|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1132.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 81 HKELAAELEVDFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 161 ELKALSPICKHIEEFPPGHYLYSKNGELTPYYKRDWETFDAVKDNSAQAQDVKEALESAVKRQLMCDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 241 SVISAITQRFAAKRIEDNDESDAWWPKLHSFSVGLEGSPDLAAAQKVADMIGTVHHPIHFTIQEGIDALREVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 321 VTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEFHEELNRKVSKLHMFDCLRANKSMAAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 401 RVPFLDKEFVDVAMRINPEAKMCKDGKIEKHILREGFDGYLPEEVLWRQKEQFSDGVGYSWIDTLKEFVNEQVSDQELAN 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567931739 481 AKFKYPINTPDSKEAYYYRSIFESHFPGDASAKCVPHGKSVACSTPEALAWDASFQNNADPSGRA-AGVHNDAY 553
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAvSGVHQSAY 554
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-510 |
0e+00 |
|
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: 534.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNAtqLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSS-GAQPLYNPEKTNILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEgGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 80 NHKELAAELEV-DFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEhGNFYV 158
Cdd:COG0367 79 NYRELRAELEAlGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 159 ASELKALSP---------------------------ICKHIEEFPPGHYLYSKNG---ELTPYYKRDWETFDAVKDNSAQ 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 209 AQDVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAKRiedndesdawwpkLHSFSVGLEGSP--DLAAAQK 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 287 VADMIGTVHHPIHFTIQEGIDALREVIYHIEtyDVTTIRASTPMYLMARQIKAMgIKMVLSGEGADELFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 367 A--QEFHEELNRKV-----------------------SKLHMFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAK 421
Cdd:COG0367 382 LlsPDFAEALGGELvprlyaesgaedplrrmlyldlkTYLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 422 MCkdGKIEKHILREGFDGYLPEEVLWRQKEQFSDGVGySWID-TLKEFVNEQVSDQELANAKFkypINtpdskeAYYYRS 500
Cdd:COG0367 462 LR--GGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FD------PDAVRR 529
|
570
....*....|
gi 567931739 501 IFESHFPGDA 510
Cdd:COG0367 530 LLEEHLAGRR 539
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
2.64e-180 |
|
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: 516.12 E-value: 2.64e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 4 IFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGV-YSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 83 ELAAELEVD-FEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDeHGNFYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 162 LKALSPICKhIEEFPPGHYLYSKNGE----LTPYYKRDWETFDAVKDNSAQA------------------------QDVK 213
Cdd:TIGR01536 160 IKALLAHPN-IKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPLDDdglnieryywerrdehtdseedlvDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 214 EALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAKriedndesdawwPKLHSFSVGLEGSPDL---AAAQKVADM 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 291 IGTVHHPIHFTIQEGIDALREVIYHIEtyDVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 371 HEELNRKVSKLHMFDCLRANKSMA-AWGVEARVPFLDKEFVDVAMRINPEAKMckDGKIEKHILREGFDGYLPEEVLWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 567931739 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
1.32e-109 |
|
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: 328.42 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 211 DVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAkriedndesdawwPKLHSFSVGLE--GSPDLAAAQKVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEgrGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 289 DMIGTVHHPIHFTIQEGIDALREVIYHIETydVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHkapNAQ 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 369 EFHEELNRKVSKLHMFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAKMCkdGKIEKHILREGFDGYLPEEVLWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLR--GGIEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931739 449 QKEQFSDGVGYSWID-TLKEFVNEQVSDQELAnakfkypintpdsKEAYYYRSIFESHFPGDASA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDSRLA-------------KEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
227-457 |
1.63e-93 |
|
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: 285.32 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 227 DVPYGVLLSGGLDSSVISAITQRFAAKriedndesdawwPKLHSFSVGLEGS--PDLAAAQKVADMIGTVHHPIHFTIQE 304
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 305 GIDALREVIYHIETYDVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNA--QEFHEELNRKVSKLH 382
Cdd:cd01991 70 LLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRLW 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931739 383 MFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAKMCKDGKIEKHILREGFDGYLPEEVLWRQKEQFSDGV 457
Cdd:cd01991 150 TRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-272 |
2.39e-24 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 107.39 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQlRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVS-SGAQPLYNPEKTNILAVNGEIY 79
Cdd:NF033535 1 MSGIVGIYYLDGRPVD-REDLQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESlLEKLPLVNQTGDLVITADARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 80 NHKELAAELEV-DFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGnFYV 158
Cdd:NF033535 80 NRDELISALQLnNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKR-FAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 159 ASELKA---LSPICKHIEE------------------------FPPGHYLY-SKNG-ELTPYYKRDWETFDAVKDNSAQA 209
Cdd:NF033535 159 ASEIKAllcLPEVPRRLNEvriadylalmledkvitfyqdifrLPPAHSMTvSQSGlQIRSYWSLDPSRELRLDSDEEYA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567931739 210 QDVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAItqrfaAKRIEDNDESdawwPKLHSFS 272
Cdd:NF033535 239 EAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFS 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1132.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 81 HKELAAELEVDFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 161 ELKALSPICKHIEEFPPGHYLYSKNGELTPYYKRDWETFDAVKDNSAQAQDVKEALESAVKRQLMCDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 241 SVISAITQRFAAKRIEDNDESDAWWPKLHSFSVGLEGSPDLAAAQKVADMIGTVHHPIHFTIQEGIDALREVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 321 VTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEFHEELNRKVSKLHMFDCLRANKSMAAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 401 RVPFLDKEFVDVAMRINPEAKMCKDGKIEKHILREGFDGYLPEEVLWRQKEQFSDGVGYSWIDTLKEFVNEQVSDQELAN 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567931739 481 AKFKYPINTPDSKEAYYYRSIFESHFPGDASAKCVPHGKSVACSTPEALAWDASFQNNADPSGRA-AGVHNDAY 553
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAvSGVHQSAY 554
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-556 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 844.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 81 HKELAAELEvDFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVAS 160
Cdd:PLN02549 81 HKELREKLK-LHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 161 ELKALSPICKHIEEFPPGHYLYSKNGELTPYYKRDWETfDAVKDNSAQAQDVKEALESAVKRQLMCDVPYGVLLSGGLDS 240
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFS-ESIPSTPYDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 241 SVISAITQRFaakrIEDNDESDAWWPKLHSFSVGLEGSPDLAAAQKVADMIGTVHHPIHFTIQEGIDALREVIYHIETYD 320
Cdd:PLN02549 239 SLVASIAARH----LAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETYD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 321 VTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEFHEELNRKVSKLHMFDCLRANKSMAAWGVEA 400
Cdd:PLN02549 315 VTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 401 RVPFLDKEFVDVAMRINPEAKMCK--DGKIEKHILREGFDG----YLPEEVLWRQKEQFSDGVGYSWIDTLKEFVNEQVS 474
Cdd:PLN02549 395 RVPFLDKEFIDVAMSIDPEWKMIRpgEGRIEKWVLRKAFDDeedpYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHVS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 475 DQELANAKFKYPINTPDSKEAYYYRSIFESHFPGDASAKCVPHGKSVACSTPEALAWDASFQNNADPSGRAA-GVHNDAY 553
Cdd:PLN02549 475 DEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAAlGVHVAAY 554
|
...
gi 567931739 554 ASK 556
Cdd:PLN02549 555 EED 557
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 836.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGVYSSEKA-----ILVHERLAIVGVSSGAQPLYNPEKTNILAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 76 GEIYNHKELAAELEVD-FEFQTQSDCEVILALYKQKGP-EFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELEKEgYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 154 GNFYVASELKALSPICKHIEEFPPGHYLYSKN--GELTPYYKRDWETFDA-VKDNSAQAQDVKEALESAVKRQLMCDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQTKekGEFVRYYNPNWHDFDHpIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 231 GVLLSGGLDSSVISAITQRFAAKriEDNDESDAWWPKLHSFSVGLEGSPDLAAAQKVADMIGTVHHPIHFTIQEGIDALR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKLIKN--GEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 311 EVIYHIETYDVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEFHEELNRKVSKLHMFDCLRAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 391 KSMAAWGVEARVPFLDKEFVDVAMRINPEAKMCK--DGKIEKHILREGFDG----YLPEEVLWRQKEQFSDGVGYSWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNafEGQMEKYILRKAFEGlekpYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 465 LKEFVNEQVSDQELANAKFKYPINTPDSKEAYYYRSIFESHFPGDASAKCVPHGKSVACSTPEALAWDASFQNNADPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|
gi 567931739 545 AA-GVHNDAY 553
Cdd:PTZ00077 559 AVlSVHNDAK 568
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-510 |
0e+00 |
|
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: 534.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNAtqLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSS-GAQPLYNPEKTNILAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEgGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 80 NHKELAAELEV-DFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEhGNFYV 158
Cdd:COG0367 79 NYRELRAELEAlGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 159 ASELKALSP---------------------------ICKHIEEFPPGHYLYSKNG---ELTPYYKRDWETFDAVKDNSAQ 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 209 AQDVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAKRiedndesdawwpkLHSFSVGLEGSP--DLAAAQK 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 287 VADMIGTVHHPIHFTIQEGIDALREVIYHIEtyDVTTIRASTPMYLMARQIKAMgIKMVLSGEGADELFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 367 A--QEFHEELNRKV-----------------------SKLHMFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAK 421
Cdd:COG0367 382 LlsPDFAEALGGELvprlyaesgaedplrrmlyldlkTYLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 422 MCkdGKIEKHILREGFDGYLPEEVLWRQKEQFSDGVGySWID-TLKEFVNEQVSDQELANAKFkypINtpdskeAYYYRS 500
Cdd:COG0367 462 LR--GGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FD------PDAVRR 529
|
570
....*....|
gi 567931739 501 IFESHFPGDA 510
Cdd:COG0367 530 LLEEHLAGRR 539
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
2.64e-180 |
|
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: 516.12 E-value: 2.64e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 4 IFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGV-YSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 83 ELAAELEVD-FEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDeHGNFYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 162 LKALSPICKhIEEFPPGHYLYSKNGE----LTPYYKRDWETFDAVKDNSAQA------------------------QDVK 213
Cdd:TIGR01536 160 IKALLAHPN-IKPFPDGAALAPGFGFvrvpPPSTFFRGVFELEPGHDLPLDDdglnieryywerrdehtdseedlvDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 214 EALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAKriedndesdawwPKLHSFSVGLEGSPDL---AAAQKVADM 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 291 IGTVHHPIHFTIQEGIDALREVIYHIEtyDVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNAQEF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 371 HEELNRKVSKLHMFDCLRANKSMA-AWGVEARVPFLDKEFVDVAMRINPEAKMckDGKIEKHILREGFDGYLPEEVLWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 567931739 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
1.32e-109 |
|
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: 328.42 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 211 DVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAITQRFAAkriedndesdawwPKLHSFSVGLE--GSPDLAAAQKVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEgrGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 289 DMIGTVHHPIHFTIQEGIDALREVIYHIETydVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHkapNAQ 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 369 EFHEELNRKVSKLHMFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAKMCkdGKIEKHILREGFDGYLPEEVLWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLR--GGIEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931739 449 QKEQFSDGVGYSWID-TLKEFVNEQVSDQELAnakfkypintpdsKEAYYYRSIFESHFPGDASA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDSRLA-------------KEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
227-457 |
1.63e-93 |
|
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: 285.32 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 227 DVPYGVLLSGGLDSSVISAITQRFAAKriedndesdawwPKLHSFSVGLEGS--PDLAAAQKVADMIGTVHHPIHFTIQE 304
Cdd:cd01991 2 DVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 305 GIDALREVIYHIETYDVTTIRASTPMYLMARQIKAMGIKMVLSGEGADELFGGYLYFHKAPNA--QEFHEELNRKVSKLH 382
Cdd:cd01991 70 LLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRLW 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931739 383 MFDCLRANKSMAAWGVEARVPFLDKEFVDVAMRINPEAKMCKDGKIEKHILREGFDGYLPEEVLWRQKEQFSDGV 457
Cdd:cd01991 150 TRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-193 |
2.67e-80 |
|
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: 250.94 E-value: 2.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 2 CSIFGVLDIKsNATQLRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLD-GASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 82 KELAAELEVD-FEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEhGNFYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDG-GGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567931739 161 ELKALSPIC---------------------------KHIEEFPPGHYLYSKNG--ELTPYYK 193
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPGgvEIRRYWD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-165 |
7.62e-52 |
|
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: 173.09 E-value: 7.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 48 HERLAIVGVSSGAQPLYN-PEKTNILAVNGEIYNHKELAAELEV-DFEFQTQSDCEVILALYK-QKGPEFLDDLNGIFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVSsEDGRYVIVFNGEIYNYRELRAELEAkGYRFRTHSDTEVILHLYEaEWGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 567931739 125 CLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVASELKAL 165
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
2.57e-48 |
|
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: 167.24 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 2 CSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGVYSSE---------------------------KAILVHERLAIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 55 GVSS--GAQPLYNPEKTNILAVNGEIYNHKELAAELEVD-FEFQTQSDCEVILALYKQKG---------PEFLDDLNGIF 122
Cdd:cd00352 81 GLPSeaNAQPFRSEDGRIALVHNGEIYNYRELREELEARgYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 123 AFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVASELKALSPIC-KHIEEFPPGHYL 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
1.05e-41 |
|
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: 146.30 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 33 PDWSGVYSSEKAILVHERLAIVGVS-SGAQPLYNPEKTNILAVNGEIYNHKELAAELEVD-FEFQTQSDCEVILALYKQK 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLPdAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 567931739 111 GPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGhDEHGNFYVASE 161
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYG-ILGGGFVFASE 130
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-272 |
2.39e-24 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 107.39 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQlRTQAIEMSKLLRHRGPDWSGVYSSEKAILVHERLAIVGVS-SGAQPLYNPEKTNILAVNGEIY 79
Cdd:NF033535 1 MSGIVGIYYLDGRPVD-REDLQQMVDILAHRGPDGADIWCEGSVGLGHRMLWTTPESlLEKLPLVNQTGDLVITADARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 80 NHKELAAELEV-DFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGnFYV 158
Cdd:NF033535 80 NRDELISALQLnNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSDKR-FAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 159 ASELKA---LSPICKHIEE------------------------FPPGHYLY-SKNG-ELTPYYKRDWETFDAVKDNSAQA 209
Cdd:NF033535 159 ASEIKAllcLPEVPRRLNEvriadylalmledkvitfyqdifrLPPAHSMTvSQSGlQIRSYWSLDPSRELRLDSDEEYA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567931739 210 QDVKEALESAVKRQLMCDVPYGVLLSGGLDSSVISAItqrfaAKRIEDNDESdawwPKLHSFS 272
Cdd:NF033535 239 EAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFS 292
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-142 |
3.62e-11 |
|
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: 62.30 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDIKSNATQLRTQAIEMSKLLRHRGPDWSGV----YSSEKAILVHERLAIVGVSSGAQPLYNPEKTNILAVNG 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTrqlsVTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567931739 77 EIYNHKELAAElevdfefqtQSDCEVI---LALYKQKGPEFLD---DLNGIFAFCLYDEENDAYLIGRDHIG 142
Cdd:cd03766 81 ELYNIDGVEDE---------ENDTEVIfelLANCSSESQDILDvlsSIEGPFAFIYYDASENKLYFGRDCLG 143
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
60-189 |
2.67e-08 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 55.16 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 60 AQPLY-NPEKTNI-LAVNGEIYNHKELAAELE-VDFEFQTQSDCEVILAL---YKQKGP------EFLDDLNGIFAFCLY 127
Cdd:cd00715 84 AQPFVvNSPLGGIaLAHNGNLVNAKELREELEeEGRIFQTTSDSEVILHLiarSLAKDDlfeaiiDALERVKGAYSLVIM 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931739 128 DEENdayLIG-RDHIGIIPLYTGHDEHGNFYVASELKALSPI-CKHIEEFPPGHYLY-SKNGELT 189
Cdd:cd00715 164 TADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCALDIIgAEFVRDVEPGEIVViDDDGLES 225
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
5.21e-08 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 55.41 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 1 MCSIFGVLDiKSNATQLrtqAIEMSKLLRHRGPDWSG-VYSSEKAILVH---------------ERL----AIVGV---- 56
Cdd:COG0034 7 ECGVFGIYG-HEDVAQL---TYYGLYALQHRGQESAGiATSDGGRFHLHkgmglvsdvfdeedlERLkgniAIGHVryst 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 57 --SSG---AQPLY-NPEKTNI-LAVNGEIYNHKELAAELE-VDFEFQTQSDCEVILAL---YKQKGPEF------LDDLN 119
Cdd:COG0034 83 tgSSSlenAQPFYvNSPFGSIaLAHNGNLTNAEELREELEeEGAIFQTTSDTEVILHLiarELTKEDLEeaikeaLRRVK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 567931739 120 GIFAFCLYDEENdayLIG-RDHIGIIPLYTGHDEHGnFYVASE 161
Cdd:COG0034 163 GAYSLVILTGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
75-172 |
4.17e-07 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 50.91 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 75 NGEIYNHKELAAELEVD-FEFQTQSDCEVI---LALYKQKGPEFLD-------DLNGIFAFCLYDEENDAYLIG--RDHi 141
Cdd:cd00714 99 NGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkRLEGAYALAVISKDEPDEIVAarNGS- 177
|
90 100 110
....*....|....*....|....*....|.
gi 567931739 142 giiPLYTGHDEHGNFyVASELKALSPICKHI 172
Cdd:cd00714 178 ---PLVIGIGDGENF-VASDAPALLEHTRRV 204
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
28-168 |
1.83e-06 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 50.42 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 28 LRHRGPDWSG-VYSSEKAILVHERLAIV----------------------------GVSSGAQPLYNPEKTNILAV--NG 76
Cdd:PRK05793 39 LQHRGQESAGiAVSDGEKIKVHKGMGLVsevfskeklkglkgnsaighvrysttgaSDLDNAQPLVANYKLGSIAIahNG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 77 EIYNHKELAAELEVDFE-FQTQSDCEVILAL---YKQKGPEF-----LDDLNGIFAFCLYDEENdayLIG-RDHIGIIPL 146
Cdd:PRK05793 119 NLVNADVIRELLEDGGRiFQTSIDSEVILNLiarSAKKGLEKalvdaIQAIKGSYALVILTEDK---LIGvRDPHGIRPL 195
|
170 180
....*....|....*....|..
gi 567931739 147 YTGHDEhGNFYVASELKALSPI 168
Cdd:PRK05793 196 CLGKLG-DDYILSSESCALDTI 216
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
76-166 |
2.02e-05 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes the formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in the biosynthesis of clavulanic acid, a clinically important beta-lactamase inhibitor. CarA and beta-LS each have two distinct domains, an N-terminal Ntn hydrolase domain and a C-terminal synthetase domain, a domain architecture similar to that of the class-B asparagine synthetases (AS-B's). The N-terminal domain of these enzymes hydrolyzes glutamine to glutamate and ammonia. CarA forms a homotetramer while betaLS forms a heterodimer. The N-terminal folds of CarA and beta-LS are similar to those of other class II glutamine amidotransferases including lucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and glutamate synthase (GltS). This fold is also somwhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238890 [Multi-domain] Cd Length: 199 Bit Score: 45.56 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 76 GEIYNHKELAAELEV-DFEFQTQSDCEVILALYKQKGPEFLDDLNGIFAFcLYDEENDAYLIGRDHIGIIPLYTGHDehG 154
Cdd:cd01909 58 GELYNRDELRSLLGAgEGRSAVLGDAELLLLLLTRLGLHAFRLAEGDFCF-FIEDGNGRLTLATDHAGSVPVYLVQA--G 134
|
90
....*....|..
gi 567931739 155 NFYVASELKALS 166
Cdd:cd01909 135 EVWATTELKLLA 146
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
115-186 |
6.66e-05 |
|
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.
Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 44.28 E-value: 6.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567931739 115 LDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVASELKALSPIC-KHIEEFPPGHYLYSKNG 186
Cdd:pfam12481 126 VRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSLVFSDDIEIVKKGCgKSFAPFPKGCFFTSSGG 198
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-287 |
9.89e-05 |
|
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467489 [Multi-domain] Cd Length: 56 Bit Score: 40.15 E-value: 9.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 567931739 230 YGVLLSGGLDSSVISAITQRFAAKriedndesdaWWPKLHSFSVGLEGSPDLAAAQKV 287
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTS----------KAEEVVVVHVGEIVEIAKAEGVDM 48
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
115-191 |
3.03e-04 |
|
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of 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). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.
Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 42.30 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567931739 115 LDDLNGIFAFCLYDEENDAYLIGRDHIGIIPLYTGHDEHGNFYVASELKALSPIC-KHIEEFPPGhYLYSKNGELTPY 191
Cdd:cd01910 122 VKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCgKSFAPFPKG-CFFHSEGGLRSF 198
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
72-172 |
3.16e-04 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 43.49 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 72 LAV--NGEIYNHKELAAELE-VDFEFQTQSDCEVI---LALYKQKGPEFLD-------DLNGIFAFCLYDEENDayligr 138
Cdd:PRK00331 95 IAVvhNGIIENYAELKEELLaKGHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkRLEGAYALAVIDKDEP------ 168
|
90 100 110
....*....|....*....|....*....|....*....
gi 567931739 139 DHIgII-----PLYTGHDEHGNFyVASELKALSPICKHI 172
Cdd:PRK00331 169 DTI-VAarngsPLVIGLGEGENF-LASDALALLPYTRRV 205
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-180 |
1.27e-03 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including 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). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 40.71 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 2 CSIFGVLDiKSNATQLRTQAIEMSKLLRHRGPDWSG-----------VYSSEKAILV----------------------- 47
Cdd:cd01907 1 CGIFGIMS-KDGEPFVGALLVEMLDAMQERGPGDGAgfalygdpdafVYSSGKDMEVfkgvgypediarrydleeykgyh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 48 ---HERLAI--VGVSSGAQP--LYNpektnILAV-NGEIYNHKELAAELE---VDFEFQTQSDC------------EVIL 104
Cdd:cd01907 80 wiaHTRQPTnsAVWWYGAHPfsIGD-----IAVVhNGEISNYGSNREYLErfgYKFETETDTEViayyldlllrkgGLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931739 105 ALYK------QKGPEFL---------DDLNGIFAFCLYDEENDAYLigRDHIGIIPLYTGHDEhGNFYVASELKALSPIC 169
Cdd:cd01907 155 EYYKhiirmpEEERELLlalrltyrlADLDGPFTIIVGTPDGFIVI--RDRIKLRPAVVAETD-DYVAIASEECAIREIP 231
|
250
....*....|....*
gi 567931739 170 ----KHIEEFPPGHY 180
Cdd:cd01907 232 drdnAKVWEPRPGEY 246
|
|
| |
