|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
66-594 |
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: 933.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 66 PAKFNFASDVIDHWASVEKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWW 145
Cdd:cd05928 2 PEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 146 LMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKE 225
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 226 ASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVL 305
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 GACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 385
Cdd:cd05928 242 GACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIGMFSGYVDNPKKTQDNIRG 465
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 466 DFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD 545
Cdd:cd05928 402 DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 74183796 546 RDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 594
Cdd:cd05928 482 PEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
106-591 |
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: 598.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 185
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHcSLGI 265
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHTH-SYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 266 KAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 345
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQG 425
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 426 NVLPPGKEGDIAIRVKpiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVE 505
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 506 NALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIE 585
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 74183796 586 RAKLRA 591
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
65-594 |
3.21e-177 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 513.51 E-value: 3.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 65 APAKFNFASDVIDHWASvekagKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW 144
Cdd:COG0365 4 VGGRLNIAYNCLDRHAE-----GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 145 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVA---------QEVDAVAPDCSFLKIKLLV----SEN 211
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 212 SREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAW 291
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 292 IMNILGAFLEPWVLGACIFVH-LLPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGET 366
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 367 LLPETLENWKAKTGLEIREIYGQTETGLICrVS--RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiW 444
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGGIF-ISnlPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-GP-W 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 445 PiGMFSGYVDNPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVIS 521
Cdd:COG0365 395 P-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 522 SPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 594
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
65-593 |
8.49e-160 |
|
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: 468.13 E-value: 8.49e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 65 APAKFNFASDVIDHWASvEKAGKRssgpALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW 144
Cdd:cd05970 12 VPENFNFAYDVVDAMAK-EYPDKL----ALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 145 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA--GDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKAL 222
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 223 LKEASTI----HQCVETESRESAAIYFTSGTSGPPKMAEHSHC-SLG--IKAKMdaasWTGLSTSDIIWTISDTAWIMNI 295
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGhiVTAKY----WQNVREGGLHLTVADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 296 LGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENW 375
Cdd:cd05970 242 WGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 376 KAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIGMFSGYVDN 455
Cdd:cd05970 322 KEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 456 PKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFV 535
Cdd:cd05970 402 AEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 536 VLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:cd05970 482 VLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
74-600 |
2.48e-117 |
|
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: 356.04 E-value: 2.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 74 DVIDHWASvekagKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMR 153
Cdd:COG0318 3 DLLRRAAA-----RHPDRPALVFGGRR-----LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 154 TGLVFMPGTIQMRSSDILYRLQASKARAIVAgdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcv 233
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 234 etesresAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHL 313
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANA-AAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT--LVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 314 LPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET 392
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 GLIC--RVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWLM 470
Cdd:COG0318 253 SPVVtvNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 471 GDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLT 550
Cdd:COG0318 328 GDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA-ELDAEELR 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 74183796 551 KVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 600
Cdd:COG0318 407 AFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-591 |
4.46e-113 |
|
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: 344.80 E-value: 4.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 184
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSL- 263
Cdd:cd05971 85 --------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 264 ----GIKAKMDAASWTGlstsDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPI 339
Cdd:cd05971 115 ghlpGVQFPFNLFPRDG----DLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 340 IYRMLLQQDLSSYKFP-HLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLI---CrvSRTMKVKPGYLGTAFAH 415
Cdd:cd05971 191 ALKMMRQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVignC--SALFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 416 YDVQVIDEQGNVLPPGKEGDIAIRV-KPIwpigMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINS 494
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVELpDPV----AFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 495 SGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVL 574
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVN 422
|
490
....*....|....*..
gi 74183796 575 DLPKTVTGKIERAKLRA 591
Cdd:cd05971 423 ELPRTATGKIRRRELRA 439
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
68-593 |
3.47e-106 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 331.47 E-value: 3.47e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 68 KFNFASDVIDHWASVEKAGKrssgPALWWMNGSGKEiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLM 147
Cdd:PRK04319 41 KVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 148 ILGCMRTGLV-------FMPGTIqmRSsdilyRLQASKARAIVAGDEVAQEVdaVAPDCSFLKIKLLVSENSR--EGWLN 218
Cdd:PRK04319 115 LLGALKNGAIvgplfeaFMEEAV--RD-----RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 219 FKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHcslgiKAkMDAASWTG-----LSTSDIIWTISDTAWIM 293
Cdd:PRK04319 186 FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-----NA-MLQHYQTGkyvldLHEDDVYWCTADPGWVT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 294 NILGAFLEPWVLGACIFVhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETLLPE 370
Cdd:PRK04319 260 GTSYGIFAPWLNGATNVI-DGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLNPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 371 TLEnWKAKT-GLEIREIYGQTETG--LICRVsRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIrvKPIWPiG 447
Cdd:PRK04319 339 VVR-WGMKVfGLPIHDNWWMTETGgiMIANY-PAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-S 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 448 MFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSR 527
Cdd:PRK04319 414 MMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVR 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74183796 528 GEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK04319 494 GEIIKAFVALRPGY--EPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
107-593 |
8.99e-103 |
|
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: 317.97 E-value: 8.99e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKArAIVAGD 186
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSLGIk 266
Cdd:cd05974 80 EN----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPV- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ 346
Cdd:cd05974 113 GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 347 QDLSSYKFPhLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGN 426
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 427 vlpPGKEGDIAIRVKPIWPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVEN 506
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 507 ALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVlDLPKTVTGKIER 586
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 74183796 587 AKLRAKE 593
Cdd:cd05974 426 VELRRRE 432
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-590 |
5.23e-101 |
|
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: 314.50 E-value: 5.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 83 EKAGKRSSGPALWWMngsGKeiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 162
Cdd:cd05936 7 EAARRFPDKTALIFM---GR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 163 IQMRSSDILYRLQASKARAIVAGDEvaqevdavapdcsflkikllvsensregwlnFKALLKEASTIHQCVETESRESAA 242
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTPEDVAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIwtisdtawIMNILGAF---------LEPWVLGACIFvhL 313
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDV--------VLAALPLFhvfgltvalLLPLALGATIV--L 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 314 LPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET 392
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 G-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGDFWL 469
Cdd:cd05936 280 SpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAFVDGWLR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQL 549
Cdd:cd05936 353 TGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG-ASLTEEEI 431
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 74183796 550 TKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05936 432 IAFCREQL----AGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
106-593 |
1.48e-98 |
|
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: 307.51 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 185
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEVAQEVDAVAPdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPKMAEHSHCSLgI 265
Cdd:cd05969 80 EELYERTDPEDP-------------------------------------------TLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 266 KAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLlPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 345
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQD---LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG--LICRVSrTMKVKPGYLGTAFAHYDVQV 420
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsiMIANYP-CMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 421 IDEQGNVLPPGKEGDIAIrvKPIWPiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIG 500
Cdd:cd05969 274 VDENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 501 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTV 580
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 74183796 581 TGKIERAKLRAKE 593
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
241-584 |
3.30e-93 |
|
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: 289.96 E-value: 3.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACIFvhLLPKFDSQ 320
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLG-ALLAGGTVV--LLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 321 TVLKVLSSYPINTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVS 399
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 400 R--TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD 477
Cdd:cd04433 159 PpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 478 PEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLTKVLQEHV 557
Cdd:cd04433 234 EDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-----ADLDAEELRAHV 308
|
330 340
....*....|....*....|....*..
gi 74183796 558 KSVTAPYKYPRKVEFVLDLPKTVTGKI 584
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
107-590 |
2.41e-89 |
|
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: 283.26 E-value: 2.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAgd 186
Cdd:cd05973 2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQevdavapdcsflkikllvsensregwlnfKALLKEASTIHQcvetesresaaiyFTSGTSGPPKMAEHSHCSL-GI 265
Cdd:cd05973 79 DAAN-----------------------------RHKLDSDPFVMM-------------FTSGTTGLPKGVPVPLRALaAF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 266 KAKMDAAswTGLSTSDIIWTISDTAWIMNILGAFLEPWVLG-ACIFVHllPKFDSQTVLKVLSSYPINTLVGAPIIYRML 344
Cdd:cd05973 117 GAYLRDA--VDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 345 LQQDLSSYKFP--HLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMK--VKPGYLGTAFAHYDVQV 420
Cdd:cd05973 193 MAAGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 421 IDEQGNVLPPGKEGDIAIRVKPIwPIGMFSGYVDNPKKTQDnirGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIG 500
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 501 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTV 580
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
490
....*....|
gi 74183796 581 TGKIERAKLR 590
Cdd:cd05973 427 SGKIQRFLLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
67-590 |
5.80e-88 |
|
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: 281.95 E-value: 5.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 67 AKFNFASDVIDHwasveKAGKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWL 146
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 147 MILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSRE--GWLNFKALLK 224
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 225 EASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEP-W 303
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 304 VLGACIfvhLLPKFDS-QTVLKVLSSYPINTLVGAPIIYR-MLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL 381
Cdd:cd05959 230 VGATTV---LMPERPTpAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 382 EIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKT 459
Cdd:cd05959 307 DILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR-------GpsSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 460 QDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP 539
Cdd:cd05959 380 RDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRP 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 74183796 540 EFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05959 460 GY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
103-590 |
1.99e-86 |
|
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: 275.90 E-value: 1.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQ-ASKARA 181
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDkARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 IVAGDEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHC 261
Cdd:cd05958 88 LCAHAL-----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 262 SLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGA-CIfvhLLPKFDSQTVLKVLSSYPINTLVGAPII 340
Cdd:cd05958 121 DPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsGV---LLEEATPDLLLSAIARYKPTVLFTAPTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 341 YRMLL------QQDLSSykfphLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFA 414
Cdd:cd05958 198 YRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 415 HYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpigmfSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:cd05958 273 GYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 SSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHdrDQLTKVLQEHVKSVTAPYKYPRKVEFV 573
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPG--PVLARELQDHAKAHIAPYKYPRAIEFV 422
|
490
....*....|....*..
gi 74183796 574 LDLPKTVTGKIERAKLR 590
Cdd:cd05958 423 TELPRTATGKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-595 |
6.47e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 271.67 E-value: 6.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 85 AGKRSSGPALWWMngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQ 164
Cdd:PRK06187 16 ARKHPDKEAVYFD-----GRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 165 MRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREG----WLNFKALLKEASTIHQCVETESRES 240
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMNiLGAFLEPWVLGACIfvhLLPK-FDS 319
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHRNLFLHS-LAVCAWLKLSRDDVYLVIVPMFHVHA-WGLPYLALMAGAKQ---VIPRrFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 320 QTVLKVLSSYPINTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRV 398
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 399 SR------TMKVKPGYLGTAFAHYDVQVIDEQGNVLPP-GKE-GDIAIRvKPiWpigMFSGYVDNPKKTQDNIRGDfWL- 469
Cdd:PRK06187 325 LPpedqlpGQWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP-W---LMQGYWNRPEATAETIDGG-WLh 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQL 549
Cdd:PRK06187 399 TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGA-TLDAKEL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 74183796 550 TKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 595
Cdd:PRK06187 478 RAFLRGRL----AKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
80-592 |
1.43e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 260.22 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 80 ASVEKAGKR-SSGPALWWMngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVF 158
Cdd:PRK07656 9 ELLARAARRfGDKEAYVFG-----DQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 159 MPGTIQMRSSDILYRLQASKARAIVAGDEVaQEVDAVAPDcSFLKIKLLV------SENSREGWLNFKALLKEASTIHQC 232
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGLF-LGVDYSATT-RLPALEHVViceteeDDPHTEKMKTFTDFLAAGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 233 VETESRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSD--II---------WTISDTAWIMNilgafle 301
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQL-LSNAADWAEYLGLTEGDryLAanpffhvfgYKAGVNAPLMR------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 302 pwvlGACIFVHllPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 380
Cdd:PRK07656 233 ----GATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 381 LE-IREIYGQTE---TGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNP 456
Cdd:PRK07656 307 VDiVLTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR----GPNVM-KGYYDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 457 KKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFV 535
Cdd:PRK07656 382 EATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74183796 536 VLAP-------EFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK07656 462 VLKPgaelteeELIAYCREHLAK------------YKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
107-590 |
5.01e-75 |
|
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: 245.83 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevDAVApdcsflkikllvsensreGWLnfkallkeastihqcvetesresaaiyFTSGTSGPPKMAEHSHCSLGIK 266
Cdd:cd05919 91 ------DDIA------------------YLL---------------------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPKfDSQTVLKVLSSYPINTLVGAPIIY-RMLL 345
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQG 425
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 426 NVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVE 505
Cdd:cd05919 279 HTIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 506 NALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIE 585
Cdd:cd05919 354 SLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
....*
gi 74183796 586 RAKLR 590
Cdd:cd05919 432 RFKLR 436
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
99-495 |
2.70e-69 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 230.28 E-value: 2.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 99 GSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASK 178
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 179 ARAIVAGDE-VAQEVDAVAPDCSFLKIKLLVS-ENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMA 256
Cdd:pfam00501 94 AKVLITDDAlKLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 EHSH---CSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI-FVHLLPKFDSQTVLKVLSSYPIN 332
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVvLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTM---KVKPGY 408
Cdd:pfam00501 254 VLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 LGTAFAHYDVQVIDEQ-GNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIG 486
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR-GP----GVMKGYLNDPELTAEAFDEDGWYrTGDLGRRDEDGYLEIVG 408
|
....*....
gi 74183796 487 RSDDIINSS 495
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
85-584 |
4.44e-69 |
|
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: 230.19 E-value: 4.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 85 AGKRSSGPALWWMNGSgkeikWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiq 164
Cdd:cd17631 5 ARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 165 mrssdILYRLQASKARAIVAgdevaqevDAVApdcsflkiKLLVSENSRegwlnfkallkeastihqcvetesresaaIY 244
Cdd:cd17631 75 -----LNFRLTPPEVAYILA--------DSGA--------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 245 FTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDI---IWTISDTAwimnILGAFLEPwVLGACIFVHLLPKFDSQT 321
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNA-VNALAALDLGPDDVllvVAPLFHIG----GLGVFTLP-TLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETG-LICRVS 399
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 400 RTMKV-KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDP 478
Cdd:cd17631 258 PEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDGWFHTGDLGRLDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 479 EGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrDQLTKV-LQEHV 557
Cdd:cd17631 333 DGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG------AELDEDeLIAHC 406
|
490 500
....*....|....*....|....*..
gi 74183796 558 KSVTAPYKYPRKVEFVLDLPKTVTGKI 584
Cdd:cd17631 407 RERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
68-590 |
1.26e-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: 230.88 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 68 KFNFASDVIDHWASVEKAGKrssgpaLWWMNGSGKeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLM 147
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGK------TAFIDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 148 ILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKiKLLVSENSREGWLNFKALLKEAS 227
Cdd:TIGR02262 72 FLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLE-HRVVVGRPEAGEVQLAELLATES 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 228 TIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGA 307
Cdd:TIGR02262 151 EQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 308 CIFVHL-LPKFDSqtVLKVLSSYPINTLVGAPIIYR-MLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 385
Cdd:TIGR02262 231 TTVLMGeRPTPDA--VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGMFS--GYVDNPKKTQDNI 463
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-------GPSSatMYWNNRAKSRDTF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 464 RGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFls 543
Cdd:TIGR02262 382 QGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 74183796 544 hdrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:TIGR02262 460 ---TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
67-584 |
1.89e-68 |
|
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: 232.85 E-value: 1.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 67 AKFNFASDVIDHwaSVEKAGKRSsgpALWWMNGSGKEIK-WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWW 145
Cdd:cd17634 50 ATLNLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 146 LMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEV---------------AQEVDAVAPDCSFLKIKLLVSE 210
Cdd:cd17634 124 VAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGvragrsvplkknvddALNPNVTSVEHVIVLKRTGSDI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 211 NSREG-WLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDT 289
Cdd:cd17634 204 DWQEGrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 290 AWIMNILGAFLEPWVLGACIFVHL-LPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGG 364
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 365 ETLLPETLENWKAKTGLEIREI---YGQTETGLICRVSRTMKV--KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIR 439
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEKCPVvdtWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 440 VKpiWPIGMFSGYVDNPKKTQDNIR--GDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSET 517
Cdd:cd17634 444 DP--WPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 518 AVISSPDPSRGEVVKAFVVLAPEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 584
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
105-591 |
4.85e-68 |
|
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: 227.56 E-value: 4.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 184
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPKMAEHSHCSLG 264
Cdd:cd05941 91 P-------------------------------------------------------ALILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKAKMDAASWTglstsdiiWTISD----------TAWIMNILGAFLepWVLGACIFvhlLPKFDSQTVLKVLSSYPINTL 334
Cdd:cd05941 116 ANVRALVDAWR--------WTEDDvllhvlplhhVHGLVNALLCPL--FAGASVEF---LPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 335 VGAPIIYRMLLQ---------QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVK 405
Cdd:cd05941 183 MGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 406 PGYLGTAFAHYDVQVIDEQGN-VLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFH 483
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYYW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 484 FIGR-SDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQLTkvlqEHVKSVTA 562
Cdd:cd05941 338 ILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWAKQRLA 413
|
490 500
....*....|....*....|....*....
gi 74183796 563 PYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
107-589 |
7.11e-67 |
|
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: 224.28 E-value: 7.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesRESAAIYFTSGTSGPPKMAEHSHCSLGIK 266
Cdd:cd05935 82 EL-------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AkMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ 346
Cdd:cd05935 113 A-LQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYV--LMARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 347 Q-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID-EQ 424
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 425 GNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQD---NIRG-DFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIG 500
Cdd:cd05935 270 GRELPPNEVGEIVVRGPQI-----FKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 501 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdRDQLTKV-LQEHVKSVTAPYKYPRKVEFVLDLPKT 579
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEY----RGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRS 420
|
490
....*....|
gi 74183796 580 VTGKIERAKL 589
Cdd:cd05935 421 ASGKILWRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
100-590 |
9.03e-67 |
|
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: 225.65 E-value: 9.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 100 SGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKA 179
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQEVD--AVAPDCSFLKIKLLV---SENSREGWLNF-KALLKEASTihqcvETESRES--AAIYFTSGTSG 251
Cdd:cd05926 88 KLVLTPKGELGPASraASKLGLAILELALDVgvlIRAPSAESLSNlLADKKNAKS-----EGVPLPDdlALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 252 PPKMAEHSHCSLgikakmdAASWTGLSTSDIIwTISDTAWIM-------NILGAFLEPWVLGACIFVHllPKFDSQTVLK 324
Cdd:cd05926 163 RPKGVPLTHRNL-------AASATNITNTYKL-TPDDRTLVVmplfhvhGLVASLLSTLAAGGSVVLP--PRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 325 VLSSYPINTLVGAPIIYRMLLQQDLSSY--KFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG--LICRVSR 400
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 401 TMKVKPGYLGTAFAhYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPE 479
Cdd:cd05926 313 PGPRKPGSVGKPVG-VEVRILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 480 GYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLApEFLSHDRDQLTKVLQEHVks 559
Cdd:cd05926 387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR-EGASVTEEELRAFCRKHL-- 463
|
490 500 510
....*....|....*....|....*....|.
gi 74183796 560 vtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05926 464 --AAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-590 |
1.27e-66 |
|
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: 223.32 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 184
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdaVAPdcsflkikllvsensregwlnfkallkeastihqcvetesresAAIYFTSGTSGPPK--MAEHSH-C 261
Cdd:cd05934 81 ----------VDP-------------------------------------------ASILYTSGTTGPPKgvVITHANlT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 262 SLGIKAkmdaASWTGLSTSDIIWTI-----SDtAWIMNILGAFlepWVLGACIfvhLLPKFDSQTVLKVLSSY--PINTL 334
Cdd:cd05934 108 FAGYYS----ARRFGLGEDDVYLTVlplfhIN-AQAVSVLAAL---SVGATLV---LLPRFSASRFWSDVRRYgaTVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 335 VGAPIiyRMLLQQDLSSYKFPH-LHSCFSGGETllPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAF 413
Cdd:cd05934 177 LGAML--SYLLAQPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 414 AHYDVQVIDEQGNVLPPGKEGDIAIRVKPiwPIGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIRGLR--GWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 SSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP-------EFLSHDRDQLtkvlqehvksvtAPYKY 566
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgetldpeELFAFCEGQL------------AYFKV 398
|
490 500
....*....|....*....|....
gi 74183796 567 PRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
102-590 |
6.38e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 221.73 E-value: 6.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 102 KEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARA 181
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 IVAGDEVAQEVDAVAPDCSFLKIKLLVSENSRE---GWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEH 258
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 259 SHCSLgIKAKMDAASWTGLSTSDIiwtisdtawimNI----------LGAFLEPWV-LGACifVHLLPKFDSQTVLKVLS 327
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDI-----------PLhalplyhcaqLDVFLGPYLyVGAT--NVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPIIYRMLL------QQDLSSykfphLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTETGLICRVSR 400
Cdd:PRK08316 258 AERITSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQTEIAPLATVLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 401 --TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDFWLMGDRGIKDP 478
Cdd:PRK08316 333 peEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRS----PQLM-LGYWDDPEKTAEAFRGGWFHSGDLGVMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 479 EGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrDQLT-KVLQEHV 557
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDELIAHC 481
|
490 500 510
....*....|....*....|....*....|...
gi 74183796 558 KSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK08316 482 RARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
48-591 |
2.04e-64 |
|
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: 222.37 E-value: 2.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 48 FHMNIKKLIPIQW-----------GHQEAPAKF-----NFASDVIDHWAsvekaGKRSSGPALWWMNGSGKEIKWSFREL 111
Cdd:cd05968 23 FWGEFVKDVGIEWyeppyqtldlsGGKPWAAWFvggrmNIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 112 SEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD----- 186
Cdd:cd05968 98 LYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 ----EVAQEVD-AVAPDCSFLKIKLLVSENSREGWLN----FKALLKEASTIHqCVETESRESAAIYFTSGTSGPPKMAE 257
Cdd:cd05968 177 grevNLKEEADkACAQCPTVEKVVVVRHLGNDFTPAKgrdlSYDEEKETAGDG-AERTESEDPLMIIYTSGTTGKPKGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 258 HSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMN---ILGAFLepwvLGACIFVHL-LPKFDSQTVL-KVLSSYPIN 332
Cdd:cd05968 256 HVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGpwlIFGGLI----LGATMVLYDgAPDHPKADRLwRMVEDHEIT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWK------AKTGLEIREIYGQTET--GLICRVSrTMKV 404
Cdd:cd05968 332 HLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNwlfetvGKGRNPIINYSGGTEIsgGILGNVL-IKPI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 405 KPGYLGTAFAHYDVQVIDEQGNVLPPgKEGDIAIRvKPiWPiGMFSGYVDNPKKTQDNIRG---DFWLMGDRGIKDPEGY 481
Cdd:cd05968 411 KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-AP-WP-GMTRGFWRDEDRYLETYWSrfdNVWVHGDFAYYDEEGY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 482 FHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD--RDQLTKVLQEHVKS 559
Cdd:cd05968 487 FYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGK 566
|
570 580 590
....*....|....*....|....*....|..
gi 74183796 560 vtaPYKyPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:cd05968 567 ---PLS-PERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
105-584 |
7.58e-64 |
|
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: 217.85 E-value: 7.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI-V 183
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIfT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 AGDEVAQEVDAVApdCSFLKIKLLVSENSREGWLNFKALLKEASTIH-----QCVETESRESAAIYFTSGTSGPPKMAEH 258
Cdd:cd05911 89 DPDGLEKVKEAAK--ELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEdedlpPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 259 SHCSLGIKAKMDAASWTGLSTS-DIIWTISDTAWIMNILGAFLEPWvLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA 337
Cdd:cd05911 167 SHRNLIANLSQVQTFLYGNDGSnDVILGFLPLYHIYGLFTTLASLL-NGAT--VIIMPKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 338 PIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTETGLICRVSRTMKVKPGYLGTAFAH 415
Cdd:cd05911 244 PPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 416 YDVQVIDEQGN-VLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:cd05911 324 VEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 SSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDrDQLTKVLQEHVksvtAPYKYPRK-VEF 572
Cdd:cd05911 399 YKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-KEVKDYVAKKV----ASYKQLRGgVVF 473
|
490
....*....|..
gi 74183796 573 VLDLPKTVTGKI 584
Cdd:cd05911 474 VDEIPKSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
79-599 |
9.47e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 210.97 E-value: 9.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 79 WASVEKAGKR-SSGPALWWMngsGKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV 157
Cdd:PRK08314 13 FHNLEVSARRyPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 158 FMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEV------------------DAVAPDC-----SFLKIKLLVSENSRE 214
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPeiavpAWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 215 GWLNFKALLKEASTIHQcVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDTAWIMN 294
Cdd:PRK08314 168 GVVAWKEALAAGLAPPP-HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA-VGSVLWSNSTPESVVLAVLPLFHVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 295 ILGAFLEPWVLGACIFvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ------DLSSYKfphlhsCFSGGETLL 368
Cdd:PRK08314 246 MVHSMNAPIYAGATVV--LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASpglaerDLSSLR------YIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 369 PETL-ENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvKPiwpi 446
Cdd:PRK08314 318 PEAVaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GP---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 447 GMFSGYVDNPKKTQD---NIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISS 522
Cdd:PRK08314 393 QVFKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 523 PDPSRGEVVKAFVVLAPEFLSH-DRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGR 599
Cdd:PRK08314 473 PDPRRGETVKAVVVLRPEARGKtTEEEIIAWAREHM----AAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
59-591 |
6.10e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 209.13 E-value: 6.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 59 QWGHQEAPAkfnfaSDVIDHWASvekagKRSSGPALWWMngsGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVL 138
Cdd:PRK06178 27 EYPHGERPL-----TEYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 139 PRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKI------KLLVSENS 212
Cdd:PRK06178 91 PNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVivtslaDVLPAEPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 213 R-------------EGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLST 279
Cdd:PRK06178 171 LplpdslraprlaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 280 SDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSYK 353
Cdd:PRK06178 251 DSVFLSFLPEFWIAGENFGLLFPLFSGAT--LVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMdhprfaEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 354 FPhlhSCFSGGETLLPETLENWKAKTGLEIREI-YGQTETGLICRVSRTMKV-------KPGYLGTAFAHYDVQVID-EQ 424
Cdd:PRK06178 329 QV---RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFQDddfdllsQPVFVGLPVPGTEFKICDfET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 425 GNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSE 503
Cdd:PRK06178 406 GELLPLGAEGEIVVRTPSL-----LKGYWNKPEATAEALR-DGWLhTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 504 VENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRDQLTkvLQEHVKSVTAPYKYPrKVEFVLDLPKTVTGK 583
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTAAA--LQAWCRENMAVYKVP-EIRIVDALPMTATGK 553
|
....*...
gi 74183796 584 IERAKLRA 591
Cdd:PRK06178 554 VRKQDLQA 561
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
106-590 |
8.89e-58 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 202.03 E-value: 8.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 185
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEVAQEVDAVAPDCSFLKIKLLVSEnsREGWLnfKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGI 265
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETLDAD--GTGSL--LEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 266 KAKMDAASWTglstsdiiWTISDTAW----IMNILGAFLEPWVL----GACIFvhlLPKFDSQTVLKVLssyPINT-LVG 336
Cdd:PRK07514 184 NALTLVDYWR--------FTPDDVLIhalpIFHTHGLFVATNVAllagASMIF---LPKFDPDAVLALM---PRATvMMG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 337 APIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLIC-------RVsrtmkvkPGY 408
Cdd:PRK07514 250 VPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTsnpydgeRR-------AGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 LGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHF 484
Cdd:PRK07514 323 VGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 485 IGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLTKVLQEHVksvtAPY 564
Cdd:PRK07514 396 VGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA-ALDEAAILAALKGRL----ARF 470
|
490 500
....*....|....*....|....*.
gi 74183796 565 KYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK07514 471 KQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
70-591 |
9.64e-58 |
|
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: 204.47 E-value: 9.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 70 NFASDVIDHWAsveKAGkRSSGPALWWMNGS-GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMI 148
Cdd:cd05967 50 NTCYNALDRHV---EAG-RGDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAIAM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 149 LGCMRTG----LVFmpGTIQmrSSDILYRLQASKARAIVAGD---------------EVAQEVDAVAPDCSFLKIKLLVS 209
Cdd:cd05967 125 LACARIGaihsVVF--GGFA--AKELASRIDDAKPKLIVTAScgiepgkvvpykpllDKALELSGHKPHHVLVLNRPQVP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 210 ENSR--EGWLNFKALLKEASTiHQCVETESRESAAIYFTSGTSGPPKmaehshcslGI----KAKMDAASWT-----GLS 278
Cdd:cd05967 201 ADLTkpGRDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPK---------GVvrdnGGHAVALNWSmrniyGIK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 279 TSDIIWTISDTAWIMN---ILGAflePWVLGA-CIFVHLLPKF--DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---- 348
Cdd:cd05967 271 PGDVWWAASDVGWVVGhsyIVYG---PLLHGAtTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgk 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 349 -LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETG----LICRVSRTMKVKPGYLGTAFAHYDVQVIDE 423
Cdd:cd05967 348 yIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 424 QGNVLPPGKEGDIAIRVkPIwPIGMFSGYVDNPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIG 500
Cdd:cd05967 428 DGEPVGPNELGNIVIKL-PL-PPGCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLS 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 501 PSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTV 580
Cdd:cd05967 506 TGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTR 584
|
570
....*....|.
gi 74183796 581 TGKIERAKLRA 591
Cdd:cd05967 585 SGKILRRTLRK 595
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
107-591 |
2.54e-57 |
|
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: 198.76 E-value: 2.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:cd05903 3 TYSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDAVAPDcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHCSLGIK 266
Cdd:cd05903 82 RFRQFDPAAMPD----------------------------------------AVALLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA-PIIYRMLL 345
Cdd:cd05903 122 IRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET-GLICRVSRTMKVKPGYL-GTAFAHYDVQVIDE 423
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 424 QGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSE 503
Cdd:cd05903 279 TGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 504 VENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEHvksVTAPYKYPRKVEFVLDLPKTVTGK 583
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFDELVAYLDRQ---GVAKQYWPERLVHVDDLPRTPSGK 429
|
....*...
gi 74183796 584 IERAKLRA 591
Cdd:cd05903 430 VQKFRLRE 437
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
106-595 |
3.38e-57 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 201.51 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 185
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEVAQ-----EVDAVAPDCSFLKIKLLVSENSRE-GWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHS 259
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVDKLAPAtSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 260 HCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSYPINTLVGA-P 338
Cdd:PRK06087 209 HNNI-LASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR--SVLLDIFTPDACLALLEQQRCTCMLGAtP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 339 IIYRMLLQQDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRV------SRTMkvkpGYLGTA 412
Cdd:PRK06087 286 FIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSPHAVVnlddplSRFM----HTDGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 413 FAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDI 491
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGEEASR-GP----NVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 492 INSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQLTKVLQEhvKSVtAPYKYPRKVE 571
Cdd:PRK06087 436 IVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSR--KRV-AKYKYPEHIV 512
|
490 500
....*....|....*....|....
gi 74183796 572 FVLDLPKTVTGKIERAKLRaKEWK 595
Cdd:PRK06087 513 VIDKLPRTASGKIQKFLLR-KDIM 535
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
92-600 |
3.04e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 195.59 E-value: 3.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 92 PALWWMNGSgkeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWL-----MILGCMRTGLVFMpGTIQmr 166
Cdd:PRK06188 29 PALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMaigaaQLAGLRRTALHPL-GSLD-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 167 ssDILYRLQASKARAIVAGD----EVAQEVDAVAPdcsflKIKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAA 242
Cdd:PRK06188 100 --DHAYVLEDAGISTLIVDPapfvERALALLARVP-----SLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASW------TGLSTSdiiwTISDTAwimnilGAFLEPWVL-GAciFVHLLP 315
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWewpadpRFLMCT----PLSHAG------GAFFLPTLLrGG--TVIVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 316 KFDSQTVLKVLSSYPIN-TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL 394
Cdd:PRK06188 241 KFDPAEVLRAIEEQRITaTFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 395 ICRVSRT---MKVKPGYLGTA---FAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDfW 468
Cdd:PRK06188 321 VITYLRKrdhDPDDPKRLTSCgrpTPGLRVALLDEDGREVAQGEVGEICVRG----PLVM-DGYWNRPEETAEAFRDG-W 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 469 L-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRD 547
Cdd:PRK06188 395 LhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG---AAVD 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 74183796 548 qlTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 600
Cdd:PRK06188 472 --AAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRA 522
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
67-591 |
4.16e-55 |
|
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: 197.01 E-value: 4.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 67 AKFNFASDVIDHWasVEKAGKRssgPALWWM-NGSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWW 145
Cdd:cd05966 50 GKLNISYNCLDRH--LKERGDK---VAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 146 LMILGCMRTGLV-------FMPGTIQMRSSDilyrlqaSKARAIVAGDEV---------AQEVDAVAPDCSFLKiKLLVS 209
Cdd:cd05966 124 IAMLACARIGAVhsvvfagFSAESLADRIND-------AQCKLVITADGGyrggkviplKEIVDEALEKCPSVE-KVLVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 210 ENS---------REGWLNfkALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCS--LGIKAKMDaasWT-GL 277
Cdd:cd05966 196 KRTggevpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGylLYAATTFK---YVfDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 278 STSDIIWTISDTAWIMN----ILGaflePWVLGACIFVH----LLPKFDS--QTVLKvlssYPINTLVGAPIIYRMLLQQ 347
Cdd:cd05966 271 HPDDIYWCTADIGWITGhsyiVYG----PLANGATTVMFegtpTYPDPGRywDIVEK----HKVTIFYTAPTAIRALMKF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 348 --------DLSSYKfpHLHSCfsgGETLLPETLENWKAKTGLE---IREIYGQTETG--LICRVSRTMKVKPGYLGTAFA 414
Cdd:cd05966 343 gdewvkkhDLSSLR--VLGSV---GEPINPEAWMWYYEVIGKErcpIVDTWWQTETGgiMITPLPGATPLKPGSATRPFF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 415 HYDVQVIDEQGNVLPPGKEGDIAIRvKPiWPiGMFSGYVDNPKKTQDNIRGDFW---LMGDRGIKDPEGYFHFIGRSDDI 491
Cdd:cd05966 418 GIEPAILDEEGNEVEGEVEGYLVIK-RP-WP-GMARTIYGDHERYEDTYFSKFPgyyFTGDGARRDEDGYYWITGRVDDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 492 INSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSVTAPYKYPRKVE 571
Cdd:cd05966 495 INVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQ 572
|
570 580
....*....|....*....|
gi 74183796 572 FVLDLPKTVTGKIERAKLRA 591
Cdd:cd05966 573 FVPGLPKTRSGKIMRRILRK 592
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
83-590 |
1.35e-54 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 193.75 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 83 EKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 162
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 163 IQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSF-LKIKLLVSENSRE--GWLNFKALL-KEASTIHQCVETESR 238
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPAddGVSSFTQLKaQQPATLCYAPPLSTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 239 ESAAIYFTSGTSGPPKMAEHSHCSL---GIkakmdAASW-TGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACiFVhLL 314
Cdd:PRK08008 174 DTAEILFTSGTTSRPKGVVITHYNLrfaGY-----YSAWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGAT-FV-LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 PKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPH--------LHscfsggetLLPETLENWKAKTGLEIREI 386
Cdd:PRK08008 247 EKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclrevmfyLN--------LSDQEKDAFEERFGVRLLTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 387 YGQTET--GLICRvsrtmkvKPG------YLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIWPIgmFSGYVDNPKK 458
Cdd:PRK08008 319 YGMTETivGIIGD-------RPGdkrrwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 459 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL 537
Cdd:PRK08008 390 TAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 538 AP-------EFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK08008 470 NEgetlseeEFFAFCEQNMAK------------FKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
103-591 |
9.74e-54 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 191.90 E-value: 9.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGW-LNFKAL-LKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 260
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 CSLGIKAKMDAASwTGLSTSDIIWTiSDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKVLSSY--PINTLVGAp 338
Cdd:PRK06155 203 AQFYWWGRNSAED-LEIGADDVLYT-TLPLFHTNALNAFFQALLAGAT--YVLEPRFSASGFWPAVRRHgaTVTYLLGA- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 339 iIYRMLLQQDLSSYKFPH-LHSCFSGGETllPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKvKPGYLGTAFAHYD 417
Cdd:PRK06155 278 -MVSILLSQPARESDRAHrVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVIDEQGNVLPPGKEGDIAIRVKPiwPIGMFSGYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSG 496
Cdd:PRK06155 354 ARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKDAIRRRG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 497 YRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP----EFLShdrdqltkvLQEHVKSVTAPYKYPRKVEF 572
Cdd:PRK06155 431 ENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgtalEPVA---------LVRHCEPRLAYFAVPRYVEF 501
|
490
....*....|....*....
gi 74183796 573 VLDLPKTVTGKIERAKLRA 591
Cdd:PRK06155 502 VAALPKTENGKVQKFVLRE 520
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
106-593 |
3.23e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 192.09 E-value: 3.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFmPGTIQMRSSDILYRLQASKARAIVA- 184
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 ----GDEVAQEVDAVAPDCSFLK-----------------IKLLVSENSREGWLNFKALLKEASTIHQCVETESRES--A 241
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDdvA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 242 AIYFTSGTSGPPKMAEHSHcslgikAKMDAASWTGLSTSDIiwTISDTawIMNILGAFLepwvLGACIFVHLLPKFDSQT 321
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTH------GNEVANAWLGALLLGL--GPGDT--VFCGLPLFH----VNALLVTGLAPLARGAH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VL-----------------KVLSSYPINTLVGAPIIYRMLLQQ-----DLSSYKFphlhsCFSGGETLLPETLENWKAKT 379
Cdd:PRK07529 283 VVlatpqgyrgpgvianfwKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY-----ALCGAAPLPVEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 380 GLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYDVQVI--DEQGNVL---PPGKEGDIAIRvKPiwpiGMFSGYV 453
Cdd:PRK07529 358 GVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GP----NVFSGYL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 454 dNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 532
Cdd:PRK07529 433 -EAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPV 511
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74183796 533 AFVVLAPEfLSHDRDQLTKVLQEHVKSVTApykYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK07529 512 AYVQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
101-595 |
1.01e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 189.47 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:PRK06710 47 GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPDCSFLKI------------KLLVSENSREGWLNFKALLKEASTIH--QCVETE---------- 236
Cdd:PRK06710 124 VILCLDLVFPRVTNVQSATKIEHVivtriadflpfpKNLLYPFVQKKQSNLVVKVSESETIHlwNSVEKEvntgvevpcd 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 237 -SRESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtglstsdIIWTISDTAWIMNILGAflEPWVLGACIFVH--- 312
Cdd:PRK06710 204 pENDLALLQYTGGTTGFPKGVMLTHKNL------------------VSNTLMGVQWLYNCKEG--EEVVLGVLPFFHvyg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 313 ----------------LLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENW 375
Cdd:PRK06710 264 mtavmnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 376 KAKTGLEIREIYGQTETGLICRVSRTMKVK-PGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYV 453
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 454 DNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 532
Cdd:PRK06710 419 NKPEETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVK 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 533 AFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 595
Cdd:PRK06710 498 AFVVLKEGTECSEEE-----LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
105-589 |
2.91e-52 |
|
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: 185.42 E-value: 2.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 184
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPKMAEHSHCSLG 264
Cdd:cd05930 90 --------------------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 --IKAKMDAaswTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACifVHLLPK---FDSQTVLKVLSSYPINTLVGAPI 339
Cdd:cd05930 120 nlLLWMQEA---YPLTPGDRVLQFTSFSFDVSVWEIFG-ALLAGAT--LVVLPEevrKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 340 IYRMLLQqDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLICRVSRTMKVKPGY----LGTAFA 414
Cdd:cd05930 194 LLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYRVPPDDEEDgrvpIGRPIP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 415 HYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGDFWLM---GDRGIKDPEGYFHFIGR 487
Cdd:cd05930 273 NTRVYVLDENLRPVPPGVPGELYIG-----GAGLARGYLNRPELTAerfvPNPFGPGERMyrtGDLVRWLPDGNLEFLGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 488 SDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdrDQLTKVLQEHVKSVTAPYKYP 567
Cdd:cd05930 348 IDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG-----ELDEEELRAHLAERLPDYMVP 422
|
490 500
....*....|....*....|..
gi 74183796 568 RKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd05930 423 SAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
97-600 |
4.62e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 186.26 E-value: 4.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 97 MNGSGKEikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQA 176
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 177 SKARAIV---AGDEVAQEVDAVAP-DCSFLkiklLVSENSREGWLNFKALLKEASTIHqcVETESRESAAIYfTSGTSGP 252
Cdd:PRK08276 82 SGAKVLIvsaALADTAAELAAELPaGVPLL----LVVAGPVPGFRSYEEALAAQPDTP--IADETAGADMLY-SSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 253 PKmaehshcslGIK----------------AKMDAASWTG-----LSTSDIIWTiSDTAWIMNILgaflepwVLGacIFV 311
Cdd:PRK08276 155 PK---------GIKrplpgldpdeapgmmlALLGFGMYGGpdsvyLSPAPLYHT-APLRFGMSAL-------ALG--GTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 312 HLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RML-LQQ------DLSSYKFphlhsCFSGGETLLPET----LENWkakt 379
Cdd:PRK08276 216 VVMEKFDAEEALALIERYRVTHSQLVPTMFvRMLkLPEevraryDVSSLRV-----AIHAAAPCPVEVkramIDWW---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 380 GLEIREIYGQTETGLICRV-SRTMKVKPGYLGTAfAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwPIGMFSgYVDNPKK 458
Cdd:PRK08276 287 GPIIHEYYASSEGGGVTVItSEDWLAHPGSVGKA-VLGEVRILDEDGNELPPGEIGTVYFEM----DGYPFE-YHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 459 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL 537
Cdd:PRK08276 361 TAAARNPHGWVtVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQP 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 538 APEFLshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 600
Cdd:PRK08276 441 ADGAD--AGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
103-591 |
2.17e-51 |
|
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: 184.04 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAgdevaqevdavapDCSFLKIKLLVSENSREGWlnfkallkeastihQCVETEsRESAAIYFTSGTSGPPKMAEHSHCS 262
Cdd:cd12118 106 FV-------------DREFEYEDLLAEGDPDFEW--------------IPPADE-WDPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 LGIKAKMDAASWTGLSTSDIIWTISD---TAWIMnilgaflePWVLGACIFVHL-LPKFDSQTVLKVLSSYPINTLVGAP 338
Cdd:cd12118 158 AYLNALANILEWEMKQHPVYLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 339 IIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTET---GLICRVSRT-----------MK 403
Cdd:cd12118 230 TVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVCAWKPEwdelpteerarLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 404 VKPG--YLGTAfahyDVQVIDEQGNVLPP--GKE-GDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGDFWLMGDRGIK 476
Cdd:cd12118 309 ARQGvrYVGLE----EVDVLDPETMKPVPrdGKTiGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 477 DPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLTKVLQEH 556
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-KVTEEEIIAFCREH 456
|
490 500 510
....*....|....*....|....*....|....*
gi 74183796 557 VksvtAPYKYPRKVEFVlDLPKTVTGKIERAKLRA 591
Cdd:cd12118 457 L----AGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
103-590 |
6.72e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 184.21 E-value: 6.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR-- 180
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRwv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 ----------------AIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQcVETESRESA--- 241
Cdd:PRK12583 122 icadafktsdyhamlqELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAWHELQARGETVSR-EALAERQASldr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 242 ----AIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASwTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIfvhLLPK- 316
Cdd:PRK12583 201 ddpiNIQYTSGTTGFPKGATLSHHNILNNGYFVAES-LGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACL---VYPNe 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 317 -FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTETG 393
Cdd:PRK12583 277 aFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 394 ---LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL- 469
Cdd:PRK12583 357 pvsLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV-----MKGYWNNPEATAESIDEDGWMh 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP-EFLSHDRdq 548
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPgHAASEEE-- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 74183796 549 ltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK12583 510 ----LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
78-592 |
2.29e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 182.67 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 78 HWAS--VEKAGKRSSGPALWWMngsGKEIKWsfRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTG 155
Cdd:PRK07786 18 NWVNqlARHALMQPDAPALRFL---GNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 156 LVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVET 235
Cdd:PRK07786 92 AIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 236 ESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLP 315
Cdd:PRK07786 172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTN-GADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 316 KFDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSykfphlhSCFSGGETLLPETLENWKAKT--GLEIREIY 387
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAVCaeqqarPRDLAL-------RVLSWGAAPASDTLLRQMAATfpEAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 388 GQTETGLI-CRVSRTMKV-KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRG 465
Cdd:PRK07786 324 GQTEMSPVtCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEATAEAFAG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 466 DFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD 545
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALT 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 74183796 546 RDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK07786 479 LEDLAEFLTDRL----ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
127-590 |
1.76e-49 |
|
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: 178.02 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 127 GLHRGDRVAVVLPRIPEW-WLM---ILGCMRTGLVFMPGTIQMRSSDILYrLQASKARAIVAGDE-VAQEVDAVAPDCSF 201
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELSfavAYAGGRLGLVFVPLNPTLKESVLRY-LVADAGGRIVLADAgAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 202 LKIKLLVsensrEGWLNFKALLkeastihQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMdAASWTGLSTSD 281
Cdd:cd05922 93 PGTVLDA-----DGIRAARASA-------PAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS-IAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 282 IIWTISDTAW---IMNILGAFLEpwvlGACIFVHLLPKFDsQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLH 358
Cdd:cd05922 160 RALTVLPLSYdygLSVLNTHLLR----GATLVLTNDGVLD-DAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 359 SCFSGGETLLPETLENWKAK-TGLEIREIYGQTETgliCRVSRTM-----KVKPGYLGTAFAHYDVQVIDEQGNVLPPGK 432
Cdd:cd05922 235 YLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEA---TRRMTYLpperiLEKPGSIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 433 EGDIAIRVkpiwPIGMfSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEH 511
Cdd:cd05922 312 PGEIVHRG----PNVM-KGYWNDPPYRRKEGRGGGVLhTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 512 PAVSETAVISSPDPSrGEVVKAFVVLAPEFLSHD-RDQLTKVLqehvksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05922 387 GLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDvLRSLAERL--------PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
98-590 |
4.81e-49 |
|
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: 178.21 E-value: 4.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 98 NGSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVL---PRIPEWWLMILGcmrTGLVFMPGTIQMRSSDILYRL 174
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 175 QASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSR------EGWLNFKALLKEASTIHQCVETESRESAAIYFTSG 248
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 249 TSGPPKMAEHSHCSLGIKA-KMDAASWTGLSTSDIIWTISD----TAWIMnilgAFLEPWVlGACifvHLLP--KFDSQT 321
Cdd:cd12119 174 TTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPmfhvNAWGL----PYAAAMV-GAK---LVLPgpYLDPAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRVSR 400
Cdd:cd12119 246 LAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAV-PRSLIEAFEERGVRVIHAWGMTETSPLGTVAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 401 TMKVKPGYLGTAFAHY-----------DVQVIDEQGNVLP-PGKE-GDIAIRvKPiWPIGmfsGYVDNPKKTQDNIRGDF 467
Cdd:cd12119 325 PPSEHSNLSEDEQLALrakqgrpvpgvELRIVDDDGRELPwDGKAvGELQVR-GP-WVTK---SYYKNDEESEALTEDGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 468 WLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRD 547
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG---ATVT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 74183796 548 QltKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd12119 477 A--EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
78-589 |
1.47e-48 |
|
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: 176.66 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 78 HWASVEKAGKRSSGPALwwMNGS-GKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGL 156
Cdd:cd05904 8 DSVSFLFASAHPSRPAL--IDAAtGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 157 VFMPGTIQMRSSDILYRLQASKARAIVAgdeVAQEVDAVAPdcsfLKIKLLVSENSREGWLNFKALLKEASTiHQCVETE 236
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFT---TAELAEKLAS----LALPVVLLDSAEFDSLSFSDLLFEADE-AEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 237 SRES--AAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDI----------IWTISdtaWIMNILGAflepwv 304
Cdd:cd05904 155 IKQDdvAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDvflcvlpmfhIYGLS---SFALGLLR------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 305 LGACIFVhlLPKFDSQTVLKVLSSYPINTL-VGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAK-TGLE 382
Cdd:cd05904 226 LGATVVV--MPRFDLEELLAAIERYKVTHLpVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 383 IREIYGQTETGLICRVSRT---MKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKK 458
Cdd:cd05904 304 LGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 459 TQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL 537
Cdd:cd05904 379 TAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVR 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 74183796 538 APE-FLSHDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd05904 459 KPGsSLTEDE------IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
73-591 |
7.68e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 175.96 E-value: 7.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 73 SDVIDHwaSVEKAGKRssgPALWWMngsGKEIkwSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCM 152
Cdd:PRK05605 35 VDLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 153 RTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSF-------------------LKIKLLVSENSR 213
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLetivsvnmiaampllqrlaLRLPIPALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 214 E-------GWLNFKALLKEA----STIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDi 282
Cdd:PRK05605 184 AaltgpapGTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGP- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 283 iwtisDT---------AWIMNILGAFlEPWVLGACIfvhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ------ 347
Cdd:PRK05605 263 -----ERvlaalpmfhAYGLTLCLTL-AVSIGGELV---LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 348 DLSSYKFphlhsCFSGGETLLPETLENWKAKTGLEIREIYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQ-- 424
Cdd:PRK05605 334 DLSGVRN-----AFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 425 GNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEV 504
Cdd:PRK05605 409 DETMPDGEEGELLVRGPQV-----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 505 ENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKI 584
Cdd:PRK05605 484 EEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEG----LRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
....*..
gi 74183796 585 ERAKLRA 591
Cdd:PRK05605 559 RRREVRE 565
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
101-598 |
7.65e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 173.03 E-value: 7.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:PRK05677 47 GKTL--TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNF-KALLKEASTIHQCVET 235
Cdd:PRK05677 125 ALVCLANMAHLAEKVLPKTgvkhvivtevadmlPPLKrllinavvkhVKKMVPAYHLPQAVKFnDALAKGAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 236 ESRESAAIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAASWTGLSTSDI------IWTISDTAWIMNILGAflepwv 304
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlQCRALMGSNLNEGCEILIAplplyhIYAFTFHCMAMMLIGN------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 305 lgacifvH--LLPK-FDSQTVLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 380
Cdd:PRK05677 279 -------HniLISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 381 LEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNPKKTQ 460
Cdd:PRK05677 352 CAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK----GPQVM-KGYWQRPEATD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 461 DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP 539
Cdd:PRK05677 427 EILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 540 eflshdRDQLTK-VLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 598
Cdd:PRK05677 507 ------GETLTKeQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
101-589 |
7.69e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 171.97 E-value: 7.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPdcsflkikllVSENSREGWLNFKALLKEASTIHQCVETESReSAAIYFTSGTSGPPKMAEHSH 260
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKIDNFVEKNESA-SFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 CSLGIKAKMDAASwTGLSTSDIIWTISDTAWIMNIlGAFLEP-WVLGACIFVHllPKFDSQTVLKVLSSYPINTLVGAPI 339
Cdd:PRK06839 172 ENMFWNALNNTFA-IDLTMHDRSIVLLPLFHIGGI-GLFAFPtLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 340 IYRMLLQQ-DLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETG--LICRVSRTMKVKPGYLGTAFAHY 416
Cdd:PRK06839 248 IHQALINCsKFETTNLQSVRWFYNGGAPC-PEELMREFIDRGFLFGQGFGMTETSptVFMLSEEDARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 417 DVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSG 496
Cdd:PRK06839 327 DYELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 497 YRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDL 576
Cdd:PRK06839 402 ENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD-----VIEHCRLFLAKYKIPKEIVFLKEL 476
|
490
....*....|...
gi 74183796 577 PKTVTGKIERAKL 589
Cdd:PRK06839 477 PKNATGKIQKAQL 489
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
242-586 |
1.11e-46 |
|
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: 167.06 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 242 AIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIM--NILGAFLEpwvLGACIFVhlLPKFDS 319
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNL-IAANLQLIHAMGLTEADVYLNMLPLFHIAglNLALATFH---AGGANVV--MEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 320 QTVLKVLSSYPInTLVG--APIIYRMLLQQDLSSYKFPHLhSCFSGGETllPETLENWKAKTGLEIREIYGQTET-GLIC 396
Cdd:cd17637 78 AEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSL-RHVLGLDA--PETIQRFEETTGATFWSLYGQTETsGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 397 rVSRTMKvKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIK 476
Cdd:cd17637 154 -LSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVFQGYWNLPELTAYTFRNGWHHTGDLGRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 477 DPEGYFHFIGRS--DDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlSHDRDQLTkvlq 554
Cdd:cd17637 227 DEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA-TLTADELI---- 301
|
330 340 350
....*....|....*....|....*....|..
gi 74183796 555 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
107-590 |
9.79e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 169.03 E-value: 9.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG- 185
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 --DEVAQEVDAVAPdcsflkikLLVSENSR-EGWLNFKALLKEASTihqcVETESRESAAIYFTSGTSGPPK-----MAE 257
Cdd:PRK13390 105 alDGLAAKVGADLP--------LRLSFGGEiDGFGSFEAALAGAGP----RLTEQPCGAVMLYSSGTTGFPKgiqpdLPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 258 HSHCSLGIKAKMDAASWTGLSTSDIIWTISDtawimnILGAFLEPWvlgaCIFVHLL-------PKFDSQTVLKVLSSYP 330
Cdd:PRK13390 173 RDVDAPGDPIVAIARAFYDISESDIYYSSAP------IYHAAPLRW----CSMVHALggtvvlaKRFDAQATLGHVERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 331 INTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETL---LPETLENWkakTGLEIREIYGQTET-GLICRVSRTMK 403
Cdd:PRK13390 243 ITVTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 404 VKPGYLGTAFAHyDVQVIDEQGNVLPPGKEGDIAIRvKPIWPigmFSgYVDNPKKTQD--NIRGDFWL-MGDRGIKDPEG 480
Cdd:PRK13390 320 AHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFE-RDRLP---FR-YLNDPEKTAAaqHPAHPFWTtVGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 481 YFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlsHDRDQLTKVLQEHVKSV 560
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI--RGSDELARELIDYTRSR 471
|
490 500 510
....*....|....*....|....*....|
gi 74183796 561 TAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
107-591 |
4.02e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 169.55 E-value: 4.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV-------FmpgtiqmrSSDILY-RLQASK 178
Cdd:PRK00174 100 TYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggF--------SAEALAdRIIDAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 179 ARAIVAGDE-------VA--QEVDAVAPDCSFLKiKLLV---------SENSREGWLNfkALLKEASTIHQCVETESRES 240
Cdd:PRK00174 171 AKLVITADEgvrggkpIPlkANVDEALANCPSVE-KVIVvrrtggdvdWVEGRDLWWH--ELVAGASDECEPEPMDAEDP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHS------HCSLGIKAKMDaaswtgLSTSDIIWTISDTAWIMN----ILGaflePWVLGACIF 310
Cdd:PRK00174 248 LFILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD------YKDGDVYWCTADVGWVTGhsyiVYG----PLANGATTL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 311 VHL-LPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQ--------DLSSYKFphLHSCfsgGETLLPETLEnWKAKT- 379
Cdd:PRK00174 318 MFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKEgdehpkkyDLSSLRL--LGSV---GEPINPEAWE-WYYKVv 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 380 GLE---IREIYGQTETG--LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPiWPiGMFSGYVD 454
Cdd:PRK00174 392 GGErcpIVDTWWQTETGgiMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIK-DP-WP-GMMRTIYG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 455 NPKKTQDNIRGDF---WLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVV 531
Cdd:PRK00174 469 DHERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGI 548
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74183796 532 KAFVVL----APEflshdrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK00174 549 YAFVTLkggeEPS------DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
105-593 |
8.86e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 165.91 E-value: 8.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTG--LVFmpgtIQMRSS--DILYRLQASKAR 180
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGavAVL----LNTRLSreELLWQLDDAEVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVdavapdcsFLKIKLLVSEnsregwlnfkaLLKEASTIHQCVETESRESAA-IYFTSGTSGPPK----- 254
Cdd:PRK03640 102 CLITDDDFEAKL--------IPGISVKFAE-----------LMNGPKEEAEIQEEFDLDEVAtIMYTSGTTGKPKgviqt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 ------MAEHSHCSLGIKAKmDaaSW---------TGLSTsdiiwtisdtawIMN--ILGaflepwvlgacIFVHLLPKF 317
Cdd:PRK03640 163 ygnhwwSAVGSALNLGLTED-D--CWlaavpifhiSGLSI------------LMRsvIYG-----------MRVVLVEKF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 318 DSQTVLKVLSSYPINTLVGAPIiyrmLLQQDLSSYKFPHLHSCF-----SGGETLLPeTLENWKAKtGLEIREIYGQTET 392
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVST----MLQRLLERLGEGTYPSSFrcmllGGGPAPKP-LLEQCKEK-GIPVYQSYGMTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 GlicrvSRTMKVKPGY----LGTA-FAHYDVQV-IDEQGNVLPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRgD 466
Cdd:PRK03640 291 A-----SQIVTLSPEDaltkLGSAgKPLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNREDATRETFQ-D 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 467 FWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshD 545
Cdd:PRK03640 360 GWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV---T 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 74183796 546 RDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK03640 437 EEELRHFCEEKL----AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
243-590 |
1.81e-44 |
|
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: 161.68 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 IYFTSGTSGPPKMAEHSHCSLgikakMDAASWTGLStsdIIWTISDTAWIMN--------ILGAFLEPWVLGACIFVHll 314
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI-----VNNGYFIGER---LGLTEQDRLCIPVplfhcfgsVLGVLACLTHGATMVFPS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 PKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL-EIREIYGQTET 392
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 GLICRVSRT---MKVKPGYLGTAFAHYDVQVIDEQGNVLPP-GKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFW 468
Cdd:cd05917 157 SPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 469 L-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRD 547
Cdd:cd05917 232 LhTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 74183796 548 qltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05917 312 -----IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
104-599 |
1.96e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 164.98 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 104 IKWSFRELSEASKQTANVLSGAcGLHRGDRVAVvLPRIPEWWLMI-LGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAqevdAVAPDCsflkikllvsensregwLNFKALLKEAstihQCVETESRESAA------IYFTSGTSGPPKMA 256
Cdd:PRK09088 99 LGDDAVA----AGRTDV-----------------EDLAAFIASA----DALEPADTPSIPpervslILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 -------EHSHCSLGIKAKMDAASwtglstsdiiwTISDTAWIMNILGAF--LEPWVL-GACIFVHllPKFDSQTVLKVL 326
Cdd:PRK09088 154 mlsernlQQTAHNFGVLGRVDAHS-----------SFLCDAPMFHIIGLItsVRPVLAvGGSILVS--NGFEPKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 327 S--SYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETGLICRVSRTMK 403
Cdd:PRK09088 221 GdpALGITHYFCVPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 404 V---KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 479
Cdd:PRK09088 300 ViraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNL-----SPGYWRRPQATARAFTGDGWFrTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 480 GYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLTKVLQEHVKS 559
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-----APLDLERIRSHLST 449
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 74183796 560 VTAPYKYPRKVEFVLDLPKTVTGKIERAKLRakEWKTSGR 599
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARLR--DALAAGR 487
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
107-593 |
5.25e-44 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 165.23 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNFKALLKEASTIhQCV--ETESRES 240
Cdd:PRK08974 130 NFAHTLEKVVFKTpvkhviltrmgdqlSTAKgtlvnfvvkyIKRLVPKYHLPDAISFRSALHKGRRM-QYVkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSlgIKAKMDAASW--------------TGLSTSDIIwtisdtAWIMNILgAFLEpwvLG 306
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN--MLANLEQAKAaygpllhpgkelvvTALPLYHIF------ALTVNCL-LFIE---LG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 307 ACIFVHLLPKfDSQTVLKVLSSYPINTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 385
Cdd:PRK08974 277 GQNLLITNPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGMfSGYVDNPKKTQDNIR 464
Cdd:PRK08974 356 GYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK----GPQVM-LGYWQRPEATDEVIK 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 465 gDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLS 543
Cdd:PRK08974 431 -DGWLaTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLT 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 74183796 544 hdRDQLTKVLQEHVKSvtapYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK08974 510 --EEELITHCRRHLTG----YKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
107-593 |
5.77e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 164.72 E-value: 5.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLsGACGLHRGDRVAVvLPRIPEWWLMILGC----------MRTGlvFMPGTIQmrssDILYRLqa 176
Cdd:PRK07788 76 TYAELDEQSNALARGL-LALGVRAGDGVAV-LARNHRGFVLALYAagkvgariilLNTG--FSGPQLA----EVAARE-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 177 sKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSEN---SREGWLNFKALLKEASTihQCVETESRESAAIYFTSGTSGPP 253
Cdd:PRK07788 146 -GVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSST--APLPKPPKPGGIVILTSGTTGTP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 254 KMAEHSHCSLgikakmdAASWTGLsTSDIIW----TISDTAWIMNILG--AFLEPWVLGACIFVHllPKFDSQTVLKVLS 327
Cdd:PRK07788 223 KGAPRPEPSP-------LAPLAGL-LSRVPFrageTTLLPAPMFHATGwaHLTLAMALGSTVVLR--RRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPI-IYRML--LQQ-----DLSSYKFphlhsCFSGGETLLPETLENWKAKTGLEIREIYGQTETGlICRVS 399
Cdd:PRK07788 293 KHKATALVVVPVmLSRILdlGPEvlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVA-FATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 400 R--TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkpiwpiGM-FSGYVDNPKKtqDNIRGdfwLM--GDRG 474
Cdd:PRK07788 367 TpeDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 475 IKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflsHDRDQltKVLQ 554
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG---AALDE--DAIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 74183796 555 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
101-590 |
1.04e-43 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 164.42 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:PRK07059 46 GKAI--TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPDCS---------------------FL--KIKLLVSENSREGWLNFKALLKE-ASTIHQCVETE 236
Cdd:PRK07059 123 AIVVLENFATTVQQVLAKTAvkhvvvasmgdllgfkghivnFVvrRVKKMVPAWSLPGHVRFNDALAEgARQTFKPVKLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 237 SRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGlstsdiiwtisdtawimnilGAFLEPWVLGACIFVHLLPK 316
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNI-VANVLQMEAWLQ--------------------PAFEKKPRPDQLNFVCALPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 317 F--------------------------DSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLP 369
Cdd:PRK07059 262 YhifaltvcgllgmrtggrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 370 ETLENWKAKTGLEIREIYGQTETGLICRVSR-TMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiWPIGM 448
Cdd:PRK07059 342 PVAERWLEMTGCPITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR----GPQVM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 449 fSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSR 527
Cdd:PRK07059 418 -AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 528 GEVVKAFVV------LAPEFLSHDRDQLTKvlqehvksvtapYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK07059 497 GEAVKLFVVkkdpalTEEDVKAFCKERLTN------------YKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
101-590 |
3.14e-43 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 163.12 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIkwSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:PRK08751 48 GKTI--TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPDC--------------SFLK----------IKLLVSENSREGWLNFKALLKEASTiHQC--VE 234
Cdd:PRK08751 126 VLVVIDNFGTTVQQVIADTpvkqvittglgdmlGFPKaalvnfvvkyVKKLVPEYRINGAIRFREALALGRK-HSMptLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 235 TESRESAAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTS-----DIIWTISDTAWIMNILGAFLEPWVLGACi 309
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNL-VANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKIGGC- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 310 fVHLL--PKfDSQTVLKVLSSYPINTLVGAPIIYRMLL------QQDLSSYKFphlhsCFSGGETLLPETLENWKAKTGL 381
Cdd:PRK08751 283 -NHLIsnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKM-----TLGGGMAVQRSVAERWKQVTGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 382 EIREIYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQ 460
Cdd:PRK08751 356 TLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV-----MKGYWKRPEETA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 461 DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP 539
Cdd:PRK08751 431 KVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 74183796 540 EFLSHDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK08751 511 PALTAED------VKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
107-519 |
6.11e-43 |
|
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: 158.97 E-value: 6.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIqmrssDILY---RLQA----SKA 179
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP--L-----DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSregwlnfkallkEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHS 259
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDD------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 260 HCSLgikakMDAASWTG---LSTSDIIW----TIS-DTAwIMNILGaflePWVLGACIFVhlLPKFDSQTVLK----VLS 327
Cdd:TIGR01733 142 HRSL-----VNLLAWLArryGLDPDDRVlqfaSLSfDAS-VEEIFG----ALLAGATLVV--PPEDEERDDAAllaaLIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKTG-LEIREIYGQTETGLICRVSRTMKVKP 406
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 GY-----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDN-IRGDFWLM--------GD 472
Cdd:TIGR01733 288 PRespvpIGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGD 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 74183796 473 RGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAV 519
Cdd:TIGR01733 363 LVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
105-591 |
6.65e-43 |
|
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: 159.05 E-value: 6.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKaraiVA 184
Cdd:cd05912 1 SYTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD----VK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GDEVAqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesresaAIYFTSGTSGPPKmaehshcslG 264
Cdd:cd05912 76 LDDIA----------------------------------------------------TIMYTSGTTGKPK---------G 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKAKMDAASWTGLSTSDIIWTISDTAW-----IMNI--LGAFLEPWVLGacIFVHLLPKFDSQTVLKVLSSYPINTLVGA 337
Cdd:cd05912 95 VQQTFGNHWWSAIGSALNLGLTEDDNWlcalpLFHIsgLSILMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 338 PIIYRMLLQQDLSSYKfPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETgliCRVSRTMK-----VKPGYLGTA 412
Cdd:cd05912 173 PTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTET---CSQIVTLSpedalNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 413 FAHYDVQVIDEQGnvlPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDII 492
Cdd:cd05912 248 LFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 493 NSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshDRDQLTKVLQEHVksvtAPYKYPRKVEF 572
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVPKKIYF 392
|
490
....*....|....*....
gi 74183796 573 VLDLPKTVTGKIERAKLRA 591
Cdd:cd05912 393 VDELPRTASGKLLRHELKQ 411
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
99-590 |
2.90e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 159.83 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 99 GSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASK 178
Cdd:PRK13295 49 GTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 179 ARAIVA-----GDEVAQEVDAVAPDCSFLKIKLLVSEnsrEGWLNFKALL----KEASTIHQCVETESR----ESAAIYF 245
Cdd:PRK13295 128 SKVLVVpktfrGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLitpaWEQEPDAPAILARLRpgpdDVTQLIY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 246 TSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACifVHLLPKFDSQTVLKV 325
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTL-MANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGAT--AVLQDIWDPARAAEL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 326 LSSYPIN-TLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL--ICRVSRTM 402
Cdd:PRK13295 282 IRTEGVTfTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 403 KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGdfWL-MGDRGIKDPEGY 481
Cdd:PRK13295 362 ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADG--WFdTGDLARIDADGY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 482 FHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQEHvkSVT 561
Cdd:PRK13295 435 IRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KVA 511
|
490 500
....*....|....*....|....*....
gi 74183796 562 APYkYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK13295 512 KQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
92-589 |
4.13e-42 |
|
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: 157.79 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 92 PALWWMNGsgkeiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdil 171
Cdd:cd05945 8 PAVVEGGR-----TLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 172 yrlqaskARAIVAGDEVAQEVDAVAPDcsflkikLLVSENSregwlnfkallkeastihqcvetesrESAAIYFTSGTSG 251
Cdd:cd05945 71 -------LDASSPAERIREILDAAKPA-------LLIADGD--------------------------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 252 PPKMAEHSHCSLgikakmdaASWTGlstsdiiWTISDTAW-----------------IMNILGAflepWVLGACIFVhlL 314
Cdd:cd05945 111 RPKGVQISHDNL--------VSFTN-------WMLSDFPLgpgdvflnqapfsfdlsVMDLYPA----LASGATLVP--V 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 PKfDSQTVLKVLSSY----PINTLVGAPIIYRMLLQ-QDLSSYKFPHL-HSCFSGgETLLPETLENWKAKT-GLEIREIY 387
Cdd:cd05945 170 PR-DATADPKQLFRFlaehGITVWVSTPSFAAMCLLsPTFTPESLPSLrHFLFCG-EVLPHKTARALQQRFpDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 388 GQTETGLIC---RVSRTM--KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQ 460
Cdd:cd05945 248 GPTEATVAVtyiEVTPEVldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPEKTA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 461 ---DNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVV 536
Cdd:cd05945 321 aafFPDEGQRAYrTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 74183796 537 LAPeflsHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd05945 401 PKP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
106-591 |
5.10e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 157.84 E-value: 5.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSGAcglhrgDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIQMRSSDilyrlqasKARAIVAG 185
Cdd:PRK07787 26 LSRSDLAGAATAVAERVAGA------RRVAVLATPTLATVLAVVGALIAGVPVVP--VPPDSGV--------AERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEVAQEVDAVAPDCSFLKIKLLVSENSReGWlnfkallkeastiHQCVETESRESAAIYFTSGTSGPPKMAEHSHcsLGI 265
Cdd:PRK07787 90 DSGAQAWLGPAPDDPAGLPHVPVRLHAR-SW-------------HRYPEPDPDAPALIVYTSGTTGPPKGVVLSR--RAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 266 KAKMD--AASWTglstsdiiWTISDT-----------AWIMNILGaflePWVLGACiFVHLLpKFDSQTVLKVLSSYpiN 332
Cdd:PRK07787 154 AADLDalAEAWQ--------WTADDVlvhglplfhvhGLVLGVLG----PLRIGNR-FVHTG-RPTPEAYAQALSEG--G 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLV-GAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGT 411
Cdd:PRK07787 218 TLYfGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 412 AFAHYDVQVIDEQGNVLPPGKE--GDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGR- 487
Cdd:PRK07787 298 PLAGVETRLVDEDGGPVPHDGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGRe 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 488 SDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLApeflshdRDQLTKVLQEHVKSVTAPYKYP 567
Cdd:PRK07787 373 STDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGA-------DDVAADELIDFVAQQLSVHKRP 445
|
490 500
....*....|....*....|....
gi 74183796 568 RKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK07787 446 REVRFVDALPRNAMGKVLKKQLLS 469
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
103-590 |
8.14e-42 |
|
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: 158.46 E-value: 8.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAQEVDAVAPDCSFLK-IKLLVSENSREGWLNFKALLKEASTIHQCVETESRES-------AAIYFTSGTSGPPK 254
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKtIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSfdrdeqvALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 MAEHSHcsLGIKAKMDAASwtglsTSDIIWTISDTAWIMNILgaflePWVLGACIF-----------VHLLPKFDSQTVL 323
Cdd:cd17642 201 GVQLTH--KNIVARFSHAR-----DPIFGNQIIPDTAILTVI-----PFHHGFGMFttlgylicgfrVVLMYKFEEELFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 324 KVLSSYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREIYGQTETGLICRVSRT 401
Cdd:cd17642 269 RSLQDYKVQSALLVPTLFAFFAKSTLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 402 MKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 479
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDED 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 480 GYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlapefLSHDRDQLTKVLQEHVKS 559
Cdd:cd17642 424 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV-----LEAGKTMTEKEVMDYVAS 498
|
490 500 510
....*....|....*....|....*....|..
gi 74183796 560 VTAPYKYPR-KVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd17642 499 QVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
105-589 |
1.60e-41 |
|
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: 156.72 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV---FMPGtiqMRSSDILYRLQASKARA 181
Cdd:cd05920 40 RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS---HRRSELSAFCAHAEAVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 IVAGDEvAQEVDavapdcsflkikllvsensregwlnFKALLKEastihqcVETESRESAAIYFTSGTSGPPKMAEHSHC 261
Cdd:cd05920 116 YIVPDR-HAGFD-------------------------HRALARE-------LAESIPEVALFLLSGGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 262 SLGIKAKMdAASWTGLStsdiiwtiSDTAWIMNILGA----FLEPWVLGACIF---VHLLPKFDSQTVLKVLSSYPIN-- 332
Cdd:cd05920 163 DYAYNVRA-SAEVCGLD--------QDTVYLAVLPAAhnfpLACPGVLGTLLAggrVVLAPDPSPDAAFPLIEREGVTvt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVgaPIIYRMLLQQ------DLSSYKFPHLhscfsGGETLLPETLENWKAKTGLEIREIYGQTEtGLIC--RVSRTMKV 404
Cdd:cd05920 234 ALV--PALVSLWLDAaasrraDLSSLRLLQV-----GGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNytRLDDPDEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 405 KPGYLGTAFAHYD-VQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEG 480
Cdd:cd05920 306 IIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 481 YFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdrdqlTKVLQEHVKSV 560
Cdd:cd05920 379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS------AAQLRRFLRER 452
|
490 500 510
....*....|....*....|....*....|
gi 74183796 561 -TAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd05920 453 gLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
87-591 |
2.58e-41 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 158.57 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 87 KRSSGPALWWMNG-SGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTG----LVFmpG 161
Cdd:PRK10524 65 KRPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihsVVF--G 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 162 TIqmrssdilyrlqaskaraivAGDEVAQEVDAVAPdcsflkiKLLVSEN--SREG-WLNFKALLKEA------------ 226
Cdd:PRK10524 142 GF--------------------ASHSLAARIDDAKP-------VLIVSADagSRGGkVVPYKPLLDEAialaqhkprhvl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 227 -------------------STIHQ--------CVETESRESAAIYFTSGTSGPPKmaehshcslGIKakMDAASWT-GLS 278
Cdd:PRK10524 195 lvdrglapmarvagrdvdyATLRAqhlgarvpVEWLESNEPSYILYTSGTTGKPK---------GVQ--RDTGGYAvALA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 279 TS----------DIIWTISDTAWIM----NILGaflePWVLG-ACIFVHLLP-KFDSQTVLKVLSSYPINTLVGAPIIYR 342
Cdd:PRK10524 264 TSmdtifggkagETFFCASDIGWVVghsyIVYA----PLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 343 MLLQQD---LSSYKFPHLHSCFSGGETLlPETLENWKAKT-GLEIREIYGQTETGL----ICRVSRTMKVKPGYLGTAFA 414
Cdd:PRK10524 340 VLKKQDpalLRKHDLSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGWpilaIARGVEDRPTRLGSPGVPMY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 415 HYDVQVIDEQ-GNVLPPGKEGDIAIRvKPIWPIGMFSGYVDNPKKTQDnirgdFW-LMG-------DRGIKDPEGYFHFI 485
Cdd:PRK10524 419 GYNVKLLNEVtGEPCGPNEKGVLVIE-GPLPPGCMQTVWGDDDRFVKT-----YWsLFGrqvystfDWGIRDADGYYFIL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 486 GRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQ---LTKVLQEHVKSVTA 562
Cdd:PRK10524 493 GRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLG 572
|
570 580
....*....|....*....|....*....
gi 74183796 563 PYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK10524 573 AVARPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
104-590 |
4.71e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 156.89 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 104 IKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMpgTIQ--MRSSDILYRLQASKARA 181
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 IVAGDEV-----AQEVDAVAPDCS-------------FLKIKLLVSENSREGWLNFKALLKEASTIHQcVETESRESAA- 242
Cdd:PRK08315 119 LIAADGFkdsdyVAMLYELAPELAtcepgqlqsarlpELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 ------IYFTSGTSGPPKMAEHSHCSLGikakmDAASWTGLStsdIIWTISDTAWI---------MnILGaflepwVL-- 305
Cdd:PRK08315 198 pddpinIQYTSGTTGFPKGATLTHRNIL-----NNGYFIGEA---MKLTEEDRLCIpvplyhcfgM-VLG------NLac 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 ---GACIfVHLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGL 381
Cdd:PRK08315 263 vthGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 382 eiREI---YGQTETG---LICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwpiG---MfSG 451
Cdd:PRK08315 342 --SEVtiaYGMTETSpvsTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTR-------GysvM-KG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 452 YVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEV 530
Cdd:PRK08315 412 YWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74183796 531 VKAFVVLAPEFlshdrdQLTKV-LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK08315 492 VCAWIILRPGA------TLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
107-590 |
7.42e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 156.14 E-value: 7.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDAVAPDCS---FLKIKLLVSENSREGWL---------------------NFKALLKE-ASTIHQCVETESRESA 241
Cdd:PRK12492 131 MFGKLVQEVLPDTGieyLIEAKMGDLLPAAKGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 242 AIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAASWTGLSTsdiiwtISDTAWIMNILGAFLEPWVLGA---CIFV-- 311
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLvanmlQVRACLSQLGPDGQPL------MKEGQEVMIAPLPLYHIYAFTAncmCMMVsg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 312 --HLL---PKfDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIRE 385
Cdd:PRK12492 285 nhNVLitnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETG-LICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIR 464
Cdd:PRK12492 364 GYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQV-----MKGYWQQPEATAEALD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 465 GDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLS 543
Cdd:PRK12492 439 AEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLS 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 74183796 544 HDRdqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK12492 519 VEE------LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
239-586 |
7.75e-41 |
|
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: 151.11 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 239 ESAAIYFTSGTSGPPK--MAEHSHcSLGIkakmdAASWtglstSDIIWTISDTAWImnILGAFLEPWVLGACIFVHLL-- 314
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQ-TLRA-----AAAW-----ADCADLTEDDRYL--IINPFFHTFGYKAGIVACLLtg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 ----PK--FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREI 386
Cdd:cd17638 68 atvvPVavFDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 387 YGQTETGL--ICRVSRTMKVKPGYLGTAFAHYDVQVIDeQGNVLPPGKEgdiairvkpiwpigMFSGYVDNPKKTQDNIR 464
Cdd:cd17638 148 YGLTEAGVatMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRGYN--------------VMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 465 GDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLS 543
Cdd:cd17638 213 ADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VT 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 74183796 544 HDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:cd17638 292 LTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
73-592 |
1.50e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.27 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 73 SDVIDHWASvekagKRSSGPALWWmngSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCM 152
Cdd:PRK06145 5 SASIAFHAR-----RTPDRAALVY---RDQEI--SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 153 RTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPdcsflkiKLLVSENSREGWLNFKALLKEASTIHQC 232
Cdd:PRK06145 74 YLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETP-------KIVIDAAAQADSRRLAQGGLEIPPQAAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 233 VETESREsaaIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSDIIWTISDtawiMNILGAFLEP-----WVLGa 307
Cdd:PRK06145 147 APTDLVR---LMYTSGTTDRPKGVMHSYGNLHWKS-IDHVIALGLTASERLLVVGP----LYHVGAFDLPgiavlWVGG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 308 ciFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIY-RMLLQQDLSSYKFPHLHSCFSGGETLlPETL--ENWKAKTGLEIR 384
Cdd:PRK06145 218 --TLRIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKT-PESRirDFTRVFTRARYI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 385 EIYGQTETgliCRVSRTMKV-----KPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKT 459
Cdd:PRK06145 295 DAYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKV-----TKGYWKDPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 460 QDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP 539
Cdd:PRK06145 367 AEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 74183796 540 EflshdrDQLT-KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK06145 447 G------ATLTlEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
100-592 |
3.66e-40 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 153.98 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 100 SGKEIKWSfrELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKA 179
Cdd:PLN02330 52 TGKAVTYG--EVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQEVDAvapdcsfLKIKLLV-SENSREGWLNFKALLKEAStihQCVETESRES------AAIYFTSGTSGP 252
Cdd:PLN02330 129 KLIVTNDTNYGKVKG-------LGLPVIVlGEEKIEGAVNWKELLEAAD---RAGDTSDNEEilqtdlCALPFSSGTTGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 253 PKMAEHSHCSLgiKAKMdAASWTGLStSDIIWTISDTAWI--MNILGaflepwVLGACIF-------VHLLPKFDSQTVL 323
Cdd:PLN02330 199 SKGVMLTHRNL--VANL-CSSLFSVG-PEMIGQVVTLGLIpfFHIYG------ITGICCAtlrnkgkVVVMSRFELRTFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 324 KVLSSYPIN----------TLVGAPIIYRMllqqDLSSYKfphLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTET 392
Cdd:PLN02330 269 NALITQEVSfapivppiilNLVKNPIVEEF----DLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 GLICRVSRTMK-----VKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGD 466
Cdd:PLN02330 342 SCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCV-----MQGYYNNKEETDRTIDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 467 FWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD 545
Cdd:PLN02330 417 GWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 74183796 546 RDQLtkvlqEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PLN02330 497 EDIL-----NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
85-595 |
3.86e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 153.31 E-value: 3.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 85 AGKRSSGPALWwMNGSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVL---PRIPE--WwlmilGCMRTGLVFM 159
Cdd:PRK13391 7 AQTTPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLEvcW-----AAERSGLYYT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 160 PGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLV-SENSREGWLNFkallkeASTIHQCVET--- 235
Cdd:PRK13391 78 CVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGY------AEAVAGLPATpia 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 236 ESRESAAIYFTSGTSGPPKmaehshcslGIKAKmdaaswtgLSTSDIIWTISDTAWIMNILG-----AFLEP-------- 302
Cdd:PRK13391 152 DESLGTDMLYSSGTTGRPK---------GIKRP--------LPEQPPDTPLPLTAFLQRLWGfrsdmVYLSPaplyhsap 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 303 --WV-----LGACIFVhlLPKFDSQTVLKVLSSYPINTLVGAPIIY-RML-------LQQDLSSykfphLHSCFSGGETL 367
Cdd:PRK13391 215 qrAVmlvirLGGTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPC 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 368 LPETLENWKAKTGLEIREIYGQTETGLICRV-SRTMKVKPGYLGTAFAHyDVQVIDEQGNVLPPGKEGDIairvkpiWPI 446
Cdd:PRK13391 288 PPQVKEQMIDWWGPIIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTI-------WFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 447 G--MFSgYVDNPKKTQD--NIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISS 522
Cdd:PRK13391 360 GgrPFE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 523 PDPSRGEVVKAFVVLAPefLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWK 595
Cdd:PRK13391 439 PNEDLGEEVKAVVQPVD--GVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
91-592 |
5.41e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 153.27 E-value: 5.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 91 GPALWWmngsgKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDI 170
Cdd:PRK07470 23 RIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 171 LYRLQASKARAIVAGDEVAQEVDAVAPDCsfLKIKLLVSENSREGWLNFKALLKE-ASTIHQCVETESRESAAIYFTSGT 249
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHAAAVRAAS--PDLTHVVAIGGARAGLDYEALVARhLGARVANAAVDHDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 250 SGPPKMAEHSHCSLG-IKAKMDAASWTGLSTSD---IIWTISDTAWIMNILGAflepwVLGACIFVHLLPKFDSQTVLKV 325
Cdd:PRK07470 175 TGRPKAAVLTHGQMAfVITNHLADLMPGTTEQDaslVVAPLSHGAGIHQLCQV-----ARGAATVLLPSERFDPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 326 LSSYPINTLVGAPIIYRMLL------QQDLSSYKfphlHSCFSGGetllPETLENWK---AKTGLEIREIYGQTE-TGLI 395
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVehpavdRYDHSSLR----YVIYAGA----PMYRADQKralAKLGKVLVQYFGLGEvTGNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 396 CRVSRTM-------KVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFW 468
Cdd:PRK07470 322 TVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEANAKAFRDGWF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 469 LMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAfVVLAPEFLSHDRDQ 548
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA-VCVARDGAPVDEAE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 74183796 549 ltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK07470 476 ----LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
238-592 |
4.62e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.68 E-value: 4.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 238 RESAAIYFTSGTSGPPKMAEHSHC--SLGIKAKMDAASWTGLSTSDII------WTISDTAwimniLGAFLepwvlgACI 309
Cdd:PRK13382 196 RKGRVILLTSGTTGTPKGARRSGPggIGTLKAILDRTPWRAEEPTVIVapmfhaWGFSQLV-----LAASL------ACT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 310 FVhLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ---QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREI 386
Cdd:PRK13382 265 IV-TRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 387 YGQTETGLICRVS-RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKPiwpigMFSGYVdnPKKTQDNIRG 465
Cdd:PRK13382 344 YNATEAGMIATATpADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT-----QFDGYT--SGSTKDFHDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 466 dFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflshD 545
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----G 490
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74183796 546 RDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK13382 491 ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
62-594 |
5.20e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 150.66 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 62 HQEAPAKFNFASdVIDhwasvEKAGKRSSGPALwwmngSGKEIKWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRI 141
Cdd:PRK06164 3 HDAAPRADTLAS-LLD-----AHARARPDAVAL-----IDEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 142 PEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG------------DEVAQEVDAVAPdcsflKIKLLVS 209
Cdd:PRK06164 71 IEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWpgfkgidfaailAAVPPDALPPLR-----AIAVVDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 210 ENS------REGWLNFKALLKEASTIHQCVETESRESAAIYFT-SGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDI 282
Cdd:PRK06164 146 AADatpapaPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAY-GYDPGAV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 283 IWTISDtawimnILGAFLEPWVLGAC---IFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHS 359
Cdd:PRK06164 225 LLAALP------FCGVFGFSTLLGALaggAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 360 C----FSGGETLLPEtlenWKAKTGLEIREIYGQTEtgLICRVS---RTMKVKPGYLG---TAFAHYDVQVIDEQ-GNVL 428
Cdd:PRK06164 299 FgfasFAPALGELAA----LARARGVPLTGLYGSSE--VQALVAlqpATDPVSVRIEGggrPASPEARVRARDPQdGALL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 429 PPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENA 507
Cdd:PRK06164 373 PDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 508 LMEHPAVSETAVISSPDPSRGEVVkAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTG---KI 584
Cdd:PRK06164 448 LEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAG-----LMAACREALAGFKVPARVQVVEAFPVTESAngaKI 521
|
570
....*....|..
gi 74183796 585 ERAKLR--AKEW 594
Cdd:PRK06164 522 QKHRLRemAQAR 533
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
85-592 |
1.83e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 147.17 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 85 AGKRSSGPALWWMNGsGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP--GT 162
Cdd:COG1022 21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPiyPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 163 IqmRSSDILYRLQASKARAIVAGD-EVAQEVDAVAPDCSFLKiKLLV----SENSREGWLNFKALLKEASTIHQCVETES 237
Cdd:COG1022 99 S--SAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLALGREVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 238 RES-------AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIiwTIS--DTAWIM-NILGAFLepWVLGA 307
Cdd:COG1022 176 RRAavkpddlATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDR--TLSflPLAHVFeRTVSYYA--LAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 308 CI-FVHllpkfDSQTVLKVLSSYPINTLVGAP--------------------------------IIYRMLLQQDLS---S 351
Cdd:COG1022 251 TVaFAE-----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalavgRRYARARLAGKSpslL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 352 YKFPH------------------LHSCFSGGETLLPETLENWKAkTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAF 413
Cdd:COG1022 326 LRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 414 AhyDVQV-IDEQGNVLppgkegdiairVK-PiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDD 490
Cdd:COG1022 405 P--GVEVkIAEDGEIL-----------VRgP----NVMKGYYKNPEATAEAFDADGWLHtGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 491 II-NSSGYRIGPSEVENALMEHPAVSETAVIsspdpsrGE---VVKAFVVLAPEFLSH----------------DRDQLT 550
Cdd:COG1022 468 LIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVPDFEALGEwaeenglpytsyaelaQDPEVR 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 74183796 551 KVLQEHVKSVTApyKYPRkVE----FVLdLPK---------TVTGKIERAKLRAK 592
Cdd:COG1022 541 ALIQEEVDRANA--GLSR-AEqikrFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
83-592 |
1.87e-37 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 146.28 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 83 EKAGKRSSGPALwwMNGSGKEIkWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGT 162
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 163 IQMRSSDILYRLQASKARAIVAgdeVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAA 242
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 IYFTSGTSGPPKMAEHSHCSL--GIKAKMDAASwtglstSDIIWTISDTawIMNILGAF----LEPWVL-----GACIFV 311
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHKGLvtSVAQQVDGEN------PNLYFHSDDV--ILCVLPMFhiysLNSVLLcglrvGAAILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 312 hlLPKFDSQTVLKVLSSYPINTlvgAPIIYRMLL---------QQDLSSYKFphlhsCFSGGETLLPETLENWKAK-TGL 381
Cdd:PLN02246 256 --MPKFEIGALLELIQRHKVTI---APFVPPIVLaiakspvveKYDLSSIRM-----VLSGAAPLGKELEDAFRAKlPNA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 382 EIREIYGQTETGLICRVS-----RTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRVKPIwpigmFSGYVDN 455
Cdd:PLN02246 326 VLGQGYGMTEAGPVLAMClafakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 456 PKKTQDNIRGDFWL-MGDRG-IKDPEGYFhFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKA 533
Cdd:PLN02246 401 PEATANTIDKDGWLhTGDIGyIDDDDELF-IVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVA 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 534 FVVLAPEFlshdrdqltKVLQEHVKSVTAP----YKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PLN02246 480 FVVRSNGS---------EITEDEIKQFVAKqvvfYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
241-591 |
1.87e-37 |
|
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: 142.62 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHcslgikakmdaaswtglstSDIIWTisdtAWIMNILGAFLEPWVL---------GACIFV 311
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTH-------------------SNEVYN----AWMLALNSLFDPDDVLlcglplfhvNGSVVT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 312 HLLPKFDSQTVL-----------------KVLSSYPINTLVGAPIIYRMLLQ----QDLSSYKFphlhsCFSGGETLLPE 370
Cdd:cd05944 62 LLTPLASGAHVVlagpagyrnpglfdnfwKLVERYRITSLSTVPTVYAALLQvpvnADISSLRF-----AMSGAAPLPVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 371 TLENWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYDVQ--VIDEQGNVL---PPGKEGDIAIRVKpiw 444
Cdd:cd05944 137 LRARFEDATGLPVVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRikVLDGVGRLLrdcAPDEVGEICVAGP--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 445 piGMFSGYVDNPKKtQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSP 523
Cdd:cd05944 214 --GVFGGYLYTEGN-KNAFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74183796 524 DPSRGEVVKAFVVLAP-------EFLSHDRDqltkvlqeHVKSVTApykYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:cd05944 291 DAHAGELPVAYVQLKPgavveeeELLAWARD--------HVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
72-589 |
2.52e-37 |
|
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: 144.96 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 72 ASDVIDHWASVEKAGkrssgpalwwmngsgkEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGC 151
Cdd:cd05923 11 ASRAPDACAIADPAR----------------GLRLTYSELRARIEAVAARLH-ARGLRPGQRVAVVLPNSVEAVIALLAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 152 MRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDeVAQEVDAVAPdcSFLKIkLLVSENSREGWL-NFKALLKEASTih 230
Cdd:cd05923 74 HRLGAVPALINPRLKAAELAELIERGEMTAAVIAV-DAQVMDAIFQ--SGVRV-LALSDLVGLGEPeSAGPLIEDPPR-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 231 qcvetESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAkMDAASWTGLSTSD--IIWTISDTAWIMNILGAFLEPWVLGAC 308
Cdd:cd05923 148 -----EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV-LFMSTQAGLRHGRhnVVLGLMPLYHVIGFFAVLVAALALDGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 309 IFVhlLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ------QDLSSYKfphlHSCFSGG---ETLLpETLENwkAKT 379
Cdd:cd05923 222 YVV--VEEFDPADALKLIEQERVTSLFATPTHLDALAAaaefagLKLSSLR----HVTFAGAtmpDAVL-ERVNQ--HLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 380 GlEIREIYGQTE--TGLICRVSRT-MKVKPGYlgtafaHYDVQVIDEQGNV---LPPGKEGDIAIRVKPIWpigMFSGYV 453
Cdd:cd05923 293 G-EKVNIYGTTEamNSLYMRDARTgTEMRPGF------FSEVRIVRIGGSPdeaLANGEEGELIVAAAADA---AFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 454 DNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKA 533
Cdd:cd05923 363 NQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 534 FVVLAPEFLSHDR-DQLTKvlqehvKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd05923 443 CVVPREGTLSADElDQFCR------ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
101-589 |
4.74e-37 |
|
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: 143.50 E-value: 4.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtIQMRSS--DILYRLQASK 178
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP--IYPTSSaeQIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 179 ARAIVAGDevaqevdavaPDcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYFTSGTSGPPKMAEH 258
Cdd:cd05907 78 AKALFVED----------PD----------------------------------------DLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 259 SHCSlgIKAKMDAASwTGLSTSDIIWTIS--DTAWIMNILGAFLEPWVLGACIfVHLLPkfdSQTVLKVLSSYPINTLVG 336
Cdd:cd05907 108 SHRN--ILSNALALA-ERLPATEGDRHLSflPLAHVFERRAGLYVPLLAGARI-YFASS---AETLLDDLSEVRPTVFLA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 337 APIIYRML----LQQDLSSYK--------FPHLHSCFSGGETLLPETLEnWKAKTGLEIREIYGQTETGLICRVSRTMKV 404
Cdd:cd05907 181 VPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLH-FFRALGIPVYEGYGLTETSAVVTLNPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 405 KPGYLGTAFahYDVQV-IDEQGNVLppgkegdiairvkpIWPIGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYF 482
Cdd:cd05907 260 RIGTVGKPL--PGVEVrIADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 483 HFIGRSDD-IINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSrgevVKAFVVLAPEFLSH----------------D 545
Cdd:cd05907 324 HITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRPF----LVALIVPDPEALEAwaeehgiaytdvaelaA 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 74183796 546 RDQLTKVLQEHVKSVTA---PYKYPRKVeFVLDLPKTV-------TGKIERAKL 589
Cdd:cd05907 400 NPAVRAEIEAAVEAANArlsRYEQIKKF-LLLPEPFTIengeltpTLKLKRPVI 452
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
103-591 |
7.03e-37 |
|
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: 144.52 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGL--VF-MPGtiqMRSSDILYRLQASKA 179
Cdd:COG1021 48 ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAipVFaLPA---HRRAEISHFAEQSEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVA-----QEVDAVAPDCSFLKIKLLVSENsrEGWLNFKALLKEASTIHQCvETESRESAAIYFTSGTSGPPK 254
Cdd:COG1021 124 VAYIIPDRHRgfdyrALARELQAEVPSLRHVLVVGDA--GEFTSLDALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 MAEHSH----CSlgIKAKMDAASWtglstsdiiwtisDTAWIM--------N-------ILGAFLepwvLGACifVHLLP 315
Cdd:COG1021 201 LIPRTHddylYS--VRASAEICGL-------------DADTVYlaalpaahNfplsspgVLGVLY----AGGT--VVLAP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 316 KFDSQTVLKVLSSYPIN--TLVgaPIIYRMLLQQ------DLSSYKFphLHScfsGGETLLPETLENWKAKTGLEIREIY 387
Cdd:COG1021 260 DPSPDTAFPLIERERVTvtALV--PPLALLWLDAaersryDLSSLRV--LQV---GGAKLSPELARRVRPALGCTLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 388 GQTEtGLIC---------RVSRTMkvkpgylGTAFAHYD-VQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDN 455
Cdd:COG1021 333 GMAE-GLVNytrlddpeeVILTTQ-------GRPISPDDeVRIVDEDGNPVPPGEVGELLTR-------GpyTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 456 PKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAF 534
Cdd:COG1021 398 PEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 535 VVLAPEFLShdrdqlTKVLQEHVKSV-TAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:COG1021 478 VVPRGEPLT------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
103-592 |
1.38e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 143.55 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEwwlMI---LGCMRTGLVFMPGTIQMRSSDILYRLQASKA 179
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPA---MVeahFGVPMAGAVLNTLNTRLDAASIAFMLRHGEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQEVDAVAPDCSFLKIkLLV-------SENSREGWLNFKALLKEASTIHQCVETESR-ESAAIYFTSGTSG 251
Cdd:PRK08162 117 KVLIVDTEFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 252 PPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGACIFVHL-LPKFDSQTVLKVLSSYP 330
Cdd:PRK08162 196 NPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLP-----MFHCNGWCFPWTVAARAGTNVcLRKVDPKLIFDLIREHG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 331 INTLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLLPETLENWKAkTGLEIREIYGQTET-GlicrvsrtmkvkPGY 408
Cdd:PRK08162 271 VTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE-IGFDLTHVYGLTETyG------------PAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 LGTAFAHYDVQVIDE-------QG---------NVLPP---------GKE-GDIAIRVKpiwpIGMfSGYVDNPKKTQDN 462
Cdd:PRK08162 338 VCAWQPEWDALPLDEraqlkarQGvryplqegvTVLDPdtmqpvpadGETiGEIMFRGN----IVM-KGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 IRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP--- 539
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDgas 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 540 ----EFLSHDRDQLtkvlqehvksvtAPYKYPRKVEFVlDLPKTVTGKIERAKLRAK 592
Cdd:PRK08162 493 ateeEIIAHCREHL------------AGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
103-590 |
1.92e-36 |
|
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: 142.48 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAQEVDAVAPDcsflkikllVSENSREGWlnfkALLKEASTIhqcVETESRESAAIYFTSGTSGPPKMAEHSHCS 262
Cdd:cd17651 97 LTHPALAGELAVELVA---------VTLLDQPGA----AAGADAEPD---PALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 L-----------GIKAKMDAASWTGLSTSDIIWTISDTawimniLGAflepwvlGACIfvHLLP---KFDSQTVLKVLSS 328
Cdd:cd17651 161 LanlvawqarasSLGPGARTLQFAGLGFDVSVQEIFST------LCA-------GATL--VLPPeevRTDPPALAAWLDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 329 YPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETL-LPETLENWKAK-TGLEIREIYGQTETGLIcrVSRTMKVK 405
Cdd:cd17651 226 QRISRVFLPTVALRALAEHgRPLGVRLAALRYLLTGGEQLvLTEDLREFCAGlPGLRLHNHYGPTETHVV--TALSLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 406 PGY------LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ-----DNIRGD--FWLMGD 472
Cdd:cd17651 304 PAAwpapppIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAerfvpDPFVPGarMYRTGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 473 RGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLTKV 552
Cdd:cd17651 379 LARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-----APVDAAE 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 74183796 553 LQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd17651 454 LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
107-600 |
2.41e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 142.53 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK12406 13 SFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEV-DAVAPDCSFLKI----KLL----VSENSR---EGWLNFKALLKEASTIHQcveTESRESAAIYFTSGTSGPPK 254
Cdd:PRK12406 92 DLLHGLaSALPAGVTVLSVptppEIAaayrISPALLtppAGAIDWEGWLAQQEPYDG---PPVPQPQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 maehshcslGIK----AKMDAASWtGLSTSDIIWTISDTAWIM---------NILGafLEPWVLGACIFvhLLPKFDSQT 321
Cdd:PRK12406 169 ---------GVRraapTPEQAAAA-EQMRALIYGLKPGIRALLtgplyhsapNAYG--LRAGRLGGVLV--LQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VLKVLSSYPINTLVGAPIIYRMLLQ--------QDLSSYKFPhLHSCFSGGETLLPETLENWkaktGLEIREIYGQTETG 393
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRHV-IHAAAPCPADVKRAMIEWW----GPVIYEYYGSTESG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 394 LI--CRVSRTMKvKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGM--FSgYVDNPKKTQDNIRGDFWL 469
Cdd:PRK12406 310 AVtfATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA-----GNpdFT-YHNKPEKRAEIDRGGFIT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LSHDrdq 548
Cdd:PRK12406 383 SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAtLDEA--- 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 74183796 549 ltkVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSGRA 600
Cdd:PRK12406 460 ---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
109-591 |
3.15e-35 |
|
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: 138.66 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 109 RELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEwwlmILGC---MRTGLVFMPGTIQMRSSDILYRLQASKAR-AIVA 184
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAA----AEGVwiaDGVYIYLINSILTVFAAAAAWKCGACPAYkSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GDEVAQEVDAVAPDcsFLKIKLLVSENSREGWLNFKALLKEASTihQCVETESRESAAIYfTSGTSGPPK--MAEHSHCS 262
Cdd:cd05929 77 PRAEACAIIEIKAA--ALVCGLFTGGGALDGLEDYEAAEGGSPE--TPIEDEAAGWKMLY-SGGTTGRPKgiKRGLPGGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 LGIKAKMDAASWTGLSTSDI------IWTISDTAWIMNILgaflepwVLGACifVHLLPKFDSQTVLKVLSSYPINTLVG 336
Cdd:cd05929 152 PDNDTLMAAALGFGPGADSVylspapLYHAAPFRWSMTAL-------FMGGT--LVLMEKFDPEEFLRLIERYRVTFAQF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 337 APIIY-RM--LLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTA 412
Cdd:cd05929 223 VPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 413 FAHyDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmfSGYVDNPKKTQDNIRGDFW-LMGDRGIKDPEGYFHFIGRSDDI 491
Cdd:cd05929 303 VLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGWsTLGDVGYLDEDGYLYLTDRRSDM 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 492 INSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAfvVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVE 571
Cdd:cd05929 376 IISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIE 453
|
490 500
....*....|....*....|
gi 74183796 572 FVLDLPKTVTGKIERAKLRA 591
Cdd:cd05929 454 FVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
69-583 |
1.61e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 137.32 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 69 FNFAsDVIDHwaSVEKAGKRssgPALWWmngsGKEiKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMI 148
Cdd:PRK07798 3 WNIA-DLFEA--VADAVPDR---VALVC----GDR-RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 149 LGCMRTGLVfmPGTIQMR--SSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSflKIKLLVS------ENSREGWLNFK 220
Cdd:PRK07798 71 LGAFKARAV--PVNVNYRyvEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLP--KLRTLVVvedgsgNDLLPGAVDYE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 221 ALLKEASTIHQCVEtesRESAAIYF--TSGTSGPPK--MAEHS---HCSLGIKAKMdaaswTGLSTSDIiWTISD----- 288
Cdd:PRK07798 147 DALAAGSPERDFGE---RSPDDLYLlyTGGTTGMPKgvMWRQEdifRVLLGGRDFA-----TGEPIEDE-EELAKraaag 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 289 --TAWIM-----------NILGAFLEpwvlGACIFVHLLPKFDSQTVLKVLSSYPIN--TLVG----APII--YRMLLQQ 347
Cdd:PRK07798 218 pgMRRFPapplmhgagqwAAFAALFS----GQTVVLLPDVRFDADEVWRTIEREKVNviTIVGdamaRPLLdaLEARGPY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 348 DLSSykfphLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLiCRVSRTMKVKPGYLGTAF-AHYDVQVIDEQG 425
Cdd:PRK07798 294 DLSS-----LFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSETGF-GGSGTVAKGAVHTGGPRFtIGPRTVVLDEDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 426 NVLPPG--KEGDIAIRvKPIwPIGmfsgYVDNPKKTQDN---IRGDFW-LMGDRGIKDPEGYFHFIGRSDDIINSSGYRI 499
Cdd:PRK07798 368 NPVEPGsgEIGWIARR-GHI-PLG----YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 500 GPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKT 579
Cdd:PRK07798 442 FPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLAE----LRAHCRSSLAGYKVPRAIWFVDEVQRS 516
|
....
gi 74183796 580 VTGK 583
Cdd:PRK07798 517 PAGK 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
238-586 |
2.40e-34 |
|
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: 133.15 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 238 RESAAIYFTSGTSGPPKMAEHSHcslgikaKMDAASWTGLSTSDIIWTISDTAWI-MNILGAFLEPWVLGACIFVHLLPK 316
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLAN-------KTFFAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 317 FDS----QTVLKVLSSYPINTLVGAPII--YRMLLQQDLSSYKfPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQT 390
Cdd:cd17635 74 GGEnttyKSLFKILTTNAVTTTCLVPTLlsKLVSELKSANATV-PSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 391 ETGLICRVSRTMKVKP-GYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIrvKPIWpigMFSGYVDNPKKTQDNIRGDFWL 469
Cdd:cd17635 153 ETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPA---NMLGYWNNPERTAEVLIDGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshDRDQL 549
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENA 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 74183796 550 TKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:cd17635 304 IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
105-590 |
6.73e-34 |
|
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: 134.42 E-value: 6.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdilyrlqaskaraiva 184
Cdd:cd17649 12 SLSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdaVAPDCSFLKIKLLVsENSREGWLnfkallkeastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCSLG 264
Cdd:cd17649 67 ----------LDPEYPAERLRYML-EDSGAGLL---------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKAKMDAASWtGLSTSDIIWTISDtawiMNILGA---FLEPWVLGACIFVHLLPKFDS-QTVLKVLSSYPINTLVGAPII 340
Cdd:cd17649 121 AHCQATAERY-GLTPGDRELQFAS----FNFDGAheqLLPPLICGACVVLRPDELWASaDELAEMVRELGVTVLDLPPAY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 341 YRMLLQQ--DLSSYKFPHLHSCFSGGETLLPETLENWkAKTGLEIREIYGQTE---TGLICRVSRTMKVKPGYL--GTAF 413
Cdd:cd17649 196 LQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEatvTPLVWKCEAGAARAGASMpiGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 414 AHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD--------FWLMGD--RGIKDpeGYFH 483
Cdd:cd17649 275 GGRSAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDlaRWRDD--GVIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 484 FIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVkAFVVL-APEFLSHDRDQLTKvlqeHVKSVTA 562
Cdd:cd17649 348 YLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQLRT----ALRASLP 422
|
490 500
....*....|....*....|....*...
gi 74183796 563 PYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd17649 423 DYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
106-589 |
2.05e-33 |
|
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: 133.19 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAG 185
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 186 DEVAQEVDAVAPdcsflkIKLLVSENSREGwlnfkalLKEASTihqcvETESRESAAIYFTSGTSGPPKMAEHSHCSL-G 264
Cdd:cd12116 92 DALPDRLPAGLP------VLLLALAAAAAA-------PAAPRT-----PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLvN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKAKMDAAswTGLSTSDIIWTISDTAWIMNILGAFLePWVLGACifVHLLPK---FDSQTVLKVLSSYPINTLVGAPIIY 341
Cdd:cd12116 154 FLHSMRER--LGLGPGDRLLAVTTYAFDISLLELLL-PLLAGAR--VVIAPRetqRDPEALARLIEAHSITVMQATPATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 342 RMLLQQDLSsyKFPHLHS-CfsGGETLLPETLENWKAKTGlEIREIYGQTET---GLICRVSRTMKVKPgyLGTAFAHYD 417
Cdd:cd12116 229 RMLLDAGWQ--GRAGLTAlC--GGEALPPDLAARLLSRVG-SLWNLYGPTETtiwSTAARVTAAAGPIP--IGRPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLMGDRGIKDPEGYFHFIGRSD 489
Cdd:cd12116 302 VYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 490 DIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVkAFVVLApEFLSHDRDQLTKVLQEHVKSVTAPYKYprk 569
Cdd:cd12116 377 GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLK-AGAAPDAAALRAHLRATLPAYMVPSAF--- 451
|
490 500
....*....|....*....|.
gi 74183796 570 veFVLD-LPKTVTGKIERAKL 589
Cdd:cd12116 452 --VRLDaLPLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
243-586 |
2.96e-33 |
|
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: 129.83 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 243 IYFTSGTSGPPKMAEHSHcslgikakmdaASWTG--LSTSDIIWTISDTAwiMNILGAFLEPWVLGACIF-------VHL 313
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSE-----------RSWIEsfVCNEDLFNISGEDA--ILAPGPLSHSLFLYGAISalylggtFIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 314 LPKFDSQTVLKVLSSYPINTLVGAPiiyrMLLQQdLSSYKFPHLH--SCFSGGETLLPETLENWKAKT-GLEIREIYGQT 390
Cdd:cd17633 72 QRKFNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESKikSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 391 ETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGnvlppGKEGDIAIRVKPiwpigMFSGYVDNPKKTQDNirgdfWL- 469
Cdd:cd17633 147 ELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEM-----VFSGYVRGGFSNPDG-----WMs 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLapeflshdrDQL 549
Cdd:cd17633 212 VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG---------DKL 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 74183796 550 T-KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:cd17633 283 TyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
306-582 |
3.08e-33 |
|
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: 129.73 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 GACIFVhllPKFDSQTVLKVLSSYPI-NTLVGAPIIYRML-----LQQDLSSYKFPhlhSCFSGGETLLPETLENWKAKT 379
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCtHAFLLPPTIDQIVelnadGLYDLSSLRSS---PAAPEWNDMATVDTSPWGRKP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 380 GLeireiYGQTETGlicrvsrTMKVKPGYLGTAFAHY-------DVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGM--FS 450
Cdd:cd17636 141 GG-----YGQTEVM-------GLATFAALGGGAIGGAgrpsplvQVRILDEDGREVPDGEVGEIVAR-------GPtvMA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 451 GYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEV 530
Cdd:cd17636 202 GYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQS 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74183796 531 VKAFVVLAPEfLSHDRDQLTkvlqEHVKSVTAPYKYPRKVEFVLDLPKTVTG 582
Cdd:cd17636 282 VKAIVVLKPG-ASVTEAELI----EHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
74-586 |
1.10e-32 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 132.32 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 74 DVIDHwasveKAGKRSSGPALWWmngSGKEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMR 153
Cdd:PRK05852 20 DLVEV-----AATRLPEAPALVV---TADRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 154 TGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCV 233
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 234 ETESR-ESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIiwtisdTAWIM------NILGAFLEPWVLG 306
Cdd:PRK05852 171 PEGLRpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDA------TVAVMplyhghGLIAALLATLASG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 307 ACIfvhLLP---KFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ---DLSSYKFPHLHSCFSGGETLLPETLENWKAKTG 380
Cdd:PRK05852 244 GAV---LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 381 LEIREIYGQTET----------GLICrvSRTMKVKPGYLGTAFAhYDVQVIDEQGNVLPPGKEGDIAIRVKPIwpigmFS 450
Cdd:PRK05852 321 APVVCAFGMTEAthqvtttqieGIGQ--TENPVVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTV-----VR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 451 GYVDNPKKTQDNIRgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGE 529
Cdd:PRK05852 393 GYLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGE 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 530 VVKAfVVLAPEFLSHDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:PRK05852 472 AVAA-VIVPRESAPPTAEELVQFCRERL----AAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
92-598 |
1.12e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 132.11 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 92 PALWWmngsgKEIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfMPGTIQMRSSDIL 171
Cdd:PRK07867 20 RGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIV-PVGLNPTRRGAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 172 YR-LQASKARAIVAGDEVAQEVDAVAPDCSFLKIkllvsenSREGWLNFKALLKEASTIHQCVETESResAAIYFTSGTS 250
Cdd:PRK07867 94 ARdIAHADCQLVLTESAHAELLDGLDPGVRVINV-------DSPAWADELAAHRDAEPPFRVADPDDL--FMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 251 GPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWtISDTAWIMN-ILGAFLEPWVLGACIfvHLLPKFDSQTVLKVLSSY 329
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQRF-GLGPDDVCY-VSMPLFHSNaVMAGWAVALAAGASI--ALRRKFSASGFLPDVRRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 330 PIN--TLVGAPIIYRmllqqdLSSYKFPH-----LHSCFsGGETLlPETLENWKAKTGLEIREIYGQTETGLIcrVSRTM 402
Cdd:PRK07867 241 GATyaNYVGKPLSYV------LATPERPDdadnpLRIVY-GNEGA-PGDIARFARRFGCVVVDGFGSTEGGVA--ITRTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 403 KVKPGYLGTAFAhyDVQVID-EQGNVLPPGkEGDIAIRVKPIWPIG---------MFSGYVDNPKKTQDNIRGDFWLMGD 472
Cdd:PRK07867 311 DTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEADAERMRGGVYWSGD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 473 RGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP--EFlshDRDQLT 550
Cdd:PRK07867 388 LAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgaKF---DPDAFA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 74183796 551 KVLqeHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 598
Cdd:PRK07867 465 EFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCAD 510
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
106-591 |
1.30e-32 |
|
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: 134.21 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLsGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtI-----QMRssdILYRLQASKAR 180
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--LdpaypAER---LAYMLEDAGAR 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVAPDCsflkikLLVSEnsregwlnfkALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 260
Cdd:COG1020 576 LVLTQSALAARLPELGVPV------LALDA----------LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 CSLG--IkakMDAASWTGLSTSDII---WTIS-DTAwIMNILGAFLepwvLGACifVHLLPK---FDSQTVLKVLSSYPI 331
Cdd:COG1020 640 RALVnlL---AWMQRRYGLGPGDRVlqfASLSfDAS-VWEIFGALL----SGAT--LVLAPPearRDPAALAELLARHRV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 332 NTLVGAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKT-GLEIREIYGQTETGLICRVSRTMKVKPGY-- 408
Cdd:COG1020 710 TVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGgs 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 --LGTAFAHYDVQVIDEQGNVLPPGKEGDIAI------RvkpiwpigmfsGYVDNPKKTQDN-IRGDFWL----M---GD 472
Cdd:COG1020 788 vpIGRPIANTRVYVLDAHLQPVPVGVPGELYIggaglaR-----------GYLNRPELTAERfVADPFGFpgarLyrtGD 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 473 RGIKDPEGYFHFIGRSDD---IinsSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQL 549
Cdd:COG1020 857 LARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG-----AAAA 928
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 74183796 550 TKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:COG1020 929 AALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
107-589 |
3.18e-32 |
|
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: 130.09 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP---GTIQMRSSDILyrlqASKARAIV 183
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPldpGYPADRLAYML----ADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 AGDEVAQEVDAVAPDcsflkIKLLVSEnsregwlnfkALLKEASTIHQcVETESRESAAIYFTSGTSGPPK--MAEHS-- 259
Cdd:cd17646 100 LTTADLAARLPAGGD-----VALLGDE----------ALAAPPATPPL-VPPRPDNLAYVIYTSGSTGRPKgvMVTHAgi 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 260 -------HCSLGIKAKMDAASWTGLStSDI-IWTisdtawimnilgaFLEPWVLGACIFV-----HLLPKFdsqtVLKVL 326
Cdd:cd17646 164 vnrllwmQDEYPLGPGDRVLQKTPLS-FDVsVWE-------------LFWPLVAGARLVVarpggHRDPAY----LAALI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 327 SSYPINTLVGAPIIYRMLLQQDLSSyKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL---ICRVSRTMK 403
Cdd:cd17646 226 REHGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvtHWPVRGPAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 404 VKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIK 476
Cdd:cd17646 305 TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALTAERFVPDpfgpgsrMYRTGDLARW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 477 DPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQltkvLQEH 556
Cdd:cd17646 380 RPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA----LRAH 455
|
490 500 510
....*....|....*....|....*....|....
gi 74183796 557 VKSVTAPYKYPrKVEFVLD-LPKTVTGKIERAKL 589
Cdd:cd17646 456 LAERLPEYMVP-AAFVVLDaLPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
105-589 |
6.66e-32 |
|
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: 129.24 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 184
Cdd:cd12117 22 SLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GDEVAQEVDAVAPDcsflkikLLVSENSREGwlnfkallkEASTIHQCVETESResAAIYFTSGTSGPPK--MAEHShcs 262
Cdd:cd12117 101 DRSLAGRAGGLEVA-------VVIDEALDAG---------PAGNPAVPVSPDDL--AYVMYTSGSTGRPKgvAVTHR--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 lGIKAKMDAASWTGLSTSDIIWTISDTAW---IMNILGAFLEpwvlGACifVHLLPK---FDSQTVLKVLSSYPINTL-V 335
Cdd:cd12117 160 -GVVRLVKNTNYVTLGPDDRVLQTSPLAFdasTFEIWGALLN----GAR--LVLAPKgtlLDPDALGALIAEEGVTVLwL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 336 GAPIiYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKT-GLEIREIYGQTETGLicrVSRTMKVKPGYL----- 409
Cdd:cd12117 233 TAAL-FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTT---FTTSHVVTELDEvagsi 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 410 --GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGD---FWLMGDRGIKDPEG 480
Cdd:cd12117 307 piGRPIANTRVYVLDEDGRPVPPGVPGELYVG-----GDGLALGYLNRPALTAerfvADPFGPgerLYRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 481 YFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPD-PSRGEVVkAFVVLAPEfLSHDRdqltkvLQEHVKS 559
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-AYVVAEGA-LDAAE------LRAFLRE 453
|
490 500 510
....*....|....*....|....*....|
gi 74183796 560 VTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd12117 454 RLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
94-590 |
1.01e-30 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 127.32 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 94 LWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYR 173
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 174 LQASKARAIVAGDEVAQEVDAVapdcsFLK--IKLLVSENSREG--------WLNFKALLKEASTIHQ------------ 231
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTI-----NLKdiVDAALDESAKNGvsvgicltYENQLAMKREDTKWQEgrdvwwqdvvpn 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 232 ----C-VE-TESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVL 305
Cdd:PLN02654 263 yptkCeVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 GACIFV-HLLPKF-DSQTVLKVLSSYPINTLVGAPIIYRMLLQQD---LSSYKFPHLHSCFSGGETLLPETLE---NWKA 377
Cdd:PLN02654 343 GATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRwffNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 378 KTGLEIREIYGQTETG--LICRVSRTMKVKPGylGTAFAHYDVQ--VIDEQGNVLppgkEGDIA--IRVKPIWPIGMFSG 451
Cdd:PLN02654 423 DSRCPISDTWWQTETGgfMITPLPGAWPQKPG--SATFPFFGVQpvIVDEKGKEI----EGECSgyLCVKKSWPGAFRTL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 452 YVDNPKKTQDNIR--GDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGE 529
Cdd:PLN02654 497 YGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQ 576
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74183796 530 VVKAFVVLApEFLSHDrDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PLN02654 577 GIYAFVTLV-EGVPYS-EELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
107-591 |
1.10e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 126.82 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWW--LMILGCMrtGLVFMPGTIQMRSSDILYRLQASKARAIVA 184
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GDEVAQEVDAVAPDCSFLKIKLLVSENS--------REGW--LNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPK 254
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDadsaaahmPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 MAEHSHCSLGIKAkmdaaswTGLSTSDIIWTISDTAW-----IMNIL--GAFLEPWVLGACIfVHLLPKFDSQTVLKVLS 327
Cdd:PRK05620 198 GVVYSHRSLYLQS-------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGTPL-VFPGPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPIIYRMLLQQDL-SSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTmkvKP 406
Cdd:PRK05620 270 TAMPRVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 GYLGTAFAHYDV-----------QVIDEqGNVLPPGKEGDIAIRVKPIWPIGmfsGYVDNPKKTQDN----IRG------ 465
Cdd:PRK05620 347 GVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTDRNEGEIQVRGNWVTA---SYYHSPTEEGGGaastFRGedveda 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 466 ------DFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLA 538
Cdd:PRK05620 423 ndrftaDGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLA 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 74183796 539 P--EFLSHDRDQLTKVLQEHVKSVTAPYKYprkvEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK05620 503 PgiEPTRETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
104-592 |
1.69e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 126.11 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 104 IKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIV 183
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 AGDEV------AQEVDAVAPDCSFLKIKLLVSENSREGWLNFK-ALLKEASTIHQCVETESRE-----------SAAIYF 245
Cdd:PLN02479 123 VDQEFftlaeeALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQyALGKGAIEYEKFLETGDPEfawkppadewqSIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 246 TSGTSGPPKMAEHSHCSLGIKAKMDAASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGA-CIFVHLLPKFDSQTVLK 324
Cdd:PLN02479 203 TSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLP-----MFHCNGWCFTWTLAAlCGTNICLRQVTAKAIYS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 325 VLSSYPINTLVGAPIIYRMLLQQDLSS--YKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTET---GLIC--- 396
Cdd:PLN02479 278 AIANYGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETygpSTVCawk 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 397 ------------RVSRTMKVKpgYLGTAfahyDVQVIDEQGNVLPP--GKE-GDIAIRVKpiwpiGMFSGYVDNPKKTQD 461
Cdd:PLN02479 357 pewdslppeeqaRLNARQGVR--YIGLE----GLDVVDTKTMKPVPadGKTmGEIVMRGN-----MVMKGYLKNPKANEE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 462 NIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF 541
Cdd:PLN02479 426 AFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGV 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 74183796 542 LSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVlDLPKTVTGKIERAKLRAK 592
Cdd:PLN02479 506 DKSDEAALAEDIMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
107-589 |
2.02e-30 |
|
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: 124.75 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:cd17655 24 TYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDavapdcsFLK-IKLLVSENSREGwlnfkallkEASTIHqcVETESRESAAIYFTSGTSGPPK--MAEHS---- 259
Cdd:cd17655 103 HLQPPIA-------FIGlIDLLDEDTIYHE---------ESENLE--PVSKSDDLAYVIYTSGSTGKPKgvMIEHRgvvn 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 260 -HCSLGIKAKMDAASWTGLSTSdiiwtISDTAWIMNILGAFLepwvLGACIfvHLLPK---FDSQTVLKVLSSYPINTLV 335
Cdd:cd17655 165 lVEWANKVIYQGEHLRVALFAS-----ISFDASVTEIFASLL----SGNTL--YIVRKetvLDGQALTQYIRQNRITIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 336 GAPIIYRMLLQQDLSSykFPHLHSCFSGGETLLPETLENWKAKTGL--EIREIYGQTETGL-----ICRVSRTMKVKPgY 408
Cdd:cd17655 234 LTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdasiyQYEPETDQQVSV-P 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD-------PEGY 481
Cdd:cd17655 311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDDPFVPGERMYRTgdlarwlPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 482 FHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHD-RDQLTKVLQEhvksv 560
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQlREFLARELPD----- 460
|
490 500 510
....*....|....*....|....*....|.
gi 74183796 561 tapYKYPRKveFV-LD-LPKTVTGKIERAKL 589
Cdd:cd17655 461 ---YMIPSY--FIkLDeIPLTPNGKVDRKAL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
107-590 |
2.10e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 122.64 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM-------PGTIQMRSSDilyrlqASKA 179
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnpsssLGEIKKRVVD------CSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQevdavapdCSFLKIK-LLVSENsregwLNFKALLKEASTIHQCVETES----------RESAAIYFTSG 248
Cdd:PLN02574 142 LAFTSPENVEK--------LSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEDFdfvpkpvikqDDVAAIMYSSG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 249 TSGPPKMAEHSH----CSLGIKAKMDAASWTGLSTSDI---------IWTISdtAWIMNILGaflepwvLGACIFVhlLP 315
Cdd:PLN02574 209 TTGASKGVVLTHrnliAMVELFVRFEASQYEYPGSDNVylaalpmfhIYGLS--LFVVGLLS-------LGSTIVV--MR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 316 KFDSQTVLKVLSSYPINTLVGAPIIYRMLLQ--QDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTE- 391
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEs 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 392 TGLICRVSRTMKVKP-GYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvKPiwpiGMFSGYVDNPKKTQDNIRGDFWL 469
Cdd:PLN02574 358 TAVGTRGFNTEKLSKySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 -MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlapeflshdRDQ 548
Cdd:PLN02574 433 rTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV---------RRQ 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 74183796 549 LTKVLQE----HVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PLN02574 504 GSTLSQEavinYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
127-592 |
3.62e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 122.83 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 127 GLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAqevDAVAPDcSFLKIKL 206
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALR---DRFQPS-RVAEAAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 207 LVSENSREGWLNFKALLKEAStihqcvetesresAAIYFTSGTSGPPKMAEHSHC-------SLGIKAKMDAASWTGLST 279
Cdd:PRK06060 127 LMSEAARVAPGGYEPMGGDAL-------------AYATYTSGTTGPPKAAIHRHAdpltfvdAMCRKALRLTPEDTGLCS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 280 SDIIWT--ISDTAWImnilgaflePWVLGACIFVHLLPKfdSQTVLKVLSS-YPINTLVGAPIIYRMLLQQdLSSYKFPH 356
Cdd:PRK06060 194 ARMYFAygLGNSVWF---------PLATGGSAVINSAPV--TPEAAAILSArFGPSVLYGVPNFFARVIDS-CSPDSFRS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 357 LHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGD 435
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 436 IAIRVKPIwpigmFSGYVDNPKKTQDNirGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVS 515
Cdd:PRK06060 342 LWVRGPAI-----AKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 516 ETAVISSPDPSRGEVVKAFVVLA-PEFLshDRDQLTKVLQEHVKSVTApYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:PRK06060 415 EAAVVAVRESTGASTLQAFLVATsGATI--DGSVMRDLHRGLLNRLSA-FKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
130-590 |
3.73e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.05 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 130 RGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDE---VAQEVDAVAP-DCSFLKIK 205
Cdd:PLN03102 63 KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfepLAREVLHLLSsEDSNLNLP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 206 -LLVSEN-------SREgwLNFKALLKEASTIHQ------CVETEsRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDA 271
Cdd:PLN03102 143 vIFIHEIdfpkrpsSEE--LDYECLIQRGEPTPSlvarmfRIQDE-HDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 272 ASWTGLSTSDIIWTISdtawiMNILGAFLEPWVLGA------CIFVHLLPKfdsqtVLKVLSSYPINTLVGAPIIYRMLL 345
Cdd:PLN03102 220 IGWEMGTCPVYLWTLP-----MFHCNGWTFTWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQDLS--SYKFPHLHsCFSGGETLlPETLENWKAKTGLEIREIYGQTE-TG--LICR-----------VSRTMKVKPGYL 409
Cdd:PLN03102 290 KGNSLdlSPRSGPVH-VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpenQQMELKARQGVS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 410 GTAFAHYDVQVIDEQGNVLPPGKE-GDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRS 488
Cdd:PLN03102 368 ILGLADVDVKNKETQESVPRDGKTmGEIVIKGSSI-----MKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 489 DDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVL--APEFLSHDRDQLT---KVLQEHVKSVTAP 563
Cdd:PLN03102 443 KDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLIEYCRENLPH 522
|
490 500
....*....|....*....|....*..
gi 74183796 564 YKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PLN03102 523 FMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
107-590 |
3.77e-29 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 120.11 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARaivagd 186
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGAT------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevdavapdcsflkikLLVSENSregwlnfkallkeastihqcveteSRESAAIYFTSGTSGPPK--MAEHShcslg 264
Cdd:cd17653 97 -------------------LLLTTDS------------------------PDDLAYIIFTSGSTGIPKgvMVPHR----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 ikakmdaaswtglSTSDIIWTISDT---------AWIMNIlgAFlepWVLGACIFV------HLLPKFDSQTVLKVLSSy 329
Cdd:cd17653 129 -------------GVLNYVSQPPARldvgpgsrvAQVLSI--AF---DACIGEIFStlcnggTLVLADPSDPFAHVART- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 330 pINTLVGAPIIYRMLLQQDlssykFPHLHSCFSGGETLLPETLENWKAktGLEIREIYGQTETGLICRVSRTMKVKPGYL 409
Cdd:cd17653 190 -VDALMSTPSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 410 GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQD----NIRGDFWLM---GDRGIKDPEGYF 482
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASkfvpDPFWPGSRMyrtGDYGRWTEDGGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 483 HFIGRSDDIINSSGYRIGPSEVENALM-EHPAVSETAVISSpdpsrGEVVKAFVvlAPEflSHDRDQLTKVLQEHVKSvt 561
Cdd:cd17653 337 EFLGREDNQVKVRGFRINLEEIEEVVLqSQPEVTQAAAIVV-----NGRLVAFV--TPE--TVDVDGLRSELAKHLPS-- 405
|
490 500
....*....|....*....|....*....
gi 74183796 562 apYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd17653 406 --YAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
107-590 |
3.82e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 121.04 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACglHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKE--SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevdavapdcsFLKIKLLVSENSREGWLNFKALL-KEASTIHQcveTESRESAAIY--FTSGTSGPPKMAEHSHcsl 263
Cdd:PRK07638 106 --------------YKLNDLPDEEGRVIEIDEWKRMIeKYLPTYAP---IENVQNAPFYmgFTSGSTGKPKAFLRAQ--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 264 gikakmdaASWT-GLSTSDIIWTISDTAWIMnILGAFLEPWVLGACIF-------VHLLPKFDSQTVLKVLSSYPINTLV 335
Cdd:PRK07638 166 --------QSWLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLYGAIStlyvgqtVHLMRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 336 GAPIIYRMLLQQDlssyKFP-HLHSCFSGGETLLPETLEnwKAKTG---LEIREIYGQTETGLICR-VSRTMKVKPGYLG 410
Cdd:PRK07638 237 TVPTMLESLYKEN----RVIeNKMKIISSGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSFVTAlVDEESERRPNSVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 411 TAFAHYDVQVIDEQGNVLPPGKEGDIAIRvKPIwpigMFSGYV-DNPKKTQDNIRGdfWL-MGDRGIKDPEGYFHFIGRS 488
Cdd:PRK07638 311 RPFHNVQVRICNEAGEEVQKGEIGTVYVK-SPQ----FFMGYIiGGVLARELNADG--WMtVRDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 489 DDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVvlapeflshDRDQLTKVLQEHVKSVTAPYKYPR 568
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPK 454
|
490 500
....*....|....*....|..
gi 74183796 569 KVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK07638 455 EWHFVDEIPYTNSGKIARMEAK 476
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
241-592 |
5.26e-29 |
|
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: 117.82 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLGIKAKMdAASWTGLSTSDiiwtisdtAWIMN-----ILG-AFLEPWVLGACIFVHLL 314
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAG-LHSRLGFGGGD--------SWLLSlplyhVGGlAILVRSLLAGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 PKFDsqtVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKtGLEIREIYGQTETGL 394
Cdd:cd17630 74 RNQA---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 395 ICRVSRTMKVKPGYLGTAFAHYDVQvIDEQGNVLPPGKegdiairvkpiwpiGMFSGYVDNPkkTQDNIRGDFWL-MGDR 473
Cdd:cd17630 150 QVATKRPDGFGRGGVGVLLPGRELR-IVEDGEIWVGGA--------------SLAMGYLRGQ--LVPEFNEDGWFtTKDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 474 GIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdrdQLTKVL 553
Cdd:cd17630 213 GELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-------ADPAEL 285
|
330 340 350
....*....|....*....|....*....|....*....
gi 74183796 554 QEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAK 592
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-586 |
8.32e-29 |
|
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: 119.85 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEvaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesRESAAIYFTSGTSGPPK--MAEH 258
Cdd:cd05914 82 AIFVSDE--------------------------------------------------DDVALINYTSGTTGNSKgvMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 259 SHcslgIKAKMDAASWTGLST-SDIIWTISDTAWIMNILGAFLEPWVLGACIfvHLLPKFDSQTVLKvLSSYPINTLVGA 337
Cdd:cd05914 112 RN----IVSNVDGVKEVVLLGkGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKIPSAKIIA-LAFAQVTPTLGV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 338 PI------IYRMLLQQDLSSYK------------------FPHLHSCF--------SGGETLLPETLENWKaKTGLEIRE 385
Cdd:cd05914 185 PVplviekIFKMDIIPKLTLKKfkfklakkinnrkirklaFKKVHEAFggnikefvIGGAKINPDVEEFLR-TIGFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQgnvlPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRG 465
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 466 DFWL-MGDRGIKDPEGYFHFIGRSDD-IINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSrgevvKAFVVLAPEFLS 543
Cdd:cd05914 335 DGWFhTGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL-----VALAYIDPDFLD 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 74183796 544 ----HDRDQLTKVLQEHVKSV---TAPYKYPRKVEFVL-DLPKTVTGKIER 586
Cdd:cd05914 410 vkalKQRNIIDAIKWEVRDKVnqkVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
107-589 |
3.14e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 121.04 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDaVAPDCSFLKIKLLvsensregwlnfKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGIK 266
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLCLDEP------------ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMdAASWTGLSTSDIIWTISDTAWIMNILGAFlepWVLGACIFVHLLPK---FDSQTVLKVLSSYPINTLVGAPIIYRM 343
Cdd:PRK12467 685 VCV-IAERLQLAADDSMLMVSTFAFDLGVTELF---GALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 344 LLQQDLSSYKFPhLHSCFSGGETLLPETLENWKAKT-GLEIREIYGQTETGLICRVSRTMK----VKPGYLGTAFAHYDV 418
Cdd:PRK12467 761 LLQASRVALPRP-QRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYELSDeerdFGNVPIGQPLANLGL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 419 QVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD--------FWLMGDRGIKDPEGYFHFIGRSDD 490
Cdd:PRK12467 840 YILDHYLNPVPVGVVGELYIGGA-----GLARGYHRRPALTAERFVPDpfgadggrLYRTGDLARYRADGVIEYLGRMDH 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 491 IINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVkAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKV 570
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHL 993
|
490
....*....|....*....
gi 74183796 571 EFVLDLPKTVTGKIERAKL 589
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKAL 1012
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
105-592 |
3.50e-28 |
|
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: 119.06 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEW-WLMI----LGCMRTGLV--FMPgtiqmrsSDILYRLQAS 177
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWvWAELaaqaIGALSLGIYqdSMA-------EEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 178 KARAIVAGDEvaQEVDAV---APDCSFLKIKLLVSE----NSREGWLN-FKALLKEASTIHQ---------CVETESRES 240
Cdd:cd17641 83 GARVVIAEDE--EQVDKLleiADRIPSVRYVIYCDPrgmrKYDDPRLIsFEDVVALGRALDRrdpglyereVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI----------- 309
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnfpeepetmme 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 310 --------FVHLLPK----FDSQTVLKVLSSYPINTLV-------------------------------GAPIIYRMLLQ 346
Cdd:cd17641 240 dlreigptFVLLPPRvwegIAADVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 347 QdlssYKFPHLHSCFSGGETLLPETLENWKAkTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQvIDEQGN 426
Cdd:cd17641 320 R----LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR-IDEVGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 427 VLPPGKegdiairvkpiwpiGMFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDIINSS-GYRIGPSEV 504
Cdd:cd17641 394 ILVRSP--------------GVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 505 ENALMEHPAVSETAVISSPDPsrgeVVKAFVVLAPEFLSH----------------DRDQLTKVLQEHVKSVTAPYKYPR 568
Cdd:cd17641 460 ENKLKFSPYIAEAVVLGAGRP----YLTAFICIDYAIVGKwaeqrgiafttytdlaSRPEVYELIRKEVEKVNASLPEAQ 535
|
570 580 590
....*....|....*....|....*....|...
gi 74183796 569 KVEFVLDLPK---------TVTGKIERAKLRAK 592
Cdd:cd17641 536 RIRRFLLLYKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-589 |
1.17e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAQEVDAVApdcsflKIKLLVSENSREgWLNFKALLKEastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCS 262
Cdd:PRK12316 4653 LTQSHLLQRLPIPD------GLASLALDRDED-WEGFPAHDPA-------VRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 LgikakMDAASWTG----LSTSDIIWTISDTAWIMNILGAFLePWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAP 338
Cdd:PRK12316 4719 L-----VNHLHATGeryeLTPDDRVLQFMSFSFDGSHEGLYH-PLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 339 IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETL-ENWKAKTGLEIREIYGQTETGLicrVSRTMKVKPGY--------L 409
Cdd:PRK12316 4793 VYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYdLAWRALKPVYLFNGYGPTETTV---TVLLWKARDGDacgaaympI 4869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 410 GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ--------DNIRGDFWLMGDRGIKDPEGY 481
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAerfvpdpfGAPGGRLYRTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 482 FHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQ--LTKVLQEHVKS 559
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRE 5024
|
490 500 510
....*....|....*....|....*....|
gi 74183796 560 VTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:PRK12316 5025 RLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
241-591 |
1.52e-27 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 117.21 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLGIK--AKMDAAswtGLSTSDIIWTISDTAWIMNILGAfLEPWVLGACifvH-LLPKF 317
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQslAKIAIV---GYGEDDVYLHTAPLCHIGGLSSA-LAMLMVGAC---HvLLPKF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 318 DSQTVLKVLSSYPINTLVGAPIIYRMLL---QQDLSSYKFPHLHSCFSGGETLLPETLENW-KAKTGLEIREIYGQTETg 393
Cdd:PLN02860 248 DAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAkKLFPNAKLFSAYGMTEA- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 394 liCRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPP-----GKEG---------DIAIRVKPIWPIG--MFSGYVDNPK 457
Cdd:PLN02860 327 --CSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPqgvcvGKPAphvelkiglDESSRVGRILTRGphVMLGYWGQNS 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 458 KTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVV 536
Cdd:PLN02860 405 ETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVR 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 537 LAPEFL-SHDRDQLTK--------VLQEHV--KSVTApYKYPRKveFVL---DLPKTVTGKIERAKLRA 591
Cdd:PLN02860 485 LRDGWIwSDNEKENAKknltlsseTLRHHCreKNLSR-FKIPKL--FVQwrkPFPLTTTGKIRRDEVRR 550
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
107-589 |
1.61e-27 |
|
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: 115.43 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVagd 186
Cdd:cd17652 14 TYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSH-CSL 263
Cdd:cd17652 90 ------------------------------------------------TTPDNLAYVIYTSGSTGRPKgvVVTHRGlANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 264 gIKAKMDAASWTGLSTSDIIWTISDTAWIMNILGAFLEpwvlGACifVHLLPKFDS---QTVLKVLSSYPINTLVGAPII 340
Cdd:cd17652 122 -AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLA----GAT--LVLAPAEELlpgEPLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 341 YRMLLQQDLssykfPHLHSCFSGGETLLPETLENWKakTGLEIREIYGQTETGL---ICRVSRTMKVKPgyLGTAFAHYD 417
Cdd:cd17652 195 LAALPPDDL-----PDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTVcatMAGPLPGGGVPP--IGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLMGDRGIKDPEGYFHFIGRSD 489
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 490 DIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflshDRDQLTKVLQEHVKSVTAPYKYPRK 569
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAA 415
|
490 500
....*....|....*....|.
gi 74183796 570 VeFVLD-LPKTVTGKIERAKL 589
Cdd:cd17652 416 F-VVLDaLPLTPNGKLDRRAL 435
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
103-589 |
6.04e-27 |
|
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: 114.29 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAGDEVAQEVDAVAPDcsflkikllvsensregwLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHcs 262
Cdd:cd12114 89 LTDGPDAQLDVAVFDV------------------LILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISH-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 lgikakmDAASWT--------GLSTSDIIWTISDTAWIM---NILGAFlepwVLGACIfvhLLP----KFDSQTVLKVLS 327
Cdd:cd12114 149 -------RAALNTildinrrfAVGPDDRVLALSSLSFDLsvyDIFGAL----SAGATL---VLPdearRRDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPIIYRMLLQQDLSSYKFPH-----LHScfsgGETL---LPETLenWKAKTGLEIREIYGQTETGL----- 394
Cdd:cd12114 215 RHGVTLWNSVPALLEMLLDVLEAAQALLPslrlvLLS----GDWIpldLPARL--RALAPDARLISLGGATEASIwsiyh 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 395 -ICRVSRTMKVKPgYlGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ-----DNIRGDFW 468
Cdd:cd12114 289 pIDEVPPDWRSIP-Y-GRPLANQRYRVLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAarfvtHPDGERLY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 469 LMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVLAPEFLSHDRDQ 548
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPIAPDA 440
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 74183796 549 LTKVLQEHVKSvtapYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd12114 441 LRAFLAQTLPA----YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
107-589 |
6.70e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 114.71 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK13383 62 SYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVdAVAPDcsflkiKLLVSENSREGwlnfkallKEASTIHQCVETESResaAIYFTSGTSGPPKmaehshcslGIK 266
Cdd:PRK13383 141 EFAERI-AGADD------AVAVIDPATAG--------AEESGGRPAVAAPGR---IVLLTSGTTGKPK---------GVP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWTGLSTSDIIWTISDTAWIMNI---------LGAFLEPWVLGACIFVHllPKFDSQTVLKVLSSYPINTLVGA 337
Cdd:PRK13383 194 RAPQLRSAVGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH--RHFDAEAALAQASLHRADAFTAV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 338 PIIYRMLLQ---QDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL-ICRVSRTMKVKPGYLGTAF 413
Cdd:PRK13383 272 PVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 414 AHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwpiGMFSG--YVDNP-KKTQDNIRGdfwlMGDRGIKDPEGYFHFIGRSDD 490
Cdd:PRK13383 352 AGCPVRILDRNNRPVGPRVTGRIFVG-------GELAGtrYTDGGgKAVVDGMTS----TGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 491 IINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQltkvLQEHVKSVTAPYKYPRKV 570
Cdd:PRK13383 421 MIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFEQPRDI 495
|
490
....*....|....*....
gi 74183796 571 EFVLDLPKTVTGKIERAKL 589
Cdd:PRK13383 496 NIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
105-590 |
9.76e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 114.42 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLsGACGLHRGDRVAVVlpripEW-----WLMILGCMRTGLVFMpgTIQMR--SSDILYRLQAS 177
Cdd:PRK07008 39 RYTYRDCERRAKQLAQAL-AALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCH--TINPRlfPEQIAYIVNHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 178 KARAIVAGDEVAQEVDAVAPDCSFLKikllvsensreGW--LNFKALLKEASTIHQCVET--------------ESRESA 241
Cdd:PRK07008 111 EDRYVLFDLTFLPLVDALAPQCPNVK-----------GWvaMTDAAHLPAGSTPLLCYETlvgaqdgdydwprfDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 242 AIYFTSGTSGPPKMAEHSHCSLGIKAKMDA-ASWTGLSTSDIIWTISD----TAWIMNILGAflepwvLGACIFVHLLPK 316
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVLHAYGAAlPDAMGLSARDAVLPVVPmfhvNAWGLPYSAP------LTGAKLVLPGPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 317 FDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET--- 392
Cdd:PRK07008 254 LDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMspl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 393 GLICRV-----SRTMKVKPGYL---GTAFAHYDVQVIDEQGNVLP-PGKE-GDIAIRvKPiWPIgmfSGYVdnpKKTQDN 462
Cdd:PRK07008 334 GTLCKLkwkhsQLPLDEQRKLLekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR-GP-WVI---DRYF---RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 IRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFl 542
Cdd:PRK07008 406 LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 74183796 543 SHDRDQLTKvlqeHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK07008 485 EVTREELLA----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
106-596 |
6.70e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 112.04 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRE-LSEASKQTAnvlsGACGLHRGDR---VAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARA 181
Cdd:PRK13388 27 WTWREvLAEAAARAA----ALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 IVAGDEVAQEVDAVA-PDcsflkIKLLVSENSRegwlnFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 260
Cdd:PRK13388 103 LVTDAEHRPLLDGLDlPG-----VRVLDVDTPA-----YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 CSLGIKAKMDAASWtGLSTSDIIWtISDTAWIMNILGAFLEPWVL-GACifVHLLPKFDSQTVLKVLSSYPIN--TLVGA 337
Cdd:PRK13388 173 GRLAFAGRALTERF-GLTRDDVCY-VSMPLFHSNAVMAGWAPAVAsGAA--VALPAKFSASGFLDDVRRYGATyfNYVGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 338 PIIYRMLLQQDLSSYKFPhLHSCFsgGETLLPETLENWKAKTGLEIREIYGQTETGliCRVSRTMKVKPGYLGTAF---A 414
Cdd:PRK13388 249 PLAYILATPERPDDADNP-LRVAF--GNEASPRDIAEFSRRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGApgvA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 415 HYD--------VQVIDEQGNVLPPGKE-GDIAIRVKPiwpiGMFSGYVDNPKKTQDNIR-GDFWlMGDRGIKDPEGYFHF 484
Cdd:PRK13388 324 IYNpetltecaVARFDAHGALLNADEAiGELVNTAGA----GFFEGYYNNPEATAERMRhGMYW-SGDLAYRDADGWIYF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 485 IGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAP----------EFLSHDRDQLTKVlq 554
Cdd:PRK13388 399 AGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDgatfdpdafaAFLAAQPDLGTKA-- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 74183796 555 ehvksvtapykYPRKVEFVLDLPKTVTGKIERAKLRAKEWKT 596
Cdd:PRK13388 477 -----------WPRYVRIAADLPSTATNKVLKRELIAQGWAT 507
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
101-562 |
2.11e-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: 110.25 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 101 GKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAR 180
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAG---DEVAQEvdAVAPDCSFLKIKLLVSE-NSREGWlnfKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMA 256
Cdd:cd05932 81 ALFVGkldDWKAMA--PGVPEGLISISLPPPSAaNCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 EHSHCSLGIKAKMdAASWTGLSTSDIIWTISDTAWIMNILGAFLEPWVLGACI-FVHLLPKF--DSQ----TVL------ 323
Cdd:cd05932 156 MLTFGSFAWAAQA-GIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVaFAESLDTFveDVQrarpTLFfsvprl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 324 ------KVLSSYP---INTLVGAPIIYRMLLQQDLSSYKFPHLHsCFSGGETLLPETLENWKAKTGLEIREIYGQTETGL 394
Cdd:cd05932 235 wtkfqqGVQDKIPqqkLNLLLKIPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 395 ICRVSRTMKVKPGYLGTAFAhyDVQV-IDEQGNVLppgkegdiaIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGD 472
Cdd:cd05932 314 YSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL---------VRSP-----ALMMGYYKDPEATAEAFTADGFLrTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 473 RGIKDPEGYFHFIGRSDDIINSS-GYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRDQLTK 551
Cdd:cd05932 378 KGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAFARAELEA 457
|
490
....*....|.
gi 74183796 552 VLQEHVKSVTA 562
Cdd:cd05932 458 SLRAHLARVNS 468
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
105-589 |
3.21e-25 |
|
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: 108.80 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 184
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHS--- 259
Cdd:cd17645 101 --------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHHnlv 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 260 ------HCSLGIKAKMDAASWTGLSTSDIIWTISDTawimnilgaflepWVLGACifVHLLP---KFDSQTVLKVLSSYP 330
Cdd:cd17645 131 nlcewhRPYFGVTPADKSLVYASFSFDASAWEIFPH-------------LTAGAA--LHVVPserRLDLDALNDYFNQEG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 331 INTLVGAPIIYRMLLQQDLSSykfphLHSCFSGGETLlpetleNWKAKTGLEIREIYGQTEtgliCRVSRTM-KVKPGY- 408
Cdd:cd17645 196 ITISFLPTGAAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYa 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 ---LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWLMGDRGIKD-------P 478
Cdd:cd17645 261 nipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 479 EGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVlAPEFLSHDRdqltkvLQEHVK 558
Cdd:cd17645 336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEIPHEE------LREWLK 408
|
490 500 510
....*....|....*....|....*....|.
gi 74183796 559 SVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17645 409 NDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
232-591 |
3.90e-25 |
|
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: 108.96 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 232 CVETESRESAAIYFTSGTSGPPKMAEHSHCSL-----GIKAKMDAaswtglSTSDIIwtisdtawiMNIL---------G 297
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP------NPEDVV---------FGALpffhsfgltG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 298 AFLEPWVLGACIFVHLLPkFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQdLSSYKFPHLHSCFSGGETLLPETLENWKA 377
Cdd:cd05909 206 CLWLPLLSGIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 378 KTGLEIREIYGQTETGLICRVSR-TMKVKPGYLGTAFAHYDVQVIDEQGNV-LPPGKEGDIAIRVKPIwpigmFSGYVDN 455
Cdd:cd05909 284 KFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNV-----MLGYLNE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 456 PKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEH-PAVSETAVISSPDPSRGEVVKAF 534
Cdd:cd05909 359 PELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 535 VVLapeflsHDRDQLTkvLQEHVKSVTAPYKY-PRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:cd05909 439 TTT------TDTDPSS--LNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
503-583 |
5.44e-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: 98.39 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 503 EVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTG 582
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 74183796 583 K 583
Cdd:pfam13193 76 K 76
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
103-590 |
1.81e-24 |
|
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: 107.13 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VagdeVAQEVDAVAPDCSFLKIKLLVSENSREGWLNFKALLKEASTIHQCVE-TESRESAAIYFTSGTSGPPKMAEHSH- 260
Cdd:cd05915 101 L----FDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 ------CSLGIKAKMDAASWTGLSTSDIIWTISDTAWImnilgaflepWVLGAC--IFVHLLPKFDSQTVLKVLSSYPIN 332
Cdd:cd05915 177 alvlhsLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP----------YAATLVgaKQVLPGPRLDPASLVELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVGAPIIYRMLLQ-QDLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTET---GLIC-----------R 397
Cdd:cd05915 247 FTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNfvkshleslseE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 398 VSRTMKVKPGYLGTAFAhydVQVIDEQGNVLP-PGKegdiAIRVKPIWPIGMFSGYVDNPKKTQ-DNIRGDFWLMGDRGI 475
Cdd:cd05915 326 EKLTLKAKTGLPIPLVR---LRVADEEGRPVPkDGK----ALGEVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 476 KDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPeflSHDRDQltKVLQE 555
Cdd:cd05915 399 WDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG---EKPTPE--ELNEH 473
|
490 500 510
....*....|....*....|....*....|....*
gi 74183796 556 HVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05915 474 LLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
107-589 |
4.62e-24 |
|
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: 105.47 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVagd 186
Cdd:cd17643 14 TYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevdavapdcsflkikllvsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSHCSLG 264
Cdd:cd17643 90 ------------------------------------------------TDPDDLAYVIYTSGSTGRPKgvVVSHANVLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKAkmdAASWTGLSTSDIIWTISDTA-----WimNILGAFL--------EPWVLGACIFVHLLPKFDSQTVLKvlssypi 331
Cdd:cd17643 122 FAA---TQRWFGFNEDDVWTLFHSYAfdfsvW--EIWGALLhggrlvvvPYEVARSPEDFARLLRDEGVTVLN------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 332 ntlvGAPIIYRMLLQQDLSSYKFPH-LHSCFSGGETLLPETLENWKAKTGL---EIREIYGQTETglicRVSRTMK-VKP 406
Cdd:cd17643 190 ----QTPSAFYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET----TVHVTFRpLDA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 GYL--------GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-FWLMGDRGIKD 477
Cdd:cd17643 262 ADLpaaaaspiGRPLPGLRVYVLDADGRPVPPGVVGELYVS-----GAGVARGYLGRPELTAERFVANpFGGPGSRMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 478 -------PEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflshdRDQLT 550
Cdd:cd17643 337 gdlarrlPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADI 411
|
490 500 510
....*....|....*....|....*....|....*....
gi 74183796 551 KVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17643 412 AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-583 |
5.79e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 103.62 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 315 PKFDSQTVLKVLSSYPIN--TLVG----APII--YRMLLQQDLSSykfphLHSCFSGGETLLPETLENW-KAKTGLEIRE 385
Cdd:cd05924 91 DRFDPEEVWRTIEKHKVTsmTIVGdamaRPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETG-LICRVSRTMKVKPGYLgtAFAHYDVQVIDEQGNVLPPGKE--GDIAIR-VKPIwpigmfsGYVDNPKKTQ- 460
Cdd:cd05924 166 AFGSSETGfTGSGHSAGSGPETGPF--TRANPDTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYGDEAKTAe 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 461 -----DNIRgdFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFV 535
Cdd:cd05924 237 tfpevDGVR--YAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVV 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74183796 536 VLAPEFlSHDRDQltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGK 583
Cdd:cd05924 315 QLREGA-GVDLEE----LREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
309-593 |
6.76e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 104.35 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 309 IFVHLLPKFdsqtVLKVLSSYPINTLVGAP----IIYRMLLQQDlssykfpHLHSCFSGGeTLLPET-LENWKAKTgLEI 383
Cdd:PRK08308 173 IITNKNPKF----ALNILRNTPQHILYAVPlmlhILGRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERT-TYM 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 384 REIYGQTETGLICrVSRTMKvKPGYLGTAFAHYDVQVIDEQGNvlpPGkegDIAIRVKpiwpigmfsgyvdnpkktQDNI 463
Cdd:PRK08308 240 MQQYGCSEAGCVS-ICPDMK-SHLDLGNPLPHVSVSAGSDENA---PE---EIVVKMG------------------DKEI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 464 RgdfwlMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFls 543
Cdd:PRK08308 294 F-----TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI-- 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74183796 544 hDRDQLTKVLQEHVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK08308 367 -DPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
83-591 |
1.98e-23 |
|
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: 103.78 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 83 EKAGKRSSGPALW-WmngsgkEIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPewWLM--ILGCMRTGLVFM 159
Cdd:cd05918 7 ERARSQPDAPAVCaW------DGSLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSK--WAVvaMLAVLKAGGAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 160 PgtiqMRSSDILYRLQaskaraivagdEVAQEVDAvapdcsflkiKLLVSensregwlnfkallkeastihqcveteSRE 239
Cdd:cd05918 78 P----LDPSHPLQRLQ-----------EILQDTGA----------KVVLT---------------------------SSP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 240 SAAIY--FTSGTSGPPK--MAEHSHCSLGIKAKMDAaswTGLSTSD-------IIWTISdtawIMNILGAflepWVLGAC 308
Cdd:cd05918 106 SDAAYviFTSGSTGKPKgvVIEHRALSTSALAHGRA---LGLTSESrvlqfasYTFDVS----ILEIFTT----LAAGGC 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 309 IFVhlLPKFDSQTVL-KVLSSYPINTLVGAPIIYRMLLQQDlssykFPHLHSCFSGGETLLPETLENWKAKTGLeiREIY 387
Cdd:cd05918 175 LCI--PSEEDRLNDLaGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTWADRVRL--INAY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 388 GQTETGLICRVSRTM-KVKPGYLGTAF---AHydvqVIDEQGN--VLPPGKEGDIAIRvKPIwpIGmfSGYVDNPKKTQD 461
Cdd:cd05918 246 GPAECTIAATVSPVVpSTDPRNIGRPLgatCW----VVDPDNHdrLVPIGAVGELLIE-GPI--LA--RGYLNDPEKTAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 462 N-IRGDFWLM-------------GDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAV---ISSPD 524
Cdd:cd05918 317 AfIEDPAWLKqegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKD 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 525 PSRGEVVKAFVVLAPEFLSHDRDQ------------LTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:cd05918 397 GSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
107-589 |
2.58e-23 |
|
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: 103.17 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgtiqmrssdilyrlqaskaraivagd 186
Cdd:cd12115 26 TYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqeVDAVAPdcsflkikllvsensregwlnfKALLKEASTIHQC--VETESRESAAIYFTSGTSGPPKMAEHSHCSLG 264
Cdd:cd12115 79 -----LDPAYP----------------------PERLRFILEDAQArlVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 -----IKAKMDAASWTG-LSTSDIIWTISdtawIMNILGaflePWVLGACIFVhllpkfdSQTVLkVLSSYP-------I 331
Cdd:cd12115 132 aflqwAAAAFSAEELAGvLASTSICFDLS----VFELFG----PLATGGKVVL-------ADNVL-ALPDLPaaaevtlI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 332 NTLvgaPIIYRMLLQQDlssyKFPHLHSCFS-GGETLLPETLENWKAKTGLE-IREIYGQTET---GLICRVSRTMKVKP 406
Cdd:cd12115 196 NTV---PSAAAELLRHD----ALPASVRVVNlAGEPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 GyLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIKDPE 479
Cdd:cd12115 269 S-IGRPLANTQAYVLDRALQPVPLGVPGELYIG-----GAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 480 GYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLShdrdqLTKVLQEHVKS 559
Cdd:cd12115 343 GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGT 417
|
490 500 510
....*....|....*....|....*....|
gi 74183796 560 VTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd12115 418 RLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
147-593 |
4.33e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 103.05 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 147 MI---LGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQEVDavapdcsflKIKLLVSENSREGWLnfkalL 223
Cdd:PRK04813 65 MLatfLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEIL---------GIPVITLDELKDIFA-----T 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 224 KEASTIHQCVETEsrESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtgLSTSDiiWTISDTA------W------ 291
Cdd:PRK04813 131 GNPYDFDHAVKGD--DNYYIIFTSGTTGKPKGVQISHDNL-------------VSFTN--WMLEDFAlpegpqFlnqapy 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 292 -----IMNILGAFlepwVLGACIFVhlLPK---FDSQTVLKVLSSYPINTLVGAPIIYRM-LLQQDLSSYKFPHL-HSCF 361
Cdd:PRK04813 194 sfdlsVMDLYPTL----ASGGTLVA--LPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLtHFLF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 362 SGgetllpETLENWKAKTGLE------IREIYGQTE-TGLICRVSRTMKVKPGY----LGTAFAHYDVQVIDEQGNVLPP 430
Cdd:PRK04813 268 CG------EELPHKTAKKLLErfpsatIYNTYGPTEaTVAVTSIEITDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 431 GKEGDIAIrvkpiwpIG--MFSGYVDNPKKTQ------DNIRgdFWLMGDRGIKDpEGYFHFIGRSDDIINSSGYRIGPS 502
Cdd:PRK04813 342 GEQGEIVI-------SGpsVSKGYLNNPEKTAeafftfDGQP--AYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 503 EVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEflSHDRD-QLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVT 581
Cdd:PRK04813 412 EIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEE--DFEREfELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPN 489
|
490
....*....|..
gi 74183796 582 GKIERAKLrAKE 593
Cdd:PRK04813 490 GKIDRKAL-IEE 500
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
107-590 |
5.99e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 102.91 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVV---LPRIPEWWLmilGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIV 183
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWY---GIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 AGDEVAQEVDAVAPDCSFLKIKLLVS------ENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAE 257
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTdaahmpQTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 258 HSHCSLGIKAKMDA-ASWTGLSTSDIIWTI----SDTAWIMnilgAFLEPWVlGACIfVHLLPKFDSQTVLKVLSSYPIN 332
Cdd:PRK06018 197 YSHRSNVLHALMANnGDALGTSAADTMLPVvplfHANSWGI----AFSAPSM-GTKL-VMPGAKLDGASVYELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVGAPIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLlPETLENWKAKTGLEIREIYGQTETGLICRVSrtmKVKPGYLGT 411
Cdd:PRK06018 271 FTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLGTLA---ALKPPFSKL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 412 ------------AFAHYDVQ--VIDEQGNVLPpgKEGDIAIRVKPIWPIgMFSGYVdnpkKTQDNIRGD--FWLMGDRGI 475
Cdd:PRK06018 347 pgdarldvlqkqGYPPFGVEmkITDDAGKELP--WDGKTFGRLKVRGPA-VAAAYY----RVDGEILDDdgFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 476 KDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEfLSHDRDQLTKVLQE 555
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG-ETATREEILKYMDG 498
|
490 500 510
....*....|....*....|....*....|....*
gi 74183796 556 HVksvtAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:PRK06018 499 KI----AKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
105-589 |
8.79e-23 |
|
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: 101.78 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVA 184
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaQEVDAVAPDCSFLKIKLLVSENSREGWLNFKallkeastihqcVETESRESAAIYFTSGTSGPPK--MAEHSHCS 262
Cdd:cd17656 92 -----QRHLKSKLSFNKSTILLEDPSISQEDTSNID------------YINNSDDLLYIIYTSGTTGKPKgvQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 LGIKAKMDaasWTGLSTSDIIW---TISDTAWIMNILGAFLEPWVLgacifvHLLP---KFDSQTVLKVLSSYPINTLvg 336
Cdd:cd17656 155 NLLHFERE---KTNINFSDKVLqfaTCSFDVCYQEIFSTLLSGGTL------YIIReetKRDVEQLFDLVKRHNIEVV-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 337 apIIYRMLLQQDLSSYKF-PHLHSC----FSGGETL-LPETLENWKAKTGLEIREIYGQTETGLI--CRVSRTMKVkPGY 408
Cdd:cd17656 224 --FLPVAFLKFIFSEREFiNRFPTCvkhiITAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVVttYTINPEAEI-PEL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 --LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGIKDPE 479
Cdd:cd17656 301 ppIGKPISNTWIYILDQEQQLQPQGIVGELYIS-----GASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 480 GYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LSHDRDQLTKVLQEhvk 558
Cdd:cd17656 376 GNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELnISQLREYLAKQLPE--- 452
|
490 500 510
....*....|....*....|....*....|.
gi 74183796 559 svtapYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17656 453 -----YMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
417-591 |
8.97e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 102.38 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 417 DVQVIDEQGNVLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQDNIRGD-FWLMGDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:PRK10946 364 EVWVADADGNPLPQGEVGRLMTR-------GpyTFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVGREKDQIN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 SSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLapeflshdRDQLTKV-LQEHVKSV-TAPYKYPRKVE 571
Cdd:PRK10946 437 RGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV--------KEPLKAVqLRRFLREQgIAEFKLPDRVE 508
|
170 180
....*....|....*....|
gi 74183796 572 FVLDLPKTVTGKIERAKLRA 591
Cdd:PRK10946 509 CVDSLPLTAVGKVDKKQLRQ 528
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
100-591 |
1.00e-22 |
|
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: 101.98 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 100 SGKEIKWSFRELSEASKQTANVLsGACGLHRGDRVAVVLPR----IPEWWlmilGCMRTGLVFMPGTIQMrssdiLYRLQ 175
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGL-RQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPP-----TYDEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 176 ASKAR------------AIVAGDEVAQEVDAVAPDCSFLKIKLLVSENsregwlnfkalLKEASTIHQCVETESRESAAI 243
Cdd:cd05906 104 NARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEE-----------LLDTAADHDLPQSRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 244 YFTSGTSGPPKMAEHSHCSlgIKAKMDAASWTGLSTSDIIwtisdtawIMNilgaflepWV----LGACIFVHLLPKF-D 318
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNGLTPQDV--------FLN--------WVpldhVGGLVELHLRAVYlG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 319 SQTV--------------LKVLSSYPInTLVGAP-IIYRMLLQQ---------DLSSYKFphlhsCFSGGETLLPETLEN 374
Cdd:cd05906 235 CQQVhvpteeiladplrwLDLIDRYRV-TITWAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 375 WK---AKTGLE---IREIYGQTET--GLI-CRVSRTMKVKPGY----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVK 441
Cdd:cd05906 309 LLrllEPYGLPpdaIRPAFGMTETcsGVIySRSFPTYDHSQALefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 442 PIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDpEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHP--AVSETA 518
Cdd:cd05906 389 VV-----TKGYYNNPEANAEAFTEDGWFrTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPgvEPSFTA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 519 VISSPDPSRGEVVKAfVVLAPEF-LSHDRDQLTKVLQEHVK---SVTAPYKYPRKVEfvlDLPKTVTGKIERAKLRA 591
Cdd:cd05906 463 AFAVRDPGAETEELA-IFFVPEYdLQDALSETLRAIRSVVSrevGVSPAYLIPLPKE---EIPKTSLGKIQRSKLKA 535
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
82-591 |
1.15e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.01 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 82 VEKAGKRSSGPALWWMNGSGKeikWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM-- 159
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADLR-AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVma 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 160 -----PGTIQmRSSDILYRLQASKARAIVAGDEVAQEVDAVAPdcsflkiklLVSENSREGWLNFKALLKEASTIHQcVE 234
Cdd:PRK05857 97 dgnlpIAAIE-RFCQITDPAAALVAPGSKMASSAVPEALHSIP---------VIAVDIAAVTRESEHSLDAASLAGN-AD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 235 TESRESAAIYFTSGTSGPPK---MAEHSHCSLGIKAKMDAASWtglstsdIIWTISDTAW----IMNILGAFlepWVL-- 305
Cdd:PRK05857 166 QGSEDPLAMIFTSGTTGEPKavlLANRTFFAVPDILQKEGLNW-------VTWVVGETTYsplpATHIGGLW---WILtc 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 ----GACIfvhlLPKFDSQTVLKVLSSYPINTLVGAP-IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAkTG 380
Cdd:PRK05857 236 lmhgGLCV----TGGENTTSLLEILTTNAVATTCLVPtLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 381 LEIREIYGQTETGLICRVSRT-----MKVKPGYLGTAFAHYDVQVIDEQGNVlPPGKEGDIAIRVKPIW---PIGMFsGY 452
Cdd:PRK05857 311 VRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDVYLAATDGIG-PTAPGAGPSASFGTLWiksPANML-GY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 453 VDNPKKTQDnIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVV 531
Cdd:PRK05857 389 WNNPERTAE-VLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALV 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 532 KAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK05857 468 GLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
233-586 |
3.67e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 100.97 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 233 VETESRESAAIYFTSGTSGPPKMAEHSHCS--LGIKAkmdaaSWTGLSTSD---IIWTISDTAWIMniLGAFLEPWVLGA 307
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPhlVGLKY-----YWRSIIEKDiptVVFSHSSIGWVS--FHGFLYGSLSLG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 308 CIFVH-----LLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD------LSSYKFPHLHSCFSGGETL---LPETLE 373
Cdd:PTZ00237 322 NTFVMfeggiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 374 NwkaKTGLEIREIYGQTETGLICRVSRTMKVKPGY-LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVkPIwPIGMFSGY 452
Cdd:PTZ00237 402 N---KLKIKSSRGYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PM-PPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 453 VDNP---KKTQDNIRGdFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGE 529
Cdd:PTZ00237 477 YKNDekfKQLFSKFPG-YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYN 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 530 VVKAFVVLAPEFLSH--DRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIER 586
Cdd:PTZ00237 556 VPIGLLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
107-568 |
6.38e-22 |
|
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: 99.67 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLV--FMPGTIqmRSSDILYRLQASKARAIVA 184
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPvaFLNTNI--RSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 GDEVAQEVDAVAPDCSFLKIKLLV--SENSREGWLNFKALLKEASTihQCVETESRE-----SAAIY-FTSGTSGPPKMA 256
Cdd:cd05938 85 APELQEAVEEVLPALRADGVSVWYlsHTSNTEGVISLLDKVDAASD--EPVPASLRAhvtikSPALYiYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 EHSHcsLGIKAKMDAASWTGLSTSDIIWTI----SDTAWIMNILGAFlepwVLGACIFvhLLPKFD-SQ----------T 321
Cdd:cd05938 163 RISH--LRVLQCSGFLSLCGVTADDVIYITlplyHSSGFLLGIGGCI----ELGATCV--LKPKFSaSQfwddcrkhnvT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VLKV---LSSYPINTlvgaPiiyrmllQQDLSSYKFPHLhscfSGGETLLPETLENWKAKTG-LEIREIYGQTE------ 391
Cdd:cd05938 235 VIQYigeLLRYLCNQ----P-------QSPNDRDHKVRL----AIGNGLRADVWREFLRRFGpIRIREFYGSTEgnigff 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 392 -----TGLICRVSRTMKVKPGYlgtAFAHYDVQ----VIDEQGNVLPPGKeGDIAIRVKPIWPIGMFSGYVDNPKKTQDN 462
Cdd:cd05938 300 nytgkIGAVGRVSYLYKLLFPF---ELIKFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKEQTEKK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 I------RGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPS-RGEVVKAF 534
Cdd:cd05938 376 LlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGhEGRIGMAA 455
|
490 500 510
....*....|....*....|....*....|....
gi 74183796 535 VVLAPEflsHDRDQltKVLQEHVKSVTAPYKYPR 568
Cdd:cd05938 456 VKLKPG---HEFDG--KKLYQHVREYLPAYARPR 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
107-600 |
9.31e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.25 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK12316 2030 SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQevdavapdcsflkiKLLVSENSREGWLNFKALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSHCSLGik 266
Cdd:PRK12316 2109 HLLE--------------RLPLPAGVARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV-- 2172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWT-GLSTSDIIWTISDTAWIMNILGAFlEPWVLGACIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLL 345
Cdd:PRK12316 2173 AHCQAAGERyELSPADCELQFMSFSFDGAHEQWF-HPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLA 2251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 346 QQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLE-IREIYGQTETGLICRVSRTMKVKPG-----YLGTAFAHYDVQ 419
Cdd:PRK12316 2252 EHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCgaayvPIGRALGNRRAY 2331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 420 VIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQ--------DNIRGDFWLMGDRGIKDPEGYFHFIGRSDDI 491
Cdd:PRK12316 2332 ILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQ 2406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 492 INSSGYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVlaPEFLSHDrdqLTKVLQEHVKSVTAPYKYPRKVE 571
Cdd:PRK12316 2407 VKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVV--PDDAAED---LLAELRAWLAARLPAYMVPAHWV 2480
|
490 500
....*....|....*....|....*....
gi 74183796 572 FVLDLPKTVTGKIERAKLRAKEWKTSGRA 600
Cdd:PRK12316 2481 VLERLPLNPNGKLDRKALPKPDVSQLRQA 2509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
233-589 |
1.62e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 233 VETESRESAAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLePWVLGACIFVH 312
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY-GLGVGDRVLQFTTFSFDVFVEELFW-PLMSGARVVLA 3268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 313 LLPKFDSQTVL-KVLSSYPINTLVGAPIIYRMLLQqDLSSYKFPHLHSCFSGGETLLPETLENWKAktGLEIREIYGQTE 391
Cdd:PRK12316 3269 GPEDWRDPALLvELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTE 3345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 392 TGLICRVSRTMKVKPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGDFWL 469
Cdd:PRK12316 3346 ATITVTHWQCVEEGKDAVpiGRPIANRACYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDPFV 3420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 470 MGDRGIKD-------PEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISspdpSRGEVVKAFVVlapefL 542
Cdd:PRK12316 3421 PGERLYRTgdlaryrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVV-----P 3491
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74183796 543 SHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:PRK12316 3492 EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
105-520 |
1.99e-19 |
|
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: 91.27 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 184
Cdd:cd17640 5 RITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcVETESRESAAIYFTSGTSGPPKMAEHSHCSLg 264
Cdd:cd17640 83 ------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANL- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 ikakmdaaswtgLSTSDIIWTISDTAwIMNILGAFLEPW---------VLGACIFVHLLPKFdsQTVLKVLSSYPINTLV 335
Cdd:cd17640 114 ------------LHQIRSLSDIVPPQ-PGDRFLSILPIWhsyersaeyFIFACGCSQAYTSI--RTLKDDLKRVKPHYIV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 336 GAPIIYRML---LQQDLSSYKFPH---LHSCFSGGETL--------LPETLENWKAKTGLEIREIYGQTETGLICRVSRT 401
Cdd:cd17640 179 SVPRLWESLysgIQKQVSKSSPIKqflFLFFLSGGIFKfgisgggaLPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 402 MKVKPGYLGTAFAHYDVQVIDEQGN-VLPPGKEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPE 479
Cdd:cd17640 259 KCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLGWLTCG 333
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 74183796 480 GYFHFIGRSDD-IINSSGYRIGPSEVENALMEHPAVSETAVI 520
Cdd:cd17640 334 GELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
241-589 |
1.21e-18 |
|
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: 89.03 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPK--MAEHS---HCSLGIKAKMdaaswtGLSTSDIIWTISDTAWIMNILGAFLEpWVLGACIFvhLLP 315
Cdd:cd17644 109 AYVIYTSGSTGKPKgvMIEHQslvNLSHGLIKEY------GITSSDRVLQFASIAFDVAAEEIYVT-LLSGATLV--LRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 316 K---FDSQTVLKVLSSYPInTLVGAPIIYRMLLQQDLSSYKFP---HLHSCFSGGETLLPETLENWKAKTGLEIR--EIY 387
Cdd:cd17644 180 EemrSSLEDFVQYIQQWQL-TVLSLPPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 388 GQTE---TGLICRVS--RTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDN 462
Cdd:cd17644 259 GPTEatiAATVCRLTqlTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPELTAEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 IRGD---------FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKA 533
Cdd:cd17644 334 FISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVA 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 74183796 534 FVVlaPEFlshDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17644 414 YIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-593 |
2.43e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAI 182
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VA----GDE--VAQEVDAVAPDcsflkikllvsensrEGWLNFKALLKEASTIHQCVEtesrESAAIYFTSGTSGPPKMA 256
Cdd:PRK12316 613 LSqshlGRKlpLAAGVQVLDLD---------------RPAAWLEGYSEENPGTELNPE----NLAYVIYTSGSTGKPKGA 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 EHSHCSLgiKAKMDAASWT-GLSTSDIIWTISDTAWIMNILGAFlepWVLGACIFVHLLPK---FDSQTVLKVLSSYPIN 332
Cdd:PRK12316 674 GNRHRAL--SNRLCWMQQAyGLGVGDTVLQKTPFSFDVSVWEFF---WPLMSGARLVVAAPgdhRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 333 TLVGAPIIYRMLLQqdlssykFPHLHSCFS------GGETL---LPETLENWKAKTGLeiREIYGQTETGL-ICRVSRTM 402
Cdd:PRK12316 749 TLHFVPSMLQAFLQ-------DEDVASCTSlrrivcSGEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdVTHWTCVE 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 403 KVKPGY-LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-------FWLMGDRG 474
Cdd:PRK12316 820 EGGDSVpIGRPIANLACYILDANLEPVPVGVLGELYLAGR-----GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLA 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 475 IKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISspdpSRGEVVKAFVVLAPEFLShdrdqLTKVLQ 554
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD-----WREALK 965
|
490 500 510
....*....|....*....|....*....|....*....
gi 74183796 555 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK12316 966 AHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPE 1004
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
107-600 |
2.48e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 89.33 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDAVaPDCSFLkikllvsensregwlNFKALLKEASTiHQCVETESRESAAIYFTSGTSGPPK--MAEHshcslg 264
Cdd:PRK10252 564 DQLPRFADV-PDLTSL---------------CYNAPLAPQGA-APLQLSQPHHTAYIIFTSGSTGRPKgvMVGQ------ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 iKAKMDAASWT----GLSTSDIIW-----TISDTAWimnilgAFLEPWVLGACIFV-----HLlpkfDSQTVLKVLSSYP 330
Cdd:PRK10252 621 -TAIVNRLLWMqnhyPLTADDVVLqktpcSFDVSVW------EFFWPFIAGAKLVMaepeaHR----DPLAMQQFFAEYG 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 331 INTLVGAPiiyRML------LQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTET----------GL 394
Cdd:PRK10252 690 VTTTHFVP---SMLaafvasLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAavdvswypafGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 395 ICRVSRTMKVKPGY--LGTAfahydVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD------ 466
Cdd:PRK10252 767 ELAAVRGSSVPIGYpvWNTG-----LRILDARMRPVPPGVAGDLYLT-----GIQLAQGYLGRPDLTASRFIADpfapge 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 467 -FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHP----AVSETAVISSPDPSRGEVVK--AFVVlAP 539
Cdd:PRK10252 837 rMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV-SQ 915
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74183796 540 EFLSHDRDqltkVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW--KTSGRA 600
Cdd:PRK10252 916 SGLPLDTS----ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELkaQVPGRA 974
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
107-589 |
3.67e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 87.52 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKAraivagd 186
Cdd:cd17650 14 TYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGA------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 evaqevdavapdcsflkiKLLVsensregwlnfkallkeastihqcveTESRESAAIYFTSGTSGPPK--MAEHSHCSLG 264
Cdd:cd17650 86 ------------------KLLL--------------------------TQPEDLAYVIYTSGTTGKPKgvMVEHRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 265 IKA-----KMDAASWTGLSTSDIIWTISdtawimniLGAFLEPWVLGACIFVhlLP---KFDSQTVLKVLSSYPINTLVG 336
Cdd:cd17650 122 AHAwrreyELDSFPVRLLQMASFSFDVF--------AGDFARSLLNGGTLVI--CPdevKLDPAALYDLILKSRITLMES 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 337 APIIYRMLLQQ-DLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREI--YGQTET-----------GLICRvSRTM 402
Cdd:cd17650 192 TPALIRPVMAYvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIInsYGVTEAtidstyyeegrDPLGD-SANV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 403 KVkpgylGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-------FWLMGDRGI 475
Cdd:cd17650 271 PI-----GRPLPNTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapgerMYRTGDLAR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 476 KDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDpSRGEVVKAFVVLAPEFLshDRDQLTKVLQE 555
Cdd:cd17650 341 WRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED-KGGEARLCAYVVAAATL--NTAELRAFLAK 417
|
490 500 510
....*....|....*....|....*....|....*
gi 74183796 556 HVKSVTAPYKYprkveFVLD-LPKTVTGKIERAKL 589
Cdd:cd17650 418 ELPSYMIPSYY-----VQLDaLPLTPNGKVDRRAL 447
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
105-590 |
4.22e-18 |
|
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: 87.48 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVa 184
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 185 gdevaqevdavapdcsflkikllvsensregwLNFKALLKEASTIHQ--CVETESRESAAIYFTSGTSGPPKMAEHSHcS 262
Cdd:cd05939 81 --------------------------------FNLLDPLLTQSSTEPpsQDDVNFRDKLFYIYTSGTTGLPKAAVIVH-S 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 263 LGIKAKMDAASWTGLSTSDIIWT---ISDTAwiMNILGaflepwvLGACIF----VHLLPKFDSQTVLKVLSSYpiNTLV 335
Cdd:cd05939 128 RYYRIAAGAYYAFGMRPEDVVYDclpLYHSA--GGIMG-------VGQALLhgstVVIRKKFSASNFWDDCVKY--NCTI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 336 GAPI--IYRMLLQQDLSSYKFPH-LHSCFSGGetLLPETLENWKAKTGL-EIREIYGQTE-----------TGLICRVSR 400
Cdd:cd05939 197 VQYIgeICRYLLAQPPSEEEQKHnVRLAVGNG--LRPQIWEQFVRRFGIpQIGEFYGATEgnsslvnidnhVGACGFNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 401 TmkvkPGYLgtafahYDVQVI-----------DEQGNVLP--PGKEGDIAIRVKPIWPIGMFSGYVD---NPKKTQDNI- 463
Cdd:cd05939 275 I----LPSV------YPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIARDVf 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 464 -RGD-FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSR-GEVVKAFVVLAPE 540
Cdd:cd05939 345 kKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAIVDPER 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 74183796 541 FLshDRDQLTKVLQehvkSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05939 425 KV--DLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
85-591 |
6.22e-18 |
|
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: 87.29 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 85 AGKRSSGPALWWMNGSGKEI-KWSFRELSEASKQTANVLSGACGlhRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPgTI 163
Cdd:cd05931 3 AAARPDRPAYTFLDDEGGREeTLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-LP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 164 QMRSSDILYRLQA----SKARAIVAGDEVAQEVDA-VAPDCSFLKIKLLVSE----NSREGWlnfkallkeastihQCVE 234
Cdd:cd05931 80 PPTPGRHAERLAAiladAGPRVVLTTAAALAAVRAfAASRPAAGTPRLLVVDllpdTSAADW--------------PPPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 235 TESRESAAIYFTSGTSGPPKMAEHSH------CSLGIKAKMDAASWTGLStsdiiwtisdtaWI-----MNILGAFLEPW 303
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHrnllanVRQIRRAYGLDPGDVVVS------------WLplyhdMGLIGGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 304 VLGACifVHLLP--KFDSQTV--LKVLSSYPInTLVGAP------IIYRMLLQQ----DLSSykfphLHSCFSGGETLLP 369
Cdd:cd05931 214 YSGGP--SVLMSpaAFLRRPLrwLRLISRYRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 370 ETLENWK---AKTGLE---IREIYGQTETGLI---------------------CRVSRTMKVKPGY-----LGTAFAHYD 417
Cdd:cd05931 286 ATLRRFAeafAPFGFRpeaFRPSYGLAEATLFvsggppgtgpvvlrvdrdalaGRAVAVAADDPAArelvsCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVIDEQGN-VLPPGKEGDIAIRvkpiwpiG--MFSGYVDNPKKTQ------DNIRGDFWL-MGDRGIKDpEGYFHFIGR 487
Cdd:cd05931 366 VRIVDPETGrELPDGEVGEIWVR-------GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 488 SDDIINSSGYRIGPSEVENALME-HPAVSET--AVISSPDPSRGEVvkafVVLAPEFLSHDRDQLTKVLQEHVKSVTAPY 564
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERL----VVVAEVERGADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|
gi 74183796 565 KY-PRKVEFVL--DLPKTVTGKIERAKLRA 591
Cdd:cd05931 514 GVaPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
344-590 |
6.54e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.59 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 344 LLQQDLSSYKfpHLHSCFSGGETLLPETLEnwKAKT-GLEIREIYGQTETGlicrvSRTMKVKPGylgtAFahydVQVID 422
Cdd:PRK07445 221 LLQLRPQWLA--QFRTILLGGAPAWPSLLE--QARQlQLRLAPTYGMTETA-----SQIATLKPD----DF----LAGNN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 423 EQGNVLP-------PGKEGDIAIRVKpiwpiGMFSGY----VDNPKktqdnirgdFWLMGDRGIKDPEGYFHFIGRSDDI 491
Cdd:PRK07445 284 SSGQVLPhaqitipANQTGNITIQAQ-----SLALGYypqiLDSQG---------IFETDDLGYLDAQGYLHILGRNSQK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 492 INSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRdqltkvLQEHVKSVTAPYKYPRKVE 571
Cdd:PRK07445 350 IITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEE------LKTAIKDQLSPFKQPKHWI 423
|
250
....*....|....*....
gi 74183796 572 FVLDLPKTVTGKIERAKLR 590
Cdd:PRK07445 424 PVPQLPRNPQGKINRQQLQ 442
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
105-590 |
1.95e-17 |
|
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: 85.10 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 105 KWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTI--QMRSSDILYRLQASKARAI 182
Cdd:cd05940 3 ALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 183 VAgdevaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesreSAAIY-FTSGTSGPPKMAEHSHC 261
Cdd:cd05940 80 VV-------------------------------------------------------DAALYiYTSGTTGLPKAAIISHR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 262 SLgIKAKMDAASWTGLSTSDIIWTI----SDTAwimNILGaflepwvLGACIF----VHLLPKFDSQTVLKVLSSYPINT 333
Cdd:cd05940 105 RA-WRGGAFFAGSGGALPSDVLYTClplyHSTA---LIVG-------WSACLAsgatLVIRKKFSASNFWDDIRKYQATI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 334 LVGAPIIYRMLLQQDLSSYKFPHLHSCFSGgETLLPETLENWKAKTGL-EIREIYGQTE-----------TGLICRVSRT 401
Cdd:cd05940 174 FQYIGELCRYLLNQPPKPTERKHKVRMIFG-NGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinffgkPGAIGRNPSL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 402 MKVKPGYlgtAFAHYDVQ----VIDEQGNV--LPPGKEGDIAIRVKPIWPigmFSGYVDnPKKTQDNI------RGDFW- 468
Cdd:cd05940 253 LRKVAPL---ALVKYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEP---FDGYTD-PAATEKKIlrdvfkKGDAWf 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 469 LMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDP-SRGEVVKAFVVLAPEflsHDRD 547
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN---EEFD 402
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 74183796 548 qLTKvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLR 590
Cdd:cd05940 403 -LSA-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
73-519 |
2.81e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.31 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 73 SDVIDHWASvekagKRSSGPALwwmNGSGKEIkwSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCM 152
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPAL---LFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 153 RTGLVF-MPGTiQMRSSDILYRLQASKARAIVAGDEVAQEVDAVAPDCS---FLKIKLLVSENSREGWLNFKALLKEAST 228
Cdd:PRK08279 109 KLGAVVaLLNT-QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLArppRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 229 ihQCVETESRESA---AIY-FTSGTSGPPKMAEHSH----CSLGIKAKMdaaswTGLSTSDIIW-----------TISDT 289
Cdd:PRK08279 188 --TNPASRSGVTAkdtAFYiYTSGTTGLPKAAVMSHmrwlKAMGGFGGL-----LRLTPDDVLYcclplyhntggTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 290 AWIMNilgaflepwvlGACIFvhLLPKFDSQTVLKVLSSYPInTLVGApI--IYRMLLQQDLSSYKFPH-LHSCFSGGet 366
Cdd:PRK08279 261 SVLAA-----------GATLA--LRRKFSASRFWDDVRRYRA-TAFQY-IgeLCRYLLNQPPKPTDRDHrLRLMIGNG-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 367 LLPETLENWKAKTGLE-IREIYGQTE--TGLI--CRVSRTMKVKPGYLGTAFA--HYDVQ----VIDEQGNVLP--PGKE 433
Cdd:PRK08279 324 LRPDIWDEFQQRFGIPrILEFYAASEgnVGFInvFNFDGTVGRVPLWLAHPYAivKYDVDtgepVRDADGRCIKvkPGEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 434 GDIAIRVKPIWPigmFSGYVDnPKKTQDNI------RGDFW-----LMGDrgikDPEGYFHFIGRSDDIINSSGYRIGPS 502
Cdd:PRK08279 404 GLLIGRITDRGP---FDGYTD-PEASEKKIlrdvfkKGDAWfntgdLMRD----DGFGHAQFVDRLGDTFRWKGENVATT 475
|
490
....*....|....*..
gi 74183796 503 EVENALMEHPAVSETAV 519
Cdd:PRK08279 476 EVENALSGFPGVEEAVV 492
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
67-584 |
5.54e-17 |
|
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: 84.63 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 67 AKFNFASDVIDHwasvekagKRSSGPALWWMNGSGKEIKWSFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEwwl 146
Cdd:cd05943 68 ARLNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPE--- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 147 MILGCMRT---GLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVA------------QEVDAVAPDcsfLKIKLLVSEN 211
Cdd:cd05943 136 AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrekvAELVKGLPS---LLAVVVVPYT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 212 SREGwlnfkalLKEASTIHQCV---ETESRESAA--------------IYFTSGTSGPPKMAEHSHCSLGIKAKMDAASW 274
Cdd:cd05943 213 VAAG-------QPDLSKIAKALtleDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAGGTLLQHLKEHILH 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 275 TGLSTSDIIWTISDTAWIM-NILGAFLepwVLGACIfvhLL----PKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQ-- 347
Cdd:cd05943 286 CDLRPGDRLFYYTTCGWMMwNWLVSGL---AVGATI---VLydgsPFYPDTNALWDLADEEGITVFGTSAKYLDALEKag 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 348 -------DLSSykfphLHSCFSGGETLLPETLE--NWKAKTGLEIREIYGQTE-TGLICRVSRTMKVKPGYLGTAFAHYD 417
Cdd:cd05943 360 lkpaethDLSS-----LRTILSTGSPLKPESFDyvYDHIKPDVLLASISGGTDiISCFVGGNPLLPVYRGEIQCRGLGMA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVIDEQGNVLPpGKEGDIAIrVKPI--WPIGmFSGYVDNPK--KTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:cd05943 435 VEAFDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWNDPDGSRyrAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLN 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 SSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFlshdrdQLTKVLQEHVKSVTA----PYKYPRK 569
Cdd:cd05943 512 PGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGV------ELDDELRKRIRSTIRsalsPRHVPAK 585
|
570
....*....|....*
gi 74183796 570 VEFVLDLPKTVTGKI 584
Cdd:cd05943 586 IIAVPDIPRTLSGKK 600
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
107-591 |
7.77e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.89 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAV-------VLPRIPEWWlmilgcMRTGLVFM-----PGT-IQMRSSDILYR 173
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLW------MRGASLTMlhqptPRTdLAVWAEDTLRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 174 LQASKARAIVAGDEVaqevDAVAPDCSFLKIK-LLVSEnsregwlnfkaLLKEASTihQCVETESRESAAIYFTSGTSGP 252
Cdd:PRK07768 104 IGMIGAKAVVVGEPF----LAAAPVLEEKGIRvLTVAD-----------LLAADPI--DPVETGEDDLALMQLTSGSTGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 253 PKMAEHSHCSL--GIKAKMDAASWTglSTSDIIwtISdtaWI-----MNILGAFLEPWVLGaCIFVHLLP-KFDSQTVL- 323
Cdd:PRK07768 167 PKAVQITHGNLyaNAEAMFVAAEFD--VETDVM--VS---WLplfhdMGMVGFLTVPMYFG-AELVKVTPmDFLRDPLLw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 324 -KVLSSYPiNTLVGAP-----IIYRMLLQQ------DLSSYKFphlhsCFSGGETLLPETLENW---KAKTGLE---IRE 385
Cdd:PRK07768 239 aELISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLldaGARFGLRpeaILP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 386 IYGQTETGL---ICRVSRTMKV------------------KPGY-----LGTAFAHYDVQVIDEQGNVLPPGKEGDIAIR 439
Cdd:PRK07768 313 AYGMAEATLavsFSPCGAGLVVdevdadllaalrravpatKGNTrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 440 VKPIWPigmfsGY--VDNPKKTQDNirgDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSE 516
Cdd:PRK07768 393 GESVTP-----GYltMDGFIPAQDA---DGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 517 --TAVISSPDPSRGEvvkAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKY-PRKVeFVL---DLPKTVTGKIERAKLR 590
Cdd:PRK07768 465 gnAVAVRLDAGHSRE---GFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKLRRANAA 540
|
.
gi 74183796 591 A 591
Cdd:PRK07768 541 E 541
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
107-556 |
5.57e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.10 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM---PGtiqMRSSDILYRLQASKARAIV 183
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 aGDEVAQEVDAVAPdCSFLKIKLLVSENSREGWLNF---KALLKEASTIHQCVETESRESAAIYFTSGTSGPPKMAEHSH 260
Cdd:PRK09274 119 -GIPKAHLARRLFG-WGKPSVRRLVTVGGRLLWGGTtlaTLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 261 CSLgiKAKMDA--ASWtGLSTSDIiwtisDTAwiMNILGAFLEPwVLGACifvHLLPKFD--------SQTVLKVLSSYP 330
Cdd:PRK09274 197 GMF--EAQIEAlrEDY-GIEPGEI-----DLP--TFPLFALFGP-ALGMT---SVIPDMDptrpatvdPAKLFAAIERYG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 331 INTLVGAPIIYRMLLQQDLSS-YKFPHLHSCFSGGETLLPETLENWKA--KTGLEIREIYGQTETGLICRV-SRTMKVK- 405
Cdd:PRK09274 263 VTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPISSIeSREILFAt 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 406 -------PGYL-GTAFAHYDVQVID---------EQGNVLPPGKEGDIAIRvkpiwpiG-MFS-GYVDNPKKTQDN---- 462
Cdd:PRK09274 343 raatdngAGICvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-------GpMVTrSYYNRPEATRLAkipd 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 IRGDFW-LMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPsrGEVVKAFVV-LAPE 540
Cdd:PRK09274 416 GQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVeLEPG 493
|
490
....*....|....*.
gi 74183796 541 fLSHDRDQLTKVLQEH 556
Cdd:PRK09274 494 -VACSKSALYQELRAL 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
241-598 |
9.29e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNIlGAFLEPWVLGACIFVHLLPKFDSQ 320
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQ-ERFLWTLICGGCLVVRDNDLWDPE 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 321 TVLKVLSSYPINTLVGAPIIYRMLLQ----QDLSSYKfphlHSCFsGGETLLPETLENWKAKtgLEIREI---YGQTETG 393
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPAYLQQFAEdaggADCASLD----IYVF-GGEAVPPAAFEQVKRK--LKPRGLtngYGPTEAV 3390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 394 LI-----CRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGD-F 467
Cdd:PRK12467 3391 VTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAERFVADpF 3465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 468 WLMGDRGIKD-------PEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSpDPSRGEVVKAFVVLAPE 540
Cdd:PRK12467 3466 SGSGGRLYRTgdlaryrADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADP 3544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 74183796 541 flshdRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEWKTSG 598
Cdd:PRK12467 3545 -----QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
103-589 |
1.68e-15 |
|
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: 78.98 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRiPEWWLM-ILGCMRTGLVFMPgtiqmrssdilyrlqaskara 181
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 182 ivagdevaqeVDAVAPDcsfLKIKLLVSEnsregwlnfkallkeasTIHQCVETESRESAAIYFTSGTSGPPK--MAEH- 258
Cdd:cd17648 68 ----------IDPSYPD---ERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHg 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 259 ----SHCSL----GIKAKMDAASwtgLSTSDIIWTISDTAWIMNILGaflepwvlGACIFVhlLP---KFDSQTVLKVLS 327
Cdd:cd17648 118 svvnLRTSLseryFGRDNGDEAV---LFFSNYVFDFFVEQMTLALLN--------GQKLVV--PPdemRFDPDRFYAYIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 328 SYPINTLVGAPiiyrMLLQQ-DLSSykFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKP 406
Cdd:cd17648 185 REKVTYLSGTP----SVLQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 --GYLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGY-----------VDNPKKT-QDNIRGDFWLM-- 470
Cdd:cd17648 259 fdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYlnrpeltaerfLPNPFQTeQERARGRNARLyk 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 471 -GDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGE--VVKAFV---VLAPEFLSh 544
Cdd:cd17648 334 tGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVgyyLPEPGHVP- 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 74183796 545 DRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17648 413 ESD-----LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-520 |
6.45e-15 |
|
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: 77.50 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSgACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTIQMRssdilyrlqaskaraiVAGD 186
Cdd:cd05910 4 SFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLIDPG----------------MGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEVDAVAPDcSFLKIkllvsensregwlnFKALlkeastihqcvetesrESAAIYFTSGTSGPPKMAEHSHCSLgiK 266
Cdd:cd05910 65 NLKQCLQEAEPD-AFIGI--------------PKAD----------------EPAAILFTSGSTGTPKGVVYRHGTF--A 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDA-ASWTGLSTSDIiwtisDTAWIMniLGAFLEPwVLGACIFV----HLLP-KFDSQTVLKVLSSYPINTLVGAPII 340
Cdd:cd05910 112 AQIDAlRQLYGIRPGEV-----DLATFP--LFALFGP-ALGLTSVIpdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 341 YRML----LQQDLssyKFPHLHSCFSGGETLLPETLENWKA--KTGLEIREIYGQTETGLIC-------RVSRTMKVKPG 407
Cdd:cd05910 184 LERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSsigsrelLATTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 408 Y---LGTAFAHYDVQVID---------EQGNVLPPGKEGDIAIRVKPIWPigmfsGYVDNPKKTQ----DNIRGDFW-LM 470
Cdd:cd05910 261 AgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTP-----TYVNRPVATAlakiDDNSEGFWhRM 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 74183796 471 GDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVI 520
Cdd:cd05910 336 GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
106-594 |
1.08e-14 |
|
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: 76.70 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 106 WSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVfmPGTIQ--MRSSDILYRLQASKARAIV 183
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 184 AGDEVaqevdavapdcsflkikllvsensregwlnfkallkeastihqcvetesrESAAIYfTSGTSGPPKMAehshcsl 263
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAA------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 264 gikakmdAASWTGLSTSDiiWTISDTAWIMNILGAFL-------EPWVLGACIFVH------LLPKFDSQTVLK--VLSS 328
Cdd:cd05937 106 -------AISWRRTLVTS--NLLSHDLNLKNGDRTYTcmplyhgTAAFLGACNCLMsggtlaLSRKFSASQFWKdvRDSG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 329 YPINTLVGAPIiyRMLLQQDLSSYKfpHLHSC-FSGGETLLPETLENWKAKTGL-EIREIYGQTETglicrVSRTMKVKP 406
Cdd:cd05937 177 ATIIQYVGELC--RYLLSTPPSPYD--RDHKVrVAWGNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 407 GYLGT-AFAHYD-------------VQVIDEQGNVL-----------PPGKEGDIAIRVkPIWPIGMFSGYVDNPKKTQD 461
Cdd:cd05937 248 GDFGAgAIGHHGlirrwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATES 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 462 NI------RGDFWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSR-GEVVKA 533
Cdd:cd05937 327 KLvrdvfrKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCA 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74183796 534 FVVLAPEflSHDRDQLTK-VLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKEW 594
Cdd:cd05937 407 AITLEES--SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
93-596 |
2.35e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 93 ALWWMNGSgkeikWSFRELSEASKQTANVLSGaCGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILY 172
Cdd:PRK05691 1149 ALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAY 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 173 RLQASKA------RAIVAGDEVAQEVDAVAPDcsflKIKLlvsensrEGWLNfkallkEASTIHqcveTESRESAAIYFT 246
Cdd:PRK05691 1223 MLADSGVellltqSHLLERLPQAEGVSAIALD----SLHL-------DSWPS------QAPGLH----LHGDNLAYVIYT 1281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 247 SGTSGPPKMAEHSHCSLGIKAKMDAASWtGLSTSDIIWTISDTAWIMNILGAFLePWVLGaCIFVHLLP--KFDSQTVLK 324
Cdd:PRK05691 1282 SGSTGQPKGVGNTHAALAERLQWMQATY-ALDDSDVLMQKAPISFDVSVWECFW-PLITG-CRLVLAGPgeHRDPQRIAE 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 325 VLSSYPINTLVGAPIIYRMLLQQDLSSyKFPHLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTETGL-----ICRV 398
Cdd:PRK05691 1359 LVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAInvthwQCQA 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 399 SRTMKVKpgyLGTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQDNIRGD--------FWLM 470
Cdd:PRK05691 1438 EDGERSP---IGRPLGNVLCRVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAERFVPDplgedgarLYRT 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 471 GDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEFLSHDRdqLT 550
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAER--LK 1587
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 74183796 551 KVLQEHVKSVTAPYKYPRkvefvLD-LPKTVTGKIERAKLRAKEWKT 596
Cdd:PRK05691 1588 AALAAELPEYMVPAQLIR-----LDqMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
471-591 |
3.75e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 74.31 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 471 GDRGIKDP-----EGYFH-------------FIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVK 532
Cdd:PRK07824 220 GYRNPVDPdpfaePGWFRtddlgalddgvltVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVV 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 533 AFVVLAPeflsHDRDQLTKvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK07824 300 AAVVGDG----GPAPTLEA-LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
67-584 |
2.63e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 72.91 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 67 AKFNFASDVIDHwasvekagKRSSGPALWWMNGSGKEIKWSFRELSEaskQTANVLSG--ACGLHRGDRVAVVLPRIPEW 144
Cdd:PRK03584 84 ARLNYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRR---QVAALAAAlrALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 145 WLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD---------EVAQEVDAVAPDCSFLKiKLLVSENSREG 215
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLE-HVVVVPYLGPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 216 wlNFKALLKEASTIHQCVETEsrESAAIYFT-------------SGTSGPPKMAEHSHCslGI-----KAK---MDaasw 274
Cdd:PRK03584 232 --AAAAALPGALLWEDFLAPA--EAAELEFEpvpfdhplwilysSGTTGLPKCIVHGHG--GIllehlKELglhCD---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 275 tgLSTSDIIWTISDTAWIM-NILGAFLepwVLGACIfvhLL----PKFDSQTVL-------KVlssypinTLVGA-PIIY 341
Cdd:PRK03584 302 --LGPGDRFFWYTTCGWMMwNWLVSGL---LVGATL---VLydgsPFYPDPNVLwdlaaeeGV-------TVFGTsAKYL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 342 RMLLQQDLS---SYKFPHLHSCFSGGETLLPETL----ENWKAktGLEIREIYGQTEtglICRV----SRTMKVKPG--- 407
Cdd:PRK03584 367 DACEKAGLVpgeTHDLSALRTIGSTGSPLPPEGFdwvyEHVKA--DVWLASISGGTD---ICSCfvggNPLLPVYRGeiq 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 408 --YLGTAfahydVQVIDEQGN-VLppGKEGDIAIRvKPI--WPIGmFSGYVDNPK------KTQDNIrgdfWLMGDRGIK 476
Cdd:PRK03584 442 crGLGMA-----VEAWDEDGRpVV--GEVGELVCT-KPFpsMPLG-FWNDPDGSRyrdayfDTFPGV----WRHGDWIEI 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 477 DPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVVLAPEF-LShdrDQLTKVLQE 555
Cdd:PRK03584 509 TEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVtLD---DALRARIRT 585
|
570 580
....*....|....*....|....*....
gi 74183796 556 HVKSVTAPYKYPRKVEFVLDLPKTVTGKI 584
Cdd:PRK03584 586 TIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
108-591 |
8.08e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 71.19 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 108 FRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQM----RSSDI--LYR-LQASKAR 180
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMgfggRESYIaqLRGmLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 181 AIVAGDEVAQEVDAVApdcsflkikllvsENSREGWLNFKALLK---EASTIHQCVETEsrESAAIYFTSGTSGPPK--- 254
Cdd:PRK09192 131 AIITPDELLPWVNEAT-------------HGNPLLHVLSHAWFKalpEADVALPRPTPD--DIAYLQYSSGSTRFPRgvi 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 255 ------MAE---HSHCSLGIKAKMDAASWTGLstsdiiwtISDtawiMNILGAFLEPwvLGACIFVHLLPKFD----SQT 321
Cdd:PRK09192 196 ithralMANlraISHDGLKVRPGDRCVSWLPF--------YHD----MGLVGFLLTP--VATQLSVDYLPTRDfarrPLQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 322 VLKVLSSYPiNTLVGAP-----IIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAK---TGLEIREI---YGQT 390
Cdd:PRK09192 262 WLDLISRNR-GTISYSPpfgyeLCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAfapAGFDDKAFmpsYGLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 391 ETGLICRVS------RTMKVKPGYL----------------------GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkp 442
Cdd:PRK09192 341 EATLAVSFSplgsgiVVEEVDRDRLeyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVR--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 443 iWPIGMfSGYVDNPKkTQDNIRGDFWL-MGDRGIKDpEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAV--SETAV 519
Cdd:PRK09192 418 -GPSLM-SGYFRDEE-SQDVLAADGWLdTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAA 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74183796 520 ISSPDPSrGEVVKAFV---VLAPEflshDRDQLTKVLQEHVKSVTApykYPRKVEFV--LDLPKTVTGKIERAKLRA 591
Cdd:PRK09192 494 FSIAQEN-GEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKAKK 562
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
107-589 |
1.37e-12 |
|
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: 70.19 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 107 SFRELSEASKQTANVLSGACGLHRGDrVAVVLPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGD 186
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERA-IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 187 EVAQEvdavapdcsflkiKLLVSENSRegwlNFKALLKEAStihqcvetesresAAIYFTSGTSGPPKMAEHSHCSlgIK 266
Cdd:cd17654 97 ELDNA-------------PLSFTPEHR----HFNIRTDECL-------------AYVIHTSGTTGTPKIVAVPHKC--IL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 267 AKMDAASWTGLSTSDIIWTIS-----DTAwIMNILGAFLEpwvlGAC-IFVHLLPKFDSQTVLKVLSSYPINTLVGA-PI 339
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTspltfDPS-VVEIFLSLSS----GATlLIVPTSVKVLPSKLADILFKRHRITVLQAtPT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 340 IYRMLLQQDLSSY---KFPHLHSCFSGGETLLPET-LENWKAK-TGLEIREIYGQTETgliCRVSRTMKVK----PGYLG 410
Cdd:cd17654 220 LFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSLViLSSWRGKgNRTRIFNIYGITEV---SCWALAYKVPeedsPVQLG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 411 TAFAHYDVQVIDEQGNvlppgkEGDIAIRVKPIWPIGMFSGYVDNPKktqdnirGDFWLMGDRgIKDPEGYFHFIGRSDD 490
Cdd:cd17654 297 SPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVPK-------GTMRATGDF-VTVKDGELFFLGRKDS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 491 IINSSGYRIGPSEVENALMEHPAVSETAVISSPDpsrgEVVKAFVVLAP-EFLSHDRDQLTKVlqehvksvtAPYKYPRK 569
Cdd:cd17654 363 QIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGESsSSRIHKELQLTLL---------SSHAIPDT 429
|
490 500
....*....|....*....|
gi 74183796 570 VEFVLDLPKTVTGKIERAKL 589
Cdd:cd17654 430 FVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
238-593 |
2.26e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 238 RESAAIYFTSGTSGPPK--MAEHS----HCSLGIKAkmdaaswTGLSTSDI---IWTIS-DTAwimniLGAFLEPWVLGA 307
Cdd:PRK05691 2333 QHQAYLIYTSGSTGKPKgvVVSHGeiamHCQAVIER-------FGMRADDCelhFYSINfDAA-----SERLLVPLLCGA 2400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 308 CIFVHLLPKFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIR-EI 386
Cdd:PRK05691 2401 RVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 387 YGQTET---GLICRVSRTMKVKPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQD 461
Cdd:PRK05691 2481 YGPTETvvmPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAE 2555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 462 NIRGD--------FWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKA 533
Cdd:PRK05691 2556 RFVADpfaadggrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGY 2635
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 534 FVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK05691 2636 LVSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD 2695
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
83-592 |
2.50e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 69.72 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 83 EKAGKRSSGPALWWMNGSGKEIKWSFRELSEASKQT---ANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFM 159
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELRSQVsrvANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 160 PGTIQMRSSDILYRLQASKARAIVAGDEV----------AQEVDAVAP-------DCSFLKIKLlvsensREG---WLNF 219
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplySRVVEAKAPkaivlpaDGKSVRVKL------REGdmsWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 220 KALLK------EASTIHQCVETESResaaIYFTSGTSGPPKMAEHSHCSlGIKAKMDAASWTGLSTSDIIwtisdtAWIM 293
Cdd:PLN03052 336 LARANglrrpdEYKAVEQPVEAFTN----ILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIV------CWPT 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 294 NiLGAFLEPWVL------GACI-FVHLLP------KF--DSQ-TVLKVLSSypintlvgapIIYRMLLQQDLSSYKFPHL 357
Cdd:PLN03052 405 N-LGWMMGPWLVyasllnGATLaLYNGSPlgrgfaKFvqDAKvTMLGTVPS----------IVKTWKNTNCMAGLDWSSI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 358 HSCFSGGETL-LPETLenW-KAKTGLE-IREIYGQTETGlICRVSRTMkVKPGYLG---TAFAHYDVQVIDEQGNVLPPG 431
Cdd:PLN03052 474 RCFGSTGEASsVDDYL--WlMSRAGYKpIIEYCGGTELG-GGFVTGSL-LQPQAFAafsTPAMGCKLFILDDSGNPYPDD 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 432 KEGDIAIRVKP----------------IWPIGMfsgyvdnPKKTQDNIRGDfwlmGDRGIKDPEGYFHFIGRSDDIINSS 495
Cdd:PLN03052 550 APCTGELALFPlmfgasstllnadhykVYFKGM-------PVFNGKILRRH----GDIFERTSGGYYRAHGRADDTMNLG 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 496 GYRIGPSEVE---NALmeHPAVSETAVISSPDPSRG--EVVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPYKYPRKV 570
Cdd:PLN03052 619 GIKVSSVEIErvcNAA--DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAV 696
|
570 580
....*....|....*....|..
gi 74183796 571 EFVLDLPKTVTGKIERAKLRAK 592
Cdd:PLN03052 697 VIVPSFPRTASNKVMRRVLRQQ 718
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
354-520 |
1.91e-11 |
|
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: 67.00 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 354 FPHLHSCFSGGETLLPETLENWkakTGLEIR--EIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVIDEQGNvlppg 431
Cdd:cd05933 319 LDRCQKFFTGAAPISRETLEFF---LSLNIPimELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD----- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 432 KEGDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDD-IINSSGYRIGPSEVENAL- 508
Cdd:cd05933 391 GIGEICFWGRHV-----FMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVk 465
|
170
....*....|..
gi 74183796 509 MEHPAVSETAVI 520
Cdd:cd05933 466 KELPIISNAMLI 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
239-590 |
3.59e-11 |
|
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: 65.59 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 239 ESAAIYFTSGTSGPPK--MAEHSHCSLGIKAKMDAASWTglsTSDIIWTISDTAWIMNILGAFLEPWVLGACIFVHLLPK 316
Cdd:cd05908 107 ELAFIQFSSGSTGDPKgvMLTHENLVHNMFAILNSTEWK---TKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 317 FDSQTV--LKVLSSYPINTLVGAPIIYRMLLQQ---------DLSsykfpHLHSCFSGGETLLPETLENWK---AKTGLE 382
Cdd:cd05908 184 FIRRPIlwLKKASEHKATIVSSPNFGYKYFLKTlkpekandwDLS-----SIRMILNGAEPIDYELCHEFLdhmSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 383 ---IREIYGQTETGL-ICRVSRTMKVKPGYL---------------------------GTAFAHYDVQVIDEQGNVLPPG 431
Cdd:cd05908 259 rnaILPVYGLAEASVgASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 432 KEGDIAIRVKPIWPigmfsGYVDNPKKTQDNIRGDFWLM-GDRG-IKDPEGYfhFIGRSDDIINSSGYRIGPSEVENALM 509
Cdd:cd05908 339 YIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLV--ITGREKDIIFVNGQNVYPHDIERIAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 510 EHPAVsetavisspdpSRGEVVKAFVvlapeFLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLD-------------- 575
Cdd:cd05908 412 ELEGV-----------ELGRVVACGV-----NNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNkrggwqinevlpir 475
|
410
....*....|....*.
gi 74183796 576 -LPKTVTGKIERAKLR 590
Cdd:cd05908 476 rIPKTTSGKVKRYELA 491
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
241-591 |
1.15e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.60 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHCSLgIKAKMDAASWTGLSTSDIIWTIsdtawimnilgaflepwvlgacifvhlLPKFDS- 319
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNL-LANRAQVAARIDFSPEDKVFNA---------------------------LPVFHSf 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 320 ----QTVLKVLSSYPInTLVGAPIIYR------------MLLQQD--LS-------SYKFPHLHSCFSGGETLLPETLEN 374
Cdd:PRK06814 848 gltgGLVLPLLSGVKV-FLYPSPLHYRiipeliydtnatILFGTDtfLNgyaryahPYDFRSLRYVFAGAEKVKEETRQT 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 375 WKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFA--HY---DVQVIDEQGNVLPPGkegdiairvkpiwPIGMf 449
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPgiEYrlePVPGIDEGGRLFVRG-------------PNVM- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 450 SGYV--DNPKKTQDNIRGdfWL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPS 526
Cdd:PRK06814 993 LGYLraENPGVLEPPADG--WYdTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDAR 1070
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74183796 527 RGEVvkafVVLapefLSHDRDQLTKVLQEHVKSVTAPYKY-PRKVEFVLDLPKTVTGKIERAKLRA 591
Cdd:PRK06814 1071 KGER----IIL----LTTASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
233-590 |
1.19e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 64.35 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 233 VETESRESAAIYFTSGTSGPPKMAEHSHCSLgikakmdaaswtgLSTSDIIWTISD-TA--WIMNILGAF---------L 300
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-------------LANVEQIKTIADfTPndRFMSALPLFhsfgltvglF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 301 EPWVLGACIFVhllpkfdsqtvlkvlssYPintlvgAPIIYRML--LQQD------------LSSY-KFPH------LHS 359
Cdd:PRK08043 427 TPLLTGAEVFL-----------------YP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 360 CFSGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID----EQGnvlppgkeGD 435
Cdd:PRK08043 484 VVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQG--------GR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 436 IAIRVKPIwpigmFSGY--VDNPKK----TQDNIRGDF---WL-MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVE 505
Cdd:PRK08043 556 LQLKGPNI-----MNGYlrVEKPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 506 N-ALMEHPAVSETAVISSpDPSRGEVVKAFVVLApeflSHDRDQLTKVLQEHVKSVTApykYPRKVEFVLDLPKTVTGKI 584
Cdd:PRK08043 631 QlALGVSPDKQHATAIKS-DASKGEALVLFTTDS----ELTREKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGKP 702
|
....*.
gi 74183796 585 ERAKLR 590
Cdd:PRK08043 703 DFVTLK 708
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
103-593 |
4.96e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 103 EIKWSFRELSEASKQTANVLSGAcGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP---GTIQMRSSDILyrlQASKA 179
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRT 3818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 180 RAIVAGDEVAQEVDAVAPDCS-FLKIKLLVSENSREGwlnfkallkEASTIHQCVETESRESAAIYFTSGTSGPPK--MA 256
Cdd:PRK05691 3819 PVLVCSAACREQARALLDELGcANRPRLLVWEEVQAG---------EVASHNPGIYSGPDNLAYVIYTSGSTGLPKgvMV 3889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 257 EHSHCslgIKAKMDAASWTGLSTSDIIWTISDTAWIMNILgAFLEPWVLGAciFVHLLPK---FDSQTVLKVLSSYPINT 333
Cdd:PRK05691 3890 EQRGM---LNNQLSKVPYLALSEADVIAQTASQSFDISVW-QFLAAPLFGA--RVEIVPNaiaHDPQGLLAHVQAQGITV 3963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 334 LVGAP-IIYRMLLQQDLSsykFPHLHSCFSGGETLLPETLENWKAK-TGLEIREIYGQTEtgliC-------RVSRTmKV 404
Cdd:PRK05691 3964 LESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAE----CsddvaffRVDLA-ST 4035
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 405 KPGYL--GTAFAHYDVQVIDEQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKTQ----DNIRGD----FWLMGDRG 474
Cdd:PRK05691 4036 RGSYLpiGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFGApgerLYRTGDLA 4110
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 475 IKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSrGEVVKAFVVLAPEFLSHdrDQLTKVLQ 554
Cdd:PRK05691 4111 RRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYLVPHQTVLAQ--GALLERIK 4187
|
490 500 510
....*....|....*....|....*....|....*....
gi 74183796 555 EHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKLRAKE 593
Cdd:PRK05691 4188 QRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALD 4226
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
241-593 |
6.38e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHcsLGIKAKMDAASwtglstsDIIWTISDTAwIMNIL---------GAFLEPWVLGACIFV 311
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSH--HNILSNIEQIS-------DVFNLRNDDV-ILSSLpffhsfgltVTLWLPLLEGIKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 312 HLLPkFDSQTVLKVLSSYPINTLVGAPIIYRMLLQQD-LSSYKFPHLHSCFSGGETLLPETLENWKAKTGLEIREIYGQT 390
Cdd:PRK08633 855 HPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 391 ETG----------LICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKEGDIAIRvkpiwPIGMFSGYVDNPKKT 459
Cdd:PRK08633 934 ETSpvasvnlpdvLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-----GPQVMKGYLGDPEKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 460 QDNIR---GDFW-LMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALmeHPAVSET----AVISSPDPSRGEVV 531
Cdd:PRK08633 1009 AEVIKdidGIGWyVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL 1086
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74183796 532 kafVVLapefLSHDRDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIE--RAKLRAKE 593
Cdd:PRK08633 1087 ---VVL----HTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDlkGLKELALA 1143
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
138-600 |
3.95e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 55.98 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 138 LPRIPEWWLMILGCMRTGLVFMPGTIQMRSSDILYRLQASKARAIVAGDEVAQE------VDAVAPDCSFLKIKLLVSEN 211
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 212 S-----REGWLNFKALLKEASTIHQCVETESRESAA-------IYFTSGTSGPPKMAEHSHCSlGIKAKMDAASWTGLST 279
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGSVGGNEYSPVYApvesvtnILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 280 SDIIWTISDTAWIMNilgaflePWVL------GACIFV-HLLP------KFDSQTVLKVLSSYPinTLVGApiiYRMLLQ 346
Cdd:PLN03051 160 GDVVCWPTNLGWMMG-------PWLLysaflnGATLALyGGAPlgrgfgKFVQDAGVTVLGLVP--SIVKA---WRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 347 QDLSSYKFPHLHSCFSGGETLLPET---LENWKAKTGlEIREIYGQTETGLICRVSRTMKVK-PGYLGTAFAHYDVQVID 422
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 423 EQGNVLPPGKE--GDIAIRVkpiwPIGMFSGYVDNpkKTQDNIRGDFWLM-----------GDRGIKDPEGYFHFIGRSD 489
Cdd:PLN03051 307 DNGVPYPDDQPcvGEVALAP----PMLGASDRLLN--ADHDKVYYKGMPMygskgmplrrhGDIMKRTPGGYFCVQGRAD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 490 DIINSSGYRIGPSEVENALME-HPAVSETAVISSPDPSRGE----VVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTAPY 564
Cdd:PLN03051 381 DTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPL 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 74183796 565 KYPRKVEFVLDLPKTVTGKIERAKLRAKEWK-TSGRA 600
Cdd:PLN03051 461 FKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRS 497
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
356-559 |
5.30e-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: 55.68 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 356 HLHSCFSGGETLLPETLEnWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID-EQGNVLPPGKE- 433
Cdd:cd17639 251 RLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYSTDKPPp 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 434 -GDIAIRVKPIwpigmFSGYVDNPKKTQDNIRGDFWLM-GDRGIKDPEGYFHFIGRSDDII-NSSGYRIGPSEVENALME 510
Cdd:cd17639 330 rGEILIRGPNV-----FKGYYKNPEKTKEAFDGDGWFHtGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRS 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74183796 511 HPAVSETAVISSPDPSRgevVKAFVVlaPeflshDRDQLTKVLQEHVKS 559
Cdd:cd17639 405 NPLVNNICVYADPDKSY---PVAIVV--P-----NEKHLTKLAEKHGVI 443
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
241-590 |
6.35e-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: 55.30 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 241 AAIYFTSGTSGPPKMAEHSHcslgikakmdaaswtglstSDIIWTISDTAWIMNILGAFLEPWVL--------------- 305
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTH-------------------GNIVSNVAGVFKILEILNKINPTDVYisylplahifervve 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 306 ------GACI-FVHLLPK--FDSQTVLK--VLSSYP----------INTLVGAPIIYRMLLQQdLSSYKFPHL------- 357
Cdd:cd05927 178 alflyhGAKIgFYSGDIRllLDDIKALKptVFPGVPrvlnriydkiFNKVQAKGPLKRKLFNF-ALNYKLAELrsgvvra 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 358 HSCF--------------------SGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYD 417
Cdd:cd05927 257 SPFWdklvfnkikqalggnvrlmlTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 418 VQVID--EQG-NVLPPGKEGDIAIRVKpiwpiGMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN 493
Cdd:cd05927 337 VKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKDPEKTAEALDEDGWLhTGDIGEWLPNGTLKIIDRKKNIFK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 494 -SSGYRIGPSEVENALMEHPAVSETAV-----------ISSPDP--------SRGEVVKAFVVLA--PEFLSHDRDQLTK 551
Cdd:cd05927 412 lSQGEYVAPEKIENIYARSPFVAQIFVygdslksflvaIVVPDPdvlkewaaSKGGGTGSFEELCknPEVKKAILEDLVR 491
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 74183796 552 VLQEH-VKSvtapYKYPRKVEFVLDLPK------TVTGKIERAKLR 590
Cdd:cd05927 492 LGKENgLKG----FEQVKAIHLEPEPFSvengllTPTFKLKRPQLK 533
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
409-590 |
9.06e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 409 LGTAFAHYDVQVIDEQGNVLPPGKE-GDIAIRvkpiwPIGMFSGYVDnpkktQDNIRGDFWL-MGDRGIKDPEGYFhFIG 486
Cdd:PRK05851 347 LGNPIPGMEVRISPGDGAAGVAGREiGEIEIR-----GASMMSGYLG-----QAPIDPDDWFpTGDLGYLVDGGLV-VCG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 487 RSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGevVKAFVVLAPEFLSHDRDQLTKVLQEHVKSVTApyKY 566
Cdd:PRK05851 416 RAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VV 491
|
170 180
....*....|....*....|....*.
gi 74183796 567 PRKVEFVL--DLPKTVTGKIERAKLR 590
Cdd:PRK05851 492 PSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
362-533 |
5.65e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.25 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 362 SGGETLLPETLENWKAKTGLEIREIYGQTETGLICRVSRTMKVKPGYLGTAFAHYDVQVID----EQGNVLPPGKEGDIA 437
Cdd:PLN02736 383 SGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemNYTSEDQPYPRGEIC 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 438 IRvKPIwpigMFSGYVDNPKKTQDNIRGDFWL-MGDRGIKDPEGYFHFIGRSDDIIN-SSGYRIGPSEVENALMEHPAVS 515
Cdd:PLN02736 463 VR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENVYAKCKFVA 537
|
170 180
....*....|....*....|....*....
gi 74183796 516 ETAV-----------ISSPDPsrgEVVKA 533
Cdd:PLN02736 538 QCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
429-594 |
9.09e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 45.58 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 429 PPgkEGDIAIRVKPiwpigMFSGYVDNPKKTQDNIRGDFWLMGDRGIKDPEGYFHFIGRSDDIIN-SSGYRIGPSEVENA 507
Cdd:PLN02430 463 PP--RGEICVRGKC-----LFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEYLENV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 508 LMEHPAVSETAVISspDPSRGEVVkAFVVLAPEFLSHDRDqltkvLQEHVKSVTAPYKYPRKVEFVLDLPKTVTgkiERA 587
Cdd:PLN02430 536 YGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEENTNKWAK-----DNGFTGSFEELCSLPELKEHILSELKSTA---EKN 604
|
....*..
gi 74183796 588 KLRAKEW 594
Cdd:PLN02430 605 KLRGFEY 611
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
463-589 |
1.57e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.43 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 463 IRGDFWLMGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSET------------AVIS--SPDPSRG 528
Cdd:cd17647 369 PRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKP 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74183796 529 EVVKAFVVLAPEFLSHDR--------DQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTVTGKIERAKL 589
Cdd:cd17647 449 DDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
452-589 |
9.29e-04 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 42.36 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 452 YVDN---PKKTQDNIRG--DFWL--------MGDRGIKDPEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETA 518
Cdd:TIGR03443 651 FVDPshwIDLDKENNKPerEFWLgprdrlyrTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENV 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 519 VISSPDPSRGEVVKAFVVLAP------EFLSHDRDQ---------------LTKVLQEHVKSVTAPYKYPrKVEFVLD-L 576
Cdd:TIGR03443 731 TLVRRDKDEEPTLVSYIVPQDksdeleEFKSEVDDEessdpvvkglikyrkLIKDIREYLKKKLPSYAIP-TVIVPLKkL 809
|
170
....*....|...
gi 74183796 577 PKTVTGKIERAKL 589
Cdd:TIGR03443 810 PLNPNGKVDKPAL 822
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
472-594 |
9.55e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 41.78 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 472 DRGIKDpEGYFHFIGRSDDIINSSGYRIGPSEVENALMEHPAVSETAVISSPDPSRGEVVKAFVvlapEFLShdrDQLTK 551
Cdd:PRK09029 338 DRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV----ESDS---EAAVV 409
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 74183796 552 VLQEHVKSVTAPYKYPrkVEFvLDLPKTV-TG--KIERAKLraKEW 594
Cdd:PRK09029 410 NLAEWLQDKLARFQQP--VAY-YLLPPELkNGgiKISRQAL--KEW 450
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
97-190 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74183796 97 MNGSGKEIK-WSFRELSEASKQTANVLSGACGLHRGDRVAVVLPRIPEWWLMILGCMRTGLVFMP--------------G 161
Cdd:cd05905 5 LDSKGKEATtLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPieppdisqqlgfllG 84
|
90 100 110
....*....|....*....|....*....|..
gi 74183796 162 TIQMR---SSDILYRLQASKARAIVAGDEVAQ 190
Cdd:cd05905 85 TCKVRvalTVEACLKGLPKKLLKSKTAAEIAK 116
|
|
| |
