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Conserved domains on  [gi|568963115|ref|XP_006511868|]
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protein ABHD14A isoform X3 [Mus musculus]

Protein Classification

alpha/beta fold 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

PubMed:  1409539|12369917

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
51-247 8.80e-25

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: 97.76  E-value: 8.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  51 LTRGNSRIFYREVLPIQQArraeVVFLHGKAFNSHTWEQLgtLQLLSERgYRAVAIDLPGFGNSAPSEEVSTEAGRVELL 130
Cdd:COG0596    7 VTVDGVRLHYREAGPDGPP----VVLLHGLPGSSYEWRPL--IPALAAG-YRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 131 ERVFQDLQVQNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRNYAQ------------------------EQFGA 186
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPlrrpglapealaallralartdlrERLAR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568963115 187 VKTPTLILYGELDHTLARESLQQL-RHLPNHSVVKLHDAGHACYLHKPEAFHLALLAFLDHL 247
Cdd:COG0596  160 ITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
51-247 8.80e-25

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: 97.76  E-value: 8.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  51 LTRGNSRIFYREVLPIQQArraeVVFLHGKAFNSHTWEQLgtLQLLSERgYRAVAIDLPGFGNSAPSEEVSTEAGRVELL 130
Cdd:COG0596    7 VTVDGVRLHYREAGPDGPP----VVLLHGLPGSSYEWRPL--IPALAAG-YRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 131 ERVFQDLQVQNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRNYAQ------------------------EQFGA 186
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPlrrpglapealaallralartdlrERLAR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568963115 187 VKTPTLILYGELDHTLARESLQQL-RHLPNHSVVKLHDAGHACYLHKPEAFHLALLAFLDHL 247
Cdd:COG0596  160 ITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
30-155 2.75e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 44.80  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  30 PGPPEQTSRlWRGPNVTVLTG-LTRGNSRIFYREVLPIQQARRAEVVFLHGKAFNSHTWEQ--LGTLQLLSERGYRAVAI 106
Cdd:PLN03087 160 GQQLHPAPR-WSDCDCKFCTSwLSSSNESLFVHVQQPKDNKAKEDVLFIHGFISSSAFWTEtlFPNFSDAAKSTYRLFAV 238
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568963115 107 DLPGFGNS-APSEEVSTEAGRVELLER-VFQDLQVQNTVLVSPSLSGSYAL 155
Cdd:PLN03087 239 DLLGFGRSpKPADSLYTLREHLEMIERsVLERYKVKSFHIVAHSLGCILAL 289
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
74-236 1.47e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 41.69  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115   74 VVFLHGkafnshTWEQLGTLQLLSERGYRAVAIDLPGFGNS-APSEEVSTEAGRVELLERVFQDLQV------------- 139
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVAVLAPDLPGHGSSsPPPLDLADLADLAALLDELGAARPVvlvghslggaval 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  140 -------QNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRNYAQEQF---------------------------- 184
Cdd:pfam12697  75 aaaaaalVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFlddlpadaewaaalarlaallaalallp 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963115  185 ----GAVKTPTLILYGElDHTLARESLQQLRHLPNHSVVKLHDAGHACYLHkPEAF 236
Cdd:pfam12697 155 laawRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGAGHLPLDD-PEEV 208
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
51-247 8.80e-25

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: 97.76  E-value: 8.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  51 LTRGNSRIFYREVLPIQQArraeVVFLHGKAFNSHTWEQLgtLQLLSERgYRAVAIDLPGFGNSAPSEEVSTEAGRVELL 130
Cdd:COG0596    7 VTVDGVRLHYREAGPDGPP----VVLLHGLPGSSYEWRPL--IPALAAG-YRVIAPDLRGHGRSDKPAGGYTLDDLADDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 131 ERVFQDLQVQNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRNYAQ------------------------EQFGA 186
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPlrrpglapealaallralartdlrERLAR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568963115 187 VKTPTLILYGELDHTLARESLQQL-RHLPNHSVVKLHDAGHACYLHKPEAFHLALLAFLDHL 247
Cdd:COG0596  160 ITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
52-245 7.56e-19

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 81.97  E-value: 7.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  52 TRGNSRIFYREVLPIQQARRAeVVFLHGkaFNSHTWEQLGTLQLLSERGYRAVAIDLPGFGNSAPseevstEAGRVELLE 131
Cdd:COG2267   10 TRDGLRLRGRRWRPAGSPRGT-VVLVHG--LGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDG------PRGHVDSFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 132 RVFQDLQV----------QNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRN-------------YAQEQFGAVK 188
Cdd:COG2267   81 DYVDDLRAaldalrarpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADpllgpsarwlralRLAEALARID 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 189 TPTLILYGELDHTLARESLQQL--RHLPNHSVVKLHDAGHACYLHKP-EAFHLALLAFLD 245
Cdd:COG2267  161 VPVLVLHGGADRVVPPEAARRLaaRLSPDVELVLLPGARHELLNEPArEEVLAAILAWLE 220
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
63-227 2.01e-10

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.82  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  63 VLPIQQARRAEVVFLHGkAFNSHTWEQlGTLQLLSERGYRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVFQDLQ---- 138
Cdd:COG0412   21 ARPAGGGPRPGVVVLHE-IFGLNPHIR-DVARRLAAAGYVVLAPDLYGRGGPGDDPDEARALMGALDPELLAADLRaald 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 139 -VQNTVLVSP--------SLSGSYALpFLMQNHHQLRGFVPIAPTSTRNYAQEQFGAVKTPTLILYGELDHTLARESLQQ 209
Cdd:COG0412   99 wLKAQPEVDAgrvgvvgfCFGGGLAL-LAAARGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAA 177
                        170       180
                 ....*....|....*....|...
gi 568963115 210 LR-----HLPNHSVVKLHDAGHA 227
Cdd:COG0412  178 LEaalaaAGVDVELHVYPGAGHG 200
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
74-248 3.86e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.55  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  74 VVFLHGKAFNSHTWEQLGtlQLLSERGYRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVFQDLQ--VQNTVLVSPSLSG 151
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKagYDKVIVIGLSMGG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 152 SYALpFLMQNHHQLRGFVPIAP-----------------------------------------TSTR---------NYAQ 181
Cdd:COG1647   96 LLAL-LLAARYPDVAGLVLLSPalkiddpsapllpllkylarslrgigsdiedpevaeyaydrTPLRalaelqrliREVR 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568963115 182 EQFGAVKTPTLILYGELDHTLARESLQQL-RHL--PNHSVVKLHDAGH-ACYLHKPEAFHLALLAFLDHLP 248
Cdd:COG1647  175 RDLPKITAPTLIIQSRKDEVVPPESARYIyERLgsPDKELVWLEDSGHvITLDKDREEVAEEILDFLERLA 245
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-246 1.33e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.09  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  63 VLPIQQARRAEVVFLHGKAFNShTWEQLGTLQLLSERGYRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVFQDLQV--Q 140
Cdd:COG1506   15 YLPADGKKYPVVVYVHGGPGSR-DDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVdpD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115 141 NTVLVSPSLSGSYALpFLMQNHHQL-RGFVPIAP--------TSTRNYAQEQFGA-------------------VKTPTL 192
Cdd:COG1506   94 RIGIYGHSYGGYMAL-LAAARHPDRfKAAVALAGvsdlrsyyGTTREYTERLMGGpwedpeayaarsplayadkLKTPLL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568963115 193 ILYGELDHT-LARESLQQLRHL----PNHSVVKLHDAGHACYLHKPEAFHLALLAFLDH 246
Cdd:COG1506  173 LIHGEADDRvPPEQAERLYEALkkagKPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
30-155 2.75e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 44.80  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  30 PGPPEQTSRlWRGPNVTVLTG-LTRGNSRIFYREVLPIQQARRAEVVFLHGKAFNSHTWEQ--LGTLQLLSERGYRAVAI 106
Cdd:PLN03087 160 GQQLHPAPR-WSDCDCKFCTSwLSSSNESLFVHVQQPKDNKAKEDVLFIHGFISSSAFWTEtlFPNFSDAAKSTYRLFAV 238
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568963115 107 DLPGFGNS-APSEEVSTEAGRVELLER-VFQDLQVQNTVLVSPSLSGSYAL 155
Cdd:PLN03087 239 DLLGFGRSpKPADSLYTLREHLEMIERsVLERYKVKSFHIVAHSLGCILAL 289
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
74-167 2.93e-05

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 44.06  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  74 VVFLHGKAFNSHTWEQLGTLQllseRGYRAVAIDLPGFGNSApSEEVSTEAGRVELLERVFQDLQVQNTVLVSPSLSGSY 153
Cdd:PRK11126   5 LVFLHGLLGSGQDWQPVGEAL----PDYPRLYIDLPGHGGSA-AISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRI 79
                         90
                 ....*....|....*
gi 568963115 154 ALPFLMQ-NHHQLRG 167
Cdd:PRK11126  80 AMYYACQgLAGGLCG 94
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
74-145 9.14e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.65  E-value: 9.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963115  74 VVFLHGKAfnshTWEQL--GTLQLLSERGYRAVAIDLPGFGNS-APSE-EVSTEAGRVELLERVFQDLQVQNTVLV 145
Cdd:PRK00870  49 VLLLHGEP----SWSYLyrKMIPILAAAGHRVIAPDLIGFGRSdKPTRrEDYTYARHVEWMRSWFEQLDLTDVTLV 120
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
74-236 1.47e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 41.69  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115   74 VVFLHGkafnshTWEQLGTLQLLSERGYRAVAIDLPGFGNS-APSEEVSTEAGRVELLERVFQDLQV------------- 139
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVAVLAPDLPGHGSSsPPPLDLADLADLAALLDELGAARPVvlvghslggaval 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  140 -------QNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTSTRNYAQEQF---------------------------- 184
Cdd:pfam12697  75 aaaaaalVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFlddlpadaewaaalarlaallaalallp 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963115  185 ----GAVKTPTLILYGElDHTLARESLQQLRHLPNHSVVKLHDAGHACYLHkPEAF 236
Cdd:pfam12697 155 laawRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGAGHLPLDD-PEEV 208
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
68-173 4.04e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 40.66  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115   68 QARRAEVVFLHGkaFNSHTW--EQLGtlQLLSERGYRAVAIDLPGFGNSAPseevstEAGRVELLERVFQDLQVQNTVLV 145
Cdd:pfam12146   1 GEPRAVVVLVHG--LGEHSGryAHLA--DALAAQGFAVYAYDHRGHGRSDG------KRGHVPSFDDYVDDLDTFVDKIR 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568963115  146 SP-----------SLSGSYALPFLMQNHHQLRGFVPIAP 173
Cdd:pfam12146  71 EEhpglplfllghSMGGLIAALYALRYPDKVDGLILSAP 109
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
74-176 5.71e-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: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115   74 VVFLHGKAFNSHTWEQLgtLQLLSERGYRAVAIDLPGFGNS--APSEEVSTEAGRVELLERVFQDLQVQNTVLVSPSLSG 151
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKL--APALARDGFRVIALDLRGFGKSsrPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100
                  ....*....|....*....|....*
gi 568963115  152 SYALPFLMQNHHQLRGFVPIAPTST 176
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDP 105
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
55-145 1.19e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.21  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  55 NSRIFYREvlpiqQARRAEVVFLHGKAFNSHTWEQLgtLQLLSERGyRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVF 134
Cdd:PRK03592  16 GSRMAYIE-----TGEGDPIVFLHGNPTSSYLWRNI--IPHLAGLG-RCLAPDLIGMGASDKPDIDYTFADHARYLDAWF 87
                         90
                 ....*....|.
gi 568963115 135 QDLQVQNTVLV 145
Cdd:PRK03592  88 DALGLDDVVLV 98
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
66-155 1.30e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.54  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963115  66 IQQARRAE-----VVFLHGKAFNSHTWeqLGTLQLLSErGYRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVFQDLQVQ 140
Cdd:PRK14875 121 VRYLRLGEgdgtpVVLIHGFGGDLNNW--LFNHAALAA-GRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIE 197
                         90
                 ....*....|....*
gi 568963115 141 NTVLVSPSLSGSYAL 155
Cdd:PRK14875 198 RAHLVGHSMGGAVAL 212
 
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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