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Conserved domains on  [gi|17558278|ref|NP_506049|]
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asparaginase [Caenorhabditis elegans]

Protein Classification

L-asparaginase family protein( domain architecture ID 13049359)

L-asparaginase family protein containing ankyrin (ANK) repeats, may catalyze the deamination of asparagine to yield aspartic acid and ammonium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
L-asparaginase_like super family cl00216
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 121-477 8.41e-131

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.


The actual alignment was detected with superfamily member PRK09461:

Pssm-ID: 469665 [Multi-domain]  Cd Length: 335  Bit Score: 390.10  E-value: 8.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  121 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 200
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  201 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 280
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  281 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 360
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  361 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 439
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 17558278  440 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 477
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
508-707 2.88e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 508 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 587
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 588 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 667
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17558278 668 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 707
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 121-477 8.41e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 390.10  E-value: 8.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  121 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 200
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  201 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 280
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  281 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 360
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  361 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 439
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 17558278  440 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 477
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 122-457 6.28e-115

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: 348.74  E-value: 6.28e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    122 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 200
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    201 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 278
Cdd:smart00870  55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    279 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 353
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    354 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 432
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291

                          330       340
                   ....*....|....*....|....*
gi 17558278    433 IGVIPGSDMTSEAAMAKLCYVLGKD 457
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 121-456 1.59e-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: 334.79  E-value: 1.59e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 198
Cdd:COG0252   5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 199 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 277
Cdd:COG0252  57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 278 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 355
Cdd:COG0252 136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 356 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 435
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                       330       340
                ....*....|....*....|.
gi 17558278 436 IPGSDMTSEAAMAKLCYVLGK 456
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQ 312
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 121-456 1.74e-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: 331.85  E-value: 1.74e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 195
Cdd:cd08963   2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 196 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 275
Cdd:cd08963  49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 276 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 355
Cdd:cd08963 129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 356 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 434
Cdd:cd08963 207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285

                       330       340
                ....*....|....*....|..
gi 17558278 435 VIPGSDMTSEAAMAKLCYVLGK 456
Cdd:cd08963 286 VIPGGDMTTEAAVAKLMWLLGQ 307
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 122-477 6.68e-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: 289.80  E-value: 6.68e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   122 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 199
Cdd:TIGR00519   4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   200 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 279
Cdd:TIGR00519  56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   280 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 346
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   347 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 425
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17558278   426 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 477
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 122-332 1.73e-73

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 235.90  E-value: 1.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   122 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 198
Cdd:pfam00710   1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   199 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 278
Cdd:pfam00710  52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558278   279 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 332
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
508-707 2.88e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 508 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 587
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 588 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 667
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17558278 668 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 707
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 520-668 8.68e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 599
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  600 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 668
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
Ank_2 pfam12796
Ankyrin repeats (3 copies);
550-675 8.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   550 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 629
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 17558278   630 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 675
Cdd:pfam12796  52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 545-574 1.63e-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: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 17558278    545 NLRTALHVAASNGHLESVNYLLKIGTNVHI 574
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 121-477 8.41e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 390.10  E-value: 8.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  121 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 200
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  201 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 280
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  281 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 360
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  361 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 439
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 17558278  440 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 477
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 122-457 6.28e-115

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: 348.74  E-value: 6.28e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    122 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 200
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    201 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 278
Cdd:smart00870  55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    279 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 353
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    354 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 432
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291

                          330       340
                   ....*....|....*....|....*
gi 17558278    433 IGVIPGSDMTSEAAMAKLCYVLGKD 457
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 121-456 1.59e-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: 334.79  E-value: 1.59e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 198
Cdd:COG0252   5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 199 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 277
Cdd:COG0252  57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 278 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 355
Cdd:COG0252 136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 356 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 435
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                       330       340
                ....*....|....*....|.
gi 17558278 436 IPGSDMTSEAAMAKLCYVLGK 456
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQ 312
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 121-456 1.74e-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: 331.85  E-value: 1.74e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 195
Cdd:cd08963   2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 196 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 275
Cdd:cd08963  49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 276 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 355
Cdd:cd08963 129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 356 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 434
Cdd:cd08963 207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285

                       330       340
                ....*....|....*....|..
gi 17558278 435 VIPGSDMTSEAAMAKLCYVLGK 456
Cdd:cd08963 286 VIPGGDMTTEAAVAKLMWLLGQ 307
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 122-477 6.68e-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: 289.80  E-value: 6.68e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   122 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 199
Cdd:TIGR00519   4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   200 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 279
Cdd:TIGR00519  56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   280 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 346
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   347 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 425
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17558278   426 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 477
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 122-332 1.73e-73

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 235.90  E-value: 1.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   122 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 198
Cdd:pfam00710   1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   199 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 278
Cdd:pfam00710  52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558278   279 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 332
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 92-477 3.90e-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: 213.01  E-value: 3.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278    92 NISATELVLEVQETAGTQQIGAPSALPE-SRVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDrryiees 166
Cdd:TIGR02153  34 EIRNIEVLEEGSEPREVPPPAEIEKKPGlPKVSIISTGGTIASRVdyeTGAVY---PAFTAEeLARAVPELLE------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   167 ysnvavrpyslppVRNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMM 245
Cdd:TIGR02153 104 -------------IANIKARAVFNIL-------SENMKPEYWIKIAEAVAKALKEgADGVVVAHGTDTMAYTAAALSFMF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   246 ENLGKPVIITGSQIPVAEVRSDGMENLIGALITAGNfDIPEVCVYFNNK-------LMRGNRTVKLDNSALEAFDSPNMH 318
Cdd:TIGR02153 164 ETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATS-PIAEVTVVMHGEtsdtyclVHRGVKVRKMHTSRRDAFQSINDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   319 PLAQMAINIKVNY---DSIFRSDMVAAFTvhENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDI 395
Cdd:TIGR02153 243 PIAKIDPDEGIEKlriDYRRRGEKELELD--DKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVSE---DW 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   396 IMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRG 474
Cdd:TIGR02153 318 IPSIKRATDDGVPVVMTSQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAG 396


                  ...
gi 17558278   475 EMT 477
Cdd:TIGR02153 397 EIN 399
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
100-477 1.70e-58

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 203.92  E-value: 1.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  100 LEVQETAGTQQIGAPSALPES-----RVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDRRyieesysnv 170
Cdd:PRK04183  51 IELLEKGEKPKQEPPPKEIEKdpglpNVSILSTGGTIASKVdyrTGAVT---PAFTAEdLLRAVPELLDIA--------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  171 avrpyslppvrNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMeNLG 249
Cdd:PRK04183 119 -----------NIRGRVLFNIL-------SENMTPEYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  250 KPVIITGSQipvaevRS------DGMENLIGALITAGNfDIPEVCVyfnnkLM------------RGNRTVKLDNSALEA 311
Cdd:PRK04183 180 VPIVFVGAQ------RSsdrpssDAAMNLICAVLAATS-DIAEVVV-----VMhgttsddycalhRGTRVRKMHTSRRDA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  312 FDSPNMHPLAqmainiKVNYDS----IFRSDMV----AAFTVHENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTF 383
Cdd:PRK04183 248 FQSINDKPLA------KVDYKEgkieFLRKDYRkrgeKELELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIEGT 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  384 GSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKdEWDLP 462
Cdd:PRK04183 322 GLGHVST---DLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGN-TYDLE 397

                        410
                 ....*....|....*
gi 17558278  463 MKRSMLQSNLRGEMT 477
Cdd:PRK04183 398 EVRELMLTNLAGEIN 412
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 121-472 6.51e-58

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: 201.69  E-value: 6.51e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDrryieesysnvavrpyslppvrnmkkrvvYWIVEYEP 196
Cdd:cd08962  72 KVSIISTGGTIASRVdyrTGAVS---PAFTAEeLLRAIPELLD-----------------------------IANIKAEV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 197 LLD--SCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLI 273
Cdd:cd08962 120 LFNilSENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLI 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 274 GALITAGNfDIPEVCVYFNNK-------LMRGNRTVKLDNSALEAFDSPNMHPLAQMAIN---IKVNYDSIFRSDmvAAF 343
Cdd:cd08962 200 AAVLVAAS-DIAEVVVVMHGTtsddyclLHRGTRVRKMHTSRRDAFQSINDEPLAKVDPPgkiEKLSKDYRKRGD--EEL 276

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 344 TVHENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN 423
Cdd:cd08962 277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIEGTGLGHVSE---DLIPSIKKAIDDGIPVVMTSQCIYGRVNLN 353

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17558278 424 -YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNL 472
Cdd:cd08962 354 vYSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 121-456 7.97e-43

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: 157.67  E-value: 7.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTIGMKTTDGVYCPVPGyLP--EVLRDIPPLNDrryieesYSNVAVRPyslppVRNmkkrvvywiveyeplL 198
Cdd:cd08964   2 RIAVLATGGTIAGTADSSGAYAAPT-LSgeELLAAVPGLAD-------VADVEVEQ-----VSN---------------L 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 199 DSCDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGAL 276
Cdd:cd08964  54 PSSDMTPADWLALAARVNEALADpdVDGVVVTHGTDTLEETAYFLD-LTLDSDKPVVLTGAMRPADAPSADGPANLLDAV 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 277 ITAGNfdiPE-----VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENlcR 351
Cdd:cd08964 133 RVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDEL--P 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 352 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVNYA--TGKI 429
Cdd:cd08964 208 RVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP---PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGAD 284

                       330       340
                ....*....|....*....|....*..
gi 17558278 430 LYDIGVIPGSDMTSEAAMAKLCYVLGK 456
Cdd:cd08964 285 LAEAGAIFAGDLSPQKARILLMLALAA 311
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 121-456 8.14e-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: 154.98  E-value: 8.14e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 121 RVLVLYTGGTI-GMKTTDGVYCPVPGYL--PEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVYWIveyepl 197
Cdd:cd00411   2 NITILATGGTIaGVGDSATYSAYVAGALgvEKLIKAVPELKE--------------------LANVKGEQLMNI------ 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 198 lDSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGAL 276
Cdd:cd00411  56 -ASEDITPDDWLKLAKEVAKLLDSdVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAV 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 277 ITAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENLCRD-- 352
Cdd:cd00411 134 RVAKDKDsrGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDESEFDVSDIKSLpk 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 353 VGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNyaTGKILYD 432
Cdd:cd00411 214 VDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPY---DVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLK 288

                       330       340
                ....*....|....*....|....
gi 17558278 433 IGVIPGSDMTSEAAMAKLCYVLGK 456
Cdd:cd00411 289 AGVIPAGDLNPEKARVLLMWALTH 312
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 352-456 3.60e-31

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: 117.58  E-value: 3.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   352 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKIL 430
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVPS---ALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDL 77

                          90       100
                  ....*....|....*....|....*.
gi 17558278   431 YDIGVIPGSDMTSEAAMAKLCYVLGK 456
Cdd:pfam17763  78 LEAGVISGGDLTPEKARIKLMLALGK 103
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
508-707 2.88e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 508 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 587
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 588 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 667
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17558278 668 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 707
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
ansB PRK11096
L-asparaginase II; Provisional
 200-413 1.90e-20

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 93.24  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  200 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITA 279
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  280 GNFDIPE--VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAiNIKVNYDSIFRSDMV--AAFTV-HENLCRDVG 354
Cdd:PRK11096 158 ADKASANrgVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIH-NGKVDYQRTPARKHTtdTPFDVsKLNELPKVG 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17558278  355 MLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMptrRQDIIMALKEAIARGVMVVNCS 413
Cdd:PRK11096 237 IVYNYANASDLPAKALVDAGYDGIVSAGVGNGNL---YKTVFDTLATAAKNGVAVVRSS 292
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-682 7.98e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 7.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 599
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 600 DAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGI 679
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                ...
gi 17558278 680 TPM 682
Cdd:COG0666 287 TLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-702 2.59e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 2.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 507 LLRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCA 586
Cdd:COG0666  15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 587 VKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQ 666
Cdd:COG0666  95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17558278 667 CGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQA 702
Cdd:COG0666 175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
526-706 6.53e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.06  E-value: 6.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 526 VEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFI 605
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278 606 DASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 685
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                       170       180
                ....*....|....*....|.
gi 17558278 686 KRRNLQNLMDMMAEHQALTNN 706
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNA 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 520-668 8.68e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 599
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  600 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 668
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
Ank_2 pfam12796
Ankyrin repeats (3 copies);
550-675 8.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   550 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 629
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 17558278   630 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 675
Cdd:pfam12796  52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 522-689 1.32e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  522 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASN--GHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIA-- 597
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkl 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  598 IRDAGGFIDAsaqKIGVELCLAVyqndmellkcneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDF 677
Cdd:PHA03100 162 LIDKGVDINA---KNRVNYLLSY--------------GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224

                        170
                 ....*....|..
gi 17558278  678 GITPMDEAKRRN 689
Cdd:PHA03100 225 GDTPLHIAILNN 236
Ank_2 pfam12796
Ankyrin repeats (3 copies);
520-607 4.73e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 4.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGtNVHIKDMfGYNALVCAVKAKAMDCIIAIR 599
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                  ....*...
gi 17558278   600 DAGGFIDA 607
Cdd:pfam12796  82 EKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 490-685 1.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  490 IPH-IAKCLRVSSSQEVQLLRD-----IILP-PMFCNaaktndvEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESV 562
Cdd:PHA02874  68 IPHpLLTAIKIGAHDIIKLLIDngvdtSILPiPCIEK-------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  563 NYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKD 642
Cdd:PHA02874 141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17558278  643 YDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDdfGITPMDEA 685
Cdd:PHA02874 221 KNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
520-566 1.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.56e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17558278   520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLL 566
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 515-668 1.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  515 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAAS-NGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMD 593
Cdd:PHA02876 310 PLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17558278  594 CIIAIRDAGGFIDASAQKIGVELCLAVY-QNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLN-KPEIVAYLLQCG 668
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
Ank_2 pfam12796
Ankyrin repeats (3 copies);
520-576 2.56e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558278   520 AAKTNDVEILKSLkAAGVNFSATDYNlRTALHVAASNGHLESVNYLLKIGTNVHIKD 576
Cdd:pfam12796  37 AAKNGHLEIVKLL-LEHADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 522-682 2.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  522 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 601
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  602 GGFIDasaqKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAA---SLNKpeIVAYLLQCGLNPHEKDDFG 678
Cdd:PHA02876 234 RSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqapSLSR--LVPKLLERGADVNAKNIKG 307


                 ....
gi 17558278  679 ITPM 682
Cdd:PHA02876 308 ETPL 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
616-702 2.21e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   616 LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNphEKDDFGITPMDEAKRRNLQNLMD 695
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                  ....*..
gi 17558278   696 MMAEHQA 702
Cdd:pfam12796  79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 515-682 2.67e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  515 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNG--HLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAM 592
Cdd:PHA03095  86 PLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  593 dciiairdaggfidasaqkigvelclavyqnDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKP--EIVAYLLQCGLN 670
Cdd:PHA03095 166 -------------------------------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCD 214

                        170
                 ....*....|..
gi 17558278  671 PHEKDDFGITPM 682
Cdd:PHA03095 215 PAATDMLGNTPL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 517-705 7.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  517 FCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTN-------VHIKDMFGYNALVCAvKA 589
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfytlVAIKDAFNNRNVEIF-KI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  590 KAMDCIIAIRDaggfIDAsaqkigVELCLAVYQNDMEL----LKCNEAAGTHMGEKDYDNrTALHVAASLNKPEIVAYLL 665
Cdd:PHA02878 120 ILTNRYKNIQT----IDL------VYIDKKSKDDIIEAeitkLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 17558278  666 QCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 705
Cdd:PHA02878 189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 516-572 1.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 1.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17558278  516 MFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNV 572
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
649-708 2.15e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 2.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278   649 LHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNNDE 708
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 525-685 2.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  525 DVEILKSLKAAGVNFSATDYN-LRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGG 603
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  604 FIDASAQKIGVELCLAV-YQNDMELLKCNEAAGTHMGEKDY-DNRTALHVaaSLNKPEIVAYLLQCGLNPHEKDDFGITP 681
Cdd:PHA02878 226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTP 303


                 ....
gi 17558278  682 MDEA 685
Cdd:PHA02878 304 LSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 521-683 3.30e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  521 AKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGH---LESVNYLLKIGTNVHIKDMFGYNALvcavkakamdciia 597
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL-------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  598 irdaggfidasaqkigveLCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHV-AASLN-KPEIVAYLLQCGLNPHEKD 675
Cdd:PHA03095  88 ------------------HLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALD 149


                 ....*...
gi 17558278  676 DFGITPMD 683
Cdd:PHA03095 150 LYGMTPLA 157
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 609-700 3.99e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  609 AQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRR 688
Cdd:PTZ00322  79 AHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                         90
                 ....*....|..
gi 17558278  689 NLQNLMDMMAEH 700
Cdd:PTZ00322 159 GFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
547-595 4.11e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17558278   547 RTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCI 595
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank_5 pfam13857
Ankyrin repeats (many copies);
641-685 4.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17558278   641 KDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 685
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 545-576 4.46e-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: 4.46e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 17558278   545 NLRTALHVAA-SNGHLESVNYLLKIGTNVHIKD 576
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
541-583 5.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 5.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 17558278   541 ATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNAL 583
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
645-685 6.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 6.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17558278   645 NRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 685
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 545-574 1.63e-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: 1.63e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 17558278    545 NLRTALHVAASNGHLESVNYLLKIGTNVHI 574
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 644-676 5.00e-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: 38.04  E-value: 5.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 17558278   644 DNRTALHVAA-SLNKPEIVAYLLQCGLNPHEKDD 676
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 545-705 5.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  545 NLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQND 624
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  625 MELLKCNEAAGTHMGEKDY-DNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQAL 703
Cdd:PHA02875  81 VKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160


                 ..
gi 17558278  704 TN 705
Cdd:PHA02875 161 LD 162
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 520-629 7.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  520 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 599
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17558278  600 DAGGFIDASAQKIGVE-LCLAVYQNDMELLK 629
Cdd:PHA02875 189 DSGANIDYFGKNGCVAaLCYAIENNKIDIVR 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 522-627 1.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  522 KTNDVEILKSLkaaGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 601
Cdd:PHA03100 171 AKNRVNYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247

                         90       100
                 ....*....|....*....|....*.
gi 17558278  602 GGFIDASAQKIgvelclaVYQNDMEL 627
Cdd:PHA03100 248 GPSIKTIIETL-------LYFKDKDL 266
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 644-673 1.37e-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: 1.37e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 17558278   644 DNRTALHVAASLNKPEIVAYLLQCGLNPHE 673
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 518-588 3.12e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17558278  518 CNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVK 588
Cdd:PTZ00322  87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 547-574 3.75e-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: 3.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 17558278   547 RTALHVAASNGHLESVNYLLKIGTNVHI 574
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 548-705 3.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  548 TALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGgfIDASAQKIGvelCLavyQNDM-- 625
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSILPIP---CI---EKDMik 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17558278  626 ELLKCneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 705
Cdd:PHA02874 109 TILDC----GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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