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Conserved domains on  [gi|1595846013|gb|TDM60296|]
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alpha/beta fold hydrolase [Acinetobacter baumannii]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11445464)

alpha/beta hydrolase family protein 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
PubMed:  12369917|19508187|37582413|31545554
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
90-224 5.90e-14

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


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 70.82  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  90 TPPPVGGWPIVVWAHGTTGVADvcapskaalaDSTKDLISKLLAAGYVVVAPDYEGLGTSGihpflnvKSEAFSITDAVV 169
Cdd:COG1506    16 LPADGKKYPVVVYVHGGPGSRD----------DSFLPLAQALASRGYAVLAPDYRGYGESA-------GDWGGDEVDDVL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595846013 170 AARNYLSQRNLLTSKKWVTVGHSQGGHAALGAAQYASRaqlEYKGTVAVAPASNL 224
Cdd:COG1506    79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPD---RFKAAVALAGVSDL 130
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 127-382 1.17e-10

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam03583:

Pssm-ID: 473884  Cd Length: 286  Bit Score: 62.06  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 127 LISKLLAAGYVVVAPDYEGLGTSgihpFLNVKSEAFSITDAVVAARNYLSQRNLLTSKKWVTVGHSQGGHAALGAA---- 202
Cdd:pfam03583  18 LISPLLLQGYYVVVPDYEGPKST----FTVGRQSGYAVLDSIRAALKSGDSTGINSDAKVGLWGYSGGSLASGWAAelqp 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 203 QYAsrAQLEYKGTVAVAPASNLGFILIAGEQSVanatldkkismYAQLdtyTALVTAGIRNTQPTF-DYPQVFT-PQISS 280
Cdd:pfam03583  94 SYA--PELQLVGAALGGFAANLTATAEAVDGTV-----------FAGL---IALALNGLANEYPDFkSILYEETnDSGRE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 281 IAQQAETICSGPlgQAFGAGMTQYVTEHNGTLdgytRTQPNFMAVPLVKTFLDKDSQPLQVKVTTPIIIYQGLADSTVP- 359
Cdd:pfam03583 158 ALKKLSEMCLAD--ALIGYPGDSMFTGDNRVF----ESGWDILKDETISKTIEDNLLSKSAVPQIPVFIYHGVIDEIIPi 231

                         250       260       270
                  ....*....|....*....|....*....|
gi 1595846013 360 -------KVATDILISNATVVGTKINSYVT 382
Cdd:pfam03583 232 kdikklyQNWCDGGISSLEFAEDLSNGHFA 261
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
90-224 5.90e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 70.82  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  90 TPPPVGGWPIVVWAHGTTGVADvcapskaalaDSTKDLISKLLAAGYVVVAPDYEGLGTSGihpflnvKSEAFSITDAVV 169
Cdd:COG1506    16 LPADGKKYPVVVYVHGGPGSRD----------DSFLPLAQALASRGYAVLAPDYRGYGESA-------GDWGGDEVDDVL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595846013 170 AARNYLSQRNLLTSKKWVTVGHSQGGHAALGAAQYASRaqlEYKGTVAVAPASNL 224
Cdd:COG1506    79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPD---RFKAAVALAGVSDL 130
LIP pfam03583
Secretory lipase; These lipases are expressed and secreted during the infection cycle of these ...
 127-382 1.17e-10

Secretory lipase; These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.


Pssm-ID: 367570  Cd Length: 286  Bit Score: 62.06  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 127 LISKLLAAGYVVVAPDYEGLGTSgihpFLNVKSEAFSITDAVVAARNYLSQRNLLTSKKWVTVGHSQGGHAALGAA---- 202
Cdd:pfam03583  18 LISPLLLQGYYVVVPDYEGPKST----FTVGRQSGYAVLDSIRAALKSGDSTGINSDAKVGLWGYSGGSLASGWAAelqp 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 203 QYAsrAQLEYKGTVAVAPASNLGFILIAGEQSVanatldkkismYAQLdtyTALVTAGIRNTQPTF-DYPQVFT-PQISS 280
Cdd:pfam03583  94 SYA--PELQLVGAALGGFAANLTATAEAVDGTV-----------FAGL---IALALNGLANEYPDFkSILYEETnDSGRE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 281 IAQQAETICSGPlgQAFGAGMTQYVTEHNGTLdgytRTQPNFMAVPLVKTFLDKDSQPLQVKVTTPIIIYQGLADSTVP- 359
Cdd:pfam03583 158 ALKKLSEMCLAD--ALIGYPGDSMFTGDNRVF----ESGWDILKDETISKTIEDNLLSKSAVPQIPVFIYHGVIDEIIPi 231

                         250       260       270
                  ....*....|....*....|....*....|
gi 1595846013 360 -------KVATDILISNATVVGTKINSYVT 382
Cdd:pfam03583 232 kdikklyQNWCDGGISSLEFAEDLSNGHFA 261
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 100-222 5.76e-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: 44.00  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 100 VVWAHGttgvadvcapskaalADSTKDLISKLLAAGYVVVAPDYEGLGTSGIHPFlnvkseAFSITDAVVAArnylsQRN 179
Cdd:pfam12697   1 VVLVHG---------------AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPL------DLADLADLAAL-----LDE 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1595846013 180 LLTSKKWVTVGHSQGGHAALGAAQYASRAqleykgTVAVAPAS 222
Cdd:pfam12697  55 LGAARPVVLVGHSLGGAVALAAAAAALVV------GVLVAPLA 91
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
90-224 5.90e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 70.82  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  90 TPPPVGGWPIVVWAHGTTGVADvcapskaalaDSTKDLISKLLAAGYVVVAPDYEGLGTSGihpflnvKSEAFSITDAVV 169
Cdd:COG1506    16 LPADGKKYPVVVYVHGGPGSRD----------DSFLPLAQALASRGYAVLAPDYRGYGESA-------GDWGGDEVDDVL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595846013 170 AARNYLSQRNLLTSKKWVTVGHSQGGHAALGAAQYASRaqlEYKGTVAVAPASNL 224
Cdd:COG1506    79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPD---RFKAAVALAGVSDL 130
LIP pfam03583
Secretory lipase; These lipases are expressed and secreted during the infection cycle of these ...
 127-382 1.17e-10

Secretory lipase; These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.


Pssm-ID: 367570  Cd Length: 286  Bit Score: 62.06  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 127 LISKLLAAGYVVVAPDYEGLGTSgihpFLNVKSEAFSITDAVVAARNYLSQRNLLTSKKWVTVGHSQGGHAALGAA---- 202
Cdd:pfam03583  18 LISPLLLQGYYVVVPDYEGPKST----FTVGRQSGYAVLDSIRAALKSGDSTGINSDAKVGLWGYSGGSLASGWAAelqp 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 203 QYAsrAQLEYKGTVAVAPASNLGFILIAGEQSVanatldkkismYAQLdtyTALVTAGIRNTQPTF-DYPQVFT-PQISS 280
Cdd:pfam03583  94 SYA--PELQLVGAALGGFAANLTATAEAVDGTV-----------FAGL---IALALNGLANEYPDFkSILYEETnDSGRE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 281 IAQQAETICSGPlgQAFGAGMTQYVTEHNGTLdgytRTQPNFMAVPLVKTFLDKDSQPLQVKVTTPIIIYQGLADSTVP- 359
Cdd:pfam03583 158 ALKKLSEMCLAD--ALIGYPGDSMFTGDNRVF----ESGWDILKDETISKTIEDNLLSKSAVPQIPVFIYHGVIDEIIPi 231

                         250       260       270
                  ....*....|....*....|....*....|
gi 1595846013 360 -------KVATDILISNATVVGTKINSYVT 382
Cdd:pfam03583 232 kdikklyQNWCDGGISSLEFAEDLSNGHFA 261
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
85-221 3.95e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 59.25  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  85 VFTPNTPPPvggwPIVVWAHGTTGVADVCAPskaaladstkdLISKLLAAGYVVVAPDYEGLGTSGiHPFLNVKSEAFSI 164
Cdd:COG2267    20 RWRPAGSPR----GTVVLVHGLGEHSGRYAE-----------LAEALAAAGYAVLAFDLRGHGRSD-GPRGHVDSFDDYV 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846013 165 TDaVVAARNYLSQRnllTSKKWVTVGHSQGGHAALgaaQYASRAQLEYKGTVAVAPA 221
Cdd:COG2267    84 DD-LRAALDALRAR---PGLPVVLLGHSMGGLIAL---LYAARYPDRVAGLVLLAPA 133
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
76-220 4.38e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 53.43  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  76 GQEVQATslVFTPNTPPPvggWPIVVWAHGTTGVADvcapskaaladSTKDLISKLLAAGYVVVAPD-YEGLGTSGIHPF 154
Cdd:COG0412    13 GVTLPGY--LARPAGGGP---RPGVVVLHEIFGLNP-----------HIRDVARRLAAAGYVVLAPDlYGRGGPGDDPDE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846013 155 LNVKSEAFSI---TDAVVAARNYLSQRNLLTSKKWVTVGHSQGGHAALgaaqYASRAQLEYKGTVAVAP 220
Cdd:COG0412    77 ARALMGALDPellAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLAL----LAAARGPDLAAAVSFYG 141
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 85-224 6.44e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 53.38  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  85 VFTPNTPPPvgGWPIVVWAHGTTGVADVCApskaaladstkDLISKLLAAGYVVVAPDYEGLGTSGIHPFLnvkSEAFSI 164
Cdd:COG1073    27 LYLPAGASK--KYPAVVVAHGNGGVKEQRA-----------LYAQRLAELGFNVLAFDYRGYGESEGEPRE---EGSPER 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 165 TDAvVAARNYLSQRNLLTSKKWVTVGHSQGGHAALGAAQYASRAqleyKGTVAVAPASNL 224
Cdd:COG1073    91 RDA-RAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRV----KAVILDSPFTSL 145
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 100-222 5.76e-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: 44.00  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 100 VVWAHGttgvadvcapskaalADSTKDLISKLLAAGYVVVAPDYEGLGTSGIHPFlnvkseAFSITDAVVAArnylsQRN 179
Cdd:pfam12697   1 VVLVHG---------------AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPL------DLADLADLAAL-----LDE 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1595846013 180 LLTSKKWVTVGHSQGGHAALGAAQYASRAqleykgTVAVAPAS 222
Cdd:pfam12697  55 LGAARPVVLVGHSLGGAVALAAAAAALVV------GVLVAPLA 91
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 98-223 6.90e-05

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: 44.03  E-value: 6.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  98 PIVVWAHGTTGVADVCAPskaaladstkdLISKLLAAGYVVVAPDYEGLGTSGIHPFLnvksEAFSiTDAVVAARNYLsq 177
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRK-----------LAPALARDGFRVIALDLRGFGKSSRPKAQ----DDYR-TDDLAEDLEYI-- 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1595846013 178 RNLLTSKKWVTVGHSQGGhaaLGAAQYASRAQLEYKGTVAVAPASN 223
Cdd:pfam00561  63 LEALGLEKVNLVGHSMGG---LIALAYAAKYPDRVKALVLLGALDP 105
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 98-203 1.75e-04

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 42.68  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  98 PIVVWAHGTTGVADVCAPskaaLADstkdliskLLAAGYVVVAPDYEGLGTSGIHPflnvksEAFSITDAVVAARNYLSQ 177
Cdd:COG0596    24 PPVVLLHGLPGSSYEWRP----LIP--------ALAAGYRVIAPDLRGHGRSDKPA------GGYTLDDLADDLAALLDA 85

                          90       100
                  ....*....|....*....|....*.
gi 1595846013 178 RNLltsKKWVTVGHSQGGHAALGAAQ 203
Cdd:COG0596    86 LGL---ERVVLVGHSMGGMVALELAA 108
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
85-202 5.90e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.63  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  85 VFTPNTPPPV----GGWPIVVWAHGTTGVADVCAPSKAALAdstkdliskllAAGYVVVAPDYEGLGTSGIHPFLNVKSE 160
Cdd:COG4188    46 VWYPATAPADapagGPFPLVVLSHGLGGSREGYAYLAEHLA-----------SHGYVVAAPDHPGSNAADLSAALDGLAD 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846013 161 AFSITDAVVAAR------NYLSQRNLLTS--------KKWVTVGHSQGGHAALGAA 202
Cdd:COG4188   115 ALDPEELWERPLdlsfvlDQLLALNKSDPplagrldlDRIGVIGHSLGGYTALALA 170
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
76-219 6.40e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 41.41  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  76 GQEVQATslVFTPNTPPPvggwPIVVWaHGTTGV-ADVCAPSKAALAdstkdliskllAAGYVVVAPDYEGLGTSGIHPf 154
Cdd:COG4757    17 GYPLAAR--LFPPAGPPR----AVVLI-NPATGVpQRFYRPFARYLA-----------ERGFAVLTYDYRGIGLSRPGS- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846013 155 lnVKSEAFSITDAVV----AARNYLSQRnlLTSKKWVTVGHSQGGHaALGAAQYASRAqleyKGTVAVA 219
Cdd:COG4757    78 --LRGFDAGYRDWGEldlpAVLDALRAR--FPGLPLLLVGHSLGGQ-LLGLAPNAERV----DRLVTVA 137
DLH pfam01738
Dienelactone hydrolase family;
84-207 1.29e-03

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 40.03  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013  84 LVFTPNTPPpvggWPIVVWAHGTTGVadvcapskaalaDSTKDLIS-KLLAAGYVVVAPD-YEGLGTSGIHP-------- 153
Cdd:pfam01738   3 YLATPKNPP----WPVVVVFQEIFGV------------NDNIREIAdRLADEGYVALAPDlYFRQGDPNDEAdaaramfe 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595846013 154 -FLNVKSEAfsITDAVVAARNYLSQRNLLTSKKWVTVGHSQGGHAALgaaQYASR 207
Cdd:pfam01738  67 lVSKRVMEK--VLDDLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAV---LLAAK 116
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
100-221 4.88e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.38  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 100 VVWAHGTTGvadvcapSKAALadstKDLISKLLAAGYVVVAPDYEGLGTSGiHPFLNVKSEAFsiTDAVVAARNYLSQRn 179
Cdd:COG1647    18 VLLLHGFTG-------SPAEM----RPLAEALAKAGYTVYAPRLPGHGTSP-EDLLKTTWEDW--LEDVEEAYEILKAG- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1595846013 180 lltSKKWVTVGHSQGGHAALGAAQYASRAqleyKGTVAVAPA 221
Cdd:COG1647    83 ---YDKVIVIGLSMGGLLALLLAARYPDV----AGLVLLSPA 117
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
131-224 9.25e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.21  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846013 131 LLAAGYVVVAPDYEGLGTSGiHPFLNVKSEAF---SITDAVVAARnYLSQRNLLTSKKWVTVGHSQGGHAALGAAQYASR 207
Cdd:pfam00326  10 LADRGYVVAIANGRGSGGYG-EAFHDAGKGDLgqnEFDDFIAAAE-YLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPD 87

                          90
                  ....*....|....*..
gi 1595846013 208 AqleYKGTVAVAPASNL 224
Cdd:pfam00326  88 L---FKAAVAHVPVVDW 101
 
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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