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Conserved domains on  [gi|2497687|sp|Q13093|]
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RecName: Full=Platelet-activating factor acetylhydrolase; Short=PAF acetylhydrolase; AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase; AltName: Full=2-acetyl-1-alkylglycerophosphocholine esterase; AltName: Full=Group-VIIA phospholipase A2; Short=gVIIA-PLA2; AltName: Full=LDL-associated phospholipase A2; Short=LDL-PLA(2); AltName: Full=PAF 2-acylhydrolase; Flags: Precursor

Protein Classification

platelet-activating factor acetylhydrolase( domain architecture ID 10506208)

platelet-activating factor acetylhydrolase is a lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response; belongs to the alpha/beta hydrolase superfamily

CATH:  3.40.50.1820
EC:  3.1.1.47
Gene Ontology:  GO:0003847|GO:0046469
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
48-416 0e+00

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


:

Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 698.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687     48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2497687    365 IGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENL 416
Cdd:pfam03403 321 IGKKLKLKGEIDPYEAIDINNRASLAFLQKHLDLHKDFDQWDNLIEGDDENL 372
 
Name Accession Description Interval E-value
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
48-416 0e+00

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 698.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687     48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2497687    365 IGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENL 416
Cdd:pfam03403 321 IGKKLKLKGEIDPYEAIDINNRASLAFLQKHLDLHKDFDQWDNLIEGDDENL 372
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
131-396 3.42e-35

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 132.92  E-value: 3.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  131 PANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASatyyfkDQSAAEIGDKSWLYLRTLk 210
Cdd:COG4188  49 PATAPADAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAA------DLSAALDGLADALDPEEL- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  211 qeeethirneqvRQRAKECSQALSLILDIDHGKPvknaldlkfdmeQLKDSIDREKIAVIGHSFGGATVIQTLSE----- 285
Cdd:COG4188 122 ------------WERPLDLSFVLDQLLALNKSDP------------PLAGRLDLDRIGVIGHSLGGYTALALAGArldfa 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  286 ---------------------------DQRFRCGIALDAWMFP-LGDEVYSRIPQPLFFINSEY---FQYPANIIKMKKc 334
Cdd:COG4188 178 alrqycgknpdlqcraldlprlaydlrDPRIKAVVALAPGGSGlFGEEGLAAITIPVLLVAGSAddvTPAPDEQIRPFD- 256
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497687  335 YSPDKERKMITIRGSVHQNFADFTFATGKIIGhmLKLKGDIDSNVAIDLSNKASLAFLQKHL 396
Cdd:COG4188 257 LLPGADKYLLTLEGATHFSFLDPCTPGAAILP--EPDPPGPDRAAIHEYLNALSLAFFDAYL 316
PLN00021 PLN00021
chlorophyllase
131-176 7.06e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 41.57  E-value: 7.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2497687   131 PANWNSPLRP---------GEkYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAA 176
Cdd:PLN00021  31 ESSRPSPPKPllvatpseaGT-YPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVA 84
 
Name Accession Description Interval E-value
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
48-416 0e+00

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 698.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687     48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687    285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2497687    365 IGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENL 416
Cdd:pfam03403 321 IGKKLKLKGEIDPYEAIDINNRASLAFLQKHLDLHKDFDQWDNLIEGDDENL 372
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
131-396 3.42e-35

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 132.92  E-value: 3.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  131 PANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASatyyfkDQSAAEIGDKSWLYLRTLk 210
Cdd:COG4188  49 PATAPADAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAA------DLSAALDGLADALDPEEL- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  211 qeeethirneqvRQRAKECSQALSLILDIDHGKPvknaldlkfdmeQLKDSIDREKIAVIGHSFGGATVIQTLSE----- 285
Cdd:COG4188 122 ------------WERPLDLSFVLDQLLALNKSDP------------PLAGRLDLDRIGVIGHSLGGYTALALAGArldfa 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  286 ---------------------------DQRFRCGIALDAWMFP-LGDEVYSRIPQPLFFINSEY---FQYPANIIKMKKc 334
Cdd:COG4188 178 alrqycgknpdlqcraldlprlaydlrDPRIKAVVALAPGGSGlFGEEGLAAITIPVLLVAGSAddvTPAPDEQIRPFD- 256
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497687  335 YSPDKERKMITIRGSVHQNFADFTFATGKIIGhmLKLKGDIDSNVAIDLSNKASLAFLQKHL 396
Cdd:COG4188 257 LLPGADKYLLTLEGATHFSFLDPCTPGAAILP--EPDPPGPDRAAIHEYLNALSLAFFDAYL 316
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
132-300 2.47e-09

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 57.62  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  132 ANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR-------DRSASATYYFKDQSAAeigdksWL 204
Cdd:COG1073  25 GDLYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRgygesegEPREEGSPERRDARAA------VD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  205 YLRTLKQeeethirneqvrqrakecsqalslildidhgkpvknaldlkfdmeqlkdsIDREKIAVIGHSFGGATVIQTLS 284
Cdd:COG1073  99 YLRTLPG--------------------------------------------------VDPERIGLLGISLGGGYALNAAA 128
                       170
                ....*....|....*.
gi 2497687  285 EDQRFRCgIALDAwMF 300
Cdd:COG1073 129 TDPRVKA-VILDS-PF 142
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
124-295 1.06e-08

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.41  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  124 LFGSMTTPANwnsplrpGEKYPLVVFSHGLGAFRTL-YSAIGIDLASHGFIVAAVEHRDRSASAtyyfKDQSAAEIGDks 202
Cdd:COG1506  10 LPGWLYLPAD-------GKKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESA----GDWGGDEVDD-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  203 wlylrtlkqeeethirneqvrqrakecsqalslildidhgkpVKNALDlkfdmeQLKDS--IDREKIAVIGHSFGGATVI 280
Cdd:COG1506  77 ------------------------------------------VLAAID------YLAARpyVDPDRIGIYGHSYGGYMAL 108
                       170
                ....*....|....*.
gi 2497687  281 QTLSED-QRFRCGIAL 295
Cdd:COG1506 109 LAAARHpDRFKAAVAL 124
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
141-320 9.11e-07

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.58  E-value: 9.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  141 GEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYyfkdqsaaeigdkswlylrtlkqeeethirNE 220
Cdd:COG0412  26 GGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDD------------------------------PD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  221 QVRQRAKECSQALsLILDIDHgkpvknALDLkfdmeqLK--DSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAW 298
Cdd:COG0412  76 EARALMGALDPEL-LAADLRA------ALDW------LKaqPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG 142
                       170       180
                ....*....|....*....|...
gi 2497687  299 -MFPLGDEVYSRIPQPLFFINSE 320
Cdd:COG0412 143 lPADDLLDLAARIKAPVLLLYGE 165
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
136-177 1.27e-05

Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.


Pssm-ID: 432755  Cd Length: 254  Bit Score: 46.55  E-value: 1.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2497687    136 SPLRPGEkYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAV 177
Cdd:pfam12740  10 TPTEAGT-YPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVAP 50
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
145-344 1.39e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 43.07  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  145 PLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR--DRSASATYYFKDQSAaeigdkswlYLRTLkqeeethirnEQV 222
Cdd:COG2267  29 GTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRghGRSDGPRGHVDSFDD---------YVDDL----------RAA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  223 RQRAKEcsqalslildiDHGKPVknaldlkfdmeqlkdsidrekiAVIGHSFGGATVIQTLSE-DQRFRcGIALDA---- 297
Cdd:COG2267  90 LDALRA-----------RPGLPV----------------------VLLGHSMGGLIALLYAARyPDRVA-GLVLLApayr 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497687  298 ----------WMFPLG-DEVYSRIPQPLFFINSE--YFQYPANIIKMKKCYSPDKERKMI 344
Cdd:COG2267 136 adpllgpsarWLRALRlAEALARIDVPVLVLHGGadRVVPPEAARRLAARLSPDVELVLL 195
PLN00021 PLN00021
chlorophyllase
131-176 7.06e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 41.57  E-value: 7.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2497687   131 PANWNSPLRP---------GEkYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAA 176
Cdd:PLN00021  31 ESSRPSPPKPllvatpseaGT-YPVLLFLHGYLLYNSFYSQLLQHIASHGFIVVA 84
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
254-322 8.26e-04

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 40.95  E-value: 8.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497687    254 DMEQLKDSIDREKIAVIGHSFGGATVIQTLSE-DQRFRCGIALDA--WMFPLGDEVYSRIPQPLFFINSEYF 322
Cdd:pfam00561  58 DLEYILEALGLEKVNLVGHSMGGLIALAYAAKyPDRVKALVLLGAldPPHELDEADRFILALFPGFFDGFVA 129
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
262-294 6.72e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.98  E-value: 6.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2497687    262 IDREKIAVIGHSFGGATVIQTL-SEDQRFRCGIA 294
Cdd:pfam00326  61 TDPDRLAIWGGSYGGYLTGAALnQRPDLFKAAVA 94
 
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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