|
Name |
Accession |
Description |
Interval |
E-value |
| ansA |
PRK09461 |
cytoplasmic asparaginase I; Provisional |
55-411 |
4.45e-131 |
|
cytoplasmic asparaginase I; Provisional
Pssm-ID: 181876 [Multi-domain] Cd Length: 335 Bit Score: 388.56 E-value: 4.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 134
Cdd:PRK09461 5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 135 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 214
Cdd:PRK09461 61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 215 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 294
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 295 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 373
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 193207372 374 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 411
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
|
|
| Asparaginase |
smart00870 |
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ... |
56-391 |
3.25e-114 |
|
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.
Pssm-ID: 214873 [Multi-domain] Cd Length: 323 Bit Score: 344.89 E-value: 3.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 134
Cdd:smart00870 1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 135 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 212
Cdd:smart00870 55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 213 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 287
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 288 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 366
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291
|
330 340
....*....|....*....|....*
gi 193207372 367 IGVIPGSDMTSEAAMAKLCYVLGKD 391
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
|
|
| AnsA |
COG0252 |
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ... |
55-390 |
6.70e-109 |
|
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];
Pssm-ID: 440022 [Multi-domain] Cd Length: 325 Bit Score: 331.33 E-value: 6.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 132
Cdd:COG0252 5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 133 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 211
Cdd:COG0252 57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 212 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 289
Cdd:COG0252 136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 290 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 369
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291
|
330 340
....*....|....*....|.
gi 193207372 370 IPGSDMTSEAAMAKLCYVLGK 390
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQ 312
|
|
| L-asparaginase_I |
cd08963 |
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ... |
55-390 |
1.88e-108 |
|
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.
Pssm-ID: 199207 [Multi-domain] Cd Length: 316 Bit Score: 329.92 E-value: 1.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 129
Cdd:cd08963 2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 130 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 209
Cdd:cd08963 49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 210 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 289
Cdd:cd08963 129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 290 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 368
Cdd:cd08963 207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285
|
330 340
....*....|....*....|..
gi 193207372 369 VIPGSDMTSEAAMAKLCYVLGK 390
Cdd:cd08963 286 VIPGGDMTTEAAVAKLMWLLGQ 307
|
|
| asnASE_I |
TIGR00519 |
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ... |
56-411 |
8.94e-92 |
|
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.
Pssm-ID: 129610 [Multi-domain] Cd Length: 336 Bit Score: 287.48 E-value: 8.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 133
Cdd:TIGR00519 4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 134 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 213
Cdd:TIGR00519 56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 214 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 280
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 281 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 359
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 193207372 360 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 411
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
|
|
| Asparaginase |
pfam00710 |
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme. |
56-266 |
3.31e-73 |
|
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
Pssm-ID: 459913 [Multi-domain] Cd Length: 188 Bit Score: 233.59 E-value: 3.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 132
Cdd:pfam00710 1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 133 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 212
Cdd:pfam00710 52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 193207372 213 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 266
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
442-641 |
8.39e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 107.73 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 442 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 521
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 522 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 601
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 193207372 602 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 641
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
454-602 |
7.78e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 74.90 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 533
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 534 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 602
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
484-609 |
1.23e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 484 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 563
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 193207372 564 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 609
Cdd:pfam12796 52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
479-508 |
1.66e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|
gi 193207372 479 NLRTALHVAASNGHLESVNYLLKIGTNVHI 508
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ansA |
PRK09461 |
cytoplasmic asparaginase I; Provisional |
55-411 |
4.45e-131 |
|
cytoplasmic asparaginase I; Provisional
Pssm-ID: 181876 [Multi-domain] Cd Length: 335 Bit Score: 388.56 E-value: 4.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 134
Cdd:PRK09461 5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 135 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 214
Cdd:PRK09461 61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 215 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 294
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 295 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 373
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 193207372 374 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 411
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
|
|
| Asparaginase |
smart00870 |
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ... |
56-391 |
3.25e-114 |
|
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.
Pssm-ID: 214873 [Multi-domain] Cd Length: 323 Bit Score: 344.89 E-value: 3.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 134
Cdd:smart00870 1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 135 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 212
Cdd:smart00870 55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 213 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 287
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 288 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 366
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291
|
330 340
....*....|....*....|....*
gi 193207372 367 IGVIPGSDMTSEAAMAKLCYVLGKD 391
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
|
|
| AnsA |
COG0252 |
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ... |
55-390 |
6.70e-109 |
|
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];
Pssm-ID: 440022 [Multi-domain] Cd Length: 325 Bit Score: 331.33 E-value: 6.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 132
Cdd:COG0252 5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 133 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 211
Cdd:COG0252 57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 212 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 289
Cdd:COG0252 136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 290 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 369
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291
|
330 340
....*....|....*....|.
gi 193207372 370 IPGSDMTSEAAMAKLCYVLGK 390
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQ 312
|
|
| L-asparaginase_I |
cd08963 |
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ... |
55-390 |
1.88e-108 |
|
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.
Pssm-ID: 199207 [Multi-domain] Cd Length: 316 Bit Score: 329.92 E-value: 1.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 129
Cdd:cd08963 2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 130 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 209
Cdd:cd08963 49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 210 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 289
Cdd:cd08963 129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 290 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 368
Cdd:cd08963 207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285
|
330 340
....*....|....*....|..
gi 193207372 369 VIPGSDMTSEAAMAKLCYVLGK 390
Cdd:cd08963 286 VIPGGDMTTEAAVAKLMWLLGQ 307
|
|
| asnASE_I |
TIGR00519 |
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ... |
56-411 |
8.94e-92 |
|
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.
Pssm-ID: 129610 [Multi-domain] Cd Length: 336 Bit Score: 287.48 E-value: 8.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 133
Cdd:TIGR00519 4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 134 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 213
Cdd:TIGR00519 56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 214 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 280
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 281 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 359
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 193207372 360 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 411
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
|
|
| Asparaginase |
pfam00710 |
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme. |
56-266 |
3.31e-73 |
|
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
Pssm-ID: 459913 [Multi-domain] Cd Length: 188 Bit Score: 233.59 E-value: 3.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 56 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 132
Cdd:pfam00710 1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 133 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 212
Cdd:pfam00710 52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 193207372 213 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 266
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
|
|
| gatD_arch |
TIGR02153 |
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ... |
22-411 |
3.47e-62 |
|
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It is part of a heterodimer, with GatE (TIGR00134), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln). The analogous amidotransferase found in bacteria is the GatABC system, although GatABC homologs in the Archaea appear to act instead on Asp-tRNA(Asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 274001 [Multi-domain] Cd Length: 404 Bit Score: 211.85 E-value: 3.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 22 IVILKGSIEELVL--EVQETAGTQQIGAPSALPE-SRVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDr 94
Cdd:TIGR02153 28 IGFKISEIRNIEVleEGSEPREVPPPAEIEKKPGlPKVSIISTGGTIASRVdyeTGAVY---PAFTAEeLARAVPELLE- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 95 ryieesysnvavrpyslppVRNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTAS 173
Cdd:TIGR02153 104 -------------------IANIKARAVFNIL-------SENMKPEYWIKIAEAVAKALKEgADGVVVAHGTDTMAYTAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 174 ALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAGNfDIPEVCVYFNNK-------LMRGNRTVKLDNSALEAF 246
Cdd:TIGR02153 158 ALSFMFETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATS-PIAEVTVVMHGEtsdtyclVHRGVKVRKMHTSRRDAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 247 DSPNMHPLAQMAINIKVNY---DSIFRSDMVAAFTvhENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMP 323
Cdd:TIGR02153 237 QSINDIPIAKIDPDEGIEKlriDYRRRGEKELELD--DKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 324 TrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSML 402
Cdd:TIGR02153 315 E---DWIPSIKRATDDGVPVVMTSQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMM 390
|
....*....
gi 193207372 403 QSNLRGEMT 411
Cdd:TIGR02153 391 RTNIAGEIN 399
|
|
| GatD |
cd08962 |
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ... |
5-406 |
4.08e-59 |
|
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain.
Pssm-ID: 199206 [Multi-domain] Cd Length: 402 Bit Score: 203.62 E-value: 4.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 5 GVLYPaftsSPLFVEDPIVILK---G-----SIEELVLEVQETAGTQQIGAPSALPES----RVLVLYTGGTIGMKT--- 69
Cdd:cd08962 14 GILMP----RPELSDDDIIVLKldnGynigiDISIEEIELIEKGEKPKPELGEEIEKKpglpKVSIISTGGTIASRVdyr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 70 TDGVYcpvPGYLPE-VLRDIPPLNDrryieesysnvavrpyslppvrnmkkrvvYWIVEYEPLLD--SCDMTFDDWIRIA 146
Cdd:cd08962 90 TGAVS---PAFTAEeLLRAIPELLD-----------------------------IANIKAEVLFNilSENMTPEYWVKIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 147 TDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAGNfDIPEVCVYF 225
Cdd:cd08962 138 EAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLVAAS-DIAEVVVVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 226 NNK-------LMRGNRTVKLDNSALEAFDSPNMHPLAQMAIN---IKVNYDSIFRSDmvAAFTVHENLCRDVGMLRIFPS 295
Cdd:cd08962 217 HGTtsddyclLHRGTRVRKMHTSRRDAFQSINDEPLAKVDPPgkiEKLSKDYRKRGD--EELELNDKLEEKVALIKFYPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 296 MTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSD 374
Cdd:cd08962 295 MDPEIIDFYVDKGYKGIVIEGTGLGHVSE---DLIPSIKKAIDDGIPVVMTSQCIYGRVNLNvYSTGRELLKAGVIPGED 371
|
410 420 430
....*....|....*....|....*....|..
gi 193207372 375 MTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNL 406
Cdd:cd08962 372 MLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
|
|
| PRK04183 |
PRK04183 |
Glu-tRNA(Gln) amidotransferase subunit GatD; |
19-411 |
6.56e-59 |
|
Glu-tRNA(Gln) amidotransferase subunit GatD;
Pssm-ID: 235245 [Multi-domain] Cd Length: 419 Bit Score: 203.54 E-value: 6.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 19 EDPIVILK---G-----SIEELV-LEVQETAGTQQIGAPSALPES-----RVLVLYTGGTIGMKT---TDGVYcpvPGYL 81
Cdd:PRK04183 27 EDDHIVIKldnGynigiDIDKIAeIELLEKGEKPKQEPPPKEIEKdpglpNVSILSTGGTIASKVdyrTGAVT---PAFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 82 PE-VLRDIPPLNDRRyieesysnvavrpyslppvrNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGF 159
Cdd:PRK04183 104 AEdLLRAVPELLDIA--------------------NIRGRVLFNIL-------SENMTPEYWVEIAEAVYEEIKNgADGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 160 VVLHGTDTLAYTASALSFMMeNLGKPVIITGSQipvaevRS------DGMENLIGALITAGNfDIPEVCVyfnnkLM--- 230
Cdd:PRK04183 157 VVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQ------RSsdrpssDAAMNLICAVLAATS-DIAEVVV-----VMhgt 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 231 ---------RGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDS----IFRSDMV----AAFTVHENLCRDVGMLRIF 293
Cdd:PRK04183 224 tsddycalhRGTRVRKMHTSRRDAFQSINDKPLA------KVDYKEgkieFLRKDYRkrgeKELELNDKLEEKVALIKFY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 294 PSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPG 372
Cdd:PRK04183 298 PGMDPEILDFYVDKGYKGIVIEGTGLGHVST---DLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPG 374
|
410 420 430
....*....|....*....|....*....|....*....
gi 193207372 373 SDMTSEAAMAKLCYVLGKdEWDLPMKRSMLQSNLRGEMT 411
Cdd:PRK04183 375 EDMLPEVAYVKLMWVLGN-TYDLEEVRELMLTNLAGEIN 412
|
|
| L-asparaginase_II |
cd08964 |
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ... |
55-390 |
3.29e-42 |
|
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase.
Pssm-ID: 199208 [Multi-domain] Cd Length: 319 Bit Score: 154.98 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTIGMKTTDGVYCPVPGyLP--EVLRDIPPLNDrryieesYSNVAVRPyslppVRNmkkrvvywiveyeplL 132
Cdd:cd08964 2 RIAVLATGGTIAGTADSSGAYAAPT-LSgeELLAAVPGLAD-------VADVEVEQ-----VSN---------------L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 133 DSCDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGAL 210
Cdd:cd08964 54 PSSDMTPADWLALAARVNEALADpdVDGVVVTHGTDTLEETAYFLD-LTLDSDKPVVLTGAMRPADAPSADGPANLLDAV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 211 ITAGNfdiPE-----VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENlcR 285
Cdd:cd08964 133 RVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDEL--P 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 286 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVNYA--TGKI 363
Cdd:cd08964 208 RVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP---PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGAD 284
|
330 340
....*....|....*....|....*..
gi 193207372 364 LYDIGVIPGSDMTSEAAMAKLCYVLGK 390
Cdd:cd08964 285 LAEAGAIFAGDLSPQKARILLMLALAA 311
|
|
| L-asparaginase_like |
cd00411 |
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ... |
55-390 |
6.09e-42 |
|
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase.
Pssm-ID: 199205 [Multi-domain] Cd Length: 320 Bit Score: 154.59 E-value: 6.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 55 RVLVLYTGGTI-GMKTTDGVYCPVPGYL--PEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVYWIveyepl 131
Cdd:cd00411 2 NITILATGGTIaGVGDSATYSAYVAGALgvEKLIKAVPELKE--------------------LANVKGEQLMNI------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 132 lDSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGAL 210
Cdd:cd00411 56 -ASEDITPDDWLKLAKEVAKLLDSdVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 211 ITAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENLCRD-- 286
Cdd:cd00411 134 RVAKDKDsrGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDESEFDVSDIKSLpk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 287 VGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNyaTGKILYD 366
Cdd:cd00411 214 VDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPY---DVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLK 288
|
330 340
....*....|....*....|....
gi 193207372 367 IGVIPGSDMTSEAAMAKLCYVLGK 390
Cdd:cd00411 289 AGVIPAGDLNPEKARVLLMWALTH 312
|
|
| Asparaginase_C |
pfam17763 |
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ... |
286-390 |
1.07e-30 |
|
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of asparaginase enzymes.
Pssm-ID: 465490 [Multi-domain] Cd Length: 114 Bit Score: 116.04 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 286 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKIL 364
Cdd:pfam17763 1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVPS---ALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDL 77
|
90 100
....*....|....*....|....*.
gi 193207372 365 YDIGVIPGSDMTSEAAMAKLCYVLGK 390
Cdd:pfam17763 78 LEAGVISGGDLTPEKARIKLMLALGK 103
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
442-641 |
8.39e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 107.73 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 442 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 521
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 522 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 601
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 193207372 602 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 641
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
|
| ansB |
PRK11096 |
L-asparaginase II; Provisional |
134-347 |
1.62e-20 |
|
L-asparaginase II; Provisional
Pssm-ID: 182958 [Multi-domain] Cd Length: 347 Bit Score: 93.24 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 134 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITA 213
Cdd:PRK11096 79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 214 GNFDIPE--VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAiNIKVNYDSIFRSDMV--AAFTV-HENLCRDVG 288
Cdd:PRK11096 158 ADKASANrgVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIH-NGKVDYQRTPARKHTtdTPFDVsKLNELPKVG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 193207372 289 MLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMptrRQDIIMALKEAIARGVMVVNCS 347
Cdd:PRK11096 237 IVYNYANASDLPAKALVDAGYDGIVSAGVGNGNL---YKTVFDTLATAAKNGVAVVRSS 292
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
454-616 |
1.63e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 86.55 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 533
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 534 DAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGI 613
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
...
gi 193207372 614 TPM 616
Cdd:COG0666 287 TLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
441-636 |
5.05e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 81.92 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 441 LLRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCA 520
Cdd:COG0666 15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 521 VKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQ 600
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 193207372 601 CGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQA 636
Cdd:COG0666 175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
454-602 |
7.78e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 74.90 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 533
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 534 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 602
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
460-640 |
1.08e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.91 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 460 VEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFI 539
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 540 DASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 619
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180
....*....|....*....|.
gi 193207372 620 KRRNLQNLMDMMAEHQALTNN 640
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNA 181
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
484-609 |
1.23e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 484 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 563
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 193207372 564 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 609
Cdd:pfam12796 52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
456-623 |
1.24e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.08 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 456 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASN--GHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIA-- 531
Cdd:PHA03100 82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 532 IRDAGGFIDAsaqKIGVELCLAVyqndmellkcneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDF 611
Cdd:PHA03100 162 LIDKGVDINA---KNRVNYLLSY--------------GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
|
170
....*....|..
gi 193207372 612 GITPMDEAKRRN 623
Cdd:PHA03100 225 GDTPLHIAILNN 236
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
454-541 |
6.31e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.97 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGtNVHIKDMfGYNALVCAVKAKAMDCIIAIR 533
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLL 81
|
....*...
gi 193207372 534 DAGGFIDA 541
Cdd:pfam12796 82 EKGADINV 89
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
424-619 |
1.19e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.67 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 424 IPH-IAKCLRVSSSQEVQLLRD-----IILP-PMFCNaaktndvEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESV 496
Cdd:PHA02874 68 IPHpLLTAIKIGAHDIIKLLIDngvdtSILPiPCIEK-------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 497 NYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKD 576
Cdd:PHA02874 141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 193207372 577 YDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDdfGITPMDEA 619
Cdd:PHA02874 221 KNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHA 261
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
454-500 |
1.40e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 1.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLL 500
Cdd:pfam13637 8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
449-602 |
1.40e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.77 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 449 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAAS-NGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMD 527
Cdd:PHA02876 310 PLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193207372 528 CIIAIRDAGGFIDASAQKIGVELCLAVY-QNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLN-KPEIVAYLLQCG 602
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
456-616 |
2.47e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.00 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 456 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 535
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 536 GGFIDasaqKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAA---SLNKpeIVAYLLQCGLNPHEKDDFG 612
Cdd:PHA02876 234 RSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqapSLSR--LVPKLLERGADVNAKNIKG 307
|
....
gi 193207372 613 ITPM 616
Cdd:PHA02876 308 ETPL 311
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
454-510 |
3.12e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 3.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 193207372 454 AAKTNDVEILKSLkAAGVNFSATDYNlRTALHVAASNGHLESVNYLLKIGTNVHIKD 510
Cdd:pfam12796 37 AAKNGHLEIVKLL-LEHADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
550-636 |
2.67e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 550 LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNphEKDDFGITPMDEAKRRNLQNLMD 629
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
....*..
gi 193207372 630 MMAEHQA 636
Cdd:pfam12796 79 LLLEKGA 85
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
449-616 |
3.07e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 449 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNG--HLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAM 526
Cdd:PHA03095 86 PLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 527 dciiairdaggfidasaqkigvelclavyqnDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKP--EIVAYLLQCGLN 604
Cdd:PHA03095 166 -------------------------------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCD 214
|
170
....*....|..
gi 193207372 605 PHEKDDFGITPM 616
Cdd:PHA03095 215 PAATDMLGNTPL 226
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
451-639 |
5.81e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 451 FCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTN-------VHIKDMFGYNALVCAvKA 523
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfytlVAIKDAFNNRNVEIF-KI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 524 KAMDCIIAIRDaggfIDAsaqkigVELCLAVYQNDMEL----LKCNEAAGTHMGEKDYDNrTALHVAASLNKPEIVAYLL 599
Cdd:PHA02878 120 ILTNRYKNIQT----IDL------VYIDKKSKDDIIEAeitkLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 193207372 600 QCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 639
Cdd:PHA02878 189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
450-506 |
1.64e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.94 E-value: 1.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 193207372 450 MFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNV 506
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
459-619 |
2.04e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.57 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 459 DVEILKSLKAAGVNFSATDYN-LRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGG 537
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 538 FIDASAQKIGVELCLAV-YQNDMELLKCNEAAGTHMGEKDY-DNRTALHVaaSLNKPEIVAYLLQCGLNPHEKDDFGITP 615
Cdd:PHA02878 226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTP 303
|
....
gi 193207372 616 MDEA 619
Cdd:PHA02878 304 LSSA 307
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
583-642 |
2.34e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.18 E-value: 2.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 583 LHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNNDE 642
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
543-634 |
3.32e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 543 AQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRR 622
Cdd:PTZ00322 79 AHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90
....*....|..
gi 193207372 623 NLQNLMDMMAEH 634
Cdd:PTZ00322 159 GFREVVQLLSRH 170
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
455-617 |
3.62e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.56 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 455 AKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGH---LESVNYLLKIGTNVHIKDMFGYNALvcavkakamdciia 531
Cdd:PHA03095 22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL-------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 532 irdaggfidasaqkigveLCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHV-AASLN-KPEIVAYLLQCGLNPHEKD 609
Cdd:PHA03095 88 ------------------HLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALD 149
|
....*...
gi 193207372 610 DFGITPMD 617
Cdd:PHA03095 150 LYGMTPLA 157
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
481-529 |
3.65e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 3.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 193207372 481 RTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCI 529
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
479-510 |
4.51e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 4.51e-05
10 20 30
....*....|....*....|....*....|...
gi 193207372 479 NLRTALHVAA-SNGHLESVNYLLKIGTNVHIKD 510
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
575-619 |
5.00e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 5.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 193207372 575 KDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 619
Cdd:pfam13857 12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
579-619 |
5.41e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 5.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 193207372 579 NRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 619
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
475-517 |
5.96e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 5.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 193207372 475 ATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNAL 517
Cdd:pfam13857 11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
479-508 |
1.66e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|
gi 193207372 479 NLRTALHVAASNGHLESVNYLLKIGTNVHI 508
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
578-610 |
4.96e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 4.96e-04
10 20 30
....*....|....*....|....*....|....
gi 193207372 578 DNRTALHVAA-SLNKPEIVAYLLQCGLNPHEKDD 610
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
479-639 |
5.18e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.06 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 479 NLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQND 558
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 559 MELLKCNEAAGTHMGEKDY-DNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQAL 637
Cdd:PHA02875 81 VKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
..
gi 193207372 638 TN 639
Cdd:PHA02875 161 LD 162
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
454-563 |
7.52e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 454 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 533
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
|
90 100 110
....*....|....*....|....*....|.
gi 193207372 534 DAGGFIDASAQKIGVE-LCLAVYQNDMELLK 563
Cdd:PHA02875 189 DSGANIDYFGKNGCVAaLCYAIENNKIDIVR 219
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
456-561 |
1.24e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.57 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 456 KTNDVEILKSLkaaGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 535
Cdd:PHA03100 171 AKNRVNYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
|
90 100
....*....|....*....|....*.
gi 193207372 536 GGFIDASAQKIgvelclaVYQNDMEL 561
Cdd:PHA03100 248 GPSIKTIIETL-------LYFKDKDL 266
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
578-607 |
1.34e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|
gi 193207372 578 DNRTALHVAASLNKPEIVAYLLQCGLNPHE 607
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
452-522 |
2.62e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207372 452 CNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVK 522
Cdd:PTZ00322 87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
481-508 |
3.57e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 3.57e-03
10 20
....*....|....*....|....*...
gi 193207372 481 RTALHVAASNGHLESVNYLLKIGTNVHI 508
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
482-639 |
3.85e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 40.33 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 482 TALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGgfIDASAQKIGvelCLavyQNDM-- 559
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSILPIP---CI---EKDMik 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207372 560 ELLKCneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 639
Cdd:PHA02874 109 TILDC----GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
|
| |
