|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
42-434 |
5.35e-132 |
|
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: 382.78 E-value: 5.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE------------------DSPLTNAGY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscp 201
Cdd:cd04514 63 GSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 202 pstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRV 281
Cdd:cd04514 139 ------------------------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 282 GQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---V 357
Cdd:cd04514 171 GPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsP 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761934 358 LGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 434
Cdd:cd04514 251 SAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-413 |
2.60e-80 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 254.02 E-value: 2.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVMAALVELEhlsalyplleaylvsivlDSP 115
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLE------------------DDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 116 FTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDH 195
Cdd:PLN02937 69 STNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 196 GIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------ 249
Cdd:PLN02937 149 GIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedci 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 250 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 328
Cdd:PLN02937 227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 329 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 402
Cdd:PLN02937 307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378
|
410
....*....|.
gi 1958761934 403 QDGKAKTHISR 413
Cdd:PLN02937 379 SMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-411 |
2.69e-62 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 203.80 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLE------------------DDPLFN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:COG1446 70 AGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 199 SCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:COG1446 140 LVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 279 GRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGV 357
Cdd:COG1446 199 GRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGG 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958761934 358 LGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 411
Cdd:COG1446 266 DGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-402 |
2.13e-55 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 185.87 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE------------------DDPLFNAGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCP 201
Cdd:pfam01112 64 GSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 202 PSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPG 279
Cdd:pfam01112 134 PEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 280 RVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflased 355
Cdd:pfam01112 205 RVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV---------- 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958761934 356 GVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 402
Cdd:pfam01112 269 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 ... |
42-434 |
5.35e-132 |
|
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: 382.78 E-value: 5.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE------------------DSPLTNAGY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscp 201
Cdd:cd04514 63 GSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 202 pstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRV 281
Cdd:cd04514 139 ------------------------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 282 GQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---V 357
Cdd:cd04514 171 GPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsP 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761934 358 LGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 434
Cdd:cd04514 251 SAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
44-400 |
3.02e-88 |
|
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: 268.67 E-value: 3.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLE------------------DDPLFNAGRGS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 124 NLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscpps 203
Cdd:cd04512 64 VLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 204 tmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQ 283
Cdd:cd04512 127 ----------------------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 284 AALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKfisspfLASEDGVLGGVIV 363
Cdd:cd04512 161 SPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDY------LRRRVGGEGGLIV 228
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958761934 364 LrscrcpsesdpsqDKQtllVEFLWSHSTESMCVGYM 400
Cdd:cd04512 229 V-------------DPD---GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-413 |
2.60e-80 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 254.02 E-value: 2.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVMAALVELEhlsalyplleaylvsivlDSP 115
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLE------------------DDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 116 FTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDH 195
Cdd:PLN02937 69 STNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 196 GIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------ 249
Cdd:PLN02937 149 GIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedci 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 250 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 328
Cdd:PLN02937 227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 329 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 402
Cdd:PLN02937 307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378
|
410
....*....|.
gi 1958761934 403 QDGKAKTHISR 413
Cdd:PLN02937 379 SMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-411 |
2.69e-62 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 203.80 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLE------------------DDPLFN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:COG1446 70 AGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 199 SCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:COG1446 140 LVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 279 GRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGV 357
Cdd:COG1446 199 GRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGG 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958761934 358 LGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 411
Cdd:COG1446 266 DGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
44-364 |
9.62e-60 |
|
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: 196.64 E-value: 9.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALE------------------DDPVFNAGYGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 124 NLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPS 203
Cdd:cd04702 66 VLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 204 TMTTRFSLAAFKRNKRKlelaervetdfiqlkrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQ 283
Cdd:cd04702 136 SLVTERARERLEKFKKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 284 AALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflasedGVLG 359
Cdd:cd04702 198 SPIIGSGGYADN------LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLG 261
|
....*
gi 1958761934 360 GVIVL 364
Cdd:cd04702 262 GLIVV 266
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-402 |
2.13e-55 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 185.87 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE------------------DDPLFNAGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCP 201
Cdd:pfam01112 64 GSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 202 PSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPG 279
Cdd:pfam01112 134 PEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 280 RVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflased 355
Cdd:pfam01112 205 RVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV---------- 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958761934 356 GVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 402
Cdd:pfam01112 269 GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
46-364 |
1.08e-43 |
|
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: 153.77 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAG 120
Cdd:cd04701 4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLE------------------DCPLFNAG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 121 VGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSC 200
Cdd:cd04701 66 KGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 201 PPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaldTVGAVVVDHEGNVAAAVSSGGLALKHPGR 280
Cdd:cd04701 136 PQG------------------------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 281 VGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLASEDGVlGG 360
Cdd:cd04701 168 IGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGEGE-GG 236
|
....
gi 1958761934 361 VIVL 364
Cdd:cd04701 237 IIAI 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-401 |
2.71e-42 |
|
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: 149.65 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGYHSESKAKE-YKHVCKRACQKAIEKLQAGAlATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVG 122
Cdd:cd14950 2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRGS-ALEAVVEAVAYME------------------DSGVFNAGVG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 123 SNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscpp 202
Cdd:cd14950 63 SVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 203 stmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVG 282
Cdd:cd14950 127 -----------------------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 283 QAALYGCGCWAENtgahnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflasedgvL 358
Cdd:cd14950 160 DSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------T 223
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958761934 359 GGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMS 401
Cdd:cd14950 224 AGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
46-323 |
3.18e-42 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 151.40 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:PLN02689 8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELE------------------NDPLFNAGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCP 201
Cdd:PLN02689 70 GSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 202 PSTMTTRfslaafkRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALK 276
Cdd:PLN02689 140 NSYFITE-------ENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNK 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958761934 277 HPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARE 323
Cdd:PLN02689 213 MVGRIGDTPIIGAGTYANHLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
66-323 |
1.62e-38 |
|
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: 140.77 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 66 KRACQKAIEKLQAGALATDAVMAAL--VELEhlsalyplLEAYLVsivldspftnaGVGSNLNLLGEIECDASIMDGKSL 143
Cdd:cd04513 9 TEAVEAAWEVLQKGGSALDAVEAGCsvCEDD--------QCDGSV-----------GYGGSPDENGETTLDAAIMDGDTM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 144 SFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLEL 223
Cdd:cd04513 70 DVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 224 AERVETD-----FIQLKRRRQSSAKENDSGalDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-G 297
Cdd:cd04513 140 WKNVVPDpskscSSPKAPSRSESAIPEDNH--DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvG 217
|
250 260
....*....|....*....|....*.
gi 1958761934 298 AhnpystAVSTsGCGEHLVRTILARE 323
Cdd:cd04513 218 A------AAAT-GDGDIMMRFLPSYQ 236
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
44-364 |
8.12e-36 |
|
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: 132.38 E-value: 8.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04703 3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLE------------------DDPRFNAGTGS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 124 NLNLLGEIECDASIMDGKSlSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIP-SCpp 202
Cdd:cd04703 60 VLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPdGC-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 203 stmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgalDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVG 282
Cdd:cd04703 127 ------------------------------------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVG 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 283 QAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflasEDGVLGGVI 362
Cdd:cd04703 158 DVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVI 222
|
..
gi 1958761934 363 VL 364
Cdd:cd04703 223 AV 224
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
44-321 |
5.72e-32 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 123.91 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGYHSESK-----AKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:PRK10226 6 IAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLE------------------ECPLFN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:PRK10226 68 AGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGME 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 199 SCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:PRK10226 138 RVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLP 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958761934 279 GRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILA 321
Cdd:PRK10226 206 GRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRALAA 242
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-321 |
4.55e-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: 101.15 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 44 VLVHAGAGyhSESKAK-EYKHVCKRACQKAIEK----LQAGAlATDAVmaalvelehlsalyplleAYLVSIVLDSPFTN 118
Cdd:cd14949 3 LIIHGGFG--SESSTNgETKAAKQEALAEIVEEvyeyLKSHS-ALEAV------------------VYAVSLLEDDPLFN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIP 198
Cdd:cd14949 62 AGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761934 199 SCPPstmttrfslaafkrnkrklelaervETDFiqlkRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:cd14949 131 EYNP-------------------------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIP 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958761934 279 GRVGQAAlygcgcwaenTGAHNpYST---AVSTSGCGEHLVRTILA 321
Cdd:cd14949 182 GRVSDSA----------TVAGN-YANafaGVSCTGIGEDIVSEALA 216
|
|
| |
