALGVGPGdrvAAYLP---NIPETVVAMLA 158
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
267-384 |
2.42e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 40.48 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727407383 267 CGY-GLTEFASTVcakeaDglADVGSPLPGREVkivnNEVWLRAASMAEGYW----------RNgQLVSLVN-------- 327
Cdd:PRK07769 393 AGKvGVSEWAVIV-----D--PETASELPDGQI----GEIWLHGNNIGTGYWgkpeetaatfQN-ILKSRLSeshaegap 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727407383 328 -DEGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVER-VIAAHPAV----LQVFIVP 384
Cdd:PRK07769 461 dDALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYtAQEATKALrtgyVAAFSVP 523
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
26-77 |
9.66e-03 |
|
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: 38.41 E-value: 9.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 727407383 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGA 77
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGA 148
|
|
| |
