|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-528 |
1.83e-60 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 208.54 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVGTGFSVSR--FAGALRLLAHRGPFGEGIAALPNGAIGMTRL---PMSGAAAVPLPPQEGQRRVAYNGEVY-- 73
Cdd:COG0367 1 MCGIAGIIDFDGGADRevLERMLDALAHRGPDGSGIWVDGGVALGHRRLsiiDLSEGGHQPMVSEDGRYVLVFNGEIYny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 74 --------QAGCEIHGE--IRLLLDGLQR---GVLP--DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPERglLAFA 138
Cdd:COG0367 81 relraeleALGHRFRTHsdTEVILHAYEEwgeDCLErlNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGG--LAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 139 SEPRALLHLLGGARA-DAEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFDLSQErPRLCQRQRLATAPASEVDSLDEQ 217
Cdd:COG0367 159 SELKALLAHPGVDRElDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVDAGGE-LEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 218 LGETLERCRQTFR-------PCALLVSGGVDSN----LLGSYLDPQLQRFHLCLEGDEESLLPHPRL---------QRFE 277
Cdd:COG0367 238 VEELRELLEDAVRrrlradvPVGAFLSGGLDSSaiaaLAARLSKGPLKTFSIGFEDSAYDESPYARAvaehlgtehHEVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 278 LRQEAFMPLLRRAVGNFGGATRMSSLLMYQRLADGIGEQgYHCVLLGEGADELFWGYPRHLELWRRrdtpeprrfaaawf 357
Cdd:COG0367 318 VTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAALL-------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 358 geyrrkaaLLAEPAGRRVAERIEELAHEALGQGLEAAIGQFDLHYSLEP-LLRRADHLLMSRTIEARTPYLHGALAQRAG 436
Cdd:COG0367 383 --------LSPDFAEALGGELVPRLYAESGAEDPLRRMLYLDLKTYLPGdLLVKVDRMSMAHSLEVRVPFLDHRLVEFAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 437 RL---QRIVGDTAKAPLVALLEQR---EKRWqaQPKRHFRLPFERWpqALGEMRRHLAERL--PALHDLGLegLDAPSVA 508
Cdd:COG0367 455 SLppeLKLRGGRGKYLLRKALEGLlpdEVLD--RPKQGFPVPLGPW--LRGPLREWLEDLLsdESLAARGL--FDPDAVR 528
|
570 580 590
....*....|....*....|....*....|
gi 15596411 509 AL----------PGDQLFTLTTLSLWQQEY 528
Cdd:COG0367 529 RLleehlagrrdHSRKLWSLLMLELWLRRF 558
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-196 |
2.07e-37 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 137.30 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 2 CGILGYV---GTGFSVSRFAGALRLLAHRGPFGEGIAALPNGAIGMTRL----------PMSGAaavplppqEGQRRVAY 68
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLsiidlsggaqPMVSE--------DGRLVLVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 69 NGEVY-----QAGCEIHG---------EIRLLL------DGLQRgvLpDGMYALASWDPQTRQLTLLRDEFGIKPLYYSY 128
Cdd:cd00712 73 NGEIYnyrelRAELEALGhrfrthsdtEVILHLyeewgeDCLER--L-NGMFAFALWDKRKRRLFLARDRFGIKPLYYGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596411 129 QPERglLAFASEPRALL-HLLGGARADAEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFDLSQERPR 196
Cdd:cd00712 150 DGGG--LAFASELKALLaLPGVPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIR 216
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
214-526 |
1.70e-35 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 133.90 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 214 LDEQLGETLERCRQTFRPCALLVSGGVDSN----LLGSYLDPQLQRFHLCLEGDEESLLPHPRL---------QRFELRQ 280
Cdd:pfam00733 2 LRELLEDAVARRLRADVPVGAFLSGGLDSSsiaaLAARQSPSPLHTFSIGFEGRGYDEAPYAREvaehlgtdhHELVVTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 281 EAFMPLLRRAV----GNFGGATRMSSLLMYQRladgIGEQGYHCVLLGEGADELFWGYPRHLelwrrrdtpeprrfaaaw 356
Cdd:pfam00733 82 EDLLDALPDVIwhldEPFADPSAIPLYLLSRL----ARRKGVKVVLSGEGADELFGGYPFYK------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 357 fgeyrrkaallaepagrrvaerieelAHEALGQGLeaaigQFDLHYSLEPLLRRADHLLMSRTIEARTPYLHGALAQRAG 436
Cdd:pfam00733 140 --------------------------GEDPLRRML-----YLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYAL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 437 RL---QRIVGDTAKAPLVALLEQR-EKRWQAQPKRHFRLPFERWPQAlGEMRRHLAERLPALHDLGLEGLDAPSVAALPG 512
Cdd:pfam00733 189 RLppeLKLRGGIEKYILREALEGIlPDEILERPKEGFSAPVGDWKLR-GPLRELAEDLLSDSRLAKEGLLDREAVRELLD 267
|
330
....*....|....
gi 15596411 513 DQLftLTTLSLWQQ 526
Cdd:pfam00733 268 EHL--AGMLELWLR 279
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
21-438 |
3.47e-33 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 131.69 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 21 LRLLAHRGPFGEGIAALPNGAI-GMTRLPM--SGAAAVPLPPQEGQRRVAYNGEVYQagceiHGEIR------------- 84
Cdd:TIGR01536 22 SDTIAHRGPDASGIEYKDGNAIlGHRRLAIidLSGGAQPMSNEGKTYVIVFNGEIYN-----HEELReeleakgytfqtd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 85 ----LLLDGLQR-GV----LPDGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPERglLAFASEPRALLHLLGGARA-D 154
Cdd:TIGR01536 97 sdteVILHLYEEwGEecvdRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQ--LYFASEIKALLAHPNIKPFpD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 155 AEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFD---LSQERPRLCQRQRLATAPASEVDSLDEQLGETLERCRQTFRP 231
Cdd:TIGR01536 175 GAALAPGFGFVRVPPPSTFFRGVFELEPGHDLPLDddgLNIERYYWERRDEHTDSEEDLVDELRSLLEDAVKRRLVADVP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 232 CALLVSGGVDSNLLGSYLDPQ-----LQRFHLCLEGDEE-SLLPHPR---------LQRFELRQEAFMPLLRRAVGNFGG 296
Cdd:TIGR01536 255 VGVLLSGGLDSSLVAAIARREaprgpVHTFSIGFEGSPDfDESKYARkvadhlgteHHEVLFSVEEGLDALPEVIYHLEE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 297 ATRM-SSLLMYqRLADGIGEQGYHCVLLGEGADELFWGYPRHLELwrrrdtpeprrfaaawfgeyrrkaallaePAGRRV 375
Cdd:TIGR01536 335 PTTIrASIPLY-LLSKLAREDGVKVVLSGEGADELFGGYLYFHEA-----------------------------PAAEAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596411 376 AERIEELahealgqgleaaigqfDLHYSLEPLLRRADHLLMSRTIEARTPYLHGALAQRAGRL 438
Cdd:TIGR01536 385 REELQYL----------------DLELYMPGLLRRKDRMSMAHSLEVRVPFLDHELVEYALSI 431
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-334 |
9.94e-20 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 92.28 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVG----TGFSVSRFAGALRLLAHRGPFGEGIAALPNGAIGMTRL----PMSGAAavPLPPQEGQRRVAYNGEV 72
Cdd:PRK09431 1 MCGIFGILDiktdADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLsivdVNGGAQ--PLYNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 73 YQagceiHGEIRLLLDG---LQRG-----VLP-------------DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQpE 131
Cdd:PRK09431 79 YN-----HQELRAELGDkyaFQTGsdcevILAlyqekgpdflddlDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYD-E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 132 RGLLAFASEPRAllhllggaradaeaiaqvvaagvpLEGQTlfQQVRLLLPGEVLRfdlSQERPRLCQRQRlataPASEV 211
Cdd:PRK09431 153 HGNLYFASEMKA------------------------LVPVC--KTIKEFPPGHYYW---SKDGEFVRYYQR----DWFDY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 212 DSLDEQLgETLERCRQTFR-----------PCALLVSGGVDSNLLGS-----------------YLDPQLQRFHLCLEGD 263
Cdd:PRK09431 200 DAVKDNV-TDKNELRDALEaavkkrlmsdvPYGVLLSGGLDSSLISAiakkyaarriedderseAWWPQLHSFAVGLEGS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 264 EEslLPHPRLQRFEL----------RQEAfMPLLRR---AVGNFGGATRMSSLLMYqRLADGIGEQGYHCVLLGEGADEL 330
Cdd:PRK09431 279 PD--LKAAREVADHLgtvhheihftVQEG-LDALRDviyHLETYDVTTIRASTPMY-LMARKIKAMGIKMVLSGEGADEL 354
|
....
gi 15596411 331 FWGY 334
Cdd:PRK09431 355 FGGY 358
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-528 |
1.83e-60 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 208.54 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVGTGFSVSR--FAGALRLLAHRGPFGEGIAALPNGAIGMTRL---PMSGAAAVPLPPQEGQRRVAYNGEVY-- 73
Cdd:COG0367 1 MCGIAGIIDFDGGADRevLERMLDALAHRGPDGSGIWVDGGVALGHRRLsiiDLSEGGHQPMVSEDGRYVLVFNGEIYny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 74 --------QAGCEIHGE--IRLLLDGLQR---GVLP--DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPERglLAFA 138
Cdd:COG0367 81 relraeleALGHRFRTHsdTEVILHAYEEwgeDCLErlNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGG--LAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 139 SEPRALLHLLGGARA-DAEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFDLSQErPRLCQRQRLATAPASEVDSLDEQ 217
Cdd:COG0367 159 SELKALLAHPGVDRElDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVDAGGE-LEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 218 LGETLERCRQTFR-------PCALLVSGGVDSN----LLGSYLDPQLQRFHLCLEGDEESLLPHPRL---------QRFE 277
Cdd:COG0367 238 VEELRELLEDAVRrrlradvPVGAFLSGGLDSSaiaaLAARLSKGPLKTFSIGFEDSAYDESPYARAvaehlgtehHEVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 278 LRQEAFMPLLRRAVGNFGGATRMSSLLMYQRLADGIGEQgYHCVLLGEGADELFWGYPRHLELWRRrdtpeprrfaaawf 357
Cdd:COG0367 318 VTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAALL-------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 358 geyrrkaaLLAEPAGRRVAERIEELAHEALGQGLEAAIGQFDLHYSLEP-LLRRADHLLMSRTIEARTPYLHGALAQRAG 436
Cdd:COG0367 383 --------LSPDFAEALGGELVPRLYAESGAEDPLRRMLYLDLKTYLPGdLLVKVDRMSMAHSLEVRVPFLDHRLVEFAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 437 RL---QRIVGDTAKAPLVALLEQR---EKRWqaQPKRHFRLPFERWpqALGEMRRHLAERL--PALHDLGLegLDAPSVA 508
Cdd:COG0367 455 SLppeLKLRGGRGKYLLRKALEGLlpdEVLD--RPKQGFPVPLGPW--LRGPLREWLEDLLsdESLAARGL--FDPDAVR 528
|
570 580 590
....*....|....*....|....*....|
gi 15596411 509 AL----------PGDQLFTLTTLSLWQQEY 528
Cdd:COG0367 529 RLleehlagrrdHSRKLWSLLMLELWLRRF 558
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-196 |
2.07e-37 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 137.30 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 2 CGILGYV---GTGFSVSRFAGALRLLAHRGPFGEGIAALPNGAIGMTRL----------PMSGAaavplppqEGQRRVAY 68
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLsiidlsggaqPMVSE--------DGRLVLVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 69 NGEVY-----QAGCEIHG---------EIRLLL------DGLQRgvLpDGMYALASWDPQTRQLTLLRDEFGIKPLYYSY 128
Cdd:cd00712 73 NGEIYnyrelRAELEALGhrfrthsdtEVILHLyeewgeDCLER--L-NGMFAFALWDKRKRRLFLARDRFGIKPLYYGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596411 129 QPERglLAFASEPRALL-HLLGGARADAEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFDLSQERPR 196
Cdd:cd00712 150 DGGG--LAFASELKALLaLPGVPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVDPGGVEIR 216
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
214-526 |
1.70e-35 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 133.90 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 214 LDEQLGETLERCRQTFRPCALLVSGGVDSN----LLGSYLDPQLQRFHLCLEGDEESLLPHPRL---------QRFELRQ 280
Cdd:pfam00733 2 LRELLEDAVARRLRADVPVGAFLSGGLDSSsiaaLAARQSPSPLHTFSIGFEGRGYDEAPYAREvaehlgtdhHELVVTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 281 EAFMPLLRRAV----GNFGGATRMSSLLMYQRladgIGEQGYHCVLLGEGADELFWGYPRHLelwrrrdtpeprrfaaaw 356
Cdd:pfam00733 82 EDLLDALPDVIwhldEPFADPSAIPLYLLSRL----ARRKGVKVVLSGEGADELFGGYPFYK------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 357 fgeyrrkaallaepagrrvaerieelAHEALGQGLeaaigQFDLHYSLEPLLRRADHLLMSRTIEARTPYLHGALAQRAG 436
Cdd:pfam00733 140 --------------------------GEDPLRRML-----YLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYAL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 437 RL---QRIVGDTAKAPLVALLEQR-EKRWQAQPKRHFRLPFERWPQAlGEMRRHLAERLPALHDLGLEGLDAPSVAALPG 512
Cdd:pfam00733 189 RLppeLKLRGGIEKYILREALEGIlPDEILERPKEGFSAPVGDWKLR-GPLRELAEDLLSDSRLAKEGLLDREAVRELLD 267
|
330
....*....|....
gi 15596411 513 DQLftLTTLSLWQQ 526
Cdd:pfam00733 268 EHL--AGMLELWLR 279
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
21-438 |
3.47e-33 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 131.69 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 21 LRLLAHRGPFGEGIAALPNGAI-GMTRLPM--SGAAAVPLPPQEGQRRVAYNGEVYQagceiHGEIR------------- 84
Cdd:TIGR01536 22 SDTIAHRGPDASGIEYKDGNAIlGHRRLAIidLSGGAQPMSNEGKTYVIVFNGEIYN-----HEELReeleakgytfqtd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 85 ----LLLDGLQR-GV----LPDGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPERglLAFASEPRALLHLLGGARA-D 154
Cdd:TIGR01536 97 sdteVILHLYEEwGEecvdRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQ--LYFASEIKALLAHPNIKPFpD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 155 AEAIAQVVAAGVPLEGQTLFQQVRLLLPGEVLRFD---LSQERPRLCQRQRLATAPASEVDSLDEQLGETLERCRQTFRP 231
Cdd:TIGR01536 175 GAALAPGFGFVRVPPPSTFFRGVFELEPGHDLPLDddgLNIERYYWERRDEHTDSEEDLVDELRSLLEDAVKRRLVADVP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 232 CALLVSGGVDSNLLGSYLDPQ-----LQRFHLCLEGDEE-SLLPHPR---------LQRFELRQEAFMPLLRRAVGNFGG 296
Cdd:TIGR01536 255 VGVLLSGGLDSSLVAAIARREaprgpVHTFSIGFEGSPDfDESKYARkvadhlgteHHEVLFSVEEGLDALPEVIYHLEE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 297 ATRM-SSLLMYqRLADGIGEQGYHCVLLGEGADELFWGYPRHLELwrrrdtpeprrfaaawfgeyrrkaallaePAGRRV 375
Cdd:TIGR01536 335 PTTIrASIPLY-LLSKLAREDGVKVVLSGEGADELFGGYLYFHEA-----------------------------PAAEAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596411 376 AERIEELahealgqgleaaigqfDLHYSLEPLLRRADHLLMSRTIEARTPYLHGALAQRAGRL 438
Cdd:TIGR01536 385 REELQYL----------------DLELYMPGLLRRKDRMSMAHSLEVRVPFLDHELVEYALSI 431
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-334 |
9.94e-20 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 92.28 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVG----TGFSVSRFAGALRLLAHRGPFGEGIAALPNGAIGMTRL----PMSGAAavPLPPQEGQRRVAYNGEV 72
Cdd:PRK09431 1 MCGIFGILDiktdADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLsivdVNGGAQ--PLYNEDGTHVLAVNGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 73 YQagceiHGEIRLLLDG---LQRG-----VLP-------------DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQpE 131
Cdd:PRK09431 79 YN-----HQELRAELGDkyaFQTGsdcevILAlyqekgpdflddlDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYD-E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 132 RGLLAFASEPRAllhllggaradaeaiaqvvaagvpLEGQTlfQQVRLLLPGEVLRfdlSQERPRLCQRQRlataPASEV 211
Cdd:PRK09431 153 HGNLYFASEMKA------------------------LVPVC--KTIKEFPPGHYYW---SKDGEFVRYYQR----DWFDY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 212 DSLDEQLgETLERCRQTFR-----------PCALLVSGGVDSNLLGS-----------------YLDPQLQRFHLCLEGD 263
Cdd:PRK09431 200 DAVKDNV-TDKNELRDALEaavkkrlmsdvPYGVLLSGGLDSSLISAiakkyaarriedderseAWWPQLHSFAVGLEGS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 264 EEslLPHPRLQRFEL----------RQEAfMPLLRR---AVGNFGGATRMSSLLMYqRLADGIGEQGYHCVLLGEGADEL 330
Cdd:PRK09431 279 PD--LKAAREVADHLgtvhheihftVQEG-LDALRDviyHLETYDVTTIRASTPMY-LMARKIKAMGIKMVLSGEGADEL 354
|
....
gi 15596411 331 FWGY 334
Cdd:PRK09431 355 FGGY 358
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-147 |
7.70e-18 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 82.50 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 2 CGILGYVGTGFSVSRFA----GALRLLAHRGPFGEGIAALPNG---------------------------AIGMTRL--- 47
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDGDglfvekragpvsdvaldlldeplksgvALGHVRLatn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 48 -PMSGAAAVPLPPQEGQRRVAYNGEVY----------QAGCEIHGE------IRLLLDGLQRGVLP----------DGMY 100
Cdd:cd00352 81 gLPSEANAQPFRSEDGRIALVHNGEIYnyrelreeleARGYRFEGEsdseviLHLLERLGREGGLFeavedalkrlDGPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596411 101 ALASWDPQTRQLTLLRDEFGIKPLYYSYQPErGLLAFASEPRALLHL 147
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKD-GGLVFASEPKALLAL 206
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-145 |
3.84e-16 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 74.86 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 66 VAYNGEVY----------QAGCEIHGEI--RLLLDGLQRGVLPD------GMYALASWDPQTRQLTLLRDEFGIKPLYYS 127
Cdd:pfam13537 26 IVFNGEIYnyrelraeleAKGYRFRTHSdtEVILHLYEAEWGEDcvdrlnGMFAFAIWDRRRQRLFLARDRFGIKPLYYG 105
|
90
....*....|....*...
gi 15596411 128 YQPERGLLaFASEPRALL 145
Cdd:pfam13537 106 RDDGGRLL-FASELKALL 122
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
29-140 |
1.02e-12 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 65.02 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 29 PFGEGIAALPNGAIGMTRLPMSG---AAAVPLPPQEGQRRVAYNGEVYQagceiHGEIRLLLDGLQR------------- 92
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDlpdAGNQPMLSRDGRLVLVHNGEIYN-----YGELREELADLGHafrsrsdtevlla 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596411 93 -------GVLP--DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPerGLLAFASE 140
Cdd:pfam13522 76 lyeewgeDCLErlRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILG--GGFVFASE 130
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-334 |
1.53e-11 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 66.66 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGY---VGTGFSVSRFAGAL-RLLAHRGPFGEGIAALPNG-----AIGMTRL----PMSGAAavPLPPQEGQRRVA 67
Cdd:PTZ00077 1 MCGILAIfnsKGERHELRRKALELsKRLRHRGPDWSGIIVLENSpgtynILAHERLaivdLSDGKQ--PLLDDDETVALM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 68 YNGEVYQagceiHGEIRLLL--DGLQRG------VLP---------------DGMYALASWDPQTRQLTLLRDEFGIKPL 124
Cdd:PTZ00077 79 QNGEIYN-----HWEIRPELekEGYKFSsnsdceIIGhlykeygpkdfwnhlDGMFATVIYDMKTNTFFAARDHIGIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 125 YYSYQPErGLLAFASEPRALLhllggaradaeaiAQVVaagvplegqtlfqQVRLLLPGEVlrFDLSQERPRLCQ----- 199
Cdd:PTZ00077 154 YIGYAKD-GSIWFSSELKALH-------------DQCV-------------EVKQFPPGHY--YDQTKEKGEFVRyynpn 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 200 -RQRLATAPASEVD--SLDEQLGETLERCRQTFRPCALLVSGGVDSNLLGSYLDPQLQrfhlclEGDEE-SLLPHPRLQR 275
Cdd:PTZ00077 205 wHDFDHPIPTGEIDleEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIK------NGEIDlSKRGMPKLHS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 276 FELRQEAfMPLLR--RAVGNFGG-----------------------------ATRMSSLLMYQrLADGIGEQGYHCVLLG 324
Cdd:PTZ00077 279 FCIGLEG-SPDLKaaRKVAEYLGtehheftftveegidalpdviyhtetydvTTIRASTPMYL-LSRRIKALGIKMVLSG 356
|
410
....*....|
gi 15596411 325 EGADELFWGY 334
Cdd:PTZ00077 357 EGSDELFGGY 366
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
230-438 |
4.69e-09 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 56.90 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 230 RPCALLVSGGVDSNLLGSYLDPQLQR-----FHLCLEGDEESLLPHPR-----LQR----FELRQEAFMPLLRRAVGNFG 295
Cdd:cd01991 3 VPVGVLLSGGLDSSLIAALAARLLPEtpidlFTVGFEGSPTPDRAAARrvaeeLGTehheVEVTIEELLDALPDVILIYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 296 GATRM---SSLLMYQrLADGIGEQGYHCVLLGEGADELFWGYPRHLELWRRRdtpePRRFAAAWfgeyrrkaallaepag 372
Cdd:cd01991 83 TDTPMdlsIAIPLYF-ASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRG----WEALEEEL---------------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596411 373 rrvAERIEELAHEALGqgleaaigqfdlhyslepllrRADHLLMSRTIEARTPYLHGALAQRAGRL 438
Cdd:cd01991 142 ---LRDLDRLWTRNLG---------------------RDDRVAMAHGLEARVPFLDEELVEFALSL 183
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-334 |
2.12e-08 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 56.70 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVG-TGFSV---SRFAGALRLLAHRGPFGEGIAALPNGAIGMTRL----PMSGAAavPLPPQEGQRRVAYNGEV 72
Cdd:PLN02549 1 MCGILAVLGcSDDSQakrSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLaimdPESGDQ--PLYNEDKTIVVTANGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 73 Y----------------QAGCEI-------HGE--IRLLldglqrgvlpDGMYALASWDPQTRQLTLLRDEFGIKPLYYS 127
Cdd:PLN02549 79 YnhkelreklklhkfrtGSDCEViahlyeeHGEefVDML----------DGMFSFVLLDTRDNSFIAARDHIGITPLYIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 128 YQpERGLLAFASEPRALlhllggaRADAEAIaQVVAAG---VPLEGQTlfqqVRLLLPGEVLRFDlsqerprlcqrqrla 204
Cdd:PLN02549 149 WG-LDGSVWFASEMKAL-------CDDCERF-EEFPPGhyySSKAGGF----RRWYNPPWFSESI--------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 205 taPASEVDSLdeQLGETLERC--RQTFR--PCALLVSGGVDSNLLGSYLDPQlqrfhlcLEGDEESLLPHPRLQRFELRQ 280
Cdd:PLN02549 201 --PSTPYDPL--VLREAFEKAviKRLMTdvPFGVLLSGGLDSSLVASIAARH-------LAETKAARQWGQQLHSFCVGL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 281 EAfMPLLR--RAVGNFGG-----------------------------ATRMSSLLMYqRLADGIGEQGYHCVLLGEGADE 329
Cdd:PLN02549 270 EG-SPDLKaaREVADYLGtvhhefhftvqegidaiedviyhletydvTTIRASTPMF-LMSRKIKSLGVKMVLSGEGSDE 347
|
....*
gi 15596411 330 LFWGY 334
Cdd:PLN02549 348 IFGGY 352
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-139 |
2.00e-04 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 239735 [Multi-domain] Cd Length: 181 Bit Score: 42.27 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 1 MCGILGYVGTGFSVSR----FAGALRLLAHRGP--FGEGIAALPNGAIGM--TRLPMSGAAAV--PLPPQEGQRRVAYNG 70
Cdd:cd03766 1 MCGILCSVSPSGPHINssllSEELLPNLRNRGPdyLSTRQLSVTNWTLLFtsSVLSLRGDHVTrqPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 71 EVYQAGCEIHGE--IRLLLDGLQR------GVLP-----DGMYALASWDPQTRQLTLLRDEFGIKPLYYSYQPERGLLAF 137
Cdd:cd03766 81 ELYNIDGVEDEEndTEVIFELLANcssesqDILDvlssiEGPFAFIYYDASENKLYFGRDCLGRRSLLYKLDPNGFELSI 160
|
..
gi 15596411 138 AS 139
Cdd:cd03766 161 SS 162
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
136-521 |
2.31e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.01 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 136 AFASEPRALLHLLGGARADA----EAIAQVVAAGVPLEGQTLFQQV---RLLLPG-----EVLRFDLSQERPRLCQRQRL 203
Cdd:COG3321 811 LAAAGDAVVLPSLRRGEDELaqllTALAQLWVAGVPVDWSALYPGRgrrRVPLPTypfqrEDAAAALLAAALAAALAAAA 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 204 ATAPASEVDSLDEQLGETLERCRQTFRPCALLVSGGVDSNLLGSYLDPQLQRFHLCLEGDEESLLPHPRLQRFELRQEAF 283
Cdd:COG3321 891 ALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAA 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 284 MPLLRRAVGNFGGATRMSSLLMYQRLADGIGEQGYHCVLLGEGADELFWGYPRHLELWRRRDTPEPRRFAAAWFGEYRRK 363
Cdd:COG3321 971 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596411 364 AALLAEPAGRRVAERIEELAHEALGQGLEAAIGQFDLHYSLEPLLRRADHLLMSRTIEARTPYLHGALAQRAGRLQRIVG 443
Cdd:COG3321 1051 LAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAAL 1130
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596411 444 DTAKAPLVALLEQREKRWQAQPKRHFRLPFERWPQALGEMRRHLAERLPALHDLGLEGLDAPSVAALPGDQLFTLTTL 521
Cdd:COG3321 1131 LAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAAL 1208
|
|
| |
