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Conserved domains on  [gi|2462532517|ref|XP_054228294|]
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protein phosphatase Slingshot homolog 1 isoform X3 [Homo sapiens]

Protein Classification

SSH-N and DSP_slingshot_1 domain-containing protein( domain architecture ID 12974745)

protein containing domains SSH-N, DEK_C, DSP_slingshot_1, and PTZ00449

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SSH-N cd11652
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 22-221 3.35e-131

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


:

Pssm-ID: 212166  Cd Length: 233  Bit Score: 396.33  E-value: 3.35e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517   22 LSESFFMVKGAALFLQQGSSPQGQRSLQHpHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQ 101
Cdd:cd11652     36 RSESFFAVKGAALILPQGDRTNRPREIAS-HKHAGELQQHLQAMFNLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQ 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  102 DTEENILLGVDFSSKESkSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNY 181
Cdd:cd11652    115 DTEESILLGVDFPPKES-SCTIGLVLPIWSDTQVHLDGDGGFSVTSDGKTHIFKPVSVQAMWSALQVLHKACEVAREANY 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462532517  182 FPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDS 221
Cdd:cd11652    194 FPGGLALTWVSYYQSRISSDQSCLNEWEAMDDLESHRPDS 233
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 290-433 6.94e-109

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.


:

Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 334.35  E-value: 6.94e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14570      1 MDKASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDA 433
Cdd:cd14570     81 HSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEGILDA 144
DEK_C pfam08766
DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and ...
 235-287 1.08e-15

DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and autoimmune disease. This domain is found at the C terminal of DEK and is of clinical importance since it can reverse the characteriztic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. The structure of this domain shows it to be homologous to the E2F/DP transcription factor family. This domain is also found in chitin synthase proteins like Swiss:Q8TF96, and in protein phosphatases such as Swiss:Q6NN85.


:

Pssm-ID: 462592  Cd Length: 54  Bit Score: 72.04  E-value: 1.08e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  235 TERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLIL 287
Cdd:pfam08766    2 TDEEIREAIREILRTADLETVTKKQVRKQLEERLGVDLSERKAFINALIDEIL 54
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 639-1028 5.43e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  639 PTASGAPEASRERCEDPN-APAICTQPAFLPHITSSPVAHLASRS-RVPEKPASgptepppflppagSRRADTsgpgAGA 716
Cdd:PTZ00449   543 PKEGGKPGETKEGEVGKKpGPAKEHKPSKIPTLSKKPEFPKDPKHpKDPEEPKK-------------PKRPRS----AQR 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  717 ALEPPASLLEPSRETPKVlPKSLLLKNSHCDKNPPSTEVVIKEESSPK--KDMKPAKDLRLLFSNESEKPTTNSYLmqhq 794
Cdd:PTZ00449   606 PTRPKSPKLPELLDIPKS-PKRPESPKSPKRPPPPQRPSSPERPEGPKiiKSPKPPKSPKPPFDPKFKEKFYDDYL---- 680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  795 esiiqlqKAGLVRKHTKEL----ERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHElgPLVMPSQAGSDEKSEAA 870
Cdd:PTZ00449   681 -------DAAAKSKETKTTvvldESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFT 751

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  871 PASLEGGSLKSPPPFFYRLDHTSSFSKDflKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQR---------TQE 941
Cdd:PTZ00449   752 PPEEERTFFHETPADTPLPDILAEEFKE--EDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRhrldglalsTTD 829

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  942 IETRL-RLAGLTVSSP--LKRSHSLAKLGSLTFStEDLSSEA------DPSTVADSQDTTLSESSFLHE-----PQGTPR 1007
Cdd:PTZ00449   830 LESDAgRIAKDASGKIvkLKRSKSFDDLTTVEEA-EEMGAEArkivvdDDGTEADDEDTHPPEEKHKSEvrrrrPPKKPS 908

                          410       420
                   ....*....|....*....|.
gi 2462532517 1008 DPAATSKPSGKPAPENLKSPS 1028
Cdd:PTZ00449   909 KPKKPSKPKKPKKPDSAFIPS 929
 
Name Accession Description Interval E-value
SSH-N cd11652
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 22-221 3.35e-131

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


Pssm-ID: 212166  Cd Length: 233  Bit Score: 396.33  E-value: 3.35e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517   22 LSESFFMVKGAALFLQQGSSPQGQRSLQHpHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQ 101
Cdd:cd11652     36 RSESFFAVKGAALILPQGDRTNRPREIAS-HKHAGELQQHLQAMFNLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQ 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  102 DTEENILLGVDFSSKESkSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNY 181
Cdd:cd11652    115 DTEESILLGVDFPPKES-SCTIGLVLPIWSDTQVHLDGDGGFSVTSDGKTHIFKPVSVQAMWSALQVLHKACEVAREANY 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462532517  182 FPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDS 221
Cdd:cd11652    194 FPGGLALTWVSYYQSRISSDQSCLNEWEAMDDLESHRPDS 233
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 290-433 6.94e-109

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.


Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 334.35  E-value: 6.94e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14570      1 MDKASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDA 433
Cdd:cd14570     81 HSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEGILDA 144
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
293-428 6.98e-47

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 163.99  E-value: 6.98e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517   293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:smart00195    1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517   373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:smart00195   81 VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYE 136
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 300-428 1.65e-38

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: 139.70  E-value: 1.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEeLQGSGVDYILNVTREiDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKM 379
Cdd:pfam00782    1 LYLGSKPTASDAF-LSKLGITAVINVTRE-VDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462532517  380 GVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:pfam00782   79 GISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
298-428 2.88e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 76.55  E-value: 2.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  298 DHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGL----FAYHNIRVYDEETTDLlAHWNEAYHFINKAKRNHSKC 373
Cdd:COG2453      5 PGLLAGGPLPGGGEADLKREGIDAVVSLTEEEELLLGLLeeagLEYLHLPIPDFGAPDD-EQLQEAVDFIDEALREGKKV 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  374 LVHCKMGVSRSASTVIAYAMKEfGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:COG2453     84 LVHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRAFLERFA 137
DEK_C pfam08766
DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and ...
 235-287 1.08e-15

DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and autoimmune disease. This domain is found at the C terminal of DEK and is of clinical importance since it can reverse the characteriztic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. The structure of this domain shows it to be homologous to the E2F/DP transcription factor family. This domain is also found in chitin synthase proteins like Swiss:Q8TF96, and in protein phosphatases such as Swiss:Q6NN85.


Pssm-ID: 462592  Cd Length: 54  Bit Score: 72.04  E-value: 1.08e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  235 TERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLIL 287
Cdd:pfam08766    2 TDEEIREAIREILRTADLETVTKKQVRKQLEERLGVDLSERKAFINALIDEIL 54
PRK12361 PRK12361
hypothetical protein; Provisional
 296-442 1.94e-11

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 67.72  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREidnfFPGL--------FAYHNIRVYDeETTDLLAHWNEAYHFINKAK 367
Cdd:PRK12361    98 IDENLYLGCRLFPADLEKLKSNKITAILDVTAE----FDGLdwslteedIDYLNIPILD-HSVPTLAQLNQAINWIHRQV 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532517  368 RNHSKCLVHCKMGVSRSASTVIAYAM-KEFGWPLEKAYNYVKQKRSITRPNAgfmRQLSEYEGILDASKQR-HNKLW 442
Cdd:PRK12361   173 RANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK---RQLRALEKMLEQGKLNiHKRAW 246
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 639-1028 5.43e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  639 PTASGAPEASRERCEDPN-APAICTQPAFLPHITSSPVAHLASRS-RVPEKPASgptepppflppagSRRADTsgpgAGA 716
Cdd:PTZ00449   543 PKEGGKPGETKEGEVGKKpGPAKEHKPSKIPTLSKKPEFPKDPKHpKDPEEPKK-------------PKRPRS----AQR 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  717 ALEPPASLLEPSRETPKVlPKSLLLKNSHCDKNPPSTEVVIKEESSPK--KDMKPAKDLRLLFSNESEKPTTNSYLmqhq 794
Cdd:PTZ00449   606 PTRPKSPKLPELLDIPKS-PKRPESPKSPKRPPPPQRPSSPERPEGPKiiKSPKPPKSPKPPFDPKFKEKFYDDYL---- 680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  795 esiiqlqKAGLVRKHTKEL----ERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHElgPLVMPSQAGSDEKSEAA 870
Cdd:PTZ00449   681 -------DAAAKSKETKTTvvldESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFT 751

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  871 PASLEGGSLKSPPPFFYRLDHTSSFSKDflKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQR---------TQE 941
Cdd:PTZ00449   752 PPEEERTFFHETPADTPLPDILAEEFKE--EDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRhrldglalsTTD 829

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  942 IETRL-RLAGLTVSSP--LKRSHSLAKLGSLTFStEDLSSEA------DPSTVADSQDTTLSESSFLHE-----PQGTPR 1007
Cdd:PTZ00449   830 LESDAgRIAKDASGKIvkLKRSKSFDDLTTVEEA-EEMGAEArkivvdDDGTEADDEDTHPPEEKHKSEvrrrrPPKKPS 908

                          410       420
                   ....*....|....*....|.
gi 2462532517 1008 DPAATSKPSGKPAPENLKSPS 1028
Cdd:PTZ00449   909 KPKKPSKPKKPKKPDSAFIPS 929
 
Name Accession Description Interval E-value
SSH-N cd11652
N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved ...
 22-221 3.35e-131

N-terminal domain conserved in slingshot (SSH) phosphatases; This domain or region conserved in Bilateria is found N-terminal to the DEK_C-like and catalytic domains of slingshot phosphatases. Slingshot is a cofilin-specific phosphatase. Dephosphorylation reactivates cofilin, which in turn depolymerizes actin and is thus required for actin filament reorganization. Slingshot is a member of the dual-specificity protein phosphatase family. This N-terminal SSH region may be involved in P-cofilin binding (the model C-terminus plus the DEK_C-like domain, which are characterized as the "B" domain in some of the literature), and may be required for the F-actin mediated activation of slingshot (the N-terminal region of this model, sometimes referred to as the "A" domain).


Pssm-ID: 212166  Cd Length: 233  Bit Score: 396.33  E-value: 3.35e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517   22 LSESFFMVKGAALFLQQGSSPQGQRSLQHpHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESAWADRVRYMVVVYSSGRQ 101
Cdd:cd11652     36 RSESFFAVKGAALILPQGDRTNRPREIAS-HKHAGELQQHLQAMFNLLRPEDTIKLAVRLESVRSNRTRYLVVVSTLGRQ 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  102 DTEENILLGVDFSSKESkSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNY 181
Cdd:cd11652    115 DTEESILLGVDFPPKES-SCTIGLVLPIWSDTQVHLDGDGGFSVTSDGKTHIFKPVSVQAMWSALQVLHKACEVAREANY 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462532517  182 FPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDS 221
Cdd:cd11652    194 FPGGLALTWVSYYQSRISSDQSCLNEWEAMDDLESHRPDS 233
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 290-433 6.94e-109

dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.


Pssm-ID: 350418 [Multi-domain]  Cd Length: 144  Bit Score: 334.35  E-value: 6.94e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14570      1 MDKASLIFDHLYLGSEWNASNLEELQGSGVGYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDA 433
Cdd:cd14570     81 HSKCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITRPNAGFMRQLLEYEGILDA 144
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 293-431 6.81e-97

dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) family of dual specificity protein phosphatases is composed of Drosophila slingshot phosphatase and its vertebrate homologs: SSH1, SSH2 and SSH3. Its members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. In Drosophila, loss of ssh gene function causes prominent elevation in the levels of P-cofilin and filamentous actin and disorganized epidermal cell morphogenesis, including bifurcation phenotypes of bristles and wing hairs. SSH family phosphatases contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, many members contain a C-terminal tail. The SSH-N domain plays critical roles in P-cofilin recognition, F-actin-mediated activation, and subcellular localization of SSHs.


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 302.01  E-value: 6.81e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14513      1 ASKIFDHLYLGSEWNASNLEELQNNGVKYILNVTREIDNFFPGRFTYHNIRVWDEESTNLLPYWNETYRFIKEARRKGSK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGIL 431
Cdd:cd14513     81 VLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRSCIKPNPGFLRQLITYEGML 139
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
 290-433 7.60e-81

dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein phosphatase slingshot homolog 2 (SSH2), also called SSH-like protein 2, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH2 has been identified as a target of protein kinase D1 that regulates cofilin phosphorylation and remodeling of the actin cytoskeleton during neutrophil chemotaxis. There are at least two human SSH2 isoforms reported: hSSH-2L (long) and hSSH-2. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-2L contains a long C-terminal tail while hSSH-2 does not.


Pssm-ID: 350417 [Multi-domain]  Cd Length: 144  Bit Score: 259.19  E-value: 7.60e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14569      1 MDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGLFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKH 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDA 433
Cdd:cd14569     81 GSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVTKPNPSFMRQLEEYQGILLA 144
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 290-433 1.57e-77

dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-3L contains a C-terminal tail while hSSH-3 does not.


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 250.17  E-value: 1.57e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14571      1 MDRPSRIFPYLYLGSEWNAANLEELQRNRVSHILNVTREIDNFFPERFTYMNIRVYDEEATQLLPHWKETHRFIEAARAQ 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDA 433
Cdd:cd14571     81 GTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIVQPNPGFLRQLQTYQGILTA 144
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 293-426 1.28e-55

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: 188.91  E-value: 1.28e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNF-FPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHS 371
Cdd:cd14498      1 PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPPPNkFPDGIKYLRIPIEDSPDEDILSHFEEAIEFIEEALKKGG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSE 426
Cdd:cd14498     81 KVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPIISPNPGFLKQLKE 135
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
293-428 6.98e-47

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 163.99  E-value: 6.98e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517   293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:smart00195    1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKGGK 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517   373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:smart00195   81 VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYE 136
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 293-428 6.98e-43

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: 152.54  E-value: 6.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14565      1 PVEILPFLYLGSAYHASRREVLKALGITAVLNVSRNCPNHFEDHFQYKSIPVEDSHNADISSWFEEAIGFIDKVKASGGR 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14565     81 VLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSVISPNFNFMGQLLQYE 136
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 300-428 1.65e-38

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: 139.70  E-value: 1.65e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEeLQGSGVDYILNVTREiDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKM 379
Cdd:pfam00782    1 LYLGSKPTASDAF-LSKLGITAVINVTRE-VDLYNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQKGGKVLVHCQA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462532517  380 GVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:pfam00782   79 GISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 299-428 1.76e-37

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: 137.10  E-value: 1.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  299 HLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCK 378
Cdd:cd14523      8 WLLLSSQDVAHDLETLKKHKVTHILNVAYGVENAFPDDFTYKTISILDLPETDITSYFPECFEFIDEAKSQDGVVLVHCN 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462532517  379 MGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14523     88 AGVSRSASIVIGYLMATENLSFEDAFSLVKNARPSIRPNPGFMEQLKEYQ 137
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 293-431 1.62e-36

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: 134.88  E-value: 1.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFF--PGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14567      1 LTPILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYHegKGGFRYKRLPATDSNKQNLRQYFEEAFEFIEEAHQSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGIL 431
Cdd:cd14567     81 KGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPIISPNLNFMGQLLEFEEDL 141
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 293-431 9.74e-36

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: 132.16  E-value: 9.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNF-FPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHS 371
Cdd:cd14568      1 PTRILPHLYLGSQRDVLDKDLMQRNGISYVLNVSNTCPKPdFIPDSHFLRIPVNDSYCEKLLPWLDKAVEFIEKARASNK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGIL 431
Cdd:cd14568     81 RVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRPTISPNFNFLGQLLEFEKKL 140
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 293-427 2.82e-35

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: 130.90  E-value: 2.82e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFP--GLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14566      1 PVEILPFLYLGNAKDSANIDLLKKYNIKYILNVTPNLPNTFEedGGFKYLQIPIDDHWSQNLSAFFPEAISFIDEARSKK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEY 427
Cdd:cd14566     81 CGVLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKRKSNISPNFNFMGQLLDF 137
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 293-424 2.10e-34

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: 128.06  E-value: 2.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEwNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14514      1 ISQITPHLFLSGA-SAATPPLLLSRGITCIINATTELPDPSYPGIEYLRVPVEDSPHADLSPHFDEVADKIHQVKRRGGR 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQL 424
Cdd:cd14514     80 TLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPIIRPNVGFWRQL 131
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 293-427 4.96e-34

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: 127.22  E-value: 4.96e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNF-FPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHS 371
Cdd:cd14512      1 PTRILPNLYLGSQRDSLNLELMQQLGIGYVLNVSNTCPNPdFIGLFHYKRIPVNDSFCQNISPWFDEAIEFIEEAKASNG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEY 427
Cdd:cd14512     81 GVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPTISPNFNFMGQLLDF 136
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 293-428 3.31e-30

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: 116.55  E-value: 3.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14639      1 PVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRSSEACKGQYHYKWIPVEDSHTADISSHFQEAIDFIDCVRRAGGK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14639     81 VLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSLISPNFGFMGQLLQYE 136
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 293-428 1.18e-29

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: 114.96  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14641      4 PVEILPFLFLGSAHHSSRRETLESLGITAVLNVSSSCPNYFEGQFQYKSIPVEDSHMADISAWFQEAIDFIDSVKNSGGR 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14641     84 VLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFE 139
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 300-428 1.31e-29

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: 115.04  E-value: 1.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHN--IRVYDEETTDLLAHWNEAYHFINKAkRNHSKCLVHC 377
Cdd:cd14520      8 LYIGNADDAADYLSLREAGITHVLTVDSEEPIDAPPVGKLVRkfVPALDEESTDLLSRLDECLDFIDEG-RAEGAVLVHC 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462532517  378 KMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14520     87 HAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPDVKPNDGFLKQLKLYE 137
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 296-428 8.26e-28

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: 109.99  E-value: 8.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFF----PGLFA-----YHNIRVYDEETTDLLAHWNEAYHFINKA 366
Cdd:cd14515      4 VWPGIYIGDESTAKNKAKLKKLGITHVLNAAEGKKNGEvntnAKFYKgsgiiYLGIPASDLPTFDISQYFDEAADFIDKA 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  367 -KRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSItRPNAGFMRQLSEYE 428
Cdd:cd14515     84 lSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKREI-RPNRGFLQQLCELN 145
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 293-428 3.90e-27

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: 108.17  E-value: 3.90e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTR-EIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKA----- 366
Cdd:cd14518      1 LSRILGGLYLGGIEPLNRNRLLKAENITHILSVIPgDVPEEYFKGYEHKQIEIDDVEDENILQHFPETNRFIDSAlfgng 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532517  367 ------KRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14518     81 kdedeeKKHGGAVLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGFMEQLELYH 148
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 293-428 6.02e-27

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), 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 I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 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: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 107.04  E-value: 6.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14640      1 PVEILPFLYLGSAYHAARRDMLDALGITALLNVSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEYIDSVKDCNGR 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14640     81 VLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFE 136
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 293-428 9.08e-27

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: 107.01  E-value: 9.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFP--GLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14644      3 PVQILPNLYLGSARDSANLETLAKLGIRYILNVTPNLPNFFEknGDFHYKQIPISDHWSQNLSQFFPEAIEFIDEALSQN 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14644     83 CGVLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVKRKKSNISPNFNFMGQLLDFE 140
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 293-431 1.50e-26

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: 106.26  E-value: 1.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFP--GLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14643      6 PVQILPYLYLGCAKDSTNLDVLGKYGIKYILNVTPNLPNMFEhdGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARSKK 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGIL 431
Cdd:cd14643     86 CGILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVKRKKSNISPNFNFMGQLLDFERTL 146
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 296-430 1.72e-26

dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling.


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 106.26  E-value: 1.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNA--SNLEELQGSGVDYILNVTREID-NF----FPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKR 368
Cdd:cd14522      8 ILPGLYLGPYSAAmkSKLEVLLKHGITHIVCVRQNIEaNFikpnFPDHFRYLVLDVADNPTENIIRHFPTVKEFIDDCLQ 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  369 NHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGI 430
Cdd:cd14522     88 TGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFCINPNEGFVHQLKEYEAI 149
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 300-428 1.75e-25

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: 103.51  E-value: 1.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFA-YHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCK 378
Cdd:cd14517     19 LYMGNYKQACDKKIQKDLKIKAHINVSMDADELFKSGNDqVLHIPVEDSVEADLLSFFERACSFIDKHKNNGSRVLVFST 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462532517  379 MGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14517     99 LGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNNMRPNRGFVKQLSEWE 148
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 293-427 4.18e-25

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: 101.46  E-value: 4.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIF-DHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHnirVYDEETTdllAHWNEAYHFINKAKRNHS 371
Cdd:cd18534      1 PTEILpGFLYLGSYDNASRAELLKAQGITRILNTVPDCQNLYKNSFTYH---VLSEEKT---VPFAEAVDFIEQCRKDKA 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEY 427
Cdd:cd18534     75 RVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSPAVAKQLQEF 130
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 293-434 6.50e-25

dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-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 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. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. 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: 350486 [Multi-domain]  Cd Length: 151  Bit Score: 101.68  E-value: 6.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSK 372
Cdd:cd14638      1 PVEILPFLYLGSAYHASRKDMLDTLGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSVKNAGGR 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  373 CLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGILDAS 434
Cdd:cd14638     81 VFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAP 142
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 300-428 4.69e-24

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also 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.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 99.17  E-value: 4.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKM 379
Cdd:cd14572     15 LYLSRGNVASNRHLLLSRGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPISLYFDSVADKIHSVGRKHGATLVHCAA 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462532517  380 GVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14572     95 GVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPVIRPNVGFWRQLIDYE 143
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 296-428 2.93e-23

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: 96.77  E-value: 2.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREidNFFPGLFAYHNIR--VYDEETTDLLAHWNEAYHFINKAKRNHSKC 373
Cdd:cd14574      4 VTDSLFISNARAACNEELLAREGVTLCVNVSRQ--QPFPRAPRVSTLRvpVFDDPAEDLYRHFEQCADAIEAAVRRGGKC 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  374 LVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14574     82 LVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPVAEPNPGFWSQLQRYE 136
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 290-429 4.35e-23

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They 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. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 95.89  E-value: 4.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKpslIFDHLYLGSEWNASNLEELQGSGVDYILNVTreiDNFFPGL--FAYHNIRVYDEETTDLLAHWNEAYHFINKAK 367
Cdd:cd14519      1 MNK---ILPGLYVGNFRDAKDAEQLRENGITHILSIH---DSARPLLedIKYLCIPAADTPEQNISQHFRECINFIHEAR 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  368 RNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEG 429
Cdd:cd14519     75 LNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCANPNFGFQRQLQEFEK 136
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 293-431 9.23e-23

dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual specificity protein phosphatase 6 (DUSP6), also called mitogen-activated protein kinase (MAPK) phosphatase 3 (MKP-3) or dual specificity protein phosphatase PYST1, 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. DUSP6/MKP-3 plays an important role in obesity-related hyperglycemia by promoting hepatic glucose output. MKP-3 deficiency attenuates body weight gain induced by a high-fat diet, protects mice from developing obesity-related hepatosteatosis, and reduces adiposity, possibly by repressing adipocyte differentiation. It also contributes to p53-controlled cellular senescence. 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: 350490 [Multi-domain]  Cd Length: 143  Bit Score: 95.14  E-value: 9.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFF--PGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14642      3 PVEILPYLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLFenAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGKN 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYEGIL 431
Cdd:cd14642     83 CGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTL 143
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 290-428 1.75e-22

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: 94.86  E-value: 1.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  290 MDKpslIFDHLYLGSEWNASNLEELQGSGVDYILNVTreiDNFFPGL--FAYHNIRVYDEETTDLLAHWNEAYHFINKAK 367
Cdd:cd14581      4 MNK---VLPGLYLGNFKDARDREQLSKNNITHILSVH---DSARPMLegMTYLCIPAADSPSQNLTQHFKESIKFIHECR 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  368 RNHSKCLVHCKMGVSRSASTVIAYAM--KEFGWplEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14581     78 LRGEGCLVHCLAGVSRSVTLVVAYIMtvTDFGW--EDALSAVKAARSCANPNMGFQRQLQEFE 138
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 293-428 4.89e-22

dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; This subfamily contains fungal proteins with similarity to dual specificity protein phosphatase PPS1 from Saccharomyces cerevisiae, which has a role in the DNA synthesis phase of the cell cycle. As a dual specificity protein phosphatase, PPS1 functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It contains a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350366 [Multi-domain]  Cd Length: 177  Bit Score: 94.26  E-value: 4.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTrEIDNFFPGLFAY--HNIRVYDEETTD------------------- 351
Cdd:cd14516      7 PSRILPHLYLGSLNHASNATLLESLGITHIVSVG-ESPSWFSNLKIKyiFDFSLQDLSNLDsnsegslwaaeykglisvl 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  352 ------------LLAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKR--SITRPN 417
Cdd:cd14516     86 yihnlkddgidsLLPQLTDALDFIQKARLLGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRRlnIIIQPN 165

                          170
                   ....*....|.
gi 2462532517  418 AGFMRQLSEYE 428
Cdd:cd14516    166 LRFFYELFKWE 176
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 300-431 1.01e-21

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), 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. DUSP26 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 is a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 92.21  E-value: 1.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVT----REIDNFFPGL-FAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHS-KC 373
Cdd:cd14578      8 LYLGDQDIAANRRELRRLGITHILNAShskwRGGAEYYEGLnIRYLGIEAHDSPAFDMSIHFYPAADFIHRALSQPGgKI 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532517  374 LVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSEYEGIL 431
Cdd:cd14578     88 LVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGII-PNRGFLRQLLALDRRL 144
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 294-428 1.04e-21

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: 92.93  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  294 SLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKC 373
Cdd:cd14573      3 SRITESLYLSNGVAANNRTLLAANRITCVINVSLEVANGLPPGIEYLHVPVADSPDTRLRDYFDPIADKIHTVEARGGRT 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  374 LVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14573     83 LLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPIIRPNNGFWEQLIHYE 137
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 293-428 9.19e-21

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: 89.70  E-value: 9.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREID--NFFPGLFaYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH 370
Cdd:cd14646      3 PTRILPHLYLGCQRDVLNKELMQQNGIGYVLNASNTCPkpDFIPESH-FLRVPVNDSFCEKILPWLDKSVDFIEKAKASN 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462532517  371 SKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14646     82 GRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDFE 139
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 296-427 1.34e-20

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: 89.83  E-value: 1.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREID--------NFFPGL-FAYHNIRVYDEETTDLLAHWNEAYHFINKA 366
Cdd:cd14579     24 VYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSfmhvntnaEFYEDTgITYHGIKANDTQHFNLSAYFEEAADFIDKA 103

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  367 -KRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSEY 427
Cdd:cd14579    104 lAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKREIG-PNDGFLKQLCQL 164
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 291-431 2.04e-20

dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, and similar proteins; This family is composed of fungal dual specificity protein phosphatases (DUSPs) including Saccharomyces cerevisiae SDP1 and MSG5, and Schizosaccharomyces pombe Pmp1. 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. SDP1 is oxidative stress-induced and dephosphorylates MAPK substrates such as SLT2. MSG5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity (CWI) pathways, respectively. Pmp1 is responsible for dephosphorylating the CWI MAPK Pmk1. These phosphatases bind to their target MAPKs through a conserved IYT motif located outside of the dual specificity phosphatase domain.


Pssm-ID: 350371 [Multi-domain]  Cd Length: 155  Bit Score: 88.92  E-value: 2.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  291 DKPSLIFD-HLYLGSEwnaSNLEELQGSGVdyILNVTREIDNFFPGLfayhnIRVYDEETTDLLA-----------HW-- 356
Cdd:cd14521      3 DGPVCVLPpNIYLYSE---PTLEEASSFDV--VINVAKEVKNPFLSD-----ASLAEKEKTILPGqqvknpeyihvPWdh 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  357 -----NEAYHFINKAKRNHS---KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14521     73 nsqiqKDLPKLTSIIEDATQsgkKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSRSPWIGPNMSLIFQLMEFE 152


                   ...
gi 2462532517  429 GIL 431
Cdd:cd14521    153 KVL 155
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 293-428 7.87e-20

dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual specificity protein phosphatase 8 (DUSP8), also called DUSP hVH-5 or M3/6, 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. DUSP8 controls basal and acute stress-induced ERK1/2 signaling in adult cardiac myocytes, which impacts contractility, ventricular remodeling, and disease susceptibility. It also plays a role in decreasing ureteric branching morphogenesis by inhibiting p38MAPK. DUSP8 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: 350493 [Multi-domain]  Cd Length: 151  Bit Score: 87.37  E-value: 7.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  293 PSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNffPGLFA---YHNIRVYDEETTDLLAHWNEAYHFINKAKRN 369
Cdd:cd14645     12 PTRILPHLYLGSQKDVLNKDLMAQNGITYVLNASNSCPK--PDFICeshFMRIPVNDNYCEKLLPWLDKSIEFIDKAKVS 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462532517  370 HSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:cd14645     90 NCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRPSISPNFNFLGQLLEYE 148
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 296-431 2.95e-18

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), 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. DUSP13A 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. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 82.50  E-value: 2.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREI------DNFFPGLFAYHNIRVYDEETTDLLAHWNEAYHFINKA-KR 368
Cdd:cd14580      4 VWPNLFLGDLATAHNRFGLWKLGITHVLNAAHGKlfcqggDDFYGTSVDYYGVPANDLPDFDISPYFYSAAEFIHRAlNT 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  369 NHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSEYEGIL 431
Cdd:cd14580     84 PGAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRWIF-PNRGFLKQLRKLDQQL 145
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 300-429 1.15e-16

dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual specificity protein phosphatase 15 (DUSP15), also called Vaccinia virus VH1-related dual-specific protein phosphatase Y (VHY) or VH1-related member Y, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). DUSP15 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 is highly expressed in the testis and is located in the plasma membrane in a myristoylation-dependent manner. It may be involved in the regulation of meiotic signal transduction in testis cells. It is also expressed in the brain and has been identified as a regulator of oligodendrocyte differentiation. DUSP15 contains an N-terminal catalytic dual specificity phosphatase domain and a short C-terminal tail.


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 78.07  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLfAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNHSKCLVHCKM 379
Cdd:cd14582     12 LYLGNFIDAKDLEQLSRNKITHIISIHESPQPLLQDI-TYLRIPLPDTPEAPIKKHFKECISFIHQCRLNGGNCLVHCLA 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462532517  380 GVSRSASTVIAYAM--KEFGWplEKAYNYVKQKRSITRPNAGFMRQLSEYEG 429
Cdd:cd14582     91 GISRSTTIVVAYVMavTELSW--QEVLEAIRAVRPIANPNPGFKQQLEEFGW 140
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 300-426 2.77e-16

dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1) was initially named as such because computational prediction appeared to encode a protein of 446 amino acids in length that included two catalytic domains: a proline isomerase and a dual specificity phosphatase (DUSP). However, it was subsequently shown that the true open reading frame only encompassed the DUSP domain and the gene product was therefore renamed DUSP27. This is distinct from inactive DUSP27. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). DUPD1/DUSP27 has been shown to have catalytic activity with preference for phosphotyrosine over phosphothreonine and phosphoserine residues. It associates with the short form of the prolactin (PRL) receptor and plays a role in PRL-mediated MAPK inhibition in ovarian cells.


Pssm-ID: 350423 [Multi-domain]  Cd Length: 160  Bit Score: 77.17  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPG-------LFAYHNIRVYDEETTDLLAHWNEAYHFINKA-KRNHS 371
Cdd:cd14575     18 LYIGDEKTALDRYSLQKLGITHILNAAHGKWNVDTGaeyykdmTIHYYGVEADDLPTFNLSQFFYSAAEFIHQAlSDPHN 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSE 426
Cdd:cd14575     98 KLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRRCIL-PNRGFLKQLRE 151
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
298-428 2.88e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 76.55  E-value: 2.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  298 DHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGL----FAYHNIRVYDEETTDLlAHWNEAYHFINKAKRNHSKC 373
Cdd:COG2453      5 PGLLAGGPLPGGGEADLKREGIDAVVSLTEEEELLLGLLeeagLEYLHLPIPDFGAPDD-EQLQEAVDFIDEALREGKKV 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  374 LVHCKMGVSRSASTVIAYAMKEfGWPLEKAYNYVKQKRSITRPNAGFMRQLSEYE 428
Cdd:COG2453     84 LVHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRAFLERFA 137
DEK_C pfam08766
DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and ...
 235-287 1.08e-15

DEK C terminal domain; DEK is a chromatin associated protein that is linked with cancers and autoimmune disease. This domain is found at the C terminal of DEK and is of clinical importance since it can reverse the characteriztic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. The structure of this domain shows it to be homologous to the E2F/DP transcription factor family. This domain is also found in chitin synthase proteins like Swiss:Q8TF96, and in protein phosphatases such as Swiss:Q6NN85.


Pssm-ID: 462592  Cd Length: 54  Bit Score: 72.04  E-value: 1.08e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  235 TERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKELKEFIDNEMLLIL 287
Cdd:pfam08766    2 TDEEIREAIREILRTADLETVTKKQVRKQLEERLGVDLSERKAFINALIDEIL 54
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 349-427 2.35e-13

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: 68.44  E-value: 2.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  349 TTDL-----LAHWNEAYHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITRPNAGFMRQ 423
Cdd:cd14524     63 TVDFtgvpsLEDLEKGVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLSQREV 142


                   ....
gi 2462532517  424 LSEY 427
Cdd:cd14524    143 LEEF 146
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 300-426 4.65e-13

dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 isoform B (DUSP13B), also called testis- and skeletal-muscle-specific DSP (TMDP) or dual specificity phosphatase SKRP4, 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. DUSP13B 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. DUSP13B inactivates MAPK activation in the order of selectivity, JNK = p38 > ERK in cells. It may play a role in protection from external stress during spermatogenesis.


Pssm-ID: 350425 [Multi-domain]  Cd Length: 163  Bit Score: 67.90  E-value: 4.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  300 LYLGSEWNASNLEELQGSGVDYILNVTR---EIDN---FFPGL-FAYHNIRVYDEETTDLLAHWNEAYHFINKA-KRNHS 371
Cdd:cd14577     25 LYLGDAYAARDKSVLIQLGITHIVNAASgkfHVNTgpkFYRDMnIDYYGVEADDNPFFDLSVYFYPVARFIRAAlSSPNG 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462532517  372 KCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSE 426
Cdd:cd14577    105 RVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVRAHRDIC-PNSGFLRQLRE 158
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 294-412 7.17e-12

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: 64.14  E-value: 7.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  294 SLIFDHLYLGSE-WNASNLEELQGSGVDYILNVTREIDNFFPGL-------------FAYHNIRVYDEETTDLLAHWNEA 359
Cdd:cd14526      4 SRILPNLIVGSCpQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVdidsirkackesgIRYVRLPIRDFDTEDLRQKLPQA 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462532517  360 YHFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKRS 412
Cdd:cd14526     84 VALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRP 136
PRK12361 PRK12361
hypothetical protein; Provisional
 296-442 1.94e-11

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 67.72  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  296 IFDHLYLGSEWNASNLEELQGSGVDYILNVTREidnfFPGL--------FAYHNIRVYDeETTDLLAHWNEAYHFINKAK 367
Cdd:PRK12361    98 IDENLYLGCRLFPADLEKLKSNKITAILDVTAE----FDGLdwslteedIDYLNIPILD-HSVPTLAQLNQAINWIHRQV 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462532517  368 RNHSKCLVHCKMGVSRSASTVIAYAM-KEFGWPLEKAYNYVKQKRSITRPNAgfmRQLSEYEGILDASKQR-HNKLW 442
Cdd:PRK12361   173 RANKSVVVHCALGRGRSVLVLAAYLLcKDPDLTVEEVLQQIKQIRKTARLNK---RQLRALEKMLEQGKLNiHKRAW 246
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
 308-426 7.01e-10

dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; Inactive dual specificity protein phosphatase 27 (DUSP27) may play a role in myofiber maturation. It is a pseudophosphatase containing a substitution of the active site cysteine into a serine. It is a large protein of more than 1000 amino acids in length with an N-terminal dual specificity phosphatase-like domain.


Pssm-ID: 350424  Cd Length: 159  Bit Score: 58.72  E-value: 7.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  308 ASNLEELQGSGVDYILNVTREID-----NFFPGL-FAYHNIRVYDEETTDLLAHWNEAYHFINKAKRNH-SKCLVHCKMG 380
Cdd:cd14576     26 AVNKGRLKRLGITHVLNAAHGTGvytgpEFYSGMnIQYMGIEVDDFPDVDISKHFRKGAEFLDEALLTYrGKVLVSSEMG 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462532517  381 VSRSASTVIAYAMKEFGWPLEKAYNYVKQKRSITrPNAGFMRQLSE 426
Cdd:cd14576    106 ISRSAVLVAAYLMIFHNMTIMEALMTLRKKRAIY-PNEGFLKQLRE 150
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 291-429 2.16e-07

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 51.12  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  291 DKPSLIFDHLYLGSEWNASNLEElqgsGVDYILNVTREidnfFPGL---FAYHNIRVYD--EETTDLLAHwneAYHFINK 365
Cdd:cd14527      3 PAYDEVLPGLYLGRWPSADELPP----GVPAVLDLTAE----LPRPrkrQAYRCVPLLDlvAPTPEQLER---AVAWIEE 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462532517  366 AKRNHSKCLVHCKMGVSRSASTVIAY--AMKEFGwPLEKAYNYVKQKRSITRPNAGFMRQLSEYEG 429
Cdd:cd14527     72 LRAQGGPVLVHCALGYGRSATVVAAWllAYGRAK-SVAEAEALIRAARPQVVLNPAQRKALEAWSG 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 362-424 1.65e-05

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: 45.03  E-value: 1.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462532517  362 FINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAYNYVKQKR-SITRPNAGFMRQL 424
Cdd:cd14494     48 VLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFL 111
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 639-1028 5.43e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.83  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  639 PTASGAPEASRERCEDPN-APAICTQPAFLPHITSSPVAHLASRS-RVPEKPASgptepppflppagSRRADTsgpgAGA 716
Cdd:PTZ00449   543 PKEGGKPGETKEGEVGKKpGPAKEHKPSKIPTLSKKPEFPKDPKHpKDPEEPKK-------------PKRPRS----AQR 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  717 ALEPPASLLEPSRETPKVlPKSLLLKNSHCDKNPPSTEVVIKEESSPK--KDMKPAKDLRLLFSNESEKPTTNSYLmqhq 794
Cdd:PTZ00449   606 PTRPKSPKLPELLDIPKS-PKRPESPKSPKRPPPPQRPSSPERPEGPKiiKSPKPPKSPKPPFDPKFKEKFYDDYL---- 680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  795 esiiqlqKAGLVRKHTKEL----ERLKSVPADPAPPSRDGPASRLEASIPEESQDPAALHElgPLVMPSQAGSDEKSEAA 870
Cdd:PTZ00449   681 -------DAAAKSKETKTTvvldESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFT 751

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  871 PASLEGGSLKSPPPFFYRLDHTSSFSKDflKTICYTPTSSSMSSNLTRSSSSDSIHSVRGKPGLVKQR---------TQE 941
Cdd:PTZ00449   752 PPEEERTFFHETPADTPLPDILAEEFKE--EDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRhrldglalsTTD 829

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462532517  942 IETRL-RLAGLTVSSP--LKRSHSLAKLGSLTFStEDLSSEA------DPSTVADSQDTTLSESSFLHE-----PQGTPR 1007
Cdd:PTZ00449   830 LESDAgRIAKDASGKIvkLKRSKSFDDLTTVEEA-EEMGAEArkivvdDDGTEADDEDTHPPEEKHKSEvrrrrPPKKPS 908

                          410       420
                   ....*....|....*....|.
gi 2462532517 1008 DPAATSKPSGKPAPENLKSPS 1028
Cdd:PTZ00449   909 KPKKPSKPKKPKKPDSAFIPS 929
 
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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