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Conserved domains on  [gi|2217363399|ref|XP_047275398|]
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mRNA-capping enzyme isoform X1 [Homo sapiens]

Protein Classification

dual specificity protein phosphatase family protein( domain architecture ID 13026128)

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

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List of domain hits

 Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 9-175 4.53e-128

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: 372.40  E-value: 4.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  89 LQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 2217363399 169 YLKELFR 175
Cdd:cd17664   161 YLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 248-461 3.10e-103

Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues.


:

Pssm-ID: 185706 [Multi-domain]  Cd Length: 215  Bit Score: 310.71  E-value: 3.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 327 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399 407 PFSVRNKPFFDICTSRKLLEGNFAKeVSHEMDGLIFQPTG-KYKPGRCDDILKWKP 461
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKIIPK-LPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
 
Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 9-175 4.53e-128

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: 372.40  E-value: 4.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  89 LQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 2217363399 169 YLKELFR 175
Cdd:cd17664   161 YLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 248-461 3.10e-103

Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues.


Pssm-ID: 185706 [Multi-domain]  Cd Length: 215  Bit Score: 310.71  E-value: 3.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 327 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399 407 PFSVRNKPFFDICTSRKLLEGNFAKeVSHEMDGLIFQPTG-KYKPGRCDDILKWKP 461
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKIIPK-LPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 272-460 5.35e-99

mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain of the mRNA capping enzyme.


Pssm-ID: 396068 [Multi-domain]  Cd Length: 194  Bit Score: 299.32  E-value: 5.35e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 272 QPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 348
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 349 DRVNGQ-AVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEG 427
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKLLGN 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217363399 428 NFAKEVSHEMDGLIFQPTG-KYKPGRCDDILKWK 460
Cdd:pfam01331 161 KFIPNLSHESDGLIFQPVDtPYVAGRCSDLLKWK 194
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
268-473 4.41e-30

mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 122.33  E-value: 4.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 268 FPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 338
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 339 NTLLDGEMIIDRVNGQAVP--RYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKpff 416
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVK--- 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363399 417 DICTSRKLLEgnFAK---EVSHEMDGLIFQPTGK-YKPGRCDDILKWKPPSLNSVDFRLKI 473
Cdd:COG5226   199 QMLKSYGFWK--IYKkipELKHGNDGLIFTPADEpYSVGKDGALLKWKPASLNTIDFRLVL 257
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 47-143 5.73e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 49.64  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  47 PSMLSNYLKSLKvKMGL--LVDLTNTSrfYDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERN-PPELI 122
Cdd:PTZ00242   26 PSNLPLYIKELQ-RYNVthLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETI 101

                          90       100
                  ....*....|....*....|.
gi 2217363399 123 GVHCTHGFNRTGFLICAFLVE 143
Cdd:PTZ00242  102 AVHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 58-161 8.47e-06

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: 45.33  E-value: 8.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  58 KVKMGLLVDLTNTsrfydrNDIEKEGIKYIKlqckghgeCPTTENTET-----------FIRLCERFNERnppelIGVHC 126
Cdd:pfam00782  16 KLGITAVINVTRE------VDLYNSGILYLR--------IPVEDNHETniskyleeaveFIDDARQKGGK-----VLVHC 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217363399 127 THGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
64-161 3.31e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  64 LVDLTnTSRFYDRNDIEKEGIKYIKLQCKGHGeCPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVE 143
Cdd:COG2453    29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVL 104

                          90
                  ....*....|....*...
gi 2217363399 144 KmDWSIEAAVATFAQARP 161
Cdd:COG2453   105 L-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
106-161 4.54e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 4.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399  106 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:smart00195  70 FIEDAESKGGK-----VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
 
Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 9-175 4.53e-128

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: 372.40  E-value: 4.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  89 LQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 2217363399 169 YLKELFR 175
Cdd:cd17664   161 YLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 248-461 3.10e-103

Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues.


Pssm-ID: 185706 [Multi-domain]  Cd Length: 215  Bit Score: 310.71  E-value: 3.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 327 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399 407 PFSVRNKPFFDICTSRKLLEGNFAKeVSHEMDGLIFQPTG-KYKPGRCDDILKWKP 461
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKIIPK-LPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 272-460 5.35e-99

mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain of the mRNA capping enzyme.


Pssm-ID: 396068 [Multi-domain]  Cd Length: 194  Bit Score: 299.32  E-value: 5.35e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 272 QPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 348
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 349 DRVNGQ-AVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEG 427
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKLLGN 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217363399 428 NFAKEVSHEMDGLIFQPTG-KYKPGRCDDILKWK 460
Cdd:pfam01331 161 KFIPNLSHESDGLIFQPVDtPYVAGRCSDLLKWK 194
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 9-175 2.10e-73

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: 231.78  E-value: 2.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399   9 RWLNCPRRGQPVA-GRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKvKMGLLVDLTNTSRFYDRNDIEKEGIKYI 87
Cdd:cd14502     1 KWLDCPPVGQPVGpTRFIPMKTPLSDDYEHLFAPEIRFTPSALAEKFRQDR-KVGLVIDLTNTDRYYDPNDLDDDGYVYY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  88 KLQCKgHGECPTTENTETFIRLCERF-NERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYK 166
Cdd:cd14502    80 KKVCV-RKEPPDAEEVNKFIELVDKFlAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIYK 158


                  ....*....
gi 2217363399 167 GDYLKELFR 175
Cdd:cd14502   159 PHYIDELYR 167
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 9-173 4.56e-42

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: 148.96  E-value: 4.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399   9 RWLNCPRRGQPVAG-RFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYI 87
Cdd:cd17665     1 RWIDYLPVGQRIPGtRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  88 KLQCKGHgECPTTENTETFIRLCERFNERN--PPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIY 165
Cdd:cd17665    81 KITCPGH-QVPDDKTIQSFKDAVKDFLEKNkdNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIE 159


                  ....*...
gi 2217363399 166 KGDYLKEL 173
Cdd:cd17665   160 RENYLEDL 167
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
268-473 4.41e-30

mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 122.33  E-value: 4.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 268 FPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 338
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 339 NTLLDGEMIIDRVNGQAVP--RYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKpff 416
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVK--- 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217363399 417 DICTSRKLLEgnFAK---EVSHEMDGLIFQPTGK-YKPGRCDDILKWKPPSLNSVDFRLKI 473
Cdd:COG5226   199 QMLKSYGFWK--IYKkipELKHGNDGLIFTPADEpYSVGKDGALLKWKPASLNTIDFRLVL 257
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 97-175 1.25e-16

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: 75.85  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  97 CPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGI-YKGDYLKELFR 175
Cdd:cd14494    36 DLTLAMVDRFLEVLDQAEKPGEP--VLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 287-461 1.77e-12

Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent polynucleotide ligases catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism. This family includes ATP-dependent DNA and RNA ligases. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent DNA ligases have a highly modular architecture, consisting of a unique arrangement of two or more discrete domains, including a DNA-binding domain, an adenylation or nucleotidyltransferase (NTase) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many active site residues. Together with the C-terminal OB-fold domain, it comprises a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases including eukaryotic GRP-dependent mRNA-capping enzymes. The catalytic core contains both the active site as well as many DNA-binding residues. The RNA circularization protein from archaea and bacteria contains the minimal catalytic unit, the adenylation domain, but does not contain an OB-fold domain. This family also includes the m3G-cap binding domain of snurportin, a nuclear import adaptor that binds m3G-capped spliceosomal U small nucleoproteins (snRNPs), but doesn't have enzymatic activity.


Pssm-ID: 185704 [Multi-domain]  Cd Length: 182  Bit Score: 65.90  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 287 KPYKVSWKADGTRYMM-LIDGtnEVFMIDRDNSVFHVSNLEFPfRKDLRMHLSNTLLDGEMIIDRVNG-QAVPRYLIYDI 364
Cdd:cd06846    19 DEYYVQEKYDGKRALIvALNG--GVFAISRTGLEVPLPSILIP-GRELLTLKPGFILDGELVVENREVaNPKPTYYAFDV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399 365 IKFNSQPVGDCDFNVRLQCIEREIISPRHEKmktglidktqePFSVRNKPFFDicTSRKLLEGNFAKEVSHEMDGLIF-Q 443
Cdd:cd06846    96 VPLSGVGLRDLPYSDRFAYLKSLLKEFEGLD-----------PVKLVPLENAP--SYDETLDDLLEKLKKKGKEGLVFkH 162

                         170       180
                  ....*....|....*....|
gi 2217363399 444 PTGKYK--PGRCDDILKWKP 461
Cdd:cd06846   163 PDAPYKgrPGSSGNQLKLKP 182
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 20-154 7.41e-10

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: 58.23  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  20 VAGRFLPLKtmlGPRYDSQVAEENR-FHPSMLSNYLKSLKVKmgLLVDLtNtSRFYDRNDIEKEGIKYIKLQCKgHGECP 98
Cdd:cd14499    22 VPGKFLAFS---GPHDTRKDENGYPtHTPEDYIPYFKKLGVT--TVVRL-N-KKLYDAKRFTDAGIRHYDLYFP-DGSTP 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399  99 TTENTETFIRLCErfnerNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVA 154
Cdd:cd14499    94 SDDIVKKFLDICE-----NEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIA 144
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 47-143 5.73e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 49.64  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  47 PSMLSNYLKSLKvKMGL--LVDLTNTSrfYDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERN-PPELI 122
Cdd:PTZ00242   26 PSNLPLYIKELQ-RYNVthLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETI 101

                          90       100
                  ....*....|....*....|.
gi 2217363399 123 GVHCTHGFNRTGFLICAFLVE 143
Cdd:PTZ00242  102 AVHCVAGLGRAPILVALALVE 122
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 74-151 6.38e-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: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  74 YDRNDIEKEGIKYIKLQCKgHGECPTTENTETFIRLCE-RF-NERNPPELIGVHCTHGFNRTGFLICAFLVE-KMDwSIE 150
Cdd:cd14500    49 YDKEPLEKAGIKVHDWPFD-DGSPPPDDVVDDWLDLLKtRFkEEGKPGACIAVHCVAGLGRAPVLVAIALIElGMK-PED 126


                  .
gi 2217363399 151 A 151
Cdd:cd14500   127 A 127
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 58-161 8.47e-06

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: 45.33  E-value: 8.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  58 KVKMGLLVDLTNTsrfydrNDIEKEGIKYIKlqckghgeCPTTENTET-----------FIRLCERFNERnppelIGVHC 126
Cdd:pfam00782  16 KLGITAVINVTRE------VDLYNSGILYLR--------IPVEDNHETniskyleeaveFIDDARQKGGK-----VLVHC 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217363399 127 THGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 98-164 1.97e-05

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: 44.58  E-value: 1.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217363399  98 PTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTG-FLICAFLVEKMDWSIEaAVATFAQARPPGI 164
Cdd:cd14504    63 PTLEQIDEFLDIVEEANAKNEA--VLVHCLAGKGRTGtMLACYLVKTGKISAVD-AINEIRRIRPGSI 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
64-161 3.31e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  64 LVDLTnTSRFYDRNDIEKEGIKYIKLQCKGHGeCPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVE 143
Cdd:COG2453    29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVL 104

                          90
                  ....*....|....*...
gi 2217363399 144 KmDWSIEAAVATFAQARP 161
Cdd:COG2453   105 L-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
106-161 4.54e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 4.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399  106 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:smart00195  70 FIEDAESKGGK-----VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 53-176 1.22e-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: 42.75  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217363399  53 YLKSLKVKmgLLVDLTNTSRFYDRNDIE--KEGIKYIKLqcKGHGECPTTENTETFIRLcERFNERNPPELIgvHCTHGF 130
Cdd:cd14529    28 LLKKLGIK--TVIDLRGADERAASEEAAakIDGVKYVNL--PLSATRPTESDVQSFLLI-MDLKLAPGPVLI--HCKHGK 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217363399 131 NRTGfLICAFLVEKMDWSIEAAVATFAQ-ARPPGIY------------KGDYLKELFRR 176
Cdd:cd14529   101 DRTG-LVSALYRIVYGGSKEEANEDYRLsNRHLEGLrsgialdskggvKGRYLAAYFER 158
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 124-166 2.00e-04

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: 41.80  E-value: 2.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217363399 124 VHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYK 166
Cdd:cd14526    99 VHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDE 141
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 106-161 3.43e-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: 37.91  E-value: 3.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217363399 106 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:cd14498    71 FIEEALKKGGK-----VLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRP 121
 
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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