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Conserved domains on  [gi|556695381|ref|NP_001273357|]
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mRNA-capping enzyme isoform c [Homo sapiens]

Protein Classification

Adenylation_mRNA_capping and mRNA_cap_C domain-containing protein( domain architecture ID 13212031)

protein containing domains PTP_DSP_cys, Adenylation_mRNA_capping, and mRNA_cap_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 188-378 2.68e-90

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: 275.28  E-value: 2.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 188 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 266
Cdd:cd07895    1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 267 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 346
Cdd:cd07895   81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556695381 347 PFSVRNKPFFDICTSRK-----------------------KYKPGRCDDILKWKP 378
Cdd:cd07895  161 PFSVRLKDFFPLYKIEKlfekiipklphendgliftpndePYVPGTDKNLLKWKP 215
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1-115 9.18e-86

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.


The actual alignment was detected with superfamily member cd17664:

Pssm-ID: 475123  Cd Length: 167  Bit Score: 261.85  E-value: 9.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   1 MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAF 80
Cdd:cd17664   53 LGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAY 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556695381  81 LVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFR 115
Cdd:cd17664  133 LVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
382-475 5.18e-28

mRNA capping enzyme, C-terminal domain;


:

Pssm-ID: 461093  Cd Length: 108  Bit Score: 107.69  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  382 NSVDFRLKIT-----------------RMGGEGLLPQNVGLLYVGgyERPFAQIKVTKElkQYDNKIIECKFENNS-WVF 443
Cdd:pfam03919   1 NSVDFRLKLRfpgpteppdydakpifeLFVWEGGLYEFFGELYVT--DEEWEELKSLGE--PLDGRIVECSWDEEGrWRF 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 556695381  444 MRQRTDKSFPNAYNTAMAVCNSISNPVTKEML 475
Cdd:pfam03919  77 MRFRDDKSNPNHISTVEKVLESIKDGVTEEDL 108
 
Name Accession Description Interval E-value
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 188-378 2.68e-90

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: 275.28  E-value: 2.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 188 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 266
Cdd:cd07895    1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 267 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 346
Cdd:cd07895   81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556695381 347 PFSVRNKPFFDICTSRK-----------------------KYKPGRCDDILKWKP 378
Cdd:cd07895  161 PFSVRLKDFFPLYKIEKlfekiipklphendgliftpndePYVPGTDKNLLKWKP 215
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 1-115 9.18e-86

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: 261.85  E-value: 9.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   1 MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAF 80
Cdd:cd17664   53 LGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAY 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556695381  81 LVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFR 115
Cdd:cd17664  133 LVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 212-377 8.07e-82

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: 252.71  E-value: 8.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  212 QPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 288
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  289 DRVNGQ-AVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRK---- 363
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKllgn 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 556695381  364 --------------------KYKPGRCDDILKWK 377
Cdd:pfam01331 161 kfipnlshesdglifqpvdtPYVAGRCSDLLKWK 194
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
208-479 6.71e-32

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 126.95  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 208 FPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 278
Cdd:COG5226   43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 279 NTLLDGEMIIDRVNGQAVP--RYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKP-- 354
Cdd:COG5226  122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQml 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 355 ----FFDICTSRKK----------------YKPGRCDDILKWKPPSLNSVDFRLKI----TRMGGEGLLPQNVGLLYV-- 408
Cdd:COG5226  202 ksygFWKIYKKIPElkhgndgliftpadepYSVGKDGALLKWKPASLNTIDFRLVLhkkwSEVDDYNYVCSPKFGLDVwf 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 409 -GGYERPFAQIKVT----KELKQ----YDNKIIEC-KFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEF 478
Cdd:COG5226  282 gRKTYRFFASGEVIdgewCELKYdcdpLYWRIVECvLKKEGAWKLLRFRDDKDTPNHISVVCNVLESIRDNVSIEDLSTF 361


                 .
gi 556695381 479 I 479
Cdd:COG5226  362 Y 362
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
382-475 5.18e-28

mRNA capping enzyme, C-terminal domain;


Pssm-ID: 461093  Cd Length: 108  Bit Score: 107.69  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  382 NSVDFRLKIT-----------------RMGGEGLLPQNVGLLYVGgyERPFAQIKVTKElkQYDNKIIECKFENNS-WVF 443
Cdd:pfam03919   1 NSVDFRLKLRfpgpteppdydakpifeLFVWEGGLYEFFGELYVT--DEEWEELKSLGE--PLDGRIVECSWDEEGrWRF 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 556695381  444 MRQRTDKSFPNAYNTAMAVCNSISNPVTKEML 475
Cdd:pfam03919  77 MRFRDDKSNPNHISTVEKVLESIKDGVTEEDL 108
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 14-83 1.73e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 48.09  E-value: 1.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556695381  14 YDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERN-PPELIGVHCTHGFNRTGFLICAFLVE 83
Cdd:PTZ00242  52 YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETIAVHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 46-101 1.28e-05

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: 44.56  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 556695381   46 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 101
Cdd:pfam00782  61 FIDDARQKGGK-----VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
4-101 2.82e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   4 LVDLTnTSRFYDRNDIEKEGIKYIKLQCKGHGeCPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVE 83
Cdd:COG2453   29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVL 104

                         90
                 ....*....|....*...
gi 556695381  84 KmDWSIEAAVATFAQARP 101
Cdd:COG2453  105 L-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
46-101 4.97e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 4.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 556695381    46 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 101
Cdd:smart00195  70 FIEDAESKGGK-----VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
 
Name Accession Description Interval E-value
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 188-378 2.68e-90

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: 275.28  E-value: 2.68e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 188 PKLGEVQQKCHQFC-GWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLE 266
Cdd:cd07895    1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 267 FPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQE 346
Cdd:cd07895   81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556695381 347 PFSVRNKPFFDICTSRK-----------------------KYKPGRCDDILKWKP 378
Cdd:cd07895  161 PFSVRLKDFFPLYKIEKlfekiipklphendgliftpndePYVPGTDKNLLKWKP 215
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 1-115 9.18e-86

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: 261.85  E-value: 9.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   1 MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAF 80
Cdd:cd17664   53 LGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRLCENFIEKNPLELIGVHCTHGFNRTGFLICAY 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556695381  81 LVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFR 115
Cdd:cd17664  133 LVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 212-377 8.07e-82

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: 252.71  E-value: 8.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  212 QPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNE-VFMIDRDNSVFHVSNLEFPFRKD--LRMHLSNTLLDGEMII 288
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  289 DRVNGQ-AVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRK---- 363
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKllgn 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 556695381  364 --------------------KYKPGRCDDILKWK 377
Cdd:pfam01331 161 kfipnlshesdglifqpvdtPYVAGRCSDLLKWK 194
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 1-115 2.18e-52

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: 175.15  E-value: 2.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   1 MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKgHGECPTTENTETFIRLCERF-NERNPPELIGVHCTHGFNRTGFLICA 79
Cdd:cd14502   53 VGLVIDLTNTDRYYDPNDLDDDGYVYYKKVCV-RKEPPDAEEVNKFIELVDKFlAEDNPDKLIAVHCTHGFNRTGFMIVS 131

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 556695381  80 FLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFR 115
Cdd:cd14502  132 YLVERLGLTVEQALEAFAQARPPGIYKPHYIDELYR 167
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
208-479 6.71e-32

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 126.95  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 208 FPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLI-----DGTNEVFMIDRDNSVFHVsNLEFPFR----KDLRMHLS 278
Cdd:COG5226   43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 279 NTLLDGEMIIDRVNGQAVP--RYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKP-- 354
Cdd:COG5226  122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQml 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 355 ----FFDICTSRKK----------------YKPGRCDDILKWKPPSLNSVDFRLKI----TRMGGEGLLPQNVGLLYV-- 408
Cdd:COG5226  202 ksygFWKIYKKIPElkhgndgliftpadepYSVGKDGALLKWKPASLNTIDFRLVLhkkwSEVDDYNYVCSPKFGLDVwf 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 409 -GGYERPFAQIKVT----KELKQ----YDNKIIEC-KFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEF 478
Cdd:COG5226  282 gRKTYRFFASGEVIdgewCELKYdcdpLYWRIVECvLKKEGAWKLLRFRDDKDTPNHISVVCNVLESIRDNVSIEDLSTF 361


                 .
gi 556695381 479 I 479
Cdd:COG5226  362 Y 362
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 1-113 9.73e-32

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: 120.07  E-value: 9.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   1 MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHgECPTTENTETFIRLCERFNERN--PPELIGVHCTHGFNRTGFLIC 78
Cdd:cd17665   54 LGLVIDLTNTTRYYDPRDLTNHGVYYKKITCPGH-QVPDDKTIQSFKDAVKDFLEKNkdNDKLIGVHCTHGLNRTGYLIC 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556695381  79 AFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKEL 113
Cdd:cd17665  133 RYLIDVDGMSPDDAIEAFEQARGHPIERENYLEDL 167
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
382-475 5.18e-28

mRNA capping enzyme, C-terminal domain;


Pssm-ID: 461093  Cd Length: 108  Bit Score: 107.69  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  382 NSVDFRLKIT-----------------RMGGEGLLPQNVGLLYVGgyERPFAQIKVTKElkQYDNKIIECKFENNS-WVF 443
Cdd:pfam03919   1 NSVDFRLKLRfpgpteppdydakpifeLFVWEGGLYEFFGELYVT--DEEWEELKSLGE--PLDGRIVECSWDEEGrWRF 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 556695381  444 MRQRTDKSFPNAYNTAMAVCNSISNPVTKEML 475
Cdd:pfam03919  77 MRFRDDKSNPNHISTVEKVLESIKDGVTEEDL 108
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 37-115 1.54e-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: 75.46  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  37 CPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGI-YKGDYLKELFR 115
Cdd:cd14494   36 DLTLAMVDRFLEVLDQAEKPGEP--VLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 227-333 1.24e-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: 54.73  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381 227 KPYKVSWKADGTRYMM-LIDGtnEVFMIDRDNSVFHVSNLEFPfRKDLRMHLSNTLLDGEMIIDRVNG-QAVPRYLIYDI 304
Cdd:cd06846   19 DEYYVQEKYDGKRALIvALNG--GVFAISRTGLEVPLPSILIP-GRELLTLKPGFILDGELVVENREVaNPKPTYYAFDV 95

                         90       100
                 ....*....|....*....|....*....
gi 556695381 305 IKFNSQPVGDCDFNVRLQCIEREIISPRH 333
Cdd:cd06846   96 VPLSGVGLRDLPYSDRFAYLKSLLKEFEG 124
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 11-94 2.77e-07

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


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 50.53  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  11 SRFYDRNDIEKEGIKYIKLQCKgHGECPTTENTETFIRLCErfnerNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIE 90
Cdd:cd14499   67 KKLYDAKRFTDAGIRHYDLYFP-DGSTPSDDIVKKFLDICE-----NEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAR 140


                 ....
gi 556695381  91 AAVA 94
Cdd:cd14499  141 EAIA 144
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 14-83 1.73e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 48.09  E-value: 1.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556695381  14 YDRNDIEKEGIKyIKLQCKGHGECPTTENTETFIRLC-ERFNERN-PPELIGVHCTHGFNRTGFLICAFLVE 83
Cdd:PTZ00242  52 YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLdQEFAKQStPPETIAVHCVAGLGRAPILVALALVE 122
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 14-91 5.90e-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: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  14 YDRNDIEKEGIKYIKLQCKgHGECPTTENTETFIRLCE-RF-NERNPPELIGVHCTHGFNRTGFLICAFLVE-KMDwSIE 90
Cdd:cd14500   49 YDKEPLEKAGIKVHDWPFD-DGSPPPDDVVDDWLDLLKtRFkEEGKPGACIAVHCVAGLGRAPVLVAIALIElGMK-PED 126


                 .
gi 556695381  91 A 91
Cdd:cd14500  127 A 127
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 46-101 1.28e-05

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: 44.56  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 556695381   46 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 101
Cdd:pfam00782  61 FIDDARQKGGK-----VLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 38-104 1.68e-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: 1.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556695381  38 PTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTG-FLICAFLVEKMDWSIEaAVATFAQARPPGI 104
Cdd:cd14504   63 PTLEQIDEFLDIVEEANAKNEA--VLVHCLAGKGRTGtMLACYLVKTGKISAVD-AINEIRRIRPGSI 127
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
4-101 2.82e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381   4 LVDLTnTSRFYDRNDIEKEGIKYIKLQCKGHGeCPTTENTETFIRLCERFNERNPPelIGVHCTHGFNRTGFLICAFLVE 83
Cdd:COG2453   29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDFIDEALREGKK--VLVHCRGGIGRTGTVAAAYLVL 104

                         90
                 ....*....|....*...
gi 556695381  84 KmDWSIEAAVATFAQARP 101
Cdd:COG2453  105 L-GLSAEEALARVRAARP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
46-101 4.97e-05

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 43.43  E-value: 4.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 556695381    46 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 101
Cdd:smart00195  70 FIEDAESKGGK-----VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 64-106 1.70e-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: 1.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 556695381  64 VHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYK 106
Cdd:cd14526   99 VHCTAGLGRAPATVIAYLYWVLGYSLDEAYYLLTSKRPCGPDE 141
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 23-116 1.59e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.28  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556695381  23 GIKYIKLqcKGHGECPTTENTETFIRLcERFNERNPPELIgvHCTHGFNRTGfLICAFLVEKMDWSIEAAVATFAQ-ARP 101
Cdd:cd14529   58 GVKYVNL--PLSATRPTESDVQSFLLI-MDLKLAPGPVLI--HCKHGKDRTG-LVSALYRIVYGGSKEEANEDYRLsNRH 131

                         90       100
                 ....*....|....*....|....*..
gi 556695381 102 PGIY------------KGDYLKELFRR 116
Cdd:cd14529  132 LEGLrsgialdskggvKGRYLAAYFER 158
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 46-101 4.01e-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: 4.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556695381  46 FIRLCERFNERnppelIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARP 101
Cdd:cd14498   71 FIEEALKKGGK-----VLVHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRP 121
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 38-101 8.81e-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: 8.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556695381  38 PTTENTETFIRLCERFNERNPPELigVHCTHGFNRTGFLICAFLV-EKMDWSIEAAVATFAQARP 101
Cdd:cd14527   57 PTPEQLERAVAWIEELRAQGGPVL--VHCALGYGRSATVVAAWLLaYGRAKSVAEAEALIRAARP 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.
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