2HCF


Conserved Protein Domain Family
HAD_like

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cd07506: HAD_like 
Click on image for an interactive view with Cn3D
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily
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.
Statistics
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PSSM-Id: 319809
View PSSM: cd07506
Aligned: 7 rows
Threshold Bit Score: 131.342
Threshold Setting Gi: 300783999
Created: 1-Apr-2008
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            #####                                                                       
2HCF_A         6 LVLFDIDGTLLkvesxnrrvladalievygtegstgshdfsgkxdgaiiyevlsnvgleraeiadkfdkaketyialfre 85
gi 83814682    3 LLLFDIDGTLVrvngrgreavnaalsslmdqpisadgvtfsgrtdpaivk--avlahndlpatdaliedvittyvdtmrd 80
gi 37523509    4 LVLFDIDGTILnvhgvgsrallaameavferqidpagysmsgktdtqivvellertggwpgevapllprvwdnylerftp 83
gi 163847625   8 LLLWDIDGTLLstdgiaanamrtalrqlvgphvriertsyagktdwqivreslpsvdeatiqsrlqefialytaeltaqr 87
gi 206889438   3 LILFDIDGTLIsaggagtrslnkafeeilgikdafknfemagktdiqiik--eglmfagiepsmslvneliesylnnlkv 80
gi 300788628  11 LVLWDVDHTLIetrgvgraiydrafpaatgrplaklaqisgrteldimae-slrvngleptdeavkqlaaalvqgyedar 89
gi 300783999   6 LVLWDIDHTLVdfselgaawygtaftaatgatlrvrpvfggrteratttd-lltangfeaseetiqalfkalvaeserhr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                       ##                                #              
2HCF_A        86 rarreditllEGVRELLDALssrsDVLLGLLTGNFeASGRHKLKLPGIdh--yfPFGAFADDaLDRNELPHIALERARRX 163
gi 83814682   81 vltpadvevlPGVSDLLARLdahpEIHLGLVTGNVePIAYEKLSAHGLde--yfPVGAFGSDhAERNRLPELATRRAADH 158
gi 37523509   84 alaachphvyAGIVPLLAALenrsEVVIGLLTGNVePAAWLKLRRVDLae--pfRLGAFGDAaPERCLLPEIAVENARKL 161
gi 163847625  88 ealiarstvfAGVVEALHALs--tHAYQAPLTGNVaAAARIKLECTGLlrwlevEAGAYGDDhFDRLALPPIAAGRARER 165
gi 206889438  81 einnnskhlkPGVKEFIEFIyyelNYPLGLLTGNLeKGARIKLEPFGLnl--ffPVGAFGSDhEDRNQLLPIAIDRFSKK 158
gi 300788628  90 qelaitgralPGAREALEHLaadpANHQGILTGNLrEVARIKLEVFGLdqyldfEASAFGDDhADRPELVRFARERAEAQ 169
gi 300783999  85 htfaetarplPGAAEALTAFaaggDVVQTLVTGNLpEISRHKLVPFGLdehldlEIGGYGTLsVHRPDLVPHAVGLAAAK 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
Feature 1                      ### ##                 
2HCF_A       164 tgan-yspsQIVIIGDTEHDIRCARELDARSIAVATG 199
gi 83814682  159 tgrafrpheHAVVVGDTAHDIECARAVGAQAVAVCTG 195
gi 37523509  162 tghh-frgkEIVIIGDTPNDVACGRHLGAKSIAVATG 197
gi 163847625 166 yrya-ftpaDVVIIGDTPRDIACGRAFGARTVAVATG 201
gi 206889438 159 fkys-idfhQCIVIGDTPRDVACAKPYGAKVIAVATG 194
gi 300788628 170 tgar-felrDVVLIGDTPNDVKAALTAGVRVVGVATG 205
gi 300783999 165 hgte-fgadAVVVIGDTPNDVRAAVDNGAISVAVATG 200

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