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Conserved domains on  [gi|42573525|ref|NP_974859|]
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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

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]; ...
47-206 1.15e-25

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 100.76  E-value: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  47 LKTRRGNEIVA-IYIKH--PKANGTLLYSHGNAADLGQMFeLFIELSNRLRLNLMGYDYSGYGQSTGKASECNTYA--DI 121
Cdd:COG1073  15 FKSRDGIKLAGdLYLPAgaSKKYPAVVVAHGNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPErrDA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 122 DAAYTCLKEHYGVKDDQLILYGQSVGSGPTIDLASRTPNLRGVVLHSPILS-----------------GMRVLYPVKRTY 184
Cdd:COG1073  94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSledlaaqrakeargaylPGVPYLPNVRLA 173
                       170       180
                ....*....|....*....|....
gi 42573525 185 WF--DIYKNIDKIGAVTCPVLVIH 206
Cdd:COG1073 174 SLlnDEFDPLAKIEKISRPLLFIH 197
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
47-206 1.15e-25

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 100.76  E-value: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  47 LKTRRGNEIVA-IYIKH--PKANGTLLYSHGNAADLGQMFeLFIELSNRLRLNLMGYDYSGYGQSTGKASECNTYA--DI 121
Cdd:COG1073  15 FKSRDGIKLAGdLYLPAgaSKKYPAVVVAHGNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPErrDA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 122 DAAYTCLKEHYGVKDDQLILYGQSVGSGPTIDLASRTPNLRGVVLHSPILS-----------------GMRVLYPVKRTY 184
Cdd:COG1073  94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSledlaaqrakeargaylPGVPYLPNVRLA 173
                       170       180
                ....*....|....*....|....
gi 42573525 185 WF--DIYKNIDKIGAVTCPVLVIH 206
Cdd:COG1073 174 SLlnDEFDPLAKIEKISRPLLFIH 197
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
67-174 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525    67 GTLLYSHGNAADLGqMFELFIELSNRLRLNLMGYDYSGYGQSTgKASECNTYADIDAA--YTCLKEHYGvkDDQLILYGQ 144
Cdd:pfam00561   1 PPVLLLHGLPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSS-RPKAQDDYRTDDLAedLEYILEALG--LEKVNLVGH 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 42573525   145 SVGSGPTIDLASRTPNL-RGVVLHSPILSGM 174
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRvKALVLLGALDPPH 107
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
47-206 1.15e-25

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 100.76  E-value: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  47 LKTRRGNEIVA-IYIKH--PKANGTLLYSHGNAADLGQMFeLFIELSNRLRLNLMGYDYSGYGQSTGKASECNTYA--DI 121
Cdd:COG1073  15 FKSRDGIKLAGdLYLPAgaSKKYPAVVVAHGNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPErrDA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 122 DAAYTCLKEHYGVKDDQLILYGQSVGSGPTIDLASRTPNLRGVVLHSPILS-----------------GMRVLYPVKRTY 184
Cdd:COG1073  94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSledlaaqrakeargaylPGVPYLPNVRLA 173
                       170       180
                ....*....|....*....|....
gi 42573525 185 WF--DIYKNIDKIGAVTCPVLVIH 206
Cdd:COG1073 174 SLlnDEFDPLAKIEKISRPLLFIH 197
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
47-206 3.28e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 71.96  E-value: 3.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  47 LKTRRGNEI-VAIYIKHPKANGTLLYSHGNAADLGQMFELFIELSNRlRLNLMGYDYSGYGQSTGKASECNTY----ADI 121
Cdd:COG2267   8 LPTRDGLRLrGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFddyvDDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 122 DAAYTCLKEHYGVKddqLILYGQSVGSGPTIDLASRTPN-LRGVVLHSPILSGMRVLYPVKRtyWFDIYKNIDKIGAVTC 200
Cdd:COG2267  87 RAALDALRARPGLP---VVLLGHSMGGLIALLYAARYPDrVAGLVLLAPAYRADPLLGPSAR--WLRALRLAEALARIDV 161

                ....*.
gi 42573525 201 PVLVIH 206
Cdd:COG2267 162 PVLVLH 167
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
47-206 2.27e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 69.66  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  47 LKTRRGNEIVAIYIKhPKANG---TLLYSHGNAADLGQMFELFIELsnrlrLNLMGY-----DYSGYGQSTGKASEcNTY 118
Cdd:COG1506   2 FKSADGTTLPGWLYL-PADGKkypVVVYVHGGPGSRDDSFLPLAQA-----LASRGYavlapDYRGYGESAGDWGG-DEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 119 ADIDAAYTCLKEHYGVKDDQLILYGQSVGSGPTIDLASRTPNL-RGVVLHSPI------------LSGMRVLYPVKRTYW 185
Cdd:COG1506  75 DDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRfKAAVALAGVsdlrsyygttreYTERLMGGPWEDPEA 154
                       170       180
                ....*....|....*....|.
gi 42573525 186 FDIYKNIDKIGAVTCPVLVIH 206
Cdd:COG1506 155 YAARSPLAYADKLKTPLLLIH 175
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
68-206 1.12e-07

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: 50.77  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  68 TLLYSHGNAADLGQMFELFIELSNRLRLnlMGYDYSGYGQSTGKASECNTYADIDAAYTCLkEHYGVkdDQLILYGQSVG 147
Cdd:COG0596  25 PVVLLHGLPGSSYEWRPLIPALAAGYRV--IAPDLRGHGRSDKPAGGYTLDDLADDLAALL-DALGL--ERVVLVGHSMG 99
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573525 148 SGPTIDLASRTPN-LRGVVLHSPILSGMRVLYPVKRTY---------WFDIYKNIDKIGAVTCPVLVIH 206
Cdd:COG0596 100 GMVALELAARHPErVAGLVLVDEVLAALAEPLRRPGLApealaallrALARTDLRERLARITVPTLVIW 168
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
67-174 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525    67 GTLLYSHGNAADLGqMFELFIELSNRLRLNLMGYDYSGYGQSTgKASECNTYADIDAA--YTCLKEHYGvkDDQLILYGQ 144
Cdd:pfam00561   1 PPVLLLHGLPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSS-RPKAQDDYRTDDLAedLEYILEALG--LEKVNLVGH 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 42573525   145 SVGSGPTIDLASRTPNL-RGVVLHSPILSGM 174
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRvKALVLLGALDPPH 107
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
94-206 4.04e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.42  E-value: 4.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  94 RLNLMGY-----DYSGYGQSTGKASECNTY----------ADIDAAYTCLKEHYGVKDDQLILYGQSVGSGPTIDLASRT 158
Cdd:COG0412  51 RLAAAGYvvlapDLYGRGGPGDDPDEARALmgaldpellaADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARG 130
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 42573525 159 PNLRGVVlhspILSGMRVLYPvkrtywfdiykNIDKIGAVTCPVLVIH 206
Cdd:COG0412 131 PDLAAAV----SFYGGLPADD-----------LLDLAARIKAPVLLLY 163
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
70-206 2.04e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 41.47  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525  70 LYSHGNAADLGQMfelfIELSNRLR---LNLMGYDYSGYGQSTGKASECNT---YADIDAAYTCLKEHYgvkdDQLILYG 143
Cdd:COG1647  19 LLLHGFTGSPAEM----RPLAEALAkagYTVYAPRLPGHGTSPEDLLKTTWedwLEDVEEAYEILKAGY----DKVIVIG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525 144 QSVGSGPTIDLASRTPNLRGVVLHSPILS-------GMRVLYPVKRT---------------YWFDIY------------ 189
Cdd:COG1647  91 LSMGGLLALLLAARYPDVAGLVLLSPALKiddpsapLLPLLKYLARSlrgigsdiedpevaeYAYDRTplralaelqrli 170
                       170       180
                ....*....|....*....|.
gi 42573525 190 ----KNIDKIgavTCPVLVIH 206
Cdd:COG1647 171 revrRDLPKI---TAPTLIIQ 188
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
62-169 6.91e-04

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: 39.89  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525    62 HPKAngTLLYSHGnaadlgqmfelFIELSNRL-----RLNLMGY-----DYSGYGQSTGKASECNTY----ADIDAAYTC 127
Cdd:pfam12146   2 EPRA--VVVLVHG-----------LGEHSGRYahladALAAQGFavyayDHRGHGRSDGKRGHVPSFddyvDDLDTFVDK 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 42573525   128 LKEHYGVKDdqLILYGQSVGSGPTIDLASRTP-NLRGVVLHSP 169
Cdd:pfam12146  69 IREEHPGLP--LFLLGHSMGGLIAALYALRYPdKVDGLILSAP 109
DUF818 pfam05677
Chlamydia CHLPS protein (DUF818); This family consists of several Chlamydia CHLPS proteins, ...
21-147 3.55e-03

Chlamydia CHLPS protein (DUF818); This family consists of several Chlamydia CHLPS proteins, the function of which are unknown.


Pssm-ID: 253315  Cd Length: 364  Bit Score: 37.84  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573525    21 SYGFVSDVDRLYItevpRRDDVDVlklktrrgnEIVAIYIKHPKANGTLLYSHGNAADL--GQMFEL----FIELSNRLR 94
Cdd:pfam05677 105 SKNRVSSVRRVPI----QQDDLLI---------DTLEICLPQAPPDRWMLISLGNSDCLeeRAMIGLkkssWQRLAKLIG 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42573525    95 LNLMGYDYSGYGQSTGKASECNTYADIDAAYTCLKEH-YGVKDDQLILYGQSVG 147
Cdd:pfam05677 172 ANILVFNYPGVMSSTGSITRENLAKAYQACVRYLRDKeQGPGAKQIIAYGYSLG 225
 
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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