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Conserved domains on  [gi|1907171303|ref|XP_036021794|]
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mesoderm-specific transcript protein isoform X3 [Mus musculus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427000)

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:  19508187|12369917|37582413

Graphical summary

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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, ...
 52-167 4.97e-21

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: 89.29  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  52 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 131
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907171303 132 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRY 167
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARH 110
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 79-296 7.13e-17

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 pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 78.32  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  79 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 157
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303 158 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 232
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907171303 233 RPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALasvSIPIHFIYGPLDPINPY 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL---DEPTLIIWGDQDPLVPP 215
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-167 4.97e-21

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: 89.29  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  52 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 131
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907171303 132 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRY 167
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARH 110
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-296 7.13e-17

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: 78.32  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  79 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 157
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303 158 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 232
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907171303 233 RPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALasvSIPIHFIYGPLDPINPY 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL---DEPTLIIWGDQDPLVPP 215
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 55-156 5.38e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 68.10  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  55 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 134
Cdd:PRK03592   10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                          90       100
                  ....*....|....*....|..
gi 1907171303 135 ESLLRHLGLqnRRINLLSHDYG 156
Cdd:PRK03592   84 DAWFDALGL--DDVVLVGHDWG 103
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-168 2.83e-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: 44.39  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  79 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDKPRPHqysiFEQASIVESLLRHLGLQNRRInLLSHDYGDI 158
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 1907171303 159 VAQELLYRYK 168
Cdd:pfam12697  72 VALAAAAAAL 81
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-167 4.97e-21

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: 89.29  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  52 TSGKFFTYKGLRIFYQDSvGVVGSPeiVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFSDKPRPHqYSIFEQA 131
Cdd:COG0596     2 STPRFVTVDGVRLHYREA-GPDGPP--VVLLHGLPGSSYEWRPLIPALAAGY-RVIAPDLRGHGRSDKPAGG-YTLDDLA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907171303 132 SIVESLLRHLGLQnrRINLLSHDYGDIVAQELLYRY 167
Cdd:COG0596    77 DDLAALLDALGLE--RVVLVGHSMGGMVALELAARH 110
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-296 7.13e-17

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: 78.32  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  79 VVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPR-PHQYSIFEQASIVESLLRHLGLQnrRINLLSHDYGD 157
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKaQDDYRTDDLAEDLEYILEALGLE--KVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303 158 IVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLKD----GGVLSPILTRLMNFFV-FSRGLTPVFGPYT 232
Cdd:pfam00561  81 LIALAYAAKYPDR------VKALVLLGALDPPHELDEADRFILALFpgffDGFVADFAPNPLGRLVaKLLALLLLRLRLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907171303 233 RPTESELWDMWAVIRNNDGNLVIDSLLQYINQRKKFRRRWVGALasvSIPIHFIYGPLDPINPY 296
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL---DEPTLIIWGDQDPLVPP 215
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 55-156 5.38e-13

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 68.10  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  55 KFFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPrPHQYSIFEQASIV 134
Cdd:PRK03592   10 RRVEVLGSRMAYIET----GEGDPIVFLHGNPTSSYLWRNIIPHLA-GLGRCLAPDLIGMGASDKP-DIDYTFADHARYL 83

                          90       100
                  ....*....|....*....|..
gi 1907171303 135 ESLLRHLGLqnRRINLLSHDYG 156
Cdd:PRK03592   84 DAWFDALGL--DDVVLVGHDWG 103
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 63-161 2.87e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 63.36  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  63 RIFYQDSvGVVGSPEiVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP---HQYSIFEQASIVESLlr 139
Cdd:PLN03084  116 RWFCVES-GSNNNPP-VLLIHGFPSQAYSYRKVLPVLSKNYH-AIAFDWLGFGFSDKPQPgygFNYTLDEYVSSLESL-- 190

                          90       100
                  ....*....|....*....|..
gi 1907171303 140 hlglqnrrINLLSHDYGDIVAQ 161
Cdd:PLN03084  191 --------IDELKSDKVSLVVQ 204
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 38-156 9.35e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 61.41  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  38 IPPPQLSPALHSWktsgkfFTYKGLRIFYQDSvgvvGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFhRVIALDFLGFGFS 117
Cdd:PRK03204    6 TPDPQLYPFESRW------FDSSRGRIHYIDE----GTGPPILLCHGNPTWSFLYRDIIVALRDRF-RCVAPDYLGFGLS 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907171303 118 DKPRPHQYSIFEQASIVESLLRHLGLQNrrINLLSHDYG 156
Cdd:PRK03204   75 ERPSGFGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 62-159 3.13e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 56.90  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  62 LRIFYQDSvgvvGSP--EIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKP-RPHQYSIFEQASIVESLL 138
Cdd:PRK00870   34 LRMHYVDE----GPAdgPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVEWMRSWF 109

                          90       100
                  ....*....|....*....|.
gi 1907171303 139 RHLGLQNrrINLLSHDYGDIV 159
Cdd:PRK00870  110 EQLDLTD--VTLVCQDWGGLI 128
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 39-124 1.01e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 55.51  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  39 PPPQLSPALHSWKtsgkfftYKGLRIFYQDSVGvvgSPEIVVLLHGFPTSSYDWYKIWEGLTLRfHRVIALDFLGFGFSD 118
Cdd:PLN02824    2 VKPEPQVETRTWR-------WKGYNIRYQRAGT---SGPALVLVHGFGGNADHWRKNTPVLAKS-HRVYAIDLLGYGYSD 70


                  ....*.
gi 1907171303 119 KPRPHQ 124
Cdd:PLN02824   71 KPNPRS 76
PLN02578 PLN02578
hydrolase
 15-119 2.14e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.85  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  15 MQMREWWVQVGLLA--VPLLAAYLHIPPPQLSPALHSWKTSGKFFTYKGLRIFYqdsvgVV---GSPeiVVLLHGFPTSS 89
Cdd:PLN02578   27 GINRRIFIFGGIVAsgVSVMGSSSASQSVQGLERLPFKKEGYNFWTWRGHKIHY-----VVqgeGLP--IVLIHGFGASA 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907171303  90 YDW-YKIWEglTLRFHRVIALDFLGFGFSDK 119
Cdd:PLN02578  100 FHWrYNIPE--LAKKYKVYALDLLGFGWSDK 128
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
51-167 1.43e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.16  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  51 KTSGKFFTYKGLRIFYQDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQ 130
Cdd:COG2267     3 RRLVTLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDY 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907171303 131 ASIVESLLRHLGLQ-NRRINLLSHDYGDIVAQELLYRY 167
Cdd:COG2267    83 VDDLRAALDALRARpGLPVVLLGHSMGGLIALLYAARY 120
PRK05855 PRK05855
SDR family oxidoreductase;
61-166 1.19e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 49.59  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  61 GLRIfyqdSVGVVGSPE--IVVLLHGFPTSSYDWYKIWEGLTLRFHrVIALDFLGFGFSDKPRP-HQYSIFEQASIVESL 137
Cdd:PRK05855   12 GVRL----AVYEWGDPDrpTVVLVHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRtAAYTLARLADDFAAV 86

                          90       100
                  ....*....|....*....|....*....
gi 1907171303 138 LRHLGlQNRRINLLSHDYGDIVAQELLYR 166
Cdd:PRK05855   87 IDAVS-PDRPVHLLAHDWGSIQGWEAVTR 114
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 48-182 2.81e-06

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 48.65  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  48 HSWKTSGKfftyKGLRIFYQDSVGVvGSPEIVVLLHGFPTSSYDWYkiwEGLTLRF-------HRVIALDFLGFGFSDKP 120
Cdd:PLN03087  178 TSWLSSSN----ESLFVHVQQPKDN-KAKEDVLFIHGFISSSAFWT---ETLFPNFsdaakstYRLFAVDLLGFGRSPKP 249

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907171303 121 RPHQYSIFEQASIVE-SLLRHLGLqnRRINLLSHDYGDIVAQELLYRYKQnrsgrlTIKSLCL 182
Cdd:PLN03087  250 ADSLYTLREHLEMIErSVLERYKV--KSFHIVAHSLGCILALALAVKHPG------AVKSLTL 304
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 79-168 2.83e-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: 44.39  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  79 VVLLHGFPTSSYDWykiwEGLTLRFHRVIALDFLGFGFSDKPRPHqysiFEQASIVESLLRHLGLQNRRInLLSHDYGDI 158
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDELGAARPVV-LVGHSLGGA 71

                          90
                  ....*....|
gi 1907171303 159 VAQELLYRYK 168
Cdd:pfam12697  72 VALAAAAAAL 81
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 74-208 2.10e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.16  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  74 GSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKpRPHQYSIFEQASIVESLLRHLGLQnrRINLLSH 153
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIE--RAHLVGH 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907171303 154 DYGDIVAQELLyrykQNRSGRltIKSLCL-SNGGIFPE-------------THRPL--LLQKLLKDGGVLS 208
Cdd:PRK14875  205 SMGGAVALRLA----ARAPQR--VASLTLiAPAGLGPEingdyidgfvaaeSRRELkpVLELLFADPALVT 269
PRK08775 PRK08775
homoserine O-succinyltransferase;
62-179 4.48e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  62 LRIFYQdSVGVVGSPEIVVL--------LHGFPTSSYD-WykiWEGLT-------LRFHRVIALDFLGfgfSDKPRPHQY 125
Cdd:PRK08775   46 LRLRYE-LIGPAGAPVVFVAggisahrhVAATATFPEKgW---WEGLVgsgraldPARFRLLAFDFIG---ADGSLDVPI 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907171303 126 SIFEQASIVESLLRHLGLQnRRINLLSHDYGDIVAQELLYRYKQnRSGRLTIKS 179
Cdd:PRK08775  119 DTADQADAIALLLDALGIA-RLHAFVGYSYGALVGLQFASRHPA-RVRTLVVVS 170
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 55-127 4.48e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 38.28  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907171303  55 KFFTYKGL-RIFY--QDSVGVVGSPEIVVLLHGFPTSSYDWYKIWEGLTlRFHRVIALDFLGFGFSDKPRPHQYSI 127
Cdd:PLN02679   64 KKWKWKGEySINYlvKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLA-KNYTVYAIDLLGFGASDKPPGFSYTM 138
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 78-214 6.36e-03

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: 37.58  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303  78 IVVLLHGFpTSSYDWY-KIWEGLTLRFHRVIALDFLGFGFSDKPRPHQYSIFEQASIVESLLRHLGLQNRRIN--LLSHD 154
Cdd:pfam12146   6 VVVLVHGL-GEHSGRYaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEHPGLPlfLLGHS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907171303 155 YGDIVAQELLYRYKQNrsgrltIKSLCLSNGGIFPETHRPLLLQKLLkdGGVLSPILTRL 214
Cdd:pfam12146  85 MGGLIAALYALRYPDK------VDGLILSAPALKIKPYLAPPILKLL--AKLLGKLFPRL 136
 
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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