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Conserved domains on  [gi|2217297394|ref|XP_047287312|]
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60 kDa lysophospholipase isoform X15 [Homo sapiens]

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) ...
 9-361 4.67e-128

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: 378.55  E-value: 4.67e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461    4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461   62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461  142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461  221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217297394 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461  301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-476 1.24e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.24e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 4.67e-128

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 378.55  E-value: 4.67e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461    4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461   62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461  142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461  221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217297394 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461  301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.71e-99

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: 304.83  E-value: 1.71e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPmfhdeehararglsedtlvlppaSRNQRILYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALLP-----------------------ALPELADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   89 TIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  167 Y--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG---LVVHSSMEQDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSpflLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  242 RLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVI 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 2217297394  321 SGFDMTSEAALAKLSYVLGQpGLSLDVRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 7.55e-96

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: 295.50  E-value: 7.55e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  10 RLLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHararglsedtlvlppasrnqrilYTVLECQPLfDSSD 87
Cdd:COG0252     5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELAD-----------------------IEVEQFANI-DSSN 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  88 MTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252    61 MTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 165 GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVGLLRL 243
Cdd:COG0252   140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVAILKL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 244 YPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGF 323
Cdd:COG0252   218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2217297394 324 DMTSEAALAKLSYVLGQpGLSLDVRKELLTK 354
Cdd:COG0252   296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.55e-95

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: 294.10  E-value: 1.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   9 RRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPmfHDEEHARarglsedtlvlppasrnqrilyTVLECQPLFDSSDM 88
Cdd:cd08963     1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLP--ELLEDCF----------------------IEVEQLPNIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963    57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 169 IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQDVGLLRLYPGIP 248
Cdd:cd08963   137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 249 AALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDMTS 327
Cdd:cd08963   215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIPGGDMTT 294

                         330
                  ....*....|....
gi 2217297394 328 EAALAKLSYVLGQP 341
Cdd:cd08963   295 EAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 4.31e-85

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: 268.22  E-value: 4.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  11 LLAVYTGGTIGM-RSE-LGVLVPGTGLAAILRTLPMFHDEEHARARGLsedtlvlppasrnqrilytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEAL------------------------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 169 ------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2217297394 322 GFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 9.62e-67

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 214.71  E-value: 9.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFhdEEHARARGlsedtlvlppasrnqrilytvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAVPEL--ADIAEIEA----------------------EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217297394 168 -VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-476 1.24e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.24e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-476 1.25e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297394 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVR 476
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAAR 70
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 406-480 2.32e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 2.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297394 406 CAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRTR 480
Cdd:PTZ00322   87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 1.06e-05

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: 42.19  E-value: 1.06e-05
                           10        20
                   ....*....|....*....|....*....
gi 2217297394  433 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 461
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 4.67e-128

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 378.55  E-value: 4.67e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461    4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461   62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461  142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461  221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217297394 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461  301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.71e-99

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: 304.83  E-value: 1.71e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPmfhdeehararglsedtlvlppaSRNQRILYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALLP-----------------------ALPELADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   89 TIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  167 Y--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG---LVVHSSMEQDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSpflLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  242 RLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVI 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 2217297394  321 SGFDMTSEAALAKLSYVLGQpGLSLDVRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 7.55e-96

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: 295.50  E-value: 7.55e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  10 RLLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHararglsedtlvlppasrnqrilYTVLECQPLfDSSD 87
Cdd:COG0252     5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELAD-----------------------IEVEQFANI-DSSN 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  88 MTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252    61 MTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 165 GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVGLLRL 243
Cdd:COG0252   140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVAILKL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 244 YPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGF 323
Cdd:COG0252   218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2217297394 324 DMTSEAALAKLSYVLGQpGLSLDVRKELLTK 354
Cdd:COG0252   296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.55e-95

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: 294.10  E-value: 1.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394   9 RRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPmfHDEEHARarglsedtlvlppasrnqrilyTVLECQPLFDSSDM 88
Cdd:cd08963     1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLP--ELLEDCF----------------------IEVEQLPNIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963    57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 169 IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQDVGLLRLYPGIP 248
Cdd:cd08963   137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 249 AALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDMTS 327
Cdd:cd08963   215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIPGGDMTT 294

                         330
                  ....*....|....
gi 2217297394 328 EAALAKLSYVLGQP 341
Cdd:cd08963   295 EAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 4.31e-85

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: 268.22  E-value: 4.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  11 LLAVYTGGTIGM-RSE-LGVLVPGTGLAAILRTLPMFHDEEHARARGLsedtlvlppasrnqrilytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEAL------------------------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 169 ------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2217297394 322 GFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 9.62e-67

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 214.71  E-value: 9.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFhdEEHARARGlsedtlvlppasrnqrilytvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAVPEL--ADIAEIEA----------------------EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217297394 168 -VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 74-365 1.83e-46

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: 167.94  E-value: 1.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  74 YTVLECQPLFD--SSDMTIAEWVCLAQTIKRHYEQYH-GFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALW 150
Cdd:TIGR02153 104 IANIKARAVFNilSENMKPEYWIKIAEAVAKALKEGAdGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPS 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 151 SDGRENLLGALLMAGQyVIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATVGAD--ITINR 216
Cdd:TIGR02153 184 SDAALNLICAVRAATS-PIAEVtvvmhgetsdtyCL-----VHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDegIEKLR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 217 ELVRKvDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNC 296
Cdd:TIGR02153 258 IDYRR-RGEKELELDDKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIE--GTGLGHVSEDWIPSIKRATDDGVPVVMT 334

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 297 THCLQGAVTTD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 365
Cdd:TIGR02153 335 SQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEINERTL 403
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 85-356 3.02e-44

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: 162.02  E-value: 3.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  85 SSDMTIAEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLM 163
Cdd:cd08962   125 SENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLV 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 164 AGQYvIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV---GADITINRELVRKvdGKAGL 228
Cdd:cd08962   205 AASD-IAEVvvvmhgttsddyCL-----LHRGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEEL 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 229 VVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD- 307
Cdd:cd08962   277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNv 354

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2217297394 308 YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDL 356
Cdd:cd08962   355 YSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
14-365 4.62e-43

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 159.24  E-value: 4.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  14 VYTGGTIGMRSELgvlvpgtglaailRT---LPMFHDEEHARARGLSEDtlvlpPASRNQRILYTVLecqplfdSSDMTI 90
Cdd:PRK04183   81 LSTGGTIASKVDY-------------RTgavTPAFTAEDLLRAVPELLD-----IANIRGRVLFNIL-------SENMTP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  91 AEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQ----VPIhalwSDGRENLLGALLMA- 164
Cdd:PRK04183  136 EYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQrssdRPS----SDAAMNLICAVLAAt 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 165 ---GQYVI-------PEVCLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV----GADITINRELVRKVDGKagLVV 230
Cdd:PRK04183  211 sdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKRGEKE--LEL 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 231 HSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YA 309
Cdd:PRK04183  284 NDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYS 361

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217297394 310 AGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 365
Cdd:PRK04183  362 TGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTY-DLEEVRELMLTNLAGEINERSR 416
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 10-340 1.36e-36

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: 138.80  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  10 RLLAVYTGGTI----GMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEdtlvlppasrnqrilytvlecqplFDS 85
Cdd:cd00411     2 NITILATGGTIagvgDSATYSAYVAGALGVEKLIKAVPELKELANVKGEQLMN------------------------IAS 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  86 SDMTIAEWVCLAQTI-KRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMA 164
Cdd:cd00411    58 EDITPDDWLKLAKEVaKLLDSDVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVRVA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 165 --GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITI--NRELVRKVDGKAGLVVHSSMEQDVGL 240
Cdd:cd00411   137 kdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKVDI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 241 LRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDyaAGMAMAGAGVI 320
Cdd:cd00411   217 VYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLKAGVI 292

                         330       340
                  ....*....|....*....|
gi 2217297394 321 SGFDMTSEAALAKLSYVLGQ 340
Cdd:cd00411   293 PAGDLNPEKARVLLMWALTH 312
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 16-308 4.13e-35

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: 134.56  E-value: 4.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  16 TGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHARARGLSedtlvlppasrNQrilytvlecqplfDSSDMTIAEW 93
Cdd:cd08964     8 TGGTIAGTadSSGAYAAPTLSGEELLAAVPGLADVADVEVEQVS-----------NL-------------PSSDMTPADW 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  94 VCLAQTIKRHYEQ--YHGFVVIHGTDTM---AFAASMLsfmlENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQyv 168
Cdd:cd08964    64 LALAARVNEALADpdVDGVVVTHGTDTLeetAYFLDLT----LDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAAS-- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 169 iPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKvdgKAGLVVHSSMEQDVGLLR 242
Cdd:cd08964   138 -PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARP---HTLPSEFDDELPRVDIVY 213

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217297394 243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDY 308
Cdd:cd08964   214 AYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVY 277
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 237-351 9.12e-29

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: 110.26  E-value: 9.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 237 DVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMA 315
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217297394 316 GAGVISGFDMTSEAALAKLSYVLGQpGLSLDVRKEL 351
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-476 1.24e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.24e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-476 6.95e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 6.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 384 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 463
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                          90
                  ....*....|...
gi 2217297394 464 DTDGFSPLLLAVR 476
Cdd:COG0666   150 DNDGNTPLHLAAA 162
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
 84-307 1.41e-16

L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) 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 periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273115 [Multi-domain]  Cd Length: 349  Bit Score: 81.35  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  84 DSSDMTIAEWVCLAQTIKRHYE--QYHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQVPIHALWSDGRENLLGAL 161
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLAsdDYDGIVITHGTDTLEETAYFLDLTV-KSDKPVVIVGAMRPATSVSADGPMNLYNAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 162 LMAGQyviPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRK--VDGKAGLVVHSS 233
Cdd:TIGR00520 160 SVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIhNGKIDYYYPPVRKhtCDTPFSVSNLDE 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217297394 234 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 307
Cdd:TIGR00520 237 PLPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSSRVGDGMVTPD 308
ansB PRK11096
L-asparaginase II; Provisional
 85-307 2.14e-16

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 80.92  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394  85 SSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSfMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMA 164
Cdd:PRK11096   79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 165 G--QYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKVDGKAGLVVhSSMEQ--DVG 239
Cdd:PRK11096  158 AdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNGKVDYQRTPARKHTTDTPFDV-SKLNElpKVG 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297394 240 LLRLYPGIPAALVRAFLQPPLKGVVmeTFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 307
Cdd:PRK11096  237 IVYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKNGVAVVRSSRVPTGATTQD 302
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-476 2.74e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 2.74e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-476 1.25e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297394 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVR 476
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAAR 70
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-476 3.93e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 383 WLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90
                  ....*....|....
gi 2217297394 463 RDTDGFSPLLLAVR 476
Cdd:COG0666   116 RDKDGETPLHLAAY 129
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 406-480 2.32e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 2.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297394 406 CAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRTR 480
Cdd:PTZ00322   87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
Ank_2 pfam12796
Ankyrin repeats (3 copies);
407-464 9.72e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 9.72e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297394 407 AAAHAGDVEALQALVELGSdlGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRD 464
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-454 1.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217297394 403 SLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLL 454
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-476 4.20e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 4.20e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
420-474 4.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 4.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217297394 420 LVELGS-DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLA 474
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-464 4.75e-07

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: 46.13  E-value: 4.75e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217297394 433 NGQTPLHAAA-RGGHTEAVTMLLQRGVDVNTRD 464
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
436-477 7.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 7.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217297394 436 TPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRG 477
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 396-476 1.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 396 LRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198


                  .
gi 2217297394 476 R 476
Cdd:PHA02874  199 E 199
PHA03095 PHA03095
ankyrin-like protein; Provisional
 420-476 2.29e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 2.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217297394 420 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Ank_2 pfam12796
Ankyrin repeats (3 copies);
438-477 3.46e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 3.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297394 438 LHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRG 477
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 404-473 4.45e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217297394 404 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDT-DGFSPLLL 473
Cdd:PLN03192  625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPTEL 695
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-475 6.67e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 6.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297394 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 381-476 9.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 381 VSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTE------------ 448
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgv 167

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217297394 449 ------AVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA03100  168 dinaknRVNYLLSYGVPINIKDVYGFTPLHYAVY 201
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 1.06e-05

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: 42.19  E-value: 1.06e-05
                           10        20
                   ....*....|....*....|....*....
gi 2217297394  433 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 461
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 408-475 2.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297394 408 AAHAGDVEALQALVELGSDLGLVDF-NGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
PHA03095 PHA03095
ankyrin-like protein; Provisional
 404-471 2.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 2.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 404 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGG--HTEAVTMLLQRGVDVNTRDTDGFSPL 471
Cdd:PHA03095   87 LHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-462 2.65e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 2.65e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217297394 433 NGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 420-476 3.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 3.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217297394 420 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 413-471 3.22e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 3.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297394 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVT-MLLQRGVDVNTRDTDGFSPL 471
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGRTPL 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 418-475 1.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297394 418 QALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAV 219
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 415-476 2.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217297394 415 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 415-475 5.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217297394 415 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA02917 PHA02917
ankyrin-like protein; Provisional
 426-475 1.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.91  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217297394 426 DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 408-462 1.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217297394 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 420-471 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217297394 420 LVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPL 471
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPL 345
PHA03095 PHA03095
ankyrin-like protein; Provisional
 413-481 1.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217297394 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH---TEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRTRL 481
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 413-476 9.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 9.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297394 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA02876  252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
 
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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