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Conserved domains on  [gi|568963202|ref|XP_006511911|]
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protein ABHD14B isoform X1 [Mus musculus]

Protein Classification

alpha/beta 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
10-209 7.86e-09

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


:

Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 54.25  E-value: 7.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETRPGSGqpvrfSVLLLHGIRFSSETWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaAPAPIGEPAP 89
Cdd:COG0596    4 LLAADGVRLAYREAGGGGP-----PLVLLHGFPGSSSVWRPVFKVLPALAARYRVIAPDLRGHGRS----DPAGYSLSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  90 GSFLAAVVDTLELGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICT------------------------------ 139
Cdd:COG0596   75 ADDLAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPpglleaalrqpagaaplaaladlllgldaa 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202 140 -------------------------------------------------------DKINAVDYASVKTPALIVYGDQDPM 164
Cdd:COG0596  155 afaallaalgllaalaaaaraglaealrapllgaaaaafaraaradlaaallallDRDLRAALARITVPTLIIHGEDDPV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568963202 165 --GSSSFQHLKQLPNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596  235 vpAELARRLAAALPNDaRLVVIPGAGHFPHLEAPEAFAAALLAFLERL 282
 
Name Accession Description Interval E-value
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
10-209 7.86e-09

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 54.25  E-value: 7.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETRPGSGqpvrfSVLLLHGIRFSSETWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaAPAPIGEPAP 89
Cdd:COG0596    4 LLAADGVRLAYREAGGGGP-----PLVLLHGFPGSSSVWRPVFKVLPALAARYRVIAPDLRGHGRS----DPAGYSLSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  90 GSFLAAVVDTLELGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICT------------------------------ 139
Cdd:COG0596   75 ADDLAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPpglleaalrqpagaaplaaladlllgldaa 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202 140 -------------------------------------------------------DKINAVDYASVKTPALIVYGDQDPM 164
Cdd:COG0596  155 afaallaalgllaalaaaaraglaealrapllgaaaaafaraaradlaaallallDRDLRAALARITVPTLIIHGEDDPV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568963202 165 --GSSSFQHLKQLPNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596  235 vpAELARRLAAALPNDaRLVVIPGAGHFPHLEAPEAFAAALLAFLERL 282
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
10-208 5.14e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.17  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETRPGSGQPVrfsvLLLHGirFSSE--TWqnLGTLQRLAeAGYRAVAIDLPGLGRSKEAAAPAPIGEP 87
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDGTPV----VLIHG--FGGDlnNW--LFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDEL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  88 ApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------LVAP---GSQ-----LRGFV---------PV---- 134
Cdd:PRK14875 184 A--AAVLAFLDALGIERAHLVGHSMGGAVALRLaarapqrvasltLIAPaglGPEingdyIDGFVaaesrrelkPVlell 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202 135 --------------------------------APICTDKINAVDY----ASVKTPALIVYGDQD---PmgsssFQHLKQL 175
Cdd:PRK14875 262 fadpalvtrqmvedllkykrldgvddalralaDALFAGGRQRVDLrdrlASLAIPVLVIWGEQDriiP-----AAHAQGL 336
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568963202 176 PNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQG 208
Cdd:PRK14875 337 PDGvAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
35-100 7.64e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729  Cd Length: 252  Bit Score: 42.20  E-value: 7.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963202   35 VLLLHGIRFSSETWQNlgtLQRLAEAGYRAVAIDLPGLGRSKEaaapapIGEPAPGSFLAAVVDTL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
Esterase_713_like cd12806
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ...
32-160 1.65e-04

Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214005  Cd Length: 261  Bit Score: 41.36  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  32 RFSVLLLHGIRFSSETWQN-----LGTLQRLAEAGYRAVAIDLPGLGRS-------KEAAAPAPI-GEPAPGSF------ 92
Cdd:cd12806   48 RYPLLLIHGCGLTGMTWETtpdgrMGWDNYFLRKGYSVYVVDQPGRGRSgwdtqfpVQGQAELWQqMVPDWLGAmptpnp 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568963202  93 ----LAAVVDTleLGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICTDKINAVDYASvKTPALIVYGD 160
Cdd:cd12806  128 tvaaLSKLADK--LDPTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCPKPEDVKPLT-SIPVLVVYGD 196
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
35-115 3.65e-04

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: 40.18  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202   35 VLLLHGIRFSSETWQNLGTLqrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGEPAPGSFLAAVVDTLELGPPVVISPSLSG 114
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                  .
gi 568963202  115 M 115
Cdd:pfam00561  81 L 81
 
Name Accession Description Interval E-value
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
10-209 7.86e-09

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 54.25  E-value: 7.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETRPGSGqpvrfSVLLLHGIRFSSETWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaAPAPIGEPAP 89
Cdd:COG0596    4 LLAADGVRLAYREAGGGGP-----PLVLLHGFPGSSSVWRPVFKVLPALAARYRVIAPDLRGHGRS----DPAGYSLSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  90 GSFLAAVVDTLELGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICT------------------------------ 139
Cdd:COG0596   75 ADDLAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPpglleaalrqpagaaplaaladlllgldaa 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202 140 -------------------------------------------------------DKINAVDYASVKTPALIVYGDQDPM 164
Cdd:COG0596  155 afaallaalgllaalaaaaraglaealrapllgaaaaafaraaradlaaallallDRDLRAALARITVPTLIIHGEDDPV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568963202 165 --GSSSFQHLKQLPNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596  235 vpAELARRLAAALPNDaRLVVIPGAGHFPHLEAPEAFAAALLAFLERL 282
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
10-208 5.14e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.17  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETRPGSGQPVrfsvLLLHGirFSSE--TWqnLGTLQRLAeAGYRAVAIDLPGLGRSKEAAAPAPIGEP 87
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDGTPV----VLIHG--FGGDlnNW--LFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDEL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  88 ApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------LVAP---GSQ-----LRGFV---------PV---- 134
Cdd:PRK14875 184 A--AAVLAFLDALGIERAHLVGHSMGGAVALRLaarapqrvasltLIAPaglGPEingdyIDGFVaaesrrelkPVlell 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202 135 --------------------------------APICTDKINAVDY----ASVKTPALIVYGDQD---PmgsssFQHLKQL 175
Cdd:PRK14875 262 fadpalvtrqmvedllkykrldgvddalralaDALFAGGRQRVDLrdrlASLAIPVLVIWGEQDriiP-----AAHAQGL 336
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568963202 176 PNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQG 208
Cdd:PRK14875 337 PDGvAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
6-142 3.29e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939  Cd Length: 330  Bit Score: 46.69  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202   6 QHEGTIKVQGQNLFFRETRPGSGQPVRFSVLLLHGI-RFSSETWQNLGTLqrLAEAGYRAVAIDLPGLGRSKEAAAPAPI 84
Cdd:PLN02298  33 SKSFFTSPRGLSLFTRSWLPSSSSPPRALIFMVHGYgNDISWTFQSTAIF--LAQMGFACFALDLEGHGRSEGLRAYVPN 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568963202  85 GEPAPG---SFLAAVVDTLELG--PPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPIC--TDKI 142
Cdd:PLN02298 111 VDLVVEdclSFFNSVKQREEFQglPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkiSDKI 175
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
25-75 6.60e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147  Cd Length: 302  Bit Score: 42.65  E-value: 6.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568963202  25 PGSGQPVrfsvLLLHGirfsSETWQNL--GTLQRLAEAGYRAVAIDLPGLGRS 75
Cdd:PRK00870  43 PADGPPV----LLLHG----EPSWSYLyrKMIPILAAAGHRVIAPDLIGFGRS 87
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
35-100 7.64e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729  Cd Length: 252  Bit Score: 42.20  E-value: 7.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963202   35 VLLLHGIRFSSETWQNlgtLQRLAEAGYRAVAIDLPGLGRSKEaaapapIGEPAPGSFLAAVVDTL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
10-102 1.38e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 41.52  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  10 TIKVQGQNLFFRETrpGSGQPVRFsvllLHGIRFSSETWQNLgtLQRLAEAGyRAVAIDLPGLGRSkeaaapapiGEPAP 89
Cdd:PRK03592  11 RVEVLGSRMAYIET--GEGDPIVF----LHGNPTSSYLWRNI--IPHLAGLG-RCLAPDLIGMGAS---------DKPDI 72
                         90       100
                 ....*....|....*....|
gi 568963202  90 G-------SFLAAVVDTLEL 102
Cdd:PRK03592  73 DytfadhaRYLDAWFDALGL 92
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
150-210 1.51e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283  Cd Length: 360  Bit Score: 41.75  E-value: 1.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568963202 150 VKTPALIVYGDQD-------PMGSSSFQHLKQLPNHRVLVMEGAGHPCYLDKPDEWHKGLLDFLQGLA 210
Cdd:PLN02679 291 ISLPILVLWGDQDpftpldgPVGKYFSSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQLP 358
Esterase_713_like cd12806
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ...
32-160 1.65e-04

Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214005  Cd Length: 261  Bit Score: 41.36  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  32 RFSVLLLHGIRFSSETWQN-----LGTLQRLAEAGYRAVAIDLPGLGRS-------KEAAAPAPI-GEPAPGSF------ 92
Cdd:cd12806   48 RYPLLLIHGCGLTGMTWETtpdgrMGWDNYFLRKGYSVYVVDQPGRGRSgwdtqfpVQGQAELWQqMVPDWLGAmptpnp 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568963202  93 ----LAAVVDTleLGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICTDKINAVDYASvKTPALIVYGD 160
Cdd:cd12806  128 tvaaLSKLADK--LDPTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCPKPEDVKPLT-SIPVLVVYGD 196
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
35-115 3.65e-04

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: 40.18  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202   35 VLLLHGIRFSSETWQNLGTLqrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGEPAPGSFLAAVVDTLELGPPVVISPSLSG 114
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                  .
gi 568963202  115 M 115
Cdd:pfam00561  81 L 81
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-79 6.60e-04

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


Pssm-ID: 225176 [Multi-domain]  Cd Length: 298  Bit Score: 39.66  E-value: 6.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568963202  29 QPVRFSVLLLHGIRFSSETWQNLGtlQRLAEAGYRAVAIDLPGLGRSKEAA 79
Cdd:COG2267   31 EPPKGVVVLVHGLGEHSGRYEELA--DDLAARGFDVYALDLRGHGRSPRGQ 79
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
35-197 9.29e-04

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


Pssm-ID: 403789 [Multi-domain]  Cd Length: 212  Bit Score: 39.00  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202   35 VLLLHGirfsseTWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaaPAPIGEPAPGSFLAAVVDTLE--LGPPVVISPSL 112
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVRVLAPDLPGHGSS-----DPPPLDLADLADLAALLDELGaaGRPVVLVGHSL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  113 SGMYSLPF---------LVAPGSQLRGFVPVAPICTDKINAV-------------------------------------- 145
Cdd:pfam12697  70 GGAVALAAaaaalvvgvLVAPLALPLGLLAALLALLARLGAAlaapawlaaeplprgflddlpadaewaaalarlaalla 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963202  146 --------DYASVKTPALIVYGDQDPMGSSSFQHLKQLPNHRVLVMEGAGHpCYLDKPDE 197
Cdd:pfam12697 150 alallplaAWRDLPAPVLVLAEEDRLVPPLAQRLLAALAGARLVVLPGAGH-LPLDDPEE 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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