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Conserved domains on  [gi|18395843|ref|NP_566139|]
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uncharacterized protein AT3G01510 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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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 ...
 290-435 2.88e-68

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: 217.83  E-value: 2.88e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 290 MRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKL 369
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQKL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395843 370 PLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAW 435
Cdd:cd14526  81 PQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 456-536 1.30e-28

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: 108.84  E-value: 1.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 456 SVTFVWNGHEGEEVLLVGDFTgNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIV 535
Cdd:cd02859   1 PVTFRWPGPGGKEVYVTGSFD-NWQQPIPLEKSGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLE 79


                .
gi 18395843 536 V 536
Cdd:cd02859  80 V 80
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 78-120 1.71e-03

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


The actual alignment was detected with superfamily member cd00136:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 81  Bit Score: 37.52  E-value: 1.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18395843  78 MVTLEK----PLGIRFALSADGK--IFVHAIKKGSNAEKARIIMVGDTL 120
Cdd:cd00136   1 TVTLEKdpggGLGFSIRGGKDGGggIFVSRVEPGGPAARDGRLRVGDRI 49
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 290-435 2.88e-68

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: 217.83  E-value: 2.88e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 290 MRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKL 369
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQKL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395843 370 PLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAW 435
Cdd:cd14526  81 PQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 456-536 1.30e-28

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: 108.84  E-value: 1.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 456 SVTFVWNGHEGEEVLLVGDFTgNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIV 535
Cdd:cd02859   1 PVTFRWPGPGGKEVYVTGSFD-NWQQPIPLEKSGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLE 79


                .
gi 18395843 536 V 536
Cdd:cd02859  80 V 80
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 457-536 1.65e-21

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: 88.74  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843   457 VTFVWNgHEGEEVLLVGDFTgNWKEPIKaTHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVV 536
Cdd:pfam16561   3 TVITWR-GGGKKVYVTGSFD-NWKKKIP-LQKSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEV 79
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
293-420 1.73e-11

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 61.91  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843    293 SKITEQIYVGSCIqTEEDVENLSEAGITAILNFQggteaqnwgidsqSINDACQKSEVLMINYPIKDADSFDLRKKLPLC 372
Cdd:smart00195   2 SEILPHLYLGSYS-DALNLALLKKLGITHVINVT-------------NEVPNYNGSDFTYLGVPIDDNTETKISPYFPEA 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 18395843    373 VGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:smart00195  68 VEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFV 115
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 78-120 1.71e-03

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 37.52  E-value: 1.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18395843  78 MVTLEK----PLGIRFALSADGK--IFVHAIKKGSNAEKARIIMVGDTL 120
Cdd:cd00136   1 TVTLEKdpggGLGFSIRGGKDGGggIFVSRVEPGGPAARDGRLRVGDRI 49
 
Name Accession Description Interval E-value
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 290-435 2.88e-68

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: 217.83  E-value: 2.88e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 290 MRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKL 369
Cdd:cd14526   1 LNYSRILPNLIVGSCPQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDSIRKACKESGIRYVRLPIRDFDTEDLRQKL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395843 370 PLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAW 435
Cdd:cd14526  81 PQAVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDEEAIRG 146
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 456-536 1.30e-28

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: 108.84  E-value: 1.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 456 SVTFVWNGHEGEEVLLVGDFTgNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIV 535
Cdd:cd02859   1 PVTFRWPGPGGKEVYVTGSFD-NWQQPIPLEKSGDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLE 79


                .
gi 18395843 536 V 536
Cdd:cd02859  80 V 80
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 457-536 1.65e-21

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: 88.74  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843   457 VTFVWNgHEGEEVLLVGDFTgNWKEPIKaTHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVV 536
Cdd:pfam16561   3 TVITWR-GGGKKVYVTGSFD-NWKKKIP-LQKSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEV 79
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 293-420 3.82e-17

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: 77.97  E-value: 3.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 293 SKITEQIYVGSCIQTEeDVENLSEAGITAILNFQGGTEAQNwgidsqsindacQKSEVLMINYPIKDADSFDLRKKLPLC 372
Cdd:cd14498   2 SEILPGLYLGSLDAAQ-DKELLKKLGITHILNVAGEPPPNK------------FPDGIKYLRIPIEDSPDEDILSHFEEA 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18395843 373 VGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:cd14498  69 IEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELV 116
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
293-420 1.73e-11

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 61.91  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843    293 SKITEQIYVGSCIqTEEDVENLSEAGITAILNFQggteaqnwgidsqSINDACQKSEVLMINYPIKDADSFDLRKKLPLC 372
Cdd:smart00195   2 SEILPHLYLGSYS-DALNLALLKKLGITHVINVT-------------NEVPNYNGSDFTYLGVPIDDNTETKISPYFPEA 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 18395843    373 VGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:smart00195  68 VEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFV 115
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 294-434 1.65e-07

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: 50.56  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGSCiQTEEDVENLSEAGITAILNFqggteaqnwgidSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCV 373
Cdd:cd14512   3 RILPNLYLGSQ-RDSLNLELMQQLGIGYVLNV------------SNTCPNPDFIGLFHYKRIPVNDSFCQNISPWFDEAI 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395843 374 GLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAIA 434
Cdd:cd14512  70 EFIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFV------KEKRPTIS 124
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
 456-534 3.29e-07

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: 48.31  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 456 SVTFVWNGHEGEEVLLVGDFTGNWKE-PIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRH--SATSPTERDDRGNTNN 532
Cdd:cd02688   1 GVTFRIFAPGAKSVYLIGSFNGWWQAqALPMTKNGGGVWSATIPLPLGTYEYKYVIDGGKNVlpYFDPYYVAGDGNSGAS 80


                ..
gi 18395843 533 II 534
Cdd:cd02688  81 IV 82
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 294-429 4.38e-07

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP12 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. It targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 49.56  E-value: 4.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGScIQTEEDVENLSEAGITAILNfqggteaqnwgIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCV 373
Cdd:cd14520   3 LVRPGLYIGN-ADDAADYLSLREAGITHVLT-----------VDSEEPIDAPPVGKLVRKFVPALDEESTDLLSRLDECL 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18395843 374 GLLLRLLKKNhRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSfvtGLHACKPD 429
Cdd:cd14520  71 DFIDEGRAEG-AVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALA---SLRECKPD 122
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 293-434 1.50e-05

dual specificity phosphatase domain of class III 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 III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. 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: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 45.10  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 293 SKITEQIYVGSciqtEEDVEN---LSEAGITAILNfqggteaqnwgidsqsINDACQKSEVL-MINY---PIKDADSFDL 365
Cdd:cd14568   2 TRILPHLYLGS----QRDVLDkdlMQRNGISYVLN----------------VSNTCPKPDFIpDSHFlriPVNDSYCEKL 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395843 366 RKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAIA 434
Cdd:cd14568  62 LPWLDKAVEFIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFV------KEKRPTIS 124
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 299-434 1.68e-05

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: 44.69  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 299 IYVGSCIQTEeDVENLSEAGITAILNFqggteaqnwgidSQSINDACQKSevlmINY---PIKDADSFDLRKKLPLCVGL 375
Cdd:cd14565   8 LYLGSAYHAS-RREVLKALGITAVLNV------------SRNCPNHFEDH----FQYksiPVEDSHNADISSWFEEAIGF 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18395843 376 LLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAIA 434
Cdd:cd14565  71 IDKVKASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYV------KQRRSVIS 123
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
 457-536 1.42e-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: 40.69  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 457 VTFVWNGHEG-EEVLLVGDFTgNW---KEPIKATHKGGprFETEVRL-TQGKYYYKYIINGD-WRHSATSPTERDDRGNT 530
Cdd:cd07184   3 VTFELPAEQGaDSVSLVGDFN-DWdpqATPMKKLKNGT--FSATLDLpAGREYQFRYLIDGErWVNDPEADAYAPNGFGE 79


                ....*.
gi 18395843 531 NNIIVV 536
Cdd:cd07184  80 ENSVVS 85
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 294-429 1.91e-04

dual specificity phosphatase domain of class II 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 II MKPs consist of DUSP6/MKP-3, DUSP7/MKP-X and DUSP9/MKP-4, and are ERK-selective cytoplasmic 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: 350414 [Multi-domain]  Cd Length: 137  Bit Score: 41.92  E-value: 1.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGsCIQTEEDVENLSEAGITAILNFqggteaqnwgidSQSINDACQKSEVL-MINYPIKDADSFDLRKKLPLC 372
Cdd:cd14566   3 EILPFLYLG-NAKDSANIDLLKKYNIKYILNV------------TPNLPNTFEEDGGFkYLQIPIDDHWSQNLSAFFPEA 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18395843 373 VGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglHACKPD 429
Cdd:cd14566  70 ISFIDEARSKKCGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFV---KKRKSN 123
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 294-433 2.13e-04

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: 41.57  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGSCiQTEEDVENLSEAGITAILNFQggteaqnWGIDSQSINDACQKsevlmiNYPIKDADSFDLRKKLPLCV 373
Cdd:cd14523   4 VIKPWLLLSSQ-DVAHDLETLKKHKVTHILNVA-------YGVENAFPDDFTYK------TISILDLPETDITSYFPECF 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 374 GLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAI 433
Cdd:cd14523  70 EFIDEAKSQDGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLV------KNARPSI 123
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 293-434 2.63e-04

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 41.53  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 293 SKITEQIYVGScIQTEEDVENLSEAGITAILNFqggteaqnwgIDSQSINDACQKSEVLMInyPIKDADSFDLRKKLPLC 372
Cdd:cd14518   2 SRILGGLYLGG-IEPLNRNRLLKAENITHILSV----------IPGDVPEEYFKGYEHKQI--EIDDVEDENILQHFPET 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395843 373 V----------GLLLRLLKKNH-RVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAysfvtgLHACKPDRPAIA 434
Cdd:cd14518  69 NrfidsalfgnGKDEDEEKKHGgAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQA------LHAVRRKRPIAE 135
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 299-405 1.30e-03

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family 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. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 39.50  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 299 IYVGSCIqTEEDVENLSEAGITAILNfqggtEAQNWGIDSQSINDACQKSevLMINY---PIKDADSFDL---------- 365
Cdd:cd14515   8 IYIGDES-TAKNKAKLKKLGITHVLN-----AAEGKKNGEVNTNAKFYKG--SGIIYlgiPASDLPTFDIsqyfdeaadf 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18395843 366 -RKKLplcvglllrlLKKNHRVFVTCTTGFDRSSACVIAYL 405
Cdd:cd14515  80 iDKAL----------SDPGGKVLVHCVEGVSRSATLVLAYL 110
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 346-431 1.51e-03

dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine.


Pssm-ID: 350367 [Multi-domain]  Cd Length: 155  Bit Score: 39.57  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 346 QKSEVLMInyPIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglHA 425
Cdd:cd14517  55 GNDQVLHI--PVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYL---LK 129


                ....*..
gi 18395843 426 CKPD-RP 431
Cdd:cd14517 130 CKNNmRP 136
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 356-434 1.53e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other 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 III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 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: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 39.35  E-value: 1.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395843 356 PIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAIA 434
Cdd:cd14567  53 PATDSNKQNLRQYFEEAFEFIEEAHQSGKGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFV------KNKRPIIS 125
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 78-120 1.71e-03

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 37.52  E-value: 1.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18395843  78 MVTLEK----PLGIRFALSADGK--IFVHAIKKGSNAEKARIIMVGDTL 120
Cdd:cd00136   1 TVTLEKdpggGLGFSIRGGKDGGggIFVSRVEPGGPAARDGRLRVGDRI 49
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 294-420 2.04e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, 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. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 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: 350489 [Multi-domain]  Cd Length: 144  Bit Score: 39.08  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGSCIQTEeDVENLSEAGITAILNfqggteaqnwgIDSQSINdaCQKSEVLMINYPIKDADSFDLRKKLPLCV 373
Cdd:cd14641   6 EILPFLFLGSAHHSS-RRETLESLGITAVLN-----------VSSSCPN--YFEGQFQYKSIPVEDSHMADISAWFQEAI 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18395843 374 GLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:cd14641  72 DFIDSVKNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFV 118
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 289-426 2.15e-03

dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), also called JNK-stimulatory phosphatase-1 (JSP-1), low molecular weight dual specificity phosphatase 2 (LMW-DSP2), mitogen-activated protein kinase phosphatase x (MKP-x) or VHR-related MKPx (VHX), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP22 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. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. It also regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity.


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 39.01  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 289 GMrySKITEQIYVGScIQTEEDVENLSEAGITAILnfqggteaqnwgidsqSINDACQK--SEVLMINYPIKDADSFDLR 366
Cdd:cd14581   3 GM--NKVLPGLYLGN-FKDARDREQLSKNNITHIL----------------SVHDSARPmlEGMTYLCIPAADSPSQNLT 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 367 KKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHAC 426
Cdd:cd14581  64 QHFKESIKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARSC 123
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 294-420 2.62e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual specificity protein phosphatase 7 (DUSP7), also called mitogen-activated protein kinase (MAPK) phosphatase X (MKP-X) or dual specificity protein phosphatase PYST2, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other 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 II subfamily and is an ERK-selective cytoplasmic MKP. DUSP7 has been shown as an essential regulator of multiple steps in oocyte meiosis. Due to alternative promoter usage, the PYST2 gene gives rise to two isoforms, PYST2-S and PYST2-L. PYST2-L is over-expressed in leukocytes derived from AML and ALL patients as well as in some solid tumors and lymphoblastoid cell lines; it plays a role in cell-crowding. It 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: 350491 [Multi-domain]  Cd Length: 149  Bit Score: 38.85  E-value: 2.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGsCIQTEEDVENLSEAGITAILNfqggteaqnwgIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCV 373
Cdd:cd14643   8 QILPYLYLG-CAKDSTNLDVLGKYGIKYILN-----------VTPNLPNMFEHDGEFKYKQIPISDHWSQNLSQFFPEAI 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18395843 374 GLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:cd14643  76 SFIDEARSKKCGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFV 122
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 293-434 3.17e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other 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 III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 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: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 38.47  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 293 SKITEQIYVGsCIQTEEDVENLSEAGITAILNfqggteaqnwgidsqsINDACQK----SEVLMINYPIKDADSFDLRKK 368
Cdd:cd14646   4 TRILPHLYLG-CQRDVLNKELMQQNGIGYVLN----------------ASNTCPKpdfiPESHFLRVPVNDSFCEKILPW 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395843 369 LPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVtglhacKPDRPAIA 434
Cdd:cd14646  67 LDKSVDFIEKAKASNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFV------KEKRPTIS 126
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 292-433 3.27e-03

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: 37.92  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 292 YSKITEQIYVGSCIQTEEdvENLSEAGITAILNFqggteaqnwgidSQSINDaCQKSEVLMINYPIKDADSFDLRKKLPL 371
Cdd:cd14514   1 ISQITPHLFLSGASAATP--PLLLSRGITCIINA------------TTELPD-PSYPGIEYLRVPVEDSPHADLSPHFDE 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395843 372 CVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYL---HWMTdtsLHAAYSFVtglhacKPDRPAI 433
Cdd:cd14514  66 VADKIHQVKRRGGRTLVHCVAGVSRSATLCLAYLmkyEGMT---LREAYKHV------KAARPII 121
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 294-420 5.77e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual specificity protein phosphatase 9 (DUSP9), also called mitogen-activated protein kinase (MAPK) phosphatase 4 (MKP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other 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 II subfamily and is an ERK-selective cytoplasmic MKP. DUSP9 is a mediator of bone morphogenetic protein (BMP) signaling to control the appropriate ERK activity critical for the determination of embryonic stem cell fate. Down-regulation of DUSP9 expression has been linked to severe pre-eclamptic placenta as well as cancers such as hepatocellular carcinoma. DUSP9 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: 350492 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 5.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 294 KITEQIYVGsCIQTEEDVENLSEAGITAILNfqggteaqnwgIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCV 373
Cdd:cd14644   5 QILPNLYLG-SARDSANLETLAKLGIRYILN-----------VTPNLPNFFEKNGDFHYKQIPISDHWSQNLSQFFPEAI 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18395843 374 GLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFV 420
Cdd:cd14644  73 EFIDEALSQNCGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLV 119
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 292-405 7.34e-03

dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also called vaccinia H1-related phosphatase (VHR), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP3 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. It favors bisphosphorylated substrates over monophosphorylated ones, and prefers pTyr peptides over pSer/pThr peptides. Reported physiological substrates includes MAPKs ERK1/2, JNK, and p38, as well as STAT5, EGFR, and ErbB2. DUSP3 has been linked to breast and prostate cancer, and may also play a role in thrombosis.


Pssm-ID: 350427 [Multi-domain]  Cd Length: 168  Bit Score: 37.82  E-value: 7.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395843 292 YSKITEQIYVGSCIqTEEDVENLSEAGITAILNFQGG-------TEAQNW---GIDSQSINdACQKSEVLMINYpIKDAD 361
Cdd:cd14579  21 CNEVYPRIYVGNAS-VAQNIMRLQRLGITHVLNAAEGksfmhvnTNAEFYedtGITYHGIK-ANDTQHFNLSAY-FEEAA 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18395843 362 SFdLRKKLplcvglllrlLKKNHRVFVTCTTGFDRSSACVIAYL 405
Cdd:cd14579  98 DF-IDKAL----------AQKNGRVLVHCREGYSRSPTLVIAYL 130
 
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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