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Conserved domains on  [gi|2220285855|ref|NP_001391082|]
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DSPc domain-containing protein [Caenorhabditis elegans]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12998007)

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

CATH:  3.90.190.10
EC:  3.1.3.16|3.1.3.48
Gene Ontology:  GO:0004721|GO:0006470|GO:0004722
PubMed:  19228121|31489884
SCOP:  3000304

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 186-349 1.64e-11

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: 61.41  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 186 QIDDVVFASAIDAVNNNSLMCRLNIEFICEIADEtadhvQEARRQNRGFEcpcfcnrssshfryYLSYSLPETEqrcmml 265
Cdd:cd14498     3 EILPGLYLGSLDAAQDKELLKKLGITHILNVAGE-----PPPNKFPDGIK--------------YLRIPIEDSP------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 266 teDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQR 345
Cdd:cd14498    58 --DEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSR----RPIISPNPGFLK 131


                  ....
gi 2220285855 346 KLMR 349
Cdd:cd14498   132 QLKE 135
 
Name Accession Description Interval E-value
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 186-349 1.64e-11

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: 61.41  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 186 QIDDVVFASAIDAVNNNSLMCRLNIEFICEIADEtadhvQEARRQNRGFEcpcfcnrssshfryYLSYSLPETEqrcmml 265
Cdd:cd14498     3 EILPGLYLGSLDAAQDKELLKKLGITHILNVAGE-----PPPNKFPDGIK--------------YLRIPIEDSP------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 266 teDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQR 345
Cdd:cd14498    58 --DEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSR----RPIISPNPGFLK 131


                  ....
gi 2220285855 346 KLMR 349
Cdd:cd14498   132 QLKE 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
273-354 3.29e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.90  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 273 DMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMsKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQRKLMRYQQ 352
Cdd:COG2453    64 EQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLV-LLGLSAEEALARVRAA----RPGAVETPAQRAFLERFAK 138


                  ..
gi 2220285855 353 HL 354
Cdd:COG2453   139 RL 140
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
266-352 4.50e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 45.74  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855  266 TEDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRPPVNisdFMqR 345
Cdd:smart00195  55 NTETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFG---FL-R 130


                   ....*..
gi 2220285855  346 KLMRYQQ 352
Cdd:smart00195 131 QLIEYER 137
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 263-351 4.14e-04

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: 39.94  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 263 MMLTEDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRPpvNISdF 342
Cdd:pfam00782  43 VEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISP--NFG-F 119


                  ....*....
gi 2220285855 343 MqRKLMRYQ 351
Cdd:pfam00782 120 K-RQLLEYE 127
cpxP PRK10363
cell-envelope stress modulator CpxP;
264-330 1.65e-03

cell-envelope stress modulator CpxP;


Pssm-ID: 182410  Cd Length: 166  Bit Score: 38.86  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 264 MLTEDTKLNDMFDG----------FLDLVQRARRAKRNVLVCSTRGRNR---APAF------ASAYLMSKEQIPRQAAVA 324
Cdd:PRK10363   35 ELTQRSTQSHMFDGisltehqrqqMRDLMQQARHEQPPVNVSEMETMHRlvtAENFdenavrAQAEKMAQEQVARQVEMA 114


                  ....*.
gi 2220285855 325 KVRTAM 330
Cdd:PRK10363  115 KVRNQM 120
 
Name Accession Description Interval E-value
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 186-349 1.64e-11

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: 61.41  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 186 QIDDVVFASAIDAVNNNSLMCRLNIEFICEIADEtadhvQEARRQNRGFEcpcfcnrssshfryYLSYSLPETEqrcmml 265
Cdd:cd14498     3 EILPGLYLGSLDAAQDKELLKKLGITHILNVAGE-----PPPNKFPDGIK--------------YLRIPIEDSP------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 266 teDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQR 345
Cdd:cd14498    58 --DEDILSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSR----RPIISPNPGFLK 131


                  ....
gi 2220285855 346 KLMR 349
Cdd:cd14498   132 QLKE 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
273-354 3.29e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.90  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 273 DMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMsKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQRKLMRYQQ 352
Cdd:COG2453    64 EQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLV-LLGLSAEEALARVRAA----RPGAVETPAQRAFLERFAK 138


                  ..
gi 2220285855 353 HL 354
Cdd:COG2453   139 RL 140
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 266-335 4.30e-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: 48.79  E-value: 4.30e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 266 TEDTKLNDMFDGFLDLVQRARrAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRP 335
Cdd:cd14520    57 EESTDLLSRLDECLDFIDEGR-AEGAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKP 125
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
266-352 4.50e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 45.74  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855  266 TEDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRPPVNisdFMqR 345
Cdd:smart00195  55 NTETKISPYFPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFG---FL-R 130


                   ....*..
gi 2220285855  346 KLMRYQQ 352
Cdd:smart00195 131 QLIEYER 137
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 275-350 1.42e-05

dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs 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. IBR5 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. It has been shown to target MPK12, which is a negative regulator of auxin signaling.


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 44.06  E-value: 1.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2220285855 275 FDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQ--IPRQAAVAKVRtamgtmRPPVNISDFMQRKLMRY 350
Cdd:cd18534    59 FAEAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGwrLAESYQWVKER------RPSINLSPAVAKQLQEF 130
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 268-351 3.16e-05

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: 43.50  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 268 DTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQRKL 347
Cdd:cd14523    58 ETDITSYFPECFEFIDEAKSQDGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNA----RPSIRPNPGFMEQL 133


                  ....
gi 2220285855 348 MRYQ 351
Cdd:cd14523   134 KEYQ 137
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 267-335 5.66e-05

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: 43.03  E-value: 5.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2220285855 267 EDTKLNDMFDGF---LDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRP 335
Cdd:cd14517    65 EDSVEADLLSFFeraCSFIDKHKNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRP 136
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 271-354 4.04e-04

dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), also called VHP, 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 that 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 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells. DUSP28 has an exceptionally low phosphatase activity due to the presence of bulky residues in the active site pocket resulting in low accessibility.


Pssm-ID: 350422 [Multi-domain]  Cd Length: 140  Bit Score: 40.15  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 271 LNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAmgtmRPPVNISDFMQRKLMRY 350
Cdd:cd14574    60 LYRHFEQCADAIEAAVRRGGKCLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAA----RPVAEPNPGFWSQLQRY 135


                  ....
gi 2220285855 351 QQHL 354
Cdd:cd14574   136 EEEL 139
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 263-351 4.14e-04

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: 39.94  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 263 MMLTEDTKLNDMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSKEQIPRQAAVAKVRTAMGTMRPpvNISdF 342
Cdd:pfam00782  43 VEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISP--NFG-F 119


                  ....*....
gi 2220285855 343 MqRKLMRYQ 351
Cdd:pfam00782 120 K-RQLLEYE 127
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 236-344 7.86e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 38.87  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 236 CPCFCNRSSSHFRYYLSYslpetEQRCM-MLTEDtklndMFDGFLDLVQRARRAKRNVLVCSTRGRNRAPAFASAYLMSK 314
Cdd:cd14494    12 GALPLSPLEADSRFLKQL-----GVTTIvDLTLA-----MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2220285855 315 EQIPRQAAVAKVRTAmGTMRPPVNISDFMQ 344
Cdd:cd14494    82 GGMSAEEAVRIVRLI-RPGGIPQTIEQLDF 110
cpxP PRK10363
cell-envelope stress modulator CpxP;
264-330 1.65e-03

cell-envelope stress modulator CpxP;


Pssm-ID: 182410  Cd Length: 166  Bit Score: 38.86  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220285855 264 MLTEDTKLNDMFDG----------FLDLVQRARRAKRNVLVCSTRGRNR---APAF------ASAYLMSKEQIPRQAAVA 324
Cdd:PRK10363   35 ELTQRSTQSHMFDGisltehqrqqMRDLMQQARHEQPPVNVSEMETMHRlvtAENFdenavrAQAEKMAQEQVARQVEMA 114


                  ....*.
gi 2220285855 325 KVRTAM 330
Cdd:PRK10363  115 KVRNQM 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.
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