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Conserved domains on  [gi|1183596685|ref|NP_001337557|]
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lysophospholipase-like protein 1 isoform e [Homo sapiens]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 13-231 8.60e-38

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam02230:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 217  Bit Score: 131.73  E-value: 8.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  13 IVSPAGRHSASLIFLHGSGDSGQGlrmwIKQVLNQDLTFQHIKIIYPTAPPSYtvgpsfarSYTPMkGGISNVWFDRFKI 92
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSGHG----WADAAKTEAPLPNIKFIFPHGPEIP--------VTLNG-GMRMPAWFDLVGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  93 TNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQK 172
Cdd:pfam02230  73 SPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596685 173 SNGVLPElFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILK 231
Cdd:pfam02230 153 VTKKTPI-FLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIK 210
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 13-231 8.60e-38

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 131.73  E-value: 8.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  13 IVSPAGRHSASLIFLHGSGDSGQGlrmwIKQVLNQDLTFQHIKIIYPTAPPSYtvgpsfarSYTPMkGGISNVWFDRFKI 92
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSGHG----WADAAKTEAPLPNIKFIFPHGPEIP--------VTLNG-GMRMPAWFDLVGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  93 TNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQK 172
Cdd:pfam02230  73 SPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596685 173 SNGVLPElFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILK 231
Cdd:pfam02230 153 VTKKTPI-FLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIK 210
YpfH COG0400
Predicted esterase [General function prediction only];
17-239 1.36e-30

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 112.31  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  17 AGRHSASLIFLHGSGDSGQGLrMWIKQVLNQDltfqHIKIIYPTAP-PSYTVGPSfarsytpmkggisnvWFDRFKITND 95
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDL-LPLAPELALP----GAAVLAPRAPvPEGPGGRA---------------WFDLSFLEGR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  96 cpEHLESIDVMCQVLTDLIDE-EVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSN 174
Cdd:COG0400    61 --EDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1183596685 175 GvlPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPnVYHELSKTELDILKLWILTKLP 239
Cdd:COG0400   139 G--TPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYP-GGHEISPEELADARAWLAERLA 200
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 13-231 8.60e-38

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 131.73  E-value: 8.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  13 IVSPAGRHSASLIFLHGSGDSGQGlrmwIKQVLNQDLTFQHIKIIYPTAPPSYtvgpsfarSYTPMkGGISNVWFDRFKI 92
Cdd:pfam02230   6 VVSPRDPAQATVIFLHGLGDSGHG----WADAAKTEAPLPNIKFIFPHGPEIP--------VTLNG-GMRMPAWFDLVGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  93 TNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQK 172
Cdd:pfam02230  73 SPNAKEDEAGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596685 173 SNGVLPElFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILK 231
Cdd:pfam02230 153 VTKKTPI-FLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIK 210
YpfH COG0400
Predicted esterase [General function prediction only];
17-239 1.36e-30

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 112.31  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  17 AGRHSASLIFLHGSGDSGQGLrMWIKQVLNQDltfqHIKIIYPTAP-PSYTVGPSfarsytpmkggisnvWFDRFKITND 95
Cdd:COG0400     1 GGPAAPLVVLLHGYGGDEEDL-LPLAPELALP----GAAVLAPRAPvPEGPGGRA---------------WFDLSFLEGR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  96 cpEHLESIDVMCQVLTDLIDE-EVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSN 174
Cdd:COG0400    61 --EDEEGLAAAAEALAAFIDElEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1183596685 175 GvlPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPnVYHELSKTELDILKLWILTKLP 239
Cdd:COG0400   139 G--TPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYP-GGHEISPEELADARAWLAERLA 200
COG4099 COG4099
Predicted peptidase [General function prediction only];
24-220 4.53e-11

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 60.75  E-value: 4.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  24 LIFLHGSGDSGQ--------GLRMWIKQVLNQDltFQHIkIIYPTAPPsytvgpsfarsytpmkggisNVWFDRFKITND 95
Cdd:COG4099    52 VLFLHGAGERGTdnekqlthGAPKFINPENQAK--FPAI-VLAPQCPE--------------------DDYWSDTKALDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  96 cpehlesidvmcqvLTDLIDEEVKS-GIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAvyQALQKsn 174
Cdd:COG4099   109 --------------VLALLDDLIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDPANA--ANLKK-- 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1183596685 175 gvLPeLFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYH 220
Cdd:COG4099   171 --VP-VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGH 213
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
96-220 1.13e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 56.42  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  96 CPEH--LESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQD----VAGVFALSSFLN-KASAVYQ 168
Cdd:COG0657    55 APEHpfPAALEDAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRggprPAAQVLIYPVLDlTASPLRA 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1183596685 169 ALQKsngvLPELFQCHGTADELVLHS--WAEetnsMLKSLGVTTKFHSFPNVYH 220
Cdd:COG0657   135 DLAG----LPPTLIVTGEADPLVDESeaLAA----ALRAAGVPVELHVYPGGGH 180
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
119-226 1.29e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.56  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685 119 KSGIKKNRILIGGFSMGGCMAIHLAYRNHQ------DVAGVFALSSFLNKASAVYQALQKSNGVLPELFQ---------- 182
Cdd:COG1506    87 RPYVDPDRIGIYGHSYGGYMALLAAARHPDrfkaavALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAarsplayadk 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1183596685 183 -------CHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTE 226
Cdd:COG1506   167 lktplllIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAG 217
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-222 2.17e-06

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 47.30  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685   1 MAAASGSVLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDltfqhikiiyptappsYTV----GPSFARSYT 76
Cdd:COG2267     8 LPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAG----------------YAVlafdLRGHGRSDG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  77 PmkggisnvwfdrfkitndcPEHLESIDVMCQVLTDLIDEEVKSGikKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFAL 156
Cdd:COG2267    72 P-------------------RGHVDSFDDYVDDLRAALDALRARP--GLPVVLLGHSMGGLIALLYAARYPDRVAGLVLL 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1183596685 157 SSFLNK------------ASAVYQALQKSNgvLPELFqCHGTADELVLhswAEETNSMLKSLGVTTKFHSFPNVYHEL 222
Cdd:COG2267   131 APAYRAdpllgpsarwlrALRLAEALARID--VPVLV-LHGGADRVVP---PEAARRLAARLSPDVELVLLPGARHEL 202
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 17-220 3.16e-06

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: 46.53  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  17 AGRHSASLIFLHGSGDSGqglRMWIKQVlnqDLTFQHIKIIYPTAPpsytvGpsFARSytpmkggisnvwfdrfkitnDC 96
Cdd:COG0596    19 AGPDGPPVVLLHGLPGSS---YEWRPLI---PALAAGYRVIAPDLR-----G--HGRS--------------------DK 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  97 PEHLESIDVMCQVLTDLIDEEvksGIKknRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNGV 176
Cdd:COG0596    66 PAGGYTLDDLADDLAALLDAL---GLE--RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEA 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183596685 177 LPELFQ--------------------CHGTADELVLHSWAEETNSMLKslgvTTKFHSFPNVYH 220
Cdd:COG0596   141 LAALLRalartdlrerlaritvptlvIWGEKDPIVPPALARRLAELLP----NAELVVLPGAGH 200
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
120-220 2.21e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.19  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685 120 SGIKKNRILIGGFSMGGCMAIHLAyRNHQDVAGVFALSSFLNKASAVyQALQKSNGvlPELFqCHGTADELVLHSWAEET 199
Cdd:COG0412   104 PEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGGLPADDLL-DLAARIKA--PVLL-LYGEKDPLVPPEQVAAL 178

                          90       100
                  ....*....|....*....|.
gi 1183596685 200 NSMLKSLGVTTKFHSFPNVYH 220
Cdd:COG0412   179 EAALAAAGVDVELHVYPGAGH 199
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
125-161 3.08e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.78  E-value: 3.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1183596685 125 NRILIGGFSMGGCMAIHLAYRnHQDVAGVFALSSFLN 161
Cdd:COG1647    84 DKVIVIGLSMGGLLALLLAAR-YPDVAGLVLLSPALK 119
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
24-216 8.23e-05

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 42.92  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  24 LIFLHGSGDSGQGL--RMWIKQVLNQdLTFQHikiiypTAPPSYTVGPSfarsytpmkggiSNVWFDRFKITNDCPEHLE 101
Cdd:COG2382   115 LYLLDGGGGDEQDWfdQGRLPTILDN-LIAAG------KIPPMIVVMPD------------GGDGGDRGTEGPGNDAFER 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685 102 SI--DVMcqvltDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNgVLPE 179
Cdd:COG2382   176 FLaeELI-----PFVEKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWAE-LLAA 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1183596685 180 --------LFQCHGTADELVLHswAEETNSMLKSLGVTTKFHSFP 216
Cdd:COG2382   250 gapkkplrFYLDVGTEDDLLEA--NRALAAALKAKGYDVEYREFP 292
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 103-156 3.81e-03

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 37.18  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1183596685 103 IDVMCQVLTDLIDEEVKSGikkNRILIGGFSMGGCMAIHLAyrNHQDVAGVFAL 156
Cdd:pfam20408  57 APKLLEAFRAVIAALRGPD---LPLFIGGKSMGGRVASLLA--DDSGVKGVIAL 105
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
 26-191 4.47e-03

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 37.26  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  26 FLHGSGDSGQGLRMWIKQvLNQDLTFQHIKIIYPTAPPSYTVGPSFARSYTPMKGGISNV----WFDRFKITNDCPEHLE 101
Cdd:pfam03959   8 CLHGFGQSGEIFRAKTGA-LRKLLKKLGVEFVYLDAPFELAEPADLPGSESEKDEGEDDEpyraWFFGDDDTNEYLGLDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685 102 SIDVmcqvltdlideeVKSGIKKNR----ILigGFSMGGCMA-IHLAYRNHQDVAGV----FAL--SSFLNkASAVYQAL 170
Cdd:pfam03959  87 SLDY------------VRDYIKENGpfdgIL--GFSQGAALAaILASLLEEGLPLSHpplkFAIlfSGFRP-RPPIYQEY 151

                         170       180
                  ....*....|....*....|..
gi 1183596685 171 QKSNGV-LPELFqCHGTADELV 191
Cdd:pfam03959 152 YSEDPIqTPSLH-VIGELDTVV 172
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 99-158 8.57e-03

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: 36.42  E-value: 8.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596685  99 HLESIDVMCQVLTDLIDEEVKSGIKKNRILIGgFSMGGCMAIHLAYRNHQDVAGVfALSS 158
Cdd:pfam12146  51 HVPSFDDYVDDLDTFVDKIREEHPGLPLFLLG-HSMGGLIAALYALRYPDKVDGL-ILSA 108
 
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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