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Conserved domains on  [gi|1580306375|gb|TAJ25443|]
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MAG: alpha/beta fold hydrolase, partial [Planctomycetota bacterium]

Protein Classification

YheT family hydrolase( domain architecture ID 10785476)

YheT family hydrolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
1-229 3.37e-72

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


:

Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 223.10  E-value: 3.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   1 CGGTEALARSIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdWLRGAAVVSPAVDLAASQQ 80
Cdd:COG0429   101 CGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDAP-PLKAAVAVSPPLDLAASAD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  81 RLDaDPRCRMYREFFLSGLKEQLRSRARVHSGLLDVSGLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPLVDSIRR 160
Cdd:COG0429   180 RLE-RGFNRLYQRYFLRSLKRKLRRKLALFPGLIDLEALKRIRTLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRV 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1580306375 161 PTLVITAQDDPFIPFDSFRGPrFQHNAWIQLLAPAQGGHVafiaaqaAAHRAWCDLDRHWAENRVAQFL 229
Cdd:COG0429   259 PTLILNAADDPFLPPECLPEA-AELNPNVTLELTKHGGHV-------GFISGKSPGRRYWLERRILEFL 319
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
1-229 3.37e-72

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 223.10  E-value: 3.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   1 CGGTEALARSIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdWLRGAAVVSPAVDLAASQQ 80
Cdd:COG0429   101 CGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDAP-PLKAAVAVSPPLDLAASAD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  81 RLDaDPRCRMYREFFLSGLKEQLRSRARVHSGLLDVSGLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPLVDSIRR 160
Cdd:COG0429   180 RLE-RGFNRLYQRYFLRSLKRKLRRKLALFPGLIDLEALKRIRTLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRV 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1580306375 161 PTLVITAQDDPFIPFDSFRGPrFQHNAWIQLLAPAQGGHVafiaaqaAAHRAWCDLDRHWAENRVAQFL 229
Cdd:COG0429   259 PTLILNAADDPFLPPECLPEA-AELNPNVTLELTKHGGHV-------GFISGKSPGRRYWLERRILEFL 319
PRK10985 PRK10985
putative hydrolase; Provisional
 7-200 1.54e-27

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 107.35  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   7 LARsIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdwLRGAAVVSPAVDLAASQQRLDADp 86
Cdd:PRK10985  105 LHR-IYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDLP--LDAAVIVSAPLMLEACSYRMEQG- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  87 RCRMYREFFLSGLKEQLRSRARVHSGLLDVS--GLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPLVDSIRRPTLV 164
Cdd:PRK10985  181 FSRVYQRYLLNLLKANAARKLAAYPGTLPINlaQLKSVRRLREFDDLITARIHGFADAIDYYRQCSALPLLNQIRKPTLI 260

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1580306375 165 ITAQDDPFIPFDSFrgPRFQH---NAWIQLLapAQGGHV 200
Cdd:PRK10985  261 IHAKDDPFMTHEVI--PKPESlppNVEYQLT--EHGGHV 295
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 17-174 2.62e-06

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: 47.11  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  17 TEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGElgasAPDWLRGAAVVSP-----AVDLAASQQRLDADPRCRMY 91
Cdd:pfam00561  52 TDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAK----YPDRVKALVLLGAldpphELDEADRFILALFPGFFDGF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  92 REFFLSGLKEQLRSRARVHSGL---LDVSGLGRVRTLLEFDRCYTGPLSRYGSAER-YYDEASALPLVDSIRRPTLVITA 167
Cdd:pfam00561 128 VADFAPNPLGRLVAKLLALLLLrlrLLKALPLLNKRFPSGDYALAKSLVTGALLFIeTWSTELRAKFLGRLDEPTLIIWG 207


                  ....*..
gi 1580306375 168 QDDPFIP 174
Cdd:pfam00561 208 DQDPLVP 214
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
1-229 3.37e-72

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 223.10  E-value: 3.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   1 CGGTEALARSIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdWLRGAAVVSPAVDLAASQQ 80
Cdd:COG0429   101 CGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDDAP-PLKAAVAVSPPLDLAASAD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  81 RLDaDPRCRMYREFFLSGLKEQLRSRARVHSGLLDVSGLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPLVDSIRR 160
Cdd:COG0429   180 RLE-RGFNRLYQRYFLRSLKRKLRRKLALFPGLIDLEALKRIRTLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRV 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1580306375 161 PTLVITAQDDPFIPFDSFRGPrFQHNAWIQLLAPAQGGHVafiaaqaAAHRAWCDLDRHWAENRVAQFL 229
Cdd:COG0429   259 PTLILNAADDPFLPPECLPEA-AELNPNVTLELTKHGGHV-------GFISGKSPGRRYWLERRILEFL 319
PRK10985 PRK10985
putative hydrolase; Provisional
 7-200 1.54e-27

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 107.35  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   7 LARsIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdwLRGAAVVSPAVDLAASQQRLDADp 86
Cdd:PRK10985  105 LHR-IYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGNMLACLLAKEGDDLP--LDAAVIVSAPLMLEACSYRMEQG- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  87 RCRMYREFFLSGLKEQLRSRARVHSGLLDVS--GLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPLVDSIRRPTLV 164
Cdd:PRK10985  181 FSRVYQRYLLNLLKANAARKLAAYPGTLPINlaQLKSVRRLREFDDLITARIHGFADAIDYYRQCSALPLLNQIRKPTLI 260

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1580306375 165 ITAQDDPFIPFDSFrgPRFQH---NAWIQLLapAQGGHV 200
Cdd:PRK10985  261 IHAKDDPFMTHEVI--PKPESlppNVEYQLT--EHGGHV 295
PLN02511 PLN02511
hydrolase
 1-236 3.64e-14

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 70.96  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375   1 CGGTEALARSIYHAGLTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGELGASAPdwLRGAAVVSPAVDLAASqq 80
Cdd:PLN02511  140 CADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSLGANILVNYLGEEGENCP--LSGAVSLCNPFDLVIA-- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  81 rlDADPRC---RMYREFFLSGLKEQLRSRARVHSGL---LDVSGLGRVRTLLEFDRCYTGPLSRYGSAERYYDEASALPL 154
Cdd:PLN02511  216 --DEDFHKgfnNVYDKALAKALRKIFAKHALLFEGLggeYNIPLVANAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDS 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375 155 VDSIRRPTLVITAQDDPFIPFDSFrgPR--FQHNAWIQLLAPAQGGHVafiaaqaaahrAWCDLDRH-----WAENRVAQ 227
Cdd:PLN02511  294 IKHVRVPLLCIQAANDPIAPARGI--PRedIKANPNCLLIVTPSGGHL-----------GWVAGPEApfgapWTDPVVME 360


                  ....*....
gi 1580306375 228 FLHHLEEGA 236
Cdd:PLN02511  361 FLEALEEGK 369
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
18-176 3.00e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 49.63  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  18 EDVAAVARELCEREGV--ERVYLVGCSLGGGMMLRwlgeLGASAPDWLRGAAVVSPAVDLAasqqrlDADPRCRMYREFF 95
Cdd:COG1506    75 DDVLAAIDYLAARPYVdpDRIGIYGHSYGGYMALL----AAARHPDRFKAAVALAGVSDLR------SYYGTTREYTERL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  96 LSGLKEqlrsrarvhsglldvsglgrvrtllefdrcytgplsrygsAERYYDEASALPLVDSIRRPTLVITAQDDPFIPF 175
Cdd:COG1506   145 MGGPWE----------------------------------------DPEAYAARSPLAYADKLKTPLLLIHGEADDRVPP 184


                  .
gi 1580306375 176 D 176
Cdd:COG1506   185 E 185
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 17-174 2.62e-06

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: 47.11  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  17 TEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGElgasAPDWLRGAAVVSP-----AVDLAASQQRLDADPRCRMY 91
Cdd:pfam00561  52 TDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAK----YPDRVKALVLLGAldpphELDEADRFILALFPGFFDGF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  92 REFFLSGLKEQLRSRARVHSGL---LDVSGLGRVRTLLEFDRCYTGPLSRYGSAER-YYDEASALPLVDSIRRPTLVITA 167
Cdd:pfam00561 128 VADFAPNPLGRLVAKLLALLLLrlrLLKALPLLNKRFPSGDYALAKSLVTGALLFIeTWSTELRAKFLGRLDEPTLIIWG 207


                  ....*..
gi 1580306375 168 QDDPFIP 174
Cdd:pfam00561 208 DQDPLVP 214
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
18-232 9.83e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.32  E-value: 9.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  18 EDVAAVARELceREGVERVYLVGCSLGGGMMLRwlgeLGASAPDwLRGAAVVSPAVDLAASQQRLdadprcrmyrEFFLS 97
Cdd:COG1647    70 EDVEEAYEIL--KAGYDKVIVIGLSMGGLLALL----LAARYPD-VAGLVLLSPALKIDDPSAPL----------LPLLK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  98 GLKEQLRSRAR-VHSGLLDVSGLGR--VRTLLEFDRcytgpLSRYgsaeryydeasALPLVDSIRRPTLVITAQDDPFIP 174
Cdd:COG1647   133 YLARSLRGIGSdIEDPEVAEYAYDRtpLRALAELQR-----LIRE-----------VRRDLPKITAPTLIIQSRKDEVVP 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1580306375 175 FDS----FRGprfQHNAWIQLLAPAQGGHVAFiaaqaaahrawCDLDRHWAENRVAQFLHHL 232
Cdd:COG1647   197 PESaryiYER---LGSPDKELVWLEDSGHVIT-----------LDKDREEVAEEILDFLERL 244
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 19-176 3.01e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.14  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  19 DVAAVARELCEREGV--ERVYLVGCSLGGGMMLrwlgELGASAPDwLRGAAVVSPAVDLAASQQRLDADPRCRMYREFFL 96
Cdd:COG1073    92 DARAAVDYLRTLPGVdpERIGLLGISLGGGYAL----NAAATDPR-VKAVILDSPFTSLEDLAAQRAKEARGAYLPGVPY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  97 sglkeqlrsrarvhsglldvsglgrvrtllefdrcytGPLSRYGSAERyyDEASALPLVDSIRRPTLVITAQDDPFIPFD 176
Cdd:COG1073   167 -------------------------------------LPNVRLASLLN--DEFDPLAKIEKISRPLLFIHGEKDEAVPFY 207
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
16-104 1.16e-04

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 41.91  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  16 LTEDVAAVARELCEREGvERVYLVGCSLGGGMMLRWLgelgASAPDWLRGAAVVSPavdlaasqqRLDADPRC----RMY 91
Cdd:COG2267    82 YVDDLRAALDALRARPG-LPVVLLGHSMGGLIALLYA----ARYPDRVAGLVLLAP---------AYRADPLLgpsaRWL 147

                          90
                  ....*....|...
gi 1580306375  92 REFFLSGLKEQLR 104
Cdd:COG2267   148 RALRLAEALARID 160
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 17-179 3.25e-04

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: 40.75  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  17 TEDVAAVARELCEREGVERVYLVGCSLGGGMMLrwlgELGASAPDWLRGAAVVSPAVDLAASQQRLDADPRcrmyreffl 96
Cdd:COG0596    72 LDDLADDLAALLDALGLERVVLVGHSMGGMVAL----ELAARHPERVAGLVLVDEVLAALAEPLRRPGLAP--------- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  97 SGLKEQLRSRARvhsglldvsglgrvrtllefdrcytgplsrygsaeryydeASALPLVDSIRRPTLVITAQDDPFIPFD 176
Cdd:COG0596   139 EALAALLRALAR----------------------------------------TDLRERLARITVPTLVIWGEKDPIVPPA 178


                  ...
gi 1580306375 177 SFR 179
Cdd:COG0596   179 LAR 181
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 20-70 4.79e-04

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 40.37  E-value: 4.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1580306375  20 VAAVARELCEREGV--ERVYLVGCSLGGGMMLRwlgeLGASAPDWLRGAAVVS 70
Cdd:COG3509   118 IAALVDDLAARYGIdpKRVYVTGLSAGGAMAYR----LACEYPDVFAAVAPVA 166
COG4099 COG4099
Predicted peptidase [General function prediction only];
35-76 1.98e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 38.41  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1580306375  35 RVYLVGCSLGGGMMLrwlgELGASAPDWLRGAAVVSPAVDLA 76
Cdd:COG4099   126 RIYLTGLSMGGYGTW----DLAARYPDLFAAAVPICGGGDPA 163
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 16-174 9.08e-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: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  16 LTEDVAAVARELCEREGVERVYLVGCSLGGGMMLRWLGElgasAPDWLRGAAVVSPAVDLAASQQRLDAdprcrmyreFF 95
Cdd:pfam12146  58 YVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALR----YPDKVDGLILSAPALKIKPYLAPPIL---------KL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580306375  96 LSGLKEQLRSRARVHSGLL------------------DVSGLGRVRTLLEFdrcytgplsrYGSAERyydeasALPLVDS 157
Cdd:pfam12146 125 LAKLLGKLFPRLRVPNNLLpdslsrdpevvaayaadpLVHGGISARTLYEL----------LDAGER------LLRRAAA 188

                         170
                  ....*....|....*..
gi 1580306375 158 IRRPTLVITAQDDPFIP 174
Cdd:pfam12146 189 ITVPLLLLHGGADRVVD 205
 
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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