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Conserved domains on  [gi|1063722359|ref|NP_001329372|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917|37582413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 35-282 1.85e-39

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 143.90  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  35 QRKDLEVKNIRGDILQCSHYMPveRPEDRPLPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLG 114
Cdd:COG1073     9 NKEDVTFKSRDGIKLAGDLYLP--AGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 115 WNEKDDLKAVVEYLRTDGNV--SLIGLWGRSMGAVTSLMYGAEDPSIAAMVLDSPFSDLVDLM-MELVDTYKFRLPKFti 191
Cdd:COG1073    87 SPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLPGV-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 192 kfaiQYMRRAVQkkANFNITDLNTIKVAKSCFVPVLFGHAVDDDFIQPHHSERIYEAYIGDKNIIKFDG-DHN---SPRP 267
Cdd:COG1073   165 ----PYLPNVRL--ASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHVdlyDRPE 238

                         250
                  ....*....|....*
gi 1063722359 268 QFYFDSINIFFHNVL 282
Cdd:COG1073   239 EEYFDKLAEFFKKNL 253
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 35-282 1.85e-39

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 143.90  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  35 QRKDLEVKNIRGDILQCSHYMPveRPEDRPLPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLG 114
Cdd:COG1073     9 NKEDVTFKSRDGIKLAGDLYLP--AGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 115 WNEKDDLKAVVEYLRTDGNV--SLIGLWGRSMGAVTSLMYGAEDPSIAAMVLDSPFSDLVDLM-MELVDTYKFRLPKFti 191
Cdd:COG1073    87 SPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLPGV-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 192 kfaiQYMRRAVQkkANFNITDLNTIKVAKSCFVPVLFGHAVDDDFIQPHHSERIYEAYIGDKNIIKFDG-DHN---SPRP 267
Cdd:COG1073   165 ----PYLPNVRL--ASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHVdlyDRPE 238

                         250
                  ....*....|....*
gi 1063722359 268 QFYFDSINIFFHNVL 282
Cdd:COG1073   239 EEYFDKLAEFFKKNL 253
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 68-213 3.35e-08

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: 54.43  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  68 VIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLGWnEKDDLKAVVEYLRTDGNVSLIGLWGRSMGAV 147
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY-RTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063722359 148 TSLMYGAEDPS-IAAMVLDSPFSDLVDLmMELVDTYKFRLPKFtikfaiqyMRRAVQKKANFNITDL 213
Cdd:pfam00561  82 IALAYAAKYPDrVKALVLLGALDPPHEL-DEADRFILALFPGF--------FDGFVADFAPNPLGRL 139
PHA02857 PHA02857
monoglyceride lipase; Provisional
 43-182 4.60e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 42.18  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  43 NIRGDILQCSHYMPVERPEdrplPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTL---GWNEKD 119
Cdd:PHA02857    7 NLDNDYIYCKYWKPITYPK----ALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIddfGVYVRD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722359 120 DLKAVVEYLRTDGNVSLIgLWGRSMGAVTSLMYGAEDPSI-AAMVLDSPFSDLVDL-MMELVDTY 182
Cdd:PHA02857   83 VVQHVVTIKSTYPGVPVF-LLGHSMGATISILAAYKNPNLfTAMILMSPLVNAEAVpRLNLLAAK 146
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 35-282 1.85e-39

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 143.90  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  35 QRKDLEVKNIRGDILQCSHYMPveRPEDRPLPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLG 114
Cdd:COG1073     9 NKEDVTFKSRDGIKLAGDLYLP--AGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 115 WNEKDDLKAVVEYLRTDGNV--SLIGLWGRSMGAVTSLMYGAEDPSIAAMVLDSPFSDLVDLM-MELVDTYKFRLPKFti 191
Cdd:COG1073    87 SPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLPGV-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 192 kfaiQYMRRAVQkkANFNITDLNTIKVAKSCFVPVLFGHAVDDDFIQPHHSERIYEAYIGDKNIIKFDG-DHN---SPRP 267
Cdd:COG1073   165 ----PYLPNVRL--ASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHVdlyDRPE 238

                         250
                  ....*....|....*
gi 1063722359 268 QFYFDSINIFFHNVL 282
Cdd:COG1073   239 EEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
40-267 7.64e-25

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 102.79  E-value: 7.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  40 EVKNIRGDILQCSHYMPverPEDRPLPCVIYCHGNSGCRADASEAAIVLLPSN-ITIFTLDFSGSGLSGGEhvtLGWNEK 118
Cdd:COG1506     1 TFKSADGTTLPGWLYLP---ADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRgYAVLAPDYRGYGESAGD---WGGDEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 119 DDLKAVVEYLRTDGNVSL--IGLWGRSMGAVTSLMYGAEDPS-IAAMVLDSPFSDLVDlMMELVDTYKFRLPKFTIKFAI 195
Cdd:COG1506    75 DDVLAAIDYLAARPYVDPdrIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVSDLRS-YYGTTREYTERLMGGPWEDPE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063722359 196 QYMRRAvqkkanfNITDLNTIKVakscfvPVLFGHAVDDDFIQPHHSERIYEAYI---GDKNIIKFDG-DHNSPRP 267
Cdd:COG1506   154 AYAARS-------PLAYADKLKT------PLLLIHGEADDRVPPEQAERLYEALKkagKPVELLVYPGeGHGFSGA 216
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
59-262 4.85e-19

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 85.82  E-value: 4.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  59 RPEDRPLPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTL-GWNE-KDDLKAVVEYLRTDGNVSL 136
Cdd:COG2267    22 RPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVdSFDDyVDDLRAALDALRARPGLPV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 137 IgLWGRSMGAVTSLMYGAEDPS-IAAMVLDSPFSDLVDLMMELVDTYKfrlpkftikfaiqymrravqkkanfnitDLNT 215
Cdd:COG2267   102 V-LLGHSMGGLIALLYAARYPDrVAGLVLLAPAYRADPLLGPSARWLR----------------------------ALRL 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1063722359 216 IKVAKSCFVPVLFGHAVDDDFIQPHHSERIYEAYIGDKNIIKFDG-DH 262
Cdd:COG2267   153 AEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGaRH 200
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
66-262 9.02e-16

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 76.90  E-value: 9.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  66 PCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLGWNE-KDDLKAVVEYLRTDG-NVSLIGLwgrS 143
Cdd:COG1647    16 KGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDwLEDVEEAYEILKAGYdKVIVIGL---S 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 144 MGAVTSLMYGAEDPSIAAMVLDSPFSDLVDLMMELVD-----TYKFRLPKFTIK----FAIQYMRRAVqkKANFNITDLn 214
Cdd:COG1647    93 MGGLLALLLAARYPDVAGLVLLSPALKIDDPSAPLLPllkylARSLRGIGSDIEdpevAEYAYDRTPL--RALAELQRL- 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063722359 215 tIKVAKSCF----VPVLFGHAVDDDFIQPHHSERIYEAYIG-DKNIIKF-DGDH 262
Cdd:COG1647   170 -IREVRRDLpkitAPTLIIQSRKDEVVPPESARYIYERLGSpDKELVWLeDSGH 222
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-265 1.43e-09

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 58.09  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  66 PCVIYCHGNSGCRADAsEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLGWNE-KDDLKAVVEYLRtDGNVSLIGLwgrSM 144
Cdd:COG0596    24 PPVVLLHGLPGSSYEW-RPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDlADDLAALLDALG-LERVVLVGH---SM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 145 GAVTSLMYGAEDPS-IAAMVLdspFSDLVDLMMELVDTYKFRLPKFtikfaiqymRRAVQKKANFNITD-LNTIKVaksc 222
Cdd:COG0596    99 GGMVALELAARHPErVAGLVL---VDEVLAALAEPLRRPGLAPEAL---------AALLRALARTDLRErLARITV---- 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1063722359 223 fvPVLFGHAVDDDFIQPHHSERIYEAyIGDKNIIKFDG-DHNSP 265
Cdd:COG0596   163 --PTLVIWGEKDPIVPPALARRLAEL-LPNAELVVLPGaGHFPP 203
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 68-213 3.35e-08

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: 54.43  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  68 VIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTLGWnEKDDLKAVVEYLRTDGNVSLIGLWGRSMGAV 147
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY-RTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063722359 148 TSLMYGAEDPS-IAAMVLDSPFSDLVDLmMELVDTYKFRLPKFtikfaiqyMRRAVQKKANFNITDL 213
Cdd:pfam00561  82 IALAYAAKYPDrVKALVLLGALDPPHEL-DEADRFILALFPGF--------FDGFVADFAPNPLGRL 139
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 62-260 2.04e-06

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 49.14  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  62 DRPLPCVIYCHG---NSGCRADASEAaivLLPSNITIFTLDFSGSGLSGGE--HVTlGWNE-KDDLKAVVEYLRTDGNVS 135
Cdd:pfam12146   1 GEPRAVVVLVHGlgeHSGRYAHLADA---LAAQGFAVYAYDHRGHGRSDGKrgHVP-SFDDyVDDLDTFVDKIREEHPGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 136 LIGLWGRSMGAVTSLMYGAEDP-SIAAMVLDSPFSDLVDLMM---------------------------------ELVDT 181
Cdd:pfam12146  77 PLFLLGHSMGGLIAALYALRYPdKVDGLILSAPALKIKPYLAppilkllakllgklfprlrvpnnllpdslsrdpEVVAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 182 YK---FRLPKFTIKFAIQYMRRA--VQKKANfNITdlntikvakscfVPVLFGHAVDDDFIQPHHSERIYEAyIG--DKN 254
Cdd:pfam12146 157 YAadpLVHGGISARTLYELLDAGerLLRRAA-AIT------------VPLLLLHGGADRVVDPAGSREFYER-AGstDKT 222


                  ....*.
gi 1063722359 255 IIKFDG 260
Cdd:pfam12146 223 LKLYPG 228
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
59-248 1.72e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 46.11  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  59 RPE-DRPLPCVIYCHGNSG--------CRADASEAAIVLLPSnitifTLDFSGSGLSGGE----HVTLGWNE-KDDLKAV 124
Cdd:COG0412    22 RPAgGGPRPGVVVLHEIFGlnphirdvARRLAAAGYVVLAPD-----LYGRGGPGDDPDEaralMGALDPELlAADLRAA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 125 VEYLRTDGNVSL--IGLWGRSMGAVTSLMYGAEDPSIAAMVldsPFsdlvdlmmelvdtykfrlpkftikfaiqYMRRAv 202
Cdd:COG0412    97 LDWLKAQPEVDAgrVGVVGFCFGGGLALLAAARGPDLAAAV---SF----------------------------YGGLP- 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063722359 203 qkkANFNITDLNTIKvakscfVPVLFGHAVDDDFIQPHHSERIYEA 248
Cdd:COG0412   145 ---ADDLLDLAARIK------APVLLLYGEKDPLVPPEQVAALEAA 181
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
54-171 2.24e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 45.63  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  54 YMPveRPEDRPLPCVIYCHG---NSGCRADASEAAIVLL-PSNITIFTLDFSgsgLSgGEH---VTLgwnekDDLKAVVE 126
Cdd:COG0657     4 YRP--AGAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAaRAGAAVVSVDYR---LA-PEHpfpAAL-----EDAYAALR 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063722359 127 YLRT-----DGNVSLIGLWGRSMG----AVTSLMYGAED-PSIAAMVLDSPFSDL 171
Cdd:COG0657    73 WLRAnaaelGIDPDRIAVAGDSAGghlaAALALRARDRGgPRPAAQVLIYPVLDL 127
PHA02857 PHA02857
monoglyceride lipase; Provisional
 43-182 4.60e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 42.18  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359  43 NIRGDILQCSHYMPVERPEdrplPCVIYCHGNSGCRADASEAAIVLLPSNITIFTLDFSGSGLSGGEHVTL---GWNEKD 119
Cdd:PHA02857    7 NLDNDYIYCKYWKPITYPK----ALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIddfGVYVRD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063722359 120 DLKAVVEYLRTDGNVSLIgLWGRSMGAVTSLMYGAEDPSI-AAMVLDSPFSDLVDL-MMELVDTY 182
Cdd:PHA02857   83 VVQHVVTIKSTYPGVPVF-LLGHSMGATISILAAYKNPNLfTAMILMSPLVNAEAVpRLNLLAAK 146
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
113-269 6.01e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 41.45  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 113 LGWNEKDDLKAVVEYLRTDGNVSL--IGLWGRSMGAVTSLMYGAEDPSI-AAMVLDSPFSDLvdLMMELVDtykfrlpkf 189
Cdd:pfam00326  40 LGQNEFDDFIAAAEYLIEQGYTDPdrLAIWGGSYGGYLTGAALNQRPDLfKAAVAHVPVVDW--LAYMSDT--------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063722359 190 TIKFAIQYMRR--AVQKKANF----NITDLNTIKVAkscfVPVLFGHAVDDDFIQPHHSERIYEAYIG-DKN---IIKFD 259
Cdd:pfam00326 109 SLPFTERYMEWgnPWDNEEGYdylsPYSPADNVKVY----PPLLLIHGLLDDRVPPWQSLKLVAALQRkGVPfllLIFPD 184

                         170
                  ....*....|
gi 1063722359 260 GDHNSPRPQF 269
Cdd:pfam00326 185 EGHGIGKPRN 194
 
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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