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Conserved domains on  [gi|453231824|ref|NP_495959|]
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RNA/RNP complex-1-interacting phosphatase homolog [Caenorhabditis elegans]

Protein Classification

RNA/RNP complex-1-interacting phosphatase family protein( domain architecture ID 13026143)

RNA/RNP complex-1-interacting phosphatase family protein similar to human RNA/RNP complex-1-interacting phosphatase DUSP11 that possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity

EC:  3.1.3.-
Gene Ontology:  GO:0016791
PubMed:  27514797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 28-199 2.77e-92

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


:

Pssm-ID: 350503  Cd Length: 169  Bit Score: 268.38  E-value: 2.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  28 RWNIYDNVGRDIDGTRFVPFKTPLDSSFFDgkNMPVELQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKTEWADHGVK 107
Cdd:cd17665    1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFA--NLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 108 YLKLNCPGHEVnEREDLVQDFINAVKEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHP 187
Cdd:cd17665   79 YKKITCPGHQV-PDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHP 157

                        170
                 ....*....|..
gi 453231824 188 MEREHYKKSLYE 199
Cdd:cd17665  158 IERENYLEDLLK 169
 
Name Accession Description Interval E-value
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 28-199 2.77e-92

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 268.38  E-value: 2.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  28 RWNIYDNVGRDIDGTRFVPFKTPLDSSFFDgkNMPVELQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKTEWADHGVK 107
Cdd:cd17665    1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFA--NLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 108 YLKLNCPGHEVnEREDLVQDFINAVKEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHP 187
Cdd:cd17665   79 YKKITCPGHQV-PDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHP 157

                        170
                 ....*....|..
gi 453231824 188 MEREHYKKSLYE 199
Cdd:cd17665  158 IERENYLEDLLK 169
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 65-201 2.10e-37

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: 127.38  E-value: 2.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824   65 LQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKtewadhgvKYLKLNCPGHEvnEREDLVQDFINAVKEFVNDKENDGK 144
Cdd:pfam00782   1 LYLGSKPTASDAFLSKLGITAVINVTREVDLYNS--------GILYLRIPVED--NHETNISKYLEEAVEFIDDARQKGG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 453231824  145 LIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHPMEREHYKKSLYEAE 201
Cdd:pfam00782  71 KVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
59-202 1.51e-34

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 120.08  E-value: 1.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824    59 KNMPVELQFGVKTLIS-LAQQANKQIGLVIDLTNTDRyykktewADHGVKYLKLNCPGHEvnEREDLVQDFINAVKEFVN 137
Cdd:smart00195   2 SEILPHLYLGSYSDALnLALLKKLGITHVINVTNEVP-------NYNGSDFTYLGVPIDD--NTETKISPYFPEAVEFIE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 453231824   138 DKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHPMEREHYKKSLYEAER 202
Cdd:smart00195  73 DAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYER 137
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
79-179 9.65e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 52.28  E-value: 9.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  79 ANKQIGLVIDLTnTDRYYKKTEWADHGVKYLKLNCPGHEVNEREDLVQdfinaVKEFVNDKENDGKLIGVHCTHGLNRTG 158
Cdd:COG2453   22 KREGIDAVVSLT-EEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQE-----AVDFIDEALREGKKVLVHCRGGIGRTG 95

                         90       100
                 ....*....|....*....|.
gi 453231824 159 YLICRYMIdVDNYSASDAISM 179
Cdd:COG2453   96 TVAAAYLV-LLGLSAEEALAR 115
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 123-177 1.69e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 38.08  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 453231824 123 DLVQDFINAVKEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAI 177
Cdd:PTZ00242  78 AVIDNWLRLLDQEFAKQSTPPETIAVHCVAGLGRAPILVALALVEYGGMEPLDAV 132
 
Name Accession Description Interval E-value
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 28-199 2.77e-92

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 268.38  E-value: 2.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  28 RWNIYDNVGRDIDGTRFVPFKTPLDSSFFDgkNMPVELQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKTEWADHGVK 107
Cdd:cd17665    1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFA--NLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 108 YLKLNCPGHEVnEREDLVQDFINAVKEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHP 187
Cdd:cd17665   79 YKKITCPGHQV-PDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHP 157

                        170
                 ....*....|..
gi 453231824 188 MEREHYKKSLYE 199
Cdd:cd17665  158 IERENYLEDLLK 169
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 43-198 1.73e-44

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: 146.67  E-value: 1.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  43 RFVPFKTPLDSSFFDgkNMPVELQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKTEWADHGVKYLKLNCPGHEVNERE 122
Cdd:cd17664   15 KFLPFKTPLGPRYDD--QVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSP 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 453231824 123 DLVQDFINAVKEFVNdkENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHPMEREHYKKSLY 198
Cdd:cd17664   93 EQTETFIRLCENFIE--KNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGDYLKELF 166
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 28-199 3.70e-43

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: 143.18  E-value: 3.70e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  28 RWNIYDNVGRDIDGTRFVPFKTPLDSSFFDgknmpvelQFGVKTLIS---LAQQ--ANKQIGLVIDLTNTDRYYKKTEWA 102
Cdd:cd14502    1 KWLDCPPVGQPVGPTRFIPMKTPLSDDYEH--------LFAPEIRFTpsaLAEKfrQDRKVGLVIDLTNTDRYYDPNDLD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 103 DHGVKYLKLNCPGHEVNEREDlVQDFINAVKEFVNDKENDgKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEY 182
Cdd:cd14502   73 DDGYVYYKKVCVRKEPPDAEE-VNKFIELVDKFLAEDNPD-KLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQ 150

                        170
                 ....*....|....*..
gi 453231824 183 YRGHPMEREHYKKSLYE 199
Cdd:cd14502  151 ARPPGIYKPHYIDELYR 167
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 65-201 2.10e-37

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: 127.38  E-value: 2.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824   65 LQFGVKTLISLAQQANKQIGLVIDLTNTDRYYKKtewadhgvKYLKLNCPGHEvnEREDLVQDFINAVKEFVNDKENDGK 144
Cdd:pfam00782   1 LYLGSKPTASDAFLSKLGITAVINVTREVDLYNS--------GILYLRIPVED--NHETNISKYLEEAVEFIDDARQKGG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 453231824  145 LIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHPMEREHYKKSLYEAE 201
Cdd:pfam00782  71 KVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFKRQLLEYE 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
59-202 1.51e-34

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 120.08  E-value: 1.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824    59 KNMPVELQFGVKTLIS-LAQQANKQIGLVIDLTNTDRyykktewADHGVKYLKLNCPGHEvnEREDLVQDFINAVKEFVN 137
Cdd:smart00195   2 SEILPHLYLGSYSDALnLALLKKLGITHVINVTNEVP-------NYNGSDFTYLGVPIDD--NTETKISPYFPEAVEFIE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 453231824   138 DKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRGHPMEREHYKKSLYEAER 202
Cdd:smart00195  73 DAESKGGKVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLIEYER 137
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
92-200 5.11e-13

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 63.15  E-value: 5.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824    92 TDRYYKKTEWADHGVkylklncpghevNEREDLVQDFINAVKEFVNDKENDGKLIgVHCTHGLNRTGYLICRYMIDVDNY 171
Cdd:smart00404   1 TVKHYHYTGWPDHGV------------PESPDSILELLRAVKKNLNQSESSGPVV-VHCSAGVGRTGTFVAIDILLQQLE 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 453231824   172 SASDAISMFEY------YRGHPMEREHYKKSLYEA 200
Cdd:smart00404  68 AEAGEVDIFDTvkelrsQRPGMVQTEEQYLFLYRA 102
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 92-200 5.11e-13

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: 63.15  E-value: 5.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824    92 TDRYYKKTEWADHGVkylklncpghevNEREDLVQDFINAVKEFVNDKENDGKLIgVHCTHGLNRTGYLICRYMIDVDNY 171
Cdd:smart00012   1 TVKHYHYTGWPDHGV------------PESPDSILELLRAVKKNLNQSESSGPVV-VHCSAGVGRTGTFVAIDILLQQLE 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 453231824   172 SASDAISMFEY------YRGHPMEREHYKKSLYEA 200
Cdd:smart00012  68 AEAGEVDIFDTvkelrsQRPGMVQTEEQYLFLYRA 102
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 106-189 1.26e-09

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: 54.28  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 106 VKYLKLNCPGHEVNEREDLVQDFInavkEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAISMFEYYRG 185
Cdd:cd14494   23 SRFLKQLGVTTIVDLTLAMVDRFL----EVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRP 98


                 ....
gi 453231824 186 HPME 189
Cdd:cd14494   99 GGIP 102
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
79-179 9.65e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 52.28  E-value: 9.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  79 ANKQIGLVIDLTnTDRYYKKTEWADHGVKYLKLNCPGHEVNEREDLVQdfinaVKEFVNDKENDGKLIGVHCTHGLNRTG 158
Cdd:COG2453   22 KREGIDAVVSLT-EEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQE-----AVDFIDEALREGKKVLVHCRGGIGRTG 95

                         90       100
                 ....*....|....*....|.
gi 453231824 159 YLICRYMIdVDNYSASDAISM 179
Cdd:COG2453   96 TVAAAYLV-LLGLSAEEALAR 115
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 43-177 4.75e-08

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 50.91  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  43 RFVPFKTPLDSSffdgKNMPVELQFGVKTLISLAQQANkqIGLVIDLTNTDryYKKTEWADHGVKYLKL-----NCPghe 117
Cdd:cd14499   25 KFLAFSGPHDTR----KDENGYPTHTPEDYIPYFKKLG--VTTVVRLNKKL--YDAKRFTDAGIRHYDLyfpdgSTP--- 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824 118 vneREDLVQDFINAVkefvndkENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAI 177
Cdd:cd14499   94 ---SDDIVKKFLDIC-------ENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAI 143
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 82-177 1.77e-06

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: 46.12  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  82 QIGLVIDLTntDRYYKKTEWADHGVKYLKLNCPGHEVNEREDLVQdFInavkEFVNDKENDGKLIGVHCTHGLNRTGYLI 161
Cdd:cd14504   28 GIRHVVTLT--EEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQIDE-FL----DIVEEANAKNEAVLVHCLAGKGRTGTML 100

                         90
                 ....*....|....*.
gi 453231824 162 CRYMIDVDNYSASDAI 177
Cdd:cd14504  101 ACYLVKTGKISAVDAI 116
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 101-177 5.53e-05

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: 42.72  E-value: 5.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 453231824 101 WADHGVKYLKLNCpghevnereDLVQDFINAVKEfvndkendGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAI 177
Cdd:cd14506   84 WKDYGVPSLTTIL---------DIVKVMAFALQE--------GGKVAVHCHAGLGRTGVLIACYLVYALRMSADQAI 143
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 123-180 1.36e-04

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 41.03  E-value: 1.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 453231824 123 DLVQDFINAVKEFVndKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNY-SASDAISMF 180
Cdd:cd14509   76 ELIKPFCEDVDEWL--KEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFpSAKEALDFY 132
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 94-161 2.68e-04

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 41.06  E-value: 2.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453231824  94 RYYKKTEWADHGVKylklncpghevNEREDLVQdFINAVKEFVNDKENDGKLIgVHCTHGLNRTGYLI 161
Cdd:cd14617  131 RHFHYTVWPDHGVP-----------ETTQSLIQ-FVRTVRDYINRTPGSGPTV-VHCSAGVGRTGTFI 185
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 116-180 4.86e-04

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 39.65  E-value: 4.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 453231824 116 HEVNEREDLVqDFINAVKEFVN-DKENdgkLIGVHCTHGLNRTGYLICRYMIDVDNY-SASDAISMF 180
Cdd:cd14510   84 HNVPTLDEML-SFTAEVREWMAaDPKN---VVAIHCKGGKGRTGTMVCAWLIYSGQFeSAKEALEYF 146
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 99-162 7.76e-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: 39.19  E-value: 7.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 453231824  99 TEWADHGVkylklncPGHEVNeredlVQDFINAVKEFVNDkeNDGKLIgVHCTHGLNRTGYLIC 162
Cdd:cd00047  110 TGWPDHGV-------PSSPED-----LLALVRRVRKEARK--PNGPIV-VHCSAGVGRTGTFIA 158
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 94-170 1.44e-03

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 38.64  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  94 RYYKKTEWADHGVKylklncpghevnEREDLVQDFINAVKEFVNDKENDGKLIgVHCTHGLNRTGYLIC----RYMIDVD 169
Cdd:cd14615  128 RHFHFTSWPDHGVP------------ETTDLLINFRHLVREYMKQNPPNSPIL-VHCSAGVGRTGTFIAidrlIYQIENE 194


                 .
gi 453231824 170 N 170
Cdd:cd14615  195 N 195
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 123-177 1.69e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 38.08  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 453231824 123 DLVQDFINAVKEFVNDKENDGKLIGVHCTHGLNRTGYLICRYMIDVDNYSASDAI 177
Cdd:PTZ00242  78 AVIDNWLRLLDQEFAKQSTPPETIAVHCVAGLGRAPILVALALVEYGGMEPLDAV 132
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 80-179 1.79e-03

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: 37.53  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  80 NKQIGLVIDLTNTDryykKTEWADHGVKYLKLNCPGhevNEREDLVQDFINAVkEFVNDKENDGKLIGVHCTHGLNRTGY 159
Cdd:cd14498   24 KLGITHILNVAGEP----PPNKFPDGIKYLRIPIED---SPDEDILSHFEEAI-EFIEEALKKGGKVLVHCQAGVSRSAT 95

                         90       100
                 ....*....|....*....|
gi 453231824 160 LICRYMIDVDNYSASDAISM 179
Cdd:cd14498   96 IVIAYLMKKYGWSLEEALEL 115
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 90-161 1.83e-03

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 38.33  E-value: 1.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 453231824  90 TNTDRYYKKTEWADHGVKylklncpghevnEREDLVQDFINAVKEFVNDKENDGKLIgVHCTHGLNRTGYLI 161
Cdd:cd14619  126 TLSVRHFHFTAWPDHGVP------------SSTDTLLAFRRLLRQWLDQTMSGGPTV-VHCSAGVGRTGTLI 184
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 82-161 1.95e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 37.74  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453231824  82 QIGLVIDLTNTDRYYKKTEWADH--GVKYLKLNCPGHEVNEREDlvqdfiNAVKEFVNDKENDGKLIgVHCTHGLNRTG- 158
Cdd:cd14529   33 GIKTVIDLRGADERAASEEAAAKidGVKYVNLPLSATRPTESDV------QSFLLIMDLKLAPGPVL-IHCKHGKDRTGl 105


                 ....*..
gi 453231824 159 ----YLI 161
Cdd:cd14529  106 vsalYRI 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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