|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
41-574 |
0e+00 |
|
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: 929.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 41 PAKFNFASDVIDHWASVEKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWW 120
Cdd:cd05928 2 PEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 121 LMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKE 200
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 201 ASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVL 280
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 GACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 360
Cdd:cd05928 242 GACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIGMFSGYVDNPKKTQDNIRG 440
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 441 DFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPE 520
Cdd:cd05928 402 DFYLTGDRGIMDEDGYFWFMGRADDVINSSG-----YRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQ 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 295789127 521 FLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 574
Cdd:cd05928 477 FLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
81-571 |
0e+00 |
|
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: 593.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 160
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHcSLGI 240
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHTH-SYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 241 KAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 320
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQG 400
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 401 NVLPPGKEGDIAIRVKpiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIG 480
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG-----YRIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 481 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTV 560
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTI 417
|
490
....*....|.
gi 295789127 561 TGKIERAKLRA 571
Cdd:cd05972 418 SGKIRRVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-574 |
2.09e-175 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 508.11 E-value: 2.09e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 40 APAKFNFASDVIDHWASvekagKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW 119
Cdd:COG0365 4 VGGRLNIAYNCLDRHAE-----GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 120 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVA---------QEVDAVAPDCSFLKIKLLV----SEN 186
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 187 SREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAW 266
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 267 IMNILGAFLEPWVLGACIFVH-LLPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGET 341
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 342 LLPETLENWKAKTGLEIREIYGQTETGLICrVS--RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiW 419
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGGIF-ISnlPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-GP-W 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 420 PiGMFSGYVDNPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSE 496
Cdd:COG0365 395 P-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSG-----HRIGTAEIESALVSHPAVAE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 497 TAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 574
Cdd:COG0365 469 AAVVGVPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
40-573 |
1.02e-157 |
|
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: 461.96 E-value: 1.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 40 APAKFNFASDVIDHWASvEKAGKRssgpALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW 119
Cdd:cd05970 12 VPENFNFAYDVVDAMAK-EYPDKL----ALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 120 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA--GDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKAL 197
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 198 LKEASTI----HQCVETESRESAAIYFTSGTSGPPKMAEHSHC-SLG--IKAKMdaasWTGLSTSDIIWTISDTAWIMNI 270
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGhiVTAKY----WQNVREGGLHLTVADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 271 LGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENW 350
Cdd:cd05970 242 WGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 351 KAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIGMFSGYVDN 430
Cdd:cd05970 322 KEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 431 PKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEV 510
Cdd:cd05970 402 AEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSG-----YRIGPFEVESALIQHPAVLECAVTGVPDPIRGQV 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789127 511 VKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:cd05970 477 VKATIVLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-580 |
3.03e-115 |
|
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: 350.26 E-value: 3.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 49 DVIDHWASvekagKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMR 128
Cdd:COG0318 3 DLLRRAAA-----RHPDRPALVFGGRR-----LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 129 TGLVFMPGTIQMRSSDILYRLQASKARAIVAgdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcv 208
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 209 etesresAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHL 288
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANA-AAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT--LVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 289 LPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET 367
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 GLIC--RVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWLM 445
Cdd:COG0318 253 SPVVtvNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 446 GDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHD 525
Cdd:COG0318 328 GDLGRLDEDGYLYIVGRKKDMIISGG-----ENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA-ELD 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 526 RDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 580
Cdd:COG0318 402 AEELRAFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-571 |
6.09e-111 |
|
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: 338.64 E-value: 6.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 159
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSL- 238
Cdd:cd05971 85 --------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 239 ----GIKAKMDAASWTGlstsDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPI 314
Cdd:cd05971 115 ghlpGVQFPFNLFPRDG----DLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 315 IYRMLLQQDLSSYKFP-HLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLI---CrvSRTMKVKPGYLGTAFAH 390
Cdd:cd05971 191 ALKMMRQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVignC--SALFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 391 YDVQVIDEQGNVLPPGKEGDIAIRV-KPIwpigMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINS 469
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVELpDPV----AFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 470 SGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRK 549
Cdd:cd05971 345 SG-----YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPRE 417
|
490 500
....*....|....*....|..
gi 295789127 550 VEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05971 418 IEFVNELPRTATGKIRRRELRA 439
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-573 |
2.28e-104 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 326.08 E-value: 2.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 43 KFNFASDVIDHWASVEKAGKrssgPALWWMNGSGKEiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLM 122
Cdd:PRK04319 41 KVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 123 ILGCMRTGLV-------FMPGTIqmRSsdilyRLQASKARAIVAGDEVAQEVdaVAPDCSFLKIKLLVSENSR--EGWLN 193
Cdd:PRK04319 115 LLGALKNGAIvgplfeaFMEEAV--RD-----RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 194 FKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHcslgiKAkMDAASWTG-----LSTSDIIWTISDTAWIM 268
Cdd:PRK04319 186 FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NA-MLQHYQTGkyvldLHEDDVYWCTADPGWVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 269 NILGAFLEPWVLGACIFVhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETLLPE 345
Cdd:PRK04319 260 GTSYGIFAPWLNGATNVI-DGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLNPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 346 TLEnWKAKT-GLEIREIYGQTETG--LICRVsRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIrvKPIWPiG 422
Cdd:PRK04319 339 VVR-WGMKVfGLPIHDNWWMTETGgiMIANY-PAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-S 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 423 MFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISS 502
Cdd:PRK04319 414 MMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSG-----ERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295789127 503 PDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK04319 489 PDPVRGEIIKAFVALRPGY--EPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-573 |
7.39e-101 |
|
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: 312.58 E-value: 7.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKArAIVAGD 161
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSLGIk 241
Cdd:cd05974 80 EN----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPV- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ 321
Cdd:cd05974 113 GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 322 QDLSSYKFPhLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGN 401
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 402 vlpPGKEGDIAIRVKPIWPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGP 481
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSD-----YRISP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 482 SEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVlDLPKTVT 561
Cdd:cd05974 344 FELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTIS 420
|
490
....*....|..
gi 295789127 562 GKIERAKLRAKE 573
Cdd:cd05974 421 GKIRRVELRRRE 432
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
58-570 |
8.11e-99 |
|
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: 308.34 E-value: 8.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 58 EKAGKRSSGPALWWMngsGKeiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 137
Cdd:cd05936 7 EAARRFPDKTALIFM---GR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 138 IQMRSSDILYRLQASKARAIVAGDEvaqevdavapdcsflkikllvsensregwlnFKALLKEASTIHQCVETESRESAA 217
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTPEDVAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIwtisdtawIMNILGAF---------LEPWVLGACIFvhL 288
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDV--------VLAALPLFhvfgltvalLLPLALGATIV--L 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 289 LPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET 367
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 G-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGDFWL 444
Cdd:cd05936 280 SpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAFVDGWLR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSH 524
Cdd:cd05936 353 TGDIGYMDEDGYFFIVDRKKDMIIVGG-----FNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG-ASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 295789127 525 DRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05936 427 TEEEIIAFCREQL----AGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
81-573 |
7.99e-97 |
|
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: 302.50 E-value: 7.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 160
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEVAQEVDAVAPdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPKMAEHSHCSLgI 240
Cdd:cd05969 80 EELYERTDPEDP-------------------------------------------TLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 241 KAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLlPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 320
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQD---LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG--LICRVSrTMKVKPGYLGTAFAHYDVQV 395
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsiMIANYP-CMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 396 IDEQGNVLPPGKEGDIAIrvKPIWPiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfc 475
Cdd:cd05969 274 VDENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSG---- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 476 rYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLD 555
Cdd:cd05969 347 -HRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDELKEEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*...
gi 295789127 556 LPKTVTGKIERAKLRAKE 573
Cdd:cd05969 424 LPKTRSGKIMRRVLKAKE 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
216-564 |
2.54e-91 |
|
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: 284.18 E-value: 2.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACIFvhLLPKFDSQ 295
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLG-ALLAGGTVV--LLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 296 TVLKVLSSYPINTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVS 374
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 375 R--TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD 452
Cdd:cd04433 159 PpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 453 PEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLTKV 532
Cdd:cd04433 234 EDGYLYIVGRLKDMIKSGG-----ENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-----ADLDAEE 303
|
330 340 350
....*....|....*....|....*....|..
gi 295789127 533 LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 564
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
42-570 |
2.95e-87 |
|
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: 279.64 E-value: 2.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 42 AKFNFASDVIDHwasveKAGKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWL 121
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 122 MILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSRE--GWLNFKALLK 199
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 200 EASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEP-W 278
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 279 VLGACIfvhLLPKFDS-QTVLKVLSSYPINTLVGAPIIYR-MLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL 356
Cdd:cd05959 230 VGATTV---LMPERPTpAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 357 EIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKT 434
Cdd:cd05959 307 DILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR-------GpsSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 435 QDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAF 514
Cdd:cd05959 380 RDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIW-----VSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 515 VVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05959 455 VVLRPGY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-570 |
3.32e-87 |
|
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: 277.09 E-value: 3.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAgd 161
Cdd:cd05973 2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQevdavapdcsflkikllvsensregwlnfKALLKEASTIHQcvetesresaaiyFTSGTSGPPKMAEHSHCSL-GI 240
Cdd:cd05973 79 DAAN-----------------------------RHKLDSDPFVMM-------------FTSGTTGLPKGVPVPLRALaAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 241 KAKMDAAswTGLSTSDIIWTISDTAWIMNILGAFLEPWVLG-ACIFVHllPKFDSQTVLKVLSSYPINTLVGAPIIYRML 319
Cdd:cd05973 117 GAYLRDA--VDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 320 LQQDLSSYKFP--HLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMK--VKPGYLGTAFAHYDVQV 395
Cdd:cd05973 193 MAAGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 396 IDEQGNVLPPGKEGDIAIRVKPIwPIGMFSGYVDNPKKTQDnirGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfc 475
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSG---- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 476 rYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLD 555
Cdd:cd05973 345 -YRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSAHAYPRTIHFVDE 421
|
490
....*....|....*
gi 295789127 556 LPKTVTGKIERAKLR 570
Cdd:cd05973 422 LPKTPSGKIQRFLLR 436
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-570 |
2.75e-84 |
|
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: 269.73 E-value: 2.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQ-ASKARA 156
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 IVAGDEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHC 236
Cdd:cd05958 88 LCAHAL-----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 237 SLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGA-CIfvhLLPKFDSQTVLKVLSSYPINTLVGAPII 315
Cdd:cd05958 121 DPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsGV---LLEEATPDLLLSAIARYKPTVLFTAPTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 316 YRMLL------QQDLSSykfphLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFA 389
Cdd:cd05958 198 YRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 390 HYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpigmfSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:cd05958 273 GYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 SSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHdrDQLTKVLQEHVKSVTAPYKYPR 548
Cdd:cd05958 345 SGG-----YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPG--PVLARELQDHAKAHIAPYKYPR 417
|
490 500
....*....|....*....|..
gi 295789127 549 KVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05958 418 AIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-575 |
1.97e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.44 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 60 AGKRSSGPALWWMngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQ 139
Cdd:PRK06187 16 ARKHPDKEAVYFD-----GRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 140 MRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREG----WLNFKALLKEASTIHQCVETESRES 215
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMNiLGAFLEPWVLGACIfvhLLPK-FDS 294
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHRNLFLHS-LAVCAWLKLSRDDVYLVIVPMFHVHA-WGLPYLALMAGAKQ---VIPRrFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 295 QTVLKVLSSYPINTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRV 373
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 374 SR------TMKVKPGYLGTAFAHYDVQVIDEQGNVLPP-GKE-GDIAIRvKPiWpigMFSGYVDNPKKTQDNIRGDfWL- 444
Cdd:PRK06187 325 LPpedqlpGQWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP-W---LMQGYWNRPEATAETIDGG-WLh 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSH 524
Cdd:PRK06187 399 TGDVGYIDEDGYLYITDRIKDVIISGGEN-----IYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGA-TL 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 295789127 525 DRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 575
Cdd:PRK06187 473 DAKELRAFLRGRL----AKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-572 |
1.91e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 254.06 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 55 ASVEKAGKR-SSGPALWWMngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVF 133
Cdd:PRK07656 9 ELLARAARRfGDKEAYVFG-----DQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 134 MPGTIQMRSSDILYRLQASKARAIVAGDEVaQEVDAVAPDcSFLKIKLLV------SENSREGWLNFKALLKEASTIHQC 207
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGLF-LGVDYSATT-RLPALEHVViceteeDDPHTEKMKTFTDFLAAGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 208 VETESRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSD--II---------WTISDTAWIMNilgafle 276
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQL-LSNAADWAEYLGLTEGDryLAanpffhvfgYKAGVNAPLMR------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 277 pwvlGACIFVHllPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 355
Cdd:PRK07656 233 ----GATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 356 LE-IREIYGQTE---TGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNP 431
Cdd:PRK07656 307 VDiVLTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR----GPNVM-KGYYDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 432 KKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEV 510
Cdd:PRK07656 382 EATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGG-----FNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295789127 511 VKAFVVLAP-------EFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PRK07656 457 GKAYVVLKPgaelteeELIAYCREHLAK------------YKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
82-570 |
4.45e-74 |
|
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: 242.75 E-value: 4.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevDAVApdcsflkikllvsensreGWLnfkallkeastihqcvetesresaaiyFTSGTSGPPKMAEHSHCSLGIK 241
Cdd:cd05919 91 ------DDIA------------------YLL---------------------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKfDSQTVLKVLSSYPINTLVGAPIIY-RMLL 320
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQG 400
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 401 NVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIG 480
Cdd:cd05919 279 HTIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW-----VS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 481 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTV 560
Cdd:cd05919 349 PVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
490
....*....|
gi 295789127 561 TGKIERAKLR 570
Cdd:cd05919 427 TGKLQRFKLR 436
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
74-470 |
1.29e-69 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 230.66 E-value: 1.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 74 GSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASK 153
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 154 ARAIVAGDE-VAQEVDAVAPDCSFLKIKLLVS-ENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMA 231
Cdd:pfam00501 94 AKVLITDDAlKLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 EHSH---CSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI-FVHLLPKFDSQTVLKVLSSYPIN 307
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVvLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTM---KVKPGY 383
Cdd:pfam00501 254 VLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 LGTAFAHYDVQVIDEQ-GNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIG 461
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR-GP----GVMKGYLNDPELTAEAFDEDGWYrTGDLGRRDEDGYLEIVG 408
|
....*....
gi 295789127 462 RSDDIINSS 470
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-570 |
5.15e-68 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 228.95 E-value: 5.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 43 KFNFASDVIDHWASVEKAGKrssgpaLWWMNGSGKeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLM 122
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGK------TAFIDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 123 ILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKiKLLVSENSREGWLNFKALLKEAS 202
Cdd:TIGR02262 72 FLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLE-HRVVVGRPEAGEVQLAELLATES 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 203 TIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGA 282
Cdd:TIGR02262 151 EQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 283 CIFVHL-LPKFDSqtVLKVLSSYPINTLVGAPIIYR-MLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 360
Cdd:TIGR02262 231 TTVLMGeRPTPDA--VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGMFS--GYVDNPKKTQDNI 438
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-------GPSSatMYWNNRAKSRDTF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 439 RGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 518
Cdd:TIGR02262 382 QGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIY-----VSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLR 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 519 PEFlshdrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:TIGR02262 457 PGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
60-564 |
5.05e-67 |
|
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: 224.03 E-value: 5.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 60 AGKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiq 139
Cdd:cd17631 5 ARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 140 mrssdILYRLQASKARAIVAgdevaqevDAVApdcsflkiKLLVSENSRegwlnfkallkeastihqcvetesresaaIY 219
Cdd:cd17631 75 -----LNFRLTPPEVAYILA--------DSGA--------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 220 FTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDI---IWTISDTAwimnILGAFLEPwVLGACIFVHLLPKFDSQT 296
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNA-VNALAALDLGPDDVllvVAPLFHIG----GLGVFTLP-TLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETG-LICRVS 374
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 375 RTMKV-KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDP 453
Cdd:cd17631 258 PEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDGWFHTGDLGRLDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 454 EGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrDQLTKV- 532
Cdd:cd17631 333 DGYLYIVDRKKDMIISGG-----ENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG------AELDEDe 401
|
490 500 510
....*....|....*....|....*....|..
gi 295789127 533 LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 564
Cdd:cd17631 402 LIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
42-564 |
7.95e-67 |
|
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: 227.84 E-value: 7.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 42 AKFNFASDVIDHwaSVEKAGKRSsgpALWWMNGSGKEIK-WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWW 120
Cdd:cd17634 50 ATLNLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 121 LMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEV---------------AQEVDAVAPDCSFLKIKLLVSE 185
Cdd:cd17634 124 VAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGvragrsvplkknvddALNPNVTSVEHVIVLKRTGSDI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 186 NSREG-WLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDT 264
Cdd:cd17634 204 DWQEGrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 265 AWIMNILGAFLEPWVLGACIFVHL-LPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGG 339
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 340 ETLLPETLENWKAKTGLEIREI---YGQTETGLICRVSRTMKV--KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIR 414
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEKCPVvdtWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 415 VKpiWPIGMFSGYVDNPKKTQDNIR--GDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHP 492
Cdd:cd17634 444 DP--WPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAG-----HRLGTAEIESVLVAHP 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789127 493 AVSETAVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 564
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
80-571 |
4.10e-66 |
|
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: 222.17 E-value: 4.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 159
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPKMAEHSHCSLG 239
Cdd:cd05941 91 P-------------------------------------------------------ALILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKAKMDAASWTglstsdiiWTISD----------TAWIMNILGAFLepWVLGACIFvhlLPKFDSQTVLKVLSSYPINTL 309
Cdd:cd05941 116 ANVRALVDAWR--------WTEDDvllhvlplhhVHGLVNALLCPL--FAGASVEF---LPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 310 VGAPIIYRMLLQ---------QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVK 380
Cdd:cd05941 183 MGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 381 PGYLGTAFAHYDVQVIDEQGN-VLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFH 458
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYYW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 459 FIGR-SDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQLTkvlqEHV 537
Cdd:cd05941 338 ILGRsSVDIIKSGG-----YKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWA 408
|
490 500 510
....*....|....*....|....*....|....
gi 295789127 538 KSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05941 409 KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
82-569 |
5.50e-65 |
|
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: 218.89 E-value: 5.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesRESAAIYFTSGTSGPPKMAEHSHCSLGIK 241
Cdd:cd05935 82 EL-------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AkMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL- 320
Cdd:cd05935 113 A-LQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYV--LMARWDRETALELIEKYKVTFWTNIPTMLVDLLa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 -----QQDLSSYKFphlhscFSGGETLLPETL-ENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQ 394
Cdd:cd05935 190 tpefkTRDLSSLKV------LTGGGAPMPPAVaEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 395 VID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQD---NIRG-DFWLMGDRGIKDPEGYFHFIGRSDDIINS 469
Cdd:cd05935 264 VIDiETGRELPPNEVGEIVVRGPQI-----FKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 470 SGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdRDQLTKV-LQEHVKSVTAPYKYPR 548
Cdd:cd05935 339 SG-----FKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEY----RGKVTEEdIIEWAREQMAAYKYPR 409
|
490 500
....*....|....*....|.
gi 295789127 549 KVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05935 410 EVEFVDELPRSASGKILWRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-570 |
8.03e-65 |
|
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: 219.88 E-value: 8.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 75 SGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKA 154
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQEVD--AVAPDCSFLKIKLLV---SENSREGWLNF-KALLKEASTihqcvETESRES--AAIYFTSGTSG 226
Cdd:cd05926 88 KLVLTPKGELGPASraASKLGLAILELALDVgvlIRAPSAESLSNlLADKKNAKS-----EGVPLPDdlALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 227 PPKMAEHSHCSLgikakmdAASWTGLSTSDIIwTISDTAWIM-------NILGAFLEPWVLGACIFVHllPKFDSQTVLK 299
Cdd:cd05926 163 RPKGVPLTHRNL-------AASATNITNTYKL-TPDDRTLVVmplfhvhGLVASLLSTLAAGGSVVLP--PRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 300 VLSSYPINTLVGAPIIYRMLLQQDLSSY--KFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG--LICRVSR 375
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 376 TMKVKPGYLGTAFAhYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPE 454
Cdd:cd05926 313 PGPRKPGSVGKPVG-VEVRILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 455 GYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLApEFLSHDRDQLTKVLQ 534
Cdd:cd05926 387 GYLFLTGRIKELINRGGE-----KISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR-EGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 295789127 535 EHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05926 461 KHL----AAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-570 |
1.25e-64 |
|
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: 217.54 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 159
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdaVAPdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPK--MAEHSH-C 236
Cdd:cd05934 81 ----------VDP-------------------------------------------ASILYTSGTTGPPKgvVITHANlT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 237 SLGIKAkmdaASWTGLSTSDIIWTI-----SDtAWIMNILGAFlepWVLGACIfvhLLPKFDSQTVLKVLSSY--PINTL 309
Cdd:cd05934 108 FAGYYS----ARRFGLGEDDVYLTVlplfhIN-AQAVSVLAAL---SVGATLV---LLPRFSASRFWSDVRRYgaTVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 310 VGAPIiyRMLLQQDLSSYKFPH-LHSCFSGGETllPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAF 388
Cdd:cd05934 177 LGAML--SYLLAQPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 389 AHYDVQVIDEQGNVLPPGKEGDIAIRVKPiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIRGLR--GWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 SSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP-------EFLSHDRDQLtkvlqehvksvt 541
Cdd:cd05934 331 RRGE-----NISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgetldpeELFAFCEGQL------------ 393
|
490 500
....*....|....*....|....*....
gi 295789127 542 APYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05934 394 AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-571 |
5.72e-63 |
|
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: 218.13 E-value: 5.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 23 FHMNIKKLIPIQW-----------GHQEAPAKF-----NFASDVIDHWAsvekaGKRSSGPALWWMNGSGKEIKWSFREL 86
Cdd:cd05968 23 FWGEFVKDVGIEWyeppyqtldlsGGKPWAAWFvggrmNIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 87 SEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD----- 161
Cdd:cd05968 98 LYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 ----EVAQEVD-AVAPDCSFLKIKLLVSENSREGWLN----FKALLKEASTIHqCVETESRESAAIYFTSGTSGPPKMAE 232
Cdd:cd05968 177 grevNLKEEADkACAQCPTVEKVVVVRHLGNDFTPAKgrdlSYDEEKETAGDG-AERTESEDPLMIIYTSGTTGKPKGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 233 HSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMN---ILGAFLepwvLGACIFVHL-LPKFDSQTVL-KVLSSYPIN 307
Cdd:cd05968 256 HVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGpwlIFGGLI----LGATMVLYDgAPDHPKADRLwRMVEDHEIT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWK------AKTGLEIREIYGQTET--GLICRVSrTMKV 379
Cdd:cd05968 332 HLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNwlfetvGKGRNPIINYSGGTEIsgGILGNVL-IKPI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 380 KPGYLGTAFAHYDVQVIDEQGNVLPPgKEGDIAIRvKPiWPiGMFSGYVDNPKKTQDNIRG---DFWLMGDRGIKDPEGY 456
Cdd:cd05968 411 KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-AP-WP-GMTRGFWRDEDRYLETYWSrfdNVWVHGDFAYYDEEGY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 457 FHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD--RDQLTKVLQ 534
Cdd:cd05968 487 FYILGRSDDTINVAGK-----RVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVA 561
|
570 580 590
....*....|....*....|....*....|....*..
gi 295789127 535 EHVKSvtaPYKyPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05968 562 DELGK---PLS-PERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
77-570 |
6.44e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 215.57 E-value: 6.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 77 KEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARA 156
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 IVAGDEVAQEVDAVAPDCSFLKIKLLVSENSRE---GWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEH 233
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 234 SHCSLgIKAKMDAASWTGLSTSDIiwtisdtawimNI----------LGAFLEPWV-LGACifVHLLPKFDSQTVLKVLS 302
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDI-----------PLhalplyhcaqLDVFLGPYLyVGAT--NVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPIIYRMLL------QQDLSSykfphLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTETGLICRVSR 375
Cdd:PRK08316 258 AERITSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQTEIAPLATVLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 376 --TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDFWLMGDRGIKDP 453
Cdd:PRK08316 333 peEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRS----PQLM-LGYWDDPEKTAEAFRGGWFHSGDLGVMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 454 EGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrDQLT-KV 532
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGE-----NVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDE 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 295789127 533 LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
80-564 |
7.78e-62 |
|
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: 211.69 E-value: 7.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI-V 158
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIfT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 AGDEVAQEVDAVApdCSFLKIKLLVSENSREGWLNFKALLKEASTIH-----QCVETESRESAAIYFTSGTSGPPKMAEH 233
Cdd:cd05911 89 DPDGLEKVKEAAK--ELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEdedlpPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 234 SHCSLGIKAKMDAASWTGLSTS-DIIWTISDTAWIMNILGAFLEPWvLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA 312
Cdd:cd05911 167 SHRNLIANLSQVQTFLYGNDGSnDVILGFLPLYHIYGLFTTLASLL-NGAT--VIIMPKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 313 PIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTETGLICRVSRTMKVKPGYLGTAFAH 390
Cdd:cd05911 244 PPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 391 YDVQVIDEQGN-VLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:cd05911 324 VEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 SSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDrDQLTKVLQEHVksvtAPYKYPR 548
Cdd:cd05911 399 YKG-----FQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-KEVKDYVAKKV----ASYKQLR 468
|
490
....*....|....*..
gi 295789127 549 K-VEFVLDLPKTVTGKI 564
Cdd:cd05911 469 GgVVFVDEIPKSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
54-579 |
1.00e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 204.81 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 54 WASVEKAGKR-SSGPALWWMngsGKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV 132
Cdd:PRK08314 13 FHNLEVSARRyPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 133 FMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEV------------------DAVAPDC-----SFLKIKLLVSENSRE 189
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPeiavpAWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 190 GWLNFKALLKEASTIHQcVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMN 269
Cdd:PRK08314 168 GVVAWKEALAAGLAPPP-HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA-VGSVLWSNSTPESVVLAVLPLFHVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 270 ILGAFLEPWVLGACIFvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ------DLSSYKfphlhsCFSGGETLL 343
Cdd:PRK08314 246 MVHSMNAPIYAGATVV--LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASpglaerDLSSLR------YIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 344 PETL-ENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwpi 421
Cdd:PRK08314 318 PEAVaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 422 G--MFSGYVDNPKKTQD---NIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVS 495
Cdd:PRK08314 391 GpqVFKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASG-----FKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 496 ETAVISSPDPSRGEVVKAFVVLAPEFLSH-DRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 574
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEARGKtTEEEIIAWAREHM----AAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
....*
gi 295789127 575 KTSGR 579
Cdd:PRK08314 542 ARAAK 546
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
34-571 |
6.17e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 203.35 E-value: 6.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 34 QWGHQEAPAkfnfaSDVIDHWASvekagKRSSGPALWWMngsGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVL 113
Cdd:PRK06178 27 EYPHGERPL-----TEYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 114 PRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKI------KLLVSENS 187
Cdd:PRK06178 91 PNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVivtslaDVLPAEPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 188 R-------------EGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLST 254
Cdd:PRK06178 171 LplpdslraprlaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 255 SDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSYK 328
Cdd:PRK06178 251 DSVFLSFLPEFWIAGENFGLLFPLFSGAT--LVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMdhprfaEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 329 FPhlhSCFSGGETLLPETLENWKAKTGLEIREI-YGQTETGLICRVSRTMKV-------KPGYLGTAFAHYDVQVID-EQ 399
Cdd:PRK06178 329 QV---RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFQDddfdllsQPVFVGLPVPGTEFKICDfET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 400 GNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSG-AYFcry 477
Cdd:PRK06178 406 GELLPLGAEGEIVVRTPSL-----LKGYWNKPEATAEALR-DGWLhTGDIGKIDEQGFLHYLGRRKEMLKVNGmSVF--- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 478 rigPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRDQLTkvLQEHVKSVTAPYKYPrKVEFVLDLP 557
Cdd:PRK06178 477 ---PSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTAAA--LQAWCRENMAVYKVP-EIRIVDALP 547
|
570
....*....|....
gi 295789127 558 KTVTGKIERAKLRA 571
Cdd:PRK06178 548 MTATGKVRKQDLQA 561
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
45-571 |
7.65e-56 |
|
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: 198.69 E-value: 7.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 45 NFASDVIDHWAsveKAGkRSSGPALWWMNGS-GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMI 123
Cdd:cd05967 50 NTCYNALDRHV---EAG-RGDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAIAM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 124 LGCMRTG----LVFmpGTIQmrSSDILYRLQASKARAIVAGD---------------EVAQEVDAVAPDCSFLKIKLLVS 184
Cdd:cd05967 125 LACARIGaihsVVF--GGFA--AKELASRIDDAKPKLIVTAScgiepgkvvpykpllDKALELSGHKPHHVLVLNRPQVP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 185 ENSR--EGWLNFKALLKEASTiHQCVETESRESAAIYFTSGTSGPPKmaehshcslGI----KAKMDAASWT-----GLS 253
Cdd:cd05967 201 ADLTkpGRDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPK---------GVvrdnGGHAVALNWSmrniyGIK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 254 TSDIIWTISDTAWIMN---ILGAflePWVLGA-CIFVHLLPKF--DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---- 323
Cdd:cd05967 271 PGDVWWAASDVGWVVGhsyIVYG---PLLHGAtTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgk 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 324 -LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG----LICRVSRTMKVKPGYLGTAFAHYDVQVIDE 398
Cdd:cd05967 348 yIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 399 QGNVLPPGKEGDIAIRVkPIwPIGMFSGYVDNPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGayfc 475
Cdd:cd05967 428 DGEPVGPNELGNIVIKL-PL-PPGCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAG---- 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 476 rYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLD 555
Cdd:cd05967 502 -HRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKR 579
|
570
....*....|....*.
gi 295789127 556 LPKTVTGKIERAKLRA 571
Cdd:cd05967 580 LPKTRSGKILRRTLRK 595
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
81-570 |
1.15e-55 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 195.86 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 160
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEVAQEVDAVAPDCSFLKIKLLVSEnsREGWLnfKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGI 240
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETLDAD--GTGSL--LEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 241 KAKMDAASWTglstsdiiWTISDTAW----IMNILGAFLEPWVL----GACIFvhlLPKFDSQTVLKVLssyPINT-LVG 311
Cdd:PRK07514 184 NALTLVDYWR--------FTPDDVLIhalpIFHTHGLFVATNVAllagASMIF---LPKFDPDAVLALM---PRATvMMG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 312 APIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLIC-------RVsrtmkvkPGY 383
Cdd:PRK07514 250 VPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTsnpydgeRR-------AGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 LGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHF 459
Cdd:PRK07514 323 VGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 460 IGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLTKVLQEHVks 539
Cdd:PRK07514 396 VGRGKDLIISGG-----YNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA-ALDEAAILAALKGRL-- 467
|
490 500 510
....*....|....*....|....*....|.
gi 295789127 540 vtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK07514 468 --ARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
82-571 |
2.00e-55 |
|
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: 193.37 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:cd05903 3 TYSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDAVAPDcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHCSLGIK 241
Cdd:cd05903 82 RFRQFDPAAMPD----------------------------------------AVALLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA-PIIYRMLL 320
Cdd:cd05903 122 IRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET-GLICRVSRTMKVKPGYL-GTAFAHYDVQVIDE 398
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 399 QGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryR 478
Cdd:cd05903 279 TGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE-----N 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 479 IGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEHvksVTAPYKYPRKVEFVLDLPK 558
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFDELVAYLDRQ---GVAKQYWPERLVHVDDLPR 424
|
490
....*....|...
gi 295789127 559 TVTGKIERAKLRA 571
Cdd:cd05903 425 TPSGKVQKFRLRE 437
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
81-575 |
2.80e-55 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 195.74 E-value: 2.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 160
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEVAQ-----EVDAVAPDCSFLKIKLLVSENSRE-GWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHS 234
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVDKLAPAtSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 235 HCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA-P 313
Cdd:PRK06087 209 HNNI-LASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR--SVLLDIFTPDACLALLEQQRCTCMLGAtP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 314 IIYRMLLQQDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRV------SRTMkvkpGYLGTA 387
Cdd:PRK06087 286 FIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSPHAVVnlddplSRFM----HTDGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 388 FAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDI 466
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGEEASR-GP----NVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 467 INSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQLTKVLQEhvKSVtAPYKY 546
Cdd:PRK06087 436 IVRGGE-----NISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSR--KRV-AKYKY 507
|
490 500
....*....|....*....|....*....
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLRaKEWK 575
Cdd:PRK06087 508 PEHIVVIDKLPRTASGKIQKFLLR-KDIM 535
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
67-580 |
2.25e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 189.81 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 67 PALWWMNGSgkeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWL-----MILGCMRTGLVFMpGTIQmr 141
Cdd:PRK06188 29 PALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMaigaaQLAGLRRTALHPL-GSLD-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 142 ssDILYRLQASKARAIVAGD----EVAQEVDAVAPdcsflKIKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAA 217
Cdd:PRK06188 100 --DHAYVLEDAGISTLIVDPapfvERALALLARVP-----SLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASW------TGLSTSdiiwTISDTAwimnilGAFLEPWVL-GAciFVHLLP 290
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWewpadpRFLMCT----PLSHAG------GAFFLPTLLrGG--TVIVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 291 KFDSQTVLKVLSSYPIN-TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL 369
Cdd:PRK06188 241 KFDPAEVLRAIEEQRITaTFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 370 ICRVSRT---MKVKPGYLGTA---FAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDfW 443
Cdd:PRK06188 321 VITYLRKrdhDPDDPKRLTSCgrpTPGLRVALLDEDGREVAQGEVGEICVRG----PLVM-DGYWNRPEETAEAFRDG-W 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 444 L-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfl 522
Cdd:PRK06188 395 LhTGDVAREDEDGFYYIVDRKKDMIVTGG-----FNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-- 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 523 sHDRDqlTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 580
Cdd:PRK06188 468 -AAVD--AAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRA 522
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
42-571 |
3.12e-53 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 191.24 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 42 AKFNFASDVIDHWasVEKAGKRssgPALWWM-NGSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWW 120
Cdd:cd05966 50 GKLNISYNCLDRH--LKERGDK---VAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 121 LMILGCMRTGLV-------FMPGTIQMRSSDilyrlqaSKARAIVAGDEV---------AQEVDAVAPDCSFLKiKLLVS 184
Cdd:cd05966 124 IAMLACARIGAVhsvvfagFSAESLADRIND-------AQCKLVITADGGyrggkviplKEIVDEALEKCPSVE-KVLVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 185 ENS---------REGWLNfkALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCS--LGIKAKMDaasWT-GL 252
Cdd:cd05966 196 KRTggevpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGylLYAATTFK---YVfDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 253 STSDIIWTISDTAWIMN----ILGaflePWVLGACIFVH----LLPKFDS--QTVLKvlssYPINTLVGAPIIYRMLLQQ 322
Cdd:cd05966 271 HPDDIYWCTADIGWITGhsyiVYG----PLANGATTVMFegtpTYPDPGRywDIVEK----HKVTIFYTAPTAIRALMKF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 323 --------DLSSYKfpHLHSCfsgGETLLPETLENWKAKTGLE---IREIYGQTETG--LICRVSRTMKVKPGYLGTAFA 389
Cdd:cd05966 343 gdewvkkhDLSSLR--VLGSV---GEPINPEAWMWYYEVIGKErcpIVDTWWQTETGgiMITPLPGATPLKPGSATRPFF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 390 HYDVQVIDEQGNVLPPGKEGDIAIRvKPiWPiGMFSGYVDNPKKTQDNIRGDFW---LMGDRGIKDPEGYFHFIGRSDDI 466
Cdd:cd05966 418 GIEPAILDEEGNEVEGEVEGYLVIK-RP-WP-GMARTIYGDHERYEDTYFSKFPgyyFTGDGARRDEDGYYWITGRVDDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 467 INSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKY 546
Cdd:cd05966 495 INVSG-----HRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIAT 567
|
570 580
....*....|....*....|....*
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05966 568 PDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
58-570 |
1.13e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 187.97 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 58 EKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 137
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 138 IQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSF-LKIKLLVSENSRE--GWLNFKALL-KEASTIHQCVETESR 213
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPAddGVSSFTQLKaQQPATLCYAPPLSTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 214 ESAAIYFTSGTSGPPKMAEHSHCSL---GIkakmdAASW-TGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACiFVhLL 289
Cdd:PRK08008 174 DTAEILFTSGTTSRPKGVVITHYNLrfaGY-----YSAWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGAT-FV-LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 PKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPH--------LHscfsggetLLPETLENWKAKTGLEIREI 361
Cdd:PRK08008 247 EKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclrevmfyLN--------LSDQEKDAFEERFGVRLLTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 362 YGQTET--GLICRvsrtmkvKPG------YLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIgmFSGYVDNPKK 433
Cdd:PRK08008 319 YGMTETivGIIGD-------RPGdkrrwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 434 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 512
Cdd:PRK08008 390 TAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGE-----NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 513 AFVVLAP-------EFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK08008 465 AFVVLNEgetlseeEFFAFCEQNMAK------------FKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-571 |
7.99e-52 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 186.12 E-value: 7.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGW-LNFKAL-LKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 235
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 CSLGIKAKMDAASwTGLSTSDIIWTiSDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSY--PINTLVGAp 313
Cdd:PRK06155 203 AQFYWWGRNSAED-LEIGADDVLYT-TLPLFHTNALNAFFQALLAGAT--YVLEPRFSASGFWPAVRRHgaTVTYLLGA- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 314 iIYRMLLQQDLSSYKFPH-LHSCFSGGETllPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKvKPGYLGTAFAHYD 392
Cdd:PRK06155 278 -MVSILLSQPARESDRAHrVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVIDEQGNVLPPGKEGDIAIRVKPiwPIGMFSGYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSG 471
Cdd:PRK06155 354 ARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKDAIRRRG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 472 AyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP----EFLShdrdqltkvLQEHVKSVTAPYKYP 547
Cdd:PRK06155 431 E-----NISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgtalEPVA---------LVRHCEPRLAYFAVP 496
|
490 500
....*....|....*....|....
gi 295789127 548 RKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK06155 497 RYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
81-573 |
2.85e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 186.31 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFmPGTIQMRSSDILYRLQASKARAIVA- 159
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 ----GDEVAQEVDAVAPDCSFLK-----------------IKLLVSENSREGWLNFKALLKEASTIHQCVETESRES--A 216
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDdvA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 217 AIYFTSGTSGPPKMAEHSHcslgikAKMDAASWTGLSTSDIiwTISDTawIMNILGAFLepwvLGACIFVHLLPKFDSQT 296
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTH------GNEVANAWLGALLLGL--GPGDT--VFCGLPLFH----VNALLVTGLAPLARGAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VL-----------------KVLSSYPINTLVGAPIIYRMLLQQ-----DLSSYKFphlhsCFSGGETLLPETLENWKAKT 354
Cdd:PRK07529 283 VVlatpqgyrgpgvianfwKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY-----ALCGAAPLPVEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 355 GLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYDVQVI--DEQGNVL---PPGKEGDIAIRvKPiwpiGMFSGYV 428
Cdd:PRK07529 358 GVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GP----NVFSGYL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 429 dNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSR 507
Cdd:PRK07529 433 -EAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGG-----HNIDPAAIEEALLRHPAVALAAAVGRPDAHA 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 508 GEVVKAFVVLAPEfLSHDRDQLTKVLQEHVKSVTApykYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK07529 507 GELPVAYVQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
76-575 |
1.04e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 183.70 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:PRK06710 47 GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPDCSFLKI------------KLLVSENSREGWLNFKALLKEASTIH--QCVETE---------- 211
Cdd:PRK06710 124 VILCLDLVFPRVTNVQSATKIEHVivtriadflpfpKNLLYPFVQKKQSNLVVKVSESETIHlwNSVEKEvntgvevpcd 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 212 -SRESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtglstsdIIWTISDTAWIMNILGAflEPWVLGACIFVH--- 287
Cdd:PRK06710 204 pENDLALLQYTGGTTGFPKGVMLTHKNL------------------VSNTLMGVQWLYNCKEG--EEVVLGVLPFFHvyg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 288 ----------------LLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENW 350
Cdd:PRK06710 264 mtavmnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 351 KAKTGLEIREIYGQTETGLICRVSRTMKVK-PGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYV 428
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 429 DNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSR 507
Cdd:PRK06710 419 NKPEETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKDMIVASG-----FNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 508 GEVVKAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 575
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEEE-----LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
72-580 |
2.15e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 181.26 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 72 MNGSGKEikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQA 151
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 152 SKARAIV---AGDEVAQEVDAVAP-DCSFLkiklLVSENSREGWLNFKALLKEASTIHqcVETESRESAAIYfTSGTSGP 227
Cdd:PRK08276 82 SGAKVLIvsaALADTAAELAAELPaGVPLL----LVVAGPVPGFRSYEEALAAQPDTP--IADETAGADMLY-SSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 228 PKmaehshcslGIK----------------AKMDAASWTG-----LSTSDIIWTiSDTAWIMNILgaflepwVLGacIFV 286
Cdd:PRK08276 155 PK---------GIKrplpgldpdeapgmmlALLGFGMYGGpdsvyLSPAPLYHT-APLRFGMSAL-------ALG--GTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 287 HLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RML-LQQ------DLSSYKFphlhsCFSGGETLLPET----LENWkakt 354
Cdd:PRK08276 216 VVMEKFDAEEALALIERYRVTHSQLVPTMFvRMLkLPEevraryDVSSLRV-----AIHAAAPCPVEVkramIDWW---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 355 GLEIREIYGQTETGLICRV-SRTMKVKPGYLGTAfAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMFSgYVDNPKK 433
Cdd:PRK08276 287 GPIIHEYYASSEGGGVTVItSEDWLAHPGSVGKA-VLGEVRILDEDGNELPPGEIGTVYFEM----DGYPFE-YHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 434 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 512
Cdd:PRK08276 361 TAAARNPHGWVtVGDVGYLDEDGYLYLTDRKSDMIISGGV-----NIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 513 AFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 580
Cdd:PRK08276 436 AVVQPADGAD--AGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-569 |
3.84e-50 |
|
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: 179.26 E-value: 3.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 159
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSLG 239
Cdd:cd05930 90 --------------------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 --IKAKMDAaswTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACifVHLLPK---FDSQTVLKVLSSYPINTLVGAPI 314
Cdd:cd05930 120 nlLLWMQEA---YPLTPGDRVLQFTSFSFDVSVWEIFG-ALLAGAT--LVVLPEevrKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 315 IYRMLLQqDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLICRVSRTMKVKPGY----LGTAFA 389
Cdd:cd05930 194 LLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYRVPPDDEEDgrvpIGRPIP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 390 HYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGDFWLM---GDRGIKDPEGYFHFIGR 462
Cdd:cd05930 273 NTRVYVLDENLRPVPPGVPGELYIG-----GAGLARGYLNRPELTAerfvPNPFGPGERMyrtGDLVRWLPDGNLEFLGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 463 SDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdrDQLTKVLQEHVKSVTA 542
Cdd:cd05930 348 IDDQVKIRG-----YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG-----ELDEEELRAHLAERLP 417
|
490 500
....*....|....*....|....*..
gi 295789127 543 PYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
78-571 |
1.34e-49 |
|
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: 178.65 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAgdevaqevdavapDCSFLKIKLLVSENSREGWlnfkallkeastihQCVETEsRESAAIYFTSGTSGPPKMAEHSHCS 237
Cdd:cd12118 106 FV-------------DREFEYEDLLAEGDPDFEW--------------IPPADE-WDPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 LGIKAKMDAASWTGLSTSDIIWTISD---TAWIMnilgaflePWVLGACIFVHL-LPKFDSQTVLKVLSSYPINTLVGAP 313
Cdd:cd12118 158 AYLNALANILEWEMKQHPVYLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 314 IIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTET---GLICRVSRT-----------MK 378
Cdd:cd12118 230 TVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVCAWKPEwdelpteerarLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 379 VKPG--YLGTAfahyDVQVIDEQGNVLPP--GKE-GDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGDFWLMGDRGIK 451
Cdd:cd12118 309 ARQGvrYVGLE----EVDVLDPETMKPVPrdGKTiGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 452 DPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLTK 531
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGE-----NISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-KVTEEEIIA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 295789127 532 VLQEHVksvtAPYKYPRKVEFVlDLPKTVTGKIERAKLRA 571
Cdd:cd12118 452 FCREHL----AGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
78-570 |
4.92e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 178.81 E-value: 4.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR-- 155
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 ----------------AIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQcVETESRESA--- 216
Cdd:PRK12583 122 icadafktsdyhamlqELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAWHELQARGETVSR-EALAERQASldr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 217 ----AIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASwTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIfvhLLPK- 291
Cdd:PRK12583 201 ddpiNIQYTSGTTGFPKGATLSHHNILNNGYFVAES-LGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACL---VYPNe 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 292 -FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTETG 368
Cdd:PRK12583 277 aFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 369 ---LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL- 444
Cdd:PRK12583 357 pvsLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV-----MKGYWNNPEATAESIDEDGWMh 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP-EFLS 523
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIRGGE-----NIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPgHAAS 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 295789127 524 HDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK12583 507 EEE------LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
53-572 |
1.12e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 177.66 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 53 HWAS--VEKAGKRSSGPALWWMngsGKEIKWsfRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTG 130
Cdd:PRK07786 18 NWVNqlARHALMQPDAPALRFL---GNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 131 LVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVET 210
Cdd:PRK07786 92 AIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 211 ESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLP 290
Cdd:PRK07786 172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTN-GADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 291 KFDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSykfphlhSCFSGGETLLPETLENWKAKT--GLEIREIY 362
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAVCaeqqarPRDLAL-------RVLSWGAAPASDTLLRQMAATfpEAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 363 GQTETGLI-CRVSRTMKV-KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRG 440
Cdd:PRK07786 324 GQTEMSPVtCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEATAEAFAG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 441 DFWLMGDRGIKDPEGYFHFIGRSDDIINSSGA-YFCryrigpSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP 519
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGEnIYC------AEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 295789127 520 EFLSHDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PRK07786 473 DDAALTLEDLAEFLTDRL----ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
73-570 |
3.54e-48 |
|
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: 175.51 E-value: 3.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 73 NGSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVL---PRIPEWWLMILGcmrTGLVFMPGTIQMRSSDILYRL 149
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 150 QASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSR------EGWLNFKALLKEASTIHQCVETESRESAAIYFTSG 223
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 224 TSGPPKMAEHSHCSLGIKA-KMDAASWTGLSTSDIIWTISD----TAWIMnilgAFLEPWVlGACifvHLLP--KFDSQT 296
Cdd:cd12119 174 TTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPmfhvNAWGL----PYAAAMV-GAK---LVLPgpYLDPAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRVSR 375
Cdd:cd12119 246 LAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAV-PRSLIEAFEERGVRVIHAWGMTETSPLGTVAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 376 TMKVKPGYLGTAFAHY-----------DVQVIDEQGNVLP-PGKE-GDIAIRvKPiWPIGmfsGYVDNPKKTQDNIRGDF 442
Cdd:cd12119 325 PPSEHSNLSEDEQLALrakqgrpvpgvELRIVDDDGRELPwDGKAvGELQVR-GP-WVTK---SYYKNDEESEALTEDGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 443 WLMGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfl 522
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEW-----ISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG-- 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 295789127 523 sHDRDQltKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd12119 473 -ATVTA--EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-570 |
2.28e-47 |
|
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: 171.85 E-value: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 102 GLHRGDRVAVVLPRIPEW-WLM---ILGCMRTGLVFMPGTIQMRSSDILYrLQASKARAIVAGDE-VAQEVDAVAPDCSF 176
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELSfavAYAGGRLGLVFVPLNPTLKESVLRY-LVADAGGRIVLADAgAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 177 LKIKLLVsensrEGWLNFKALLkeastihQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMdAASWTGLSTSD 256
Cdd:cd05922 93 PGTVLDA-----DGIRAARASA-------PAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS-IAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 257 IIWTISDTAW---IMNILGAFLEpwvlGACIFVHLLPKFDsQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLH 333
Cdd:cd05922 160 RALTVLPLSYdygLSVLNTHLLR----GATLVLTNDGVLD-DAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 334 SCFSGGETLLPETLENWKAK-TGLEIREIYGQTETgliCRVSRTM-----KVKPGYLGTAFAHYDVQVIDEQGNVLPPGK 407
Cdd:cd05922 235 YLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEA---TRRMTYLpperiLEKPGSIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 408 EGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVEN 486
Cdd:cd05922 312 PGEIVHRG----PNVM-KGYWNDPPYRRKEGRGGGVLhTGDLARRDEDGFLFIVGRRDRMIKLFG-----NRISPTEIEA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 487 ALMEHPAVSETAVISSPDPSrGEVVKAFVVLAPEFLSHD-RDQLTKVLqehvksvtAPYKYPRKVEFVLDLPKTVTGKIE 565
Cdd:cd05922 382 AARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDvLRSLAERL--------PPYKVPATVRVVDELPLTASGKVD 452
|
....*
gi 295789127 566 RAKLR 570
Cdd:cd05922 453 YAALR 457
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
53-569 |
1.83e-46 |
|
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: 170.49 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 53 HWASVEKAGKRSSGPALwwMNGS-GKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGL 131
Cdd:cd05904 8 DSVSFLFASAHPSRPAL--IDAAtGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 132 VFMPGTIQMRSSDILYRLQASKARAIVAgdeVAQEVDAVAPdcsfLKIKLLVSENSREGWLNFKALLKEASTiHQCVETE 211
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFT---TAELAEKLAS----LALPVVLLDSAEFDSLSFSDLLFEADE-AEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 212 SRES--AAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDI----------IWTISdtaWIMNILGAflepwv 279
Cdd:cd05904 155 IKQDdvAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDvflcvlpmfhIYGLS---SFALGLLR------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 280 LGACIFVhlLPKFDSQTVLKVLSSYPINTL-VGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAK-TGLE 357
Cdd:cd05904 226 LGATVVV--MPRFDLEELLAAIERYKVTHLpVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 358 IREIYGQTETGLICRVSRT---MKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKK 433
Cdd:cd05904 304 LGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 434 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 512
Cdd:cd05904 379 TAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKG-----FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPM 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 513 AFVVLAPE-FLSHDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05904 454 AFVVRKPGsSLTEDE------IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
48-571 |
8.97e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 169.80 E-value: 8.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 48 SDVIDHwaSVEKAGKRssgPALWWMngsGKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCM 127
Cdd:PRK05605 35 VDLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 128 RTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSF-------------------LKIKLLVSENSR 188
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLetivsvnmiaampllqrlaLRLPIPALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 189 E-------GWLNFKALLKEA----STIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDi 257
Cdd:PRK05605 184 AaltgpapGTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGP- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 258 iwtisDT---------AWIMNILGAFlEPWVLGACIfvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ------ 322
Cdd:PRK05605 263 -----ERvlaalpmfhAYGLTLCLTL-AVSIGGELV---LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 323 DLSSYKFphlhsCFSGGETLLPETLENWKAKTGLEIREIYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQ-- 399
Cdd:PRK05605 334 DLSGVRN-----AFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 400 GNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRI 479
Cdd:PRK05605 409 DETMPDGEEGELLVRGPQV-----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGG-----FNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 480 GPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKT 559
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEG----LRAYCREHLTRYKVPRRFYHVDELPRD 553
|
570
....*....|..
gi 295789127 560 VTGKIERAKLRA 571
Cdd:PRK05605 554 QLGKVRRREVRE 565
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
76-569 |
6.25e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 166.19 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPdcsflkikllVSENSREGWLNFKALLKEASTIHQCVETESReSAAIYFTSGTSGPPKMAEHSH 235
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKIDNFVEKNESA-SFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 CSLGIKAKMDAASwTGLSTSDIIWTISDTAWIMNIlGAFLEP-WVLGACIFVHllPKFDSQTVLKVLSSYPINTLVGAPI 314
Cdd:PRK06839 172 ENMFWNALNNTFA-IDLTMHDRSIVLLPLFHIGGI-GLFAFPtLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 315 IYRMLLQQ-DLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETG--LICRVSRTMKVKPGYLGTAFAHY 391
Cdd:PRK06839 248 IHQALINCsKFETTNLQSVRWFYNGGAPC-PEELMREFIDRGFLFGQGFGMTETSptVFMLSEEDARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 392 DVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSG 471
Cdd:PRK06839 327 DYELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 472 AyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVE 551
Cdd:PRK06839 402 E-----NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD-----VIEHCRLFLAKYKIPKEIV 471
|
490
....*....|....*...
gi 295789127 552 FVLDLPKTVTGKIERAKL 569
Cdd:PRK06839 472 FLKELPKNATGKIQKAQL 489
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
76-578 |
8.95e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 166.86 E-value: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:PRK05677 47 GKTL--TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNF-KALLKEASTIHQCVET 210
Cdd:PRK05677 125 ALVCLANMAHLAEKVLPKTgvkhvivtevadmlPPLKrllinavvkhVKKMVPAYHLPQAVKFnDALAKGAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 211 ESRESAAIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAASWTGLSTSDI------IWTISDTAWIMNILGAflepwv 279
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlQCRALMGSNLNEGCEILIAplplyhIYAFTFHCMAMMLIGN------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 280 lgacifvH--LLPK-FDSQTVLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 355
Cdd:PRK05677 279 -------HniLISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 356 LEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNPKKTQ 435
Cdd:PRK05677 352 CAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK----GPQVM-KGYWQRPEATD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 436 DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAF 514
Cdd:PRK05677 427 EILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSG-----FNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVF 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 515 VVLAPeflshdRDQLTK-VLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 578
Cdd:PRK05677 502 VVVKP------GETLTKeQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
217-566 |
9.20e-45 |
|
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: 161.67 E-value: 9.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 217 AIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIM--NILGAFLEpwvLGACIFVhlLPKFDS 294
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNL-IAANLQLIHAMGLTEADVYLNMLPLFHIAglNLALATFH---AGGANVV--MEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 295 QTVLKVLSSYPInTLVG--APIIYRMLLQQDLSSYKFPHLhSCFSGGETllPETLENWKAKTGLEIREIYGQTET-GLIC 371
Cdd:cd17637 78 AEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSL-RHVLGLDA--PETIQRFEETTGATFWSLYGQTETsGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 372 rVSRTMKvKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIK 451
Cdd:cd17637 154 -LSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVFQGYWNLPELTAYTFRNGWHHTGDLGRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 452 DPEGYFHFIGRS--DDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQL 529
Cdd:cd17637 227 DEDGYLWYAGRKpeKELIKPGGE-----NVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA-TLTADEL 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 295789127 530 TkvlqEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:cd17637 301 I----EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
82-570 |
8.28e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 163.26 E-value: 8.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG- 160
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 --DEVAQEVDAVAPdcsflkikLLVSENSR-EGWLNFKALLKEASTihqcVETESRESAAIYFTSGTSGPPK-----MAE 232
Cdd:PRK13390 105 alDGLAAKVGADLP--------LRLSFGGEiDGFGSFEAALAGAGP----RLTEQPCGAVMLYSSGTTGFPKgiqpdLPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 233 HSHCSLGIKAKMDAASWTGLSTSDIIWTISDtawimnILGAFLEPWvlgaCIFVHLL-------PKFDSQTVLKVLSSYP 305
Cdd:PRK13390 173 RDVDAPGDPIVAIARAFYDISESDIYYSSAP------IYHAAPLRW----CSMVHALggtvvlaKRFDAQATLGHVERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 306 INTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETL---LPETLENWkakTGLEIREIYGQTET-GLICRVSRTMK 378
Cdd:PRK13390 243 ITVTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 379 VKPGYLGTAFAHyDVQVIDEQGNVLPPGKEGDIAIRvKPIWPigmFSgYVDNPKKTQD--NIRGDFWL-MGDRGIKDPEG 455
Cdd:PRK13390 320 AHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFE-RDRLP---FR-YLNDPEKTAAaqHPAHPFWTtVGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 456 YFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQE 535
Cdd:PRK13390 394 YLYLADRKSFMIISGGV-----NIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI--RGSDELARELID 466
|
490 500 510
....*....|....*....|....*....|....*
gi 295789127 536 HVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK13390 467 YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
82-571 |
2.42e-43 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 164.16 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV-------FmpgtiqmrSSDILY-RLQASK 153
Cdd:PRK00174 100 TYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggF--------SAEALAdRIIDAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 154 ARAIVAGDE-------VA--QEVDAVAPDCSFLKiKLLV---------SENSREGWLNfkALLKEASTIHQCVETESRES 215
Cdd:PRK00174 171 AKLVITADEgvrggkpIPlkANVDEALANCPSVE-KVIVvrrtggdvdWVEGRDLWWH--ELVAGASDECEPEPMDAEDP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHS------HCSLGIKAKMDaaswtgLSTSDIIWTISDTAWIMN----ILGaflePWVLGACIF 285
Cdd:PRK00174 248 LFILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD------YKDGDVYWCTADVGWVTGhsyiVYG----PLANGATTL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 286 VHL-LPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQ--------DLSSYKFphLHSCfsgGETLLPETLEnWKAKT- 354
Cdd:PRK00174 318 MFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKEgdehpkkyDLSSLRL--LGSV---GEPINPEAWE-WYYKVv 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 355 GLE---IREIYGQTETG--LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiWPiGMFSGYVD 429
Cdd:PRK00174 392 GGErcpIVDTWWQTETGgiMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIK-DP-WP-GMMRTIYG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 430 NPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPS 506
Cdd:PRK00174 469 DHERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSG-----HRLGTAEIESALVAHPKVAEAAVVGRPDDI 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295789127 507 RGEVVKAFVVL----APEflshdrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK00174 544 KGQGIYAFVTLkggeEPS------DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
80-573 |
4.88e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 160.51 E-value: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTG--LVFmpgtIQMRSS--DILYRLQASKAR 155
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGavAVL----LNTRLSreELLWQLDDAEVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVdavapdcsFLKIKLLVSEnsregwlnfkaLLKEASTIHQCVETESRESAA-IYFTSGTSGPPK----- 229
Cdd:PRK03640 102 CLITDDDFEAKL--------IPGISVKFAE-----------LMNGPKEEAEIQEEFDLDEVAtIMYTSGTTGKPKgviqt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 ------MAEHSHCSLGIKAKmDaaSW---------TGLSTsdiiwtisdtawIMN--ILGaflepwvlgacIFVHLLPKF 292
Cdd:PRK03640 163 ygnhwwSAVGSALNLGLTED-D--CWlaavpifhiSGLSI------------LMRsvIYG-----------MRVVLVEKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 293 DSQTVLKVLSSYPINTLVGAPIiyrmLLQQDLSSYKFPHLHSCF-----SGGETLLPeTLENWKAKtGLEIREIYGQTET 367
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVST----MLQRLLERLGEGTYPSSFrcmllGGGPAPKP-LLEQCKEK-GIPVYQSYGMTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 GlicrvSRTMKVKPGY----LGTAF-AHYDVQV-IDEQGNVLPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRgD 441
Cdd:PRK03640 291 A-----SQIVTLSPEDaltkLGSAGkPLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNREDATRETFQ-D 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 442 FWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPE 520
Cdd:PRK03640 360 GWFkTGDIGYLDEEGFLYVLDRRSDLIISGGE-----NIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 295789127 521 FlshDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK03640 435 V---TEEELRHFCEEKL----AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
79-579 |
1.14e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 159.59 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 79 IKWSFRELSEASKQTANVLSGAcGLHRGDRVAVvLPRIPEWWLMI-LGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAqevdAVAPDCsflkikllvsensregwLNFKALLKEAstihQCVETESRESAA------IYFTSGTSGPPKMA 231
Cdd:PRK09088 99 LGDDAVA----AGRTDV-----------------EDLAAFIASA----DALEPADTPSIPpervslILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 -------EHSHCSLGIKAKMDAASwtglstsdiiwTISDTAWIMNILGAF--LEPWVL-GACIFVHllPKFDSQTVLKVL 301
Cdd:PRK09088 154 mlsernlQQTAHNFGVLGRVDAHS-----------SFLCDAPMFHIIGLItsVRPVLAvGGSILVS--NGFEPKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 302 S--SYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETGLICRVSRTMK 378
Cdd:PRK09088 221 GdpALGITHYFCVPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 379 V---KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 454
Cdd:PRK09088 300 ViraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNL-----SPGYWRRPQATARAFTGDGWFrTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 455 GYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLTKVLQ 534
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGE-----NVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-----APLDLERIR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 295789127 535 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRakEWKTSGR 579
Cdd:PRK09088 445 SHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR--DALAAGR 487
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-570 |
1.68e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 155.90 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 IYFTSGTSGPPKMAEHSHCSLgikakMDAASWTGLStsdIIWTISDTAWIMN--------ILGAFLEPWVLGACIFVHll 289
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI-----VNNGYFIGER---LGLTEQDRLCIPVplfhcfgsVLGVLACLTHGATMVFPS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 PKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTET 367
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 GLICRVSRT---MKVKPGYLGTAFAHYDVQVIDEQGNVLPP-GKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFW 443
Cdd:cd05917 157 SPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 444 L-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFL 522
Cdd:cd05917 232 LhTGDLAVMDEDGYCRIVGRIKDMIIRGGE-----NIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 295789127 523 SHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05917 307 LTEED-----IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
82-573 |
4.46e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 159.32 E-value: 4.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLsGACGLHRGDRVAVvLPRIPEWWLMILGC----------MRTGlvFMPGTIQmrssDILYRLqa 151
Cdd:PRK07788 76 TYAELDEQSNALARGL-LALGVRAGDGVAV-LARNHRGFVLALYAagkvgariilLNTG--FSGPQLA----EVAARE-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 152 sKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSEN---SREGWLNFKALLKEASTihQCVETESRESAAIYFTSGTSGPP 228
Cdd:PRK07788 146 -GVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSST--APLPKPPKPGGIVILTSGTTGTP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 229 KMAEHSHCSLgikakmdAASWTGLsTSDIIW----TISDTAWIMNILG--AFLEPWVLGACIFVHllPKFDSQTVLKVLS 302
Cdd:PRK07788 223 KGAPRPEPSP-------LAPLAGL-LSRVPFrageTTLLPAPMFHATGwaHLTLAMALGSTVVLR--RRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPI-IYRML--LQQ-----DLSSYKFphlhsCFSGGETLLPETLENWKAKTGLEIREIYGQTETGlICRVS 374
Cdd:PRK07788 293 KHKATALVVVPVmLSRILdlGPEvlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVA-FATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 375 R--TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwpiGM-FSGYVDNPKKtqDNIRGdfwLM--GDRG 449
Cdd:PRK07788 367 TpeDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 450 IKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRDQl 529
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGE-----NVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG---AALDE- 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 295789127 530 tKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK07788 507 -DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
82-573 |
6.00e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 159.06 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNFKALLKEASTIhQCV--ETESRES 215
Cdd:PRK08974 130 NFAHTLEKVVFKTpvkhviltrmgdqlSTAKgtlvnfvvkyIKRLVPKYHLPDAISFRSALHKGRRM-QYVkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSlgIKAKMDAASW--------------TGLSTSDIIwtisdtAWIMNILgAFLEpwvLG 281
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN--MLANLEQAKAaygpllhpgkelvvTALPLYHIF------ALTVNCL-LFIE---LG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 282 ACIFVHLLPKfDSQTVLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 360
Cdd:PRK08974 277 GQNLLITNPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNPKKTQDNIR 439
Cdd:PRK08974 356 GYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK----GPQVM-LGYWQRPEATDEVIK 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 440 gDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 518
Cdd:PRK08974 431 -DGWLaTGDIAVMDEEGFLRIVDRKKDMILVSG-----FNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 519 PEFLShdRDQLTKVLQEHVKSvtapYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK08974 505 DPSLT--EEELITHCRRHLTG----YKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
76-570 |
9.91e-42 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 158.26 E-value: 9.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:PRK07059 46 GKAI--TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPDCS---------------------FL--KIKLLVSENSREGWLNFKALLKE-ASTIHQCVETE 211
Cdd:PRK07059 123 AIVVLENFATTVQQVLAKTAvkhvvvasmgdllgfkghivnFVvrRVKKMVPAWSLPGHVRFNDALAEgARQTFKPVKLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 212 SRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGlstsdiiwtisdtawimnilGAFLEPWVLGACIFVHLLPK 291
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNI-VANVLQMEAWLQ--------------------PAFEKKPRPDQLNFVCALPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 292 F--------------------------DSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLP 344
Cdd:PRK07059 262 YhifaltvcgllgmrtggrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 345 ETLENWKAKTGLEIREIYGQTETGLICRVSR-TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGM 423
Cdd:PRK07059 342 PVAERWLEMTGCPITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR----GPQVM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 424 fSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGayFCRYrigPSEVENALMEHPAVSETAVISS 502
Cdd:PRK07059 418 -AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSG--FNVY---PNEIEEVVASHPGVLEVAAVGV 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295789127 503 PDPSRGEVVKAFVV------LAPEFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK07059 492 PDEHSGEAVKLFVVkkdpalTEEDVKAFCKERLTN------------YKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
76-570 |
3.56e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 156.96 E-value: 3.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:PRK08751 48 GKTI--TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNFKALLKEASTiHQC--VE 209
Cdd:PRK08751 126 VLVVIDNFGTTVQQVIADTpvkqvittglgdmlGFPKaalvnfvvkyVKKLVPEYRINGAIRFREALALGRK-HSMptLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 210 TESRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTS-----DIIWTISDTAWIMNILGAFLEPWVLGACi 284
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNL-VANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKIGGC- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 285 fVHLL--PKfDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSYKFphlhsCFSGGETLLPETLENWKAKTGL 356
Cdd:PRK08751 283 -NHLIsnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKM-----TLGGGMAVQRSVAERWKQVTGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 357 EIREIYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQ 435
Cdd:PRK08751 356 TLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV-----MKGYWKRPEETA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 436 DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAF 514
Cdd:PRK08751 431 KVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSG-----FNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVV 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 515 VVLAPEFLSHDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK08751 506 IVKKDPALTAED------VKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
80-571 |
5.70e-41 |
|
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: 153.27 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKaraiVA 159
Cdd:cd05912 1 SYTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD----VK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GDEVAqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesresaAIYFTSGTSGPPKmaehshcslG 239
Cdd:cd05912 76 LDDIA----------------------------------------------------TIMYTSGTTGKPK---------G 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKAKMDAASWTGLSTSDIIWTISDTAW-----IMNI--LGAFLEPWVLGacIFVHLLPKFDSQTVLKVLSSYPINTLVGA 312
Cdd:cd05912 95 VQQTFGNHWWSAIGSALNLGLTEDDNWlcalpLFHIsgLSILMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 313 PIIYRMLLQQDLSSYKfPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETgliCRVSRTMK-----VKPGYLGTA 387
Cdd:cd05912 173 PTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTET---CSQIVTLSpedalNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 388 FAHYDVQVIDEQGnvlPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDII 467
Cdd:cd05912 248 LFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 468 NSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshDRDQLTKVLQEHVksvtAPYKYP 547
Cdd:cd05912 320 ISGGE-----NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVP 387
|
490 500
....*....|....*....|....
gi 295789127 548 RKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05912 388 KKIYFVDELPRTASGKLLRHELKQ 411
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
82-499 |
7.90e-41 |
|
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: 152.80 E-value: 7.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIqmrssDILY---RLQA----SKA 154
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP--L-----DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSregwlnfkallkEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHS 234
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDD------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 235 HCSLgikakMDAASWTG---LSTSDIIW----TIS-DTAwIMNILGaflePWVLGACIFVhlLPKFDSQTVLK----VLS 302
Cdd:TIGR01733 142 HRSL-----VNLLAWLArryGLDPDDRVlqfaSLSfDAS-VEEIFG----ALLAGATLVV--PPEDEERDDAAllaaLIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKTG-LEIREIYGQTETGLICRVSRTMKVKP 381
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 GY-----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDN-IRGDFWLM--------GD 447
Cdd:TIGR01733 288 PRespvpIGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGD 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 448 RGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAV 499
Cdd:TIGR01733 363 LVRYLPDGNLEFLGRIDDQVKIRG-----YRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-570 |
2.28e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 154.44 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 74 GSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASK 153
Cdd:PRK13295 49 GTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 154 ARAIVA-----GDEVAQEVDAVAPDCSFLKIKLLVSEnsrEGWLNFKALL----KEASTIHQCVETESR----ESAAIYF 220
Cdd:PRK13295 128 SKVLVVpktfrGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLitpaWEQEPDAPAILARLRpgpdDVTQLIY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 221 TSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKV 300
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTL-MANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGAT--AVLQDIWDPARAAEL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 301 LSSYPIN-TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL--ICRVSRTM 377
Cdd:PRK13295 282 IRTEGVTfTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 378 KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGdfWL-MGDRGIKDPEGY 456
Cdd:PRK13295 362 ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADG--WFdTGDLARIDADGY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 457 FHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEH 536
Cdd:PRK13295 435 IRISGRSKDVIIRGGE-----NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ 508
|
490 500 510
....*....|....*....|....*....|....
gi 295789127 537 vkSVTAPYkYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK13295 509 --KVAKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
81-571 |
3.47e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 152.45 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSGAcglhrgDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIQMRSSDilyrlqasKARAIVAG 160
Cdd:PRK07787 26 LSRSDLAGAATAVAERVAGA------RRVAVLATPTLATVLAVVGALIAGVPVVP--VPPDSGV--------AERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEVAQEVDAVAPDCSFLKIKLLVSENSReGWlnfkallkeastiHQCVETESRESAAIYFTSGTSGPPKMAEHSHcsLGI 240
Cdd:PRK07787 90 DSGAQAWLGPAPDDPAGLPHVPVRLHAR-SW-------------HRYPEPDPDAPALIVYTSGTTGPPKGVVLSR--RAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 241 KAKMD--AASWTglstsdiiWTISDT-----------AWIMNILGaflePWVLGACiFVHLLpKFDSQTVLKVLSSyPIN 307
Cdd:PRK07787 154 AADLDalAEAWQ--------WTADDVlvhglplfhvhGLVLGVLG----PLRIGNR-FVHTG-RPTPEAYAQALSE-GGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTA 387
Cdd:PRK07787 219 LYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 388 FAHYDVQVIDEQGNVLPPGKE--GDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGR-S 463
Cdd:PRK07787 299 LAGVETRLVDEDGGPVPHDGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGReS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 464 DDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLApeflshdRDQLTKVLQEHVKSVTAP 543
Cdd:PRK07787 374 TDLIKSGG-----YRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGA-------DDVAADELIDFVAQQLSV 441
|
490 500
....*....|....*....|....*...
gi 295789127 544 YKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK07787 442 HKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
67-569 |
5.14e-40 |
|
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: 151.63 E-value: 5.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 67 PALWWMNGsgkeiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdil 146
Cdd:cd05945 8 PAVVEGGR-----TLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 147 yrlqaskARAIVAGDEVAQEVDAVAPDcsflkikLLVSENSregwlnfkallkeastihqcvetesrESAAIYFTSGTSG 226
Cdd:cd05945 71 -------LDASSPAERIREILDAAKPA-------LLIADGD--------------------------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 227 PPKMAEHSHCSLgikakmdaASWTGlstsdiiWTISDTAW-----------------IMNILGAflepWVLGACIFVhlL 289
Cdd:cd05945 111 RPKGVQISHDNL--------VSFTN-------WMLSDFPLgpgdvflnqapfsfdlsVMDLYPA----LASGATLVP--V 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 PKfDSQTVLKVLSSY----PINTLVGAPIIYRMLLQ-QDLSSYKFPHL-HSCFSGgETLLPETLENWKAKT-GLEIREIY 362
Cdd:cd05945 170 PR-DATADPKQLFRFlaehGITVWVSTPSFAAMCLLsPTFTPESLPSLrHFLFCG-EVLPHKTARALQQRFpDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 363 GQTETGLIC---RVSRTM--KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQ 435
Cdd:cd05945 248 GPTEATVAVtyiEVTPEVldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPEKTA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 436 ---DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVV 511
Cdd:cd05945 321 aafFPDEGQRAYrTGDLVRLEADGLLFYRGRLDFQVKLNG-----YRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 512 KAFVVLAPeflsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05945 396 IAFVVPKP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
78-570 |
9.36e-40 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 152.30 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAQEVDAVAPDCSFLK-IKLLVSENSREGWLNFKALLKEASTIHQCVETESRES-------AAIYFTSGTSGPPK 229
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKtIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSfdrdeqvALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 MAEHSHcsLGIKAKMDAASwtglsTSDIIWTISDTAWIMNILgaflePWVLGACIF-----------VHLLPKFDSQTVL 298
Cdd:cd17642 201 GVQLTH--KNIVARFSHAR-----DPIFGNQIIPDTAILTVI-----PFHHGFGMFttlgylicgfrVVLMYKFEEELFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 299 KVLSSYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREIYGQTETGLICRVSRT 376
Cdd:cd17642 269 RSLQDYKVQSALLVPTLFAFFAKSTLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 377 MKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 454
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDED 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 455 GYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlapefLSHDRDQLTKVLQ 534
Cdd:cd17642 424 GHFFIVDRLKSLIKYKG-----YQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV-----LEAGKTMTEKEVM 493
|
490 500 510
....*....|....*....|....*....|....*..
gi 295789127 535 EHVKSVTAPYKYPR-KVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd17642 494 DYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-569 |
1.30e-39 |
|
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: 150.94 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV---FMPGtiqMRSSDILYRLQASKARA 156
Cdd:cd05920 40 RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS---HRRSELSAFCAHAEAVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 IVAGDEvAQEVDavapdcsflkikllvsensregwlnFKALLKEastihqcVETESRESAAIYFTSGTSGPPKMAEHSHC 236
Cdd:cd05920 116 YIVPDR-HAGFD-------------------------HRALARE-------LAESIPEVALFLLSGGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 237 SLGIKAKMdAASWTGLStsdiiwtiSDTAWIMNILGA----FLEPWVLGACIF---VHLLPKFDSQTVLKVLSSYPIN-- 307
Cdd:cd05920 163 DYAYNVRA-SAEVCGLD--------QDTVYLAVLPAAhnfpLACPGVLGTLLAggrVVLAPDPSPDAAFPLIEREGVTvt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVgaPIIYRMLLQQ------DLSSYKFPHLhscfsGGETLLPETLENWKAKTGLEIREIYGQTEtGLIC--RVSRTMKV 379
Cdd:cd05920 234 ALV--PALVSLWLDAaasrraDLSSLRLLQV-----GGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNytRLDDPDEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 380 KPGYLGTAFAHYD-VQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEG 455
Cdd:cd05920 306 IIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 456 YFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdrdqlTKVLQE 535
Cdd:cd05920 379 YLVVEGRIKDQINRGGE-----KIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS------AAQLRR 447
|
490 500 510
....*....|....*....|....*....|....*
gi 295789127 536 HVKSV-TAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05920 448 FLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
62-571 |
2.07e-39 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 152.80 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 62 KRSSGPALWWMNG-SGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTG----LVFmpG 136
Cdd:PRK10524 65 KRPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihsVVF--G 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 137 TIqmrssdilyrlqaskaraivAGDEVAQEVDAVAPdcsflkiKLLVSEN--SREG-WLNFKALLKEA------------ 201
Cdd:PRK10524 142 GF--------------------ASHSLAARIDDAKP-------VLIVSADagSRGGkVVPYKPLLDEAialaqhkprhvl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 202 -------------------STIHQ--------CVETESRESAAIYFTSGTSGPPKmaehshcslGIKakMDAASWT-GLS 253
Cdd:PRK10524 195 lvdrglapmarvagrdvdyATLRAqhlgarvpVEWLESNEPSYILYTSGTTGKPK---------GVQ--RDTGGYAvALA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 254 TS----------DIIWTISDTAWIM----NILGaflePWVLG-ACIFVHLLP-KFDSQTVLKVLSSYPINTLVGAPIIYR 317
Cdd:PRK10524 264 TSmdtifggkagETFFCASDIGWVVghsyIVYA----PLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 318 MLLQQD---LSSYKFPHLHSCFSGGETLlPETLENWKAKT-GLEIREIYGQTETGL----ICRVSRTMKVKPGYLGTAFA 389
Cdd:PRK10524 340 VLKKQDpalLRKHDLSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGWpilaIARGVEDRPTRLGSPGVPMY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 390 HYDVQVIDEQ-GNVLPPGKEGDIAIRvKPIWPIGMFSGYVDNPKKTQDnirgdFW-LMG-------DRGIKDPEGYFHFI 460
Cdd:PRK10524 419 GYNVKLLNEVtGEPCGPNEKGVLVIE-GPLPPGCMQTVWGDDDRFVKT-----YWsLFGrqvystfDWGIRDADGYYFIL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 461 GRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQ---LTKVLQEHV 537
Cdd:PRK10524 493 GRTDDVINVAG-----HRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALV 567
|
570 580 590
....*....|....*....|....*....|....
gi 295789127 538 KSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK10524 568 DSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
79-570 |
3.56e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 151.12 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 79 IKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMpgTIQ--MRSSDILYRLQASKARA 156
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 IVAGDEV-----AQEVDAVAPDCS-------------FLKIKLLVSENSREGWLNFKALLKEASTIHQcVETESRESAA- 217
Cdd:PRK08315 119 LIAADGFkdsdyVAMLYELAPELAtcepgqlqsarlpELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 ------IYFTSGTSGPPKMAEHSHCSLGikakmDAASWTGLStsdIIWTISDTAWI---------MnILGaflepwVL-- 280
Cdd:PRK08315 198 pddpinIQYTSGTTGFPKGATLTHRNIL-----NNGYFIGEA---MKLTEEDRLCIpvplyhcfgM-VLG------NLac 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 ---GACIfVHLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL 356
Cdd:PRK08315 263 vthGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 357 eiREI---YGQTETG---LICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwpiG---MfSG 426
Cdd:PRK08315 342 --SEVtiaYGMTETSpvsTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTR-------GysvM-KG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 427 YVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDP 505
Cdd:PRK08315 412 YWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGE-----NIYPREIEEFLYTHPKIQDVQVVGVPDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 506 SRGEVVKAFVVLAPEFlshdrdQLTKV-LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK08315 487 KYGEEVCAWIILRPGA------TLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
48-572 |
7.78e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 149.27 E-value: 7.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 48 SDVIDHWASvekagKRSSGPALWWmngSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCM 127
Cdd:PRK06145 5 SASIAFHAR-----RTPDRAALVY---RDQEI--SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 128 RTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPdcsflkiKLLVSENSREGWLNFKALLKEASTIHQC 207
Cdd:PRK06145 74 YLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETP-------KIVIDAAAQADSRRLAQGGLEIPPQAAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 208 VETESREsaaIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDtawiMNILGAFLEP-----WVLGa 282
Cdd:PRK06145 147 APTDLVR---LMYTSGTTDRPKGVMHSYGNLHWKS-IDHVIALGLTASERLLVVGP----LYHVGAFDLPgiavlWVGG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 283 ciFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLlPETL--ENWKAKTGLEIR 359
Cdd:PRK06145 218 --TLRIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKT-PESRirDFTRVFTRARYI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 360 EIYGQTETgliCRVSRTMKV-----KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKT 434
Cdd:PRK06145 295 DAYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKV-----TKGYWKDPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 435 QDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAF 514
Cdd:PRK06145 367 AEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGE-----NIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 295789127 515 VVLAPEflshdrDQLT-KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PRK06145 442 VVLNPG------ATLTlEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
82-570 |
8.21e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 149.97 E-value: 8.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDAVAPDCS---FLKIKLLVSENSREGWL---------------------NFKALLKE-ASTIHQCVETESRESA 216
Cdd:PRK12492 131 MFGKLVQEVLPDTGieyLIEAKMGDLLPAAKGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 217 AIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAASWTGLSTsdiiwtISDTAWIMNILGAFLEPWVLGA---CIFV-- 286
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLvanmlQVRACLSQLGPDGQPL------MKEGQEVMIAPLPLYHIYAFTAncmCMMVsg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 287 --HLL---PKfDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 360
Cdd:PRK12492 285 nhNVLitnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIR 439
Cdd:PRK12492 364 GYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQV-----MKGYWQQPEATAEALD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 440 GDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 518
Cdd:PRK12492 439 AEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSG-----FNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 519 PEFLSHDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK12492 514 DPGLSVEE------LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
214-566 |
1.05e-38 |
|
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: 144.95 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 214 ESAAIYFTSGTSGPPK--MAEHSHcSLGIkakmdAASWtglstSDIIWTISDTAWImnILGAFLEPWVLGACIFVHLL-- 289
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQ-TLRA-----AAAW-----ADCADLTEDDRYL--IINPFFHTFGYKAGIVACLLtg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 ----PK--FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREI 361
Cdd:cd17638 68 atvvPVavFDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 362 YGQTETGL--ICRVSRTMKVKPGYLGTAFAHYDVQVIDeQGNVLPPGKEgdiairvkpiwpigMFSGYVDNPKKTQDNIR 439
Cdd:cd17638 148 YGLTEAGVatMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRGYN--------------VMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 440 GDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 518
Cdd:cd17638 213 ADGWLhTGDVGELDERGYLRITDRLKDMYIVGG-----FNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 295789127 519 PEfLSHDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:cd17638 288 PG-VTLTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-572 |
3.08e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 147.88 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 66 GPALWWmngsgKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDI 145
Cdd:PRK07470 23 RIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 146 LYRLQASKARAIVAGDEVAQEVDAVAPDCsfLKIKLLVSENSREGWLNFKALLKE-ASTIHQCVETESRESAAIYFTSGT 224
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHAAAVRAAS--PDLTHVVAIGGARAGLDYEALVARhLGARVANAAVDHDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 225 SGPPKMAEHSHCSLG-IKAKMDAASWTGLSTSD---IIWTISDTAWIMNILGAflepwVLGACIFVHLLPKFDSQTVLKV 300
Cdd:PRK07470 175 TGRPKAAVLTHGQMAfVITNHLADLMPGTTEQDaslVVAPLSHGAGIHQLCQV-----ARGAATVLLPSERFDPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 301 LSSYPINTLVGAPIIYRMLL------QQDLSSYKfphlHSCFSGGetllPETLENWK---AKTGLEIREIYGQTE-TGLI 370
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVehpavdRYDHSSLR----YVIYAGA----PMYRADQKralAKLGKVLVQYFGLGEvTGNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 371 CRVSRTM-------KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFW 443
Cdd:PRK07470 322 TVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEANAKAFRDGWF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 444 LMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAfVVLAPEFLS 523
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGS-----NVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA-VCVARDGAP 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 295789127 524 HDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PRK07470 471 VDEAE----LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
60-575 |
3.14e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 147.53 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 60 AGKRSSGPALWwMNGSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVL---PRIPE--WwlmilGCMRTGLVFM 134
Cdd:PRK13391 7 AQTTPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLEvcW-----AAERSGLYYT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 135 PGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLV-SENSREGWLNFkallkeASTIHQCVET--- 210
Cdd:PRK13391 78 CVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGY------AEAVAGLPATpia 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 211 ESRESAAIYFTSGTSGPPKmaehshcslGIKAKmdaaswtgLSTSDIIWTISDTAWIMNILG-----AFLEP-------- 277
Cdd:PRK13391 152 DESLGTDMLYSSGTTGRPK---------GIKRP--------LPEQPPDTPLPLTAFLQRLWGfrsdmVYLSPaplyhsap 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 278 --WV-----LGACIFVhlLPKFDSQTVLKVLSSYPINTLVGAPIIY-RML-------LQQDLSSykfphLHSCFSGGETL 342
Cdd:PRK13391 215 qrAVmlvirLGGTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPC 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 343 LPETLENWKAKTGLEIREIYGQTETGLICRV-SRTMKVKPGYLGTAFAHyDVQVIDEQGNVLPPGKEGDIairvkpiWPI 421
Cdd:PRK13391 288 PPQVKEQMIDWWGPIIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTI-------WFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 422 G--MFSgYVDNPKKTQD--NIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSET 497
Cdd:PRK13391 360 GgrPFE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGV-----NIYPQEAENLLITHPKVADA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 498 AVISSPDPSRGEVVKAFVVLAPefLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 575
Cdd:PRK13391 434 AVFGVPNEDLGEEVKAVVQPVD--GVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
75-572 |
4.08e-38 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 147.82 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 75 SGKEIKWSfrELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKA 154
Cdd:PLN02330 52 TGKAVTYG--EVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQEVDAvapdcsfLKIKLLV-SENSREGWLNFKALLKEAStihQCVETESRES------AAIYFTSGTSGP 227
Cdd:PLN02330 129 KLIVTNDTNYGKVKG-------LGLPVIVlGEEKIEGAVNWKELLEAAD---RAGDTSDNEEilqtdlCALPFSSGTTGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 228 PKMAEHSHCSLgiKAKMdAASWTGLStSDIIWTISDTAWI--MNILGaflepwVLGACIF-------VHLLPKFDSQTVL 298
Cdd:PLN02330 199 SKGVMLTHRNL--VANL-CSSLFSVG-PEMIGQVVTLGLIpfFHIYG------ITGICCAtlrnkgkVVVMSRFELRTFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 299 KVLSSYPIN----------TLVGAPIIYRMllqqDLSSYKfphLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTET 367
Cdd:PLN02330 269 NALITQEVSfapivppiilNLVKNPIVEEF----DLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 GLICRVSRTMK-----VKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGD 441
Cdd:PLN02330 342 SCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCV-----MQGYYNNKEETDRTIDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 442 FWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPE 520
Cdd:PLN02330 417 GWLhTGDIGYIDDDGDIFIVDRIKELIKYKG-----FQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPK 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 521 FLSHDRDQLtkvlqEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PLN02330 492 AKESEEDIL-----NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
213-572 |
3.46e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 144.90 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 213 RESAAIYFTSGTSGPPKMAEHSHC--SLGIKAKMDAASWTGLSTSDII------WTISDTAwimniLGAFLepwvlgACI 284
Cdd:PRK13382 196 RKGRVILLTSGTTGTPKGARRSGPggIGTLKAILDRTPWRAEEPTVIVapmfhaWGFSQLV-----LAASL------ACT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 285 FVhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ---QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREI 361
Cdd:PRK13382 265 IV-TRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 362 YGQTETGLICRVS-RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPiwpigMFSGYVdnPKKTQDNIRG 440
Cdd:PRK13382 344 YNATEAGMIATATpADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT-----QFDGYT--SGSTKDFHDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 441 dFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPe 520
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRDDEMIVSGGE-----NVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP- 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 521 flshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PRK13382 490 ----GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
60-572 |
4.64e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 145.63 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 60 AGKRSSGPALWWMNGsGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP--GT 137
Cdd:COG1022 21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPiyPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 138 IqmRSSDILYRLQASKARAIVAGD-EVAQEVDAVAPDCSFLKiKLLV----SENSREGWLNFKALLKEASTIHQCVETES 212
Cdd:COG1022 99 S--SAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLALGREVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 213 RES-------AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIiwTIS--DTAWIM-NILGAFLepWVLGA 282
Cdd:COG1022 176 RRAavkpddlATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDR--TLSflPLAHVFeRTVSYYA--LAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 283 CI-FVHllpkfDSQTVLKVLSSYPINTLVGAP--------------------------------IIYRMLLQQDLS---S 326
Cdd:COG1022 251 TVaFAE-----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalavgRRYARARLAGKSpslL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 327 YKFPH------------------LHSCFSGGETLLPETLENWKAkTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAF 388
Cdd:COG1022 326 LRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 389 AhyDVQV-IDEQGNVLppgkegdiairVK-PiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDD 465
Cdd:COG1022 405 P--GVEVkIAEDGEIL-----------VRgP----NVMKGYYKNPEATAEAFDADGWLHtGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 466 II-NSSGAYfcryrIGPSEVENALMEHPAVSETAVIsspdpsrGE---VVKAFVVLAPEFLSH----------------D 525
Cdd:COG1022 468 LIvTSGGKN-----VAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVPDFEALGEwaeenglpytsyaelaQ 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 526 RDQLTKVLQEHVKSVTApyKYPRkVE----FVLdLPK---------TVTGKIERAKLRAK 572
Cdd:COG1022 536 DPEVRALIQEEVDRANA--GLSR-AEqikrFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
37-574 |
5.76e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 144.50 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 37 HQEAPAKFNFASdVIDhwasvEKAGKRSSGPALwwmngSGKEIKWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRI 116
Cdd:PRK06164 3 HDAAPRADTLAS-LLD-----AHARARPDAVAL-----IDEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 117 PEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG------------DEVAQEVDAVAPdcsflKIKLLVS 184
Cdd:PRK06164 71 IEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWpgfkgidfaailAAVPPDALPPLR-----AIAVVDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 185 ENS------REGWLNFKALLKEASTIHQCVETESRESAAIYFT-SGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDI 257
Cdd:PRK06164 146 AADatpapaPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAY-GYDPGAV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 258 IWTISDtawimnILGAFLEPWVLGAC---IFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHS 334
Cdd:PRK06164 225 LLAALP------FCGVFGFSTLLGALaggAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 335 C----FSGGETLLPEtlenWKAKTGLEIREIYGQTEtgLICRVS---RTMKVKPGYLG---TAFAHYDVQVIDEQ-GNVL 403
Cdd:PRK06164 299 FgfasFAPALGELAA----LARARGVPLTGLYGSSE--VQALVAlqpATDPVSVRIEGggrPASPEARVRARDPQdGALL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 404 PPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPS 482
Cdd:PRK06164 373 PDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGG-----FLVNPA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 483 EVENALMEHPAVSETAVISSPDPSRGEVVkAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTG 562
Cdd:PRK06164 443 EIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAG-----LMAACREALAGFKVPARVQVVEAFPVTESA 516
|
570
....*....|....*..
gi 295789127 563 ---KIERAKLR--AKEW 574
Cdd:PRK06164 517 ngaKIQKHRLRemAQAR 533
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
76-569 |
4.49e-36 |
|
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: 140.42 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIQMRSS--DILYRLQASK 153
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP--IYPTSSaeQIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 154 ARAIVAGDevaqevdavaPDcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEH 233
Cdd:cd05907 78 AKALFVED----------PD----------------------------------------DLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 234 SHCSlgIKAKMDAASwTGLSTSDIIWTIS--DTAWIMNILGAFLEPWVLGACIfVHLLPkfdSQTVLKVLSSYPINTLVG 311
Cdd:cd05907 108 SHRN--ILSNALALA-ERLPATEGDRHLSflPLAHVFERRAGLYVPLLAGARI-YFASS---AETLLDDLSEVRPTVFLA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 312 APIIYRML----LQQDLSSYK--------FPHLHSCFSGGETLLPETLEnWKAKTGLEIREIYGQTETGLICRVSRTMKV 379
Cdd:cd05907 181 VPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLH-FFRALGIPVYEGYGLTETSAVVTLNPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 380 KPGYLGTAFahYDVQV-IDEQGNVLppgkegdiairvkpIWPIGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYF 457
Cdd:cd05907 260 RIGTVGKPL--PGVEVrIADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 458 HFIGRSDD-IINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSrgevVKAFVVLAPEFLSH------------ 524
Cdd:cd05907 324 HITGRKKDlIITSGGKN-----ISPEPIENALKASPLISQAVVIGDGRPF----LVALIVPDPEALEAwaeehgiaytdv 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 295789127 525 ----DRDQLTKVLQEHVKSVTA---PYKYPRKVeFVLDLPKTV-------TGKIERAKL 569
Cdd:cd05907 395 aelaANPAVRAEIEAAVEAANArlsRYEQIKKF-LLLPEPFTIengeltpTLKLKRPVI 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-571 |
1.89e-35 |
|
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: 136.46 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHcslgikakmdaaswtglstSDIIWTisdtAWIMNILGAFLEPWVL---------GACIFV 286
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTH-------------------SNEVYN----AWMLALNSLFDPDDVLlcglplfhvNGSVVT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 287 HLLPKFDSQTVL-----------------KVLSSYPINTLVGAPIIYRMLLQ----QDLSSYKFphlhsCFSGGETLLPE 345
Cdd:cd05944 62 LLTPLASGAHVVlagpagyrnpglfdnfwKLVERYRITSLSTVPTVYAALLQvpvnADISSLRF-----AMSGAAPLPVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 346 TLENWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYDVQ--VIDEQGNVL---PPGKEGDIAIRVKpiw 419
Cdd:cd05944 137 LRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRikVLDGVGRLLrdcAPDEVGEICVAGP--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 420 piGMFSGYVDNPKKtQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETA 498
Cdd:cd05944 214 --GVFGGYLYTEGN-KNAFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGG-----HNIDPALIEEALLRHPAVAFAG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 499 VISSPDPSRGEVVKAFVVLAP-------EFLSHDRDqltkvlqeHVKSVTApykYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05944 286 AVGQPDAHAGELPVAYVQLKPgavveeeELLAWARD--------HVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
47-569 |
1.93e-35 |
|
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: 139.18 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 47 ASDVIDHWASVEKAGkrssgpalwwmngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGC 126
Cdd:cd05923 11 ASRAPDACAIADPAR----------------GLRLTYSELRARIEAVAARLH-ARGLRPGQRVAVVLPNSVEAVIALLAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 127 MRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDeVAQEVDAVAPdcSFLKIkLLVSENSREGWL-NFKALLKEASTih 205
Cdd:cd05923 74 HRLGAVPALINPRLKAAELAELIERGEMTAAVIAV-DAQVMDAIFQ--SGVRV-LALSDLVGLGEPeSAGPLIEDPPR-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 206 qcvetESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSD--IIWTISDTAWIMNILGAFLEPWVLGAC 283
Cdd:cd05923 148 -----EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV-LFMSTQAGLRHGRhnVVLGLMPLYHVIGFFAVLVAALALDGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 284 IFVhlLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ------QDLSSYKfphlHSCFSGG---ETLLpETLENwkAKT 354
Cdd:cd05923 222 YVV--VEEFDPADALKLIEQERVTSLFATPTHLDALAAaaefagLKLSSLR----HVTFAGAtmpDAVL-ERVNQ--HLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 355 GlEIREIYGQTE--TGLICRVSRT-MKVKPGYlgtafaHYDVQVIDEQGNV---LPPGKEGDIAIRVKPIWpigMFSGYV 428
Cdd:cd05923 293 G-EKVNIYGTTEamNSLYMRDARTgTEMRPGF------FSEVRIVRIGGSPdeaLANGEEGELIVAAAADA---AFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 429 DNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRG 508
Cdd:cd05923 363 NQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGE-----NIHPSEIERVLSRHPGVTEVVVIGVADERWG 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789127 509 EVVKAFVVLAPEFLSHDR-DQLTKvlqehvKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd05923 438 QSVTACVVPREGTLSADElDQFCR------ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
58-572 |
2.04e-35 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 140.12 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 58 EKAGKRSSGPALwwMNGSGKEIkWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 137
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 138 IQMRSSDILYRLQASKARAIVAgdeVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAA 217
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 IYFTSGTSGPPKMAEHSHCSL--GIKAKMDAASwtglstSDIIWTISDTawIMNILGAF----LEPWVL-----GACIFV 286
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHKGLvtSVAQQVDGEN------PNLYFHSDDV--ILCVLPMFhiysLNSVLLcglrvGAAILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 287 hlLPKFDSQTVLKVLSSYPINTlvgAPIIYRMLL---------QQDLSSYKFphlhsCFSGGETLLPETLENWKAK-TGL 356
Cdd:PLN02246 256 --MPKFEIGALLELIQRHKVTI---APFVPPIVLaiakspvveKYDLSSIRM-----VLSGAAPLGKELEDAFRAKlPNA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 357 EIREIYGQTETGLICRVS-----RTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDN 430
Cdd:PLN02246 326 VLGQGYGMTEAGPVLAMClafakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 431 PKKTQDNIRGDFWL-MGDRG-IKDPEGYFhFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRG 508
Cdd:PLN02246 401 PEATANTIDKDGWLhTGDIGyIDDDDELF-IVDRLKELIKYKG-----FQVAPAELEALLISHPSIADAAVVPMKDEVAG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 509 EVVKAFVVLAPEFlshdrdqltKVLQEHVKSVTAP----YKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PLN02246 475 EVPVAFVVRSNGS---------EITEDEIKQFVAKqvvfYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
78-571 |
5.23e-35 |
|
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: 138.74 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGL--VF-MPGtiqMRSSDILYRLQASKA 154
Cdd:COG1021 48 ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAipVFaLPA---HRRAEISHFAEQSEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVA-----QEVDAVAPDCSFLKIKLLVSENsrEGWLNFKALLKEASTIHQCvETESRESAAIYFTSGTSGPPK 229
Cdd:COG1021 124 VAYIIPDRHRgfdyrALARELQAEVPSLRHVLVVGDA--GEFTSLDALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 MAEHSH----CSlgIKAKMDAASWtglstsdiiwtisDTAWIM--------N-------ILGAFLepwvLGACifVHLLP 290
Cdd:COG1021 201 LIPRTHddylYS--VRASAEICGL-------------DADTVYlaalpaahNfplsspgVLGVLY----AGGT--VVLAP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 291 KFDSQTVLKVLSSYPIN--TLVgaPIIYRMLLQQ------DLSSYKFphLHScfsGGETLLPETLENWKAKTGLEIREIY 362
Cdd:COG1021 260 DPSPDTAFPLIERERVTvtALV--PPLALLWLDAaersryDLSSLRV--LQV---GGAKLSPELARRVRPALGCTLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 363 GQTEtGLIC---------RVSRTMkvkpgylGTAFAHYD-VQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDN 430
Cdd:COG1021 333 GMAE-GLVNytrlddpeeVILTTQ-------GRPISPDDeVRIVDEDGNPVPPGEVGELLTR-------GpyTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 431 PKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGE 509
Cdd:COG1021 398 PEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGE-----KIAAEEVENLLLAHPAVHDAAVVAMPDEYLGE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789127 510 VVKAFVVLAPEFLShdrdqlTKVLQEHVKSV-TAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:COG1021 473 RSCAFVVPRGEPLT------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
78-572 |
9.27e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 138.16 E-value: 9.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEwwlMI---LGCMRTGLVFMPGTIQMRSSDILYRLQASKA 154
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPA---MVeahFGVPMAGAVLNTLNTRLDAASIAFMLRHGEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQEVDAVAPDCSFLKIkLLV-------SENSREGWLNFKALLKEASTIHQCVETESR-ESAAIYFTSGTSG 226
Cdd:PRK08162 117 KVLIVDTEFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 227 PPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGACIFVHL-LPKFDSQTVLKVLSSYP 305
Cdd:PRK08162 196 NPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLP-----MFHCNGWCFPWTVAARAGTNVcLRKVDPKLIFDLIREHG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 306 INTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAkTGLEIREIYGQTET-GlicrvsrtmkvkPGY 383
Cdd:PRK08162 271 VTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE-IGFDLTHVYGLTETyG------------PAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 LGTAFAHYDVQVIDE-------QG---------NVLPP---------GKE-GDIAIRVKpiwpIGMfSGYVDNPKKTQDN 437
Cdd:PRK08162 338 VCAWQPEWDALPLDEraqlkarQGvryplqegvTVLDPdtmqpvpadGETiGEIMFRGN----IVM-KGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 438 IRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL 517
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGE-----NISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVEL 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789127 518 AP-------EFLSHDRDQLtkvlqehvksvtAPYKYPRKVEFVlDLPKTVTGKIERAKLRAK 572
Cdd:PRK08162 488 KDgasateeEIIAHCREHL------------AGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
78-570 |
2.17e-34 |
|
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: 136.32 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAQEVDAVAPDcsflkikllVSENSREGWlnfkALLKEASTIhqcVETESRESAAIYFTSGTSGPPKMAEHSHCS 237
Cdd:cd17651 97 LTHPALAGELAVELVA---------VTLLDQPGA----AAGADAEPD---PALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 L-----------GIKAKMDAASWTGLSTSDIIWTISDTawimniLGAflepwvlGACIfvHLLP---KFDSQTVLKVLSS 303
Cdd:cd17651 161 LanlvawqarasSLGPGARTLQFAGLGFDVSVQEIFST------LCA-------GATL--VLPPeevRTDPPALAAWLDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 304 YPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETL-LPETLENWKAK-TGLEIREIYGQTETGLIcrVSRTMKVK 380
Cdd:cd17651 226 QRISRVFLPTVALRALAEHgRPLGVRLAALRYLLTGGEQLvLTEDLREFCAGlPGLRLHNHYGPTETHVV--TALSLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 381 PGY------LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ-----DNIRGD--FWLMGD 447
Cdd:cd17651 304 PAAwpapppIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAerfvpDPFVPGarMYRTGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 448 RGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRD 527
Cdd:cd17651 379 LARWLPDGELEFLGRADDQVKIRG-----FRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-----AP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 295789127 528 QLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd17651 449 VDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
82-580 |
2.45e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 136.37 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK12406 13 SFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEV-DAVAPDCSFLKI----KLL----VSENSR---EGWLNFKALLKEASTIHQcveTESRESAAIYFTSGTSGPPK 229
Cdd:PRK12406 92 DLLHGLaSALPAGVTVLSVptppEIAaayrISPALLtppAGAIDWEGWLAQQEPYDG---PPVPQPQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 maehshcslGIK----AKMDAASWtGLSTSDIIWTISDTAWIM---------NILGafLEPWVLGACIFvhLLPKFDSQT 296
Cdd:PRK12406 169 ---------GVRraapTPEQAAAA-EQMRALIYGLKPGIRALLtgplyhsapNAYG--LRAGRLGGVLV--LQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VLKVLSSYPINTLVGAPIIYRMLLQ--------QDLSSYKFPhLHSCFSGGETLLPETLENWkaktGLEIREIYGQTETG 368
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRHV-IHAAAPCPADVKRAMIEWW----GPVIYEYYGSTESG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 369 LI--CRVSRTMKvKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGM--FSgYVDNPKKTQDNIRGDFWL 444
Cdd:PRK12406 310 AVtfATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA-----GNpdFT-YHNKPEKRAEIDRGGFIT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LS 523
Cdd:PRK12406 383 SGDVGYLDADGYLFLCDRKRDMVISGGV-----NIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAtLD 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 295789127 524 HDrdqltkVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 580
Cdd:PRK12406 458 EA------DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
84-571 |
8.73e-34 |
|
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: 134.43 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 84 RELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEwwlmILGC---MRTGLVFMPGTIQMRSSDILYRLQASKAR-AIVA 159
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAA----AEGVwiaDGVYIYLINSILTVFAAAAAWKCGACPAYkSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GDEVAQEVDAVAPDcsFLKIKLLVSENSREGWLNFKALLKEASTihQCVETESRESAAIYfTSGTSGPPK--MAEHSHCS 237
Cdd:cd05929 77 PRAEACAIIEIKAA--ALVCGLFTGGGALDGLEDYEAAEGGSPE--TPIEDEAAGWKMLY-SGGTTGRPKgiKRGLPGGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 LGIKAKMDAASWTGLSTSDI------IWTISDTAWIMNILgaflepwVLGACifVHLLPKFDSQTVLKVLSSYPINTLVG 311
Cdd:cd05929 152 PDNDTLMAAALGFGPGADSVylspapLYHAAPFRWSMTAL-------FMGGT--LVLMEKFDPEEFLRLIERYRVTFAQF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 312 APIIY-RM--LLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTA 387
Cdd:cd05929 223 VPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 388 FAHyDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmfSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDI 466
Cdd:cd05929 303 VLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGWStLGDVGYLDEDGYLYLTDRRSDM 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 467 INSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAfvVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKY 546
Cdd:cd05929 376 IISGGV-----NIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKC 448
|
490 500
....*....|....*....|....*
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05929 449 PRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
44-563 |
1.15e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 131.93 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 44 FNFAsDVIDHwaSVEKAGKRssgPALWWmngsGKEiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMI 123
Cdd:PRK07798 3 WNIA-DLFEA--VADAVPDR---VALVC----GDR-RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 124 LGCMRTGLVfmPGTIQMR--SSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSflKIKLLVS------ENSREGWLNFK 195
Cdd:PRK07798 71 LGAFKARAV--PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLP--KLRTLVVvedgsgNDLLPGAVDYE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 196 ALLKEASTIHQCVEtesRESAAIYF--TSGTSGPPK--MAEHS---HCSLGIKAKMdaaswTGLSTSDIiWTISD----- 263
Cdd:PRK07798 147 DALAAGSPERDFGE---RSPDDLYLlyTGGTTGMPKgvMWRQEdifRVLLGGRDFA-----TGEPIEDE-EELAKraaag 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 264 --TAWIM-----------NILGAFLEpwvlGACIFVHLLPKFDSQTVLKVLSSYPIN--TLVG----APII--YRMLLQQ 322
Cdd:PRK07798 218 pgMRRFPapplmhgagqwAAFAALFS----GQTVVLLPDVRFDADEVWRTIEREKVNviTIVGdamaRPLLdaLEARGPY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 323 DLSSykfphLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLiCRVSRTMKVKPGYLGTAF-AHYDVQVIDEQG 400
Cdd:PRK07798 294 DLSS-----LFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSETGF-GGSGTVAKGAVHTGGPRFtIGPRTVVLDEDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 401 NVLPPG--KEGDIAIRvKPIwPIGmfsgYVDNPKKTQDN---IRGDFW-LMGDRGIKDPEGYFHFIGRSDDIINSSGAyf 474
Cdd:PRK07798 368 NPVEPGsgEIGWIARR-GHI-PLG----YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGE-- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 475 cryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVL 554
Cdd:PRK07798 440 ---KVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLAE----LRAHCRSSLAGYKVPRAIWFVD 511
|
....*....
gi 295789127 555 DLPKTVTGK 563
Cdd:PRK07798 512 EVQRSPAGK 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
213-566 |
1.76e-32 |
|
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: 127.76 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 213 RESAAIYFTSGTSGPPKMAEHSHcslgikaKMDAASWTGLSTSDIIWTISDTAWI-MNILGAFLEPWVLGACIFVHLLPK 291
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLAN-------KTFFAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 292 FDS----QTVLKVLSSYPINTLVGAPII--YRMLLQQDLSSYKfPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQT 365
Cdd:cd17635 74 GGEnttyKSLFKILTTNAVTTTCLVPTLlsKLVSELKSANATV-PSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 366 ETGLICRVSRTMKVKP-GYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIrvKPIWpigMFSGYVDNPKKTQDNIRGDFWL 444
Cdd:cd17635 153 ETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPA---NMLGYWNNPERTAEVLIDGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsh 524
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGV-----KIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE---- 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 295789127 525 DRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
80-570 |
7.70e-32 |
|
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: 128.25 E-value: 7.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdilyrlqaskaraiva 159
Cdd:cd17649 12 SLSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdaVAPDCSFLKIKLLVsENSREGWLnfkallkeastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCSLG 239
Cdd:cd17649 67 ----------LDPEYPAERLRYML-EDSGAGLL---------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKAKMDAASWtGLSTSDIIWTISDtawiMNILGA---FLEPWVLGACIFVHLLPKFDS-QTVLKVLSSYPINTLVGAPII 315
Cdd:cd17649 121 AHCQATAERY-GLTPGDRELQFAS----FNFDGAheqLLPPLICGACVVLRPDELWASaDELAEMVRELGVTVLDLPPAY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 316 YRMLLQQ--DLSSYKFPHLHSCFSGGETLLPETLENWkAKTGLEIREIYGQTE---TGLICRVSRTMKVKPGYL--GTAF 388
Cdd:cd17649 196 LQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEatvTPLVWKCEAGAARAGASMpiGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 389 AHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD--------FWLMGD--RGIKDpeGYFH 458
Cdd:cd17649 275 GGRSAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDlaRWRDD--GVIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 459 FIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVkAFVVL-APEFLSHDRDQLTKvlqeHV 537
Cdd:cd17649 348 YLGRVDHQVKIRG-----FRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQLRT----AL 417
|
490 500 510
....*....|....*....|....*....|...
gi 295789127 538 KSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd17649 418 RASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
281-562 |
2.24e-31 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 124.34 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 GACIFVhllPKFDSQTVLKVLSSYPI-NTLVGAPIIYRML-----LQQDLSSYKFPhlhSCFSGGETLLPETLENWKAKT 354
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCtHAFLLPPTIDQIVelnadGLYDLSSLRSS---PAAPEWNDMATVDTSPWGRKP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 355 GLeireiYGQTETGlicrvsrTMKVKPGYLGTAFAHY-------DVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGM--FS 425
Cdd:cd17636 141 GG-----YGQTEVM-------GLATFAALGGGAIGGAgrpsplvQVRILDEDGREVPDGEVGEIVAR-------GPtvMA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 426 GYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDP 505
Cdd:cd17636 202 GYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAE-----NIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 295789127 506 SRGEVVKAFVVLAPEfLSHDRDQLTkvlqEHVKSVTAPYKYPRKVEFVLDLPKTVTG 562
Cdd:cd17636 277 RWAQSVKAIVVLKPG-ASVTEAELI----EHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
81-569 |
2.28e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 127.02 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 160
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 161 DEVAQEVDAVAPdcsflkIKLLVSENSREGwlnfkalLKEASTihqcvETESRESAAIYFTSGTSGPPKMAEHSHCSL-G 239
Cdd:cd12116 92 DALPDRLPAGLP------VLLLALAAAAAA-------PAAPRT-----PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLvN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKAKMDAAswTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACifVHLLPK---FDSQTVLKVLSSYPINTLVGAPIIY 316
Cdd:cd12116 154 FLHSMRER--LGLGPGDRLLAVTTYAFDISLLELLL-PLLAGAR--VVIAPRetqRDPEALARLIEAHSITVMQATPATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 317 RMLLQQDLSsyKFPHLHS-CfsGGETLLPETLENWKAKTGlEIREIYGQTET---GLICRVSRTMKVKPgyLGTAFAHYD 392
Cdd:cd12116 229 RMLLDAGWQ--GRAGLTAlC--GGEALPPDLAARLLSRVG-SLWNLYGPTETtiwSTAARVTAAAGPIP--IGRPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLMGDRGIKDPEGYFHFIGRSD 464
Cdd:cd12116 302 VYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 465 DIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVkAFVVLApEFLSHDRDQLTKVLQEHVKSVTAPY 544
Cdd:cd12116 377 GQVKIRG-----HRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLK-AGAAPDAAALRAHLRATLPAYMVPS 449
|
490 500
....*....|....*....|....*.
gi 295789127 545 KYprkveFVLD-LPKTVTGKIERAKL 569
Cdd:cd12116 450 AF-----VRLDaLPLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
218-566 |
3.21e-31 |
|
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: 123.67 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 218 IYFTSGTSGPPKMAEHSHcslgikakmdaASWTG--LSTSDIIWTISDTAwiMNILGAFLEPWVLGACIF-------VHL 288
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSE-----------RSWIEsfVCNEDLFNISGEDA--ILAPGPLSHSLFLYGAISalylggtFIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 289 LPKFDSQTVLKVLSSYPINTLVGAPiiyrMLLQQdLSSYKFPHLH--SCFSGGETLLPETLENWKAKT-GLEIREIYGQT 365
Cdd:cd17633 72 QRKFNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESKikSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 366 ETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGnvlppGKEGDIAIRVKPiwpigMFSGYVDNPKKTQDNirgdfWL- 444
Cdd:cd17633 147 ELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEM-----VFSGYVRGGFSNPDG-----WMs 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLapeflsh 524
Cdd:cd17633 212 VGDIGYVDEEGYLYLVGRESDMIIIGG-----INIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 295789127 525 drDQLT-KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:cd17633 280 --DKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
49-566 |
4.08e-31 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 127.31 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 49 DVIDHwasveKAGKRSSGPALWWmngSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMR 128
Cdd:PRK05852 20 DLVEV-----AATRLPEAPALVV---TADRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 129 TGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCV 208
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 209 ETESR-ESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIiwtisdTAWIM------NILGAFLEPWVLG 281
Cdd:PRK05852 171 PEGLRpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDA------TVAVMplyhghGLIAALLATLASG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 282 ACIfvhLLP---KFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ---DLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 355
Cdd:PRK05852 244 GAV---LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 356 LEIREIYGQTET----------GLICrvSRTMKVKPGYLGTAFAhYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFS 425
Cdd:PRK05852 321 APVVCAFGMTEAthqvtttqieGIGQ--TENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTV-----VR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 426 GYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPD 504
Cdd:PRK05852 393 GYLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGE-----KISPERVEGVLASHPNVMEAAVFGVPD 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789127 505 PSRGEVVKAfVVLAPEFLSHDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:PRK05852 467 QLYGEAVAA-VIVPRESAPPTAEELVQFCRERL----AAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
81-571 |
5.94e-31 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 128.82 E-value: 5.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtI-----QMRssdILYRLQASKAR 155
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--LdpaypAER---LAYMLEDAGAR 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVAPDCsflkikLLVSEnsregwlnfkALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 235
Cdd:COG1020 576 LVLTQSALAARLPELGVPV------LALDA----------LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 CSLG--IkakMDAASWTGLSTSDII---WTIS-DTAwIMNILGAFLepwvLGACifVHLLPK---FDSQTVLKVLSSYPI 306
Cdd:COG1020 640 RALVnlL---AWMQRRYGLGPGDRVlqfASLSfDAS-VWEIFGALL----SGAT--LVLAPPearRDPAALAELLARHRV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 307 NTLVGAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKT-GLEIREIYGQTETGLICRVSRTMKVKPGY-- 383
Cdd:COG1020 710 TVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGgs 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 --LGTAFAHYDVQVIDEQGNVLPPGKEGDIAI------RvkpiwpigmfsGYVDNPKKTQDN-IRGDFWL----M---GD 447
Cdd:COG1020 788 vpIGRPIANTRVYVLDAHLQPVPVGVPGELYIggaglaR-----------GYLNRPELTAERfVADPFGFpgarLyrtGD 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 448 RGIKDPEGYFHFIGRSDD---IinssgayfcR-YRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfls 523
Cdd:COG1020 857 LARWLPDGNLEFLGRADDqvkI---------RgFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG--- 924
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 295789127 524 hdRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:COG1020 925 --AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
67-578 |
7.90e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 126.33 E-value: 7.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 67 PALWWmngsgKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfMPGTIQMRSSDIL 146
Cdd:PRK07867 20 RGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIV-PVGLNPTRRGAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 147 YR-LQASKARAIVAGDEVAQEVDAVAPDCSFLKIkllvsenSREGWLNFKALLKEASTIHQCVETESResAAIYFTSGTS 225
Cdd:PRK07867 94 ARdIAHADCQLVLTESAHAELLDGLDPGVRVINV-------DSPAWADELAAHRDAEPPFRVADPDDL--FMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 226 GPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWtISDTAWIMN-ILGAFLEPWVLGACIfvHLLPKFDSQTVLKVLSSY 304
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQRF-GLGPDDVCY-VSMPLFHSNaVMAGWAVALAAGASI--ALRRKFSASGFLPDVRRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 305 PIN--TLVGAPIIYRmllqqdLSSYKFPH-----LHSCFsGGETLlPETLENWKAKTGLEIREIYGQTETGLIcrVSRTM 377
Cdd:PRK07867 241 GATyaNYVGKPLSYV------LATPERPDdadnpLRIVY-GNEGA-PGDIARFARRFGCVVVDGFGSTEGGVA--ITRTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 378 KVKPGYLGTAFAhyDVQVID-EQGNVLPPGkEGDIAIRVKPIWPIG---------MFSGYVDNPKKTQDNIRGDFWLMGD 447
Cdd:PRK07867 311 DTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEADAERMRGGVYWSGD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 448 RGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP--EFlshD 525
Cdd:PRK07867 388 LAYRDADGYAYFAGRLGDWMRVDGE-----NLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgaKF---D 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 295789127 526 RDQLTKVLqeHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 578
Cdd:PRK07867 460 PDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCAD 510
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-569 |
3.41e-30 |
|
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: 123.92 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP---GTIQMRSSDILyrlqASKARAIV 158
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPldpGYPADRLAYML----ADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 AGDEVAQEVDAVAPDcsflkIKLLVSEnsregwlnfkALLKEASTIHQcVETESRESAAIYFTSGTSGPPK--MAEHS-- 234
Cdd:cd17646 100 LTTADLAARLPAGGD-----VALLGDE----------ALAAPPATPPL-VPPRPDNLAYVIYTSGSTGRPKgvMVTHAgi 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 235 -------HCSLGIKAKMDAASWTGLStSDI-IWTisdtawimnilgaFLEPWVLGACIFV-----HLLPKFdsqtVLKVL 301
Cdd:cd17646 164 vnrllwmQDEYPLGPGDRVLQKTPLS-FDVsVWE-------------LFWPLVAGARLVVarpggHRDPAY----LAALI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 302 SSYPINTLVGAPIIYRMLLQQDLSSyKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL---ICRVSRTMK 378
Cdd:cd17646 226 REHGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvtHWPVRGPAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 379 VKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIK 451
Cdd:cd17646 305 TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALTAERFVPDpfgpgsrMYRTGDLARW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 452 DPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQltk 531
Cdd:cd17646 380 RPDGALEFLGRSDDQVKIRG-----FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA--- 451
|
490 500 510
....*....|....*....|....*....|....*....
gi 295789127 532 vLQEHVKSVTAPYKYPrKVEFVLD-LPKTVTGKIERAKL 569
Cdd:cd17646 452 -LRAHLAERLPEYMVP-AAFVVLDaLPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
80-569 |
7.16e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 123.08 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 159
Cdd:cd12117 22 SLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GDEVAQEVDAVAPDcsflkikLLVSENSREGwlnfkallkEASTIHQCVETESResAAIYFTSGTSGPPK--MAEHShcs 237
Cdd:cd12117 101 DRSLAGRAGGLEVA-------VVIDEALDAG---------PAGNPAVPVSPDDL--AYVMYTSGSTGRPKgvAVTHR--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 lGIKAKMDAASWTGLSTSDIIWTISDTAW---IMNILGAFLEpwvlGACifVHLLPK---FDSQTVLKVLSSYPINTL-V 310
Cdd:cd12117 160 -GVVRLVKNTNYVTLGPDDRVLQTSPLAFdasTFEIWGALLN----GAR--LVLAPKgtlLDPDALGALIAEEGVTVLwL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 311 GAPIiYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKT-GLEIREIYGQTETGLicrVSRTMKVKPGYL----- 384
Cdd:cd12117 233 TAAL-FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTT---FTTSHVVTELDEvagsi 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 385 --GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGD---FWLMGDRGIKDPEG 455
Cdd:cd12117 307 piGRPIANTRVYVLDEDGRPVPPGVPGELYVG-----GDGLALGYLNRPALTAerfvADPFGPgerLYRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 456 YFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPD-PSRGEVVkAFVVLAPEfLSHDRdqltkvLQ 534
Cdd:cd12117 382 RLEFLGRIDDQVKIRG-----FRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-AYVVAEGA-LDAAE------LR 448
|
490 500 510
....*....|....*....|....*....|....*
gi 295789127 535 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd12117 449 AFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
82-571 |
7.83e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 123.74 E-value: 7.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWW--LMILGCMrtGLVFMPGTIQMRSSDILYRLQASKARAIVA 159
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GDEVAQEVDAVAPDCSFLKIKLLVSENS--------REGW--LNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPK 229
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDadsaaahmPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 MAEHSHCSLGIKAkmdaaswTGLSTSDIIWTISDTAW-----IMNIL--GAFLEPWVLGACIfVHLLPKFDSQTVLKVLS 302
Cdd:PRK05620 198 GVVYSHRSLYLQS-------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGTPL-VFPGPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTmkvKP 381
Cdd:PRK05620 270 TAMPRVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 GYLGTAFAHYDV-----------QVIDEqGNVLPPGKEGDIAIRVKPIWPIGmfsGYVDNPKKTQDN----IRG------ 440
Cdd:PRK05620 347 GVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTDRNEGEIQVRGNWVTA---SYYHSPTEEGGGaastFRGedveda 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 441 ------DFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKA 513
Cdd:PRK05620 423 ndrftaDGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEW-----IYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 514 FVVLAP--EFLSHDRDQLTKVLQEHVKSVTAPYKYprkvEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK05620 498 VTVLAPgiEPTRETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
69-570 |
8.25e-29 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 121.54 E-value: 8.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 69 LWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYR 148
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 149 LQASKARAIVAGDEVAQEVDAVapdcsFLK--IKLLVSENSREG--------WLNFKALLKEASTIHQ------------ 206
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTI-----NLKdiVDAALDESAKNGvsvgicltYENQLAMKREDTKWQEgrdvwwqdvvpn 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 207 ----C-VE-TESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVL 280
Cdd:PLN02654 263 yptkCeVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 GACIFV-HLLPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETLLPETLE---NWKA 352
Cdd:PLN02654 343 GATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRwffNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 353 KTGLEIREIYGQTETG--LICRVSRTMKVKPGylGTAFAHYDVQ--VIDEQGNVLppgkEGDIA--IRVKPIWPIGMFSG 426
Cdd:PLN02654 423 DSRCPISDTWWQTETGgfMITPLPGAWPQKPG--SATFPFFGVQpvIVDEKGKEI----EGECSgyLCVKKSWPGAFRTL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 427 YVDNPKKTQDNIR--GDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPD 504
Cdd:PLN02654 497 YGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSG-----HRIGTAEVESALVSHPQCAEAAVVGIEH 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 505 PSRGEVVKAFVVLApEFLSHDrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PLN02654 572 EVKGQGIYAFVTLV-EGVPYS-EELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
79-572 |
9.07e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 120.72 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 79 IKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIV 158
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 AGDEV------AQEVDAVAPDCSFLKIKLLVSENSREGWLNFK-ALLKEASTIHQCVETESRE-----------SAAIYF 220
Cdd:PLN02479 123 VDQEFftlaeeALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQyALGKGAIEYEKFLETGDPEfawkppadewqSIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 221 TSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGA-CIFVHLLPKFDSQTVLK 299
Cdd:PLN02479 203 TSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLP-----MFHCNGWCFTWTLAAlCGTNICLRQVTAKAIYS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 300 VLSSYPINTLVGAPIIYRMLLQQDLSS--YKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTET---GLIC--- 371
Cdd:PLN02479 278 AIANYGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETygpSTVCawk 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 372 ------------RVSRTMKVKpgYLGTAfahyDVQVIDEQGNVLPP--GKE-GDIAIRVKpiwpiGMFSGYVDNPKKTQD 436
Cdd:PLN02479 357 pewdslppeeqaRLNARQGVR--YIGLE----GLDVVDTKTMKPVPadGKTmGEIVMRGN-----MVMKGYLKNPKANEE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 437 NIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVV 516
Cdd:PLN02479 426 AFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGE-----NISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVT 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 517 LAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVlDLPKTVTGKIERAKLRAK 572
Cdd:PLN02479 501 LKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
82-569 |
2.11e-28 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 118.58 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:cd17655 24 TYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDavapdcsFLK-IKLLVSENSREGwlnfkallkEASTIHqcVETESRESAAIYFTSGTSGPPK--MAEHS---- 234
Cdd:cd17655 103 HLQPPIA-------FIGlIDLLDEDTIYHE---------ESENLE--PVSKSDDLAYVIYTSGSTGKPKgvMIEHRgvvn 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 235 -HCSLGIKAKMDAASWTGLSTSdiiwtISDTAWIMNILGAFLepwvLGACIfvHLLPK---FDSQTVLKVLSSYPINTLV 310
Cdd:cd17655 165 lVEWANKVIYQGEHLRVALFAS-----ISFDASVTEIFASLL----SGNTL--YIVRKetvLDGQALTQYIRQNRITIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 311 GAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKTGL--EIREIYGQTETGL-----ICRVSRTMKVKPgY 383
Cdd:cd17655 234 LTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdasiyQYEPETDQQVSV-P 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD-------PEGY 456
Cdd:cd17655 311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDDPFVPGERMYRTgdlarwlPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 457 FHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD-RDQLTKVLQE 535
Cdd:cd17655 386 IEFLGRIDHQVKIRG-----YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQlREFLARELPD 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 295789127 536 hvksvtapYKYPRKveFV-LD-LPKTVTGKIERAKL 569
Cdd:cd17655 461 --------YMIPSY--FIkLDeIPLTPNGKVDRKAL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
82-570 |
1.70e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 116.86 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM-------PGTIQMRSSDilyrlqASKA 154
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnpsssLGEIKKRVVD------CSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQevdavapdCSFLKIK-LLVSENsregwLNFKALLKEASTIHQCVETES----------RESAAIYFTSG 223
Cdd:PLN02574 142 LAFTSPENVEK--------LSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEDFdfvpkpvikqDDVAAIMYSSG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 224 TSGPPKMAEHSH----CSLGIKAKMDAASWTGLSTSDI---------IWTISdtAWIMNILGaflepwvLGACIFVhlLP 290
Cdd:PLN02574 209 TTGASKGVVLTHrnliAMVELFVRFEASQYEYPGSDNVylaalpmfhIYGLS--LFVVGLLS-------LGSTIVV--MR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 291 KFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ--QDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTE- 366
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEs 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 367 TGLICRVSRTMKVKP-GYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL 444
Cdd:PLN02574 358 TAVGTRGFNTEKLSKySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 -MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlapefls 523
Cdd:PLN02574 433 rTGDIAYFDEDGYLYIVDRLKEIIKYKG-----FQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV------- 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 295789127 524 hdRDQLTKVLQE----HVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PLN02574 501 --RRQGSTLSQEavinYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
102-572 |
2.21e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 117.05 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 102 GLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAqevDAVAPDcSFLKIKL 181
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALR---DRFQPS-RVAEAAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 182 LVSENSREGWLNFKALLKEAStihqcvetesresAAIYFTSGTSGPPKMAEHSHC-------SLGIKAKMDAASWTGLST 254
Cdd:PRK06060 127 LMSEAARVAPGGYEPMGGDAL-------------AYATYTSGTTGPPKAAIHRHAdpltfvdAMCRKALRLTPEDTGLCS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 255 SDIIWT--ISDTAWImnilgaflePWVLGACIFVHLLPKfdSQTVLKVLSS-YPINTLVGAPIIYRMLLQQdLSSYKFPH 331
Cdd:PRK06060 194 ARMYFAygLGNSVWF---------PLATGGSAVINSAPV--TPEAAAILSArFGPSVLYGVPNFFARVIDS-CSPDSFRS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 332 LHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGD 410
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 411 IAIRVKPIwpigmFSGYVDNPKKTQDNirGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALME 490
Cdd:PRK06060 342 LWVRGPAI-----AKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV-----NVDPREVERLIIE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 491 HPAVSETAVISSPDPSRGEVVKAFVVLA-PEFLshDRDQLTKVLQEHVKSVTApYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:PRK06060 410 DEAVAEAAVVAVRESTGASTLQAFLVATsGATI--DGSVMRDLHRGLLNRLSA-FKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
...
gi 295789127 570 RAK 572
Cdd:PRK06060 487 RKQ 489
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-570 |
2.39e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 116.27 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 105 RGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDE---VAQEVDAVAP-DCSFLKIK 180
Cdd:PLN03102 63 KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfepLAREVLHLLSsEDSNLNLP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 181 -LLVSEN-------SREgwLNFKALLKEASTIHQ------CVETEsRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDA 246
Cdd:PLN03102 143 vIFIHEIdfpkrpsSEE--LDYECLIQRGEPTPSlvarmfRIQDE-HDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 247 ASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGA------CIFVHLLPKfdsqtVLKVLSSYPINTLVGAPIIYRMLL 320
Cdd:PLN03102 220 IGWEMGTCPVYLWTLP-----MFHCNGWTFTWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQDLS--SYKFPHLHsCFSGGETLlPETLENWKAKTGLEIREIYGQTE-TG--LICR-----------VSRTMKVKPGYL 384
Cdd:PLN03102 290 KGNSLdlSPRSGPVH-VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpenQQMELKARQGVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 385 GTAFAHYDVQVIDEQGNVLPPGKE-GDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRS 463
Cdd:PLN03102 368 ILGLADVDVKNKETQESVPRDGKTmGEIVIKGSSI-----MKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 464 DDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL--APEFLSHDRDQLT---KVLQEHVK 538
Cdd:PLN03102 443 KDIIISGGE-----NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLIEYCR 517
|
490 500 510
....*....|....*....|....*....|..
gi 295789127 539 SVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PLN03102 518 ENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
216-572 |
3.47e-27 |
|
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: 112.42 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLGIKAKMdAASWTGLSTSDiiwtisdtAWIMN-----ILG-AFLEPWVLGACIFVHLL 289
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAG-LHSRLGFGGGD--------SWLLSlplyhVGGlAILVRSLLAGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 PKFDsqtVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETGL 369
Cdd:cd17630 74 RNQA---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 370 ICRVSRTMKVKPGYLGTAFAHYDVQvIDEQGNVLPPGKegdiairvkpiwpiGMFSGYVDNPkkTQDNIRGDFWL-MGDR 448
Cdd:cd17630 150 QVATKRPDGFGRGGVGVLLPGRELR-IVEDGEIWVGGA--------------SLAMGYLRGQ--LVPEFNEDGWFtTKDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 449 GIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrdQ 528
Cdd:cd17630 213 GELHADGRLTVLGRADNMIISGG-----ENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-------A 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 295789127 529 LTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
82-570 |
3.71e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.88 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACglHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKE--SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevdavapdcsFLKIKLLVSENSREGWLNFKALL-KEASTIHQcveTESRESAAIY--FTSGTSGPPKMAEHSHcsl 238
Cdd:PRK07638 106 --------------YKLNDLPDEEGRVIEIDEWKRMIeKYLPTYAP---IENVQNAPFYmgFTSGSTGKPKAFLRAQ--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 239 gikakmdaASWT-GLSTSDIIWTISDTAWIMnILGAFLEPWVLGACIF-------VHLLPKFDSQTVLKVLSSYPINTLV 310
Cdd:PRK07638 166 --------QSWLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLYGAIStlyvgqtVHLMRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 311 GAPIIYRMLLQQDlssyKFP-HLHSCFSGGETLLPETLEnwKAKTG---LEIREIYGQTETGLICR-VSRTMKVKPGYLG 385
Cdd:PRK07638 237 TVPTMLESLYKEN----RVIeNKMKIISSGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSFVTAlVDEESERRPNSVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 386 TAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPIwpigMFSGYV-DNPKKTQDNIRGdfWL-MGDRGIKDPEGYFHFIGRS 463
Cdd:PRK07638 311 RPFHNVQVRICNEAGEEVQKGEIGTVYVK-SPQ----FFMGYIiGGVLARELNADG--WMtVRDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 464 DDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVvlapeflshDRDQLTKVLQEHVKSVTAP 543
Cdd:PRK07638 384 KNMILFGG-----INIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSS 449
|
490 500
....*....|....*....|....*..
gi 295789127 544 YKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
82-570 |
4.12e-27 |
|
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: 113.94 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARaivagd 161
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGAT------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevdavapdcsflkikLLVSENSregwlnfkallkeastihqcveteSRESAAIYFTSGTSGPPK--MAEHShcslg 239
Cdd:cd17653 97 -------------------LLLTTDS------------------------PDDLAYIIFTSGSTGIPKgvMVPHR----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 ikakmdaaswtglSTSDIIWTISDT---------AWIMNIlgAFlepWVLGACIFV------HLLPKFDSQTVLKVLSSy 304
Cdd:cd17653 129 -------------GVLNYVSQPPARldvgpgsrvAQVLSI--AF---DACIGEIFStlcnggTLVLADPSDPFAHVART- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 305 pINTLVGAPIIYRMLLQQDlssykFPHLHSCFSGGETLLPETLENWKAktGLEIREIYGQTETGLICRVSRTMKVKPGYL 384
Cdd:cd17653 190 -VDALMSTPSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 385 GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQD----NIRGDFWLM---GDRGIKDPEGYF 457
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASkfvpDPFWPGSRMyrtGDYGRWTEDGGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 458 HFIGRSDDIINSSGayfcrYRIGPSEVENALM-EHPAVSETAVISSpdpsrGEVVKAFVvlAPEflSHDRDQLTKVLQEH 536
Cdd:cd17653 337 EFLGREDNQVKVRG-----FRINLEEIEEVVLqSQPEVTQAAAIVV-----NGRLVAFV--TPE--TVDVDGLRSELAKH 402
|
490 500 510
....*....|....*....|....*....|....
gi 295789127 537 VKSvtapYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd17653 403 LPS----YAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
76-566 |
6.37e-27 |
|
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: 114.08 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesRESAAIYFTSGTSGPPK--MAEH 233
Cdd:cd05914 82 AIFVSDE--------------------------------------------------DDVALINYTSGTTGNSKgvMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 234 SHcslgIKAKMDAASWTGLST-SDIIWTISDTAWIMNILGAFLEPWVLGACIfvHLLPKFDSQTVLKvLSSYPINTLVGA 312
Cdd:cd05914 112 RN----IVSNVDGVKEVVLLGkGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKIPSAKIIA-LAFAQVTPTLGV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 313 PI------IYRMLLQQDLSSYK------------------FPHLHSCF--------SGGETLLPETLENWKaKTGLEIRE 360
Cdd:cd05914 185 PVplviekIFKMDIIPKLTLKKfkfklakkinnrkirklaFKKVHEAFggnikefvIGGAKINPDVEEFLR-TIGFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQgnvlPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRG 440
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 441 DFWL-MGDRGIKDPEGYFHFIGRSDD-IINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSrgevvKAFVVLA 518
Cdd:cd05914 335 DGWFhTGDLGKIDAEGYLYIRGRKKEmIVLSSGK-----NIYPEEIEAKINNMPFVLESLVVVQEKKL-----VALAYID 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 519 PEFLS----HDRDQLTKVLQEHVKSV---TAPYKYPRKVEFVL-DLPKTVTGKIER 566
Cdd:cd05914 405 PDFLDvkalKQRNIIDAIKWEVRDKVnqkVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
80-572 |
1.57e-26 |
|
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: 113.67 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW-WLMI----LGCMRTGLV--FMPgtiqmrsSDILYRLQAS 152
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWvWAELaaqaIGALSLGIYqdSMA-------EEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 153 KARAIVAGDEvaQEVDAV---APDCSFLKIKLLVSE----NSREGWLN-FKALLKEASTIHQ---------CVETESRES 215
Cdd:cd17641 83 GARVVIAEDE--EQVDKLleiADRIPSVRYVIYCDPrgmrKYDDPRLIsFEDVVALGRALDRrdpglyereVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI----------- 284
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnfpeepetmme 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 285 --------FVHLLPK----FDSQTVLKVLSSYPINTLV-------------------------------GAPIIYRMLLQ 321
Cdd:cd17641 240 dlreigptFVLLPPRvwegIAADVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 322 QdlssYKFPHLHSCFSGGETLLPETLENWKAkTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQvIDEQGN 401
Cdd:cd17641 320 R----LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR-IDEVGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 402 VLPPGKegdiairvkpiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDIINSSGAyfcrYRIG 480
Cdd:cd17641 394 ILVRSP--------------GVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSDG----TRFS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 481 PSEVENALMEHPAVSETAVISSPDPsrgeVVKAFVVLAPEFLSH----------------DRDQLTKVLQEHVKSVTAPY 544
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLGAGRP----YLTAFICIDYAIVGKwaeqrgiafttytdlaSRPEVYELIRKEVEKVNASL 531
|
570 580 590
....*....|....*....|....*....|....*..
gi 295789127 545 KYPRKVEFVLDLPK---------TVTGKIERAKLRAK 572
Cdd:cd17641 532 PEAQRIRRFLLLYKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
216-571 |
5.27e-26 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 112.20 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLGIK--AKMDAAswtGLSTSDIIWTISDTAWIMNILGAfLEPWVLGACifvH-LLPKF 292
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQslAKIAIV---GYGEDDVYLHTAPLCHIGGLSSA-LAMLMVGAC---HvLLPKF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 293 DSQTVLKVLSSYPINTLVGAPIIYRMLL---QQDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETg 368
Cdd:PLN02860 248 DAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAkKLFPNAKLFSAYGMTEA- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 369 liCRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPP-----GKEG---------DIAIRVKPIWPIG--MFSGYVDNPK 432
Cdd:PLN02860 327 --CSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPqgvcvGKPAphvelkiglDESSRVGRILTRGphVMLGYWGQNS 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 433 KTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVV 511
Cdd:PLN02860 405 ETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGE-----NVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMV 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295789127 512 KAFVVLAPEFL-SHDRDQLTK--------VLQEHV--KSVTApYKYPRKveFVL---DLPKTVTGKIERAKLRA 571
Cdd:PLN02860 480 VACVRLRDGWIwSDNEKENAKknltlsseTLRHHCreKNLSR-FKIPKL--FVQwrkPFPLTTTGKIRRDEVRR 550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-569 |
9.08e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.13 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAQEVDAVApdcsflKIKLLVSENSREgWLNFKALLKEastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCS 237
Cdd:PRK12316 4653 LTQSHLLQRLPIPD------GLASLALDRDED-WEGFPAHDPA-------VRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 LgikakMDAASWTG----LSTSDIIWTISDTAWIMNILGAFLePWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAP 313
Cdd:PRK12316 4719 L-----VNHLHATGeryeLTPDDRVLQFMSFSFDGSHEGLYH-PLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 314 IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETL-ENWKAKTGLEIREIYGQTETGLicrVSRTMKVKPGY--------L 384
Cdd:PRK12316 4793 VYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYdLAWRALKPVYLFNGYGPTETTV---TVLLWKARDGDacgaaympI 4869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 385 GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ--------DNIRGDFWLMGDRGIKDPEGY 456
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAerfvpdpfGAPGGRLYRTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 457 FHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQ--LTKVLQ 534
Cdd:PRK12316 4945 IDYLGRVDHQVKIRG-----FRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELK 5019
|
490 500 510
....*....|....*....|....*....|....*
gi 295789127 535 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:PRK12316 5020 AALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
80-570 |
9.42e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 111.34 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLsGACGLHRGDRVAVVlpripEW-----WLMILGCMRTGLVFMpgTIQMR--SSDILYRLQAS 152
Cdd:PRK07008 39 RYTYRDCERRAKQLAQAL-AALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCH--TINPRlfPEQIAYIVNHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 153 KARAIVAGDEVAQEVDAVAPDCSFLKikllvsensreGW--LNFKALLKEASTIHQCVET--------------ESRESA 216
Cdd:PRK07008 111 EDRYVLFDLTFLPLVDALAPQCPNVK-----------GWvaMTDAAHLPAGSTPLLCYETlvgaqdgdydwprfDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 217 AIYFTSGTSGPPKMAEHSHCSLGIKAKMDA-ASWTGLSTSDIIWTISD----TAWIMNILGAflepwvLGACIFVHLLPK 291
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVLHAYGAAlPDAMGLSARDAVLPVVPmfhvNAWGLPYSAP------LTGAKLVLPGPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 292 FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET--- 367
Cdd:PRK07008 254 LDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMspl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 368 GLICRV-----SRTMKVKPGYL---GTAFAHYDVQVIDEQGNVLP-PGKE-GDIAIRvKPiWPIgmfSGYVdnpKKTQDN 437
Cdd:PRK07008 334 GTLCKLkwkhsQLPLDEQRKLLekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR-GP-WVI---DRYF---RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 438 IRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL 517
Cdd:PRK07008 406 LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEW-----ISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVK 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 295789127 518 APEFlSHDRDQLTKvlqeHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK07008 481 RPGA-EVTREELLA----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
82-569 |
1.71e-25 |
|
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: 109.26 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVagd 161
Cdd:cd17652 14 TYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSH-CSL 238
Cdd:cd17652 90 ------------------------------------------------TTPDNLAYVIYTSGSTGRPKgvVVTHRGlANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 239 gIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEpwvlGACifVHLLPKFDS---QTVLKVLSSYPINTLVGAPII 315
Cdd:cd17652 122 -AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLA----GAT--LVLAPAEELlpgEPLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 316 YRMLLQQDLssykfPHLHSCFSGGETLLPETLENWKakTGLEIREIYGQTETGL---ICRVSRTMKVKPgyLGTAFAHYD 392
Cdd:cd17652 195 LAALPPDDL-----PDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTVcatMAGPLPGGGVPP--IGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLMGDRGIKDPEGYFHFIGRSD 464
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 465 DIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflshDRDQLTKVLQEHVKSVTAPY 544
Cdd:cd17652 341 DQVKIRG-----FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGY 410
|
490 500
....*....|....*....|....*.
gi 295789127 545 KYPRKVeFVLD-LPKTVTGKIERAKL 569
Cdd:cd17652 411 MVPAAF-VVLDaLPLTPNGKLDRRAL 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
82-569 |
4.39e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 108.93 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK13383 62 SYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVdAVAPDcsflkiKLLVSENSREGwlnfkallKEASTIHQCVETESResaAIYFTSGTSGPPKmaehshcslGIK 241
Cdd:PRK13383 141 EFAERI-AGADD------AVAVIDPATAG--------AEESGGRPAVAAPGR---IVLLTSGTTGKPK---------GVP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWTGLSTSDIIWTISDTAWIMNI---------LGAFLEPWVLGACIFVHllPKFDSQTVLKVLSSYPINTLVGA 312
Cdd:PRK13383 194 RAPQLRSAVGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH--RHFDAEAALAQASLHRADAFTAV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 313 PIIYRMLLQ---QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL-ICRVSRTMKVKPGYLGTAF 388
Cdd:PRK13383 272 PVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 389 AHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGMFSG--YVDNP-KKTQDNIRGdfwlMGDRGIKDPEGYFHFIGRSDD 465
Cdd:PRK13383 352 AGCPVRILDRNNRPVGPRVTGRIFVG-------GELAGtrYTDGGgKAVVDGMTS----TGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 466 IINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYK 545
Cdd:PRK13383 421 MIISGGE-----NVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFE 490
|
490 500
....*....|....*....|....
gi 295789127 546 YPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
76-542 |
5.20e-25 |
|
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: 108.71 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 76 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 155
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAG---DEVAQEvdAVAPDCSFLKIKLLVSE-NSREGWlnfKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMA 231
Cdd:cd05932 81 ALFVGkldDWKAMA--PGVPEGLISISLPPPSAaNCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 EHSHCSLGIKAKMdAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI-FVHLLPKF--DSQ----TVL------ 298
Cdd:cd05932 156 MLTFGSFAWAAQA-GIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVaFAESLDTFveDVQrarpTLFfsvprl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 299 ------KVLSSYP---INTLVGAPIIYRMLLQQDLSSYKFPHLHsCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL 369
Cdd:cd05932 235 wtkfqqGVQDKIPqqkLNLLLKIPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 370 ICRVSRTMKVKPGYLGTAFAhyDVQV-IDEQGNVLppgkegdiaIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGD 447
Cdd:cd05932 314 YSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL---------VRSP-----ALMMGYYKDPEATAEAFTADGFLrTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 448 RGIKDPEGYFHFIGRSDDIINSS-GAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDR 526
Cdd:cd05932 378 KGELDADGNLTITGRVKDIFKTSkGKY-----VAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAFAR 452
|
490
....*....|....*.
gi 295789127 527 DQLTKVLQEHVKSVTA 542
Cdd:cd05932 453 AELEASLRAHLARVNS 468
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
78-569 |
6.08e-25 |
|
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: 108.13 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAGDEVAQEVDAVAPDcsflkikllvsensregwLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHcs 237
Cdd:cd12114 89 LTDGPDAQLDVAVFDV------------------LILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISH-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 lgikakmDAASWT--------GLSTSDIIWTISDTAWIM---NILGAFlepwVLGACIfvhLLP----KFDSQTVLKVLS 302
Cdd:cd12114 149 -------RAALNTildinrrfAVGPDDRVLALSSLSFDLsvyDIFGAL----SAGATL---VLPdearRRDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPIIYRMLLQQDLSSYKFPH-----LHScfsgGETL---LPETLenWKAKTGLEIREIYGQTETGL----- 369
Cdd:cd12114 215 RHGVTLWNSVPALLEMLLDVLEAAQALLPslrlvLLS----GDWIpldLPARL--RALAPDARLISLGGATEASIwsiyh 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 370 -ICRVSRTMKVKPgYlGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ-----DNIRGDFW 443
Cdd:cd12114 289 pIDEVPPDWRSIP-Y-GRPLANQRYRVLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAarfvtHPDGERLY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 444 LMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVLAPEFLS 523
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKVRG-----YRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTP 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 295789127 524 HDRDQLTKVLQEHVKSvtapYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd12114 436 IAPDALRAFLAQTLPA----YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
483-563 |
7.71e-25 |
|
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: 98.00 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 483 EVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTG 562
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 295789127 563 K 563
Cdd:pfam13193 76 K 76
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
81-576 |
4.28e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 106.26 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRE-LSEASKQTAnvlsGACGLHRGDR---VAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARA 156
Cdd:PRK13388 27 WTWREvLAEAAARAA----ALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 IVAGDEVAQEVDAVA-PDcsflkIKLLVSENSRegwlnFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 235
Cdd:PRK13388 103 LVTDAEHRPLLDGLDlPG-----VRVLDVDTPA-----YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 CSLGIKAKMDAASWtGLSTSDIIWtISDTAWIMNILGAFLEPWVL-GACifVHLLPKFDSQTVLKVLSSYPIN--TLVGA 312
Cdd:PRK13388 173 GRLAFAGRALTERF-GLTRDDVCY-VSMPLFHSNAVMAGWAPAVAsGAA--VALPAKFSASGFLDDVRRYGATyfNYVGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 313 PIIYRMLLQQDLSSYKFPhLHSCFsgGETLLPETLENWKAKTGLEIREIYGQTETGliCRVSRTMKVKPGYLGTAF---A 389
Cdd:PRK13388 249 PLAYILATPERPDDADNP-LRVAF--GNEASPRDIAEFSRRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGApgvA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 390 HYD--------VQVIDEQGNVLPPGKE-GDIAIRVKPiwpiGMFSGYVDNPKKTQDNIR-GDFWlMGDRGIKDPEGYFHF 459
Cdd:PRK13388 324 IYNpetltecaVARFDAHGALLNADEAiGELVNTAGA----GFFEGYYNNPEATAERMRhGMYW-SGDLAYRDADGWIYF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 460 IGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP----------EFLSHDRDQL 529
Cdd:PRK13388 399 AGRTADWMRVDGE-----NLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDgatfdpdafaAFLAAQPDLG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 295789127 530 TKVlqehvksvtapykYPRKVEFVLDLPKTVTGKIERAKLRAKEWKT 576
Cdd:PRK13388 474 TKA-------------WPRYVRIAADLPSTATNKVLKRELIAQGWAT 507
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
207-571 |
1.95e-23 |
|
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: 103.95 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 207 CVETESRESAAIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAaswtglSTSDIIwtisdtawiMNIL---------G 272
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP------NPEDVV---------FGALpffhsfgltG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 273 AFLEPWVLGACIFVHLLPkFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQdLSSYKFPHLHSCFSGGETLLPETLENWKA 352
Cdd:cd05909 206 CLWLPLLSGIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 353 KTGLEIREIYGQTETGLICRVSR-TMKVKPGYLGTAFAHYDVQVIDEQGNV-LPPGKEGDIAIRVKPIwpigmFSGYVDN 430
Cdd:cd05909 284 KFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNV-----MLGYLNE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 431 PKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRsddiinssgayFCRY-RIGP-----SEVENALMEH-PAVSETAVISSP 503
Cdd:cd05909 359 PELTSFAFGDGWYDTGDIGKIDGEGFLTITGR-----------LSRFaKIAGemvslEAIEDILSEIlPEDNEVAVVSVP 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295789127 504 DPSRGEVVKAFVVLapeflsHDRDQLTkvLQEHVKSVTAPYKY-PRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:cd05909 428 DGRKGEKIVLLTTT------TDTDPSS--LNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
80-569 |
3.28e-23 |
|
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: 102.63 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 159
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHS--- 234
Cdd:cd17645 101 --------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHHnlv 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 235 ------HCSLGIKAKMDAASWTGLSTSDIIWTISDTawimnilgaflepWVLGACifVHLLP---KFDSQTVLKVLSSYP 305
Cdd:cd17645 131 nlcewhRPYFGVTPADKSLVYASFSFDASAWEIFPH-------------LTAGAA--LHVVPserRLDLDALNDYFNQEG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 306 INTLVGAPIIYRMLLQQDLSSykfphLHSCFSGGETLlpetleNWKAKTGLEIREIYGQTEtgliCRVSRTM-KVKPGY- 383
Cdd:cd17645 196 ITISFLPTGAAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYa 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 ---LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD-------P 453
Cdd:cd17645 261 nipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 454 EGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlAPEFLSHDRdqltkvL 533
Cdd:cd17645 336 DGNIEFLGRLDQQVKIRG-----YRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEIPHEE------L 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 295789127 534 QEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-570 |
7.49e-23 |
|
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: 102.12 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VagdeVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVE-TESRESAAIYFTSGTSGPPKMAEHSH- 235
Cdd:cd05915 101 L----FDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 ------CSLGIKAKMDAASWTGLSTSDIIWTISDTAWImnilgaflepWVLGAC--IFVHLLPKFDSQTVLKVLSSYPIN 307
Cdd:cd05915 177 alvlhsLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP----------YAATLVgaKQVLPGPRLDPASLVELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTET---GLIC-----------R 372
Cdd:cd05915 247 FTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNfvkshleslseE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 373 VSRTMKVKPGYLGTAFAhydVQVIDEQGNVLP-PGKegdiAIRVKPIWPIGMFSGYVDNPKKTQ-DNIRGDFWLMGDRGI 450
Cdd:cd05915 326 EKLTLKAKTGLPIPLVR---LRVADEEGRPVPkDGK----ALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 451 KDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflSHDRDQlt 530
Cdd:cd05915 399 WDEEGYVEIKDRLKDLIKSGGEW-----ISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG---EKPTPE-- 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 295789127 531 KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05915 469 ELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
82-570 |
4.12e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 100.21 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVV---LPRIPEWWLmilGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIV 158
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWY---GIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 AGDEVAQEVDAVAPDCSFLKIKLLVS------ENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAE 232
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTdaahmpQTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 233 HSHCSLGIKAKM----DAaswTGLSTSDIIWTI----SDTAWIMnilgAFLEPWVlGACIfVHLLPKFDSQTVLKVLSSY 304
Cdd:PRK06018 197 YSHRSNVLHALManngDA---LGTSAADTMLPVvplfHANSWGI----AFSAPSM-GTKL-VMPGAKLDGASVYELLDTE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 305 PINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRVSrtmKVKPGY 383
Cdd:PRK06018 268 KVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLGTLA---ALKPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 LGT------------AFAHYDVQ--VIDEQGNVLPpgKEGDIAIRVKPIWPIgMFSGYVdnpkKTQDNIRGD--FWLMGD 447
Cdd:PRK06018 344 SKLpgdarldvlqkqGYPPFGVEmkITDDAGKELP--WDGKTFGRLKVRGPA-VAAAYY----RVDGEILDDdgFFDTGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 448 RGIKDPEGYFHFIGRSDDIINSSGAYfcryrIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRD 527
Cdd:PRK06018 417 VATIDAYGYMRITDRSKDVIKSGGEW-----ISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG-ETATRE 490
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 295789127 528 QLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK06018 491 EILKYMDGKI----AKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-563 |
4.32e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 98.22 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 290 PKFDSQTVLKVLSSYPIN--TLVG----APII--YRMLLQQDLSSykfphLHSCFSGGETLLPETLENW-KAKTGLEIRE 360
Cdd:cd05924 91 DRFDPEEVWRTIEKHKVTsmTIVGdamaRPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETG-LICRVSRTMKVKPGYLgtAFAHYDVQVIDEQGNVLPPGKE--GDIAIR-VKPIwpigmfsGYVDNPKKTQ- 435
Cdd:cd05924 166 AFGSSETGfTGSGHSAGSGPETGPF--TRANPDTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYGDEAKTAe 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 436 -----DNIRgdFWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEV 510
Cdd:cd05924 237 tfpevDGVR--YAVPGDRATVEADGTVTLLGRGSVCINTGGE-----KVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 295789127 511 VKAFVVLAPEFlSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGK 563
Cdd:cd05924 310 VVAVVQLREGA-GVDLEE----LREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
82-569 |
4.59e-22 |
|
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: 99.30 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVagd 161
Cdd:cd17643 14 TYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSHCSLG 239
Cdd:cd17643 90 ------------------------------------------------TDPDDLAYVIYTSGSTGRPKgvVVSHANVLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKAkmdAASWTGLSTSDIIWTISDTA-----WimNILGAFL--------EPWVLGACIFVHLLPKFDSQTVLKvlssypi 306
Cdd:cd17643 122 FAA---TQRWFGFNEDDVWTLFHSYAfdfsvW--EIWGALLhggrlvvvPYEVARSPEDFARLLRDEGVTVLN------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 307 ntlvGAPIIYRMLLQQDLSSYKFPH-LHSCFSGGETLLPETLENWKAKTGL---EIREIYGQTETglicRVSRTMK-VKP 381
Cdd:cd17643 190 ----QTPSAFYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET----TVHVTFRpLDA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 GYL--------GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-FWLMGDRGIKD 452
Cdd:cd17643 262 ADLpaaaaspiGRPLPGLRVYVLDADGRPVPPGVVGELYVS-----GAGVARGYLGRPELTAERFVANpFGGPGSRMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 453 -------PEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshd 525
Cdd:cd17643 337 gdlarrlPDGELEYLGRADEQVKIRG-----FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG----- 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 295789127 526 RDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17643 407 AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
58-571 |
6.64e-22 |
|
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: 99.15 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 58 EKAGKRSSGPALW-WmngsgkEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPewWLM--ILGCMRTGLVFM 134
Cdd:cd05918 7 ERARSQPDAPAVCaW------DGSLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSK--WAVvaMLAVLKAGGAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 135 PgtiqMRSSDILYRLQaskaraivagdEVAQEVDAvapdcsflkiKLLVSensregwlnfkallkeastihqcveteSRE 214
Cdd:cd05918 78 P----LDPSHPLQRLQ-----------EILQDTGA----------KVVLT---------------------------SSP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 215 SAAIY--FTSGTSGPPK--MAEHSHCSLGIKAKMDAaswTGLSTSD-------IIWTISdtawIMNILGAflepWVLGAC 283
Cdd:cd05918 106 SDAAYviFTSGSTGKPKgvVIEHRALSTSALAHGRA---LGLTSESrvlqfasYTFDVS----ILEIFTT----LAAGGC 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 284 IFVhlLPKFDSQTVL-KVLSSYPINTLVGAPIIYRMLLQQDlssykFPHLHSCFSGGETLLPETLENWKAKTGLeiREIY 362
Cdd:cd05918 175 LCI--PSEEDRLNDLaGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTWADRVRL--INAY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 363 GQTETGLICRVSR-TMKVKPGYLGTAF---AHydvqVIDEQGN--VLPPGKEGDIAIRvKPIwpIGmfSGYVDNPKKTQD 436
Cdd:cd05918 246 GPAECTIAATVSPvVPSTDPRNIGRPLgatCW----VVDPDNHdrLVPIGAVGELLIE-GPI--LA--RGYLNDPEKTAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 437 N-IRGDFWLM-------------GDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAV--- 499
Cdd:cd05918 317 AfIEDPAWLKqegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQ-----RVELGEIEHHLRQSLPGAKEVVvev 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 500 ISSPDPSRGEVVKAFVVLAPEFLSHDRDQ------------LTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERA 567
Cdd:cd05918 392 VKPKDGSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR 471
|
....
gi 295789127 568 KLRA 571
Cdd:cd05918 472 ALRE 475
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
284-573 |
7.01e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.18 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 284 IFVHLLPKFdsqtVLKVLSSYPINTLVGAP----IIYRMLLQQDlssykfpHLHSCFSGGeTLLPET-LENWKAKTgLEI 358
Cdd:PRK08308 173 IITNKNPKF----ALNILRNTPQHILYAVPlmlhILGRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERT-TYM 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 359 REIYGQTETGLICrVSRTMKvKPGYLGTAFAHYDVQVIDEQGNvlpPGkegDIAIRVKpiwpigmfsgyvdnpkktQDNI 438
Cdd:PRK08308 240 MQQYGCSEAGCVS-ICPDMK-SHLDLGNPLPHVSVSAGSDENA---PE---EIVVKMG------------------DKEI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 439 RgdfwlMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 518
Cdd:PRK08308 294 F-----TKDLGYKSERGTLHFMGRMDDVINVSG-----LNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 519 PEFlshDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK08308 364 EEI---DPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
75-571 |
1.33e-21 |
|
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: 98.51 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 75 SGKEIKWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPR----IPEWWlmilGCMRTGLVFMPGTIQMrssdiLYRLQ 150
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGL-RQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPP-----TYDEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 151 ASKAR------------AIVAGDEVAQEVDAVAPDCSFLKIKLLVSENsregwlnfkalLKEASTIHQCVETESRESAAI 218
Cdd:cd05906 104 NARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEE-----------LLDTAADHDLPQSRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 219 YFTSGTSGPPKMAEHSHCSlgIKAKMDAASWTGLSTSDIIwtisdtawIMNilgaflepWV----LGACIFVHLLPKF-D 293
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNGLTPQDV--------FLN--------WVpldhVGGLVELHLRAVYlG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 294 SQTV--------------LKVLSSYPInTLVGAP-IIYRMLLQQ---------DLSSYKFphlhsCFSGGETLLPETLEN 349
Cdd:cd05906 235 CQQVhvpteeiladplrwLDLIDRYRV-TITWAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 350 WK---AKTGLE---IREIYGQTET--GLI-CRVSRTMKVKPGY----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVK 416
Cdd:cd05906 309 LLrllEPYGLPpdaIRPAFGMTETcsGVIySRSFPTYDHSQALefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 417 PIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDpEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHP--A 493
Cdd:cd05906 389 VV-----TKGYYNNPEANAEAFTEDGWFrTGDLGFLD-NGNLTITGRTKDTIIVNGV-----NYYSHEIEAAVEEVPgvE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 494 VSETAVISSPDPSRGEVVKAfVVLAPEF-LSHDRDQLTKVLQEHVK---SVTAPYKYPRKVEfvlDLPKTVTGKIERAKL 569
Cdd:cd05906 458 PSFTAAFAVRDPGAETEELA-IFFVPEYdLQDALSETLRAIRSVVSrevGVSPAYLIPLPKE---EIPKTSLGKIQRSKL 533
|
..
gi 295789127 570 RA 571
Cdd:cd05906 534 KA 535
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
82-569 |
2.54e-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: 97.00 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdilyrlqaskaraivagd 161
Cdd:cd12115 26 TYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqeVDAVAPdcsflkikllvsensregwlnfKALLKEASTIHQC--VETESRESAAIYFTSGTSGPPKMAEHSHCSLG 239
Cdd:cd12115 79 -----LDPAYP----------------------PERLRFILEDAQArlVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 -----IKAKMDAASWTG-LSTSDIIWTISdtawIMNILGaflePWVLGACIFVhllpkfdSQTVLkVLSSYP-------I 306
Cdd:cd12115 132 aflqwAAAAFSAEELAGvLASTSICFDLS----VFELFG----PLATGGKVVL-------ADNVL-ALPDLPaaaevtlI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 307 NTLvgaPIIYRMLLQQDlssyKFPHLHSCFS-GGETLLPETLENWKAKTGLE-IREIYGQTET---GLICRVSRTMKVKP 381
Cdd:cd12115 196 NTV---PSAAAELLRHD----ALPASVRVVNlAGEPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 GyLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIKDPE 454
Cdd:cd12115 269 S-IGRPLANTQAYVLDRALQPVPLGVPGELYIG-----GAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 455 GYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdrdqLTKVLQ 534
Cdd:cd12115 343 GLLEFLGRADNQVKVRG-----FRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLR 412
|
490 500 510
....*....|....*....|....*....|....*
gi 295789127 535 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd12115 413 RHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
122-573 |
4.01e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 96.89 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 122 MI---LGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDavapdcsflKIKLLVSENSREGWLnfkalL 198
Cdd:PRK04813 65 MLatfLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEIL---------GIPVITLDELKDIFA-----T 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 199 KEASTIHQCVETEsrESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtgLSTSDiiWTISDTA------W------ 266
Cdd:PRK04813 131 GNPYDFDHAVKGD--DNYYIIFTSGTTGKPKGVQISHDNL-------------VSFTN--WMLEDFAlpegpqFlnqapy 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 267 -----IMNILGAFlepwVLGACIFVhlLPK---FDSQTVLKVLSSYPINTLVGAPIIYRM-LLQQDLSSYKFPHL-HSCF 336
Cdd:PRK04813 194 sfdlsVMDLYPTL----ASGGTLVA--LPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLtHFLF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 337 SGgetllpETLENWKAKTGLE------IREIYGQTE-TGLICRVSRTMKVKPGY----LGTAFAHYDVQVIDEQGNVLPP 405
Cdd:PRK04813 268 CG------EELPHKTAKKLLErfpsatIYNTYGPTEaTVAVTSIEITDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 406 GKEGDIAIrvkpiwpIG--MFSGYVDNPKKTQ------DNIRgdFWLMGDRGIKDpEGYFHFIGRSDDIINSSGayfcrY 477
Cdd:PRK04813 342 GEQGEIVI-------SGpsVSKGYLNNPEKTAeafftfDGQP--AYHTGDAGYLE-DGLLFYQGRIDFQIKLNG-----Y 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 478 RIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflSHDRD-QLTKVLQEHVKSVTAPYKYPRKVEFVLDL 556
Cdd:PRK04813 407 RIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEE--DFEREfELTKAIKKELKERLMEYMIPRKFIYRDSL 484
|
490
....*....|....*..
gi 295789127 557 PKTVTGKIERAKLrAKE 573
Cdd:PRK04813 485 PLTPNGKIDRKAL-IEE 500
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
392-571 |
5.55e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 96.60 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 392 DVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:PRK10946 364 EVWVADADGNPLPQGEVGRLMTR-------GpyTFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVGREKDQIN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 SSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLapeflshdRDQLTKV-LQEHVKSV-TAPYKY 546
Cdd:PRK10946 437 RGGE-----KIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV--------KEPLKAVqLRRFLREQgIAEFKL 503
|
170 180
....*....|....*....|....*
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK10946 504 PDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
57-571 |
7.42e-21 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 96.23 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 57 VEKAGKRSSGPALWWMNGSGKeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM-- 134
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADLR-AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVma 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 135 -----PGTIQmRSSDILYRLQASKARAIVAGDEVAQEVDAVAPdcsflkiklLVSENSREGWLNFKALLKEASTIHQcVE 209
Cdd:PRK05857 97 dgnlpIAAIE-RFCQITDPAAALVAPGSKMASSAVPEALHSIP---------VIAVDIAAVTRESEHSLDAASLAGN-AD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 210 TESRESAAIYFTSGTSGPPK---MAEHSHCSLGIKAKMDAASWtglstsdIIWTISDTAW----IMNILGAFlepWVL-- 280
Cdd:PRK05857 166 QGSEDPLAMIFTSGTTGEPKavlLANRTFFAVPDILQKEGLNW-------VTWVVGETTYsplpATHIGGLW---WILtc 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 ----GACIfvhlLPKFDSQTVLKVLSSYPINTLVGAP-IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAkTG 355
Cdd:PRK05857 236 lmhgGLCV----TGGENTTSLLEILTTNAVATTCLVPtLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 356 LEIREIYGQTETGLICRVSRT-----MKVKPGYLGTAFAHYDVQVIDEQGNVlPPGKEGDIAIRVKPIW---PIGMFsGY 427
Cdd:PRK05857 311 VRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDVYLAATDGIG-PTAPGAGPSASFGTLWiksPANML-GY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 428 VDNPKKTQDnIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPS 506
Cdd:PRK05857 389 WNNPERTAE-VLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGGV-----NIAPDEVDRIAEGVSGVREAACYEIPDEE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 507 RGEVVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK05857 463 FGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
80-569 |
8.29e-21 |
|
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: 95.62 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 159
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaQEVDAVAPDCSFLKIKLLVSENSREGWLNFKallkeastihqcVETESRESAAIYFTSGTSGPPK--MAEHSHCS 237
Cdd:cd17656 92 -----QRHLKSKLSFNKSTILLEDPSISQEDTSNID------------YINNSDDLLYIIYTSGTTGKPKgvQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 LGIKAKMDaasWTGLSTSDIIW---TISDTAWIMNILGAFLEPWVLgacifvHLLP---KFDSQTVLKVLSSYPINTLvg 311
Cdd:cd17656 155 NLLHFERE---KTNINFSDKVLqfaTCSFDVCYQEIFSTLLSGGTL------YIIReetKRDVEQLFDLVKRHNIEVV-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 312 apIIYRMLLQQDLSSYKF-PHLHSC----FSGGETL-LPETLENWKAKTGLEIREIYGQTETGLI--CRVSRTMKVkPGY 383
Cdd:cd17656 224 --FLPVAFLKFIFSEREFiNRFPTCvkhiITAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVVttYTINPEAEI-PEL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 384 --LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIKDPE 454
Cdd:cd17656 301 ppIGKPISNTWIYILDQEQQLQPQGIVGELYIS-----GASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 455 GYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LSHDRDQLTKVL 533
Cdd:cd17656 376 GNIEFLGRADHQVKIRG-----YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELnISQLREYLAKQL 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 295789127 534 QEhvksvtapYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17656 451 PE--------YMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
208-566 |
3.14e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 94.81 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 208 VETESRESAAIYFTSGTSGPPKMAEHSHCS--LGIKAkmdaaSWTGLSTSD---IIWTISDTAWIMniLGAFLEPWVLGA 282
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPhlVGLKY-----YWRSIIEKDiptVVFSHSSIGWVS--FHGFLYGSLSLG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 283 CIFVH-----LLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD------LSSYKFPHLHSCFSGGETL---LPETLE 348
Cdd:PTZ00237 322 NTFVMfeggiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 349 NwkaKTGLEIREIYGQTETGLICRVSRTMKVKPGY-LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkPIwPIGMFSGY 427
Cdd:PTZ00237 402 N---KLKIKSSRGYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PM-PPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 428 VDNP---KKTQDNIRGdFWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPD 504
Cdd:PTZ00237 477 YKNDekfKQLFSKFPG-YYNSGDLGFKDENGYYTIVSRSDDQIKISG-----NKVQLNTIETSILKHPLVLECCSIGIYD 550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295789127 505 PSRGEVVKAFVVLAPEFLSH--DRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 566
Cdd:PTZ00237 551 PDCYNVPIGLLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
82-548 |
3.92e-20 |
|
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: 93.90 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV--FMPGTIqmRSSDILYRLQASKARAIVA 159
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPvaFLNTNI--RSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 GDEVAQEVDAVAPDCSFLKIKLLV--SENSREGWLNFKALLKEASTihQCVETESRE-----SAAIY-FTSGTSGPPKMA 231
Cdd:cd05938 85 APELQEAVEEVLPALRADGVSVWYlsHTSNTEGVISLLDKVDAASD--EPVPASLRAhvtikSPALYiYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 EHSHcsLGIKAKMDAASWTGLSTSDIIWTI----SDTAWIMNILGAFlepwVLGACIFvhLLPKFD-SQ----------T 296
Cdd:cd05938 163 RISH--LRVLQCSGFLSLCGVTADDVIYITlplyHSSGFLLGIGGCI----ELGATCV--LKPKFSaSQfwddcrkhnvT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VLKV---LSSYPINTlvgaPiiyrmllQQDLSSYKFPHLhscfSGGETLLPETLENWKAKTG-LEIREIYGQTE------ 366
Cdd:cd05938 235 VIQYigeLLRYLCNQ----P-------QSPNDRDHKVRL----AIGNGLRADVWREFLRRFGpIRIREFYGSTEgnigff 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 367 -----TGLICRVSRTMKVKPGYlgtAFAHYDVQ----VIDEQGNVLPPGKeGDIAIRVKPIWPIGMFSGYVDNPKKTQDN 437
Cdd:cd05938 300 nytgkIGAVGRVSYLYKLLFPF---ELIKFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKEQTEKK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 438 I------RGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPS-RGE 509
Cdd:cd05938 376 LlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGE-----NVATTEVADVLGLLDFLQEVNVYGVTVPGhEGR 450
|
490 500 510
....*....|....*....|....*....|....*....
gi 295789127 510 VVKAFVVLAPEflsHDRDQltKVLQEHVKSVTAPYKYPR 548
Cdd:cd05938 451 IGMAAVKLKPG---HEFDG--KKLYQHVREYLPAYARPR 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-580 |
7.07e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK12316 2030 SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQevdavapdcsflkiKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGik 241
Cdd:PRK12316 2109 HLLE--------------RLPLPAGVARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV-- 2172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWT-GLSTSDIIWTISDTAWIMNILGAFlEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 320
Cdd:PRK12316 2173 AHCQAAGERyELSPADCELQFMSFSFDGAHEQWF-HPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLA 2251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 321 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREIYGQTETGLICRVSRTMKVKPG-----YLGTAFAHYDVQ 394
Cdd:PRK12316 2252 EHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCgaayvPIGRALGNRRAY 2331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 395 VIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ--------DNIRGDFWLMGDRGIKDPEGYFHFIGRSDDI 466
Cdd:PRK12316 2332 ILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQ 2406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 467 INSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVlaPEFLSHDrdqLTKVLQEHVKSVTAPYKY 546
Cdd:PRK12316 2407 VKIRG-----FRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVV--PDDAAED---LLAELRAWLAARLPAYMV 2475
|
490 500 510
....*....|....*....|....*....|....
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 580
Cdd:PRK12316 2476 PAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQA 2509
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-500 |
9.56e-18 |
|
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: 86.26 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 159
Cdd:cd17640 5 RITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCSLg 239
Cdd:cd17640 83 ------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANL- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 ikakmdaaswtgLSTSDIIWTISDTAwIMNILGAFLEPW---------VLGACIFVHLLPKFdsQTVLKVLSSYPINTLV 310
Cdd:cd17640 114 ------------LHQIRSLSDIVPPQ-PGDRFLSILPIWhsyersaeyFIFACGCSQAYTSI--RTLKDDLKRVKPHYIV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 311 GAPIIYRML---LQQDLSSYKFPH---LHSCFSGGETL--------LPETLENWKAKTGLEIREIYGQTETGLICRVSRT 376
Cdd:cd17640 179 SVPRLWESLysgIQKQVSKSSPIKqflFLFFLSGGIFKfgisgggaLPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 377 MKVKPGYLGTAFAHYDVQVIDEQGN-VLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 454
Cdd:cd17640 259 KCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLGWLTCG 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 295789127 455 GYFHFIGRSDDIINSSGAyfcrYRIGPSEVENALMEHPAVSETAVI 500
Cdd:cd17640 334 GELVLTGRAKDTIVLSNG----ENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
208-569 |
1.23e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 208 VETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLePWVLGACIFVH 287
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY-GLGVGDRVLQFTTFSFDVFVEELFW-PLMSGARVVLA 3268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 288 LLPKFDSQTVL-KVLSSYPINTLVGAPIIYRMLLQqDLSSYKFPHLHSCFSGGETLLPETLENWKAktGLEIREIYGQTE 366
Cdd:PRK12316 3269 GPEDWRDPALLvELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTE 3345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 367 TGLICRVSRTMKVKPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWL 444
Cdd:PRK12316 3346 ATITVTHWQCVEEGKDAVpiGRPIANRACYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDPFV 3420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 445 MGDRGIKD-------PEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISspdpSRGEVVKAFVVl 517
Cdd:PRK12316 3421 PGERLYRTgdlaryrADGVIEYIGRVDHQVKIRG-----FRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVV- 3490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 518 apefLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:PRK12316 3491 ----PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
216-569 |
1.10e-16 |
|
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: 82.87 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPK--MAEHS---HCSLGIKAKMdaaswtGLSTSDIIWTISDTAWIMNILGAFLEpWVLGACIFvhLLP 290
Cdd:cd17644 109 AYVIYTSGSTGKPKgvMIEHQslvNLSHGLIKEY------GITSSDRVLQFASIAFDVAAEEIYVT-LLSGATLV--LRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 291 K---FDSQTVLKVLSSYPInTLVGAPIIYRMLLQQDLSSYKFP---HLHSCFSGGETLLPETLENWKAKTGLEIR--EIY 362
Cdd:cd17644 180 EemrSSLEDFVQYIQQWQL-TVLSLPPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 363 GQTE---TGLICRVS--RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDN 437
Cdd:cd17644 259 GPTEatiAATVCRLTqlTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPELTAEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 438 IRGD---------FWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRG 508
Cdd:cd17644 334 FISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRG-----FRIELGEIEAVLSQHNDVKTAVVIVREDQPGN 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295789127 509 EVVKAFVVlaPEFlshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17644 409 KRLVAYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-499 |
1.43e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.00 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 48 SDVIDHWASvekagKRSSGPALwwmNGSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCM 127
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPAL---LFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 128 RTGLVF-MPGTiQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCS---FLKIKLLVSENSREGWLNFKALLKEAST 203
Cdd:PRK08279 109 KLGAVVaLLNT-QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLArppRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 204 ihQCVETESRESA---AIY-FTSGTSGPPKMAEHSH----CSLGIKAKMdaaswTGLSTSDIIW-----------TISDT 264
Cdd:PRK08279 188 --TNPASRSGVTAkdtAFYiYTSGTTGLPKAAVMSHmrwlKAMGGFGGL-----LRLTPDDVLYcclplyhntggTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 265 AWIMNilgaflepwvlGACIFvhLLPKFDSQTVLKVLSSYPInTLVGApI--IYRMLLQQDLSSYKFPH-LHSCFSGGet 341
Cdd:PRK08279 261 SVLAA-----------GATLA--LRRKFSASRFWDDVRRYRA-TAFQY-IgeLCRYLLNQPPKPTDRDHrLRLMIGNG-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 342 LLPETLENWKAKTGLE-IREIYGQTE--TGLI--CRVSRTMKVKPGYLGTAFA--HYDVQ----VIDEQGNVLP--PGKE 408
Cdd:PRK08279 324 LRPDIWDEFQQRFGIPrILEFYAASEgnVGFInvFNFDGTVGRVPLWLAHPYAivKYDVDtgepVRDADGRCIKvkPGEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 409 GDIAIRVKPIWPigmFSGYVDnPKKTQDNI------RGDFW-----LMGDrgikDPEGYFHFIGRSDDIinssgayfcrY 477
Cdd:PRK08279 404 GLLIGRITDRGP---FDGYTD-PEASEKKIlrdvfkKGDAWfntgdLMRD----DGFGHAQFVDRLGDT----------F 465
|
490 500
....*....|....*....|....*..
gi 295789127 478 R-----IGPSEVENALMEHPAVSETAV 499
Cdd:PRK08279 466 RwkgenVATTEVENALSGFPGVEEAVV 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
78-573 |
1.84e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 157
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VA----GDE--VAQEVDAVAPDcsflkikllvsensrEGWLNFKALLKEASTIHQCVEtesrESAAIYFTSGTSGPPKMA 231
Cdd:PRK12316 613 LSqshlGRKlpLAAGVQVLDLD---------------RPAAWLEGYSEENPGTELNPE----NLAYVIYTSGSTGKPKGA 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 EHSHCSLgiKAKMDAASWT-GLSTSDIIWTISDTAWIMNILGAFlepWVLGACIFVHLLPK---FDSQTVLKVLSSYPIN 307
Cdd:PRK12316 674 GNRHRAL--SNRLCWMQQAyGLGVGDTVLQKTPFSFDVSVWEFF---WPLMSGARLVVAAPgdhRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 308 TLVGAPIIYRMLLQqdlssykFPHLHSCFS------GGETL---LPETLENWKAKTGLeiREIYGQTETGL-ICRVSRTM 377
Cdd:PRK12316 749 TLHFVPSMLQAFLQ-------DEDVASCTSlrrivcSGEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdVTHWTCVE 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 378 KVKPGY-LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-------FWLMGDRG 449
Cdd:PRK12316 820 EGGDSVpIGRPIANLACYILDANLEPVPVGVLGELYLAGR-----GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLA 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 450 IKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISspdpSRGEVVKAFVVLAPEFLShdrdqL 529
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKLRG-----LRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD-----W 960
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 295789127 530 TKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK12316 961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPE 1004
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-580 |
1.91e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 83.17 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDAVaPDCSFLkikllvsensregwlNFKALLKEASTiHQCVETESRESAAIYFTSGTSGPPK--MAEHshcslg 239
Cdd:PRK10252 564 DQLPRFADV-PDLTSL---------------CYNAPLAPQGA-APLQLSQPHHTAYIIFTSGSTGRPKgvMVGQ------ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 iKAKMDAASWT----GLSTSDIIW-----TISDTAWimnilgAFLEPWVLGACIFV-----HLlpkfDSQTVLKVLSSYP 305
Cdd:PRK10252 621 -TAIVNRLLWMqnhyPLTADDVVLqktpcSFDVSVW------EFFWPFIAGAKLVMaepeaHR----DPLAMQQFFAEYG 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 306 INTLVGAPiiyRML------LQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET----------GL 369
Cdd:PRK10252 690 VTTTHFVP---SMLaafvasLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAavdvswypafGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 370 ICRVSRTMKVKPGY--LGTAfahydVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD------ 441
Cdd:PRK10252 767 ELAAVRGSSVPIGYpvWNTG-----LRILDARMRPVPPGVAGDLYLT-----GIQLAQGYLGRPDLTASRFIADpfapge 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 442 -FWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHP----AVSETAVISSPDPSRGEVVK--AF 514
Cdd:PRK10252 837 rMYRTGDVARWLDDGAVEYLGRSDDQLKIRG-----QRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGY 911
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295789127 515 VVlAPEFLSHDRDqltkVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW--KTSGRA 580
Cdd:PRK10252 912 LV-SQSGLPLDTS----ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELkaQVPGRA 974
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
80-570 |
2.62e-16 |
|
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: 81.70 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 159
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 160 gdevaqevdavapdcsflkikllvsensregwLNFKALLKEASTIHQ--CVETESRESAAIYFTSGTSGPPKMAEHSHcS 237
Cdd:cd05939 81 --------------------------------FNLLDPLLTQSSTEPpsQDDVNFRDKLFYIYTSGTTGLPKAAVIVH-S 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 238 LGIKAKMDAASWTGLSTSDIIWT---ISDTAwiMNILGaflepwvLGACIF----VHLLPKFDSQTVLKVLSSYpiNTLV 310
Cdd:cd05939 128 RYYRIAAGAYYAFGMRPEDVVYDclpLYHSA--GGIMG-------VGQALLhgstVVIRKKFSASNFWDDCVKY--NCTI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 311 GAPI--IYRMLLQQDLSSYKFPH-LHSCFSGGetLLPETLENWKAKTGL-EIREIYGQTE-----------TGLICRVSR 375
Cdd:cd05939 197 VQYIgeICRYLLAQPPSEEEQKHnVRLAVGNG--LRPQIWEQFVRRFGIpQIGEFYGATEgnsslvnidnhVGACGFNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 376 TmkvkPGYLgtafahYDVQVI-----------DEQGNVLP--PGKEGDIAIRVKPIWPIGMFSGYVD---NPKKTQDNI- 438
Cdd:cd05939 275 I----LPSV------YPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIARDVf 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 439 -RGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSR-GEVVKAFV 515
Cdd:cd05939 345 kKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGE-----NVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAI 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 516 VLAPEFLshDRDQLTKVLQehvkSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05939 420 VDPERKV--DLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
319-570 |
2.74e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 81.58 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 319 LLQQDLSSYKfpHLHSCFSGGETLLPETLEnwKAKT-GLEIREIYGQTETGlicrvSRTMKVKPGylgtAFahydVQVID 397
Cdd:PRK07445 221 LLQLRPQWLA--QFRTILLGGAPAWPSLLE--QARQlQLRLAPTYGMTETA-----SQIATLKPD----DF----LAGNN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 398 EQGNVLP-------PGKEGDIAIRVKpiwpiGMFSGY----VDNPKktqdnirgdFWLMGDRGIKDPEGYFHFIGRSDDI 466
Cdd:PRK07445 284 SSGQVLPhaqitipANQTGNITIQAQ-----SLALGYypqiLDSQG---------IFETDDLGYLDAQGYLHILGRNSQK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 467 INSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRdqltkvLQEHVKSVTAPYKY 546
Cdd:PRK07445 350 IITGGE-----NVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEE------LKTAIKDQLSPFKQ 418
|
250 260
....*....|....*....|....
gi 295789127 547 PRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:PRK07445 419 PKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-571 |
2.97e-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: 81.90 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 60 AGKRSSGPALWWMNGSGKEI-KWSFRELSEASKQTANVLSGACGlhRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgTI 138
Cdd:cd05931 3 AAARPDRPAYTFLDDEGGREeTLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-LP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 139 QMRSSDILYRLQA----SKARAIVAGDEVAQEVDA-VAPDCSFLKIKLLVSE----NSREGWlnfkallkeastihQCVE 209
Cdd:cd05931 80 PPTPGRHAERLAAiladAGPRVVLTTAAALAAVRAfAASRPAAGTPRLLVVDllpdTSAADW--------------PPPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 210 TESRESAAIYFTSGTSGPPKMAEHSH------CSLGIKAKMDAASWTGLStsdiiwtisdtaWI-----MNILGAFLEPW 278
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHrnllanVRQIRRAYGLDPGDVVVS------------WLplyhdMGLIGGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 279 VLGACifVHLLP--KFDSQTV--LKVLSSYPInTLVGAP------IIYRMLLQQ----DLSSykfphLHSCFSGGETLLP 344
Cdd:cd05931 214 YSGGP--SVLMSpaAFLRRPLrwLRLISRYRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 345 ETLENWK---AKTGLE---IREIYGQTETGLI---------------------CRVSRTMKVKPGY-----LGTAFAHYD 392
Cdd:cd05931 286 ATLRRFAeafAPFGFRpeaFRPSYGLAEATLFvsggppgtgpvvlrvdrdalaGRAVAVAADDPAArelvsCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVIDEQGN-VLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQ------DNIRGDFWL-MGDRGIKDpEGYFHFIGR 462
Cdd:cd05931 366 VRIVDPETGrELPDGEVGEIWVR-------GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 463 SDDIINSSGAyfcryRIGPSEVENALME-HPAVSET--AVISSPDPSRGEVVkafvVLAPEFLSHDRDQLTKVLQEHVKS 539
Cdd:cd05931 438 LKDLIIVRGR-----NHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV----VVAEVERGADPADLAAIAAAIRAA 508
|
570 580 590
....*....|....*....|....*....|....*
gi 295789127 540 VTAPYKY-PRKVEFVL--DLPKTVTGKIERAKLRA 571
Cdd:cd05931 509 VAREHGVaPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
82-569 |
3.37e-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: 81.36 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAraivagd 161
Cdd:cd17650 14 TYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGA------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 evaqevdavapdcsflkiKLLVsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSHCSLG 239
Cdd:cd17650 86 ------------------KLLL--------------------------TQPEDLAYVIYTSGTTGKPKgvMVEHRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 240 IKA-----KMDAASWTGLSTSDIIWTISdtawimniLGAFLEPWVLGACIFVhlLP---KFDSQTVLKVLSSYPINTLVG 311
Cdd:cd17650 122 AHAwrreyELDSFPVRLLQMASFSFDVF--------AGDFARSLLNGGTLVI--CPdevKLDPAALYDLILKSRITLMES 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 312 APIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREI--YGQTET-----------GLICRvSRTM 377
Cdd:cd17650 192 TPALIRPVMAYvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIInsYGVTEAtidstyyeegrDPLGD-SANV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 378 KVkpgylGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGI 450
Cdd:cd17650 271 PI-----GRPLPNTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapgerMYRTGDLAR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 451 KDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDpSRGEVVKAFVVLAPEFLshDRDQLT 530
Cdd:cd17650 341 WRADGNVELLGRVDHQVKIRG-----FRIELGEIESQLARHPAIDEAVVAVRED-KGGEARLCAYVVAAATL--NTAELR 412
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 295789127 531 KVLQEHVKSVTAPYKYprkveFVLD-LPKTVTGKIERAKL 569
Cdd:cd17650 413 AFLAKELPSYMIPSYY-----VQLDaLPLTPNGKVDRRAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
82-536 |
5.91e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.10 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM---PGtiqMRSSDILYRLQASKARAIV 158
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 aGDEVAQEVDAVAPdCSFLKIKLLVSENSREGWLNF---KALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 235
Cdd:PRK09274 119 -GIPKAHLARRLFG-WGKPSVRRLVTVGGRLLWGGTtlaTLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 236 CSLgiKAKMDA--ASWtGLSTSDIiwtisDTAwiMNILGAFLEPwVLGACifvHLLPKFD--------SQTVLKVLSSYP 305
Cdd:PRK09274 197 GMF--EAQIEAlrEDY-GIEPGEI-----DLP--TFPLFALFGP-ALGMT---SVIPDMDptrpatvdPAKLFAAIERYG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 306 INTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKA--KTGLEIREIYGQTETGLICRV-SRTMKVK- 380
Cdd:PRK09274 263 VTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPISSIeSREILFAt 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 381 -------PGYL-GTAFAHYDVQVID---------EQGNVLPPGKEGDIAIRvkpiwpiG-MFS-GYVDNPKKTQDN---- 437
Cdd:PRK09274 343 raatdngAGICvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-------GpMVTrSYYNRPEATRLAkipd 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 438 IRGDFW-LMGDRGIKDPEGYFHFIGR-SDDIINSSGAYFcryrigPSEVENALMEHPAVSETAVISSPDPsrGEVVKAFV 515
Cdd:PRK09274 416 GQGDVWhRMGDLGYLDAQGRLWFCGRkAHRVETAGGTLY------TIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLC 487
|
490 500
....*....|....*....|..
gi 295789127 516 V-LAPEfLSHDRDQLTKVLQEH 536
Cdd:PRK09274 488 VeLEPG-VACSKSALYQELRAL 508
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
80-570 |
1.23e-15 |
|
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: 79.32 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 80 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTI--QMRSSDILYRLQASKARAI 157
Cdd:cd05940 3 ALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 158 VAgdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesreSAAIY-FTSGTSGPPKMAEHSHC 236
Cdd:cd05940 80 VV-------------------------------------------------------DAALYiYTSGTTGLPKAAIISHR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 237 SLgIKAKMDAASWTGLSTSDIIWTI----SDTAwimNILGaflepwvLGACIF----VHLLPKFDSQTVLKVLSSYPINT 308
Cdd:cd05940 105 RA-WRGGAFFAGSGGALPSDVLYTClplyHSTA---LIVG-------WSACLAsgatLVIRKKFSASNFWDDIRKYQATI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 309 LVGAPIIYRMLLQQDLSSYKFPHLHSCFSGgETLLPETLENWKAKTGL-EIREIYGQTE-----------TGLICRVSRT 376
Cdd:cd05940 174 FQYIGELCRYLLNQPPKPTERKHKVRMIFG-NGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinffgkPGAIGRNPSL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 377 MKVKPGYlgtAFAHYDVQ----VIDEQGNV--LPPGKEGDIAIRVKPIWPigmFSGYVDnPKKTQDNI------RGDFW- 443
Cdd:cd05940 253 LRKVAPL---ALVKYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEP---FDGYTD-PAATEKKIlrdvfkKGDAWf 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 444 LMGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDP-SRGEVVKAFVVLAPEfl 522
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGE-----NVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN-- 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 295789127 523 sHDRDqLTKvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 570
Cdd:cd05940 399 -EEFD-LSA-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
42-564 |
2.84e-15 |
|
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: 78.85 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 42 AKFNFASDVIDHwasvekagKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEwwl 121
Cdd:cd05943 68 ARLNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPE--- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 122 MILGCMRT---GLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVA------------QEVDAVAPDcsfLKIKLLVSEN 186
Cdd:cd05943 136 AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrekvAELVKGLPS---LLAVVVVPYT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 187 SREGwlnfkalLKEASTIHQCV---ETESRESAA--------------IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASW 249
Cdd:cd05943 213 VAAG-------QPDLSKIAKALtleDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAGGTLLQHLKEHILH 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 250 TGLSTSDIIWTISDTAWIM-NILGAFLepwVLGACIfvhLL----PKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-- 322
Cdd:cd05943 286 CDLRPGDRLFYYTTCGWMMwNWLVSGL---AVGATI---VLydgsPFYPDTNALWDLADEEGITVFGTSAKYLDALEKag 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 323 -------DLSSykfphLHSCFSGGETLLPETLE--NWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYD 392
Cdd:cd05943 360 lkpaethDLSS-----LRTILSTGSPLKPESFDyvYDHIKPDVLLASISGGTDiISCFVGGNPLLPVYRGEIQCRGLGMA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVIDEQGNVLPpGKEGDIAIrVKPI--WPIGmFSGYVDNPK--KTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:cd05943 435 VEAFDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWNDPDGSRyrAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLN 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 SSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdrdQLTKVLQEHVKSVTA----PY 544
Cdd:cd05943 512 PGGV-----RIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGV------ELDDELRKRIRSTIRsalsPR 580
|
570 580
....*....|....*....|
gi 295789127 545 KYPRKVEFVLDLPKTVTGKI 564
Cdd:cd05943 581 HVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
82-571 |
5.53e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 77.73 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGAcGLHRGDRVAV-------VLPRIPEWWlmilgcMRTGLVFM-----PGT-IQMRSSDILYR 148
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLW------MRGASLTMlhqptPRTdLAVWAEDTLRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 149 LQASKARAIVAGDEVaqevDAVAPDCSFLKIK-LLVSEnsregwlnfkaLLKEASTihQCVETESRESAAIYFTSGTSGP 227
Cdd:PRK07768 104 IGMIGAKAVVVGEPF----LAAAPVLEEKGIRvLTVAD-----------LLAADPI--DPVETGEDDLALMQLTSGSTGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 228 PKMAEHSHCSL--GIKAKMDAASWTglSTSDIIwtISdtaWI-----MNILGAFLEPWVLGaCIFVHLLP-KFDSQTVL- 298
Cdd:PRK07768 167 PKAVQITHGNLyaNAEAMFVAAEFD--VETDVM--VS---WLplfhdMGMVGFLTVPMYFG-AELVKVTPmDFLRDPLLw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 299 -KVLSSYPiNTLVGAP-----IIYRMLLQQ------DLSSYKFphlhsCFSGGETLLPETLENW---KAKTGLE---IRE 360
Cdd:PRK07768 239 aELISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLldaGARFGLRpeaILP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 361 IYGQTETGL---ICRVSRTMKV------------------KPGY-----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIR 414
Cdd:PRK07768 313 AYGMAEATLavsFSPCGAGLVVdevdadllaalrravpatKGNTrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 415 VKPIWPigmfsGY--VDNPKKTQDNirgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcryR-IGPSEVENALME 490
Cdd:PRK07768 393 GESVTP-----GYltMDGFIPAQDA---DGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAG------RnIYPTDIERAAAR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 491 HPAVSE--TAVISSPDPSRGEvvkAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKY-PRKVeFVL---DLPKTVTGKI 564
Cdd:PRK07768 459 VEGVRPgnAVAVRLDAGHSRE---GFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKL 534
|
....*..
gi 295789127 565 ERAKLRA 571
Cdd:PRK07768 535 RRANAAE 541
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
216-578 |
6.99e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.20 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNIlGAFLEPWVLGACIFVHLLPKFDSQ 295
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQ-ERFLWTLICGGCLVVRDNDLWDPE 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 296 TVLKVLSSYPINTLVGAPIIYRMLLQ----QDLSSYKfphlHSCFsGGETLLPETLENWKAKtgLEIREI---YGQTETG 368
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPAYLQQFAEdaggADCASLD----IYVF-GGEAVPPAAFEQVKRK--LKPRGLtngYGPTEAV 3390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 369 LI-----CRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-F 442
Cdd:PRK12467 3391 VTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAERFVADpF 3465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 443 WLMGDRGIKD-------PEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSpDPSRGEVVKAFV 515
Cdd:PRK12467 3466 SGSGGRLYRTgdlaryrADGVIEYLGRIDHQVKIRG-----FRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYV 3539
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789127 516 VLAPEflshdRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 578
Cdd:PRK12467 3540 VPADP-----QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-500 |
1.46e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.88 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTIQMRssdilyrlqaskaraiVAGD 161
Cdd:cd05910 4 SFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLIDPG----------------MGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEVDAVAPDcSFLKIkllvsensregwlnFKALlkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHCSLgiK 241
Cdd:cd05910 65 NLKQCLQEAEPD-AFIGI--------------PKAD----------------EPAAILFTSGSTGTPKGVVYRHGTF--A 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDA-ASWTGLSTSDIiwtisDTAWIMniLGAFLEPwVLGACIFV----HLLP-KFDSQTVLKVLSSYPINTLVGAPII 315
Cdd:cd05910 112 AQIDAlRQLYGIRPGEV-----DLATFP--LFALFGP-ALGLTSVIpdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 316 YRML----LQQDLssyKFPHLHSCFSGGETLLPETLENWKA--KTGLEIREIYGQTETGLIC-------RVSRTMKVKPG 382
Cdd:cd05910 184 LERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSsigsrelLATTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 383 Y---LGTAFAHYDVQVID---------EQGNVLPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQ----DNIRGDFW-LM 445
Cdd:cd05910 261 AgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTP-----TYVNRPVATAlakiDDNSEGFWhRM 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 295789127 446 GDRGIKDPEGYFHFIGR-SDDIINSSGAYFCryrigpSEVENALMEHPAVSETAVI 500
Cdd:cd05910 336 GDLGYLDDEGRLWFCGRkAHRVITTGGTLYT------EPVERVFNTHPGVRRSALV 385
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
78-569 |
1.48e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 72.82 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRiPEWWLM-ILGCMRTGLVFMPgtiqmrssdilyrlqaskara 156
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 157 ivagdevaqeVDAVAPDcsfLKIKLLVSEnsregwlnfkallkeasTIHQCVETESRESAAIYFTSGTSGPPK--MAEH- 233
Cdd:cd17648 68 ----------IDPSYPD---ERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHg 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 234 ----SHCSL----GIKAKMDAASwtgLSTSDIIWTISDTAWIMNILGaflepwvlGACIFVhlLP---KFDSQTVLKVLS 302
Cdd:cd17648 118 svvnLRTSLseryFGRDNGDEAV---LFFSNYVFDFFVEQMTLALLN--------GQKLVV--PPdemRFDPDRFYAYIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 303 SYPINTLVGAPiiyrMLLQQ-DLSSykFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKP 381
Cdd:cd17648 185 REKVTYLSGTP----SVLQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 --GYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGY-----------VDNPKKT-QDNIRGDFWLM-- 445
Cdd:cd17648 259 fdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYlnrpeltaerfLPNPFQTeQERARGRNARLyk 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 446 -GDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGE--VVKAFV---VLAP 519
Cdd:cd17648 334 tGDLVRWLPSGELEYLGRNDFQVKIRG-----QRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVgyyLPEP 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 295789127 520 EFLShDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17648 409 GHVP-ESD-----LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
81-574 |
6.51e-13 |
|
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: 70.92 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 81 WSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTIQ--MRSSDILYRLQASKARAIV 158
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 159 AGDEVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYfTSGTSGPPKMAehshcsl 238
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAA------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 239 gikakmdAASWTGLSTSDiiWTISDTAWIMNILGAFL-------EPWVLGACIFVH------LLPKFDSQTVLK--VLSS 303
Cdd:cd05937 106 -------AISWRRTLVTS--NLLSHDLNLKNGDRTYTcmplyhgTAAFLGACNCLMsggtlaLSRKFSASQFWKdvRDSG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 304 YPINTLVGAPIiyRMLLQQDLSSYKfpHLHSC-FSGGETLLPETLENWKAKTGL-EIREIYGQTETglicrVSRTMKVKP 381
Cdd:cd05937 177 ATIIQYVGELC--RYLLSTPPSPYD--RDHKVrVAWGNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 382 GYLGT-AFAHYD-------------VQVIDEQGNVL-----------PPGKEGDIAIRVkPIWPIGMFSGYVDNPKKTQD 436
Cdd:cd05937 248 GDFGAgAIGHHGlirrwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATES 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 437 NI------RGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSR-G 508
Cdd:cd05937 327 KLvrdvfrKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSE-----NVSTTEVADVLGAHPDIAEANVYGVKVPGHdG 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295789127 509 EVVKAFVVLAPEflSHDRDQLTK-VLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 574
Cdd:cd05937 402 RAGCAAITLEES--SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-576 |
1.76e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 68 ALWWMNGSgkeikWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILY 147
Cdd:PRK05691 1149 ALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAY 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 148 RLQASKA------RAIVAGDEVAQEVDAVAPDcsflKIKLlvsensrEGWLNfkallkEASTIHqcveTESRESAAIYFT 221
Cdd:PRK05691 1223 MLADSGVellltqSHLLERLPQAEGVSAIALD----SLHL-------DSWPS------QAPGLH----LHGDNLAYVIYT 1281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 222 SGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLePWVLGaCIFVHLLP--KFDSQTVLK 299
Cdd:PRK05691 1282 SGSTGQPKGVGNTHAALAERLQWMQATY-ALDDSDVLMQKAPISFDVSVWECFW-PLITG-CRLVLAGPgeHRDPQRIAE 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 300 VLSSYPINTLVGAPIIYRMLLQQDLSSyKFPHLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTETGL-----ICRV 373
Cdd:PRK05691 1359 LVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAInvthwQCQA 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 374 SRTMKVKpgyLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLM 445
Cdd:PRK05691 1438 EDGERSP---IGRPLGNVLCRVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAERFVPDplgedgarLYRT 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 446 GDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD 525
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRG-----FRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAE 1584
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 295789127 526 RdqLTKVLQEHVKSVTAPYKYPRkvefvLD-LPKTVTGKIERAKLRAKEWKT 576
Cdd:PRK05691 1585 R--LKAALAAELPEYMVPAQLIR-----LDqMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
446-571 |
3.63e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.15 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 446 GDRGIKDP-----EGYFH-------------FIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSR 507
Cdd:PRK07824 220 GYRNPVDPdpfaePGWFRtddlgalddgvltVLGRADDAISTGG-----LTVLPQVVEAALATHPAVADCAVFGLPDDRL 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295789127 508 GEVVKAFVVLAPeflsHDRDQLTKvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK07824 295 GQRVVAAVVGDG----GPAPTLEA-LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
42-564 |
1.14e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 67.51 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 42 AKFNFASDVIDHwasvekagKRSSGPALWWMNGSGKEIKWSFRELSEaskQTANVLSG--ACGLHRGDRVAVVLPRIPEW 119
Cdd:PRK03584 84 ARLNYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRR---QVAALAAAlrALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 120 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD---------EVAQEVDAVAPDCSFLKiKLLVSENSREG 190
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLE-HVVVVPYLGPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 191 wlNFKALLKEASTIHQCVETEsrESAAIYFT-------------SGTSGPPKMAEHSHCslGI-----KAK---MDaasw 249
Cdd:PRK03584 232 --AAAAALPGALLWEDFLAPA--EAAELEFEpvpfdhplwilysSGTTGLPKCIVHGHG--GIllehlKELglhCD---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 250 tgLSTSDIIWTISDTAWIM-NILGAFLepwVLGACIfvhLL----PKFDSQTVL-------KVlssypinTLVGA-PIIY 316
Cdd:PRK03584 302 --LGPGDRFFWYTTCGWMMwNWLVSGL---LVGATL---VLydgsPFYPDPNVLwdlaaeeGV-------TVFGTsAKYL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 317 RMLLQQDLS---SYKFPHLHSCFSGGETLLPETL----ENWKAktGLEIREIYGQTEtglICRV----SRTMKVKPG--- 382
Cdd:PRK03584 367 DACEKAGLVpgeTHDLSALRTIGSTGSPLPPEGFdwvyEHVKA--DVWLASISGGTD---ICSCfvggNPLLPVYRGeiq 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 383 --YLGTAfahydVQVIDEQGN-VLppGKEGDIAIRvKPI--WPIGmFSGYVDNPK------KTQDNIrgdfWLMGDRGIK 451
Cdd:PRK03584 442 crGLGMA-----VEAWDEDGRpVV--GEVGELVCT-KPFpsMPLG-FWNDPDGSRyrdayfDTFPGV----WRHGDWIEI 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 452 DPEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LShdrDQLT 530
Cdd:PRK03584 509 TEHGGVVIYGRSDATLNRGGV-----RIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVtLD---DALR 580
|
570 580 590
....*....|....*....|....*....|....
gi 295789127 531 KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 564
Cdd:PRK03584 581 ARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
58-572 |
3.59e-11 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 65.87 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 58 EKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQT---ANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM 134
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELRSQVsrvANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 135 PGTIQMRSSDILYRLQASKARAIVAGDEV----------AQEVDAVAP-------DCSFLKIKLlvsensREG---WLNF 194
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplySRVVEAKAPkaivlpaDGKSVRVKL------REGdmsWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 195 KALLK------EASTIHQCVETESResaaIYFTSGTSGPPKMAEHSHCSlGIKAKMDAASWTGLSTSDIIwtisdtAWIM 268
Cdd:PLN03052 336 LARANglrrpdEYKAVEQPVEAFTN----ILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIV------CWPT 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 269 NiLGAFLEPWVL------GACI-FVHLLP------KF--DSQ-TVLKVLSSypintlvgapIIYRMLLQQDLSSYKFPHL 332
Cdd:PLN03052 405 N-LGWMMGPWLVyasllnGATLaLYNGSPlgrgfaKFvqDAKvTMLGTVPS----------IVKTWKNTNCMAGLDWSSI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 333 HSCFSGGETL-LPETLenW-KAKTGLE-IREIYGQTETGlICRVSRTMkVKPGYLG---TAFAHYDVQVIDEQGNVLPPG 406
Cdd:PLN03052 474 RCFGSTGEASsVDDYL--WlMSRAGYKpIIEYCGGTELG-GGFVTGSL-LQPQAFAafsTPAMGCKLFILDDSGNPYPDD 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 407 KEGDIAIRVKP----------------IWPIGMfsgyvdnPKKTQDNIRGDfwlmGDRGIKDPEGYFHFIGRSDDIINSS 470
Cdd:PLN03052 550 APCTGELALFPlmfgasstllnadhykVYFKGM-------PVFNGKILRRH----GDIFERTSGGYYRAHGRADDTMNLG 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 471 GayfcryrIGPSEVE-----NALmeHPAVSETAVISSPDPSRG--EVVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAP 543
Cdd:PLN03052 619 G-------IKVSSVEiervcNAA--DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNP 689
|
570 580
....*....|....*....|....*....
gi 295789127 544 YKYPRKVEFVLDLPKTVTGKIERAKLRAK 572
Cdd:PLN03052 690 LFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
83-571 |
5.50e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.41 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 83 FRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQM----RSSDI--LYR-LQASKAR 155
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMgfggRESYIaqLRGmLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 156 AIVAGDEVAQEVDAVApdcsflkikllvsENSREGWLNFKALLK---EASTIHQCVETEsrESAAIYFTSGTSGPPK--- 229
Cdd:PRK09192 131 AIITPDELLPWVNEAT-------------HGNPLLHVLSHAWFKalpEADVALPRPTPD--DIAYLQYSSGSTRFPRgvi 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 230 ------MAE---HSHCSLGIKAKMDAASWTGLstsdiiwtISDtawiMNILGAFLEPwvLGACIFVHLLPKFD----SQT 296
Cdd:PRK09192 196 ithralMANlraISHDGLKVRPGDRCVSWLPF--------YHD----MGLVGFLLTP--VATQLSVDYLPTRDfarrPLQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 297 VLKVLSSYPiNTLVGAP-----IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAK---TGLEIREI---YGQT 365
Cdd:PRK09192 262 WLDLISRNR-GTISYSPpfgyeLCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAfapAGFDDKAFmpsYGLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 366 ETGLICRVS------RTMKVKPGYL----------------------GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkp 417
Cdd:PRK09192 341 EATLAVSFSplgsgiVVEEVDRDRLeyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVR--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 418 iWPIGMfSGYVDNPKkTQDNIRGDFWL-MGDRGIKDpEGYFHFIGRSDDIINSSGAyfcryRIGPSEVENALMEHPAV-- 494
Cdd:PRK09192 418 -GPSLM-SGYFRDEE-SQDVLAADGWLdTGDLGYLL-DGYLYITGRAKDLIIINGR-----NIWPQDIEWIAEQEPELrs 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 495 SETAVISSPDPSrGEVVKAFV---VLAPEflshDRDQLTKVLQEHVKSVTApykYPRKVEFV--LDLPKTVTGKIERAKL 569
Cdd:PRK09192 489 GDAAAFSIAQEN-GEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKA 560
|
..
gi 295789127 570 RA 571
Cdd:PRK09192 561 KK 562
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
82-569 |
1.18e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 64.03 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 82 SFRELSEASKQTANVLSGACGLHRGDrVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 161
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERA-IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 162 EVAQEvdavapdcsflkiKLLVSENSRegwlNFKALLKEAStihqcvetesresAAIYFTSGTSGPPKMAEHSHCSlgIK 241
Cdd:cd17654 97 ELDNA-------------PLSFTPEHR----HFNIRTDECL-------------AYVIHTSGTTGTPKIVAVPHKC--IL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 242 AKMDAASWTGLSTSDIIWTIS-----DTAwIMNILGAFLEpwvlGAC-IFVHLLPKFDSQTVLKVLSSYPINTLVGA-PI 314
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTspltfDPS-VVEIFLSLSS----GATlLIVPTSVKVLPSKLADILFKRHRITVLQAtPT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 315 IYRMLLQQDLSSY---KFPHLHSCFSGGETLLPET-LENWKAK-TGLEIREIYGQTETgliCRVSRTMKVK----PGYLG 385
Cdd:cd17654 220 LFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSLViLSSWRGKgNRTRIFNIYGITEV---SCWALAYKVPeedsPVQLG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 386 TAFAHYDVQVIDEQGNvlppgkEGDIAIRVKPIWPIGMFSGYVDNPKktqdnirGDFWLMGDRgIKDPEGYFHFIGRSDD 465
Cdd:cd17654 297 SPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVPK-------GTMRATGDF-VTVKDGELFFLGRKDS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 466 IINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDpsrgEVVKAFVVLAP-EFLSHDRDQLTKVlqehvksvtAPY 544
Cdd:cd17654 363 QIKRRG-----KRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGESsSSRIHKELQLTLL---------SSH 424
|
490 500
....*....|....*....|....*
gi 295789127 545 KYPRKVEFVLDLPKTVTGKIERAKL 569
Cdd:cd17654 425 AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
213-573 |
1.69e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 213 RESAAIYFTSGTSGPPK--MAEHS----HCSLGIKAkmdaaswTGLSTSDI---IWTIS-DTAwimniLGAFLEPWVLGA 282
Cdd:PRK05691 2333 QHQAYLIYTSGSTGKPKgvVVSHGeiamHCQAVIER-------FGMRADDCelhFYSINfDAA-----SERLLVPLLCGA 2400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 283 CIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIR-EI 361
Cdd:PRK05691 2401 RVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 362 YGQTET---GLICRVSRTMKVKPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQD 436
Cdd:PRK05691 2481 YGPTETvvmPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAE 2555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 437 NIRGD--------FWLMGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSRG 508
Cdd:PRK05691 2556 RFVADpfaadggrLYRTGDLVRLRADGLVEYVGRIDHQVKIRG-----FRIELGEIESRLLEHPAVREAVVLALDTPSGK 2630
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 509 EVVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK05691 2631 QLAGYLVSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD 2695
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
329-500 |
3.24e-10 |
|
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: 62.76 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 329 FPHLHSCFSGGETLLPETLENWkakTGLEIR--EIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNvlppg 406
Cdd:cd05933 319 LDRCQKFFTGAAPISRETLEFF---LSLNIPimELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD----- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 407 KEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGAyfcrYRIGPSEVE 485
Cdd:cd05933 391 GIGEICFWGRHV-----FMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKELIITAGG----ENVPPVPIE 461
|
170
....*....|....*.
gi 295789127 486 NAL-MEHPAVSETAVI 500
Cdd:cd05933 462 DAVkKELPIISNAMLI 477
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
216-573 |
2.56e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.32 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHcsLGIKAKMDAASwtglstsDIIWTISDTAwIMNIL---------GAFLEPWVLGACIFV 286
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSH--HNILSNIEQIS-------DVFNLRNDDV-ILSSLpffhsfgltVTLWLPLLEGIKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 287 HLLPkFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD-LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQT 365
Cdd:PRK08633 855 HPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 366 ETG----------LICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKT 434
Cdd:PRK08633 934 ETSpvasvnlpdvLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-----GPQVMKGYLGDPEKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 435 QDNIR---GDFW-LMGDRGIKDPEGYFHFIGRsddiinssgayFCRY-RIG----P-SEVENALmeHPAVSET----AVI 500
Cdd:PRK08633 1009 AEVIKdidGIGWyVTGDKGHLDEDGFLTITDR-----------YSRFaKIGgemvPlGAVEEEL--AKALGGEevvfAVT 1075
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295789127 501 SSPDPSRGEVVkafVVLapefLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIE--RAKLRAKE 573
Cdd:PRK08633 1076 AVPDEKKGEKL---VVL----HTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDlkGLKELALA 1143
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
214-570 |
2.58e-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: 59.81 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 214 ESAAIYFTSGTSGPPK--MAEHSHCSLGIKAKMDAASWTglsTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPK 291
Cdd:cd05908 107 ELAFIQFSSGSTGDPKgvMLTHENLVHNMFAILNSTEWK---TKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 292 FDSQTV--LKVLSSYPINTLVGAPIIYRMLLQQ---------DLSsykfpHLHSCFSGGETLLPETLENWK---AKTGLE 357
Cdd:cd05908 184 FIRRPIlwLKKASEHKATIVSSPNFGYKYFLKTlkpekandwDLS-----SIRMILNGAEPIDYELCHEFLdhmSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 358 ---IREIYGQTETGL-ICRVSRTMKVKPGYL---------------------------GTAFAHYDVQVIDEQGNVLPPG 406
Cdd:cd05908 259 rnaILPVYGLAEASVgASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 407 KEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRGDFWLM-GDRG-IKDPEGYfhFIGRSDDII--NSSGAYfcryrigPS 482
Cdd:cd05908 339 YIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLV--ITGREKDIIfvNGQNVY-------PH 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 483 EVENALMEHPAVsetavisspdpSRGEVVKAFVvlapeFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLD------- 555
Cdd:cd05908 405 DIERIAEELEGV-----------ELGRVVACGV-----NNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNkrggwqi 468
|
410 420
....*....|....*....|...
gi 295789127 556 --------LPKTVTGKIERAKLR 570
Cdd:cd05908 469 nevlpirrIPKTTSGKVKRYELA 491
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
208-570 |
5.91e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 58.95 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 208 VETESRESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtgLSTSDIIWTISD-TA--WIMNILGAF---------L 275
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-------------LANVEQIKTIADfTPndRFMSALPLFhsfgltvglF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 276 EPWVLGACIFVhllpkfdsqtvlkvlssYPintlvgAPIIYRML--LQQD------------LSSY-KFPH------LHS 334
Cdd:PRK08043 427 TPLLTGAEVFL-----------------YP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 335 CFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID----EQGnvlppgkeGD 410
Cdd:PRK08043 484 VVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQG--------GR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 411 IAIRVKPIwpigmFSGY--VDNPKK----TQDNIRGDF---WL-MGDRGIKDPEGYFHFIGRSDDIINSSGAYfcryrIG 480
Cdd:PRK08043 556 LQLKGPNI-----MNGYlrVEKPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEM-----VS 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 481 PSEVEN-ALMEHPAVSETAVISSpDPSRGEVVKAFVVLApeflSHDRDQLTKVLQEHVKSVTApykYPRKVEFVLDLPKT 559
Cdd:PRK08043 626 LEMVEQlALGVSPDKQHATAIKS-DASKGEALVLFTTDS----ELTREKLQQYAREHGVPELA---VPRDIRYLKQLPLL 697
|
410
....*....|.
gi 295789127 560 VTGKIERAKLR 570
Cdd:PRK08043 698 GSGKPDFVTLK 708
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
216-571 |
7.09e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.82 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTIsdtawimnilgaflepwvlgacifvhlLPKFDS- 294
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNL-LANRAQVAARIDFSPEDKVFNA---------------------------LPVFHSf 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 295 ----QTVLKVLSSYPInTLVGAPIIYR------------MLLQQD--LS-------SYKFPHLHSCFSGGETLLPETLEN 349
Cdd:PRK06814 848 gltgGLVLPLLSGVKV-FLYPSPLHYRiipeliydtnatILFGTDtfLNgyaryahPYDFRSLRYVFAGAEKVKEETRQT 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 350 WKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFA--HY---DVQVIDEQGNVLPPGkegdiairvkpiwPIGMf 424
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPgiEYrlePVPGIDEGGRLFVRG-------------PNVM- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 425 SGYV--DNPKKTQDNIRGdfWL-MGDRGIKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVIS 501
Cdd:PRK06814 993 LGYLraENPGVLEPPADG--WYdTGDIVTIDEEGFITIKGRAKRFAKIAG-----EMISLAAVEELAAELWPDALHAAVS 1065
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295789127 502 SPDPSRGEVvkafVVLapefLSHDRDQLTKVLQEHVKSVTAPYKY-PRKVEFVLDLPKTVTGKIERAKLRA 571
Cdd:PRK06814 1066 IPDARKGER----IIL----LTTASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
78-573 |
3.69e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 78 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP---GTIQMRSSDILyrlQASKA 154
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRT 3818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 155 RAIVAGDEVAQEVDAVAPDCS-FLKIKLLVSENSREGwlnfkallkEASTIHQCVETESRESAAIYFTSGTSGPPK--MA 231
Cdd:PRK05691 3819 PVLVCSAACREQARALLDELGcANRPRLLVWEEVQAG---------EVASHNPGIYSGPDNLAYVIYTSGSTGLPKgvMV 3889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 232 EHSHCslgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILgAFLEPWVLGAciFVHLLPK---FDSQTVLKVLSSYPINT 308
Cdd:PRK05691 3890 EQRGM---LNNQLSKVPYLALSEADVIAQTASQSFDISVW-QFLAAPLFGA--RVEIVPNaiaHDPQGLLAHVQAQGITV 3963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 309 LVGAP-IIYRMLLQQDLSsykFPHLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTEtgliC-------RVSRTmKV 379
Cdd:PRK05691 3964 LESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAE----CsddvaffRVDLA-ST 4035
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 380 KPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGD----FWLMGDRG 449
Cdd:PRK05691 4036 RGSYLpiGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFGApgerLYRTGDLA 4110
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 450 IKDPEGYFHFIGRSDDIINSSGayfcrYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVLAPEFLSHdrDQL 529
Cdd:PRK05691 4111 RRRSDGVLEYVGRIDHQVKIRG-----YRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYLVPHQTVLAQ--GAL 4182
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 295789127 530 TKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 573
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALD 4226
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
331-539 |
7.37e-08 |
|
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: 55.30 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 331 HLHSCFSGGETLLPETLEnWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKE- 408
Cdd:cd17639 251 RLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYSTDKPPp 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 409 -GDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDII-NSSGAYfcryrIGPSEVE 485
Cdd:cd17639 330 rGEILIRGPNV-----FKGYYKNPEKTKEAFDGDGWFHtGDIGEFHPDGTLKIIDRKKDLVkLQNGEY-----IALEKLE 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 295789127 486 NALMEHPAVSETAVISSPDPSRgevVKAFVVlaPeflshDRDQLTKVLQEHVKS 539
Cdd:cd17639 400 SIYRSNPLVNNICVYADPDKSY---PVAIVV--P-----NEKHLTKLAEKHGVI 443
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
216-570 |
9.79e-08 |
|
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: 54.91 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 216 AAIYFTSGTSGPPKMAEHSHcslgikakmdaaswtglstSDIIWTISDTAWIMNILGAFLEPWVL--------------- 280
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTH-------------------GNIVSNVAGVFKILEILNKINPTDVYisylplahifervve 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 281 ------GACI-FVHLLPK--FDSQTVLK--VLSSYP----------INTLVGAPIIYRMLLQQdLSSYKFPHL------- 332
Cdd:cd05927 178 alflyhGAKIgFYSGDIRllLDDIKALKptVFPGVPrvlnriydkiFNKVQAKGPLKRKLFNF-ALNYKLAELrsgvvra 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 333 HSCF--------------------SGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYD 392
Cdd:cd05927 257 SPFWdklvfnkikqalggnvrlmlTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 393 VQVID--EQG-NVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN 468
Cdd:cd05927 337 VKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKDPEKTAEALDEDGWLhTGDIGEWLPNGTLKIIDRKKNIFK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 469 -SSGAYfcryrIGPSEVENALMEHPAVSETAV-----------ISSPDP--------SRGEVVKAFVVLA--PEFLSHDR 526
Cdd:cd05927 412 lSQGEY-----VAPEKIENIYARSPFVAQIFVygdslksflvaIVVPDPdvlkewaaSKGGGTGSFEELCknPEVKKAIL 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 295789127 527 DQLTKVLQEH-VKSvtapYKYPRKVEFVLDLPK------TVTGKIERAKLR 570
Cdd:cd05927 487 EDLVRLGKENgLKG----FEQVKAIHLEPEPFSvengllTPTFKLKRPQLK 533
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
113-580 |
2.69e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 50.20 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 113 LPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQE------VDAVAPDCSFLKIKLLVSEN 186
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 187 S-----REGWLNFKALLKEASTIHQCVETESRESAA-------IYFTSGTSGPPKMAEHSHCSlGIKAKMDAASWTGLST 254
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGSVGGNEYSPVYApvesvtnILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 255 SDIIWTISDTAWIMNilgaflePWVL------GACIFV-HLLP------KFDSQTVLKVLSSYPinTLVGApiiYRMLLQ 321
Cdd:PLN03051 160 GDVVCWPTNLGWMMG-------PWLLysaflnGATLALyGGAPlgrgfgKFVQDAGVTVLGLVP--SIVKA---WRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 322 QDLSSYKFPHLHSCFSGGETLLPET---LENWKAKTGlEIREIYGQTETGLICRVSRTMKVK-PGYLGTAFAHYDVQVID 397
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 398 EQGNVLPPGKE--GDIAIRVkpiwPIGMFSGYVDNpkKTQDNIRGDFWLM-----------GDRGIKDPEGYFHFIGRSD 464
Cdd:PLN03051 307 DNGVPYPDDQPcvGEVALAP----PMLGASDRLLN--ADHDKVYYKGMPMygskgmplrrhGDIMKRTPGGYFCVQGRAD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 465 DIINSSGayfcrYRIGPSEVENALME-HPAVSETAVISSPDPSRGE----VVKAFVVLAPEFLSHDRDQLTKVLQEHVKS 539
Cdd:PLN03051 381 DTMNLGG-----IKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQT 455
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 295789127 540 VTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK-TSGRA 580
Cdd:PLN03051 456 NLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRS 497
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
337-513 |
1.21e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.09 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 337 SGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID----EQGNVLPPGKEGDIA 412
Cdd:PLN02736 383 SGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemNYTSEDQPYPRGEIC 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 413 IRvKPIwpigMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN-SSGAYfcryrIGPSEVENALME 490
Cdd:PLN02736 463 VR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEY-----IAPEKIENVYAK 532
|
170 180 190
....*....|....*....|....*....|....
gi 295789127 491 HPAVSETAV-----------ISSPDPsrgEVVKA 513
Cdd:PLN02736 533 CKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
404-574 |
2.61e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 44.04 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 404 PPgkEGDIAIRVKPiwpigMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN-SSGAYfcryrIGPS 482
Cdd:PLN02430 463 PP--RGEICVRGKC-----LFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEY-----VALE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 483 EVENALMEHPAVSETAVISspDPSRGEVVkAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTg 562
Cdd:PLN02430 531 YLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEENTNKWAK-----DNGFTGSFEELCSLPELKEHILSELKSTA- 601
|
170
....*....|..
gi 295789127 563 kiERAKLRAKEW 574
Cdd:PLN02430 602 --EKNKLRGFEY 611
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
72-165 |
5.40e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 39.64 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789127 72 MNGSGKEIK-WSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP--------------G 136
Cdd:cd05905 5 LDSKGKEATtLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPieppdisqqlgfllG 84
|
90 100 110
....*....|....*....|....*....|..
gi 295789127 137 TIQMR---SSDILYRLQASKARAIVAGDEVAQ 165
Cdd:cd05905 85 TCKVRvalTVEACLKGLPKKLLKSKTAAEIAK 116
|
|
| |
