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Conserved domains on  [gi|1039762209|ref|XP_017174800|]
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threonine aspartase 1 isoform X4 [Mus musculus]

Protein Classification

threonine aspartase 1( domain architecture ID 10139957)

threonine aspartase 1 (also known as taspase-1) is protease which cleaves the mixed-lineage leukemia (MLL) and transcription factor (TF) IIA families of nuclear proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-393 6.48e-122

Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer.


:

Pssm-ID: 271336  Cd Length: 313  Bit Score: 355.43  E-value: 6.48e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDASIMD 98
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAaaavlkaggsaldaveaaikvleDSPLTNAGYGSNLTEDGTVECDASIMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  99 GKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrnkr 178
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 179 klelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ 258
Cdd:cd04514   138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 259 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesds 334
Cdd:cd04514   189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK------- 261

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039762209 335 sqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 393
Cdd:cd04514   262 ---KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-393 6.48e-122

Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer.


Pssm-ID: 271336  Cd Length: 313  Bit Score: 355.43  E-value: 6.48e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDASIMD 98
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAaaavlkaggsaldaveaaikvleDSPLTNAGYGSNLTEDGTVECDASIMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  99 GKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrnkr 178
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 179 klelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ 258
Cdd:cd04514   138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 259 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesds 334
Cdd:cd04514   189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK------- 261

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039762209 335 sqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 393
Cdd:cd04514   262 ---KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-372 1.84e-74

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.46  E-value: 1.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQ------------------------KDSPFTNAGIGSNLNLLGEIEC 92
Cdd:PLN02937    7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLaaaailrqgsggcidavsaaiqvlEDDPSTNAGRGSNLTEDGHVEC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  93 DASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT------- 165
Cdd:PLN02937   87 DASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlv 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 166 TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAA 226
Cdd:PLN02937  165 TERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 227 VSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLET 299
Cdd:PLN02937  245 ASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSV 324

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039762209 300 MQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 372
Cdd:PLN02937  325 IQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-370 2.92e-55

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 184.16  E-value: 2.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDAS 95
Cdd:COG1446     8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAgyavleaggsaldaveaavrvleDDPLFNAGKGAVLTRDGTVELDAS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  96 IMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKR 175
Cdd:COG1446    88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 176 NKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 255
Cdd:COG1446   149 EKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 256 GAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesds 334
Cdd:COG1446   217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV----------- 272

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1039762209 335 sqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 370
Cdd:COG1446   273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
68-361 9.53e-50

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 170.07  E-value: 9.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  68 ACQ--KDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGE 145
Cdd:pfam01112  49 AVRllEDDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 146 GAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNV 223
Cdd:pfam01112 119 GAEQFAREMGLERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 224 AAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLET 299
Cdd:pfam01112 190 AAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITE 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039762209 300 MQNKFisspflacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 361
Cdd:pfam01112 264 MLKRV----------GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-393 6.48e-122

Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer.


Pssm-ID: 271336  Cd Length: 313  Bit Score: 355.43  E-value: 6.48e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDASIMD 98
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAaaavlkaggsaldaveaaikvleDSPLTNAGYGSNLTEDGTVECDASIMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  99 GKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrnkr 178
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 179 klelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ 258
Cdd:cd04514   138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 259 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesds 334
Cdd:cd04514   189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK------- 261

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039762209 335 sqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 393
Cdd:cd04514   262 ---KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 44-359 2.07e-79

L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. The family is circularly permuted relative to other NTN-hydrolase families.


Pssm-ID: 271334  Cd Length: 249  Bit Score: 244.78  E-value: 2.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAGYHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDASIMDGK 100
Cdd:cd04512     2 LIVHGGAGTIEDEDAEAYREGLLRALEAgrevlekggsaldaveaavrlleDDPLFNAGRGSVLNEDGEVEMDAAIMDGK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 101 SLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrkl 180
Cdd:cd04512    82 TLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 181 elaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgaqnp 260
Cdd:cd04512   127 ----------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE----- 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 261 ySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSpflaceDGVLGGVIVLrscrcssesdssqDKQt 340
Cdd:cd04512   174 -TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYLRRR------VGGEGGLIVV-------------DPD- 232

                         330
                  ....*....|....*....
gi 1039762209 341 llVEFLWSHTTESMCVGYM 359
Cdd:cd04512   233 --GRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-372 1.84e-74

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.46  E-value: 1.84e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQ------------------------KDSPFTNAGIGSNLNLLGEIEC 92
Cdd:PLN02937    7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLaaaailrqgsggcidavsaaiqvlEDDPSTNAGRGSNLTEDGHVEC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  93 DASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT------- 165
Cdd:PLN02937   87 DASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlv 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 166 TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAA 226
Cdd:PLN02937  165 TERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 227 VSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLET 299
Cdd:PLN02937  245 ASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSV 324

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039762209 300 MQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 372
Cdd:PLN02937  325 IQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-370 2.92e-55

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 184.16  E-value: 2.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQK-----------------------DSPFTNAGIGSNLNLLGEIECDAS 95
Cdd:COG1446     8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAgyavleaggsaldaveaavrvleDDPLFNAGKGAVLTRDGTVELDAS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  96 IMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKR 175
Cdd:COG1446    88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 176 NKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 255
Cdd:COG1446   149 EKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 256 GAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesds 334
Cdd:COG1446   217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV----------- 272

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1039762209 335 sqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 370
Cdd:COG1446   273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 44-323 1.45e-52

Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the L-Asparaginase type 2-like enzymes. The wider family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. The proenzymes undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. ASRGL1, or asparaginase-like 1, has been cloned from mammalian testis cDNA libraries. It has been identified as a sperm antigen that may induce the production of autoantibodies following obstruction of the male reproductive tract, e.g. vasectomy.


Pssm-ID: 271338  Cd Length: 289  Bit Score: 176.61  E-value: 1.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAGYHSESKAKEYKHVCKRA-----------------------CQKDSPFTNAGIGSNLNLLGEIECDASIMDGK 100
Cdd:cd04702     4 IVVHGGAGSIPDDRIKGSREGVKRAaragysvlkaggsaldaveaavrALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 101 SLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKl 180
Cdd:cd04702    84 TLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKE- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 181 elaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnp 260
Cdd:cd04702   153 -----------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------ 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039762209 261 YSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflacedGVLGGVIVL 323
Cdd:cd04702   210 LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
Asparaginase_2 pfam01112
Asparaginase;
68-361 9.53e-50

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 170.07  E-value: 9.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  68 ACQ--KDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGE 145
Cdd:pfam01112  49 AVRllEDDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 146 GAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNV 223
Cdd:pfam01112 119 GAEQFAREMGLERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 224 AAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLET 299
Cdd:pfam01112 190 AAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITE 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039762209 300 MQNKFisspflacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 361
Cdd:pfam01112 264 MLKRV----------GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 44-360 4.56e-38

Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271341  Cd Length: 251  Bit Score: 137.71  E-value: 4.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAG----YHSESKAKEY-KHVCKR------------------ACQKDSPFTNAGIGSNLNLLGEIECDASIMDGK 100
Cdd:cd14950     2 LVVHGGAGswknSDDEEKALRAlREALERgyealrrgsaleavveavAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 101 SLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrkl 180
Cdd:cd14950    82 TLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------------------------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 181 elaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnp 260
Cdd:cd14950   127 ----------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN------ 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 261 ySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflacedgvLGGVIVLrscrcssesdssq 336
Cdd:cd14950   173 -GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI------------- 229

                         330       340
                  ....*....|....*....|....
gi 1039762209 337 DKQTllvEFLWSHTTESMCVGYMS 360
Cdd:cd14950   230 DARG---NIAAAFNTEAMPRGYID 250
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 67-316 1.78e-37

Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.


Pssm-ID: 271335  Cd Length: 294  Bit Score: 137.31  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  67 RACQKDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEG 146
Cdd:cd04513    34 SVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 147 AYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLELAERVETD---FIQLKRRRQSSAKENDSGTLDTVGAVVVDHEGNV 223
Cdd:cd04513   104 ATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDpskSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 224 AAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAqnpystAVSTsGCGEhlvrtILARECShalqaedAHQAlLETMQN 302
Cdd:cd04513   184 AAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGD-----IMMRFLP-------SYQA-VELMRQ 243

                         250
                  ....*....|....
gi 1039762209 303 KFisSPFLACEDGV 316
Cdd:cd04513   244 GM--SPQEACEDAI 255
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 72-323 7.61e-37

Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes.


Pssm-ID: 271337  Cd Length: 264  Bit Score: 134.51  E-value: 7.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  72 DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWA 151
Cdd:cd04701    58 DCPLFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 152 VDHGIPSCPPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtldTVGAVVVDHEGNVAAAVSSGG 231
Cdd:cd04701   128 REQGLELVPQG------------------------------------------------TVGAVALDSDGNLAAATSTGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 232 LALKHPGRVGQAALYGCGCWAENtgaqnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLA 311
Cdd:cd04701   160 LTNKLPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGE 229

                         250
                  ....*....|..
gi 1039762209 312 CEDGVlGGVIVL 323
Cdd:cd04701   230 LGEGE-GGIIAI 240
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-282 1.32e-36

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 135.60  E-value: 1.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  46 VHAGAGYHSESKAKEYKHVCKRACQK---------------------------DSPFTNAGIGSNLNLLGEIECDASIMD 98
Cdd:PLN02689    8 LHGGAGDIDPNLPRERQEEAEAALRRcldlgiaalrsslpaldvvelvvreleNDPLFNAGRGSVLTEDGTVEMEASIMD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  99 GKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRNKR 178
Cdd:PLN02689   88 GRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------ENVE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 179 KLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAE 253
Cdd:PLN02689  151 RLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYAN 230

                         250       260
                  ....*....|....*....|....*....
gi 1039762209 254 NTGaqnpystAVSTSGCGEHLVRTILARE 282
Cdd:PLN02689  231 HLC-------AVSATGKGEAIIRGTVARD 252
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 71-280 8.95e-31

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 119.67  E-value: 8.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  71 KDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRW 150
Cdd:PRK10226   61 EECPLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 151 AVDHGIPSCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSG 230
Cdd:PRK10226  131 AFAHGMERVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTG 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039762209 231 GLALKHPGRVGQAALYGCGCWAENTgaqnpySTAVSTSGCGEHLVRTILA 280
Cdd:PRK10226  199 GMTNKLPGRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRALAA 242
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 44-323 2.48e-29

Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271339  Cd Length: 243  Bit Score: 113.89  E-value: 2.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAGyhsesKAKEYKHVCKRACQ-----------------------KDSPFTNAGIGSNLNLLGEIECDASIMDGK 100
Cdd:cd04703     3 VLVHGGAG-----SDPERQDGLERAAEaglaelqnggdaldavvaavrvlEDDPRFNAGTGSVLRDDGSIQMDAAVMTSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 101 SlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPScppstmttrfslaafkrnkrkl 180
Cdd:cd04703    78 G-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPD---------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 181 elaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGaqnp 260
Cdd:cd04703   125 ---------------------------GCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG---- 172

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039762209 261 ystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflacEDGVLGGVIVL 323
Cdd:cd04703   173 ---AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 44-280 5.50e-24

Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271340  Cd Length: 280  Bit Score: 100.38  E-value: 5.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  44 VLVHAGAGyhSESKAKE-----------------YKHVCK--------RACQ--KDSPFTNAGIGSNLNLLGEIECDASI 96
Cdd:cd14949     3 LIIHGGFG--SESSTNGetkaakqealaeiveevYEYLKShsaleavvYAVSllEDDPLFNAGTGSQIQSDGQIRMSASL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209  97 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkrn 176
Cdd:cd14949    81 MDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP--------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762209 177 krklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTG 256
Cdd:cd14949   135 ----------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TV 190

                         250       260
                  ....*....|....*....|....*..
gi 1039762209 257 AQNpYST---AVSTSGCGEHLVRTILA 280
Cdd:cd14949   191 AGN-YANafaGVSCTGIGEDIVSEALA 216
 
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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