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Conserved domains on  [gi|1958791068|ref|XP_038935694|]
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serine hydrolase-like protein 2 isoform X2 [Rattus norvegicus]

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

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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, ...
34-144 2.55e-24

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: 96.61  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  34 IAVKVWGLQKnPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHysPGLPYYHHNFVSEVRRVVSAFKWTR 113
Cdd:COG0596    14 LHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 114 LSLLGHSFGGVVGGLFACMFPEMVDKLILLD 144
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
34-144 2.55e-24

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: 96.61  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  34 IAVKVWGLQKnPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHysPGLPYYHHNFVSEVRRVVSAFKWTR 113
Cdd:COG0596    14 LHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 114 LSLLGHSFGGVVGGLFACMFPEMVDKLILLD 144
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
45-154 5.52e-19

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: 82.94  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  45 PPVLCLHGWLDNANSFDKLIPFLPKD-FCYVAMDFGGHGLSTHYSPGLPYYHHNFVSEVRRVVSAFKWTRLSLLGHSFGG 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 124 VVGGLFACMFPEMVDKLILLDSTPLLMDLNE 154
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDE 111
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
45-154 2.84e-16

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


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 75.33  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  45 PPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHYSPGLPYYHHNFVSEV-RRVVSAFKWTRLSLLGHSFGG 123
Cdd:TIGR03695   3 PVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMGG 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 124 VVGGLFACMFPEMVDKLILLDSTPLLMDLNE 154
Cdd:TIGR03695  83 RIALYYALQYPERVQGLILESGSPGLQTEEE 113
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
40-144 7.06e-09

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 55.27  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  40 GLQKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLST--HYSPGLPYYHHNFVSEVRRVVSAFKWTRLSLL 117
Cdd:PLN03084  123 GSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpQPGYGFNYTLDEYVSSLESLIDELKSDKVSLV 202
                          90       100
                  ....*....|....*....|....*....
gi 1958791068 118 --GHSFGGVVGglFACMFPEMVDKLILLD 144
Cdd:PLN03084  203 vqGYFSPPVVK--YASAHPDKIKKLILLN 229
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
34-144 2.55e-24

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: 96.61  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  34 IAVKVWGLQKnPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHysPGLPYYHHNFVSEVRRVVSAFKWTR 113
Cdd:COG0596    14 LHYREAGPDG-PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 114 LSLLGHSFGGVVGGLFACMFPEMVDKLILLD 144
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
45-154 5.52e-19

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: 82.94  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  45 PPVLCLHGWLDNANSFDKLIPFLPKD-FCYVAMDFGGHGLSTHYSPGLPYYHHNFVSEVRRVVSAFKWTRLSLLGHSFGG 123
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 124 VVGGLFACMFPEMVDKLILLDSTPLLMDLNE 154
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDE 111
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
45-154 2.84e-16

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


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 75.33  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  45 PPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHYSPGLPYYHHNFVSEV-RRVVSAFKWTRLSLLGHSFGG 123
Cdd:TIGR03695   3 PVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMGG 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958791068 124 VVGGLFACMFPEMVDKLILLDSTPLLMDLNE 154
Cdd:TIGR03695  83 RIALYYALQYPERVQGLILESGSPGLQTEEE 113
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
33-145 2.46e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 64.25  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  33 HIAVKVWGLQKNP--PVLCLHGWLDNANSFDKLIPFL-PKDFCYVAMDFGGHGLSthysPGLPYYHHNF---VSEVRRVV 106
Cdd:COG2267    15 RLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRS----DGPRGHVDSFddyVDDLRAAL 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958791068 107 SAFK---WTRLSLLGHSFGGVVGGLFACMFPEMVDKLILLDS 145
Cdd:COG2267    91 DALRarpGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
40-144 7.06e-09

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 55.27  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  40 GLQKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLST--HYSPGLPYYHHNFVSEVRRVVSAFKWTRLSLL 117
Cdd:PLN03084  123 GSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpQPGYGFNYTLDEYVSSLESLIDELKSDKVSLV 202
                          90       100
                  ....*....|....*....|....*....
gi 1958791068 118 --GHSFGGVVGglFACMFPEMVDKLILLD 144
Cdd:PLN03084  203 vqGYFSPPVVK--YASAHPDKIKKLILLN 229
PRK05855 PRK05855
SDR family oxidoreductase;
34-124 1.05e-08

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 54.99  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  34 IAVKVWGLQKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHYSPGLPYYHHNFVSEVRRVVSAFKWTR 113
Cdd:PRK05855   15 LAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDR 94
                          90
                  ....*....|..
gi 1958791068 114 -LSLLGHSFGGV 124
Cdd:PRK05855   95 pVHLLAHDWGSI 106
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
47-152 1.54e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 50.55  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  47 VLCLHGWldnANSFDKLIPFLPKDFCYVAMDFGGHGLSTHyspglPYYHHNFVSEVRRVVSAFK-WTRLSLLGHSFGGVV 125
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSP-----PPLDLADLADLAALLDELGaARPVVLVGHSLGGAV 72
                          90       100
                  ....*....|....*....|....*..
gi 1958791068 126 GGLFACMfpeMVDKLILLDSTPLLMDL 152
Cdd:pfam12697  73 ALAAAAA---ALVVGVLVAPLAAPPGL 96
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
42-147 1.86e-07

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 50.59  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  42 QKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHYSP-GLPYYHHNFVSEVRRVVSafkWtrlslLGHS 120
Cdd:TIGR01738   2 QGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPlSLADMAEAIAAQAPDPAI---W-----LGWS 73
                          90       100
                  ....*....|....*....|....*..
gi 1958791068 121 FGGVVGGLFACMFPEMVDKLILLDSTP 147
Cdd:TIGR01738  74 LGGLVALHIAATHPDRVRALVTVASSP 100
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
47-142 9.15e-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: 48.36  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  47 VLCLHGWLDNANSFDKLIPFLPK-DFCYVAMDFGGHGLSthysPGLPYYHHNF-------VSEVRRVVSAFKWTRLSLLG 118
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAqGFAVYAYDHRGHGRS----DGKRGHVPSFddyvddlDTFVDKIREEHPGLPLFLLG 82
                          90       100
                  ....*....|....*....|....
gi 1958791068 119 HSFGGVVGGLFACMFPEMVDKLIL 142
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLIL 106
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
46-147 1.57e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 45.59  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  46 PVLCLHGWLDNANSFDKLIPFLPKD-FCYVAMDFGGHGLST-HYSPGLpyyhHNFVSEVRRVVSAfkwTRLSLLGHSFGG 123
Cdd:COG1075     7 PVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIeDSAEQL----AAFVDAVLAATGA---EKVDLVGHSMGG 79
                          90       100
                  ....*....|....*....|....*.
gi 1958791068 124 VVGGLFACMF--PEMVDKLILLdSTP 147
Cdd:COG1075    80 LVARYYLKRLggAAKVARVVTL-GTP 104
PRK10673 PRK10673
esterase;
42-148 2.11e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.42  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  42 QKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHySPGLPYyhHNFVSEVRRVVSAFKWTRLSLLGHSF 121
Cdd:PRK10673   14 HNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPR-DPVMNY--PAMAQDLLDTLDALQIEKATFIGHSM 90
                          90       100
                  ....*....|....*....|....*..
gi 1958791068 122 GGVVGGLFACMFPEMVDKLILLDSTPL 148
Cdd:PRK10673   91 GGKAVMALTALAPDRIDKLVAIDIAPV 117
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
47-151 1.46e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 41.85  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  47 VLCLHGWLDNANSFDKLIPFLPKDFCYV-AMDFGGHGlsTHYSPGLPYYHHNFVSEVRRVVSAFK--WTRLSLLGHSFGG 123
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAKAGYTVyAPRLPGHG--TSPEDLLKTTWEDWLEDVEEAYEILKagYDKVIVIGLSMGG 95
                          90       100
                  ....*....|....*....|....*...
gi 1958791068 124 VVGGLFACMFPEmVDKLILLdSTPLLMD 151
Cdd:COG1647    96 LLALLLAARYPD-VAGLVLL-SPALKID 121
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
45-143 1.26e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 39.51  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  45 PPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSthyspGLPYYHHNFVSEVRR--VVSAFKWTR---LS---L 116
Cdd:PLN02894  106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGS-----SRPDFTCKSTEETEAwfIDSFEEWRKaknLSnfiL 180
                          90       100
                  ....*....|....*....|....*..
gi 1958791068 117 LGHSFGGVVGGLFACMFPEMVDKLILL 143
Cdd:PLN02894  181 LGHSFGGYVAAKYALKHPEHVQHLILV 207
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
29-145 2.26e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.77  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  29 VPWGHIAVKVWGLQKNPPVLCLHGWLDNANSFDKLIPFLPKDFCYVAMDFGGHGLSTHY--SPGLPyyhhNFVSEVRRVV 106
Cdd:PRK14875  116 IGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvgAGSLD----ELAAAVLAFL 191
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958791068 107 SAFKWTRLSLLGHSFGGVVGGLFACMFPEMVDKLILLDS 145
Cdd:PRK14875  192 DALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
42-143 6.19e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 36.92  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791068  42 QKNPPVLCLHGWLDNA-NSFDKLIPFLPKD-FCYVAMDFGGHGLSTHyspglpyyhHNFVSEVRRVVSAFKW-------- 111
Cdd:COG1506    21 KKYPVVVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGESAG---------DWGGDEVDDVLAAIDYlaarpyvd 91
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958791068 112 -TRLSLLGHSFGGVVGGLFACMFPEMVDKLILL 143
Cdd:COG1506    92 pDRIGIYGHSYGGYMALLAAARHPDRFKAAVAL 124
 
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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