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Conserved domains on  [gi|1910430613|ref|XP_036081942|]
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protein ABHD11 isoform X1 [Rousettus aegyptiacus]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
66-350 3.65e-46

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 157.58  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  66 RPALVLLHGLFGSKTNLNSVAktlaqqtgrRDLspgsppatcrpsrplavytqnldasvVTVHPTPQVltvDARNHGDSF 145
Cdd:PRK10673   16 NSPIVLVHGLFGSLDNLGVLA---------RDL--------------------------VNDHDIIQV---DMRNHGLSP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 146 YSPDMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVEDISPVDSKFgLEYLTYIAAMRAVDI 225
Cdd:PRK10673   58 RDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHV-RRHDEIFAAINAVSE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 226 PDKVPHSHARKLADEQLshvvQDIAVRQFLLTNLVEADgrfvWRPNLDALAQHMEKLVAFPPrQESYPGPTLFLFGENSH 305
Cdd:PRK10673  137 AGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVDGE----WRFNVPVLWDQYPHIVGWEK-IPAWPHPALFIRGGNSP 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1910430613 306 FIHSSHHPEIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:PRK10673  208 YVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
66-350 3.65e-46

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 157.58  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  66 RPALVLLHGLFGSKTNLNSVAktlaqqtgrRDLspgsppatcrpsrplavytqnldasvVTVHPTPQVltvDARNHGDSF 145
Cdd:PRK10673   16 NSPIVLVHGLFGSLDNLGVLA---------RDL--------------------------VNDHDIIQV---DMRNHGLSP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 146 YSPDMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVEDISPVDSKFgLEYLTYIAAMRAVDI 225
Cdd:PRK10673   58 RDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHV-RRHDEIFAAINAVSE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 226 PDKVPHSHARKLADEQLshvvQDIAVRQFLLTNLVEADgrfvWRPNLDALAQHMEKLVAFPPrQESYPGPTLFLFGENSH 305
Cdd:PRK10673  137 AGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVDGE----WRFNVPVLWDQYPHIVGWEK-IPAWPHPALFIRGGNSP 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1910430613 306 FIHSSHHPEIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:PRK10673  208 YVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 53-350 1.81e-31

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: 118.18  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  53 VRLSYKLLDGDAvrPALVLLHGLFGSKTNLNSVAKTLAQqtGRRdlspgsppatcrpsrplavytqnldasvvtvhptpq 132
Cdd:COG0596    12 VRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAA--GYR------------------------------------ 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDSFYSP-DMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVEDispvdskfgl 211
Cdd:COG0596    52 VIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD---------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 212 EYLTYIAAMravdipdkvphsharkladeqlshvVQDIAVRQFLLTNLVEADGRFVWRPNLDALAQhmeklvafpprqes 291
Cdd:COG0596   122 EVLAALAEP-------------------------LRRPGLAPEALAALLRALARTDLRERLARITV-------------- 162

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1910430613 292 ypgPTLFLFGENSHFIHSSHHPEIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:COG0596   163 ---PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 67-335 6.19e-18

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: 81.78  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  67 PALVLLHGLFGSKTNLNSVAKTLAQQtGRRdlspgsppatcrpsrplavytqnldasvvtvhptpqVLTVDARNHGDSF- 145
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFR------------------------------------VIALDLRGFGKSSr 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 146 --YSPDMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVedISPVDSKFGLEYLTYIAAMRAV 223
Cdd:pfam00561  44 pkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVL--LGALDPPHELDEADRFILALFP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 224 DIPDKVPHSHARKladeQLSHVVQDIAVRQFLLTNLVEADGRFVWRP----------NLDALAQHMEKLVAFPPRQE--S 291
Cdd:pfam00561 122 GFFDGFVADFAPN----PLGRLVAKLLALLLLRLRLLKALPLLNKRFpsgdyalaksLVTGALLFIETWSTELRAKFlgR 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1910430613 292 YPGPTLFLFGENSHFIHSSHHPEIRRLFPQAQVQTIPNAGHWIH 335
Cdd:pfam00561 198 LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
66-350 3.65e-46

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 157.58  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  66 RPALVLLHGLFGSKTNLNSVAktlaqqtgrRDLspgsppatcrpsrplavytqnldasvVTVHPTPQVltvDARNHGDSF 145
Cdd:PRK10673   16 NSPIVLVHGLFGSLDNLGVLA---------RDL--------------------------VNDHDIIQV---DMRNHGLSP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 146 YSPDMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVEDISPVDSKFgLEYLTYIAAMRAVDI 225
Cdd:PRK10673   58 RDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHV-RRHDEIFAAINAVSE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 226 PDKVPHSHARKLADEQLshvvQDIAVRQFLLTNLVEADgrfvWRPNLDALAQHMEKLVAFPPrQESYPGPTLFLFGENSH 305
Cdd:PRK10673  137 AGATTRQQAAAIMRQHL----NEEGVIQFLLKSFVDGE----WRFNVPVLWDQYPHIVGWEK-IPAWPHPALFIRGGNSP 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1910430613 306 FIHSSHHPEIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:PRK10673  208 YVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 53-350 1.81e-31

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: 118.18  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  53 VRLSYKLLDGDAvrPALVLLHGLFGSKTNLNSVAKTLAQqtGRRdlspgsppatcrpsrplavytqnldasvvtvhptpq 132
Cdd:COG0596    12 VRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAA--GYR------------------------------------ 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDSFYSP-DMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVEDispvdskfgl 211
Cdd:COG0596    52 VIAPDLRGHGRSDKPAgGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD---------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 212 EYLTYIAAMravdipdkvphsharkladeqlshvVQDIAVRQFLLTNLVEADGRFVWRPNLDALAQhmeklvafpprqes 291
Cdd:COG0596   122 EVLAALAEP-------------------------LRRPGLAPEALAALLRALARTDLRERLARITV-------------- 162

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1910430613 292 ypgPTLFLFGENSHFIHSSHHPEIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:COG0596   163 ---PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFL 218
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 67-335 6.19e-18

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: 81.78  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  67 PALVLLHGLFGSKTNLNSVAKTLAQQtGRRdlspgsppatcrpsrplavytqnldasvvtvhptpqVLTVDARNHGDSF- 145
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARD-GFR------------------------------------VIALDLRGFGKSSr 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 146 --YSPDMSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVedISPVDSKFGLEYLTYIAAMRAV 223
Cdd:pfam00561  44 pkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVL--LGALDPPHELDEADRFILALFP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 224 DIPDKVPHSHARKladeQLSHVVQDIAVRQFLLTNLVEADGRFVWRP----------NLDALAQHMEKLVAFPPRQE--S 291
Cdd:pfam00561 122 GFFDGFVADFAPN----PLGRLVAKLLALLLLRLRLLKALPLLNKRFpsgdyalaksLVTGALLFIETWSTELRAKFlgR 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1910430613 292 YPGPTLFLFGENSHFIHSSHHPEIRRLFPQAQVQTIPNAGHWIH 335
Cdd:pfam00561 198 LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
57-350 1.01e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 60.79  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  57 YKLLDGDAVRPALVLLHGLFGSKTNLNSVAKTLAQQtGRRdlspgsppatcrpsrplavytqnldasvvtvhptpqVLTV 136
Cdd:COG2267    19 RRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYA------------------------------------VLAF 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 137 DARNHGDS--FYSPDMSYEAMSQDLQ---DFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVedISPvdskfgl 211
Cdd:COG2267    62 DLRGHGRSdgPRGHVDSFDDYVDDLRaalDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVL--LAP------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 212 eyltyiaAMRAvdipDKVPHSHARKLADEQLSHVVQDIAVrqflltnlveadgrfvwrpnldalaqhmeklvafpprqes 291
Cdd:COG2267   133 -------AYRA----DPLLGPSARWLRALRLAEALARIDV---------------------------------------- 161

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910430613 292 ypgPTLFLFGENSHFIHSSHHPEI-RRLFPQAQVQTIPNAGHWIHASHLQD-FVAAIRDFL 350
Cdd:COG2267   162 ---PVLVLHGGADRVVPPEAARRLaARLSPDVELVLLPGARHELLNEPAREeVLAAILAWL 219
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 133-350 7.42e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.57  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDSfySPDM---SYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQRAELVERLIVedISPVdskf 209
Cdd:PRK14875  160 VIALDLPGHGAS--SKAVgagSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL--IAPA---- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 210 GL------EYLT-YIAAMRAVDIpdkvpHSHARKL-ADEQL--SHVVQDIaVRQFLLTNLVEAdgrfvwrpnLDALAQHm 279
Cdd:PRK14875  232 GLgpeingDYIDgFVAAESRREL-----KPVLELLfADPALvtRQMVEDL-LKYKRLDGVDDA---------LRALADA- 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 280 eklvAFPP-RQ--------ESYPGPTLFLFGENSHFIHSSHhpeIRRLFPQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:PRK14875  296 ----LFAGgRQrvdlrdrlASLAIPVLVIWGEQDRIIPAAH---AQGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFL 368
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 132-345 7.32e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 52.48  E-value: 7.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 132 QVLTVDARNHGDSFySPDMSYEAMsQDLQDFLPQLGLV-PCVLIGHSMGGktAMLLALQRAELVERLIVEDispvdskfg 210
Cdd:pfam12697  23 AVLAPDLPGHGSSS-PPPLDLADL-ADLAALLDELGAArPVVLVGHSLGG--AVALAAAAAALVVGVLVAP--------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 211 leyltyiAAMRAVDIPDKVPHSHARKLADEQLSHVVQDIAVRQFLLtnlvEADGRFVWRPNLDALAQHMEKLVAFPPRQE 290
Cdd:pfam12697  90 -------LAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD----DLPADAEWAAALARLAALLAALALLPLAAW 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910430613 291 SYPGPTLFLFGENSHFIHsSHHPEIRRLFPQAQVQTIPNAGHWIHASHlQDFVAA 345
Cdd:pfam12697 159 RDLPVPVLVLAEEDRLVP-ELAQRLLAALAGARLVVLPGAGHLPLDDP-EEVAEA 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 133-335 6.38e-07

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: 49.91  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDSF----YSPdmSYEAMSQDLQDFLPQL----GLVPCVLIGHSMGGKTAMLLALQRAELVERLIVedISP 204
Cdd:pfam12146  34 VYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIreehPGLPLFLLGHSMGGLIAALYALRYPDKVDGLIL--SAP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 205 ---VDSKFGLEYLTYIAAMRAVDIPDKVPHShaRKLADeQLSHvvqDIAVRQFLltnlvEADGRFVWRPNLDALAQ---H 278
Cdd:pfam12146 110 alkIKPYLAPPILKLLAKLLGKLFPRLRVPN--NLLPD-SLSR---DPEVVAAY-----AADPLVHGGISARTLYElldA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910430613 279 MEKLVAfppRQESYPGPTLFLFGENSHFIhssHHPEIRRLF-----PQAQVQTIPNAGHWIH 335
Cdd:pfam12146 179 GERLLR---RAAAITVPLLLLHGGADRVV---DPAGSREFYeragsTDKTLKLYPGLYHELL 234
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 66-350 2.61e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 47.91  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613  66 RPALVLLHGLFGSKTNLNSVAKTLAQqtgrrdlspgsppatcrpsrplavytqnldasvvtvHPtpqVLTVDARNHGDS- 144
Cdd:PRK11126    2 LPWLVFLHGLLGSGQDWQPVGEALPD------------------------------------YP---RLYIDLPGHGGSa 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 145 FYSPDmSYEAMSQDLQDFLPQLGLVPCVLIGHSMGGKTAMLLALQ-RAELVERLIVEdispvDSKFGLEYLTYIAAMRAV 223
Cdd:PRK11126   43 AISVD-GFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMYYACQgLAGGLCGLIVE-----GGNPGLQNAEERQARWQN 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 224 DipdkvpHSHARKLADEQLSHVVQD-----------IAVRQFLLTnlveadgrfVWRPNL-DALAQHME-----KLVAFP 286
Cdd:PRK11126  117 D------RQWAQRFRQEPLEQVLADwyqqpvfaslnAEQRQQLVA---------KRSNNNgAAVAAMLEatslaKQPDLR 181

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910430613 287 PRQESYPGPTLFLFGENSH-FihsshhpeiRRLFPQAQV--QTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:PRK11126  182 PALQALTFPFYYLCGERDSkF---------QALAQQLALplHVIPNAGHNAHRENPAAFAASLAQIL 239
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 133-350 2.40e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 42.21  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDS--FYSPDMSYEAmsQDLQ---DFLPQLGLVP---CVLIGHSMGGKTAMLLA--LQRAelveRLIVEDi 202
Cdd:COG1073    67 VLAFDYRGYGESegEPREEGSPER--RDARaavDYLRTLPGVDperIGLLGISLGGGYALNAAatDPRV----KAVILD- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 203 SPVDSkfgleyltyiaamravdipdkvphsharkladeqLSHVVQDIAVRQFLLTNlveadGRFVWRPNLdALAQHMEKl 282
Cdd:COG1073   140 SPFTS----------------------------------LEDLAAQRAKEARGAYL-----PGVPYLPNV-RLASLLND- 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1910430613 283 vAFPPRQ--ESYPGPTLFLFGENSHFiHSSHHpeIRRLFPQA----QVQTIPNAGHWIHASHLQD-FVAAIRDFL 350
Cdd:COG1073   179 -EFDPLAkiEKISRPLLFIHGEKDEA-VPFYM--SEDLYEAAaepkELLIVPGAGHVDLYDRPEEeYFDKLAEFF 249
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
133-350 6.51e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 40.77  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 133 VLTVDARNHGDSfysPDMSYEAMSQDLQ---DFLPQLGLVP---CVLIGHSMGGKTAMLLALQRAELVERLIveDISPVd 206
Cdd:COG1506    54 VLAPDYRGYGES---AGDWGGDEVDDVLaaiDYLAARPYVDpdrIGIYGHSYGGYMALLAAARHPDRFKAAV--ALAGV- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 207 skfgleyltyiaamravdipdkvphsharkladeqlshvvqdiavrqfllTNLVEADGRFVWRPN--LDALAQHMEKLVA 284
Cdd:COG1506   128 --------------------------------------------------SDLRSYYGTTREYTErlMGGPWEDPEAYAA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1910430613 285 FPPRQ--ESYPGPTLFLFGENSHFIHSSHhpeIRRLF-------PQAQVQTIPNAGHWIHASHLQDFVAAIRDFL 350
Cdd:COG1506   158 RSPLAyaDKLKTPLLLIHGEADDRVPPEQ---AERLYealkkagKPVELLVYPGEGHGFSGAGAPDYLERILDFL 229
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
 169-332 1.71e-03

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 39.58  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 169 VPCVLIGHSMGGKTAMLLALQ-RAELVERLI-----VEDI--SPVDSKFG--LEYLTYIAAM--RAVDIPDKVPHSHARK 236
Cdd:pfam10230  83 VKLILIGHSIGAYIALEVLKRlSERGIIKCVllfptIEDMarSPNGRILTrlLCYIPFLALVagFLLRVFKLLPESVKSL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910430613 237 LADEQLSHVVqdiAVRQFLLTNLVEADGRFVWRPNLDALAQHMEKLVAFPPRQ--ESYPGPTLFLFGENSHFIHSSHHPE 314
Cdd:pfam10230 163 LIRKVMGGMS---SPPHAVQTTLKFLLNPHCVRNALHMARDEMREVREDDDEDfiKANQERLWFYYGTTDHWVPVSTRDE 239

                         170
                  ....*....|....*....
gi 1910430613 315 IRRLFPQAQ-VQTIPNAGH 332
Cdd:pfam10230 240 LKELYPDGDlVVDEDGIPH 258
 
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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