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Conserved domains on  [gi|568927210|ref|XP_006538234|]
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aprataxin isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
98-199 1.92e-47

aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin.


:

Pssm-ID: 238609 [Multi-domain]  Cd Length: 104  Bit Score: 153.70  E-value: 1.92e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  98 LGHWSQGLKMSMKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIADFAGSSK 177
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80
                         90       100
                 ....*....|....*....|....
gi 568927210 178 LRFRLGYHAIP--SMSHVHLHVIS 199
Cdd:cd01278   81 SEFRFGFHAPPftSVSHLHLHVIA 104
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
217-274 2.63e-17

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


:

Pssm-ID: 435254  Cd Length: 60  Bit Score: 73.86  E-value: 2.63e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927210  217 NTEYFLESQAVIKMVQEAGRVTVKDGTCELLKLPLRCHECQQLLPSIPQLKEHLRKHW 274
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHF 58
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
1-42 3.45e-17

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


The actual alignment was detected with superfamily member cd22735:

Pssm-ID: 444676  Cd Length: 100  Bit Score: 74.83  E-value: 3.45e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568927210   1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEE 42
Cdd:cd22735   59 LGVNPTSIDLVDIGKDEEVKLKPGQVLHIVNQLYPYIVEFEE 100
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
98-199 1.92e-47

aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin.


Pssm-ID: 238609 [Multi-domain]  Cd Length: 104  Bit Score: 153.70  E-value: 1.92e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  98 LGHWSQGLKMSMKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIADFAGSSK 177
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80
                         90       100
                 ....*....|....*....|....
gi 568927210 178 LRFRLGYHAIP--SMSHVHLHVIS 199
Cdd:cd01278   81 SEFRFGFHAPPftSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
109-212 1.39e-42

Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.


Pssm-ID: 432228 [Multi-domain]  Cd Length: 114  Bit Score: 141.59  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  109 MKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIAD-FAGSSKLRFRLGYHAI 187
Cdd:pfam11969  10 GEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLKHMREVAKKVIEEkYIGVDRDELRLGFHYP 89
                          90       100
                  ....*....|....*....|....*
gi 568927210  188 PSMSHVHLHVISQDFDSPCLKNKKH 212
Cdd:pfam11969  90 PSVYHLHLHVISPDFDSPGLGRKKH 114
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
217-274 2.63e-17

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


Pssm-ID: 435254  Cd Length: 60  Bit Score: 73.86  E-value: 2.63e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927210  217 NTEYFLESQAVIKMVQEAGRVTVKDGTCELLKLPLRCHECQQLLPSIPQLKEHLRKHW 274
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHF 58
FHA_APTX cd22735
forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1. ...
1-42 3.45e-17

forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). Mutations in the gene APTX have been associated with ataxia-ocular apraxia. Aprataxin contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438787  Cd Length: 100  Bit Score: 74.83  E-value: 3.45e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568927210   1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEE 42
Cdd:cd22735   59 LGVNPTSIDLVDIGKDEEVKLKPGQVLHIVNQLYPYIVEFEE 100
FHA_2 pfam17913
FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated ...
2-41 1.99e-09

FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated segment of XRCC1.


Pssm-ID: 436135  Cd Length: 97  Bit Score: 53.45  E-value: 1.99e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568927210    2 GVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFE 41
Cdd:pfam17913  58 GANPSGLNGFKLKKGESYELKHGDVLELLNGKHPHRVEFN 97
Hit COG0537
Diadenosine tetraphosphate (Ap4A) hydrolase or other HIT family hydrolase [Nucleotide ...
116-198 2.43e-08

Diadenosine tetraphosphate (Ap4A) hydrolase or other HIT family hydrolase [Nucleotide transport and metabolism, Carbohydrate transport and metabolism, General function prediction only];


Pssm-ID: 223611 [Multi-domain]  Cd Length: 138  Bit Score: 51.61  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210 116 VYKDDQVVVIKDKYPKARHHWLVLPWASISSLkvvTSEHLELLKHMHAVGEKV-----IADFAGSSKLRFRLGYHAIPSM 190
Cdd:COG0537   18 VYEDEHVLAFLDIYPAAPGHTLVIPKRHVSDL---EDLDPEELAELFLLAQKIakalkEAFGADGYNIGINNGKAAGQEV 94

                 ....*...
gi 568927210 191 SHVHLHVI 198
Cdd:COG0537   95 FHLHIHII 102
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
1-169 1.32e-04

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 43.09  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210    1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEEVAESPNltqrkrkrsdcdseEMEAESGTGLAPGSSPSQ 80
Cdd:TIGR01663  70 LGVNPCGTGGLELKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEP--------------EPDKEKAEPLSSQDEKRD 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210   81 CSVSPKKDKNGATKKESLGHW----SQGLKMSmkdPKMQVYKDDQvVVIKDK----YPKARHHWlvlpwasisslKVVTS 152
Cdd:TIGR01663 136 AEKPEKRDRKGNPGWENLEKLliftAAGVKGQ---EKIAGFDLDG-TIIKTKsgkvFPKGPDDW-----------QIIFP 200
                         170
                  ....*....|....*..
gi 568927210  153 EHLELLKHMHAVGEKVI 169
Cdd:TIGR01663 201 EIPEKLKELEADGFKIC 217
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
98-199 1.92e-47

aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin.


Pssm-ID: 238609 [Multi-domain]  Cd Length: 104  Bit Score: 153.70  E-value: 1.92e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  98 LGHWSQGLKMSMKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIADFAGSSK 177
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80
                         90       100
                 ....*....|....*....|....
gi 568927210 178 LRFRLGYHAIP--SMSHVHLHVIS 199
Cdd:cd01278   81 SEFRFGFHAPPftSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
109-212 1.39e-42

Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.


Pssm-ID: 432228 [Multi-domain]  Cd Length: 114  Bit Score: 141.59  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  109 MKDPKMQVYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHLELLKHMHAVGEKVIAD-FAGSSKLRFRLGYHAI 187
Cdd:pfam11969  10 GEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLKHMREVAKKVIEEkYIGVDRDELRLGFHYP 89
                          90       100
                  ....*....|....*....|....*
gi 568927210  188 PSMSHVHLHVISQDFDSPCLKNKKH 212
Cdd:pfam11969  90 PSVYHLHLHVISPDFDSPGLGRKKH 114
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
217-274 2.63e-17

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


Pssm-ID: 435254  Cd Length: 60  Bit Score: 73.86  E-value: 2.63e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927210  217 NTEYFLESQAVIKMVQEAGRVTVKDGTCELLKLPLRCHECQQLLPSIPQLKEHLRKHW 274
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHF 58
FHA_APTX cd22735
forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1. ...
1-42 3.45e-17

forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). Mutations in the gene APTX have been associated with ataxia-ocular apraxia. Aprataxin contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438787  Cd Length: 100  Bit Score: 74.83  E-value: 3.45e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568927210   1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEE 42
Cdd:cd22735   59 LGVNPTSIDLVDIGKDEEVKLKPGQVLHIVNQLYPYIVEFEE 100
FHA_APTX_PNKP cd22716
forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase ...
1-42 9.87e-10

forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase/kinase (PNKP), and similar proteins; The subfamily includes aprataxin and PNKP. Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. Both aprataxin and PNKP contain an FHA domain at their N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438768  Cd Length: 97  Bit Score: 54.59  E-value: 9.87e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568927210   1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEE 42
Cdd:cd22716   56 LGPNPSSVGGKLLEKGDEAELSPGETLHLLNGKYPHTVYFEG 97
FHA_2 pfam17913
FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated ...
2-41 1.99e-09

FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated segment of XRCC1.


Pssm-ID: 436135  Cd Length: 97  Bit Score: 53.45  E-value: 1.99e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568927210    2 GVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFE 41
Cdd:pfam17913  58 GANPSGLNGFKLKKGESYELKHGDVLELLNGKHPHRVEFN 97
HIT pfam01230
HIT domain;
116-203 4.32e-09

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 52.70  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210  116 VYKDDQVVVIKDKYPKARHHWLVLPWASISSLKVVTSEHL-ELLKHMHAVGEKVIADFAGSSklrFRL----GYHAIPSM 190
Cdd:pfam01230   9 VYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELgDLMSVAQKVARALGKVFKADG---YRIvinnGAHAGQSV 85
                          90
                  ....*....|...
gi 568927210  191 SHVHLHVISQDFD 203
Cdd:pfam01230  86 PHLHIHVIPRRKH 98
Hit COG0537
Diadenosine tetraphosphate (Ap4A) hydrolase or other HIT family hydrolase [Nucleotide ...
116-198 2.43e-08

Diadenosine tetraphosphate (Ap4A) hydrolase or other HIT family hydrolase [Nucleotide transport and metabolism, Carbohydrate transport and metabolism, General function prediction only];


Pssm-ID: 223611 [Multi-domain]  Cd Length: 138  Bit Score: 51.61  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210 116 VYKDDQVVVIKDKYPKARHHWLVLPWASISSLkvvTSEHLELLKHMHAVGEKV-----IADFAGSSKLRFRLGYHAIPSM 190
Cdd:COG0537   18 VYEDEHVLAFLDIYPAAPGHTLVIPKRHVSDL---EDLDPEELAELFLLAQKIakalkEAFGADGYNIGINNGKAAGQEV 94

                 ....*...
gi 568927210 191 SHVHLHVI 198
Cdd:COG0537   95 FHLHIHII 102
FHA_PNKP cd22736
forkhead associated (FHA) domain found in bifunctional polynucleotide phosphatase/kinase (PNKP) ...
1-42 8.95e-08

forkhead associated (FHA) domain found in bifunctional polynucleotide phosphatase/kinase (PNKP) and similar proteins; PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. PNKP contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438788  Cd Length: 99  Bit Score: 49.01  E-value: 8.95e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568927210   1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEE 42
Cdd:cd22736   58 LGVNPSSVGEQELKPGLSGSLKEGQTLYLVNGLYPLTLRFEE 99
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
116-198 6.19e-06

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


Pssm-ID: 238263 [Multi-domain]  Cd Length: 86  Bit Score: 43.61  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210 116 VYKDDQVVVIKDKYPKARHHWLVLPWASISSLkvvtSEHLE-LLKHMHAVGEKVIADFAGS---SKLRFRLGYHAIP--S 189
Cdd:cd00468    1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETL----PDLDEaLLADLVITAQRVAAELEKHgnvPSLTVFVNDGAAAgqS 76

                 ....*....
gi 568927210 190 MSHVHLHVI 198
Cdd:cd00468   77 VPHVHLHVL 85
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
1-169 1.32e-04

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 43.09  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210    1 MGVNPTSIDSGVIGKDQEKKLLPGQVLHMVNGLYPYIVEFEEVAESPNltqrkrkrsdcdseEMEAESGTGLAPGSSPSQ 80
Cdd:TIGR01663  70 LGVNPCGTGGLELKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEP--------------EPDKEKAEPLSSQDEKRD 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927210   81 CSVSPKKDKNGATKKESLGHW----SQGLKMSmkdPKMQVYKDDQvVVIKDK----YPKARHHWlvlpwasisslKVVTS 152
Cdd:TIGR01663 136 AEKPEKRDRKGNPGWENLEKLliftAAGVKGQ---EKIAGFDLDG-TIIKTKsgkvFPKGPDDW-----------QIIFP 200
                         170
                  ....*....|....*..
gi 568927210  153 EHLELLKHMHAVGEKVI 169
Cdd:TIGR01663 201 EIPEKLKELEADGFKIC 217
FHA_APTX-like cd22671
forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase ...
1-40 2.68e-04

forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase/kinase (PNKP), aprataxin and PNK-like factor (APLF), and similar proteins; The family includes aprataxin, PNKP, and APLF. Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. APLF, also called apurinic-apyrimidinic endonuclease APLF, PNK and APTX-like FHA domain-containing protein, or XRCC1-interacting protein 1 (XIP1), is a novel apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease with conserved zinc-finger-like motifs involved in single-strand and double-strand DNA break repair. It is recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. It can introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, APLF promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Members of this family contain an FHA domain at their N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438723 [Multi-domain]  Cd Length: 101  Bit Score: 39.22  E-value: 2.68e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568927210   1 MGVNPTSIDSG-----VIGKDQEKKLLPGQVLHMVNGLYPYIVEF 40
Cdd:cd22671   57 LGTNPSFVNRAdgegkVLKKGESVELKDGDVISLLPGKYPFRVEI 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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