NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|302566226]
View 

Chain A, SEX4 glucan phosphatase

Protein Classification

dual specificity protein phosphatase family protein; protein-tyrosine phosphatase family protein( domain architecture ID 12998398)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases; protein-tyrosine phosphatase family protein, similar to Saccharomyces cerevisiae OCA6 that is required for replication of Brome mosaic virus, but may be inactive as a protein-tyrosine phosphatase as it lacks the CxxxxxR catalytic motif

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 12-158 7.93e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


:

Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 227.85  E-value: 7.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  12 NYNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDISSIQAYAKKySDIQHIRCEIRDFDAFDLR*RL 91
Cdd:cd14526    2 NYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKE-SGIRYVRLPIRDFDTEDLRQKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302566226  92 PAVVGTLYKAVKrNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCFPKLDAIRN 158
Cdd:cd14526   81 PQAVALLYRLLK-NGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 171-252 9.91e-21

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


:

Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 84.19  E-value: 9.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226 171 TVTLTLKDKGFSRVEISGLDIGWGQRIPLTLgKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIgPNKDGHTNNYA 250
Cdd:cd02859    1 PVTFRWPGPGGKEVYVTGSFDNWQQPIPLEK-SGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTV-TDEFGNLNNVL 78


                 ..
gi 302566226 251 KV 252
Cdd:cd02859   79 EV 80
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 12-158 7.93e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 227.85  E-value: 7.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  12 NYNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDISSIQAYAKKySDIQHIRCEIRDFDAFDLR*RL 91
Cdd:cd14526    2 NYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKE-SGIRYVRLPIRDFDTEDLRQKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302566226  92 PAVVGTLYKAVKrNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCFPKLDAIRN 158
Cdd:cd14526   81 PQAVALLYRLLK-NGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 171-252 9.91e-21

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 84.19  E-value: 9.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226 171 TVTLTLKDKGFSRVEISGLDIGWGQRIPLTLgKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIgPNKDGHTNNYA 250
Cdd:cd02859    1 PVTFRWPGPGGKEVYVTGSFDNWQQPIPLEK-SGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTV-TDEFGNLNNVL 78


                 ..
gi 302566226 251 KV 252
Cdd:cd02859   79 EV 80
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 184-256 7.04e-17

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 73.72  E-value: 7.04e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302566226  184 VEISGLDIGWGQRIPLTlgKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIgPNKDGHTNNYAKVVDDP 256
Cdd:pfam16561  14 VYVTGSFDNWKKKIPLQ--KSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTA-TDDMGNLNNYIEVKASD 83
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
16-150 3.30e-10

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 57.29  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226    16 IRPDLIVGSClQTPEDVDKLRKIGVKTIFCLQQDpdleyfgvdissiqAYAKKYSDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:smart00195   4 ILPHLYLGSY-SDALNLALLKKLGITHVINVTNE--------------VPNYNGSDFTYLGVPIDDNTETKISPYFPEAV 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 302566226    96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCF 150
Cdd:smart00195  69 EFIEDAESKGGKV-LVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPII 122
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
16-149 2.17e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.98  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  16 IRPDLIVGSCLQTPEDVDkLRKIGVKTIFCLqqdpdLEYFGVDISSIQAYakkysDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:COG2453    3 IIPGLLAGGPLPGGGEAD-LKREGIDAVVSL-----TEEEELLLGLLEEA-----GLEYLHLPIPDFGAPDDE-QLQEAV 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302566226  96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWvQGYKL*EAHKLL*SKRSC 149
Cdd:COG2453   71 DFIDEALREGKKV-LVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPG 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 67-150 2.21e-09

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 54.58  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226   67 KKYSDIQHIRCEIRDFDAFDLR*RLPAVVGTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SK 146
Cdd:pfam00782  31 LYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKV-LVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKER 109


                  ....
gi 302566226  147 RSCF 150
Cdd:pfam00782 110 RPGI 113
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 12-158 7.93e-76

dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain.


Pssm-ID: 350375 [Multi-domain]  Cd Length: 146  Bit Score: 227.85  E-value: 7.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  12 NYNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDISSIQAYAKKySDIQHIRCEIRDFDAFDLR*RL 91
Cdd:cd14526    2 NYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKE-SGIRYVRLPIRDFDTEDLRQKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302566226  92 PAVVGTLYKAVKrNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCFPKLDAIRN 158
Cdd:cd14526   81 PQAVALLYRLLK-NGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 171-252 9.91e-21

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 84.19  E-value: 9.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226 171 TVTLTLKDKGFSRVEISGLDIGWGQRIPLTLgKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIgPNKDGHTNNYA 250
Cdd:cd02859    1 PVTFRWPGPGGKEVYVTGSFDNWQQPIPLEK-SGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTV-TDEFGNLNNVL 78


                 ..
gi 302566226 251 KV 252
Cdd:cd02859   79 EV 80
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 14-149 5.77e-19

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 81.05  E-value: 5.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  14 NFIRPDLIVGSCLQTpEDVDKLRKIGVKTIFCLQQDPDLEYFGvdissiqayakkySDIQHIRCEIRDFDAFDLR*RLPA 93
Cdd:cd14498    2 SEILPGLYLGSLDAA-QDKELLKKLGITHILNVAGEPPPNKFP-------------DGIKYLRIPIEDSPDEDILSHFEE 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302566226  94 VVGTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSC 149
Cdd:cd14498   68 AIEFIEEALKKGGKV-LVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPI 122
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 184-256 7.04e-17

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 73.72  E-value: 7.04e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302566226  184 VEISGLDIGWGQRIPLTlgKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIgPNKDGHTNNYAKVVDDP 256
Cdd:pfam16561  14 VYVTGSFDNWKKKIPLQ--KSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTA-TDDMGNLNNYIEVKASD 83
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
16-150 3.30e-10

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 57.29  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226    16 IRPDLIVGSClQTPEDVDKLRKIGVKTIFCLQQDpdleyfgvdissiqAYAKKYSDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:smart00195   4 ILPHLYLGSY-SDALNLALLKKLGITHVINVTNE--------------VPNYNGSDFTYLGVPIDDNTETKISPYFPEAV 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 302566226    96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCF 150
Cdd:smart00195  69 EFIEDAESKGGKV-LVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPII 122
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
16-149 2.17e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.98  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  16 IRPDLIVGSCLQTPEDVDkLRKIGVKTIFCLqqdpdLEYFGVDISSIQAYakkysDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:COG2453    3 IIPGLLAGGPLPGGGEAD-LKREGIDAVVSL-----TEEEELLLGLLEEA-----GLEYLHLPIPDFGAPDDE-QLQEAV 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302566226  96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWvQGYKL*EAHKLL*SKRSC 149
Cdd:COG2453   71 DFIDEALREGKKV-LVHCRGGIGRTGTVAAAYLVL-LGLSAEEALARVRAARPG 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 67-150 2.21e-09

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 54.58  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226   67 KKYSDIQHIRCEIRDFDAFDLR*RLPAVVGTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SK 146
Cdd:pfam00782  31 LYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKV-LVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKER 109


                  ....
gi 302566226  147 RSCF 150
Cdd:pfam00782 110 RPGI 113
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 16-149 5.60e-07

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 47.93  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  16 IRPDLIVGSCLQTpeDVDKLRKIGVKTIF-CLQQDPDLEYfgvdissiqayakkySDIQHIRCEIRDFDAFDLR*RLpAV 94
Cdd:cd14514    4 ITPHLFLSGASAA--TPPLLLSRGITCIInATTELPDPSY---------------PGIEYLRVPVEDSPHADLSPHF-DE 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 302566226  95 VGTLYKAVKRNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSC 149
Cdd:cd14514   66 VADKIHQVKRRGGRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPI 120
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
 172-253 5.07e-06

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199878 [Multi-domain]  Cd Length: 82  Bit Score: 43.69  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226 172 VTLTLKDKGFSRVEISGLDIGWGQRIPLTL-GKGTGFWILKRELPEGQFEYKYIIDGEWthNEAEPFIGPNKDGHTNNYA 250
Cdd:cd02688    2 VTFRIFAPGAKSVYLIGSFNGWWQAQALPMtKNGGGVWSATIPLPLGTYEYKYVIDGGK--NVLPYFDPYYVAGDGNSGA 79


                 ...
gi 302566226 251 KVV 253
Cdd:cd02688   80 SIV 82
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 13-148 3.86e-05

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 43.02  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  13 YNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGvdiSSIQAYAKkySDIQHIRCEIRDFDAFDLR*RLP 92
Cdd:cd14524    2 YDRIDDTVILGALPFRSMTVALVAKENVRGVITMNEEYETRFFC---NSKEEWKA--LGVEQLRLPTVDFTGVPSLEDLE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302566226  93 AVVGTLYKAVKRnGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRS 148
Cdd:cd14524   77 KGVDFILKHREK-GKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRP 131
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 101-154 1.40e-04

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 41.22  E-value: 1.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 302566226 101 AVKRNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSCF-PKLD 154
Cdd:cd14565   73 KVKASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVIsPNFN 127
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
 172-250 2.43e-04

N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199892 [Multi-domain]  Cd Length: 86  Bit Score: 39.15  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226 172 VTLTL-KDKGFSRVEISGlDI-GWG-QRIPLTLGKGTGFWIlKRELPEGQ-FEYKYIIDGE-WtHNEAEPfigpnkDGHT 246
Cdd:cd07184    3 VTFELpAEQGADSVSLVG-DFnDWDpQATPMKKLKNGTFSA-TLDLPAGReYQFRYLIDGErW-VNDPEA------DAYA 73


                 ....
gi 302566226 247 NNYA 250
Cdd:cd07184   74 PNGF 77
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 16-148 7.07e-04

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 39.00  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  16 IRPDLIVGSClQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGvdissiqayakkySDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:cd14512    4 ILPNLYLGSQ-RDSLNLELMQQLGIGYVLNVSNTCPNPDFI-------------GLFHYKRIPVNDSFCQNISPWFDEAI 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302566226  96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRS 148
Cdd:cd14512   70 EFIEEAKASNGGV-LVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRP 121
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 102-148 7.37e-04

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 39.13  E-value: 7.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 302566226 102 VKRNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRS 148
Cdd:cd14639   74 VRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRS 120
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 16-149 1.74e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 37.72  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  16 IRPDLIVGSClQTPEDVDKLRKIGVKTIFCLQqdpdleyFGVDissiQAYAkkySDIQHIRCEIRDFDAFDLR*RLPAVV 95
Cdd:cd14523    5 IKPWLLLSSQ-DVAHDLETLKKHKVTHILNVA-------YGVE----NAFP---DDFTYKTISILDLPETDITSYFPECF 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302566226  96 GTLYKAVKRNGGVtYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKLL*SKRSC 149
Cdd:cd14523   70 EFIDEAKSQDGVV-LVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARPS 122
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 28-124 3.31e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 37.63  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  28 TPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDiSSIQAYAKKysDIQHIRCEIRDFDAFDLR*RLPAVVGTLyKAVKRNGG 107
Cdd:cd14505   32 LQADLEELKDQGVDDVVTLCTDGELEELGVP-DLLEQYQQA--GITWHHLPIPDGGVPSDIAQWQELLEEL-LSALENGK 107

                         90
                 ....*....|....*..
gi 302566226 108 VTYVHSTAG*GRAPAVA 124
Cdd:cd14505  108 KVLIHCKGGLGRTGLIA 124
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 69-147 3.44e-03

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 37.46  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302566226  69 YSDIQHIRCEIRD------FDAFDlr*rlpaVVGTLYKAVKRNGGVTYVHSTAG*GRAPAVALTY*FWVQGYKL*EAHKL 142
Cdd:cd14573   43 PPGIEYLHVPVADspdtrlRDYFD-------PIADKIHTVEARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTW 115


                 ....*
gi 302566226 143 L*SKR 147
Cdd:cd14573  116 VKSCR 120
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH