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Conserved domains on  [gi|406647874|ref|NP_001258331|]
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bifunctional epoxide hydrolase 2 isoform b [Mus musculus]

Protein Classification

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein (domain architecture ID 11552356)

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
204-477 9.65e-46

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: 159.98  E-value: 9.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  204 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 283
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  284 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 363
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  364 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 443
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647874  444 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 477
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
1-161 2.23e-44

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 154.81  E-value: 2.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   1 MKGKITFSQwvplMDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkr 80
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  81 dslAQMMC--ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALR 158
Cdd:cd02603  116 ---FQLELlpRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALR 192

                 ...
gi 406647874 159 ELE 161
Cdd:cd02603  193 ELA 195
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
204-477 9.65e-46

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: 159.98  E-value: 9.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  204 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 283
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  284 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 363
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  364 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 443
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647874  444 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 477
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
1-161 2.23e-44

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 154.81  E-value: 2.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   1 MKGKITFSQwvplMDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkr 80
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  81 dslAQMMC--ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALR 158
Cdd:cd02603  116 ---FQLELlpRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALR 192

                 ...
gi 406647874 159 ELE 161
Cdd:cd02603  193 ELA 195
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
1-150 1.22e-37

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 136.01  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874    1 MKGKITFSQWvplmdESYRKSSKACGANLPENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKR 80
Cdd:TIGR01509  41 LELALRRFKA-----QYGRTISPEDAQLLYKQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RA 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   81 DSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 150
Cdd:TIGR01509 109 HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
185-490 1.91e-35

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 133.60  E-value: 1.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 185 GYVTVKPGIRLHFVEMGSG-PALCLCHGFPESWFSWRYQIPALAQ--AGFRVLAIDMKGYGDSSSPPeieeYAMELLCKE 261
Cdd:COG0596    2 SLLLAADGVRLAYREAGGGgPPLVLLHGFPGSSSVWRPVFKVLPAlaARYRVIAPDLRGHGRSDPAG----YSLSAYADD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 262 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSIPVFnyqlyfqepgVAEAE 341
Cdd:COG0596   78 LAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQPAGAAPLA----------ALADL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 342 LEKNMSRTFKSFFRASDETGFIAvhkateiggilvntpedPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNT-ERNWK 420
Cdd:COG0596  148 LLGLDAAAFAALLAALGLLAALA-----------------AAARAGLAEALRAPLLGAAAAAFARAARADLAAAlLALLD 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 406647874 421 WSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGH-IEDCGHWTQIEKPTEVNQILIKWLQT 490
Cdd:COG0596  211 RDLRAALARITVPTLIIHGEDDPVVPAELARRLAAALPNDARLVvIPGAGHFPHLEAPEAFAAALLAFLER 281
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
186-497 6.61e-22

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 95.83  E-value: 6.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 186 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 262
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 263 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 341
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 342 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 414
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 415 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 486
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284
                        330
                 ....*....|.
gi 406647874 487 WLQTEVQNPSV 497
Cdd:PRK03592 285 WLRRLRLAVSA 295
YigB COG1011
FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];
51-159 4.97e-14

FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];


Pssm-ID: 223943 [Multi-domain]  Cd Length: 229  Bit Score: 71.47  E-value: 4.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  51 PMLQAAIALKKKGFTTCIVTNNwlDDGDKRDSLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFL 130
Cdd:COG1011  102 PEALEALKELGKKYKLGILTNG--ARPHQERKLRQ--LGLLDYFDAVFISEDVGVAKPDPEIFEYALEKLGVPPEEALFV 177
                         90       100       110
                 ....*....|....*....|....*....|
gi 406647874 131 DDFGSNL-KPARDMGMVTILVHNTASALRE 159
Cdd:COG1011  178 GDSLENDiLGARALGMKTVWINRGGKPLPD 207
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
50-144 2.65e-10

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Pseudomonas sp. (S)-2-haloacid dehalogenase 1. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 395571 [Multi-domain]  Cd Length: 191  Bit Score: 59.52  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   50 RPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 128
Cdd:pfam00702 100 YPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVL 175
                          90
                  ....*....|....*.
gi 406647874  129 FLDDFGSNLKPARDMG 144
Cdd:pfam00702 176 MVGDGVNDIPAAKAAG 191
biphenyl_bphD TIGR03343
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; Members of this family are ...
186-297 1.02e-08

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; Members of this family are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, or HOPD hydrolase, the BphD protein of biphenyl degradation. BphD acts on the product of ring meta-cleavage by BphC. Many species carrying bphC and bphD are capable of degrading polychlorinated biphenyls as well as biphenyl itself.


Pssm-ID: 132386 [Multi-domain]  Cd Length: 282  Bit Score: 56.46  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  186 YVTV-KPGI---RLHFVEMGSGPALCLCHGF---PESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMeLL 258
Cdd:TIGR03343   9 FVKInEKGLsnfRIHYNEAGNGEAVIMLHGGgpgAGGWSNYYRNIGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGL-VN 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 406647874  259 CKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERV 297
Cdd:TIGR03343  88 ARAVKGLMDALDIEKAHLVGNSMGGATALNFALEYPDRI 126
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
89-152 1.89e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872  Cd Length: 199  Bit Score: 51.58  E-value: 1.89e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647874  89 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 152
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
estX NF033124
alpha/beta fold putative hydrolase EstX;
226-314 2.92e-03

alpha/beta fold putative hydrolase EstX;


Pssm-ID: 411093 [Multi-domain]  Cd Length: 280  Bit Score: 39.68  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 226 LAQAGFRVLAIDMKGYGDSSS-PPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLN 304
Cdd:NF033124  47 LAKMGRYVIRYDHRDTGKSTSyEPGQAPYSVEELADDVVRVIDGYGLEAAHLVGMSLGGFLSQLVALKYPKRVKSLTLIA 126
                         90
                 ....*....|.
gi 406647874 305 TPFMP-PDPDV 314
Cdd:NF033124 127 SERLAdADPDM 137
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
204-477 9.65e-46

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: 159.98  E-value: 9.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  204 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 283
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  284 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 363
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  364 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 443
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211
                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647874  444 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 477
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
1-161 2.23e-44

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 154.81  E-value: 2.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   1 MKGKITFSQwvplMDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkr 80
Cdd:cd02603   49 ERGRITEEE----FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  81 dslAQMMC--ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALR 158
Cdd:cd02603  116 ---FQLELlpRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALR 192

                 ...
gi 406647874 159 ELE 161
Cdd:cd02603  193 ELA 195
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
1-150 1.22e-37

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 136.01  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874    1 MKGKITFSQWvplmdESYRKSSKACGANLPENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKR 80
Cdd:TIGR01509  41 LELALRRFKA-----QYGRTISPEDAQLLYKQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RA 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   81 DSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 150
Cdd:TIGR01509 109 HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
185-490 1.91e-35

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 133.60  E-value: 1.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 185 GYVTVKPGIRLHFVEMGSG-PALCLCHGFPESWFSWRYQIPALAQ--AGFRVLAIDMKGYGDSSSPPeieeYAMELLCKE 261
Cdd:COG0596    2 SLLLAADGVRLAYREAGGGgPPLVLLHGFPGSSSVWRPVFKVLPAlaARYRVIAPDLRGHGRSDPAG----YSLSAYADD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 262 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSIPVFnyqlyfqepgVAEAE 341
Cdd:COG0596   78 LAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALRQPAGAAPLA----------ALADL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 342 LEKNMSRTFKSFFRASDETGFIAvhkateiggilvntpedPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNT-ERNWK 420
Cdd:COG0596  148 LLGLDAAAFAALLAALGLLAALA-----------------AAARAGLAEALRAPLLGAAAAAFARAARADLAAAlLALLD 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 406647874 421 WSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGH-IEDCGHWTQIEKPTEVNQILIKWLQT 490
Cdd:COG0596  211 RDLRAALARITVPTLIIHGEDDPVVPAELARRLAAALPNDARLVvIPGAGHFPHLEAPEAFAAALLAFLER 281
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
25-165 3.11e-30

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.


Pssm-ID: 274054  Cd Length: 211  Bit Score: 116.85  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   25 CGANLPENFSISQIFSQAMAARSINRPMLQAAI-ALKKKGFTTCIVTNNWLDDGDKRDSLAqmMCELSQHFDFLIESCQV 103
Cdd:TIGR02247  71 YGLRLGHDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSAEEALL--PGDIMALFDAVVESCLE 148
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406647874  104 GMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTG 165
Cdd:TIGR02247 149 GLRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATK 210
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
186-497 6.61e-22

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 95.83  E-value: 6.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 186 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 262
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 263 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 341
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 342 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 414
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 415 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 486
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284
                        330
                 ....*....|.
gi 406647874 487 WLQTEVQNPSV 497
Cdd:PRK03592 285 WLRRLRLAVSA 295
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
186-326 3.99e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 179147  Cd Length: 302  Bit Score: 87.72  E-value: 3.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 186 YVTVKPG----IRLHFVEMGSG---PALCLcHGFPeSW-FSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMEL 257
Cdd:PRK00870  23 YVDVDDGdggpLRMHYVDEGPAdgpPVLLL-HGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYAR 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406647874 258 LCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTpfMPPDPDVSPMKV-------IRSIPVF 326
Cdd:PRK00870 101 HVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT--GLPTGDGPMPDAfwawrafSQYSPVL 174
PRK05855 PRK05855
SDR family oxidoreductase;
187-477 1.54e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.34  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 187 VTVKPGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVT 264
Cdd:PRK05855   7 VVSSDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLA-DRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 265 FLDKLGIPQAV-FIGHDWAGVMVWNmALFYPERVRAVASLnTPFMPPDPD------------VSPMKVIRsipVFN---- 327
Cdd:PRK05855  86 VIDAVSPDRPVhLLAHDWGSIQGWE-AVTRPRAAGRIASF-TSVSGPSLDhvgfwlrsglrrPTPRRLAR---ALGqllr 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 328 --YQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATeiggilvnTPEDpnlskitteeeiefyiqqfkktGF 405
Cdd:PRK05855 161 swYIYLFHLPVLPELLWRLGLGRAWPRLLRRVEGTPVDPIPTQT--------TLSD----------------------GA 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 406647874 406 RGpLNWYR-NTERNwkwSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIeDCGHWTQIEKP 477
Cdd:PRK05855 211 HG-VKLYRaNMIRS---LSRPRERYTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREI-KAGHWLPMSHP 278
PLN02578 PLN02578
hydrolase
192-305 7.87e-16

hydrolase


Pssm-ID: 215315  Cd Length: 354  Bit Score: 78.73  E-value: 7.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 192 GIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPpeIEEYAMELLCKEMVTFLDKLGI 271
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA--LIEYDAMVWRDQVADFVKEVVK 151
                         90       100       110
                 ....*....|....*....|....*....|....
gi 406647874 272 PQAVFIGHDWAGVMVWNMALFYPERVRAVASLNT 305
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
194-311 5.64e-15

haloalkane dehalogenase; Provisional


Pssm-ID: 179554  Cd Length: 286  Bit Score: 75.28  E-value: 5.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 194 RLHFVEMGSGPALCLCHGFPESWFSWRYQIPALaQAGFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQ 273
Cdd:PRK03204  25 RIHYIDEGTGPPILLCHGNPTWSFLYRDIIVAL-RDRFRCVAPDYLGFGLSERPSGF-GYQIDEHARVIGEFVDHLGLDR 102
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 406647874 274 AVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPD 311
Cdd:PRK03204 103 YLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
YigB COG1011
FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];
51-159 4.97e-14

FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism];


Pssm-ID: 223943 [Multi-domain]  Cd Length: 229  Bit Score: 71.47  E-value: 4.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  51 PMLQAAIALKKKGFTTCIVTNNwlDDGDKRDSLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFL 130
Cdd:COG1011  102 PEALEALKELGKKYKLGILTNG--ARPHQERKLRQ--LGLLDYFDAVFISEDVGVAKPDPEIFEYALEKLGVPPEEALFV 177
                         90       100       110
                 ....*....|....*....|....*....|
gi 406647874 131 DDFGSNL-KPARDMGMVTILVHNTASALRE 159
Cdd:COG1011  178 GDSLENDiLGARALGMKTVWINRGGKPLPD 207
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
191-301 1.47e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.90  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 191 PGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSspPEIEEYAMELLCKEMVTFLDK 268
Cdd:PRK14875 117 GGRTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASS--KAVGAGSLDELAAAVLAFLDA 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 406647874 269 LGIPQAVFIGHDWAGVMVWNMALFYPERVRAVA 301
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLT 226
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
201-304 8.57e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419  Cd Length: 294  Bit Score: 62.83  E-value: 8.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 201 GSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSP-----PEIEEYAMELLCKEMVTFLDKLGIPQAV 275
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105
                         90       100
                 ....*....|....*....|....*....
gi 406647874 276 FIGHDWAGVMVWNMALFYPERVRAVASLN 304
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLIN 134
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
179-488 2.48e-10

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


Pssm-ID: 225176 [Multi-domain]  Cd Length: 298  Bit Score: 61.62  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 179 PNDVSHGYVTVKPGIRLHF----VEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPP-----E 249
Cdd:COG2267    6 PRTRTEGYFTGADGTRLRYrtwaAPEPPKGVVVLVHGLGEHSGRYEELADDLAARGFDVYALDLRGHGRSPRGQrghvdS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 250 IEEYAMELLckemvTFLDKL-----GIPQAVFiGHDWAGVMVWNMALFYPERVRAVAsLNTPFMPPDPDVSPMKVIRsip 324
Cdd:COG2267   86 FADYVDDLD-----AFVETIaepdpGLPVFLL-GHSMGGLIALLYLARYPPRIDGLV-LSSPALGLGGAILRLILAR--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 325 vfnyqlyfqepgvaeaeleknMSRTFKSFFRASdeTGFIAvhkateiggilvNTPEDPNLSKIT-TEEEIEFYIQQfKKT 403
Cdd:COG2267  156 ---------------------LALKLLGRIRPK--LPVDS------------NLLEGVLTDDLSrDPAEVAAYEAD-PLI 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 404 GFRGPLN-WYRN---TERNWKWSCKGlgrKILVPALMVTAEKD-IVLRPEMSKNMEKWIPFLKRGH--IEDCGHWTQIEK 476
Cdd:COG2267  200 GVGGPVSrWVDLallAGRVPALRDAP---AIALPVLLLQGGDDrVVDNVEGLARFFERAGSPDKELkvIPGAYHELLNEP 276
                        330
                 ....*....|....*
gi 406647874 477 PTEVNQIL---IKWL 488
Cdd:COG2267  277 DRAREEVLkdiLAWL 291
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
50-144 2.65e-10

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Pseudomonas sp. (S)-2-haloacid dehalogenase 1. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 395571 [Multi-domain]  Cd Length: 191  Bit Score: 59.52  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   50 RPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 128
Cdd:pfam00702 100 YPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVL 175
                          90
                  ....*....|....*.
gi 406647874  129 FLDDFGSNLKPARDMG 144
Cdd:pfam00702 176 MVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
48-150 1.29e-09

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 55.48  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  48 INRPMLQAaiaLKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEV 127
Cdd:cd01427   11 LAVELLKR---LRAAGIKLAIVTNRSREALRAL--LEK--LGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEV 83
                         90       100
                 ....*....|....*....|...
gi 406647874 128 VFLDDFGSNLKPARDMGMVTILV 150
Cdd:cd01427   84 LFVGDSENDIEAARAAGGRTVAV 106
biphenyl_bphD TIGR03343
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; Members of this family are ...
186-297 1.02e-08

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; Members of this family are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, or HOPD hydrolase, the BphD protein of biphenyl degradation. BphD acts on the product of ring meta-cleavage by BphC. Many species carrying bphC and bphD are capable of degrading polychlorinated biphenyls as well as biphenyl itself.


Pssm-ID: 132386 [Multi-domain]  Cd Length: 282  Bit Score: 56.46  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  186 YVTV-KPGI---RLHFVEMGSGPALCLCHGF---PESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMeLL 258
Cdd:TIGR03343   9 FVKInEKGLsnfRIHYNEAGNGEAVIMLHGGgpgAGGWSNYYRNIGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGL-VN 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 406647874  259 CKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERV 297
Cdd:TIGR03343  88 ARAVKGLMDALDIEKAHLVGNSMGGATALNFALEYPDRI 126
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
59-150 3.60e-08

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 52.97  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874   59 LKKKGFTTCIVTNNWlddgdkRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSN 136
Cdd:pfam13419  91 LKEQGYKLGIVTSKS------RENVEEFLkqLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRD 164
                          90
                  ....*....|....
gi 406647874  137 LKPARDMGMVTILV 150
Cdd:pfam13419 165 IEAAKNAGIKVIAV 178
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
205-316 3.98e-08

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: 403389 [Multi-domain]  Cd Length: 237  Bit Score: 54.14  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  205 ALCLCHGFPESwfSWRYQ--IPALAQAGFRVLAIDMKGYGDSSSPP-EIEEYamELLCKEMVTFLDKL-----GIPQAVF 276
Cdd:pfam12146   6 VVVLVHGLGEH--SGRYAhlADALAAQGFAVYAYDHRGHGRSDGKRgHVPSF--DDYVDDLDTFVDHVrarhpGLPLFLL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 406647874  277 iGHDWAGVMVWNMALFYPERVRAVAsLNTPFMPPDPDVSP 316
Cdd:pfam12146  82 -GHSMGGLIAALYALRYPDKVAGLI-LSAPALKIKPYAPP 119
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
202-278 5.51e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283  Cd Length: 360  Bit Score: 54.85  E-value: 5.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406647874 202 SGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQAVFIG 278
Cdd:PLN02679  87 SGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGF-SYTMETWAELILDFLEEVVQKPTVLIG 161
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
208-318 8.33e-08

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


Pssm-ID: 403789 [Multi-domain]  Cd Length: 212  Bit Score: 52.87  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  208 LCHGfpesWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPP-EIEEYAmellckEMVTFLDKLG--IPQAVFIGHDWAGV 284
Cdd:pfam12697   3 LVHG----AGLSAAPLAALLAAGVRVLAPDLPGHGSSDPPPlDLADLA------DLAALLDELGaaGRPVVLVGHSLGGA 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 406647874  285 MVWNMALFYPERVRAVASLNTPFMPPDPDVSPMK 318
Cdd:pfam12697  73 VALAAAAAALVVGVLVAPLALPLGLLAALLALLA 106
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
89-152 1.89e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872  Cd Length: 199  Bit Score: 51.58  E-value: 1.89e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647874  89 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 152
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
48-152 6.89e-07

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 48.06  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  48 INRPMLQAaiaLKKKGFTTCIVTNNwlddgDKRdsLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPN 125
Cdd:cd16415   11 LAVETLKD---LKEKGLKLAVVSNF-----DRR--LRELLeaLGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPE 80
                         90       100
                 ....*....|....*....|....*...
gi 406647874 126 EVVFL-DDFGSNLKPARDMGMVTILVHN 152
Cdd:cd16415   81 EALHVgDDLKNDYLGARAVGWHALLVDR 108
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
61-148 1.04e-06

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 47.15  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  61 KKGFTTCIVTNnwlddGDK---RDSLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFL-DDFGSN 136
Cdd:cd04305   22 KKGYKLGIITN-----GPTevqWEKLEQ--LGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSLESD 94
                         90
                 ....*....|..
gi 406647874 137 LKPARDMGMVTI 148
Cdd:cd04305   95 ILGAKNAGIKTV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
58-150 5.94e-06

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 47.26  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  58 ALKKKGFTTCIVTNnwlddGDkRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGS 135
Cdd:cd02588  102 RLREAGYRLAILSN-----GS-PDLIEDVVanAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAW 175
                         90
                 ....*....|....*
gi 406647874 136 NLKPARDMGMVTILV 150
Cdd:cd02588  176 DLAGARALGLRTAWI 190
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
50-163 1.63e-05

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 45.73  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  50 RPMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQM---MCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNE 126
Cdd:cd02616   86 YETLAR---LKSQGIKLGVVTT-------KLRETALKglkLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 406647874 127 VVFLDDFGSNLKPARDMGMVTILVhntASALRELEKV 163
Cdd:cd02616  156 ALMVGDSPHDILAGKNAGVKTVGV---TWGYKGREYL 189
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
204-321 2.29e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484  Cd Length: 402  Bit Score: 46.44  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 204 PALCLCHGFPESW-FSWRyQIPALAqAGFRVLAIDMKGYGDSSSPP-------EIEEYamellckemvtFLDKL------ 269
Cdd:PLN02894 106 PTLVMVHGYGASQgFFFR-NFDALA-SRFRVIAIDQLGWGGSSRPDftcksteETEAW-----------FIDSFeewrka 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 406647874 270 -GIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIR 321
Cdd:PLN02894 173 kNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTK 225
PRK10673 PRK10673
esterase;
233-297 3.89e-05

esterase;


Pssm-ID: 182637  Cd Length: 255  Bit Score: 45.11  E-value: 3.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406647874 233 VLAIDMKGYGDSSSPPEIEEYAMellCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERV 297
Cdd:PRK10673  45 IIQVDMRNHGLSPRDPVMNYPAM---AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRI 106
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
194-309 8.47e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.87  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 194 RLHFVEMGS--GPALCLCHGFPESWFSWRYQIPALAQaGFRVLAIDMKGYGDSSSPP-------EIEEY--AMELLCKEM 262
Cdd:PLN03084 116 RWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQpgygfnyTLDEYvsSLESLIDEL 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 406647874 263 VTflDKLGIpqaVFIGHdWAGVMVwNMALFYPERVRAVASLNTPFMP 309
Cdd:PLN03084 195 KS--DKVSL---VVQGY-FSPPVV-KYASAHPDKIKKLILLNPPLTK 234
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
150-303 1.79e-04

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


Pssm-ID: 224423 [Multi-domain]  Cd Length: 620  Bit Score: 44.06  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 150 VHNTASALRELEKVTGTQfPEaPLPVPCNPNDVSHGYVTVKPGirlhFVEMGSGPALCLCHGFPES----WFSWRYQIpa 225
Cdd:COG1506  347 AKLTSSNNSGLKKVKLAE-PE-PVTYKSNDGETIHGWLYKPPG----FDPRKKYPLIVYIHGGPSAqvgySFNPEIQV-- 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 226 LAQAGFRVLAIDMK---GYGDSSSPPEIEEYAMELL--CKEMVTFLDKLGI--PQAVFI-GHDWAGVMVwNMALFYPERV 297
Cdd:COG1506  419 LASAGYAVLAPNYRgstGYGREFADAIRGDWGGVDLedLIAAVDALVKLPLvdPERIGItGGSYGGYMT-LLAATKTPRF 497

                 ....*.
gi 406647874 298 RAVASL 303
Cdd:COG1506  498 KAAVAV 503
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
58-152 3.27e-04

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 40.68  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  58 ALKKKGFTTCIVTNNWLDDGDKRDSLAQmmcELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNL 137
Cdd:cd07505   52 ALKAAGIPVAVATSSSRRNVELLLLELG---LLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGI 128
                         90
                 ....*....|....*
gi 406647874 138 KPARDMGMVTILVHN 152
Cdd:cd07505  129 EAAKAAGMTVVAVPD 143
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
90-152 1.06e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 39.92  E-value: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647874  90 LSQHFDFLIESCQVGMI-KPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 152
Cdd:cd02604  119 LADLFDGIFDIEYAGPDpKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
YcjU COG0637
Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and ...
58-156 1.17e-03

Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only];


Pssm-ID: 223710 [Multi-domain]  Cd Length: 221  Bit Score: 40.49  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  58 ALKKKGFTTCIVTNNwlDDGDKRDSLAQMmcELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNL 137
Cdd:COG0637   97 QLKARGIPLAVASSS--PRRAAERVLARL--GLLDYFDVIVTADDVARGKPAPDIYLLAAERLGVDPEECVVVEDSPAGI 172
                         90
                 ....*....|....*....
gi 406647874 138 KPARDMGMVTILVHNTASA 156
Cdd:COG0637  173 QAAKAAGMRVVGVPAGHDR 191
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
107-162 1.43e-03

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 223720  Cd Length: 269  Bit Score: 40.27  E-value: 1.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 406647874 107 KPEPQIYNFLLDTLKAKPNEVVFL-DDFGSNLKPARDMGMVTILVHNTASALRELEK 162
Cdd:COG0647  190 KPSPAIYEAALEKLGLDRSEVLMVgDRLDTDILGAKAAGLDTLLVLTGVSSAEDLDR 246
estX NF033124
alpha/beta fold putative hydrolase EstX;
226-314 2.92e-03

alpha/beta fold putative hydrolase EstX;


Pssm-ID: 411093 [Multi-domain]  Cd Length: 280  Bit Score: 39.68  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874 226 LAQAGFRVLAIDMKGYGDSSS-PPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLN 304
Cdd:NF033124  47 LAKMGRYVIRYDHRDTGKSTSyEPGQAPYSVEELADDVVRVIDGYGLEAAHLVGMSLGGFLSQLVALKYPKRVKSLTLIA 126
                         90
                 ....*....|.
gi 406647874 305 TPFMP-PDPDV 314
Cdd:NF033124 127 SERLAdADPDM 137
Hydrolase_like pfam13242
HAD-hyrolase-like;
107-150 3.78e-03

HAD-hyrolase-like;


Pssm-ID: 404179 [Multi-domain]  Cd Length: 75  Bit Score: 36.06  E-value: 3.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 406647874  107 KPEPQIYNFLLDTLKAKPNEVVFL-DDFGSNLKPARDMGMVTILV 150
Cdd:pfam13242   4 KPNPGMLRRALEALGLDPERTVMIgDRLDTDIEAAREAGARTILV 48
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
51-150 8.92e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 35.90  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647874  51 PMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQMMCE--LSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 128
Cdd:cd16421   14 ELLKA---LRQKGIKLAVLSN-------KPNEAVQVLVEelFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVL 83
                         90       100
                 ....*....|....*....|..
gi 406647874 129 FLDDFGSNLKPARDMGMVTILV 150
Cdd:cd16421   84 YVGDSGVDMQTARNAGMDEIGV 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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