NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568976004|ref|XP_006534369|]
View 

dual specificity protein phosphatase 3 isoform X2 [Mus musculus]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 12998615)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 10-177 5.68e-119

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: 334.81  E-value: 5.68e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  10 QDLNDLLSDGSGCYSLPSQPCNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYEDSGITYLGIK 89
Cdd:cd14579    1 QELNDLLADGSGCYSLPSQHCNEVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSFMHVNTNAEFYEDTGITYHGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  90 ANDTQEFNLSAYFERATDFIDQALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQ 169
Cdd:cd14579   81 ANDTQHFNLSAYFEEAADFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKREIGPNDGFLKQ 160


                 ....*...
gi 568976004 170 LCQLNDRL 177
Cdd:cd14579  161 LCQLNDKL 168
 
Name Accession Description Interval E-value
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 10-177 5.68e-119

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: 334.81  E-value: 5.68e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  10 QDLNDLLSDGSGCYSLPSQPCNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYEDSGITYLGIK 89
Cdd:cd14579    1 QELNDLLADGSGCYSLPSQHCNEVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSFMHVNTNAEFYEDTGITYHGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  90 ANDTQEFNLSAYFERATDFIDQALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQ 169
Cdd:cd14579   81 ANDTQHFNLSAYFEEAADFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKREIGPNDGFLKQ 160


                 ....*...
gi 568976004 170 LCQLNDRL 177
Cdd:cd14579  161 LCQLNDKL 168
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
30-176 2.82e-48

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 154.75  E-value: 2.82e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004    30 CNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFmhvntsasfYEDSGITYLGIKANDTQEFNLSAYFERATDFI 109
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPN---------YNGSDFTYLGVPIDDNTETKISPYFPEAVEFI 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976004   110 DQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDR 176
Cdd:smart00195  72 EDAES-KGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPiISPNFGFLRQLIEYERK 138
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 37-172 1.09e-43

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: 142.40  E-value: 1.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004   37 VYVGNASVAQDItQLQKLGITHVLNAAEGRSFmhvntsasfyEDSGITYLGIKANDTQEFNLSAYFERATDFIDQALAhK 116
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDL----------YNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQ-K 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004  117 NGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:pfam00782  69 GGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPgISPNFGFKRQLLE 125
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
32-177 1.82e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.09  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFmhvntSASFYEDSGITYLGIKANDTQEFNLSAyFERATDFIDQ 111
Cdd:COG2453    2 WIIPGLLAGGPLPGGGEADLKREGIDAVVSLTEEEEL-----LLGLLEEAGLEYLHLPIPDFGAPDDEQ-LQEAVDFIDE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 112 ALAhKNGRVLVHCREGYSRSPTLVIAYLmMRQKMDVKSALSTVRQNR-EIGPNDGFLAQLCQLNDRL 177
Cdd:COG2453   76 ALR-EGKKVLVHCRGGIGRTGTVAAAYL-VLLGLSAEEALARVRAARpGAVETPAQRAFLERFAKRL 140
PRK12361 PRK12361
hypothetical protein; Provisional
 29-175 6.67e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 48.85  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  29 PCNEVVPRVYVGNASVAQDITQLQKLGITHVLN-AAEgrsFMHVNTSAsfyEDSGITYLGIKANDTQEFNLsAYFERATD 107
Cdd:PRK12361  94 AIQKIDENLYLGCRLFPADLEKLKSNKITAILDvTAE---FDGLDWSL---TEEDIDYLNIPILDHSVPTL-AQLNQAIN 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 108 FIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQK-MDVKSALSTVRQNRE-IGPNDGFLAQLCQLND 175
Cdd:PRK12361 167 WIHRQVR-ANKSVVVHCALGRGRSVLVLAAYLLCKDPdLTVEEVLQQIKQIRKtARLNKRQLRALEKMLE 235
 
Name Accession Description Interval E-value
DUSP3 cd14579
dual specificity protein phosphatase 3; Dual specificity protein phosphatase 3 (DUSP3), also ...
 10-177 5.68e-119

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: 334.81  E-value: 5.68e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  10 QDLNDLLSDGSGCYSLPSQPCNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYEDSGITYLGIK 89
Cdd:cd14579    1 QELNDLLADGSGCYSLPSQHCNEVYPRIYVGNASVAQNIMRLQRLGITHVLNAAEGKSFMHVNTNAEFYEDTGITYHGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  90 ANDTQEFNLSAYFERATDFIDQALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQ 169
Cdd:cd14579   81 ANDTQHFNLSAYFEEAADFIDKALAQKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVKSALSTVRQKREIGPNDGFLKQ 160


                 ....*...
gi 568976004 170 LCQLNDRL 177
Cdd:cd14579  161 LCQLNDKL 168
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 30-177 6.31e-91

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: 262.92  E-value: 6.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  30 CNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFI 109
Cdd:cd14515    1 VDEVWPGIYIGDESTAKNKAKLKKLGITHVLNAAEGKKNGEVNTNAKFYKGSGIIYLGIPASDLPTFDISQYFDEAADFI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976004 110 DQALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRL 177
Cdd:cd14515   81 DKALSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKREIRPNRGFLQQLCELNDKL 148
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 30-172 8.54e-57

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: 176.20  E-value: 8.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  30 CNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSfmhvntsaSFYEDSGITYLGIKANDTQEFNLSAYFERATDFI 109
Cdd:cd14498    1 PSEILPGLYLGSLDAAQDKELLKKLGITHILNVAGEPP--------PNKFPDGIKYLRIPIEDSPDEDILSHFEEAIEFI 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568976004 110 DQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:cd14498   73 EEALK-KGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRPiISPNPGFLKQLKE 135
DUPD1 cd14575
dual specificity phosphatase and pro isomerase domain containing 1; Dual specificity ...
 31-180 3.67e-53

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: 167.69  E-value: 3.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRsfMHVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14575   12 NEVWPGLYIGDEKTALDRYSLQKLGITHILNAAHGK--WNVDTGAEYYKDMTIHYYGVEADDLPTFNLSQFFYSAAEFIH 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 111 QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRLAKE 180
Cdd:cd14575   90 QALSDPHNKLLVHCVMGRSRSATLVLAYLMIYKNMTVVDAIEQVAQRRCILPNRGFLKQLRELDIQLAEE 159
DUSP13B cd14577
dual specificity protein phosphatase 13 isoform B; Dual specificity protein phosphatase 13 ...
 31-177 3.76e-51

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: 162.66  E-value: 3.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRsfMHVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14577   19 NEVWPNLYLGDAYAARDKSVLIQLGITHIVNAASGK--FHVNTGPKFYRDMNIDYYGVEADDNPFFDLSVYFYPVARFIR 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 111 QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRL 177
Cdd:cd14577   97 AALSSPNGRVLVHCAMGISRSATLVLAFLMICEDLTLVDAIQTVRAHRDICPNSGFLRQLRELDNRL 163
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 31-177 1.63e-49

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: 158.08  E-value: 1.63e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14578    2 DEVWPGLYLGDQDIAANRRELRRLGITHILNASHSK----WRGGAEYYEGLNIRYLGIEAHDSPAFDMSIHFYPAADFIH 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 111 QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRL 177
Cdd:cd14578   78 RALSQPGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTVKDHRGIIPNRGFLRQLLALDRRL 144
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
30-176 2.82e-48

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 154.75  E-value: 2.82e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004    30 CNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFmhvntsasfYEDSGITYLGIKANDTQEFNLSAYFERATDFI 109
Cdd:smart00195   1 PSEILPHLYLGSYSDALNLALLKKLGITHVINVTNEVPN---------YNGSDFTYLGVPIDDNTETKISPYFPEAVEFI 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976004   110 DQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDR 176
Cdd:smart00195  72 EDAES-KGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPiISPNFGFLRQLIEYERK 138
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 31-177 3.09e-48

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: 154.91  E-value: 3.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSasFYEDSgITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14580    2 DEVWPNLFLGDLATAHNRFGLWKLGITHVLNAAHGKLFCQGGDD--FYGTS-VDYYGVPANDLPDFDISPYFYSAAEFIH 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 111 QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRL 177
Cdd:cd14580   79 RALNTPGAKVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERRWIFPNRGFLKQLRKLDQQL 145
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 37-172 1.09e-43

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: 142.40  E-value: 1.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004   37 VYVGNASVAQDItQLQKLGITHVLNAAEGRSFmhvntsasfyEDSGITYLGIKANDTQEFNLSAYFERATDFIDQALAhK 116
Cdd:pfam00782   1 LYLGSKPTASDA-FLSKLGITAVINVTREVDL----------YNSGILYLRIPVEDNHETNISKYLEEAVEFIDDARQ-K 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004  117 NGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:pfam00782  69 GGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPgISPNFGFKRQLLE 125
DSP_iDUSP27 cd14576
dual specificity phosphatase-like domain of inactive dual specificity protein phosphatase 27; ...
 26-180 1.34e-41

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: 138.46  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  26 PSQPCNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERA 105
Cdd:cd14576    7 PRNAVDEVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAHGTG---VYTGPEFYSGMNIQYMGIEVDDFPDVDISKHFRKG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976004 106 TDFIDQALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPNDGFLAQLCQLNDRLAKE 180
Cdd:cd14576   84 AEFLDEALLTYRGKVLVSSEMGISRSAVLVAAYLMIFHNMTIMEALMTLRKKRAIYPNEGFLKQLRELNEKLLEE 158
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 32-172 1.04e-33

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: 117.20  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmhvNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14512    3 RILPNLYLGSQRDSLNLELMQQLGIGYVLNVS--------NTCPNPDFIGLFHYKRIPVNDSFCQNISPWFDEAIEFIEE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568976004 112 ALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:cd14512   75 AKA-SNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRPtISPNFNFMGQLLD 135
DSP_MKP_classII cd14566
dual specificity phosphatase domain of class II mitogen-activated protein kinase phosphatase; ...
 32-170 1.15e-32

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: 114.72  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14566    3 EILPFLYLGNAKDSANIDLLKKYNIKYILNVTP-------NLPNTFEEDGGFKYLQIPIDDHWSQNLSAFFPEAISFIDE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 112 ALAHKNGrVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQ-NREIGPNDGFLAQL 170
Cdd:cd14566   76 ARSKKCG-VLVHCLAGISRSVTVTVAYLMQKLHLSLNDAYDFVKKrKSNISPNFNFMGQL 134
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 33-179 1.07e-31

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: 112.54  E-value: 1.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  33 VVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHvntsasfYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQA 112
Cdd:cd14567    4 ILPFLYLGNERDAQDIDTLQRLNIGYVLNVTTHLPLYH-------EGKGGFRYKRLPATDSNKQNLRQYFEEAFEFIEEA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568976004 113 laHKNG-RVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDRLAK 179
Cdd:cd14567   77 --HQSGkGVLVHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRPiISPNLNFMGQLLEFEEDLNN 143
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 32-170 2.24e-31

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: 111.29  E-value: 2.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGrsfmhvNTSAsfYEDSgITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14523    4 VIKPWLLLSSQDVAHDLETLKKHKVTHILNVAYG------VENA--FPDD-FTYKTISILDLPETDITSYFPECFEFIDE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 112 AlAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR-EIGPNDGFLAQL 170
Cdd:cd14523   75 A-KSQDGVVLVHCNAGVSRSASIVIGYLMATENLSFEDAFSLVKNARpSIRPNPGFMEQL 133
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 32-176 7.87e-31

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: 110.17  E-value: 7.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvNTSASFYEDsgITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14565    3 EILPFLYLGSAYHASRREVLKALGITAVLNVSR-------NCPNHFEDH--FQYKSIPVEDSHNADISSWFEEAIGFIDK 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568976004 112 ALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDR 176
Cdd:cd14565   74 VKA-SGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRSvISPNFNFMGQLLQYESQ 138
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 32-170 1.06e-30

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: 109.57  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDiTQLQKLGITHVLNAAEGrsfmHVNTSasfyeDSGITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14514    3 QITPHLFLSGASAATP-PLLLSRGITCIINATTE----LPDPS-----YPGIEYLRVPVEDSPHADLSPHFDEVADKIHQ 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 112 ALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14514   73 VKR-RGGRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARPiIRPNVGFWRQL 131
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 31-170 7.19e-30

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: 107.45  E-value: 7.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvnTSASFYEDsgITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14519    2 NKILPGLYVGNFRDAKDAEQLRENGITHILSIHD--------SARPLLED--IKYLCIPAADTPEQNISQHFRECINFIH 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIG-PNDGFLAQL 170
Cdd:cd14519   72 EARL-NGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARPCAnPNFGFQRQL 131
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 31-170 5.64e-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: 105.41  E-value: 5.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfMHVNTSASfyeDSGITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14520    2 KLVRPGLYIGNADDAADYLSLREAGITHVLTVDS----EEPIDAPP---VGKLVRKFVPALDEESTDLLSRLDECLDFID 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAHknGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQ-NREIGPNDGFLAQL 170
Cdd:cd14520   75 EGRAE--GAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLREcKPDVKPNDGFLKQL 133
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 51-170 8.28e-29

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: 105.09  E-value: 8.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  51 LQKLGITHVLNAAEGrsfmhvnTSASFYeDSGITYLGIKANDTQEFNLSAYFERATDFIDQAL-----------AHKnGR 119
Cdd:cd14518   22 LKAENITHILSVIPG-------DVPEEY-FKGYEHKQIEIDDVEDENILQHFPETNRFIDSALfgngkdedeekKHG-GA 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568976004 120 VLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREI-GPNDGFLAQL 170
Cdd:cd14518   93 VLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIaEPNDGFMEQL 144
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 30-170 1.84e-28

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: 104.34  E-value: 1.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  30 CNEVVPRVYVGNASVAQ--DITQLQKLGITHVLNAAEgrsfmhvNTSASFYE---DSGITYLGIKANDTQEFNLSAYFER 104
Cdd:cd14522    5 MQEILPGLYLGPYSAAMksKLEVLLKHGITHIVCVRQ-------NIEANFIKpnfPDHFRYLVLDVADNPTENIIRHFPT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 105 ATDFIDQALaHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14522   78 VKEFIDDCL-QTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVQQRRFcINPNEGFVHQL 143
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 33-170 2.11e-27

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: 101.34  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  33 VVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmhvNTSA--SFYEDSgiTYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14568    4 ILPHLYLGSQRDVLDKDLMQRNGISYVLNVS--------NTCPkpDFIPDS--HFLRIPVNDSYCEKLLPWLDKAVEFIE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR-EIGPNDGFLAQL 170
Cdd:cd14568   74 KARA-SNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRpTISPNFNFLGQL 133
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 32-173 1.36e-25

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: 96.86  E-value: 1.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNaaegrsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDq 111
Cdd:cd14641    6 EILPFLFLGSAHHSSRRETLESLGITAVLN---------VSSSCPNYFEGQFQYKSIPVEDSHMADISAWFQEAIDFID- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568976004 112 ALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQL 173
Cdd:cd14641   76 SVKNSGGRVLVHCQAGISRSATICLAYLIQSQRVRLDEAFDFVKQRRGvISPNFSFMGQLLQF 138
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 32-172 1.66e-23

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: 91.13  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvNTSASFYEDsgITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14639    3 EILPFLYLGSAYHASKCEFLANLHITALLNVSR-------RSSEACKGQ--YHYKWIPVEDSHTADISSHFQEAIDFIDC 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568976004 112 aLAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:cd14639   74 -VRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRRSlISPNFGFMGQLLQ 134
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 32-177 3.31e-23

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: 90.48  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNaaegrsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDq 111
Cdd:cd14640    3 EILPFLYLGSAYHAARRDMLDALGITALLN---------VSSDCPNHFEGHYQYKCIPVEDNHKADISSWFMEAIEYID- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 112 ALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDRL 177
Cdd:cd14640   73 SVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRRSiISPNFSFMGQLLQFESQV 139
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 32-170 3.55e-23

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: 90.15  E-value: 3.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmhvNTSASFYEDSgITYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14513    3 KIFDHLYLGSEWNASNLEELQNNGVKYILNVT--------REIDNFFPGR-FTYHNIRVWDEESTNLLPYWNETYRFIKE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 112 ALAHkNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14513   74 ARRK-GSKVLVHCKMGVSRSASTVIAYAMKEYGWSLEQALEHVKERRScIKPNPGFLRQL 132
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 31-170 8.71e-23

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: 89.47  E-value: 8.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNaaegrsfMHvNTSASFYEDsgITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14581    5 NKVLPGLYLGNFKDARDREQLSKNNITHILS-------VH-DSARPMLEG--MTYLCIPAADSPSQNLTQHFKESIKFIH 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14581   75 ECRL-RGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAARScANPNMGFQRQL 134
DSP_DUSP9 cd14644
dual specificity phosphatase domain of dual specificity protein phosphatase 9; Dual ...
 24-177 4.51e-22

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: 87.75  E-value: 4.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  24 SLPSQpcneVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvNTSASFYEDSGITYLGIKANDTQEFNLSAYFE 103
Cdd:cd14644    1 SFPVQ----ILPNLYLGSARDSANLETLAKLGIRYILNVTP-------NLPNFFEKNGDFHYKQIPISDHWSQNLSQFFP 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976004 104 RATDFIDQALAHKNGrVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTV-RQNREIGPNDGFLAQLCQLNDRL 177
Cdd:cd14644   70 EAIEFIDEALSQNCG-VLVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDLVkRKKSNISPNFNFMGQLLDFEKSL 143
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 24-171 1.71e-21

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: 86.94  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  24 SLPSQpcneVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMH----------------------VNTSASFYEDS 81
Cdd:cd14516    5 SLPSR----ILPHLYLGSLNHASNATLLESLGITHIVSVGESPSWFSnlkikyifdfslqdlsnldsnsEGSLWAAEYKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  82 GITYLGIK-----ANDTqefnLSAYFERATDFIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQ 156
Cdd:cd14516   81 LISVLYIHnlkddGIDS----LLPQLTDALDFIQKARL-LGGKTLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRV 155

                        170
                 ....*....|....*...
gi 568976004 157 NRE---IGPNDGFLAQLC 171
Cdd:cd14516  156 RRLniiIQPNLRFFYELF 173
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 31-170 3.61e-21

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: 85.39  E-value: 3.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvnTSASFYEDsgITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14582    6 TKVLPGLYLGNFIDAKDLEQLSRNKITHIISIHE--------SPQPLLQD--ITYLRIPLPDTPEAPIKKHFKECISFIH 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAHkNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIG-PNDGFLAQL 170
Cdd:cd14582   76 QCRLN-GGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRPIAnPNPGFKQQL 135
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 24-172 5.95e-21

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: 85.02  E-value: 5.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  24 SLPSQPCnEVVP-RVYVGNASVAQDITQLQKLGITHVLNAAegrsfmhvNTSASFYEDSGITYLGIKANDTQEFNLSAYF 102
Cdd:cd14517    6 NLKTYPV-EILPgFLYMGNYKQACDKKIQKDLKIKAHINVS--------MDADELFKSGNDQVLHIPVEDSVEADLLSFF 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 103 ERATDFIDQALaHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQ 172
Cdd:cd14517   77 ERACSFIDKHK-NNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNnMRPNRGFVKQLSE 146
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 32-177 1.88e-20

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: 83.58  E-value: 1.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNaaegrsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDq 111
Cdd:cd14638    3 EILPFLYLGSAYHASRKDMLDTLGITALIN---------VSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFID- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 112 ALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDRL 177
Cdd:cd14638   73 SVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSiISPNFSFMGQLLQFESQV 139
DUSP28 cd14574
dual specificity protein phosphatase 28; Dual specificity protein phosphatase 28 (DUSP28), ...
 33-177 1.98e-20

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: 83.29  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  33 VVPRVYVGNASVAQDITQLQKLGITHVLNaaegrsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQA 112
Cdd:cd14574    4 VTDSLFISNARAACNEELLAREGVTLCVN---------VSRQQPFPRAPRVSTLRVPVFDDPAEDLYRHFEQCADAIEAA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568976004 113 lAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDRL 177
Cdd:cd14574   75 -VRRGGKCLVYCKNGRSRSAAVCIAYLMKHRGLSLQDAFQVVKAARPvAEPNPGFWSQLQRYEEEL 139
DSP_DUSP7 cd14643
dual specificity phosphatase domain of dual specificity protein phosphatase 7; Dual ...
 24-170 6.94e-20

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: 81.99  E-value: 6.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  24 SLPSQPCnEVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvNTSASFYEDSGITYLGIKANDTQEFNLSAYFE 103
Cdd:cd14643    1 SQPAFPV-QILPYLYLGCAKDSTNLDVLGKYGIKYILNVTP-------NLPNMFEHDGEFKYKQIPISDHWSQNLSQFFP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976004 104 RATDFIDQALAHKNGrVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTV-RQNREIGPNDGFLAQL 170
Cdd:cd14643   73 EAISFIDEARSKKCG-ILVHCLAGISRSVTVTVAYLMQKLNLSLNDAYDFVkRKKSNISPNFNFMGQL 139
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 31-170 2.23e-19

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: 80.99  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmhVNTSASFYEdsGITYLGIKANDTQEFNLSAYFERATDFId 110
Cdd:cd14573    3 SRITESLYLSNGVAANNRTLLAANRITCVINVS-------LEVANGLPP--GIEYLHVPVADSPDTRLRDYFDPIADKI- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14573   73 HTVEARGGRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRPiIRPNNGFWEQL 133
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 31-170 4.85e-19

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: 79.52  E-value: 4.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfMHVNtsaSFYEDSgITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14571    5 SRIFPYLYLGSEWNAANLEELQRNRVSHILNVT-----REID---NFFPER-FTYMNIRVYDEEATQLLPHWKETHRFIE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QAlAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREI-GPNDGFLAQL 170
Cdd:cd14571   76 AA-RAQGTRVLVHCKMGVSRSASTVIAYAMKQYGWTLEQALRHVRERRPIvQPNPGFLRQL 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
32-177 1.82e-18

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 78.09  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFmhvntSASFYEDSGITYLGIKANDTQEFNLSAyFERATDFIDQ 111
Cdd:COG2453    2 WIIPGLLAGGPLPGGGEADLKREGIDAVVSLTEEEEL-----LLGLLEEAGLEYLHLPIPDFGAPDDEQ-LQEAVDFIDE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 112 ALAhKNGRVLVHCREGYSRSPTLVIAYLmMRQKMDVKSALSTVRQNR-EIGPNDGFLAQLCQLNDRL 177
Cdd:COG2453   76 ALR-EGKKVLVHCRGGIGRTGTVAAAYL-VLLGLSAEEALARVRAARpGAVETPAQRAFLERFAKRL 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 30-172 2.46e-17

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: 74.31  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  30 CNEVVP-RVYVGN---ASVAQDITQLQKLGITHVLNAAEgrsfmhvntsasfyedsgitylgikandtqefnlsAYFERA 105
Cdd:cd14494    1 FNWIDPlRLIAGAlplSPLEADSRFLKQLGVTTIVDLTL-----------------------------------AMVDRF 45

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568976004 106 TDFIDQALAHkNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIG--PNDGFLAQLCQ 172
Cdd:cd14494   46 LEVLDQAEKP-GEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGipQTIEQLDFLIK 113
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 33-180 3.22e-17

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: 75.06  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  33 VVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmHVNTSASFYEDSgiTYLGIKANDTQEFNLSAYFERATDFIDQA 112
Cdd:cd14646    6 ILPHLYLGCQRDVLNKELMQQNGIGYVLNAS------NTCPKPDFIPES--HFLRVPVNDSFCEKILPWLDKSVDFIEKA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568976004 113 LAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR-EIGPNDGFLAQLCQLNDRLAKE 180
Cdd:cd14646   78 KA-SNGRVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRpTISPNFNFLGQLLDFEKKIKNQ 145
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 31-163 1.33e-16

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: 73.38  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  31 NEVVPRVYVGNA-SVAQDITQLQKLGITHVLNAAEGRSFMHVNTSAS----FYEDSGITYLGIKANDTQEFNLSAYFERA 105
Cdd:cd14526    4 SRILPNLIVGSCpQNPEDVDRLKKEGVTAVLNLQTDSDMEYWGVDIDsirkACKESGIRYVRLPIRDFDTEDLRQKLPQA 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568976004 106 TDFIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIGPN 163
Cdd:cd14526   84 VALLYRLLK-NGGTVYVHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPD 140
DSP_DUSP6 cd14642
dual specificity phosphatase domain of dual specificity protein phosphatase 6; Dual ...
 32-170 1.70e-16

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: 73.18  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEgrsfmhvnTSASFYEDSG-ITYLGIKANDTQEFNLSAYFERATDFID 110
Cdd:cd14642    5 EILPYLYLGCAKDSTNLDVLEEFGIKYILNVTP--------NLPNLFENAGeFKYKQIPISDHWSQNLSQFFPEAISFID 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004 111 QALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQL 170
Cdd:cd14642   77 EARG-KNCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSnISPNFNFMGQL 136
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 32-172 2.46e-16

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: 72.18  E-value: 2.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPR-VYVGNASVAQDITQLQKLGITHVLNAaegrsfmhVNTSASFYEDSgITYLGIKANDTQEFNlsayfeRATDFID 110
Cdd:cd18534    3 EILPGfLYLGSYDNASRAELLKAQGITRILNT--------VPDCQNLYKNS-FTYHVLSEEKTVPFA------EAVDFIE 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568976004 111 QALAHKNgRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR-EIGPNDGFLAQLCQ 172
Cdd:cd18534   68 QCRKDKA-RVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRpSINLSPAVAKQLQE 129
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 32-177 3.00e-16

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: 72.59  E-value: 3.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAaegrSFMHVNTSASFYEdsgitYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14572   10 QITPSLYLSRGNVASNRHLLLSRGITCIVNA----TIEIPNFNWPQFE-----YVKVPLADMPHAPISLYFDSVADKIHS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 112 aLAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNRE-IGPNDGFLAQLCQLNDRL 177
Cdd:cd14572   81 -VGRKHGATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRPvIRPNVGFWRQLIDYERKL 146
DSP_slingshot_1 cd14570
dual specificity phosphatase domain of slingshot homolog 1; Dual specificity protein ...
 37-172 4.54e-15

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: 69.33  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  37 VYVGNASVAQDITQLQKLGITHVLNaaegrsfmhVNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQALAHK 116
Cdd:cd14570   11 LYLGSEWNASNLEELQGSGVGYILN---------VTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNDAYHFINKAKKNH 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 117 NgRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIG-PNDGFLAQLCQ 172
Cdd:cd14570   82 S-KCLVHCKMGVSRSASTVIAYAMKEFGWSLEKAYNFVKQKRSITrPNAGFMRQLLE 137
DSP_DUSP8 cd14645
dual specificity phosphatase domain of dual specificity protein phosphatase 8; Dual ...
 22-177 1.26e-14

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: 68.11  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  22 CYSLPSQPCNEVVPRVYVGNASVAQDITQLQKLGITHVLNAAegrsfmHVNTSASFYEDSgiTYLGIKANDTQEFNLSAY 101
Cdd:cd14645    4 CLPVANVGPTRILPHLYLGSQKDVLNKDLMAQNGITYVLNAS------NSCPKPDFICES--HFMRIPVNDNYCEKLLPW 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 102 FERATDFIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR-EIGPNDGFLAQLCQLNDRL 177
Cdd:cd14645   76 LDKSIEFIDKAKV-SNCRVIVHCLAGISRSATIAIAYIMKTMGLSSDDAYRFVKDRRpSISPNFNFLGQLLEYEKSL 151
DSP_slingshot_2 cd14569
dual specificity phosphatase domain of slingshot homolog 2; Dual specificity protein ...
 32-170 4.90e-12

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: 61.19  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  32 EVVPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSfmhvNTSASFYEdsgitYLGIKANDTQEFNLSAYFERATDFIDQ 111
Cdd:cd14569    6 QIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREID----NFFPGLFE-----YHNIRVYDEEATDLLAYWNDTYKFISK 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 112 ALAHkNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREI-GPNDGFLAQL 170
Cdd:cd14569   77 AKKH-GSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYDYVKERRTVtKPNPSFMRQL 135
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 37-158 6.05e-12

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: 61.12  E-value: 6.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  37 VYVGNASVA-QDITQLQKLGITHVLNAAE---GRSFMhvnTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQA 112
Cdd:cd14524    9 VILGALPFRsMTVALVAKENVRGVITMNEeyeTRFFC---NSKEEWKALGVEQLRLPTVDFTGVPSLEDLEKGVDFILKH 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568976004 113 LAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR 158
Cdd:cd14524   86 RE-KGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKR 130
DSP_fungal_SDP1-like cd14521
dual specificity phosphatase domain of fungal dual specificity protein phosphatase SDP1, MSG5, ...
 106-170 9.16e-12

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: 60.80  E-value: 9.16e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568976004 106 TDFIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQ-NREIGPNDGFLAQL 170
Cdd:cd14521   84 TSIIEDATQ-SGKKVLIHCQCGVSRSASLIIAYIMKKLGLSLNDAYDLLKSrSPWIGPNMSLIFQL 148
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 43-158 1.64e-10

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), 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. DUSP23 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 able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 56.90  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  43 SVAQDITQLQKLGITHVLnaaegrSFMHVNTSASFYEDSGITYLGIKAND----TQEfnlsaYFERATDFIDQALAhKNG 118
Cdd:cd14504   16 RLPEHYAYLNENGIRHVV------TLTEEPPPEHSDTCPGLRYHHIPIEDytppTLE-----QIDEFLDIVEEANA-KNE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568976004 119 RVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR 158
Cdd:cd14504   84 AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIR 123
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 103-158 9.63e-10

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: 54.59  E-value: 9.63e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 103 ERATDFIDqALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQKM-DVKSALSTVRQNR 158
Cdd:cd14527   63 ERAVAWIE-ELRAQGGPVLVHCALGYGRSATVVAAWLLAYGRAkSVAEAEALIRAAR 118
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
 33-156 4.62e-08

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 49.83  E-value: 4.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  33 VVPRVYVGNASVAQDITQLQKLGITHVLN---AAEGRSFMHVNTSASFYEDSGITYL-------GIKANDTQEFnlsayf 102
Cdd:COG3453    4 ITDRLSVSGQPTPEDLAALAAAGFKTVINlrpDGEEPDQPAAADEAAAAEAAGLEYVhipvtggAITDEDVEAF------ 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568976004 103 eratdfiDQALAHKNGRVLVHCREGYsRSPTLVIAYLMMRQKMDVKSALSTVRQ 156
Cdd:COG3453   78 -------AAALAAAPGPVLAHCRSGT-RSSALWALYQAGKGGMSPEEALAAAAA 123
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 48-158 1.24e-07

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 50.04  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  48 ITQLQKLGITHVLNAAEgrSFMHVNTSASFYEDSGITYLgikANDTQEFNLSAY-----------FERATDFI---DQAL 113
Cdd:cd14506   32 IEQFKEKGIKTVINLQE--PGEHASCGPGLEPESGFSYL---PEAFMRAGIYFYnfgwkdygvpsLTTILDIVkvmAFAL 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568976004 114 aHKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNR 158
Cdd:cd14506  107 -QEGGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKR 150
PRK12361 PRK12361
hypothetical protein; Provisional
 29-175 6.67e-07

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 48.85  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  29 PCNEVVPRVYVGNASVAQDITQLQKLGITHVLN-AAEgrsFMHVNTSAsfyEDSGITYLGIKANDTQEFNLsAYFERATD 107
Cdd:PRK12361  94 AIQKIDENLYLGCRLFPADLEKLKSNKITAILDvTAE---FDGLDWSL---TEEDIDYLNIPILDHSVPTL-AQLNQAIN 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004 108 FIDQALAhKNGRVLVHCREGYSRSPTLVIAYLMMRQK-MDVKSALSTVRQNRE-IGPNDGFLAQLCQLND 175
Cdd:PRK12361 167 WIHRQVR-ANKSVVVHCALGRGRSVLVLAAYLLCKDPdLTVEEVLQQIKQIRKtARLNKRQLRALEKMLE 235
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 43-158 1.17e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 46.87  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  43 SVAQDITQLQKLGITHVLNAAEGRSFMH--VNTSASFYEDSGITYLGIKANDTQEFNLSAYFERATDFIDQALahKNG-R 119
Cdd:cd14505   31 DLQADLEELKDQGVDDVVTLCTDGELEElgVPDLLEQYQQAGITWHHLPIPDGGVPSDIAQWQELLEELLSAL--ENGkK 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568976004 120 VLVHCREGYSRSPTLVIAYLMMR-QKMDVKSALSTVRQNR 158
Cdd:cd14505  109 VLIHCKGGLGRTGLIAACLLLELgDTLDPEQAIAAVRALR 148
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 115-172 2.32e-04

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 40.33  E-value: 2.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568976004 115 HKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSTVRQNREIG-PNDGFLAQLCQ 172
Cdd:cd14502  109 NPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGiYKPHYIDELYR 167
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 103-158 3.94e-04

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 39.96  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976004 103 ERATDFID------QALAHKNGRVLVHCREGYSRSPTLVIAYLMMRQ-----KMDVKSALSTVRQNR 158
Cdd:cd00047  119 SSPEDLLAlvrrvrKEARKPNGPIVVHCSAGVGRTGTFIAIDILLERleaegEVDVFEIVKALRKQR 185
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
117-158 3.94e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 38.49  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568976004   117 NGRVLVHCREGYSRSPTLVIAYLMMRQ------KMDVKSALSTVRQNR 158
Cdd:smart00404  39 SGPVVVHCSAGVGRTGTFVAIDILLQQleaeagEVDIFDTVKELRSQR 86
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 117-158 3.94e-04

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 38.49  E-value: 3.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568976004   117 NGRVLVHCREGYSRSPTLVIAYLMMRQ------KMDVKSALSTVRQNR 158
Cdd:smart00012  39 SGPVVVHCSAGVGRTGTFVAIDILLQQleaeagEVDIFDTVKELRSQR 86
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
107-158 1.39e-03

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 38.38  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976004  107 DFIDQALAHK----NGRVLVHCREGYSRSPTLVIAYLMMRQ-----KMDVKSALSTVRQNR 158
Cdd:pfam00102 155 DLLRKVRKSSldgrSGPIVVHCSAGIGRTGTFIAIDIALQQleaegEVDIFQIVKELRSQR 215
PTP-bact cd14503
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ...
 35-156 1.87e-03

bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown.


Pssm-ID: 350353 [Multi-domain]  Cd Length: 136  Bit Score: 37.23  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976004  35 PRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYEDSGITYLGIK---ANDTQEfNLSAYFEratdFIDQ 111
Cdd:cd14503    7 DRLATAGQPTPEQFAALAAAGFKTVINLRPDGEENALPNEAAAVTAAGMEYVHIPvdwDNPTPE-DVERFFE----VMDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568976004 112 ALAHKngrVLVHCREGYsRSPTLVIAYLMMRQKMDVKSALSTVRQ 156
Cdd:cd14503   82 AQGKP---VLVHCASNM-RASAFWYLYRALDGGVSEEEAIQLMRS 122
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 108-161 4.63e-03

N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans.


Pssm-ID: 350502  Cd Length: 167  Bit Score: 36.50  E-value: 4.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568976004 108 FIDQalaHKNGRVLVHCREGYSRSPTLVIAYLMmrQKMD--VKSALSTVRQNREIG 161
Cdd:cd17664  105 FIEK---NPLELIGVHCTHGFNRTGFLICAYLV--EKMDwsVEAAVATFAQARPPG 155
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 109-173 6.39e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 36.02  E-value: 6.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568976004 109 IDQALAHKNGRV-LVHCREGYSRSPTLVIAYLMMR-QKMDVKSALSTVRQNReigPNDGFLA--QLCQL 173
Cdd:cd14497   86 IDSWLSEDPNNVaVVHCKAGKGRTGTVICAYLLYYgQYSTADEALEYFAKKR---FKEGLPGvtIPSQL 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH