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Conserved domains on  [gi|193207374|ref|NP_001122864|]
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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) ...
 92-448 3.62e-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: 3.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 171
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 172 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 251
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 252 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 331
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 332 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 410
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193207374 411 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 448
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
479-678 5.18e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 5.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 479 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 558
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 559 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 638
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193207374 639 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 678
Cdd:COG0666  209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 92-448 3.62e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 390.10  E-value: 3.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 171
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 172 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 251
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 252 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 331
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 332 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 410
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193207374 411 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 448
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 93-428 4.34e-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: 348.35  E-value: 4.34e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374    93 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 171
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   172 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 249
Cdd:smart00870  55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   250 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 324
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   325 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 403
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291

                          330       340
                   ....*....|....*....|....*
gi 193207374   404 IGVIPGSDMTSEAAMAKLCYVLGKD 428
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 92-427 1.01e-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: 334.41  E-value: 1.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 169
Cdd:COG0252    5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 170 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 248
Cdd:COG0252   57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 249 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 326
Cdd:COG0252  136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 327 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 406
Cdd:COG0252  215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                        330       340
                 ....*....|....*....|.
gi 193207374 407 IPGSDMTSEAAMAKLCYVLGK 427
Cdd:COG0252  292 ISGGDLTPEKARIKLMLALGQ 312
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 92-427 8.27e-109

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: 8.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 166
Cdd:cd08963    2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 167 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 246
Cdd:cd08963   49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 247 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 326
Cdd:cd08963  129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 327 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 405
Cdd:cd08963  207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285

                        330       340
                 ....*....|....*....|..
gi 193207374 406 VIPGSDMTSEAAMAKLCYVLGK 427
Cdd:cd08963  286 VIPGGDMTTEAAVAKLMWLLGQ 307
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 93-448 5.26e-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: 289.03  E-value: 5.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   93 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 170
Cdd:TIGR00519   4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  171 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 250
Cdd:TIGR00519  56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  251 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 317
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  318 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 396
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 193207374  397 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 448
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 93-303 1.22e-73

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 235.51  E-value: 1.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   93 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 169
Cdd:pfam00710   1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  170 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 249
Cdd:pfam00710  52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193207374  250 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 303
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
479-678 5.18e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 5.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 479 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 558
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 559 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 638
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193207374 639 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 678
Cdd:COG0666  209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 491-639 8.20e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 8.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 570
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 571 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 639
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-646 1.13e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  521 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 600
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 193207374  601 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 646
Cdd:pfam12796  52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 516-545 1.76e-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: 1.76e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 193207374   516 NLRTALHVAASNGHLESVNYLLKIGTNVHI 545
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 92-448 3.62e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 390.10  E-value: 3.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVPGYLPEVLRDIPplndrryieESYsnvavRPySLPpvrnmkkrvVYWIVEYEPLLDS 171
Cdd:PRK09461   5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP---------EFH-----RP-EMP---------DFTIHEYTPLIDS 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 172 CDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITAG 251
Cdd:PRK09461  61 SDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 252 NFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMvAAFTVHENLCRDVGMLRIFP 331
Cdd:PRK09461 141 NYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGE-GELIVHPITPQPIGVVTIYP 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 332 SMTIESVRAFLQPPTRGCILQTFGSGNMPtRRQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGS 410
Cdd:PRK09461 220 GISAEVVRNFLRQPVKALILRSYGVGNAP-QNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGA 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193207374 411 DMTSEAAMAKLCYVLGKdewDLPMK--RSMLQSNLRGEMT 448
Cdd:PRK09461 299 DMTVEAALTKLHYLLSQ---ELSTEeiRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 93-428 4.34e-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: 348.35  E-value: 4.34e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374    93 VLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRryieesysnvavrpyslppvrnmkkrVVYWIVEYEPLLDS 171
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPtAGAEELLALLPALPEL--------------------------ADDIEVEQVANIDS 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   172 CDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 249
Cdd:smart00870  55 SNMTPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRV 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   250 AGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAF---TVHENLCRDV 324
Cdd:smart00870 135 AASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPfllDLKDALLPKV 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   325 GMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQV-DVNYATGKILYD 403
Cdd:smart00870 215 AIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVdPGYYATGRDLAK 291

                          330       340
                   ....*....|....*....|....*
gi 193207374   404 IGVIPGSDMTSEAAMAKLCYVLGKD 428
Cdd:smart00870 292 AGVISAGDLTPEKARIKLMLALGKG 316
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 92-427 1.01e-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: 334.41  E-value: 1.01e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVP-GYLPEVLRDIPPLNDRRYIE-ESYSNVavrpyslppvrnmkkrvvywiveyepll 169
Cdd:COG0252    5 KILVLATGGTIAMRADPAGYAVAPaLSAEELLAAVPELAELADIEvEQFANI---------------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 170 DSCDMTFDDWIRIATDIKKAY-HKYDGFVVLHGTDTLAYTASALSFMMEnLGKPVIITGSQIPVAEVRSDGMENLIGALI 248
Cdd:COG0252   57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 249 TAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINiKVNYDSIFRSDMVAAFTVHENLCRDVGM 326
Cdd:COG0252  136 VAASPEarGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 327 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNYATGKILYDIGV 406
Cdd:COG0252  215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291

                        330       340
                 ....*....|....*....|.
gi 193207374 407 IPGSDMTSEAAMAKLCYVLGK 427
Cdd:COG0252  292 ISGGDLTPEKARIKLMLALGQ 312
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 92-427 8.27e-109

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: 8.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGvycpvpGYLP-----EVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYE 166
Cdd:cd08963    2 KILLLYTGGTIASVKTEG------GLAPaltaeELLSYLPELLEDCFIE---------------------------VEQL 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 167 PLLDSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGA 246
Cdd:cd08963   49 PNIDSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDA 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 247 LITAGNFDIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFtvHENLCRDVGM 326
Cdd:cd08963  129 LRAASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 327 LRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTRRqDIIMALKEAIARGVMVVNCSQCLKGQVDV-NYATGKILYDIG 405
Cdd:cd08963  207 LKLIPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLsVYAVGQALLEAG 285

                        330       340
                 ....*....|....*....|..
gi 193207374 406 VIPGSDMTSEAAMAKLCYVLGK 427
Cdd:cd08963  286 VIPGGDMTTEAAVAKLMWLLGQ 307
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 93-448 5.26e-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: 289.03  E-value: 5.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   93 VLVLYTGGTIGMKT--TDGVYCPVpGYLPEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVywiveyePLLD 170
Cdd:TIGR00519   4 ISIISTGGTIASKVdyRTGAVHPV-FTADELLSAVPELLD--------------------IANIDGEAL-------MNIL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  171 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGALITA 250
Cdd:TIGR00519  56 SENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAA 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  251 GNfDIPEVCV-------YFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAqmainiKVNYDSI------FRSDMVAAFTVH 317
Cdd:TIGR00519 135 TE-YIAEVTVcmhgvtlDFNCRLHRGVKVRKAHTSRRDAFASINAPPLA------EINPDGIeylnevYRPRGEDELEVH 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  318 ENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YA 396
Cdd:TIGR00519 208 DRLEEKVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAP---QNKLQELQEASDRGVVVVMTTQCLNGRVNMNvYS 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 193207374  397 TGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRGEMT 448
Cdd:TIGR00519 285 TGRRLLQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEIE 335
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 93-303 1.22e-73

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 235.51  E-value: 1.22e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   93 VLVLYTGGTIGMK---TTDGVYCPVPGylPEVLRDIPPLNDRRYIEesysnvavrpyslppvrnmkkrvvywiVEYEPLL 169
Cdd:pfam00710   1 VLILATGGTIASRadsSGGAVVPALTG--EELLAAVPELADIAEIE---------------------------AEQVANI 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  170 DSCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLIGALIT 249
Cdd:pfam00710  52 DSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRV 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193207374  250 AGNF--DIPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMA-INIKVNYD 303
Cdd:pfam00710 132 AASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVDgGQVELYRE 188
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 63-448 2.40e-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: 2.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374   63 NISATELVLEVQETAGTQQIGAPSALPE-SRVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDrryiees 137
Cdd:TIGR02153  34 EIRNIEVLEEGSEPREVPPPAEIEKKPGlPKVSIISTGGTIASRVdyeTGAVY---PAFTAEeLARAVPELLE------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  138 ysnvavrpyslppVRNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMM 216
Cdd:TIGR02153 104 -------------IANIKARAVFNIL-------SENMKPEYWIKIAEAVAKALKEgADGVVVAHGTDTMAYTAAALSFMF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  217 ENLGKPVIITGSQIPVAEVRSDGMENLIGALITAGNfDIPEVCVYFNNK-------LMRGNRTVKLDNSALEAFDSPNMH 289
Cdd:TIGR02153 164 ETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATS-PIAEVTVVMHGEtsdtyclVHRGVKVRKMHTSRRDAFQSINDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  290 PLAQMAINIKVNY---DSIFRSDMVAAFTvhENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDI 366
Cdd:TIGR02153 243 PIAKIDPDEGIEKlriDYRRRGEKELELD--DKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVSE---DW 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  367 IMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNLRG 445
Cdd:TIGR02153 318 IPSIKRATDDGVPVVMTSQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAG 396


                  ...
gi 193207374  446 EMT 448
Cdd:TIGR02153 397 EIN 399
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
71-448 1.43e-58

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 203.54  E-value: 1.43e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  71 LEVQETAGTQQIGAPSALPES-----RVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDRRyieesysnv 141
Cdd:PRK04183  51 IELLEKGEKPKQEPPPKEIEKdpglpNVSILSTGGTIASKVdyrTGAVT---PAFTAEdLLRAVPELLDIA--------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 142 avrpyslppvrNMKKRVVYWIVeyeplldSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMeNLG 220
Cdd:PRK04183 119 -----------NIRGRVLFNIL-------SENMTPEYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 221 KPVIITGSQipvaevRS------DGMENLIGALITAGNfDIPEVCVyfnnkLM------------RGNRTVKLDNSALEA 282
Cdd:PRK04183 180 VPIVFVGAQ------RSsdrpssDAAMNLICAVLAATS-DIAEVVV-----VMhgttsddycalhRGTRVRKMHTSRRDA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 283 FDSPNMHPLAqmainiKVNYDS----IFRSDMV----AAFTVHENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTF 354
Cdd:PRK04183 248 FQSINDKPLA------KVDYKEgkieFLRKDYRkrgeKELELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIEGT 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 355 GSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKdEWDLP 433
Cdd:PRK04183 322 GLGHVST---DLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGN-TYDLE 397

                        410
                 ....*....|....*
gi 193207374 434 MKRSMLQSNLRGEMT 448
Cdd:PRK04183 398 EVRELMLTNLAGEIN 412
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 92-443 4.17e-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: 4.17e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKT---TDGVYcpvPGYLPE-VLRDIPPLNDrryieesysnvavrpyslppvrnmkkrvvYWIVEYEP 167
Cdd:cd08962   72 KVSIISTGGTIASRVdyrTGAVS---PAFTAEeLLRAIPELLD-----------------------------IANIKAEV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 168 LLD--SCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENLGKPVIITGSQIPVAEVRSDGMENLI 244
Cdd:cd08962  120 LFNilSENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLI 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 245 GALITAGNfDIPEVCVYFNNK-------LMRGNRTVKLDNSALEAFDSPNMHPLAQMAIN---IKVNYDSIFRSDmvAAF 314
Cdd:cd08962  200 AAVLVAAS-DIAEVVVVMHGTtsddyclLHRGTRVRKMHTSRRDAFQSINDEPLAKVDPPgkiEKLSKDYRKRGD--EEL 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 315 TVHENLCRDVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN 394
Cdd:cd08962  277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIEGTGLGHVSE---DLIPSIKKAIDDGIPVVMTSQCIYGRVNLN 353

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 193207374 395 -YATGKILYDIGVIPGSDMTSEAAMAKLCYVLGKDEwDLPMKRSMLQSNL 443
Cdd:cd08962  354 vYSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 92-427 8.38e-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: 157.29  E-value: 8.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTIGMKTTDGVYCPVPGyLP--EVLRDIPPLNDrryieesYSNVAVRPyslppVRNmkkrvvywiveyeplL 169
Cdd:cd08964    2 RIAVLATGGTIAGTADSSGAYAAPT-LSgeELLAAVPGLAD-------VADVEVEQ-----VSN---------------L 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 170 DSCDMTFDDWIRIATDIKKAYHK--YDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGAL 247
Cdd:cd08964   54 PSSDMTPADWLALAARVNEALADpdVDGVVVTHGTDTLEETAYFLD-LTLDSDKPVVLTGAMRPADAPSADGPANLLDAV 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 248 ITAGNfdiPE-----VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENlcR 322
Cdd:cd08964  133 RVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDEL--P 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 323 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPtrrQDIIMALKEAIARGVMVVNCSQCLKGQVDVNYA--TGKI 400
Cdd:cd08964  208 RVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP---PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGAD 284

                        330       340
                 ....*....|....*....|....*..
gi 193207374 401 LYDIGVIPGSDMTSEAAMAKLCYVLGK 427
Cdd:cd08964  285 LAEAGAIFAGDLSPQKARILLMLALAA 311
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 92-427 6.51e-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: 6.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  92 RVLVLYTGGTI-GMKTTDGVYCPVPGYL--PEVLRDIPPLNDrryieesysnvavrpyslppVRNMKKRVVYWIveyepl 168
Cdd:cd00411    2 NITILATGGTIaGVGDSATYSAYVAGALgvEKLIKAVPELKE--------------------LANVKGEQLMNI------ 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 169 lDSCDMTFDDWIRIATDIKKAYHK-YDGFVVLHGTDTLAYTASALSFMMENlGKPVIITGSQIPVAEVRSDGMENLIGAL 247
Cdd:cd00411   56 -ASEDITPDDWLKLAKEVAKLLDSdVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAV 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 248 ITAGNFD--IPEVCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAINIKVNYDSIFRSDMVAAFTVHENLCRD-- 323
Cdd:cd00411  134 RVAKDKDsrGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDESEFDVSDIKSLpk 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 324 VGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVNyaTGKILYD 403
Cdd:cd00411  214 VDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPY---DVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLK 288

                        330       340
                 ....*....|....*....|....
gi 193207374 404 IGVIPGSDMTSEAAMAKLCYVLGK 427
Cdd:cd00411  289 AGVIPAGDLNPEKARVLLMWALTH 312
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 323-427 3.10e-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: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  323 DVGMLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMPTrrqDIIMALKEAIARGVMVVNCSQCLKGQVDVN-YATGKIL 401
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVPS---ALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDL 77

                          90       100
                  ....*....|....*....|....*.
gi 193207374  402 YDIGVIPGSDMTSEAAMAKLCYVLGK 427
Cdd:pfam17763  78 LEAGVISGGDLTPEKARIKLMLALGK 103
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
479-678 5.18e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 5.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 479 LRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAV 558
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 559 KAKAMDCIIAIRDAGGFIDAsaqkigvelclavyqndmellkcneaagthmgeKDYDNRTALHVAASLNKPEIVAYLLQC 638
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNA---------------------------------RDNDGETPLHLAAENGHLEIVKLLLEA 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193207374 639 GLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNND 678
Cdd:COG0666  209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
ansB PRK11096
L-asparaginase II; Provisional
 171-384 1.78e-20

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 93.24  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 171 SCDMTFDDWIRIATDIKKAYHKYDGFVVLHGTDTLAYTASALSfMMENLGKPVIITGSQIPVAEVRSDGMENLIGALITA 250
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 251 GNFDIPE--VCVYFNNKLMRGNRTVKLDNSALEAFDSPNMHPLAQMAiNIKVNYDSIFRSDMV--AAFTV-HENLCRDVG 325
Cdd:PRK11096 158 ADKASANrgVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIH-NGKVDYQRTPARKHTtdTPFDVsKLNELPKVG 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193207374 326 MLRIFPSMTIESVRAFLQPPTRGCILQTFGSGNMptrRQDIIMALKEAIARGVMVVNCS 384
Cdd:PRK11096 237 IVYNYANASDLPAKALVDAGYDGIVSAGVGNGNL---YKTVFDTLATAAKNGVAVVRSS 292
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
491-653 1.09e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 570
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 571 DAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGI 650
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                 ...
gi 193207374 651 TPM 653
Cdd:COG0666  287 TLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-673 3.73e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.69  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 478 LLRDIILPPMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCA 557
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 558 VKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQ 637
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 193207374 638 CGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQA 673
Cdd:COG0666  175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 491-639 8.20e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 8.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 570
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 571 DaggFIDASAQKIGVE-LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCG 639
Cdd:PLN03192 612 H---FASISDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
497-677 8.30e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 497 VEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFI 576
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 577 DASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 656
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180
                 ....*....|....*....|.
gi 193207374 657 KRRNLQNLMDMMAEHQALTNN 677
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNA 181
Ank_2 pfam12796
Ankyrin repeats (3 copies);
521-646 1.13e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  521 LHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIiairdaggfidasaqkigvelclavyqndMELLK 600
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-----------------------------KLLLE 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 193207374  601 CNeaagthMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKD 646
Cdd:pfam12796  52 HA------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 493-660 1.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 493 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASN--GHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIA-- 568
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkl 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 569 IRDAGGFIDAsaqKIGVELCLAVyqndmellkcneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDF 648
Cdd:PHA03100 162 LIDKGVDINA---KNRVNYLLSY--------------GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224

                        170
                 ....*....|..
gi 193207374 649 GITPMDEAKRRN 660
Cdd:PHA03100 225 GDTPLHIAILNN 236
Ank_2 pfam12796
Ankyrin repeats (3 copies);
491-578 5.67e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGtNVHIKDMfGYNALVCAVKAKAMDCIIAIR 570
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                  ....*...
gi 193207374  571 DAGGFIDA 578
Cdd:pfam12796  82 EKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-656 1.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 461 IPH-IAKCLRVSSSQEVQLLRD-----IILP-PMFCNaaktndvEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESV 533
Cdd:PHA02874  68 IPHpLLTAIKIGAHDIIKLLIDngvdtSILPiPCIEK-------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 534 NYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKD 613
Cdd:PHA02874 141 KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 193207374 614 YDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDdfGITPMDEA 656
Cdd:PHA02874 221 KNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
491-537 1.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 193207374  491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLL 537
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 486-639 1.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 486 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAAS-NGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMD 564
Cdd:PHA02876 310 PLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193207374 565 CIIAIRDAGGFIDASAQKIGVELCLAVY-QNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLN-KPEIVAYLLQCG 639
Cdd:PHA02876 390 IINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
Ank_2 pfam12796
Ankyrin repeats (3 copies);
491-547 2.97e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.97e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193207374  491 AAKTNDVEILKSLkAAGVNFSATDYNlRTALHVAASNGHLESVNYLLKIGTNVHIKD 547
Cdd:pfam12796  37 AAKNGHLEIVKLL-LEHADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 493-653 3.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 493 KTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 572
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 573 GGFIDasaqKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAA---SLNKpeIVAYLLQCGLNPHEKDDFG 649
Cdd:PHA02876 234 RSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqapSLSR--LVPKLLERGADVNAKNIKG 307


                 ....
gi 193207374 650 ITPM 653
Cdd:PHA02876 308 ETPL 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
587-673 2.59e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  587 LCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNphEKDDFGITPMDEAKRRNLQNLMD 666
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                  ....*..
gi 193207374  667 MMAEHQA 673
Cdd:pfam12796  79 LLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 486-653 2.84e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 486 PMFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNG--HLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAM 563
Cdd:PHA03095  86 PLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 564 dciiairdaggfidasaqkigvelclavyqnDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKP--EIVAYLLQCGLN 641
Cdd:PHA03095 166 -------------------------------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCD 214

                        170
                 ....*....|..
gi 193207374 642 PHEKDDFGITPM 653
Cdd:PHA03095 215 PAATDMLGNTPL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 488-676 8.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 8.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 488 FCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTN-------VHIKDMFGYNALVCAvKA 560
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfytlVAIKDAFNNRNVEIF-KI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 561 KAMDCIIAIRDaggfIDAsaqkigVELCLAVYQNDMEL----LKCNEAAGTHMGEKDYDNrTALHVAASLNKPEIVAYLL 636
Cdd:PHA02878 120 ILTNRYKNIQT----IDL------VYIDKKSKDDIIEAeitkLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193207374 637 QCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 676
Cdd:PHA02878 189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 487-543 1.75e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 1.75e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193207374 487 MFCNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNV 543
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 496-656 2.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 496 DVEILKSLKAAGVNFSATDYN-LRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGG 574
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 575 FIDASAQKIGVELCLAV-YQNDMELLKCNEAAGTHMGEKDY-DNRTALHVaaSLNKPEIVAYLLQCGLNPHEKDDFGITP 652
Cdd:PHA02878 226 STDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTP 303


                 ....
gi 193207374 653 MDEA 656
Cdd:PHA02878 304 LSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
620-679 2.39e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374  620 LHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTNNDE 679
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN 60
PHA03095 PHA03095
ankyrin-like protein; Provisional
 492-654 3.58e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 492 AKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGH---LESVNYLLKIGTNVHIKDMFGYNALvcavkakamdciia 568
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL-------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 569 irdaggfidasaqkigveLCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHV-AASLN-KPEIVAYLLQCGLNPHEKD 646
Cdd:PHA03095  88 ------------------HLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALD 149


                 ....*...
gi 193207374 647 DFGITPMD 654
Cdd:PHA03095 150 LYGMTPLA 157
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 580-671 3.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 580 AQKIGVELCLAVYQNDMELLKCNEAAGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRR 659
Cdd:PTZ00322  79 AHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                         90
                 ....*....|..
gi 193207374 660 NLQNLMDMMAEH 671
Cdd:PTZ00322 159 GFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
518-566 4.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 193207374  518 RTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCI 566
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
Ank_5 pfam13857
Ankyrin repeats (many copies);
612-656 5.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 5.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 193207374  612 KDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 656
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 516-547 5.47e-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: 5.47e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 193207374  516 NLRTALHVAA-SNGHLESVNYLLKIGTNVHIKD 547
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
616-656 6.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 6.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193207374  616 NRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEA 656
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
512-554 6.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 6.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 193207374  512 ATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNAL 554
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 516-545 1.76e-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: 1.76e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 193207374   516 NLRTALHVAASNGHLESVNYLLKIGTNVHI 545
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 516-676 5.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 516 NLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGGFIDASAQKIGVELCLAVYQND 595
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 596 MELLKCNEAAGTHMGEKDY-DNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQAL 674
Cdd:PHA02875  81 VKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160


                 ..
gi 193207374 675 TN 676
Cdd:PHA02875 161 LD 162
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 615-647 6.14e-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: 6.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 193207374  615 DNRTALHVAA-SLNKPEIVAYLLQCGLNPHEKDD 647
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 491-600 7.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 7.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 491 AAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIR 570
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                         90       100       110
                 ....*....|....*....|....*....|.
gi 193207374 571 DAGGFIDASAQKIGVE-LCLAVYQNDMELLK 600
Cdd:PHA02875 189 DSGANIDYFGKNGCVAaLCYAIENNKIDIVR 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 493-598 1.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 493 KTNDVEILKSLkaaGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDA 572
Cdd:PHA03100 171 AKNRVNYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247

                         90       100
                 ....*....|....*....|....*.
gi 193207374 573 GGFIDASAQKIgvelclaVYQNDMEL 598
Cdd:PHA03100 248 GPSIKTIIETL-------LYFKDKDL 266
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 615-644 1.44e-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: 1.44e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 193207374  615 DNRTALHVAASLNKPEIVAYLLQCGLNPHE 644
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 489-559 3.04e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207374 489 CNAAKTNDVEILKSLKAAGVNFSATDYNLRTALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVK 559
Cdd:PTZ00322  87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 518-545 3.89e-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: 3.89e-03
                          10        20
                  ....*....|....*....|....*...
gi 193207374  518 RTALHVAASNGHLESVNYLLKIGTNVHI 545
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 519-676 4.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 519 TALHVAASNGHLESVNYLLKIGTNVHIKDMFGYNALVCAVKAKAMDCIIAIRDAGgfIDASAQKIGvelCLavyQNDM-- 596
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSILPIP---CI---EKDMik 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207374 597 ELLKCneaaGTHMGEKDYDNRTALHVAASLNKPEIVAYLLQCGLNPHEKDDFGITPMDEAKRRNLQNLMDMMAEHQALTN 676
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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