NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958776138|ref|XP_038965755|]
View 

mRNA-capping enzyme isoform X8 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.76e-127

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: 365.08  E-value: 1.76e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  89 LQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 1958776138 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 ...
 248-419 2.41e-85

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: 259.48  E-value: 2.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 327 FPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170
                  ....*....|...
gi 1958776138 407 PFSVRPKQFFDIN 419
Cdd:cd07895   161 PFSVRLKDFFPLY 173
 
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 1.76e-127

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: 365.08  E-value: 1.76e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  89 LQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 1958776138 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 ...
 248-419 2.41e-85

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: 259.48  E-value: 2.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 327 FPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170
                  ....*....|...
gi 1958776138 407 PFSVRPKQFFDIN 419
Cdd:cd07895   161 PFSVRLKDFFPLY 173
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 272-424 8.52e-74

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: 229.22  E-value: 8.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 272 QPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 348
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776138 349 DKVNGQ-AVPRYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKK 424
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKL 157
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
268-414 4.26e-20

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 91.52  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 268 FPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 338
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776138 339 NTLLDGEMIIDKVNGQAVP--RYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQ 414
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQ 199
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 47-143 2.67e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 50.02  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  47 PSMLSNYLKSLK-VKMSLLVDLTNTSrfYDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERS-PPELIG 123
Cdd:PTZ00242   26 PSNLPLYIKELQrYNVTHLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETIA 102

                          90       100
                  ....*....|....*....|
gi 1958776138 124 VHCTHGFNRTGFLICAFLVE 143
Cdd:PTZ00242  103 VHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 58-161 7.14e-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: 44.95  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  58 KVKMSLLVDLTNTsrfydrNDIEKEGIKYIKlqckghgeCPTTENTET-----------FIRLCERFNERsppelIGVHC 126
Cdd:pfam00782  16 KLGITAVINVTRE------VDLYNSGILYLR--------IPVEDNHETniskyleeaveFIDDARQKGGK-----VLVHC 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958776138 127 THGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
124-161 2.64e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 2.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958776138 124 VHCTHGFNRTGFLICAFLVEKmDWSIEAAVATFAQARP 161
Cdd:COG2453    85 VHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
106-161 3.99e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 3.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776138  106 FIRLCERFNERsppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 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 1.76e-127

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: 365.08  E-value: 1.76e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138   9 RWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIK 88
Cdd:cd17664     1 RWLNCPRKGQPVAGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  89 LQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGD 168
Cdd:cd17664    81 LQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGD 160


                  ....*..
gi 1958776138 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 ...
 248-419 2.41e-85

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: 259.48  E-value: 2.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 248 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 326
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 327 FPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQE 406
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170
                  ....*....|...
gi 1958776138 407 PFSVRPKQFFDIN 419
Cdd:cd07895   161 PFSVRLKDFFPLY 173
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 272-424 8.52e-74

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: 229.22  E-value: 8.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 272 QPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 348
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776138 349 DKVNGQ-AVPRYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKK 424
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKL 157
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 9-175 6.69e-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: 226.00  E-value: 6.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138   9 RWLNCPRRGQPVA-GRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKvKMSLLVDLTNTSRFYDRNDIEKEGIKYI 87
Cdd:cd14502     1 KWLDCPPVGQPVGpTRFIPMKTPLSDDYEHLFAPEIRFTPSALAEKFRQDR-KVGLVIDLTNTDRYYDPNDLDDDGYVYY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  88 KLQCKgHGECPTTENTETFIRLCERF-NERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYK 166
Cdd:cd14502    80 KKVCV-RKEPPDAEEVNKFIELVDKFlAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIYK 158


                  ....*....
gi 1958776138 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 2.58e-41

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: 144.34  E-value: 2.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138   9 RWLNCPRRGQPVAG-RFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYI 87
Cdd:cd17665     1 RWIDYLPVGQRIPGtRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  88 KLQCKGHgECPTTENTETFIRLCERFNER--SPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIY 165
Cdd:cd17665    81 KITCPGH-QVPDDKTIQSFKDAVKDFLEKnkDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIE 159


                  ....*...
gi 1958776138 166 KGDYLKEL 173
Cdd:cd17665   160 RENYLEDL 167
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
268-414 4.26e-20

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 91.52  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 268 FPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 338
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776138 339 NTLLDGEMIIDKVNGQAVP--RYLIYDIIKFNAQPVGECDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQ 414
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQ 199
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 97-175 2.99e-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: 74.31  E-value: 2.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  97 CPTTENTETFIRLCERFNerSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGI-YKGDYLKELFR 175
Cdd:cd14494    36 DLTLAMVDRFLEVLDQAE--KPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 20-154 6.86e-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: 57.85  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  20 VAGRFLPLKtmlGPRYDSQVAEENR-FHPSMLSNYLKSLKVKmsLLVDLtNtSRFYDRNDIEKEGIKYIKLQCKgHGECP 98
Cdd:cd14499    22 VPGKFLAFS---GPHDTRKDENGYPtHTPEDYIPYFKKLGVT--TVVRL-N-KKLYDAKRFTDAGIRHYDLYFP-DGSTP 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776138  99 TTENTETFIRLCERfnersPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVA 154
Cdd:cd14499    94 SDDIVKKFLDICEN-----EKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIA 144
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 284-393 1.43e-08

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: 54.35  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138 284 LEQKPYKVSWKADGTRYMM-LIDGtnEVFMIDRDNSVFHVSNLEFPfRKDLRMHLSNTLLDGEMIIDKVNG-QAVPRYLI 361
Cdd:cd06846    16 DEQDEYYVQEKYDGKRALIvALNG--GVFAISRTGLEVPLPSILIP-GRELLTLKPGFILDGELVVENREVaNPKPTYYA 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958776138 362 YDIIKFNAQPVGECDFNIRLQCIEREIISPRH 393
Cdd:cd06846    93 FDVVPLSGVGLRDLPYSDRFAYLKSLLKEFEG 124
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 47-143 2.67e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 50.02  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  47 PSMLSNYLKSLK-VKMSLLVDLTNTSrfYDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERS-PPELIG 123
Cdd:PTZ00242   26 PSNLPLYIKELQrYNVTHLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETIA 102

                          90       100
                  ....*....|....*....|
gi 1958776138 124 VHCTHGFNRTGFLICAFLVE 143
Cdd:PTZ00242  103 VHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 58-161 7.14e-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: 44.95  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  58 KVKMSLLVDLTNTsrfydrNDIEKEGIKYIKlqckghgeCPTTENTET-----------FIRLCERFNERsppelIGVHC 126
Cdd:pfam00782  16 KLGITAVINVTRE------VDLYNSGILYLR--------IPVEDNHETniskyleeaveFIDDARQKGGK-----VLVHC 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958776138 127 THGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:pfam00782  77 QAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 74-151 7.78e-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: 45.67  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  74 YDRNDIEKEGIKYIKLQCKgHGECPTTENTETFIRLCE-RF-NERSPPELIGVHCTHGFNRTGFLICAFLVE-KMDwSIE 150
Cdd:cd14500    49 YDKEPLEKAGIKVHDWPFD-DGSPPPDDVVDDWLDLLKtRFkEEGKPGACIAVHCVAGLGRAPVLVAIALIElGMK-PED 126


                  .
gi 1958776138 151 A 151
Cdd:cd14500   127 A 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
124-161 2.64e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 2.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958776138 124 VHCTHGFNRTGFLICAFLVEKmDWSIEAAVATFAQARP 161
Cdd:COG2453    85 VHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
106-161 3.99e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 3.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776138  106 FIRLCERFNERsppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:smart00195  70 FIEDAESKGGK-----VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 98-164 1.05e-04

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: 42.26  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776138  98 PTTENTETFIRLCERFNERSPPelIGVHCTHGFNRTG-FLICAFLVEKMDWSIEaAVATFAQARPPGI 164
Cdd:cd14504    63 PTLEQIDEFLDIVEEANAKNEA--VLVHCLAGKGRTGtMLACYLVKTGKISAVD-AINEIRRIRPGSI 127
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 124-166 1.36e-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: 1.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958776138 124 VHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYK 166
Cdd:cd14526    99 VHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDE 141
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 53-176 2.23e-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: 41.59  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776138  53 YLKSLKVKmsLLVDLTNTSRFYDRNDIE--KEGIKYIKLqcKGHGECPTTENTETFIRLcERFNERSPPELIgvHCTHGF 130
Cdd:cd14529    28 LLKKLGIK--TVIDLRGADERAASEEAAakIDGVKYVNL--PLSATRPTESDVQSFLLI-MDLKLAPGPVLI--HCKHGK 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776138 131 NRTGfLICAFLVEKMDWSIEAAVATFAQ-ARPPGIY------------KGDYLKELFRR 176
Cdd:cd14529   101 DRTG-LVSALYRIVYGGSKEEANEDYRLsNRHLEGLrsgialdskggvKGRYLAAYFER 158
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 106-161 3.17e-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: 3.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776138 106 FIRLCERFNERsppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 161
Cdd:cd14498    71 FIEEALKKGGK-----VLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRP 121
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 98-161 6.82e-03

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


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 36.87  E-value: 6.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776138  98 PTTENTETFIRLCERfnERSPPELIGVHCTHGFNRTGFLICAFLV-EKMDWSIEAAVATFAQARP 161
Cdd:cd14527    57 PTPEQLERAVAWIEE--LRAQGGPVLVHCALGYGRSATVVAAWLLaYGRAKSVAEAEALIRAARP 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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