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Conserved domains on  [gi|111306785|gb|AAI20734|]
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Poly (ADP-ribose) polymerase family, member 12 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 571-687 3.68e-57

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


:

Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 189.84  E-value: 3.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 571 QLFHGTSANFVDAICQQNFDWRVCGLHGTSYGKGSYFARDAAYSHHYSKSDTHS---HMMFLARVLVGDFVRGSTSFVRP 647
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 111306785 648 PAK-EGQSNAFYDSCVNSMSDPTIFVVFEKHQVYPEYLIQY 687
Cdd:cd01439   81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 388-468 3.32e-13

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 65.01  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  388 IWYWMDEFGSWQEYGRQgsghpvttiSSSDVERAYLAfcapgaDAQAATLKFQAGKHNYELHFKAFLQKNLVYGTIRKVC 467
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQK------GKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65


                  .
gi 111306785  468 R 468
Cdd:pfam02825  66 R 66
WWE super family cl46925
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 309-382 3.80e-06

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


The actual alignment was detected with superfamily member smart00678:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 45.02  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785   309 YRWQFLD-GGKWKDLD--NMELIEEAY--SNPSKDRIV----YTesaagfhfdnLDFNSMKFGNTLARRLSTASSVTKPP 379
Cdd:smart00678   1 YVWEYEGrNGKWWPYDprVSEDIEEAYaaGKKLCELSIcgfpYT----------IDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 111306785   380 HFI 382
Cdd:smart00678  71 YSK 73
ZnF_C3H1 smart00356
zinc finger;
186-208 2.68e-03

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|...
gi 111306785   186 KLHICQYFLQGECKFGTSCKRSH 208
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAH 25
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 571-687 3.68e-57

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 189.84  E-value: 3.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 571 QLFHGTSANFVDAICQQNFDWRVCGLHGTSYGKGSYFARDAAYSHHYSKSDTHS---HMMFLARVLVGDFVRGSTSFVRP 647
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 111306785 648 PAK-EGQSNAFYDSCVNSMSDPTIFVVFEKHQVYPEYLIQY 687
Cdd:cd01439   81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 517-689 7.76e-44

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 156.34  E-value: 7.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  517 SEEYQKVWNIFNRTLP-----FYFVQKIERIQNMGLWEVYQWQKCQMqkqnggkevDERQLFHGTSANFVDAICQQNF-- 589
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR---------NRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  590 DWRVCGLHGTSYGKGSYFARDAAYSHHYSKS--DTHSHMMFLARVLVGD------------------FVRGSTSFVR--- 646
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPseAHGNGLMLLSEVALGDmnelkkadyaeklppgkhSVKGLGKTAPesf 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 111306785  647 -----PPAKEGQSNaFYDSCVnsmSDPTIFVVFEKHQVYPEYLIQYST 689
Cdd:pfam00644 152 vdldgVPLGKLVAT-GYDSSV---LLYNEYVVYNVNQVRPKYLLEVKF 195
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 388-468 3.32e-13

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 65.01  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  388 IWYWMDEFGSWQEYGRQgsghpvttiSSSDVERAYLAfcapgaDAQAATLKFQAGKHNYELHFKAFLQKNLVYGTIRKVC 467
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQK------GKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65


                  .
gi 111306785  468 R 468
Cdd:pfam02825  66 R 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 387-476 1.70e-11

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 60.05  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785   387 WIWYWMDEFGSWqeygrqgsgHPVTTISSSDVERAYLAfcapgaDAQAATLKFQAgkHNYELHFKAFLQKNLVYGTIRKV 466
Cdd:smart00678   1 YVWEYEGRNGKW---------WPYDPRVSEDIEEAYAA------GKKLCELSICG--FPYTIDFNAMTQYNQATGTTRKV 63

                           90
                   ....*....|
gi 111306785   467 cRRPKYVSPQ 476
Cdd:smart00678  64 -RRVTYSPYS 72
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 309-382 3.80e-06

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 45.02  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785   309 YRWQFLD-GGKWKDLD--NMELIEEAY--SNPSKDRIV----YTesaagfhfdnLDFNSMKFGNTLARRLSTASSVTKPP 379
Cdd:smart00678   1 YVWEYEGrNGKWWPYDprVSEDIEEAYaaGKKLCELSIcgfpYT----------IDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 111306785   380 HFI 382
Cdd:smart00678  71 YSK 73
ZnF_C3H1 smart00356
zinc finger;
186-208 2.68e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|...
gi 111306785   186 KLHICQYFLQGECKFGTSCKRSH 208
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAH 25
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 571-687 3.68e-57

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 189.84  E-value: 3.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 571 QLFHGTSANFVDAICQQNFDWRVCGLHGTSYGKGSYFARDAAYSHHYSKSDTHS---HMMFLARVLVGDFVRGSTSFVRP 647
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKAdglKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 111306785 648 PAK-EGQSNAFYDSCVNSMSDPTIFVVFEKHQVYPEYLIQY 687
Cdd:cd01439   81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 517-689 7.76e-44

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 156.34  E-value: 7.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  517 SEEYQKVWNIFNRTLP-----FYFVQKIERIQNMGLWEVYQWQKCQMqkqnggkevDERQLFHGTSANFVDAICQQNF-- 589
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR---------NRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  590 DWRVCGLHGTSYGKGSYFARDAAYSHHYSKS--DTHSHMMFLARVLVGD------------------FVRGSTSFVR--- 646
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPseAHGNGLMLLSEVALGDmnelkkadyaeklppgkhSVKGLGKTAPesf 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 111306785  647 -----PPAKEGQSNaFYDSCVnsmSDPTIFVVFEKHQVYPEYLIQYST 689
Cdd:pfam00644 152 vdldgVPLGKLVAT-GYDSSV---LLYNEYVVYNVNQVRPKYLLEVKF 195
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 388-468 3.32e-13

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 65.01  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785  388 IWYWMDEFGSWQEYGRQgsghpvttiSSSDVERAYLAfcapgaDAQAATLKFQAGKHNYELHFKAFLQKNLVYGTIRKVC 467
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPE---------VSSLIEEAYQK------GKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65


                  .
gi 111306785  468 R 468
Cdd:pfam02825  66 R 66
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 387-476 1.70e-11

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 60.05  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785   387 WIWYWMDEFGSWqeygrqgsgHPVTTISSSDVERAYLAfcapgaDAQAATLKFQAgkHNYELHFKAFLQKNLVYGTIRKV 466
Cdd:smart00678   1 YVWEYEGRNGKW---------WPYDPRVSEDIEEAYAA------GKKLCELSICG--FPYTIDFNAMTQYNQATGTTRKV 63

                           90
                   ....*....|
gi 111306785   467 cRRPKYVSPQ 476
Cdd:smart00678  64 -RRVTYSPYS 72
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 526-687 1.05e-09

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 59.14  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 526 IFNRtlpfYFVQKIERIQNMGLWEVYQWQKCQMQKQNGgKEVDERQLFHGTSanFVDAICQQNFDWRVCGLHGTsYGKGS 605
Cdd:cd01438   51 IFNR----YNIIRIQKVVNKKLRERYCHRQKEIAEENH-NHHNERMLFHGSP--FINAIIHKGFDERHAYIGGM-FGAGI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 606 YFARDAAYSHHY-------SKSDTH--------SHMMFLARVLVGDFVRGSTSFVRPPAKEGQSNAFYDSCVNSMSDPTi 670
Cdd:cd01438  123 YFAENSSKSNQYvygigggTGCPTHkdrscyvcHRQMLFCRVTLGKSFLQFSAMKMAHAPPGHHSVIGRPSVNGLAYAE- 201

                        170
                 ....*....|....*..
gi 111306785 671 FVVFEKHQVYPEYLIQY 687
Cdd:cd01438  202 YVIYRGEQAYPEYLITY 218
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 572-683 1.06e-07

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 51.41  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785 572 LFHGTSANFVDAICQQNFDWRVCG--LHGTSYGKGSYFARDAAYSHHYSK--SDTHS--------------HMMFLARVL 633
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPASYGvlLNGGMFGKGIYSAPNISKSNGYSVgcDGQHVfqngkpkvcgrelcVFGFLTLGV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 111306785 634 VgDFVRGSTSFVRPPAKEGQSNAF--YDSCVNSMSD----PTIFVVFEKH-QVYPEY 683
Cdd:cd01341   82 M-SGATEESSRVLFPRNFRGATGAevVDLLVAMCRDalllPREYIIFEPYsQVSIRY 137
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 309-382 3.80e-06

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 45.02  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111306785   309 YRWQFLD-GGKWKDLD--NMELIEEAY--SNPSKDRIV----YTesaagfhfdnLDFNSMKFGNTLARRLSTASSVTKPP 379
Cdd:smart00678   1 YVWEYEGrNGKWWPYDprVSEDIEEAYaaGKKLCELSIcgfpYT----------IDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 111306785   380 HFI 382
Cdd:smart00678  71 YSK 73
ZnF_C3H1 smart00356
zinc finger;
186-208 2.68e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|...
gi 111306785   186 KLHICQYFLQGECKFGTSCKRSH 208
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAH 25
 
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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