NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|62859673|ref|NP_001017276|]
View 

alpha/beta hydrolase domain-containing protein 14B [Xenopus tropicalis]

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

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 8-210 9.68e-27

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: 102.00  E-value: 9.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   8 ESTVKVSGQTLFYREAlpvapGTNKPPVLLLHGIRFSSQEWQNLktlHTLAAAGHRAVALDLPGLGHSADAVAPSPLGEL 87
Cdd:COG0596   4 PRFVTVDGVRLHYREA-----GPDGPPVVLLHGLPGSSYEWRPL---IPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  88 AppGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAPI------------------------CTDKFS 143
Cdd:COG0596  76 A--DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVlaalaeplrrpglapealaallraLARTDL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62859673 144 VQDYAHVQVPALIVYGDKDEQLGELSLRNL-KNLPNHRVFCMKGAGHACYLDDPDTWHQGLMEFLSSL 210
Cdd:COG0596 154 RERLARITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 8-210 9.68e-27

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: 102.00  E-value: 9.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   8 ESTVKVSGQTLFYREAlpvapGTNKPPVLLLHGIRFSSQEWQNLktlHTLAAAGHRAVALDLPGLGHSADAVAPSPLGEL 87
Cdd:COG0596   4 PRFVTVDGVRLHYREA-----GPDGPPVVLLHGLPGSSYEWRPL---IPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  88 AppGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAPI------------------------CTDKFS 143
Cdd:COG0596  76 A--DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVlaalaeplrrpglapealaallraLARTDL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62859673 144 VQDYAHVQVPALIVYGDKDEQLGELSLRNL-KNLPNHRVFCMKGAGHACYLDDPDTWHQGLMEFLSSL 210
Cdd:COG0596 154 RERLARITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-136 1.85e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.19  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   10 TVKVSGQTLFYREALPVAPgtnkPPVLLLHGirFSSqEWQNLKTLHTLAAAGHRAVALDLPGLGHSADAVAPSPLGELAp 89
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDG----TPVVLIHG--FGG-DLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELA- 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 62859673   90 pGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAP 136
Cdd:PRK14875 185 -AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-137 1.62e-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: 47.11  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    33 PPVLLLHGIRFSSQEWQNLKTLhtLAAAGHRAVALDLPGLGHSADAVAPSPLGELAPPGFLQEVLESLNMVPAVLISPSL 112
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100
                  ....*....|....*....|....*
gi 62859673   113 SGMYSLPFLLSSPQSVAAYVPVAPI 137
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL 103
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 8-210 9.68e-27

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: 102.00  E-value: 9.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   8 ESTVKVSGQTLFYREAlpvapGTNKPPVLLLHGIRFSSQEWQNLktlHTLAAAGHRAVALDLPGLGHSADAVAPSPLGEL 87
Cdd:COG0596   4 PRFVTVDGVRLHYREA-----GPDGPPVVLLHGLPGSSYEWRPL---IPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  88 AppGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAPI------------------------CTDKFS 143
Cdd:COG0596  76 A--DDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVlaalaeplrrpglapealaallraLARTDL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62859673 144 VQDYAHVQVPALIVYGDKDEQLGELSLRNL-KNLPNHRVFCMKGAGHACYLDDPDTWHQGLMEFLSSL 210
Cdd:COG0596 154 RERLARITVPTLVIWGEKDPIVPPALARRLaELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-194 5.71e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 67.72  E-value: 5.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  15 GQTLFYREALPVAPGtnKPPVLLLHGIRFSSQEWQNLktLHTLAAAGHRAVALDLPGLGHSadavaPSPLGELapPGF-- 92
Cdd:COG2267  13 GLRLRGRRWRPAGSP--RGTVVLVHGLGEHSGRYAEL--AEALAAAGYAVLAFDLRGHGRS-----DGPRGHV--DSFdd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  93 ----LQEVLESLNM---VPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAP-ICTDKFS------------VQDYAHVQV 152
Cdd:COG2267  82 yvddLRAALDALRArpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPaYRADPLLgpsarwlralrlAEALARIDV 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 62859673 153 PALIVYGDKDEQL-GELSLRNLKNL-PNHRVFCMKGAGHACYLD 194
Cdd:COG2267 162 PVLVLHGGADRVVpPEAARRLAARLsPDVELVLLPGARHELLNE 205
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-136 1.85e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.19  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   10 TVKVSGQTLFYREALPVAPgtnkPPVLLLHGirFSSqEWQNLKTLHTLAAAGHRAVALDLPGLGHSADAVAPSPLGELAp 89
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDG----TPVVLIHG--FGG-DLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELA- 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 62859673   90 pGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAP 136
Cdd:PRK14875 185 -AAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
23-201 1.14e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 47.65  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  23 ALPVAPGtNKPPVLLLHGIrFSSQEWqNLKTLHTLAAAGHRAVALDL--PGLGHSADAVAPSPLGELAPPGFLQEVLESL 100
Cdd:COG0412  21 ARPAGGG-PRPGVVVLHEI-FGLNPH-IRDVARRLAAAGYVVLAPDLygRGGPGDDPDEARALMGALDPELLAADLRAAL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673 101 NMV---PAVLISP------SLSGMYSLPFLLSSPQsVAAYVPVAPICTDKFSVQDYAHVQVPALIVYGDKD-----EQLG 166
Cdd:COG0412  98 DWLkaqPEVDAGRvgvvgfCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDplvppEQVA 176

                       170       180       190
                ....*....|....*....|....*....|....*
gi 62859673 167 ELSLRNLKNLPNHRVFCMKGAGHACYLDDPDTWHQ 201
Cdd:COG0412 177 ALEAALAAAGVDVELHVYPGAGHGFTNPGRPRYDP 211
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-137 1.62e-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: 47.11  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    33 PPVLLLHGIRFSSQEWQNLKTLhtLAAAGHRAVALDLPGLGHSADAVAPSPLGELAPPGFLQEVLESLNMVPAVLISPSL 112
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100
                  ....*....|....*....|....*
gi 62859673   113 SGMYSLPFLLSSPQSVAAYVPVAPI 137
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGAL 103
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 3-128 3.74e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 46.27  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    3 EVQIKESTVKVSGQTLFYREAlpvapGTNKPPVLLLHGIRFSSQEW-QNLKTLhtlaAAGHRAVALDLPGLGHSADavaP 81
Cdd:PLN02824   5 EPQVETRTWRWKGYNIRYQRA-----GTSGPALVLVHGFGGNADHWrKNTPVL----AKSHRVYAIDLLGYGYSDK---P 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62859673   82 SPLgeLAPPG--------------FLQEVLESlnmvPAVLISPSLSGMYSLPFLLSSPQSV 128
Cdd:PLN02824  73 NPR--SAPPNsfytfetwgeqlndFCSDVVGD----PAFVICNSVGGVVGLQAAVDAPELV 127
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 33-75 1.75e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 44.57  E-value: 1.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 62859673   33 PPVLLLHGirfsSQEWQNL--KTLHTLAAAGHRAVALDLPGLGHS 75
Cdd:PRK00870  47 PPVLLLHG----EPSWSYLyrKMIPILAAAGHRVIAPDLIGFGRS 87
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 31-116 1.53e-04

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 41.36  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   31 NKPPVLLLHGIRFSSQEWQNLKTlhtlAAAGHRAVALDLPGLGHSADavapsplgeLAPPGF------LQEVLESLNMVP 104
Cdd:PRK11126   1 GLPWLVFLHGLLGSGQDWQPVGE----ALPDYPRLYIDLPGHGGSAA---------ISVDGFadvsrlLSQTLQSYNILP 67

                         90
                 ....*....|....*
gi 62859673  105 AVLISPSLSG---MY 116
Cdd:PRK11126  68 YWLVGYSLGGriaMY 82
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 7-138 1.86e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 41.30  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    7 KESTVKVSGQTLFYREALPVAPGTNKPPVLLLHGIRFSSQeWQNLKTLHTLAAAGHRAVALDLPGLGHSADAVAPSPLGE 86
Cdd:PLN02298  34 KSFFTSPRGLSLFTRSWLPSSSSPPRALIFMVHGYGNDIS-WTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVPNVD 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62859673   87 LAppgfLQEVLESLNMV---------PAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAPIC 138
Cdd:PLN02298 113 LV----VEDCLSFFNSVkqreefqglPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMC 169
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 31-108 2.56e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.04  E-value: 2.56e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62859673  31 NKPPVLLLHGIRFSSQEWQNLKtlHTLAAAGHRAVALDLPGLGHSADAVApsplGELAPpgFLQEVLESLNMVPAVLI 108
Cdd:COG1075   4 TRYPVVLVHGLGGSAASWAPLA--PRLRAAGYPVYALNYPSTNGSIEDSA----EQLAA--FVDAVLAATGAEKVDLV 73
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-197 9.13e-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: 38.99  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    35 VLLLHGIrfssqeWQNLKTLHTLAAAGHRAVALDLPG--------------------------------LGHS-----AD 77
Cdd:pfam12697   1 VVLVHGA------GLSAAPLAALLAAGVAVLAPDLPGhgssspppldladladlaalldelgaarpvvlVGHSlggavAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673    78 AVAPSPL-------GELAPPGFLQEVLESLNMVPAVLISPSLSGMYSLPFLLSSPQSVAAYVPVAPI-------CTDKFS 143
Cdd:pfam12697  75 AAAAAALvvgvlvaPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALArlaallaALALLP 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 62859673   144 VQDYAHVQVPALIVYGDkDEQLGELSLRNLKNLPNHRVFCMKGAGHaCYLDDPD 197
Cdd:pfam12697 155 LAAWRDLPVPVLVLAEE-DRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPE 206
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
31-210 1.07e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673  31 NKPPVLLLHGIRFSSQEWQNLKtlHTLAAAGHRAVALDLPGLGHSADAvapspLGELAPPGFLQEVLESLNMVPA----- 105
Cdd:COG1647  14 GRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPED-----LLKTTWEDWLEDVEEAYEILKAgydkv 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673 106 -------------------------VLISPSLS----GMYSLPFLLSSPQSVAAYVP------VAPICTDKFSV------ 144
Cdd:COG1647  87 iviglsmggllalllaarypdvaglVLLSPALKiddpSAPLLPLLKYLARSLRGIGSdiedpeVAEYAYDRTPLralael 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62859673 145 --------QDYAHVQVPALIVYGDKDEQLGELSLRNLKNL---PNHRVFCMKGAGH-ACYLDDPDTWHQGLMEFLSSL 210
Cdd:COG1647 167 qrlirevrRDLPKITAPTLIIQSRKDEVVPPESARYIYERlgsPDKELVWLEDSGHvITLDKDREEVAEEILDFLERL 244
PLN02578 PLN02578
hydrolase
 33-136 2.98e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 37.90  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62859673   33 PPVLLLHGIRFSSQEWQ-NLKTLhtlaAAGHRAVALDLPGLGHSADAvapspLGELAPPGFLQEVLESLNMV---PAVLI 108
Cdd:PLN02578  87 LPIVLIHGFGASAFHWRyNIPEL----AKKYKVYALDLLGFGWSDKA-----LIEYDAMVWRDQVADFVKEVvkePAVLV 157

                         90       100
                 ....*....|....*....|....*...
gi 62859673  109 SPSLSGMYSLPFLLSSPQSVAAYVPVAP 136
Cdd:PLN02578 158 GNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 10-75 4.43e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 37.28  E-value: 4.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62859673   10 TVKVSGQTLFYREAlpvapGTNkPPVLLLHGIRFSSQEWQNLktLHTLAAAGhRAVALDLPGLGHS 75
Cdd:PRK03592  11 RVEVLGSRMAYIET-----GEG-DPIVFLHGNPTSSYLWRNI--IPHLAGLG-RCLAPDLIGMGAS 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH