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Conserved domains on  [gi|22749259|ref|NP_689828|]
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protein mono-ADP-ribosyltransferase PARP15 isoform 2 [Homo sapiens]

Protein Classification

macro domain-containing protein( domain architecture ID 10121076)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 63-229 3.16e-70

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: 219.82  E-value: 3.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  63 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 141
Cdd:cd02903   1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 142 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 214
Cdd:cd02903  81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                       170
                ....*....|....*
gi 22749259 215 QPELLNIFYDSMKKR 229
Cdd:cd02903 161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 322-442 1.77e-59

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: 190.22  E-value: 1.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 322 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 401
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22749259 402 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 442
Cdd:cd01439  81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 63-229 3.16e-70

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: 219.82  E-value: 3.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  63 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 141
Cdd:cd02903   1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 142 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 214
Cdd:cd02903  81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                       170
                ....*....|....*
gi 22749259 215 QPELLNIFYDSMKKR 229
Cdd:cd02903 161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 322-442 1.77e-59

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: 190.22  E-value: 1.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 322 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 401
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22749259 402 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 442
Cdd:cd01439  81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 271-442 1.74e-26

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: 105.49  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   271 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 343
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   344 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 404
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 22749259   405 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 442
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 72-228 1.09e-25

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: 102.56  E-value: 1.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  72 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 146
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 147 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPEL 218
Cdd:COG2110  81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEED 158

                       170
                ....*....|
gi 22749259 219 LNIFYDSMKK 228
Cdd:COG2110 159 YEAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 72-188 1.63e-19

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: 84.28  E-value: 1.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259     72 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 147
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 22749259    148 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 188
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
PRK00431 PRK00431
ADP-ribose-binding protein;
68-222 5.10e-15

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 72.95  E-value: 5.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   68 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 143
Cdd:PRK00431   1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  144 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVI 213
Cdd:PRK00431  81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVC 158


                 ....*....
gi 22749259  214 FQPELLNIF 222
Cdd:PRK00431 159 YDEEAYRLY 167
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 88-180 4.35e-10

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: 56.80  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259    88 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 154
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 22749259   155 TSVLEECEQRKYTSVSLPAIGTGNAG 180
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 63-229 3.16e-70

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: 219.82  E-value: 3.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  63 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 141
Cdd:cd02903   1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 142 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 214
Cdd:cd02903  81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                       170
                ....*....|....*
gi 22749259 215 QPELLNIFYDSMKKR 229
Cdd:cd02903 161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 322-442 1.77e-59

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: 190.22  E-value: 1.77e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 322 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 401
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22749259 402 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 442
Cdd:cd01439  81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 70-207 6.93e-31

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: 116.44  E-value: 6.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  70 ITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESEC-AVLAAQ---PHRDFIITPGGCLKCKIIIHV- 144
Cdd:cd02907   2 IKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECdKYIKKNgklRVGEVVVTSAGKLPCKYVIHAv 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22749259 145 -P---GGKD------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLK 207
Cdd:cd02907  82 gPrwsGGSKeecedlLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLK 154
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 271-442 1.74e-26

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: 105.49  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   271 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 343
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   344 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 404
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 22749259   405 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 442
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 72-228 1.09e-25

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: 102.56  E-value: 1.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  72 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 146
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 147 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPEL 218
Cdd:COG2110  81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEED 158

                       170
                ....*....|
gi 22749259 219 LNIFYDSMKK 228
Cdd:COG2110 159 YEAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 72-188 1.63e-19

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: 84.28  E-value: 1.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259     72 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 147
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 22749259    148 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 188
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 85-193 4.14e-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: 79.75  E-value: 4.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  85 DVIVNSTARTFNRKSGVSRAILEGAGQAVESECA-VLAAQPHR--DFIITPGGCLKCKIIIHVPGGK---------DVRK 152
Cdd:cd02749   1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEeRKKNGYLKvgEVAVTKGGNLPARYIIHVVGPVasskkktyePLKK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22749259 153 TVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDA 193
Cdd:cd02749  81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 74-228 8.65e-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: 75.43  E-value: 8.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  74 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHV--PGG 147
Cdd:cd02904  22 VVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSngplEVAGAAISPGHNLPAKFVIHCnsPSW 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 148 KDVR------KTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNI 221
Cdd:cd02904 102 GSDKceelleKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVSVMSSSLKQIYFVLFDMESIGI 181


                ....*..
gi 22749259 222 FYDSMKK 228
Cdd:cd02904 182 YTSELAK 188
PRK00431 PRK00431
ADP-ribose-binding protein;
68-222 5.10e-15

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 72.95  E-value: 5.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   68 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 143
Cdd:PRK00431   1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  144 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVI 213
Cdd:PRK00431  81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVC 158


                 ....*....
gi 22749259  214 FQPELLNIF 222
Cdd:PRK00431 159 YDEEAYRLY 167
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 72-180 6.00e-15

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: 71.70  E-value: 6.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  72 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKD-- 149
Cdd:cd03330   2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHAAVMGMpg 81

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22749259 150 ------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAG 180
Cdd:cd03330  82 rsseesIRDATRNALAKAEELGLESVAFPAIGTGVGG 118
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 77-227 1.22e-14

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: 71.39  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  77 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ-PHRDFIITPGGCLKCKIIIHV--PGGKDV--- 150
Cdd:cd02908   7 GDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVcPTGEAKITPGYNLPAKYVIHTvgPIGEGGvee 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 151 -----RKTVTSVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFSSQHSTPSLktVKVVIFQPELLNIFYD 224
Cdd:cd02908  87 epellASCYRSSLELALENGLKSIAFPCISTGIYGY-PNEEAAEIaLNTVREWLEEHDKIDR--IIFVVFLDEDYKIYEE 163


                ...
gi 22749259 225 SMK 227
Cdd:cd02908 164 LLP 166
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 262-442 1.01e-10

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: 61.45  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 262 MVQLEPGQSEYNTIKDKFTRTC-------------SSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTd 328
Cdd:cd01438  18 LLDLAPDDKEYQSVEEEMQSTIrehrdggnaggifNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGS- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259 329 adsvPYVN---QHGFNRSCAGKNAVsYGKGTYFAVDASYSAKDTYSKPDSNG------------RKHMYVVRVltgvfTK 393
Cdd:cd01438  97 ----PFINaiiHKGFDERHAYIGGM-FGAGIYFAENSSKSNQYVYGIGGGTGcpthkdrscyvcHRQMLFCRV-----TL 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 22749259 394 GRAGLVTPPPKNPHNPTDlFDSVTNNTRSPKL----FVVFFDNQAYPEYLITF 442
Cdd:cd01438 167 GKSFLQFSAMKMAHAPPG-HHSVIGRPSVNGLayaeYVIYRGEQAYPEYLITY 218
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 88-180 4.35e-10

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: 56.80  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259    88 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 154
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 22749259   155 TSVLEECEQRKYTSVSLPAIGTGNAG 180
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 77-180 1.83e-08

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: 53.78  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  77 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVT- 155
Cdd:cd02905   8 GDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNEKYRTa 87

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22749259 156 ----------SVLEECEQRKYTSVSLPAIGTGNAG 180
Cdd:cd02905  88 aesalyscyrNVLQLAKEHKLRSVAFPVIHSERRG 122
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
77-222 4.35e-05

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 44.97  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259   77 GDIATEQVDVIVNSTARTF------NRKSgVSRAILEGAGQAVESECAVL-AAQPHRDFI----ITPGGCLKCKIIIHVP 145
Cdd:PRK04143  90 GDITRLKVDAIVNAANSRLlgcfqpNHDC-IDNAIHTFAGVQLRLDCAEImTEQGRKEATgqakITRAYNLPAKYVIHTV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749259  146 GGKDVRKTVT------------SVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFssQHSTPSLKTVKVV 212
Cdd:PRK04143 169 GPIIRKQPVSpiradllascyrSCLKLAEKAGLKSIAFCCISTGVFGF-PKEEAAEIaIKTVLSW--LKENPSKLKVVFN 245

                        170
                 ....*....|
gi 22749259  213 IFQPELLNIF 222
Cdd:PRK04143 246 VFTDEDLELY 255
 
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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