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Conserved domains on  [gi|24586353|ref|NP_724597|]
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Gdap2, isoform C [Drosophila melanogaster]

Protein Classification

Macro_GDAP2_like and SEC14 domain-containing protein( domain architecture ID 10121093)

Macro_GDAP2_like and SEC14 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 67-234 6.03e-87

macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


:

Pssm-ID: 394876  Cd Length: 169  Bit Score: 265.64  E-value: 6.03e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  67 NRFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKeCRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:cd02905   1 RKIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG-CRTGEAKLTKGYNLPARYVIHTVGPR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 147 YREKFKTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKC--TLQVVILCVGSSER 224
Cdd:cd02905  80 YNEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHgsSFEAVVFVVTEEEM 159

                       170
                ....*....|
gi 24586353 225 GTYEVLAPLY 234
Cdd:cd02905 160 ETYERLLPLY 169
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 393-524 2.07e-32

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 121.28  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   393 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 468
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586353   469 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 524
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 67-234 6.03e-87

macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 265.64  E-value: 6.03e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  67 NRFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKeCRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:cd02905   1 RKIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG-CRTGEAKLTKGYNLPARYVIHTVGPR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 147 YREKFKTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKC--TLQVVILCVGSSER 224
Cdd:cd02905  80 YNEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHgsSFEAVVFVVTEEEM 159

                       170
                ....*....|
gi 24586353 225 GTYEVLAPLY 234
Cdd:cd02905 160 ETYERLLPLY 169
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 69-228 5.39e-38

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 137.23  E-value: 5.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  69 FVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVK--ECRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKqgGCPTGEAVITPAGNLPAKYVIHTVGPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 147 YREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKCTL--QVVILCVGSSER 224
Cdd:COG2110  81 WRGGGPSEEEL-LASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSleEVRFVLFDEEDY 159


                ....
gi 24586353 225 GTYE 228
Cdd:COG2110 160 EAYR 163
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 393-524 2.07e-32

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 121.28  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   393 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 468
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586353   469 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 524
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
PRK00431 PRK00431
ADP-ribose-binding protein;
68-229 8.80e-29

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 112.24  E-value: 8.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   68 RFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREE---LSTTVKECRTGDVRITRGYNLPAKYVLHTVA 144
Cdd:PRK00431   4 RIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEEcreLRQQQGPCPTGEAVITSAGRLPAKYVIHTVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  145 PAYREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDK-CTLQVVILCVGSSE 223
Cdd:PRK00431  84 PVWRGGEDNEAEL-LASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRhKSPEEVYFVCYDEE 162


                 ....*.
gi 24586353  224 rgTYEV 229
Cdd:PRK00431 163 --AYRL 166
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 86-199 1.23e-28

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 109.96  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353    86 NTSDETLTESNSISERIFAVAGNQLREELSTTVK-ECRTGDVRITRGYNLPAKYVLHTVAPAYREKFKTAAENTLHCCYR 164
Cdd:pfam01661   2 NAANSRLLGGGGVAGAIHRAAGPELLEECRELKKgGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCYR 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24586353   165 NVLCKAKELNLHTIALCNISAHQKSFPADVAAHIA 199
Cdd:pfam01661  82 NALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 372-517 3.55e-27

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 107.03  E-value: 3.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 372 VEDLTEVSGiGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIVKGDYVISYFHTL------TSTNNYP 445
Cdd:cd00170   1 LEELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586353 446 SLHWLREVYSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVHSLPG-VEHLYSAITKDQLEIP 517
Cdd:cd00170  80 DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 381-515 2.12e-20

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 88.13  E-value: 2.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353    381 IGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIV---KGDYVISYFHTLTSTNNYPSLH----WLREV 453
Cdd:smart00516   7 AYIPGGRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMSNpdlsVLRKI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586353    454 YSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVH--SLPGVEHLYSAITKDQLE 515
Cdd:smart00516  87 LKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRfvGNDSKEELLEYIDKEQLP 150
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 68-196 7.51e-16

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 74.26  E-value: 7.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353     68 RFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTV--KECRTGDVRITRGYNLPAKYVLHTVAP 145
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24586353    146 AYREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAA 196
Cdd:smart00506  81 RASGHSKEGFEL-LENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSA 130
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 67-234 6.03e-87

macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 265.64  E-value: 6.03e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  67 NRFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKeCRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:cd02905   1 RKIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG-CRTGEAKLTKGYNLPARYVIHTVGPR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 147 YREKFKTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKC--TLQVVILCVGSSER 224
Cdd:cd02905  80 YNEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHgsSFEAVVFVVTEEEM 159

                       170
                ....*....|
gi 24586353 225 GTYEVLAPLY 234
Cdd:cd02905 160 ETYERLLPLY 169
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 70-219 5.87e-44

macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 153.44  E-value: 5.87e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  70 VIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKECRTGDVRITRGYNLPAKYVLHTVAPAYRE 149
Cdd:cd02908   3 SLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVCPTGEAKITPGYNLPAKYVIHTVGPIGEG 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586353 150 KFKTAAEnTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKCT-LQVVILCV 219
Cdd:cd02908  83 GVEEEPE-LLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDkIDRIIFVV 152
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 69-228 5.39e-38

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 137.23  E-value: 5.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  69 FVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVK--ECRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKqgGCPTGEAVITPAGNLPAKYVIHTVGPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 147 YREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKCTL--QVVILCVGSSER 224
Cdd:COG2110  81 WRGGGPSEEEL-LASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSleEVRFVLFDEEDY 159


                ....
gi 24586353 225 GTYE 228
Cdd:COG2110 160 EAYR 163
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 393-524 2.07e-32

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 121.28  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   393 GRPVIVFCGKWFPAQNI---DLEKALLYLI-KLLDPIVKGDYVISYFHTLTSTNNYPSLHWLREVYSVLPYKYKKNLKAF 468
Cdd:pfam13716   1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLkTLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586353   469 YIVHPTFWTKMMTW-WFTTFMAPAIKAKVHSLPGVEHLYSAITKDQL--EIPaYITEYD 524
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYD 138
PRK00431 PRK00431
ADP-ribose-binding protein;
68-229 8.80e-29

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 112.24  E-value: 8.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   68 RFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREE---LSTTVKECRTGDVRITRGYNLPAKYVLHTVA 144
Cdd:PRK00431   4 RIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEEcreLRQQQGPCPTGEAVITSAGRLPAKYVIHTVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  145 PAYREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDK-CTLQVVILCVGSSE 223
Cdd:PRK00431  84 PVWRGGEDNEAEL-LASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRhKSPEEVYFVCYDEE 162


                 ....*.
gi 24586353  224 rgTYEV 229
Cdd:PRK00431 163 --AYRL 166
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
71-209 1.18e-28

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 114.69  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353   71 IWDGDMTTLEVDAITNTSDETLT-----ESNSISERIFAVAGNQLREELSTTVKEC----RTGDVRITRGYNLPAKYVLH 141
Cdd:PRK04143  87 LWQGDITRLKVDAIVNAANSRLLgcfqpNHDCIDNAIHTFAGVQLRLDCAEIMTEQgrkeATGQAKITRAYNLPAKYVIH 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24586353  142 TVAPA-YREKFKTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDK 209
Cdd:PRK04143 167 TVGPIiRKQPVSPIRADLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLKE 235
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 86-199 1.23e-28

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 109.96  E-value: 1.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353    86 NTSDETLTESNSISERIFAVAGNQLREELSTTVK-ECRTGDVRITRGYNLPAKYVLHTVAPAYREKFKTAAENTLHCCYR 164
Cdd:pfam01661   2 NAANSRLLGGGGVAGAIHRAAGPELLEECRELKKgGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCYR 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24586353   165 NVLCKAKELNLHTIALCNISAHQKSFPADVAAHIA 199
Cdd:pfam01661  82 NALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 372-517 3.55e-27

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 107.03  E-value: 3.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 372 VEDLTEVSGiGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIVKGDYVISYFHTL------TSTNNYP 445
Cdd:cd00170   1 LEELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586353 446 SLHWLREVYSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVHSLPG-VEHLYSAITKDQLEIP 517
Cdd:cd00170  80 DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 70-209 3.05e-26

macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394877 [Multi-domain]  Cd Length: 158  Bit Score: 104.49  E-value: 3.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  70 VIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKE---CRTGDVRITRGYNLPAKYVLHTVAPA 146
Cdd:cd02907   5 SVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKngkLRVGEVVVTSAGKLPCKYVIHAVGPR 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586353 147 YREKFKTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDK 209
Cdd:cd02907  85 WSGGSKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSES 147
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 381-515 2.12e-20

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 88.13  E-value: 2.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353    381 IGCLYQSGVDRLGRPVIVFCGKWFPAQNIDLEKALLYLIKLLDPIV---KGDYVISYFHTLTSTNNYPSLH----WLREV 453
Cdd:smart00516   7 AYIPGGRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMSNpdlsVLRKI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586353    454 YSVLPYKYKKNLKAFYIVHPTFWTKMMTWWFTTFMAPAIKAKVH--SLPGVEHLYSAITKDQLE 515
Cdd:smart00516  87 LKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRfvGNDSKEELLEYIDKEQLP 150
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 74-209 3.25e-19

macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 85.00  E-value: 3.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  74 GDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKECRTGDVRITRGYNLPAKYVLHTVAPAYREKFKT 153
Cdd:cd02903  15 GDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKYVYHVVLPHYNPGNEK 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24586353 154 AAENTLhccyRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDK 209
Cdd:cd02903  95 TLKDIV----RKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSK 146
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 82-202 1.25e-18

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 81.68  E-value: 1.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  82 DAITNTSDETLTESNSISERIFAVAGNQLREELSTTVK--ECRTGDVRITRGYNLPAKYVLHTVAPAYREkfKTAAENTL 159
Cdd:cd02749   1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKngYLKVGEVAVTKGGNLPARYIIHVVGPVASS--KKKTYEPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24586353 160 HCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRT 202
Cdd:cd02749  79 KKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 74-206 5.74e-16

macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 76.20  E-value: 5.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  74 GDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKE---CRTGDVRITRGYNLPAKYVLHTVAPAYREk 150
Cdd:cd02904  25 GDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSngpLEVAGAAISPGHNLPAKFVIHCNSPSWGS- 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24586353 151 fkTAAENTLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRY 206
Cdd:cd02904 104 --DKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNY 157
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 68-196 7.51e-16

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 74.26  E-value: 7.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353     68 RFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTV--KECRTGDVRITRGYNLPAKYVLHTVAP 145
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24586353    146 AYREKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAA 196
Cdd:smart00506  81 RASGHSKEGFEL-LENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSA 130
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 68-214 1.64e-14

Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132.


Pssm-ID: 394879  Cd Length: 147  Bit Score: 70.93  E-value: 1.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353  68 RFVIWDGDMTTLEVDAITNTSDETLTESNSISERIFAVAGNQLREELSTTVKeCRTGDVRITRGYNLPAKYVLHtvAPAY 147
Cdd:cd03330   1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGP-IRVGEAVETGAGKLPAKYVIH--AAVM 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24586353 148 REKFKTAAENtLHCCYRNVLCKAKELNLHTIALCNISAHQKSFPADVAAHIALRTIRRYLDKCTLQV 214
Cdd:cd03330  78 GMPGRSSEES-IRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPPLLEEV 143
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 102-214 4.11e-03

X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The X-domain, also called Mac1, is the macrodomain found in riboviral non-structural protein 3 (Nsp3), including the Nsp3 of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) as well as SARS-CoV-2, and other coronaviruses (alpha-, beta-, gamma-, and deltacoronavirus), among others. The SARS-CoV-2 Nsp3 Mac1 is highly conserved among all CoVs, and binds to and hydrolyzes mono-ADP-ribose (MAR) from target proteins. It appears to counter host-mediated antiviral ADP-ribosylation, a post-translational modification that is part of the host response to viral infections. Mac1 is essential for pathogenesis in multiple animal models of CoV infection, implicating it as a virulence factor and potential therapeutic target. Assays show that the de-MARylating activity leads to a rapid loss of substrate, and that Mac1 could not hydrolyze poly-ADP-ribose; thus, Mac1 is a MAR-hydrolase (mono-ADP ribosylhydrolase). Mac1 was originally named ADP-ribose-1"-phosphatase (ADRP) based on data demonstrating that it could remove the phosphate group from ADP-ribose-1"-phosphate; however, activity was modest and was unclear why this would impact a virus infection. This family also includes the X-domain of Avian infectious bronchitis virus (IBV) strain Beaudette coronavirus that does not bind ADP-ribose; the triple glycine sequence found in the X-domains of SARS-CoV and human coronavirus 229E (HCoV229E), which are involved in ADP-ribose binding, is not conserved in the IBV X-domain. SARS-CoVs have two other macrodomains referred to as the SUD-N (N-terminal subdomain, or Mac2) and SUD-M (middle SUD subdomain, or Mac3) of the SARS-unique domain (SUD), which also do not bind ADP-ribose; these bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). SARS-CoV SUD-N and SUD-M are not included in this group.


Pssm-ID: 438957  Cd Length: 127  Bit Score: 37.53  E-value: 4.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586353 102 IFAVAGNQLREELS--TTVKECRTGDVRITRGYNLpAKYVLHTVAPAYRekfKTAAENTLHCCYRNVLckakeLNLHTIA 179
Cdd:cd21557  22 IYKATGGAFQKESDyiKKNGPLKVGTAVLLPGHGL-AKNIIHVVGPRKR---KGQDDQLLAAAYKAVN-----KEYGSVL 92

                        90       100       110
                ....*....|....*....|....*....|....*
gi 24586353 180 LCNISAHQKSFPADVAAHIALRTIRRYLDKCTLQV 214
Cdd:cd21557  93 TPLLSAGIFGVPPEQSLNALLDAVDTTDADVTVYC 127
 
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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