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Conserved domains on  [gi|1832480075|ref|WP_168390323|]
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alpha/beta hydrolase [Acinetobacter indicus]

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]; ...
25-302 6.85e-32

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 119.25  E-value: 6.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  25 GDMCSATLHVPKEsATQKLPAVLMVGGWGS--IQGALtdsFINHFVTQGYAVMEFDYPGWGLSGGLPRQDINPWKRvkTV 102
Cdd:COG1073    20 GIKLAGDLYLPAG-ASKKYPAVVVAHGNGGvkEQRAL---YAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERR--DA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 103 NKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPELKGAIIQVPMLDgistvrsvpLPQMFkflgyglADRIKPGK 182
Cdd:COG1073    94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS---------LEDLA-------AQRAKEAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 183 RICIPTVSqpgqlgavdrdqawnamelakeklnidYDNRVTARSLLTMGFyRPWKRLKQVKVPMLIVGATQDTVAPF-VA 261
Cdd:COG1073   158 GAYLPGVP---------------------------YLPNVRLASLLNDEF-DPLAKIEKISRPLLFIHGEKDEAVPFyMS 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1832480075 262 KKI-EKVKNPfiqmKKI----EADHFDPYFEPyFSQNLRYQLDFLN 302
Cdd:COG1073   210 EDLyEAAAEP----KELlivpGAGHVDLYDRP-EEEYFDKLAEFFK 250
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
25-302 6.85e-32

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 119.25  E-value: 6.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  25 GDMCSATLHVPKEsATQKLPAVLMVGGWGS--IQGALtdsFINHFVTQGYAVMEFDYPGWGLSGGLPRQDINPWKRvkTV 102
Cdd:COG1073    20 GIKLAGDLYLPAG-ASKKYPAVVVAHGNGGvkEQRAL---YAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERR--DA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 103 NKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPELKGAIIQVPMLDgistvrsvpLPQMFkflgyglADRIKPGK 182
Cdd:COG1073    94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS---------LEDLA-------AQRAKEAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 183 RICIPTVSqpgqlgavdrdqawnamelakeklnidYDNRVTARSLLTMGFyRPWKRLKQVKVPMLIVGATQDTVAPF-VA 261
Cdd:COG1073   158 GAYLPGVP---------------------------YLPNVRLASLLNDEF-DPLAKIEKISRPLLFIHGEKDEAVPFyMS 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1832480075 262 KKI-EKVKNPfiqmKKI----EADHFDPYFEPyFSQNLRYQLDFLN 302
Cdd:COG1073   210 EDLyEAAAEP----KELlivpGAGHVDLYDRP-EEEYFDKLAEFFK 250
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
63-258 4.98e-11

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: 61.46  E-value: 4.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  63 FINHFVTQGYAVMEFDYPGWGLSGGLpRQDINPWKR-VKTVNKALSHLKSM-PQVdadNIIAWGTSFGGGHVVDLVAEHP 140
Cdd:pfam12146  23 LADALAAQGFAVYAYDHRGHGRSDGK-RGHVPSFDDyVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 141 E-LKGAIIQVPMLDgistVRSVPLPQMFKFLGYgLADRIKPGKRiciptVSQPGQLGAVDRDQAWNAmELAKEKLNIDyd 219
Cdd:pfam12146  99 DkVDGLILSAPALK----IKPYLAPPILKLLAK-LLGKLFPRLR-----VPNNLLPDSLSRDPEVVA-AYAADPLVHG-- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1832480075 220 nRVTARSLLTM--GFYRPWKRLKQVKVPMLIVGATQDTVAP 258
Cdd:pfam12146 166 -GISARTLYELldAGERLLRRAAAITVPLLLLHGGADRVVD 205
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
71-270 3.96e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 41.66  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  71 GYAVMEFDYPGWGLSGGL----PRQDinpwKRVKTVNKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHP-ELKGA 145
Cdd:PLN02385  115 GYGVFAMDYPGFGLSEGLhgyiPSFD----DLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPnAWDGA 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 146 IIQVPMLDGISTVrsVPLPQMFKFLgYGLAdRIKPGKRIciptVSQpgqlgavdRDQAWNAM-ELAKEKLN----IDYDN 220
Cdd:PLN02385  191 ILVAPMCKIADDV--VPPPLVLQIL-ILLA-NLLPKAKL----VPQ--------KDLAELAFrDLKKRKMAeynvIAYKD 254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1832480075 221 RVTARSLLTMgfYRPWK----RLKQVKVPMLIVGATQDTVA-PFVAKKI-EKVKNP 270
Cdd:PLN02385  255 KPRLRTAVEL--LRTTQeiemQLEEVSLPLLILHGEADKVTdPSVSKFLyEKASSS 308
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
25-302 6.85e-32

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 119.25  E-value: 6.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  25 GDMCSATLHVPKEsATQKLPAVLMVGGWGS--IQGALtdsFINHFVTQGYAVMEFDYPGWGLSGGLPRQDINPWKRvkTV 102
Cdd:COG1073    20 GIKLAGDLYLPAG-ASKKYPAVVVAHGNGGvkEQRAL---YAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERR--DA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 103 NKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPELKGAIIQVPMLDgistvrsvpLPQMFkflgyglADRIKPGK 182
Cdd:COG1073    94 RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS---------LEDLA-------AQRAKEAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 183 RICIPTVSqpgqlgavdrdqawnamelakeklnidYDNRVTARSLLTMGFyRPWKRLKQVKVPMLIVGATQDTVAPF-VA 261
Cdd:COG1073   158 GAYLPGVP---------------------------YLPNVRLASLLNDEF-DPLAKIEKISRPLLFIHGEKDEAVPFyMS 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1832480075 262 KKI-EKVKNPfiqmKKI----EADHFDPYFEPyFSQNLRYQLDFLN 302
Cdd:COG1073   210 EDLyEAAAEP----KELlivpGAGHVDLYDRP-EEEYFDKLAEFFK 250
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
25-259 1.06e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 88.54  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  25 GDMCSATLHVPKESatQKLPAVLMVGGWGSIQGALTDSFINHFVTQGYAVMEFDYPGWGLSGGLPRQDinpwkRVKTVNK 104
Cdd:COG1506     7 GTTLPGWLYLPADG--KKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGD-----EVDDVLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 105 ALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPEL-KGAIIQVPMLDGISTVRSVPlpqmfkflgygladrikpgkr 183
Cdd:COG1506    80 AIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRfKAAVALAGVSDLRSYYGTTR--------------------- 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832480075 184 iciptvsqpgQLGAVDRDQAWNAMELAKEklnidydnrvtarslltmgfYRPWKRLKQVKVPMLIVGATQDTVAPF 259
Cdd:COG1506   139 ----------EYTERLMGGPWEDPEAYAA--------------------RSPLAYADKLKTPLLLIHGEADDRVPP 184
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
23-146 4.20e-14

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 70.38  E-value: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  23 TEGDMCSATLHVPKESAtqKLPAVLMVGGWGSIQGALTDsFINHFVTQGYAVMEFDYPGWGLSGGLPRQD------INPW 96
Cdd:COG0412    11 PDGVTLPGYLARPAGGG--PRPGVVVLHEIFGLNPHIRD-VARRLAAAGYVVLAPDLYGRGGPGDDPDEAralmgaLDPE 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1832480075  97 KRVKTVNKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPELKGAI 146
Cdd:COG0412    88 LLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAV 137
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
24-303 1.71e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 62.71  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  24 EGDMCSATLHVPKESATqklPAVLMVGGWGSIQGALtDSFINHFVTQGYAVMEFDYPGWGLSGGlPRQDINPWKR-VKTV 102
Cdd:COG2267    12 DGLRLRGRRWRPAGSPR---GTVVLVHGLGEHSGRY-AELAEALAAAGYAVLAFDLRGHGRSDG-PRGHVDSFDDyVDDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 103 NKALSHLKSMPqvdADNIIAWGTSFGGGHVVDLVAEHPE-LKGAIIQVPMLdgistvRSVPLPqmfkflgygladrikpg 181
Cdd:COG2267    87 RAALDALRARP---GLPVVLLGHSMGGLIALLYAARYPDrVAGLVLLAPAY------RADPLL----------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 182 kriciptvsqpgqlgavdrdqawnamelakeklnidydnRVTARSLLTMgfyRPWKRLKQVKVPMLIVGATQDTVAPfvA 261
Cdd:COG2267   141 ---------------------------------------GPSARWLRAL---RLAEALARIDVPVLVLHGGADRVVP--P 176
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1832480075 262 KKIEKVKN---PFIQMKKIE-ADHfDPYFEPYFSQNLRYQLDFLNS 303
Cdd:COG2267   177 EAARRLAArlsPDVELVLLPgARH-ELLNEPAREEVLAAILAWLER 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
63-258 4.98e-11

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: 61.46  E-value: 4.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  63 FINHFVTQGYAVMEFDYPGWGLSGGLpRQDINPWKR-VKTVNKALSHLKSM-PQVdadNIIAWGTSFGGGHVVDLVAEHP 140
Cdd:pfam12146  23 LADALAAQGFAVYAYDHRGHGRSDGK-RGHVPSFDDyVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 141 E-LKGAIIQVPMLDgistVRSVPLPQMFKFLGYgLADRIKPGKRiciptVSQPGQLGAVDRDQAWNAmELAKEKLNIDyd 219
Cdd:pfam12146  99 DkVDGLILSAPALK----IKPYLAPPILKLLAK-LLGKLFPRLR-----VPNNLLPDSLSRDPEVVA-AYAADPLVHG-- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1832480075 220 nRVTARSLLTM--GFYRPWKRLKQVKVPMLIVGATQDTVAP 258
Cdd:pfam12146 166 -GISARTLYELldAGERLLRRAAAITVPLLLLHGGADRVVD 205
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
29-152 2.00e-08

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 54.81  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  29 SATLHVPKesATQKLPAVLMVGGWGSIQGALTDSFinHFVTQGYAVMEFDYPGWGLSGGL---PRQDINPW--------- 96
Cdd:COG3458    70 YGWLLRPK--GEGPLPAVVEFHGYGGGRGLPHEDL--DWAAAGYAVLVMDTRGQGSSWGDtpdPGGYSGGAlpgymtrgi 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832480075  97 --------KRVKT-VNKALSHLKSMPQVDADNIIAWGTSFGGGhvVDLVAE--HPELKGAIIQVPML 152
Cdd:COG3458   146 ddpdtyyyRRVYLdAVRAVDALRSLPEVDGKRIGVTGGSQGGG--LALAAAalDPRVKAAAADVPFL 210
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
44-304 7.86e-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: 49.23  E-value: 7.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  44 PAVLMVGGWGSiQGALTDSFINHFvTQGYAVMEFDYPGWGLSGGlPRQDINPWKRVKTVNKALSHLksmpqvDADNIIAW 123
Cdd:COG0596    24 PPVVLLHGLPG-SSYEWRPLIPAL-AAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDAL------GLERVVLV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 124 GTSFGGGHVVDLVAEHPELkgaiiqvpmldgistVRSvplpqmfkflgygladrikpgkriciptvsqpgqLGAVDRDQA 203
Cdd:COG0596    95 GHSMGGMVALELAARHPER---------------VAG----------------------------------LVLVDEVLA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 204 WnameLAKEKLNIDYDNRVTARSLLTMGFYRPWKRLKQVKVPMLIVGATQDTVAPF-VAKKIEKVkNPFIQMKKIE-ADH 281
Cdd:COG0596   126 A----LAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPaLARRLAEL-LPNAELVVLPgAGH 200
                         250       260
                  ....*....|....*....|....
gi 1832480075 282 FDPYFEP-YFSQNLRyqlDFLNSL 304
Cdd:COG0596   201 FPPLEQPeAFAAALR---DFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
44-288 7.21e-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: 46.34  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  44 PAVLMVGGWGSIqGALTDSFINHFVTQGYAVMEFDYPGWGLSGGLPRQDINP-WKRVKTVNKALSHLksmpqvDADNIIA 122
Cdd:pfam00561   1 PPVLLLHGLPGS-SDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRtDDLAEDLEYILEAL------GLEKVNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 123 WGTSFGGGHVVDLVAEHPEL-KGAIIQVPMLDGISTvRSVPLPQMFKFLGYGLADRIKPGKRICIPTVS-------QPGQ 194
Cdd:pfam00561  74 VGHSMGGLIALAYAAKYPDRvKALVLLGALDPPHEL-DEADRFILALFPGFFDGFVADFAPNPLGRLVAkllalllLRLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 195 LGAVDRDQAWNA--MELAKEKLNIDYdnRVTARSLLTMGFYRPWKRlkQVKVPMLIVGATQDTVAP-FVAKKIEKVKNPF 271
Cdd:pfam00561 153 LLKALPLLNKRFpsGDYALAKSLVTG--ALLFIETWSTELRAKFLG--RLDEPTLIIWGDQDPLVPpQALEKLAQLFPNA 228
                         250
                  ....*....|....*..
gi 1832480075 272 IQMKKIEADHFDPYFEP 288
Cdd:pfam00561 229 RLVVIPDAGHFAFLEGP 245
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
29-254 8.91e-06

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 46.84  E-value: 8.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  29 SATLHVPKEsATQKLPAVLM-----VGGWGSIQGALTDsfiNHFVTQGYAVMEFDYPGWGLSGGLPRqdinPWKRVktvn 103
Cdd:COG2936    26 AADIYRPKD-AEGPVPVILErtpygKRDGTAGRDLGPH---PYFAERGYAVVVQDVRGTGGSEGEFD----PYRVD---- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 104 kalshlksmPQVDADNIIAW--------------GTSFgGGHVVDLVAE--HPELKGAIIQVPMLDGISTVR----SVPL 163
Cdd:COG2936    94 ---------EQTDGYDTIDWlakqpwsngkvgmiGISY-GGFTQLAAAAdrPPALKAIVPQAPTSDRYDDDHyhggAFLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 164 PQMFKFLGYGLADRIKPGKriciPTVSQPGQLGAVDRDQAWNAMELAkeklNIDYDNRV--TARSLLTMGFYRPW----- 236
Cdd:COG2936   164 GFNLGWAATMGAYKERPPD----PADARWRELLPDDYADRLEHLPLS----DADALGEQlpFWEDWLAHPDYDAFwqers 235
                         250       260
                  ....*....|....*....|
gi 1832480075 237 --KRLKQVKVPMLIVGATQD 254
Cdd:COG2936   236 llEDLDRIKVPVLAVGGWYD 255
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
70-153 1.35e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 45.30  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  70 QGYAVMEFDYPGwglSGGLPRQDINPWKRVKTVN------KALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPEL- 142
Cdd:pfam00326  13 RGYVVAIANGRG---SGGYGEAFHDAGKGDLGQNefddfiAAAEYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPDLf 89
                          90
                  ....*....|.
gi 1832480075 143 KGAIIQVPMLD 153
Cdd:pfam00326  90 KAAVAHVPVVD 100
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
29-147 1.86e-05

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 46.02  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  29 SATLHVPKESAtqKLPAVLMVGGWGSIQGALTDSFINHFVTQGYAVMEFDYPGWGLSGGLP-RQDINPWKRvktvnKALS 107
Cdd:pfam06500 182 TGFLHMPKGDG--PFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWKlTQDSSCLHQ-----AVLN 254
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1832480075 108 HLKSMPQVDADNIIAWGTSFGGGHVVDL-VAEHPELK-----GAII 147
Cdd:pfam06500 255 ALADVPWVDHTRVGLFGFRFGANVAVRLaYLESPRVKavaclGPPV 300
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
46-288 1.89e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 44.77  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  46 VLMVGGWGSIQGALTDsfinhFVTQGYAVMEFDYPGWGLSGGLPRqdinPWKRVKTVNKALSHLksmpqVDADNIIAWGT 125
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA-----LLAAGVAVLAPDLPGHGSSSPPPL----DLADLADLAALLDEL-----GAARPVVLVGH 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 126 SFgGGHVVDLVAEHPELKGAII--QVPMLDGISTVRSVPLPQMFKFLGYGLADRIKPGKRIciptvsqpgqLGAVDRDQA 203
Cdd:pfam12697  67 SL-GGAVALAAAAAALVVGVLVapLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGF----------LDDLPADAE 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 204 WNAMelakeklnidydnRVTARSLLTMGFYRPWKRLKQVKVPMLIVGATQDTVAPFVAKKIEKVKNPFIQMKKiEADHFd 283
Cdd:pfam12697 136 WAAA-------------LARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLP-GAGHL- 200

                  ....*
gi 1832480075 284 PYFEP 288
Cdd:pfam12697 201 PLDDP 205
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
30-152 4.82e-05

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 44.31  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  30 ATLHVPKESAtQKLPAVLMVGGWGSIQGALTDsfINHFVTQGYAVMEFD-------------------YPGWGLSGGLPR 90
Cdd:pfam05448  70 AWYVVPKESE-EKHPAVVHFHGYNGRRGDWHD--MLHWAAHGYAVFVMDvrgqgglseddprgpkgntYKGHITRGLLDR 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832480075  91 QDINpWKRVKT-VNKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHPELKGAIIQVPML 152
Cdd:pfam05448 147 ETYY-YRRVFLdAVRAVEIVMSFPEVDEERIVVTGGSQGGALALAAAALSPRIKAVVADYPFL 208
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
66-281 5.94e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.78  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  66 HFVTQGYAVMEFDYPGWGLSGG-LPRQDINPWkrVKTVNKALSHLKSmpqvDADNIIAWGTSFGGGHVVDLVAEHPELKG 144
Cdd:COG1647    37 ALAKAGYTVYAPRLPGHGTSPEdLLKTTWEDW--LEDVEEAYEILKA----GYDKVIVIGLSMGGLLALLLAARYPDVAG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 145 AIIQVPMLDGIStvRSVPLPQMFKFLGYGLadrikpgkriciptvsqpgqlgavdrdQAWNAMELAKEKLNIDYDnRVTA 224
Cdd:COG1647   111 LVLLSPALKIDD--PSAPLLPLLKYLARSL---------------------------RGIGSDIEDPEVAEYAYD-RTPL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832480075 225 RSLLTM-GFYRPWKR-LKQVKVPMLIVGATQDTVAPF-VAKKI-EKVKNPFIQMKKIE-ADH 281
Cdd:COG1647   161 RALAELqRLIREVRRdLPKITAPTLIIQSRKDEVVPPeSARYIyERLGSPDKELVWLEdSGH 222
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
25-254 3.19e-04

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 41.56  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  25 GDMCSATLHVPKESAtQKLPAVLMVGGWGSIQGALTDSFINH----FVTQGYAVMEFDYPGWGLSGGLPrqDINPWKRVK 100
Cdd:pfam02129   2 GVRLAADIYRPTKTG-GPVPALLTRSPYGARRDGASDLALAHpeweFAARGYAVVYQDVRGTGGSEGVF--TVGGPQEAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 101 TVNKALSHLKSMPQvDADNIIAWGTSFGGGHVVdLVAE--HPELKGAIIQVPMLDG---ISTVRSVPLPQMFKFLGYGL- 174
Cdd:pfam02129  79 DGKDVIDWLAGQPW-CNGKVGMTGISYLGTTQL-AAAAtgPPGLKAIAPESGISDLydyYREGGAVRAPGGLGWEDLDLl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 175 --------ADRIKPGKRICIPTVSQPGQLGAVDRDQAWNAMELAKEklniDYDNRVTARSLLtmgfyrpwKRLKQVKVPM 246
Cdd:pfam02129 157 aealtsrrADDGDAYRAAARYEAAGDELLAELDRQLFLLEWLLQTG----DYDAFWQDRNYL--------EDADKVKAPV 224

                  ....*...
gi 1832480075 247 LIVGATQD 254
Cdd:pfam02129 225 LLVGGWQD 232
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
71-270 3.96e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 41.66  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075  71 GYAVMEFDYPGWGLSGGL----PRQDinpwKRVKTVNKALSHLKSMPQVDADNIIAWGTSFGGGHVVDLVAEHP-ELKGA 145
Cdd:PLN02385  115 GYGVFAMDYPGFGLSEGLhgyiPSFD----DLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVALKVHLKQPnAWDGA 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832480075 146 IIQVPMLDGISTVrsVPLPQMFKFLgYGLAdRIKPGKRIciptVSQpgqlgavdRDQAWNAM-ELAKEKLN----IDYDN 220
Cdd:PLN02385  191 ILVAPMCKIADDV--VPPPLVLQIL-ILLA-NLLPKAKL----VPQ--------KDLAELAFrDLKKRKMAeynvIAYKD 254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1832480075 221 RVTARSLLTMgfYRPWK----RLKQVKVPMLIVGATQDTVA-PFVAKKI-EKVKNP 270
Cdd:PLN02385  255 KPRLRTAVEL--LRTTQeiemQLEEVSLPLLILHGEADKVTdPSVSKFLyEKASSS 308
 
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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