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Conserved domains on  [gi|71043696|ref|NP_001020821|]
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RNA/RNP complex-1-interacting phosphatase [Rattus norvegicus]

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 ...
 32-199 2.78e-105

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: 304.97  E-value: 2.78e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  32 RWKDYLPVGQRMPGTRFIAFKVPLQKKFEAKLMPEECFSPLDLFNKIQEQNEELGLIIDLTYTQRYYKVEDLPKTISYIK 111
Cdd:cd17665   1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 112 ILTV-GHQVPDSGTIFQFKSAVKEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIER 190
Cdd:cd17665  81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160


                ....*....
gi 71043696 191 QNYIENLQK 199
Cdd:cd17665 161 ENYLEDLLK 169
 
Name Accession Description Interval E-value
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 32-199 2.78e-105

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: 304.97  E-value: 2.78e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  32 RWKDYLPVGQRMPGTRFIAFKVPLQKKFEAKLMPEECFSPLDLFNKIQEQNEELGLIIDLTYTQRYYKVEDLPKTISYIK 111
Cdd:cd17665   1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 112 ILTV-GHQVPDSGTIFQFKSAVKEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIER 190
Cdd:cd17665  81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160


                ....*....
gi 71043696 191 QNYIENLQK 199
Cdd:cd17665 161 ENYLEDLLK 169
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 77-194 5.27e-13

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: 64.98  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696    77 KIQEQNEELGLIIDLTYTQRYYKVEDLpktisYIKIltvghQVPDSGT--IFQFKSAVKEFLKRNKNNDKLIGVHCTHGL 154
Cdd:pfam00782  11 DAFLSKLGITAVINVTREVDLYNSGIL-----YLRI-----PVEDNHEtnISKYLEEAVEFIDDARQKGGKVLVHCQAGI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 71043696   155 NRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIERQNYI 194
Cdd:pfam00782  81 SRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFK 120
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
79-198 4.56e-12

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 62.69  E-value: 4.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696     79 QEQNEELG--LIIDLTYTQRYYKvedlPKTISYIKIltvghQVPDSGT--IFQFKSAVKEFLKRNKNNDKLIGVHCTHGL 154
Cdd:smart00195  19 LALLKKLGitHVINVTNEVPNYN----GSDFTYLGV-----PIDDNTEtkISPYFPEAVEFIEDAESKGGKVLVHCQAGV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 71043696    155 NRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIERQNYIENLQ 198
Cdd:smart00195  90 SRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLI 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
81-201 3.12e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  81 QNEELGLIIDLTYTQRYYKVEDLPKTISYIKILTVGHQVPDsgtIFQFKSAVKEFLKRNKNNDKLIgVHCTHGLNRTGYL 160
Cdd:COG2453  22 KREGIDAVVSLTEEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDFIDEALREGKKVL-VHCRGGIGRTGTV 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71043696 161 ICRYLIdVEGMRPDDAIELFNRCRGHCIE---RQNYIENLQKRR 201
Cdd:COG2453  98 AAAYLV-LLGLSAEEALARVRAARPGAVEtpaQRAFLERFAKRL 140
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 133-206 9.98e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 45.01  E-value: 9.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71043696  133 KEFLKRNKNNDKlIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIErQNYIENLQKRRVRKNQ 206
Cdd:PTZ00242  89 QEFAKQSTPPET-IAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKRKGAIN-QTQLQFLKKYKPRKKA 160
 
Name Accession Description Interval E-value
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 32-199 2.78e-105

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: 304.97  E-value: 2.78e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  32 RWKDYLPVGQRMPGTRFIAFKVPLQKKFEAKLMPEECFSPLDLFNKIQEQNEELGLIIDLTYTQRYYKVEDLPKTISYIK 111
Cdd:cd17665   1 RWIDYLPVGQRIPGTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 112 ILTV-GHQVPDSGTIFQFKSAVKEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIER 190
Cdd:cd17665  81 KITCpGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160


                ....*....
gi 71043696 191 QNYIENLQK 199
Cdd:cd17665 161 ENYLEDLLK 169
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 32-199 4.42e-67

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: 207.51  E-value: 4.42e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  32 RWKDYLPVGQRMPGTRFIAFKVPLQKKFEAKLMPEECFSPLDLFNKiQEQNEELGLIIDLTYTQRYYKVEDLPK-TISYI 110
Cdd:cd14502   1 KWLDCPPVGQPVGPTRFIPMKTPLSDDYEHLFAPEIRFTPSALAEK-FRQDRKVGLVIDLTNTDRYYDPNDLDDdGYVYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 111 KILTVGHQVPDSGTIFQFKSAVKEFLKRNkNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIER 190
Cdd:cd14502  80 KKVCVRKEPPDAEEVNKFIELVDKFLAED-NPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIYK 158


                ....*....
gi 71043696 191 QNYIENLQK 199
Cdd:cd14502 159 PHYIDELYR 167
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 32-197 3.83e-37

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: 130.88  E-value: 3.83e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  32 RWKDYLPVGQRMPGtRFIAFKVPLQKKFEAKlMPEEC-FSPLDLFNKIQEQNEELGLIIDLTYTQRYYKVEDLPK-TISY 109
Cdd:cd17664   1 RWLNCPRKGQPVAG-KFLPFKTPLGPRYDDQ-VPEENrFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKeGCKY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 110 IKILTVGH-QVPDSGTIFQFKSAVKEFLKRNKNndKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCI 188
Cdd:cd17664  79 IKLQCKGHgECPSPEQTETFIRLCENFIEKNPL--ELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGI 156


                ....*....
gi 71043696 189 ERQNYIENL 197
Cdd:cd17664 157 YKGDYLKEL 165
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 77-194 5.27e-13

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: 64.98  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696    77 KIQEQNEELGLIIDLTYTQRYYKVEDLpktisYIKIltvghQVPDSGT--IFQFKSAVKEFLKRNKNNDKLIGVHCTHGL 154
Cdd:pfam00782  11 DAFLSKLGITAVINVTREVDLYNSGIL-----YLRI-----PVEDNHEtnISKYLEEAVEFIDDARQKGGKVLVHCQAGI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 71043696   155 NRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIERQNYI 194
Cdd:pfam00782  81 SRSATLIIAYLMKTRNLSLNEAYSFVKERRPGISPNFGFK 120
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
79-198 4.56e-12

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 62.69  E-value: 4.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696     79 QEQNEELG--LIIDLTYTQRYYKvedlPKTISYIKIltvghQVPDSGT--IFQFKSAVKEFLKRNKNNDKLIGVHCTHGL 154
Cdd:smart00195  19 LALLKKLGitHVINVTNEVPNYN----GSDFTYLGV-----PIDDNTEtkISPYFPEAVEFIEDAESKGGKVLVHCQAGV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 71043696    155 NRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIERQNYIENLQ 198
Cdd:smart00195  90 SRSATLIIAYLMKTRNMSLNDAYDFVKDRRPIISPNFGFLRQLI 133
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
81-201 3.12e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  81 QNEELGLIIDLTYTQRYYKVEDLPKTISYIKILTVGHQVPDsgtIFQFKSAVKEFLKRNKNNDKLIgVHCTHGLNRTGYL 160
Cdd:COG2453  22 KREGIDAVVSLTEEEELLLGLLEEAGLEYLHLPIPDFGAPD---DEQLQEAVDFIDEALREGKKVL-VHCRGGIGRTGTV 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71043696 161 ICRYLIdVEGMRPDDAIELFNRCRGHCIE---RQNYIENLQKRR 201
Cdd:COG2453  98 AAAYLV-LLGLSAEEALARVRAARPGAVEtpaQRAFLERFAKRL 140
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 85-190 2.75e-08

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: 51.89  E-value: 2.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  85 LGLIIDLTYTQRYYKVEDLPKtISYIKILTVGHQVPdsgTIFQFKSAVKEFLKRNKNNDKlIGVHCTHGLNRTGYLICRY 164
Cdd:cd14504  29 IRHVVTLTEEPPPEHSDTCPG-LRYHHIPIEDYTPP---TLEQIDEFLDIVEEANAKNEA-VLVHCLAGKGRTGTMLACY 103

                        90       100
                ....*....|....*....|....*.
gi 71043696 165 LIDVEGMRPDDAIELFNRCRGHCIER 190
Cdd:cd14504 104 LVKTGKISAVDAINEIRRIRPGSIET 129
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 134-186 3.39e-08

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: 51.20  E-value: 3.39e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71043696 134 EFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGH 186
Cdd:cd14494  47 EVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPG 99
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 96-194 1.04e-07

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: 50.72  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696  96 RYYKVEDLPKTISYIKILTVGHQVPDSGT---IFQFKSAVKEFLKRNKNNDKLIgVHCTHGLNRTGYLICRYLIDVEG-M 171
Cdd:cd14505  57 EELGVPDLLEQYQQAGITWHHLPIPDGGVpsdIAQWQELLEELLSALENGKKVL-IHCKGGLGRTGLIAACLLLELGDtL 135

                        90       100
                ....*....|....*....|....*.
gi 71043696 172 RPDDAIELFNRCRGHCIE--RQ-NYI 194
Cdd:cd14505 136 DPEQAIAAVRALRPGAIQtpKQeNFL 161
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 146-184 1.34e-06

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: 48.11  E-value: 1.34e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 71043696 146 IGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCR 184
Cdd:cd14506 112 VAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKR 150
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 120-201 3.14e-06

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 46.45  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 120 PDSGTIFQFKSAVKEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVeGMRPDDAIELFNRCRGHCI-ERQ-NYIENL 197
Cdd:cd14500  72 PPDDVVDDWLDLLKTRFKEEGKPGACIAVHCVAGLGRAPVLVAIALIEL-GMKPEDAVEFIRKKRRGAInSKQlQFLEKY 150


                ....
gi 71043696 198 QKRR 201
Cdd:cd14500 151 KPKK 154
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
117-166 4.95e-06

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 44.66  E-value: 4.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 71043696    117 HQVPDSGT-IFQFKSAVKEFLKRNKNNdKLIGVHCTHGLNRTGYLICRYLI 166
Cdd:smart00404  13 HGVPESPDsILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDIL 62
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 117-166 4.95e-06

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: 44.66  E-value: 4.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 71043696    117 HQVPDSGT-IFQFKSAVKEFLKRNKNNdKLIGVHCTHGLNRTGYLICRYLI 166
Cdd:smart00012  13 HGVPESPDsILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDIL 62
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 133-206 9.98e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 45.01  E-value: 9.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71043696  133 KEFLKRNKNNDKlIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRGHCIErQNYIENLQKRRVRKNQ 206
Cdd:PTZ00242  89 QEFAKQSTPPET-IAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKRKGAIN-QTQLQFLKKYKPRKKA 160
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 117-167 1.26e-05

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: 45.05  E-value: 1.26e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71043696 117 HQVPDSGTIFQFKSAVKEFLKRNKNNdkLIGVHCTHGLNRTGYLICRYLID 167
Cdd:cd14510  84 HNVPTLDEMLSFTAEVREWMAADPKN--VVAIHCKGGKGRTGTMVCAWLIY 132
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 132-200 1.84e-05

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: 44.37  E-value: 1.84e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71043696 132 VKEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIElFNR-CRGHCI--ERQNYIENLQKR 200
Cdd:cd14499  98 VKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIA-WLRiCRPGSVigPQQQFLEEKEAR 168
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 117-184 2.43e-05

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: 43.73  E-value: 2.43e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71043696 117 HQVPDSGTIFQFKSAVKEFLKRNKNNdkLIGVHCTHGLNRTGYLICRYLIDVEGMR-PDDAIELFNRCR 184
Cdd:cd14509  70 HNPPPLELIKPFCEDVDEWLKEDEKN--VAAVHCKAGKGRTGVMICCYLLYLGKFPsAKEALDFYGAKR 136
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 116-184 2.98e-05

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: 43.72  E-value: 2.98e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 116 GHQVPDSGTIFQFKSAVKEFLKRNKNNdkLIGVHCTHGLNRTGYLICRYLI-DVEGMRPDDAIELFNRCR 184
Cdd:cd14497  70 DHHPPPLGLLLEIVDDIDSWLSEDPNN--VAVVHCKAGKGRTGTVICAYLLyYGQYSTADEALEYFAKKR 137
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 101-199 3.01e-04

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: 40.22  E-value: 3.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 101 EDLPKTISYIKILTVghQVPDSGT---IFQFKSAVkEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAI 177
Cdd:cd14498  37 PPPNKFPDGIKYLRI--PIEDSPDediLSHFEEAI-EFIEEALKKGGKVLVHCQAGVSRSATIVIAYLMKKYGWSLEEAL 113

                        90       100
                ....*....|....*....|..
gi 71043696 178 ELFNRCRGHCIERQNYIENLQK 199
Cdd:cd14498 114 ELVKSRRPIISPNPGFLKQLKE 135
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 107-199 7.56e-04

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: 39.17  E-value: 7.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043696 107 ISYIKILTVGH-QVPDSGTIFQfksAVkEFLKRNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRPDDAIELFNRCRG 185
Cdd:cd14524  56 VEQLRLPTVDFtGVPSLEDLEK---GV-DFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRP 131

                        90
                ....*....|....
gi 71043696 186 HCIERQNYIENLQK 199
Cdd:cd14524 132 HILLRLSQREVLEE 145
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 129-178 8.49e-04

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: 39.28  E-value: 8.49e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71043696 129 KSAVKEFLK--RNKNNDKLIGVHCTHGLNRTGYLICRYLIDVEGMRpDDAIE 178
Cdd:cd14529  73 ESDVQSFLLimDLKLAPGPVLIHCKHGKDRTGLVSALYRIVYGGSK-EEANE 123
 
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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