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Conserved domains on  [gi|530382617|ref|XP_005249465|]
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platelet-activating factor acetylhydrolase isoform X1 [Homo sapiens]

Protein Classification

PAF-AH_p_II domain-containing protein( domain architecture ID 10506208)

PAF-AH_p_II domain-containing protein

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 530382617   48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382617  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 530382617   48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382617  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 530382617 131 PANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASatyyfkDQSAAEIGDKSWLYLRTLk 210
Cdd:COG4188   49 PATAPADAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAA------DLSAALDGLADALDPEEL- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 211 qeeethirneqvRQRAKECSQALSLILDIDHGKPvknaldlkfdmeQLKDSIDREKIAVIGHSFGGATVIQTLSE----- 285
Cdd:COG4188  122 ------------WERPLDLSFVLDQLLALNKSDP------------PLAGRLDLDRIGVIGHSLGGYTALALAGArldfa 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 286 ---------------------------DQRFRCGIALDAWMFP-LGDEVYSRIPQPLFFINSEY---FQYPANIIKMKKc 334
Cdd:COG4188  178 alrqycgknpdlqcraldlprlaydlrDPRIKAVVALAPGGSGlFGEEGLAAITIPVLLVAGSAddvTPAPDEQIRPFD- 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382617 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 530382617 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 530382617   48 AASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPSQ--DNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNIL-RLL 124
Cdd:pfam03403   1 AGSSGQVKIPAGNGPYPVGCTDLMIGHTLRGSFLRLYYPSDqaDEDREDTLWIPNKEYFQGLSEFLGTSSWLGNRLfALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  125 FGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWL 204
Cdd:pfam03403  81 VGSLTLPASWNSPFKTGEKYPLIVFSHGLGAFRTIYSAICIELASHGFVVAAVEHRDRSASATYFFKDKPAAEEEQKSWI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  205 YLRTLKQEEETHIRNEQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLS 284
Cdd:pfam03403 161 YLRKVKEEEEFHLRNEQVQQRAQECSKALSLILDINLGTPVENVLDSDFDWQQLKGNLDMSKIAVIGHSFGGATVIQSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617  285 EDQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFATGKI 364
Cdd:pfam03403 241 EDTRFRCGIALDAWMFPVGDDVYSKARQPLLFINSEKFQWAEDIFKMKKIYSPDKESKMITIKGSVHQNFSDFTFVTGKI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382617  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 530382617 131 PANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASatyyfkDQSAAEIGDKSWLYLRTLk 210
Cdd:COG4188   49 PATAPADAPAGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDHPGSNAA------DLSAALDGLADALDPEEL- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 211 qeeethirneqvRQRAKECSQALSLILDIDHGKPvknaldlkfdmeQLKDSIDREKIAVIGHSFGGATVIQTLSE----- 285
Cdd:COG4188  122 ------------WERPLDLSFVLDQLLALNKSDP------------PLAGRLDLDRIGVIGHSLGGYTALALAGArldfa 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 286 ---------------------------DQRFRCGIALDAWMFP-LGDEVYSRIPQPLFFINSEY---FQYPANIIKMKKc 334
Cdd:COG4188  178 alrqycgknpdlqcraldlprlaydlrDPRIKAVVALAPGGSGlFGEEGLAAITIPVLLVAGSAddvTPAPDEQIRPFD- 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382617 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 530382617 132 ANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR-------DRSASATYYFKDQSAAeigdksWL 204
Cdd:COG1073   25 GDLYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRgygesegEPREEGSPERRDARAA------VD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 205 YLRTLKQeeethirneqvrqrakecsqalslildidhgkpvknaldlkfdmeqlkdsIDREKIAVIGHSFGGATVIQTLS 284
Cdd:COG1073   99 YLRTLPG--------------------------------------------------VDPERIGLLGISLGGGYALNAAA 128
                        170
                 ....*....|....*.
gi 530382617 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 530382617 124 LFGSMTTPANwnsplrpGEKYPLVVFSHGLGAFRTL-YSAIGIDLASHGFIVAAVEHRDRSASAtyyfKDQSAAEIGDks 202
Cdd:COG1506   10 LPGWLYLPAD-------GKKYPVVVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESA----GDWGGDEVDD-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 203 wlylrtlkqeeethirneqvrqrakecsqalslildidhgkpVKNALDlkfdmeQLKDS--IDREKIAVIGHSFGGATVI 280
Cdd:COG1506   77 ------------------------------------------VLAAID------YLAARpyVDPDRIGIYGHSYGGYMAL 108
                        170
                 ....*....|....*.
gi 530382617 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 530382617 141 GEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYyfkdqsaaeigdkswlylrtlkqeeethirNE 220
Cdd:COG0412   26 GGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDLYGRGGPGDD------------------------------PD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 221 QVRQRAKECSQALsLILDIDHgkpvknALDLkfdmeqLK--DSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAW 298
Cdd:COG0412   76 EARALMGALDPEL-LAADLRA------ALDW------LKaqPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG 142
                        170       180
                 ....*....|....*....|...
gi 530382617 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 530382617  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 530382617 145 PLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR--DRSASATYYFKDQSAaeigdkswlYLRTLkqeeethirnEQV 222
Cdd:COG2267   29 GTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRghGRSDGPRGHVDSFDD---------YVDDL----------RAA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 223 RQRAKEcsqalslildiDHGKPVknaldlkfdmeqlkdsidrekiAVIGHSFGGATVIQTLSE-DQRFRcGIALDA---- 297
Cdd:COG2267   90 LDALRA-----------RPGLPV----------------------VLLGHSMGGLIALLYAARyPDRVA-GLVLLApayr 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382617 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 530382617 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 530382617  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 530382617  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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