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Conserved domains on  [gi|1721621667|gb|QEC26364|]
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alpha/beta hydrolase [Mannheimia haemolytica]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11455169)

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
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
30-248 1.16e-23

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


:

Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 94.68  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlkSNTKFGERLSSKykGYAALAFDFPCHGDDARKK---LSVEESITYLQLVIDYAKTSLNAKnLYAY 106
Cdd:COG2267    30 TVVLVHGLGEHSG--RYAELAEALAAA--GYAVLAFDLRGHGRSDGPRghvDSFDDYVDDLRAALDALRARPGLP-VVLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 107 GTSFGGYLTLKYLAEKGNPFRKIALRAPAvqiyhslmnrlseeerqklakgreilWGFDRQMKISQAFFDELTditqndY 186
Cdd:COG2267   105 GHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------YRADPLLGPSARWLRALR------L 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721621667 187 LDYAEQI----LILHGTEDEMVALSTSQQFAD--NNVIELLPIEGADHAFSNPKLMDIAIGKIVEFFA 248
Cdd:COG2267   153 AEALARIdvpvLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGARHELLNEPAREEVLAAILAWLE 220
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
30-248 1.16e-23

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 94.68  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlkSNTKFGERLSSKykGYAALAFDFPCHGDDARKK---LSVEESITYLQLVIDYAKTSLNAKnLYAY 106
Cdd:COG2267    30 TVVLVHGLGEHSG--RYAELAEALAAA--GYAVLAFDLRGHGRSDGPRghvDSFDDYVDDLRAALDALRARPGLP-VVLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 107 GTSFGGYLTLKYLAEKGNPFRKIALRAPAvqiyhslmnrlseeerqklakgreilWGFDRQMKISQAFFDELTditqndY 186
Cdd:COG2267   105 GHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------YRADPLLGPSARWLRALR------L 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721621667 187 LDYAEQI----LILHGTEDEMVALSTSQQFAD--NNVIELLPIEGADHAFSNPKLMDIAIGKIVEFFA 248
Cdd:COG2267   153 AEALARIdvpvLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGARHELLNEPAREEVLAAILAWLE 220
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
30-215 6.25e-12

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: 63.39  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSkdlkSNT--KFGERLSSKykGYAALAFDFPCHGDDARKKL---SVEESITYLQLVIDYAKTSLNAKNLY 104
Cdd:pfam12146   6 VVVLVHGLGEH----SGRyaHLADALAAQ--GFAVYAYDHRGHGRSDGKRGhvpSFDDYVDDLDTFVDKIREEHPGLPLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 105 AYGTSFGGYLTLKYLAEKGNPFRKIALRAPAVQIYHSLMNRLSEEERQKLAK---GREILWGFDRQM------------- 168
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKlfpRLRVPNNLLPDSlsrdpevvaayaa 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1721621667 169 ------KISQAFFDELTDITQnDYLDYAEQI----LILHGTEDEMVALSTSQQFADN 215
Cdd:pfam12146 160 dplvhgGISARTLYELLDAGE-RLLRRAAAItvplLLLHGGADRVVDPAGSREFYER 215
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
30-248 1.16e-23

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 94.68  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlkSNTKFGERLSSKykGYAALAFDFPCHGDDARKK---LSVEESITYLQLVIDYAKTSLNAKnLYAY 106
Cdd:COG2267    30 TVVLVHGLGEHSG--RYAELAEALAAA--GYAVLAFDLRGHGRSDGPRghvDSFDDYVDDLRAALDALRARPGLP-VVLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 107 GTSFGGYLTLKYLAEKGNPFRKIALRAPAvqiyhslmnrlseeerqklakgreilWGFDRQMKISQAFFDELTditqndY 186
Cdd:COG2267   105 GHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------YRADPLLGPSARWLRALR------L 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721621667 187 LDYAEQI----LILHGTEDEMVALSTSQQFAD--NNVIELLPIEGADHAFSNPKLMDIAIGKIVEFFA 248
Cdd:COG2267   153 AEALARIdvpvLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGARHELLNEPAREEVLAAILAWLE 220
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
30-248 1.96e-22

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 92.00  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlKSNTKFGERLSSKykGYAALAFDFPCHGDDARKKLSVEesITYLQLVIDYAKTS--LNAKNLYAYG 107
Cdd:COG1506    25 VVVYVHGGPGSRD-DSFLPLAQALASR--GYAVLAPDYRGYGESAGDWGGDE--VDDVLAAIDYLAARpyVDPDRIGIYG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 108 TSFGGYLTLKYLAEKGNPFRKIALRAPAV--QIYHSLMNRLSEEERQKLAKGREILWgfdrqmkisqaffdeltditQND 185
Cdd:COG1506   100 HSYGGYMALLAAARHPDRFKAAVALAGVSdlRSYYGTTREYTERLMGGPWEDPEAYA--------------------ARS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721621667 186 YLDYAEQI----LILHGTEDEMVALSTSQQFAD----NNV-IELLPIEGADHAFSNPKLMDiAIGKIVEFFA 248
Cdd:COG1506   160 PLAYADKLktplLLIHGEADDRVPPEQAERLYEalkkAGKpVELLVYPGEGHGFSGAGAPD-YLERILDFLD 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
30-247 2.84e-19

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 83.84  E-value: 2.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSK-DLKSntkFGERLSSKykGYAALAFDFPCHGDDAR--KKLSVEESITYLQLVIDYAKTslNAKNLYAY 106
Cdd:COG1647    17 GVLLLHGFTGSPaEMRP---LAEALAKA--GYTVYAPRLPGHGTSPEdlLKTTWEDWLEDVEEAYEILKA--GYDKVIVI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 107 GTSFGGYLTLkYLAEKGNPFRKIALRAPAVQIYHS------LMNRLSEE---ERQKLAKGREILWGFDRQMKISQAFFDE 177
Cdd:COG1647    90 GLSMGGLLAL-LLAARYPDVAGLVLLSPALKIDDPsapllpLLKYLARSlrgIGSDIEDPEVAEYAYDRTPLRALAELQR 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721621667 178 LTDITQNDYLDYAEQILILHGTEDEMVALSTSQQFADN---NVIELLPIEGADHAFSNPKLMDIAIGKIVEFF 247
Cdd:COG1647   169 LIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERlgsPDKELVWLEDSGHVITLDKDREEVAEEILDFL 241
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
8-247 3.34e-17

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 78.03  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667   8 NEQGLSIRCKLFYEKELQQIENVVIVLHGFGSSKDLKSntKFGERLSSKykGYAALAFDFPCHGD---DARkklsveESI 84
Cdd:COG1073    17 SRDGIKLAGDLYLPAGASKKYPAVVVAHGNGGVKEQRA--LYAQRLAEL--GFNVLAFDYRGYGEsegEPR------EEG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  85 TY----LQLVIDYAKTSL--NAKNLYAYGTSFGGYLTLKYLAEKGNPfRKIALRAPAVQIYHSLmnrlseEERQKLAKGR 158
Cdd:COG1073    87 SPerrdARAAVDYLRTLPgvDPERIGLLGISLGGGYALNAAATDPRV-KAVILDSPFTSLEDLA------AQRAKEARGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 159 EILWGFDRQMKISQAFFDELTDItqndyLDYAEQI----LILHGTEDEMVALSTSQQFAD--NNVIELLPIEGADHAFSN 232
Cdd:COG1073   160 YLPGVPYLPNVRLASLLNDEFDP-----LAKIEKIsrplLFIHGEKDEAVPFYMSEDLYEaaAEPKELLIVPGAGHVDLY 234
                         250
                  ....*....|....*
gi 1721621667 233 PKLMDIAIGKIVEFF 247
Cdd:COG1073   235 DRPEEEYFDKLAEFF 249
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
30-248 1.43e-14

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: 70.42  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlkSNTKFGERLSskyKGYAALAFDFPCHG--DDARKKLSVEESITYLQLVIDYaktsLNAKNLYAYG 107
Cdd:COG0596    25 PVVLLHGLPGSSY--EWRPLIPALA---AGYRVIAPDLRGHGrsDKPAGGYTLDDLADDLAALLDA----LGLERVVLVG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 108 TSFGGYLTLKYLAEKGNPFRKIALRAPAVQIYHSLMNRlseeerqklakgreilWGFDRqmkisQAFFDELTDITQNDYL 187
Cdd:COG0596    96 HSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR----------------PGLAP-----EALAALLRALARTDLR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721621667 188 DYAEQI----LILHGTEDEMVALSTSQQFADNNV-IELLPIEGADHA--FSNPklmDIAIGKIVEFFA 248
Cdd:COG0596   155 ERLARItvptLVIWGEKDPIVPPALARRLAELLPnAELVVLPGAGHFppLEQP---EAFAAALRDFLA 219
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
30-215 6.25e-12

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: 63.39  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSkdlkSNT--KFGERLSSKykGYAALAFDFPCHGDDARKKL---SVEESITYLQLVIDYAKTSLNAKNLY 104
Cdd:pfam12146   6 VVVLVHGLGEH----SGRyaHLADALAAQ--GFAVYAYDHRGHGRSDGKRGhvpSFDDYVDDLDTFVDKIREEHPGLPLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 105 AYGTSFGGYLTLKYLAEKGNPFRKIALRAPAVQIYHSLMNRLSEEERQKLAK---GREILWGFDRQM------------- 168
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKlfpRLRVPNNLLPDSlsrdpevvaayaa 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1721621667 169 ------KISQAFFDELTDITQnDYLDYAEQI----LILHGTEDEMVALSTSQQFADN 215
Cdd:pfam12146 160 dplvhgGISARTLYELLDAGE-RLLRRAAAItvplLLLHGGADRVVDPAGSREFYER 215
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
31-234 1.82e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 55.94  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  31 VIVLHGFGSSkdlksNTKFGERLSskyKGYAALAFDFPCHGDDARKKLSVEESITYLQLVIDYAktslNAKNLYAYGTSF 110
Cdd:pfam12697   1 VVLVHGAGLS-----AAPLAALLA---AGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELG----AARPVVLVGHSL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 111 GGYLTLKYLA--------------EKGNPFRKIALRAPAVQIYHSLMNRLSEEERQKLAKGREILWGFDRQMKISQAFFD 176
Cdd:pfam12697  69 GGAVALAAAAaalvvgvlvaplaaPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721621667 177 ELTDITQNDYLDYAEQILILHgTEDEMVALSTSQQFADNNVIELLPIEGADHA-FSNPK 234
Cdd:pfam12697 149 ALALLPLAAWRDLPVPVLVLA-EEDRLVPELAQRLLAALAGARLVVLPGAGHLpLDDPE 206
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
30-233 5.14e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 54.97  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGFGSSKDlkSNTKFGERLSSKykGYAALAFDFPCHG------DDARK---KLSVEESITYLQLVIDYAKT--SL 98
Cdd:COG0412    31 GVVVLHEIFGLNP--HIRDVARRLAAA--GYVVLAPDLYGRGgpgddpDEARAlmgALDPELLAADLRAALDWLKAqpEV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  99 NAKNLYAYGTSFGGYLTLkYLAEKGNPFRkialrapAVQIYHSLMNRLSEEERQKLAKGReilwgfdrqmkisqaffdel 178
Cdd:COG0412   107 DAGRVGVVGFCFGGGLAL-LAAARGPDLA-------AAVSFYGGLPADDLLDLAARIKAP-------------------- 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 179 tditqndyldyaeqILILHGTEDEMVALSTSQQFAD-----NNVIELLPIEGADHAFSNP 233
Cdd:COG0412   159 --------------VLLLYGEKDPLVPPEQVAALEAalaaaGVDVELHVYPGAGHGFTNP 204
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
29-230 6.23e-08

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: 52.12  E-value: 6.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  29 NVVIVLHGFGSSKDLksNTKFGERLSSKykGYAALAFDFPCHGDDARKKLSVEESITYLQLVIDYAKTSLNAKNLYAYGT 108
Cdd:pfam00561   1 PPVLLLHGLPGSSDL--WRKLAPALARD--GFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 109 SFGGYLTLKYLAEKGNPFRKIALRAP-------------AVQIYHSLMNRLSEE-----ERQKLAKGREILWGFDRQMKI 170
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGAldppheldeadrfILALFPGFFDGFVADfapnpLGRLVAKLLALLLLRLRLLKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 171 SQAFF-------------------DELTDITQNDY----LDYAEQILILHGTEDEMVALSTSQQFAD--NNVIELLPIEG 225
Cdd:pfam00561 157 LPLLNkrfpsgdyalakslvtgalLFIETWSTELRakflGRLDEPTLIIWGDQDPLVPPQALEKLAQlfPNARLVVIPDA 236

                  ....*
gi 1721621667 226 ADHAF 230
Cdd:pfam00561 237 GHFAF 241
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
30-239 4.49e-07

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 49.01  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLH---GFGSSKDLKSNTKFGERLSSKykGYAALAFDF---------PCHG----DDARKklsveesitylqlVIDY 93
Cdd:COG2945    25 VALILHphpLFGGTMDNKVVYTLARALVAA--GFAVLRFNFrgvgrsegeFDEGrgelDDAAA-------------ALDW 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  94 AKTsLNAKNLYAYGTSFGGYLTLKYLAEkGNPFRKIALRAPAVQIYHslmnrlseeerqklakgreilwgfdrqmkisqa 173
Cdd:COG2945    90 LRA-QNPLPLWLAGFSFGAYVALQLAMR-LPEVEGLILVAPPVNRYD--------------------------------- 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721621667 174 fFDELTDItqndyldyAEQILILHGTEDEMVALSTSQQFAD--NNVIELLPIEGADHAFSNpKLMDIA 239
Cdd:COG2945   135 -FSFLAPC--------PAPTLVIHGEQDEVVPPAEVLDWARplSPPLPVVVVPGADHFFHG-KLDELK 192
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
102-248 2.63e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 43.76  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667 102 NLYAYGTSFGGYLTLKYLAEKGNPFRKIALRAPAV--QIYHSLMNRLSEEerqklakgREILWGFDRQmkiSQAFFDELT 179
Cdd:pfam00326  65 RLAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVdwLAYMSDTSLPFTE--------RYMEWGNPWD---NEEGYDYLS 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721621667 180 DIT-QNDYLDYAeQILILHGTEDEMVALSTSQQFAD-----NNVIELLPIEGADHAFSNPKLMDIAIGKIVEFFA 248
Cdd:pfam00326 134 PYSpADNVKVYP-PLLLIHGLLDDRVPPWQSLKLVAalqrkGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLL 207
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
30-168 5.81e-04

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 40.51  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  30 VVIVLHGF-GSSKdlksntkfgerlsSKY----------KGYAALAFDF-PCHGDDARKKLS-----VEEsityLQLVID 92
Cdd:COG0429    63 LVVLLHGLeGSSD-------------SHYarglaralyaRGWDVVRLNFrGCGGEPNLLPRLyhsgdTED----LVWVLA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721621667  93 YAKTSLNAKNLYAYGTSFGGYLTLKYLAEKGN---PFRKIA--------------LRAPAVQIYHS-LMNRLSEEERQKL 154
Cdd:COG0429   126 HLRARYPYAPLYAVGFSLGGNLLLKYLGEQGDdapPLKAAVavsppldlaasadrLERGFNRLYQRyFLRSLKRKLRRKL 205
                         170       180
                  ....*....|....*....|....*
gi 1721621667 155 AKGREI-----------LWGFDRQM 168
Cdd:COG0429   206 ALFPGLidlealkrirtLREFDDAY 230
 
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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