|
Name |
Accession |
Description |
Interval |
E-value |
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
39-426 |
4.38e-20 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 92.38 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 39 EWNHITVAEFAAEVDRVAIFvmteLKARGIPPRSAVtVLYSGSRYQDLIYAIALARASYIPQMCPHILTHPGVIFALmEK 118
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAG----LRALGVGKGDRV-AILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYIL-ED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 119 AGSKIILYD-----PSLEPATTDCPYPKM-----ALNPIETIDSSSTINSDSALPTIEDLSSGHaDVCFFYLTSGSTsGS 188
Cdd:pfam00501 92 SGAKVLITDdalklEELLEALGKLEVVKLvlvldRDPVLKEEPLPEEAKPADVPPPPPPPPDPD-DLAYIIYTSGTT-GK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 189 PKVVPLTQKFVSTYYKTQFGIWLDGRRFDTQNAFLSRGS---ICAVAPIIqyFGCLYTGSCIVQPSKM-RFSTEELLTLV 264
Cdd:pfam00501 170 PKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPlfhDFGLSLGL--LGPLLAGATVVLPPGFpALDPAALLELI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 265 NVcglNRMTTFgtWLAP--HIQAAKKDPAALKLLQEMRTVSYGGVPISIADDDWCFQ-NGIPLMDMYATTECGTLMVSAP 341
Cdd:pfam00501 248 ER---YKVTVL--YGVPtlLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 342 GKPARFM------QPVPGISYR-FDPFTDTTTGADNPAStqllkliLLADSPQI-----PQPQL----LSEDGNFHTGDL 405
Cdd:pfam00501 323 PLDEDLRslgsvgRPLPGTEVKiVDDETGEPVPPGEPGE-------LCVRGPGVmkgylNDPELtaeaFDEDGWYRTGDL 395
|
410 420
....*....|....*....|.
gi 2203519039 406 FEKQLDGSYLFRGRGDDWIKS 426
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKL 416
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
174-519 |
4.83e-18 |
|
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: 85.41 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 174 DVCFFYLTSGSTsGSPKVVPLTQK-FVSTYYktqfgIWLDGRRFDTQNAFLSRGSICAVAPIIQYFGCLYTGSCIVQPSK 252
Cdd:cd04433 1 DPALILYTSGTT-GKPKGVVLSHRnLLAAAA-----ALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 253 mrFSTEELLTLVNvcgLNRMTTFGTW------LAPHIQAAKKDPAALkllqemRTVSYGGVPISIADDDWcFQN--GIPL 324
Cdd:cd04433 75 --FDPEAALELIE---REKVTILLGVptllarLLKAPESAGYDLSSL------RALVSGGAPLPPELLER-FEEapGIKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 325 MDMYATTECGTLMVSAPG-----KPARFMQPVPGISYR-FDPftDTTTGADNPASTQLLKlilladSPQIPQ-------- 390
Cdd:cd04433 143 VNGYGLTETGGTVATGPPdddarKPGSVGRPVPGVEVRiVDP--DGGELPPGEIGELVVR------GPSVMKgywnnpea 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 391 PQLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKS--------EdsrfidtkaIEEKINDVcsDLVKGCIVVGH----L 458
Cdd:cd04433 215 TAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSggenvypaE---------VEAVLLGH--PGVAEAAVVGVpdpeW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203519039 459 RPSPALFIEAyhDSISTISEDGLKELVLRRLEDFnarqlkheRITDKrlIFIVDEgnLPRT 519
Cdd:cd04433 284 GERVVAVVVL--RPGADLDAEELRAHVRERLAPY--------KVPRR--VVFVDA--LPRT 330
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
39-519 |
1.85e-17 |
|
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: 84.86 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 39 EWNHITVAEFAAEVDRVAifvmTELKARGIPPRSAVTVLY-SGSRYQDLIYAIALARASYIPqmCPHILTHPGVIFALmE 117
Cdd:COG0318 21 GGRRLTYAELDARARRLA----AALRALGVGPGDRVALLLpNSPEFVVAFLAALRAGAVVVP--LNPRLTAEELAYIL-E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 118 KAGSKIILYdpslepattdcpypkmalnpietidssstinsdsalptiedlssghADVCFfylTSGSTsGSPKVVPLTQK 197
Cdd:COG0318 94 DSGARALVT----------------------------------------------ALILY---TSGTT-GRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 198 FVSTYYkTQFGIWLDGRRFDTqnaflsrgsICAVAP-------IIQYFGCLYTGSCIVQPSkmRFSTEELLTLVNVCGLN 270
Cdd:COG0318 124 NLLANA-AAIAAALGLTPGDV---------VLVALPlfhvfglTVGLLAPLLAGATLVLLP--RFDPERVLELIERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 271 RMT---TFGTWLAPHIQAAKKDPAALkllqemRTVSYGGVPISIAD-DDWCFQNGIPLMDMYATTECGTLMVSAPGKPAR 346
Cdd:COG0318 192 VLFgvpTMLARLLRHPEFARYDLSSL------RLVVSGGAPLPPELlERFEERFGVRIVEGYGLTETSPVVTVNPEDPGE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 347 FM-----QPVPGISYR-FDPftdttTGADNPASTQLLkliLLADSPQIPQ-----PQLLSE---DGNFHTGDLFEKQLDG 412
Cdd:COG0318 266 RRpgsvgRPLPGVEVRiVDE-----DGRELPPGEVGE---IVVRGPNVMKgywndPEATAEafrDGWLRTGDLGRLDEDG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 413 SYLFRGRGDDWIKSEDSRfIDTKAIEEKINDVcsDLVKGCIVVGhlRPSP------ALFIEAYHDsiSTISEDGLKELVL 486
Cdd:COG0318 338 YLYIVGRKKDMIISGGEN-VYPAEVEEVLAAH--PGVAEAAVVG--VPDEkwgervVAFVVLRPG--AELDAEELRAFLR 410
|
490 500 510
....*....|....*....|....*....|...
gi 2203519039 487 RRLEdfnarqlKHERItdkRLIFIVDEgnLPRT 519
Cdd:COG0318 411 ERLA-------RYKVP---RRVEFVDE--LPRT 431
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
174-520 |
2.12e-13 |
|
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: 71.98 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 174 DVCFFYLTSGsTSGSPKVVPLTQKFVSTYYKTQfGIWLDGRRFDTQNAFLSRGSI-CAVAPIiqyFGCLYTGSCIVQPSK 252
Cdd:cd05972 82 DPALIYFTSG-TTGLPKGVLHTHSYPLGHIPTA-AYWLGLRPDDIHWNIADPGWAkGAWSSF---FGPWLLGATVFVYEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 253 MRFSTEELLTLVNVCGLNRMTTfgtwlAPHI--QAAKKDPAALKLLqEMRTVSYGGVP-----ISIADDDWcfqnGIPLM 325
Cdd:cd05972 157 PRFDAERILELLERYGVTSFCG-----PPTAyrMLIKQDLSSYKFS-HLRLVVSAGEPlnpevIEWWRAAT----GLPIR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 326 DMYATTECG-TLMVS--APGKPARFMQPVPGisYRFDpFTDTTTGADNPASTQLLKLilladspQIPQPQLLSE------ 396
Cdd:cd05972 227 DGYGQTETGlTVGNFpdMPVKPGSMGRPTPG--YDVA-IIDDDGRELPPGEEGDIAI-------KLPPPGLFLGyvgdpe 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 397 -------DGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSRfIDTKAIEEKIndVCSDLVKGCIVVGHLRPSPALFIEAY 469
Cdd:cd05972 297 kteasirGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR-IGPFEVESAL--LEHPAVAEAAVVGSPDPVRGEVVKAF 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2203519039 470 hdSISTISEDGLKELVlRRLEDFNARQL---KHERITDkrlifIVDEgnLPRTV 520
Cdd:cd05972 374 --VVLTSGYEPSEELA-EELQGHVKKVLapyKYPREIE-----FVEE--LPKTI 417
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
174-519 |
2.29e-11 |
|
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: 65.96 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 174 DVCFFYLTSGSTsGSPKVVPLTQKFVSTYYKTqFGIWLDGRRFDTQnaflsrgsICAVAPIIQYFGC-------LYTG-S 245
Cdd:cd05958 98 DICILAFTSGTT-GAPKATMHFHRDPLASADR-YAVNVLRLREDDR--------FVGSPPLAFTFGLggvllfpFGVGaS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 246 CIVQPskmRFSTEELLTLVnvcGLNRMTTFGTwlAPHIQAA---KKDPAALKLLQEMRTVSYGGVPISIADDDWCFQNGI 322
Cdd:cd05958 168 GVLLE---EATPDLLLSAI---ARYKPTVLFT--APTAYRAmlaHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 323 PLMDMYATTECGTLMVSA-PG--KPARFMQPVPGisYRFDPFTDttTGADNPASTQLLkliLLADSPQI------PQPQL 393
Cdd:cd05958 240 PIIDGIGSTEMFHIFISArPGdaRPGATGKPVPG--YEAKVVDD--EGNPVPDGTIGR---LAVRGPTGcryladKRQRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 394 LSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEdSRFIDTKAIEEKIndVCSDLVKGCIVVGHLRPSPALFIEAYhdsI 473
Cdd:cd05958 313 YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVL--LQHPAVAECAVVGHPDESRGVVVKAF---V 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2203519039 474 STISEDGLKELVLRRLEDFNARQL-KHERitdKRLIFIVDEgnLPRT 519
Cdd:cd05958 387 VLRPGVIPGPVLARELQDHAKAHIaPYKY---PRAIEFVTE--LPRT 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
42-519 |
8.06e-10 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 61.28 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 42 HITVAEFAAEVDRVAIFvmteLKARGIP---------PRS--------------AV-TVLYSGSRYQDLIYAIALARASy 97
Cdd:COG0365 39 TLTYAELRREVNRFANA----LRALGVKkgdrvaiylPNIpeaviamlacarigAVhSPVFPGFGAEALADRIEDAEAK- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 98 ipqmcpHILTHPGVIFalmekaGSKIILYDPSLEPATTDCPYPK---------MALNPIETIDSSSTINSDSALPTIEDL 168
Cdd:COG0365 114 ------VLITADGGLR------GGKVIDLKEKVDEALEELPSLEhvivvgrtgADVPMEGDLDWDELLAAASAEFEPEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 169 SSghADVCFFYLTSGSTsGSPKVVPLTQKFVSTYYKTQFGIWLDGRRFDTqnaflsrgsICAVAPI--------IQYFGc 240
Cdd:COG0365 182 DA--DDPLFILYTSGTT-GKPKGVVHTHGGYLVHAATTAKYVLDLKPGDV---------FWCTADIgwatghsyIVYGP- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 241 LYTGSCIV-QPSKMRFSTEEllTLVNVCGLNRMTTFGTwlAP---------HIQAAKK-DPAALKLLqemrtVSyGGVPI 309
Cdd:COG0365 249 LLNGATVVlYEGRPDFPDPG--RLWELIEKYGVTVFFT--APtairalmkaGDEPLKKyDLSSLRLL-----GS-AGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 310 SIADDDWCFQN-GIPLMDMYATTECGTLMVSAPG----KPARFMQPVPGISYR-FDPftdttTGADNPASTQ---LLKLi 380
Cdd:COG0365 319 NPEVWEWWYEAvGVPIVDGWGQTETGGIFISNLPglpvKPGSMGKPVPGYDVAvVDE-----DGNPVPPGEEgelVIKG- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 381 lladspqiPQPQLLSE----------------DGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSRfIDTKAIEEKINDV 444
Cdd:COG0365 393 --------PWPGMFRGywndperyretyfgrfPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHR-IGTAEIESALVSH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 445 csDLVKGCIVVGhlRP------SPALFI---EAYHDSISTISEdgLKELVLRRLEdfnarqlKHERItdkRLIFIVDEgn 515
Cdd:COG0365 464 --PAVAEAAVVG--VPdeirgqVVKAFVvlkPGVEPSDELAKE--LQAHVREELG-------PYAYP---REIEFVDE-- 525
|
....
gi 2203519039 516 LPRT 519
Cdd:COG0365 526 LPKT 529
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
44-502 |
9.68e-10 |
|
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: 60.95 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 44 TVAEFAAEVDRVAifvmTELKARGIPPRSAVTVLySGSRYQDLIYAIALARASYI---------PQMCPHILTHpgvifa 114
Cdd:cd05932 8 TWGEVADKARRLA----AALRALGLEPGSKIALI-SKNCAEWFITDLAIWMAGHIsvplyptlnPDTIRYVLEH------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 115 lmekAGSKII----LYD-PSLEPATTDCP--YPKMALNPIETIDSSSTINSDSAlPTIEDLSSGHADVCFFYLTSGSTsG 187
Cdd:cd05932 77 ----SESKALfvgkLDDwKAMAPGVPEGLisISLPPPSAANCQYQWDDLIAQHP-PLEERPTRFPEQLATLIYTSGTT-G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 188 SPKVVPLTqkFVSTYYKTQFGIwldgRRFDT--QNAFLSRGSICAVAPIIQYF-GCLYTGSCIvqpskmrFSTEELLTLV 264
Cdd:cd05932 151 QPKGVMLT--FGSFAWAAQAGI----EHIGTeeNDRMLSYLPLAHVTERVFVEgGSLYGGVLV-------AFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 265 NVCGLNRMTTFGT----WLAPHIQAAKKDPAA-----LKL----------------LQEMRTVSYGGVPISIADDDWCFQ 319
Cdd:cd05932 218 EDVQRARPTLFFSvprlWTKFQQGVQDKIPQQklnllLKIpvvnslvkrkvlkglgLDQCRLAGCGSAPVPPALLEWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 320 NGIPLMDMYATTE-CGTLMVSAPG--KPARFMQPVPGISYRFDPftdttTGAdnpastqllkliLLADSPQI-----PQP 391
Cdd:cd05932 298 LGLNILEAYGMTEnFAYSHLNYPGrdKIGTVGNAGPGVEVRISE-----DGE------------ILVRSPALmmgyyKDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 392 ----QLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSRFIDTKAIEEKIndVCSDLVKGCIVVGHLRPSPALFI- 466
Cdd:cd05932 361 eataEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL--AEHDRVEMVCVIGSGLPAPLALVv 438
|
490 500 510
....*....|....*....|....*....|....*...
gi 2203519039 467 --EAYHDSISTISEDGLKELVLRRLEDFNARQLKHERI 502
Cdd:cd05932 439 lsEEARLRADAFARAELEASLRAHLARVNSTLDSHEQL 476
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
173-519 |
1.33e-09 |
|
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: 60.17 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 173 ADVCFFYLTSGSTsGSPKVVPLTQK----FVSTYYKTQFGIWLDGRRFDTQNAFLSRGSICAVapiiqyFGCLYTG-SCI 247
Cdd:cd05919 91 DDIAYLLYSSGTT-GPPKGVMHAHRdpllFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSL------WFPLAVGaSAV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 248 VQPSkmRFSTEELL-TLVNvcglNRMTTFgtWLAPHIQAAKKDPAAL--KLLQEMRTVSYGG--VPISIADDdWCFQNGI 322
Cdd:cd05919 164 LNPG--WPTAERVLaTLAR----FRPTVL--YGVPTFYANLLDSCAGspDALRSLRLCVSAGeaLPRGLGER-WMEHFGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 323 PLMDMYATTECGTLMVSA-PG--KPARFMQPVPGISYRFDPFTDTTTGADNPAstqllklILLADSPQIP--------QP 391
Cdd:cd05919 235 PILDGIGATEVGHIFLSNrPGawRLGSTGRPVPGYEIRLVDEEGHTIPPGEEG-------DLLVRGPSAAvgywnnpeKS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 392 QLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKSeDSRFIDTKAIEEKINDVcsDLVKGCIVVGHLRPS----PALFIE 467
Cdd:cd05919 308 RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQH--PAVAEAAVVAVPESTglsrLTAFVV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2203519039 468 AYHDSIStisedglKELVLRRLEDFNARQLK-HERitdKRLIFIVDEgnLPRT 519
Cdd:cd05919 385 LKSPAAP-------QESLARDIHRHLLERLSaHKV---PRRIAFVDE--LPRT 425
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
47-426 |
3.90e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.78 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 47 EFAAEVDRVAifvmTELKARGIPPRSAVTVLySGSRYQDLIYAIALARASYIPQMCPHILThPGVIFALMEKAGSKIILY 126
Cdd:PRK05857 46 ELVAEVGGLA----ADLRAQSVSRGSRVLVI-SDNGPETYLSVLACAKLGAIAVMADGNLP-IAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 127 DPSLEPATTDCPYPKMALNPIETIDSSSTI----NSDSALPTIEdLSSGHADVCFFYLTSGSTsGSPKVVPLTQKfvsty 202
Cdd:PRK05857 120 APGSKMASSAVPEALHSIPVIAVDIAAVTResehSLDAASLAGN-ADQGSEDPLAMIFTSGTT-GEPKAVLLANR----- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 203 ykTQFGI----------WLDGRRFDTQNAFLSRGSICAVAPIIQyfGCLYTGSCIVqpskmrfSTEELLTLVNVCGLNRM 272
Cdd:PRK05857 193 --TFFAVpdilqkeglnWVTWVVGETTYSPLPATHIGGLWWILT--CLMHGGLCVT-------GGENTTSLLEILTTNAV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 273 TTfgTWLAPHIQAakKDPAALKL----LQEMRTVSYGGVPISIADDDWCFQNGIPLMDMYATTECGTLMVSAP---GKPA 345
Cdd:PRK05857 262 AT--TCLVPTLLS--KLVSELKSanatVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCLPtddGSIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 346 RFMQ-----PVPGIS-YRFDPFTDTTTGADNPASTQLLKLILLA--------DSPQIPQPQLLseDGNFHTGDLFEKQLD 411
Cdd:PRK05857 338 KIEAgavgrPYPGVDvYLAATDGIGPTAPGAGPSASFGTLWIKSpanmlgywNNPERTAEVLI--DGWVNTGDLLERRED 415
|
410
....*....|....*
gi 2203519039 412 GSYLFRGRGDDWIKS 426
Cdd:PRK05857 416 GFFYIKGRSSEMIIC 430
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
81-430 |
1.06e-07 |
|
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: 54.11 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 81 SRYQDLIYAIALARASYIPQMCPHILTHPGVIFALMeKAGSKIIlydpslePATTdcpypkmALNPIETIDSsstINSDS 160
Cdd:cd05974 11 SRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAM-KLGAVVI-------PATT-------LLTPDDLRDR---VDRGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 161 ALPTIEDLSSGHADVCFFYLTSGSTSgSPKVVPLTQK-----FVSTYYktqfgiWLDGRRFDTQNAFLSRGsiCAVAPII 235
Cdd:cd05974 73 AVYAAVDENTHADDPMLLYFTSGTTS-KPKLVEHTHRsypvgHLSTMY------WIGLKPGDVHWNISSPG--WAKHAWS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 236 QYFGCLYTGSCIVQPSKMRFSTEELLTLVNVCGLNRMTTFGTWLAPHIQAakkDPAALKLlqEMRTVSYGGVP-----IS 310
Cdd:cd05974 144 CFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ---DLASFDV--KLREVVGAGEPlnpevIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 311 IADDDWcfqnGIPLMDMYATTECGTLMVSAPG---KPARFMQPVPGisYR---FDPftdtttgADNPASTQLLKLILLAD 384
Cdd:cd05974 219 QVRRAW----GLTIRDGYGQTETTALVGNSPGqpvKAGSMGRPLPG--YRvalLDP-------DGAPATEGEVALDLGDT 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2203519039 385 SP------QIPQPQLLSE---DGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSR 430
Cdd:cd05974 286 RPvglmkgYAGDPDKTAHamrGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR 340
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
104-519 |
1.34e-07 |
|
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: 54.14 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 104 HILTHPGVIFALMEKA-----GSKIILYDPSLEPATtdcpypkmalnPIETIDSSSTINSDSALPTIEDLssGHADVCFF 178
Cdd:cd05911 85 VIFTDPDGLEKVKEAAkelgpKDKIIVLDDKPDGVL-----------SIEDLLSPTLGEEDEDLPPPLKD--GKDDTAAI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 179 YLTSGsTSGSPKVVPLTQK-FVSTYYKTQFGIWLDGRRFDTQNAFLSRGSICAVapIIQYFGCLYTGSCIVQPskmRFST 257
Cdd:cd05911 152 LYSSG-TTGLPKGVCLSHRnLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGL--FTTLASLLNGATVIIMP---KFDS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 258 EELLTLVNvcglNRMTTFgTWLAPHIQAA-KKDPAALKL-LQEMRTVSYGGVPIS--------IADDDWCFQNGiplmdm 327
Cdd:cd05911 226 ELFLDLIE----KYKITF-LYLVPPIAAAlAKSPLLDKYdLSSLRVILSGGAPLSkelqellaKRFPNATIKQG------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 328 YATTECGTLMVSAPGKPARFM---QPVPGISYRF-DPFTDTTTGADNPAstqllklILLADSPQI-------PQP--QLL 394
Cdd:cd05911 295 YGMTETGGILTVNPDGDDKPGsvgRLLPNVEAKIvDDDGKDSLGPNEPG-------EICVRGPQVmkgyynnPEAtkETF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 395 SEDGNFHTGDL--FEKqlDGSYLFRGRGDDWIK--------SEdsrfidtkaIEE------KINDVC---------SDLV 449
Cdd:cd05911 368 DEDGWLHTGDIgyFDE--DGYLYIVDRKKELIKykgfqvapAE---------LEAvllehpGVADAAvigipdevsGELP 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203519039 450 KGCIVvghLRPSPalfieayhdsisTISEDGLKELVLRRLEDFnarqlkheritdKRL---IFIVDEgnLPRT 519
Cdd:cd05911 437 RAYVV---RKPGE------------KLTEKEVKDYVAKKVASY------------KQLrggVVFVDE--IPKS 480
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
289-456 |
3.68e-07 |
|
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: 51.95 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 289 DPAALKLLqemRTVSYGGVPISIADDDWCFQNGIPLMDMYATTECGTlMVSApGKPARFM-----QPVPGISYRFDPftd 363
Cdd:cd17630 106 GPAALKSL---RAVLLGGAPIPPELLERAADRGIPLYTTYGMTETAS-QVAT-KRPDGFGrggvgVLLPGRELRIVE--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 364 ttTGADNPASTQLLKLILLADSPQipqpqLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKS--EDsrfIDTKAIEEKI 441
Cdd:cd17630 178 --DGEIWVGGASLAMGYLRGQLVP-----EFNEDGWFTTKDLGELHADGRLTVLGRADNMIISggEN---IQPEEIEAAL 247
|
170
....*....|....*
gi 2203519039 442 NDVcsDLVKGCIVVG 456
Cdd:cd17630 248 AAH--PAVRDAFVVG 260
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
38-513 |
5.18e-07 |
|
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: 52.21 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 38 QEWNHITVAEFAAEVDRVAIfvmtELKARGIPPRSAVtVLYSGSRYQDLI--YAIALARASYIP-------QMCPHILTH 108
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAK----GLIALGVEPGDRV-AILSRNRPEWTIadLAILAIGAVPVPiyptssaEQIAYILND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 109 pgvifalmekAGSKIILydpslepattdcpypkmalnpIETIDSSSTINsdsalptiedlssghadvcffYlTSGSTsGS 188
Cdd:cd05907 76 ----------SEAKALF---------------------VEDPDDLATII---------------------Y-TSGTT-GR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 189 PKVVPLTQK-FVSTYYKTqfgiwLDGRRFDTQNAFLSRGSICAV-APIIQYFGCLYTGSCIVQPSKMRFSTEELLTLvnv 266
Cdd:cd05907 102 PKGVMLSHRnILSNALAL-----AERLPATEGDRHLSFLPLAHVfERRAGLYVPLLAGARIYFASSAETLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 267 cglnRMTTFgtwLA------PHIQAAK--KDPAALKLL------QEMRTVSYGGVPISIADDDWCFQNGIPLMDMYATTE 332
Cdd:cd05907 174 ----RPTVF---LAvprvweKVYAAIKvkAVPGLKRKLfdlavgGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 333 C-GTLMVSAPGKPaRFM---QPVPGISYRFDPftdtttgaDNpastqllklILLADSPQI-------PQP--QLLSEDGN 399
Cdd:cd05907 247 TsAVVTLNPPGDN-RIGtvgKPLPGVEVRIAD--------DG---------EILVRGPNVmlgyyknPEAtaEALDADGW 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 400 FHTGDLFEKQLDGsYLF-RGRGDDWIKSEDSRFIDTKAIEEKINDvcSDLVKGCIVVGHLRPSPALFI------------ 466
Cdd:cd05907 309 LHTGDLGEIDEDG-FLHiTGRKKDLIITSGGKNISPEPIENALKA--SPLISQAVVIGDGRPFLVALIvpdpealeawae 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2203519039 467 ---EAYHDSISTISEDGLKELVLRRLEDFNARQLKHERItdKRLIFIVDE 513
Cdd:cd05907 386 ehgIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQI--KKFLLLPEP 433
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
44-430 |
1.17e-06 |
|
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: 50.96 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 44 TVAEFAAEVDRVAifvmTELKARGIPPRSAVTVLysGSRYQDLiYAIALARASYIPQMCPHILTH-PGVIFALMEKAGSK 122
Cdd:cd05969 2 TFAQLKVLSARFA----NVLKSLGVGKGDRVFVL--SPRSPEL-YFSMLGIGKIGAVICPLFSAFgPEAIRDRLENSEAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 123 IILYDPSLepattdcpYPKMalnpietidssstinsdsalpTIEDLSsghadvcFFYLTSGSTsGSPKVVPLTQKFVSTY 202
Cdd:cd05969 75 VLITTEEL--------YERT---------------------DPEDPT-------LLHYTSGTT-GTPKGVLHVHDAMIFY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 203 YKT---QFGIWLDGRRFDTQNAFLSRGSICAV-APIIQyfgclytgSCIVQPSKMRFSTEELLTLVNVCGLNRMTTfgtw 278
Cdd:cd05969 118 YFTgkyVLDLHPDDIYWCTADPGWVTGTVYGIwAPWLN--------GVTNVVYEGRFDAESWYGIIERVKVTVWYT---- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 279 lAP-HIQAAKK---DPAALKLLQEMRTVSYGGVPISIADDDWCFQN-GIPLMDMYATTECGTLMV----SAPGKPARFMQ 349
Cdd:cd05969 186 -APtAIRMLMKegdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVfGVPIHDTWWQTETGSIMIanypCMPIKPGSMGK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 350 PVPG-----ISYRFDPFTDTTTGadnpastqllKLILLADSPQIPQPQLLSE--------DGNFHTGDLFEKQLDGSYLF 416
Cdd:cd05969 265 PLPGvkaavVDENGNELPPGTKG----------ILALKPGWPSMFRGIWNDEeryknsfiDGWYLTGDLAYRDEDGYFWF 334
|
410
....*....|....
gi 2203519039 417 RGRGDDWIKSEDSR 430
Cdd:cd05969 335 VGRADDIIKTSGHR 348
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4-513 |
1.26e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 51.25 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 4 ALEDNHIA-LLQHRAKNSGNTVLFKLPilrgsePPQEWNHITVAEFAAEVDRVAIFvmteLKARGIPPRSAVtVLYSGSR 82
Cdd:COG1022 7 VPPADTLPdLLRRRAARFPDRVALREK------EDGIWQSLTWAEFAERVRALAAG----LLALGVKPGDRV-AILSDNR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 83 YQDLI--YAIALARASYIP--------QMcPHILTHPGVIFALMEKAGskiiLYDpSLEPATTDCPypkmALNPIETIDs 152
Cdd:COG1022 76 PEWVIadLAILAAGAVTVPiyptssaeEV-AYILNDSGAKVLFVEDQE----QLD-KLLEVRDELP----SLRHIVVLD- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 153 SSTINSDSALPTIEDL------------------SSGHADVCFFYLTSGSTsGSPKVVPLTQK-FVStyyktQFGIWLDG 213
Cdd:COG1022 145 PRGLRDDPRLLSLDELlalgrevadpaelearraAVKPDDLATIIYTSGTT-GRPKGVMLTHRnLLS-----NARALLER 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 214 RRFDTQNAFLS---------RgsicavapIIQYFgCLYTGSCI---------------VQPSKMrFST----EELLTLVN 265
Cdd:COG1022 219 LPLGPGDRTLSflplahvfeR--------TVSYY-ALAAGATVafaespdtlaedlreVKPTFM-LAVprvwEKVYAGIQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 266 VcGLNRMTTFGTWL-----------APHIQAAKKDPAALKL------------LQE-----MRTVSYGGVPISiADDDWC 317
Cdd:COG1022 289 A-KAEEAGGLKRKLfrwalavgrryARARLAGKSPSLLLRLkhaladklvfskLREalggrLRFAVSGGAALG-PELARF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 318 FQN-GIPLMDMYATTE-CGTLMVSAPGKPaRFM---QPVPGISYRFdpftdtttGAD----------------NPASTQl 376
Cdd:COG1022 367 FRAlGIPVLEGYGLTEtSPVITVNRPGDN-RIGtvgPPLPGVEVKI--------AEDgeilvrgpnvmkgyykNPEATA- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 377 lklilladspqipqpQLLSEDGNFHTGDLFEKQLDGsYLF-RGRGDDWIKSEDSRFIDTKAIEEKINDvcSDLVKGCIVV 455
Cdd:COG1022 437 ---------------EAFDADGWLHTGDIGELDEDG-FLRiTGRKKDLIVTSGGKNVAPQPIENALKA--SPLIEQAVVV 498
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203519039 456 GHLRPSPALFI----EA-----------YHDSISTISEDGLKELVLRRLEDFNARQLKHERItdKRLIFIVDE 513
Cdd:COG1022 499 GDGRPFLAALIvpdfEAlgewaeenglpYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQI--KRFRLLPKE 569
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
290-489 |
7.23e-06 |
|
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: 48.28 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 290 PAALKLlqEMRTVSYGGVPISIADDDWCFQN-GIPLMDMYATTECGTLMVS--APGKPAR---FMQPVPGisYRFDPFTD 363
Cdd:cd05973 200 PARPKG--RLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhALEHPVHagsAGRAMPG--WRVAVLDD 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 364 TTtgaDNPASTQLLKL-ILLADSP--------QIPQPqllSEDGNFH-TGDLFEKQLDGSYLFRGRGDDWIKSE------ 427
Cdd:cd05973 276 DG---DELGPGEPGRLaIDIANSPlmwfrgyqLPDTP---AIDGGYYlTGDTVEFDPDGSFSFIGRADDVITMSgyrigp 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203519039 428 ---DSRFIDTKAIEE-----KINDVCSDLVKGCIVV--GHlRPSPALfieayhdsistisEDGLKELVLRRL 489
Cdd:cd05973 350 fdvESALIEHPAVAEaavigVPDPERTEVVKAFVVLrgGH-EGTPAL-------------ADELQLHVKKRL 407
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
43-256 |
1.29e-05 |
|
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: 47.69 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 43 ITVAEFAAEVDRVAIFvmteLKARGIPPRSAVTV-LYSGSRYQDLIYAIALARA---------------SYIPQMCPHIL 106
Cdd:cd05926 15 LTYADLAELVDDLARQ----LAALGIKKGDRVAIaLPNGLEFVVAFLAAARAGAvvaplnpaykkaefeFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 107 THPGVIFALMEKAGSKIILY--DPSLEPATTDcpypkmalnpieTIDSSSTINSDSALPTiEDLSSGHA---DVCFFYLT 181
Cdd:cd05926 91 LTPKGELGPASRAASKLGLAilELALDVGVLI------------RAPSAESLSNLLADKK-NAKSEGVPlpdDLALILHT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203519039 182 SGSTsGSPKVVPLTQKFV---STYYKTQFGIWLDGRRFDTQNAFLSRGSICAVAPIiqyfgcLYTGSCIVQPskMRFS 256
Cdd:cd05926 158 SGTT-GRPKGVPLTHRNLaasATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLST------LAAGGSVVLP--PRFS 226
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
321-505 |
4.76e-05 |
|
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: 45.90 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 321 GIPLMDMYATTECGTLMVSAPgkPARFM-----QPVPGISYRFD-PFTDTTTGA-------------DNPASTQllklil 381
Cdd:cd05914 258 GFPYTIGYGMTETAPIISYSP--PNRIRlgsagKVIDGVEVRIDsPDPATGEGEiivrgpnvmkgyyKNPEATA------ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 382 ladspqipqpQLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSRFIDTKAIEEKINDVCSDLVKgCIVVGHlrps 461
Cdd:cd05914 330 ----------EAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLES-LVVVQE---- 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2203519039 462 palfieayhdsistisedglKELVLRRLEDFNARQLKHERITDK 505
Cdd:cd05914 395 --------------------KKLVALAYIDPDFLDVKALKQRNI 418
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
35-197 |
4.63e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 42.80 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 35 EPPQEWNHITVAEFAAEVDRVAIFvmteLKARGIPPRSAVTVLySGSRYQDLIYAIAlARASYIPQmCP----------- 103
Cdd:cd05921 18 EGNGGWRRVTYAEALRQVRAIAQG----LLDLGLSAERPLLIL-SGNSIEHALMALA-AMYAGVPA-APvspayslmsqd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 104 -----HI--LTHPGVIFA----LMEKAGSKIILYDPSLEPATTDCPYPKMALNPiETIDSSSTINSDSALPTIedlssGH 172
Cdd:cd05921 91 laklkHLfeLLKPGLVFAqdaaPFARALAAIFPLGTPLVVSRNAVAGRGAISFA-ELAATPPTAAVDAAFAAV-----GP 164
|
170 180
....*....|....*....|....*
gi 2203519039 173 ADVCFFYLTSGSTsGSPKVVPLTQK 197
Cdd:cd05921 165 DTVAKFLFTSGST-GLPKAVINTQR 188
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
42-416 |
1.49e-03 |
|
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: 41.07 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 42 HITVAEFAAEVDRVAifvmTELKARGIPPRSAVTVLYSGSRYQDLIYAIALARASYIPQMCPhiLTHPGVIFALMEKAGS 121
Cdd:cd05904 32 ALTYAELERRVRRLA----AGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP--LSTPAEIAKQVKDSGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 122 KIILYDPSLEPATTDCPYPKMALNPIE----TIDSSSTINSDSALPTIEDLSSghaDVCFFYLTSGsTSGSPKVVPLTQK 197
Cdd:cd05904 106 KLAFTTAELAEKLASLALPVVLLDSAEfdslSFSDLLFEADEAEPPVVVIKQD---DVAALLYSSG-TTGRSKGVMLTHR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 198 -FVSTyykTQFGIWLDGRRFDTQNAFLsrgsicAVAPIIQYFG---CLYT----GSCIVQPSkmRFSTEELLTLVNVCGL 269
Cdd:cd05904 182 nLIAM---VAQFVAGEGSNSDSEDVFL------CVLPMFHIYGlssFALGllrlGATVVVMP--RFDLEELLAAIERYKV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 270 NRMttfgtWLAPHIQAA-KKDPAALKL-LQEMRTVSYGGVPISIADDDWCFQN--GIPLMDMYATTE--CGTLMVSAPGK 343
Cdd:cd05904 251 THL-----PVVPPIVLAlVKSPIVDKYdLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTEstGVVAMCFAPEK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 344 -PARfmqpvPGISYRFDP-----FTDTTTGADNPASTQ---LLKlilladSPQIPQPQL---------LSEDGNFHTGDL 405
Cdd:cd05904 326 dRAK-----YGSVGRLVPnveakIVDPETGESLPPNQTgelWIR------GPSIMKGYLnnpeataatIDKEGWLHTGDL 394
|
410
....*....|.
gi 2203519039 406 FEKQLDGsYLF 416
Cdd:cd05904 395 CYIDEDG-YLF 404
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
181-519 |
2.43e-03 |
|
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: 40.35 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 181 TSGSTsGSPKVVPLTQKFVSTYYKTQFGIWldgrrfdtqnAFLSRGSICAVAPIIQYFG------C-LYTG-SCIVQPsk 252
Cdd:cd05941 97 TSGTT-GRPKGVVLTHANLAANVRALVDAW----------RWTEDDVLLHVLPLHHVHGlvnallCpLFAGaSVEFLP-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 253 mRFSTEELLTLvnvCGLNRMT------TFGTWLAPHIQAAKKDPA-ALKLLQE-MRTVSYGGVPISIAD-DDWCFQNGIP 323
Cdd:cd05941 164 -KFDPKEVAIS---RLMPSITvfmgvpTIYTRLLQYYEAHFTDPQfARAAAAErLRLMVSGSAALPVPTlEEWEAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 324 LMDMYATTECGTLM---VSAPGKPARFMQPVPGISYRFdpfTDTTTGADNPASTQllklillaDSPQIPQPQLLSE---- 396
Cdd:cd05941 240 LLERYGMTEIGMALsnpLDGERRPGTVGMPLPGVQARI---VDEETGEPLPRGEV--------GEIQVRGPSVFKEywnk 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 397 ----------DGNFHTGDLFEKQLDGSYLFRGRG-DDWIKSEDSRfIDTKAIEEKINDvcSDLVKGCIVVGhlRPSPAL- 464
Cdd:cd05941 309 peatkeeftdDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYK-VSALEIERVLLA--HPGVSECAVIG--VPDPDWg 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203519039 465 ----FIEAYHDSISTISEDGLKELVLRRLEdfnarqlKHERitDKRLIFiVDEgnLPRT 519
Cdd:cd05941 384 ervvAVVVLRAGAAALSLEELKEWAKQRLA-------PYKR--PRRLIL-VDE--LPRN 430
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
321-457 |
2.60e-03 |
|
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: 40.42 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 321 GIPLMDMYATTEcgTLMVSAPGKPARFM-----QPVPGISYRF-DPFTDTTTgadNPAStqllKLILLADSPQI-----P 389
Cdd:cd17640 237 GIEVLNGYGLTE--TSPVVSARRLKCNVrgsvgRPLPGTEIKIvDPEGNVVL---PPGE----KGIVWVRGPQVmkgyyK 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203519039 390 QP----QLLSEDGNFHTGDLFEKQLDGSYLFRGRGDDWIKSEDSRFIDTKAIEEKIndVCSDLVKGCIVVGH 457
Cdd:cd17640 308 NPeatsKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL--MRSPFIEQIMVVGQ 377
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
397-438 |
4.13e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 39.66 E-value: 4.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2203519039 397 DGNFHTGDLFEKQLDGSYLFRGRGDDWIKSeDSRFIDTKAIE 438
Cdd:PRK07867 380 GGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIE 420
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
43-197 |
4.71e-03 |
|
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: 39.57 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 43 ITVAEFAAEVDRVAifvmTELKARGIPPRSAVTVLysGSRYQDLIYAI-ALARASYIPQMCP---------HILTHpgvI 112
Cdd:cd05906 40 QSYQDLLEDARRLA----AGLRQLGLRPGDSVILQ--FDDNEDFIPAFwACVLAGFVPAPLTvpptydepnARLRK---L 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519039 113 FALMEKAGSKIILYDPSLEPAttdcpypkmaLNPIETIDSsstiNSDSALPTIEDLSSGHA----------DVCFFYLTS 182
Cdd:cd05906 111 RHIWQLLGSPVVLTDAELVAE----------FAGLETLSG----LPGIRVLSIEELLDTAAdhdlpqsrpdDLALLMLTS 176
|
170
....*....|....*
gi 2203519039 183 GSTsGSPKVVPLTQK 197
Cdd:cd05906 177 GST-GFPKAVPLTHR 190
|
|
| |
