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Conserved domains on  [gi|79330737|ref|NP_001032065|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
22-314 1.06e-29

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: 114.33  E-value: 1.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  22 IKIFYRTYGHGPIKALLIIGLAGTHESWGPQIMGLtgtdkpnddddddggivsdDSGIEVCAFDNRGMGRSSVPThkSEY 101
Cdd:COG0596  12 VRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL-------------------AAGYRVIAPDLRGHGRSDKPA--GGY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 102 TTTIMANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGGFECFPKLDRKSLSIAIRFLKAKTP 181
Cdd:COG0596  71 TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 182 EQRAAvdldthyskdyleesvgtntrrailyqqyvkgisetgmqskygfdgqinacWLHKITkveielIRsagflVSVIH 261
Cdd:COG0596 151 TDLRE---------------------------------------------------RLARIT------VP-----TLVIW 168
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 79330737 262 GRHDVIAQICYARRLAQRLyPVARMVDL-HGGHLVSHERTEEVNKALLELIKAS 314
Cdd:COG0596 169 GEKDPIVPPALARRLAELL-PNAELVVLpGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
22-314 1.06e-29

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: 114.33  E-value: 1.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  22 IKIFYRTYGHGPIKALLIIGLAGTHESWGPQIMGLtgtdkpnddddddggivsdDSGIEVCAFDNRGMGRSSVPThkSEY 101
Cdd:COG0596  12 VRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL-------------------AAGYRVIAPDLRGHGRSDKPA--GGY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 102 TTTIMANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGGFECFPKLDRKSLSIAIRFLKAKTP 181
Cdd:COG0596  71 TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 182 EQRAAvdldthyskdyleesvgtntrrailyqqyvkgisetgmqskygfdgqinacWLHKITkveielIRsagflVSVIH 261
Cdd:COG0596 151 TDLRE---------------------------------------------------RLARIT------VP-----TLVIW 168
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 79330737 262 GRHDVIAQICYARRLAQRLyPVARMVDL-HGGHLVSHERTEEVNKALLELIKAS 314
Cdd:COG0596 169 GEKDPIVPPALARRLAELL-PNAELVVLpGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
35-300 3.12e-23

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: 97.19  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737    35 KALLII-GLAGTHESWGPQIMGLtgtdkpnddddddggivsDDSGIEVCAFDNRGMGRSSVPTHKSEYTTTIMANDSISL 113
Cdd:pfam00561   1 PPVLLLhGLPGSSDLWRKLAPAL------------------ARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   114 LDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLnvtgGGFECFPKLDRKSLSIAIRFLK------AKTPEQRAAV 187
Cdd:pfam00561  63 LEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLL----GALDPPHELDEADRFILALFPGffdgfvADFAPNPLGR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   188 DLDTHYSKDYLEESVGTNTRRAIL--YQQYVKGISETGMQSKYGFDGQINACWLHKITKVEIELIrsagflvsVIHGRHD 265
Cdd:pfam00561 139 LVAKLLALLLLRLRLLKALPLLNKrfPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTL--------IIWGDQD 210
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 79330737   266 VIAQICYARRLAQRLYPVARMVDLHGGHLVSHERT 300
Cdd:pfam00561 211 PLVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
21-314 5.92e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.67  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   21 AIKIFYRTYGHG-PIKALLIIGLAGTHESWGPQIMGLtgtdkpnddddddggivsdDSGIEVCAFDNRGMGRSSvpthKS 99
Cdd:PRK14875 118 GRTVRYLRLGEGdGTPVVLIHGFGGDLNNWLFNHAAL-------------------AAGRPVIALDLPGHGASS----KA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  100 EYTTTI--MANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGGfecfPKLDRKSLSiaiRFLK 177
Cdd:PRK14875 175 VGAGSLdeLAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLG----PEINGDYID---GFVA 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  178 AKTpeqRAAVdldthysKDYLEESV---GTNTRR---AILYQQYVKGISETGMQ-SKYGFDGQINAcwlhkitKVEIELI 250
Cdd:PRK14875 248 AES---RREL-------KPVLELLFadpALVTRQmveDLLKYKRLDGVDDALRAlADALFAGGRQR-------VDLRDRL 310
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79330737  251 RSAGFLVSVIHGRHDviaQICYARRlAQRLYPVARMVDLHG-GHLVSHERTEEVNKALLELIKAS 314
Cdd:PRK14875 311 ASLAIPVLVIWGEQD---RIIPAAH-AQGLPDGVAVHVLPGaGHMPQMEAAADVNRLLAEFLGKA 371
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
22-314 1.06e-29

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: 114.33  E-value: 1.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  22 IKIFYRTYGHGPIKALLIIGLAGTHESWGPQIMGLtgtdkpnddddddggivsdDSGIEVCAFDNRGMGRSSVPThkSEY 101
Cdd:COG0596  12 VRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPAL-------------------AAGYRVIAPDLRGHGRSDKPA--GGY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 102 TTTIMANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGGFECFPKLDRKSLSIAIRFLKAKTP 181
Cdd:COG0596  71 TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 182 EQRAAvdldthyskdyleesvgtntrrailyqqyvkgisetgmqskygfdgqinacWLHKITkveielIRsagflVSVIH 261
Cdd:COG0596 151 TDLRE---------------------------------------------------RLARIT------VP-----TLVIW 168
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 79330737 262 GRHDVIAQICYARRLAQRLyPVARMVDL-HGGHLVSHERTEEVNKALLELIKAS 314
Cdd:COG0596 169 GEKDPIVPPALARRLAELL-PNAELVVLpGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
35-300 3.12e-23

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: 97.19  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737    35 KALLII-GLAGTHESWGPQIMGLtgtdkpnddddddggivsDDSGIEVCAFDNRGMGRSSVPTHKSEYTTTIMANDSISL 113
Cdd:pfam00561   1 PPVLLLhGLPGSSDLWRKLAPAL------------------ARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   114 LDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLnvtgGGFECFPKLDRKSLSIAIRFLK------AKTPEQRAAV 187
Cdd:pfam00561  63 LEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLL----GALDPPHELDEADRFILALFPGffdgfvADFAPNPLGR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   188 DLDTHYSKDYLEESVGTNTRRAIL--YQQYVKGISETGMQSKYGFDGQINACWLHKITKVEIELIrsagflvsVIHGRHD 265
Cdd:pfam00561 139 LVAKLLALLLLRLRLLKALPLLNKrfPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTL--------IIWGDQD 210
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 79330737   266 VIAQICYARRLAQRLYPVARMVDLHGGHLVSHERT 300
Cdd:pfam00561 211 PLVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
21-314 5.92e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.67  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   21 AIKIFYRTYGHG-PIKALLIIGLAGTHESWGPQIMGLtgtdkpnddddddggivsdDSGIEVCAFDNRGMGRSSvpthKS 99
Cdd:PRK14875 118 GRTVRYLRLGEGdGTPVVLIHGFGGDLNNWLFNHAAL-------------------AAGRPVIALDLPGHGASS----KA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  100 EYTTTI--MANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGGfecfPKLDRKSLSiaiRFLK 177
Cdd:PRK14875 175 VGAGSLdeLAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLG----PEINGDYID---GFVA 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  178 AKTpeqRAAVdldthysKDYLEESV---GTNTRR---AILYQQYVKGISETGMQ-SKYGFDGQINAcwlhkitKVEIELI 250
Cdd:PRK14875 248 AES---RREL-------KPVLELLFadpALVTRQmveDLLKYKRLDGVDDALRAlADALFAGGRQR-------VDLRDRL 310
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79330737  251 RSAGFLVSVIHGRHDviaQICYARRlAQRLYPVARMVDLHG-GHLVSHERTEEVNKALLELIKAS 314
Cdd:PRK14875 311 ASLAIPVLVIWGEQD---RIIPAAH-AQGLPDGVAVHVLPGaGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
22-152 4.79e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 59.25  E-value: 4.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  22 IKIFYRTYG-HGPIKALLII--GLAGTHESWGPQIMGLTGtdkpnddddddggivsddSGIEVCAFDNRGMGRSSVPTHk 98
Cdd:COG2267  14 LRLRGRRWRpAGSPRGTVVLvhGLGEHSGRYAELAEALAA------------------AGYAVLAFDLRGHGRSDGPRG- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79330737  99 SEYTTTIMANDSISLLDHL---GWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLN 152
Cdd:COG2267  75 HVDSFDDYVDDLRAALDALrarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
PRK10673 PRK10673
esterase;
106-153 1.25e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 58.20  E-value: 1.25e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 79330737  106 MANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNV 153
Cdd:PRK10673  67 MAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDI 114
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
78-200 1.56e-08

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: 54.91  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737    78 GIEVCAFDNRGMGRSsvPTHKSEYT-TTIMANDSISLLDHL----GWKKAHIIGHSMGAMIACKLAAMAPERVLSLALln 152
Cdd:pfam12146  31 GFAVYAYDHRGHGRS--DGKRGHVPsFDDYVDDLDTFVDKIreehPGLPLFLLGHSMGGLIAALYALRYPDKVDGLIL-- 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 79330737   153 vTGGGFECFPKLDRKSLSIAIRFLKAKTPEQRAAVDLDTHYSKDYLEE 200
Cdd:pfam12146 107 -SAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSRDPEV 153
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
77-306 1.37e-06

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.62  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737    77 SGIEVCAFDNRGMGRSSVPTHksEYTTtimANDSISLLDHLG-WKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTG 155
Cdd:pfam12697  20 AGVAVLAPDLPGHGSSSPPPL--DLAD---LADLAALLDELGaARPVVLVGHSLGGAVALAAAAAALVVGVLVAPLAAPP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   156 GGFecfpkldrksLSIAIRFLKAKTPEQRAAVDLDTHYSKDYLEESVGTNTRRAILyqqyvkgisETGMQSKYGFDGQIN 235
Cdd:pfam12697  95 GLL----------AALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAAL---------ARLAALLAALALLPL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79330737   236 ACWLHKITKVeielirsagflvsVIHGRHDVIAQICYARRLAQRlyPVARMVDL-HGGHLVsHERTEEVNKA 306
Cdd:pfam12697 156 AAWRDLPVPV-------------LVLAEEDRLVPELAQRLLAAL--AGARLVVLpGAGHLP-LDDPEEVAEA 211
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
113-229 2.11e-05

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 46.24  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 113 LLDHLGWKKAH-IIGHSMGAMIACKLAAMAPERVLSLALLNVTgggfecfPKLDrkSLSIAIRFLkaktpeQRAAVDLDT 191
Cdd:COG2021 120 LLDHLGIERLAaVIGGSMGGMQALEWAVSYPDRVRRAIVIATA-------ARLS--AQNIAFNEV------QRQAIRADP 184
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 79330737 192 HYSK-DYLEESVGTN---TRRAILYQQYVkgiSETGMQSKYG 229
Cdd:COG2021 185 NWNGgDYYDGEGPRRglaLARMIGHITYR---SDDELNRKFG 223
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
78-312 4.06e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 44.55  E-value: 4.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  78 GIEVCAFDNRGMGRSsvPTHKSEYTTTIMANDSISLLDHL--GWKKAHIIGHSMGAMIACKLAAMAPErVLSLALLNVTg 155
Cdd:COG1647  42 GYTVYAPRLPGHGTS--PEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPA- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 156 ggfecfPKLDRKSLSIA--IRFLKAKTPEQRAAVDLDTHYSKDYleesvgTNTRRAILYQQYvkgisetgmqskygfdgq 233
Cdd:COG1647 118 ------LKIDDPSAPLLplLKYLARSLRGIGSDIEDPEVAEYAY------DRTPLRALAELQ------------------ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737 234 inacWLHKITKVEIELIRSAgflVSVIHGRHDVIAQICYARRLAQRLypVARMVDLH----GGHLVSHER-TEEVNKALL 308
Cdd:COG1647 168 ----RLIREVRRDLPKITAP---TLIIQSRKDEVVPPESARYIYERL--GSPDKELVwledSGHVITLDKdREEVAEEIL 238

                ....
gi 79330737 309 ELIK 312
Cdd:COG1647 239 DFLE 242
PRK05855 PRK05855
SDR family oxidoreductase;
81-131 5.46e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 45.36  E-value: 5.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 79330737   81 VCAFDNRGMGRSSVPTHKSEYTTTIMANDSISLLDHLG-WKKAHIIGHSMGA 131
Cdd:PRK05855  54 VVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSpDRPVHLLAHDWGS 105
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
78-145 1.19e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.08  E-value: 1.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79330737  78 GIEVCAFDNRGMGRSSVPTHKSEYtttimaNDSISLLDHL---GW---KKAHIIGHSMGAMIACKLAAMAPERV 145
Cdd:COG1506  51 GYAVLAPDYRGYGESAGDWGGDEV------DDVLAAIDYLaarPYvdpDRIGIYGHSYGGYMALLAAARHPDRF 118
metX PRK00175
homoserine O-acetyltransferase; Provisional
113-229 8.64e-04

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 40.94  E-value: 8.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  113 LLDHLGWKKAH-IIGHSMGAMIACKLAAMAPERVLSLALLNVTgggfecfPKLdrKSLSIAIRFLkaktpeQRAAVDLDT 191
Cdd:PRK00175 139 LLDALGITRLAaVVGGSMGGMQALEWAIDYPDRVRSALVIASS-------ARL--SAQNIAFNEV------ARQAILADP 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 79330737  192 HYSK-DYLEESVGTNT-----RRA--ILYqqyvkgISETGMQSKYG 229
Cdd:PRK00175 204 DWHGgDYYEHGVVPERglavaRMIghITY------LSDDELDEKFG 243
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
78-188 2.30e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 39.57  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737   78 GIEVCAFDNRGMGRSSVPTHKSEYTTTIMANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNV---- 153
Cdd:PRK00870  73 GHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTglpt 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 79330737  154 ----TGGGFECFPKLDRKSLSIAI-RFLKAKT-----PEQRAAVD 188
Cdd:PRK00870 153 gdgpMPDAFWAWRAFSQYSPVLPVgRLVNGGTvrdlsDAVRAAYD 197
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
36-138 2.52e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.23  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737    36 ALLIIGLAGTHESWGPQIMGLTGTDkpnddddddggivsddsgiEVCAFDNRGMGRSSVPTHKSE------YTTTIMAND 109
Cdd:PLN02980 1374 VLFLHGFLGTGEDWIPIMKAISGSA-------------------RCISIDLPGHGGSKIQNHAKEtqteptLSVELVADL 1434
                          90       100
                  ....*....|....*....|....*....
gi 79330737   110 SISLLDHLGWKKAHIIGHSMGAMIACKLA 138
Cdd:PLN02980 1435 LYKLIEHITPGKVTLVGYSMGARIALYMA 1463
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
106-157 5.24e-03

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 38.49  E-value: 5.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 79330737   106 MANDSISLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALLNVTGGG 157
Cdd:pfam03096  85 LADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKA 136
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
83-151 7.89e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 38.25  E-value: 7.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79330737   83 AFDNRGMGRSSVPThKSEYTTTIMAnDSI--SLLDHLGWKKAHIIGHSMGAMIACKLAAMAPERVLSLALL 151
Cdd:PLN03087 237 AVDLLGFGRSPKPA-DSLYTLREHL-EMIerSVLERYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLL 305
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
78-150 8.62e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 37.59  E-value: 8.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79330737  78 GIEVCAFDNRGMGRSS-VPTHKSEYTTtimaNDSISLLDHLGWKKAH------IIGHSMGAMIACKLAAMAPeRVLSLAL 150
Cdd:COG1073  64 GFNVLAFDYRGYGESEgEPREEGSPER----RDARAAVDYLRTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVIL 138
 
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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