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Conserved domains on  [gi|30680771|ref|NP_187522|]
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mRNA capping enzyme family protein [Arabidopsis thaliana]

Protein Classification

RNA 5'-triphosphatase domain-containing protein; DNA ligase-like domain-containing protein( domain architecture ID 12998197)

RNA 5'-triphosphatase domain-containing protein is an RNA-specific cysteine phosphatase belonging to the cys-based protein-tyrosine phosphatase (PTP) family, similar to the RNA triphosphatase domain of mRNA-capping enzymes that catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end| DNA ligase-like domain-containing protein similar to ATP-dependent polynucleotide ligases, such as DNA and RNA ligases, which catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 86-252 2.61e-68

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: 215.60  E-value: 2.61e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771  86 GWLDCPPSGNEIGF--LVPSKVPLNESYNNHVPPGSRYSFKQVIhNQRIAGRKLGLVIDLTNTTRYYSTTDLKKEGIKHV 163
Cdd:cd14502   1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTPSALA-EKFRQDRKVGLVIDLTNTDRYYDPNDLDDDGYVYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 164 KIACKgRDAVPDNVSVNAFVNEVNQFvLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIY 243
Cdd:cd14502  80 KKVCV-RKEPPDAEEVNKFIELVDKF-LAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIY 157


                ....*....
gi 30680771 244 KPDYIDALY 252
Cdd:cd14502 158 KPHYIDELY 166
Adenylation_DNA_ligase_like super family cl12015
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 354-460 2.84e-49

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.


The actual alignment was detected with superfamily member pfam01331:

Pssm-ID: 448381 [Multi-domain]  Cd Length: 194  Bit Score: 166.81  E-value: 2.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771   354 HPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTD--GCYIVDRSFRFRRVQ-MRFPFRHPTEgiSDKVHHFTLLDGEM 430
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDpeGCYIIDRDNNVYLVEnLRFPRENDEG--LEKHLDGTLLDGEL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 30680771   431 IIDTLPdKQKQERRYLIYDMVAINGQSVVE 460
Cdd:pfam01331  79 VIDTVP-GQKQQPRYLIYDIVAINGQTVMQ 107
 
Name Accession Description Interval E-value
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 86-252 2.61e-68

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: 215.60  E-value: 2.61e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771  86 GWLDCPPSGNEIGF--LVPSKVPLNESYNNHVPPGSRYSFKQVIhNQRIAGRKLGLVIDLTNTTRYYSTTDLKKEGIKHV 163
Cdd:cd14502   1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTPSALA-EKFRQDRKVGLVIDLTNTDRYYDPNDLDDDGYVYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 164 KIACKgRDAVPDNVSVNAFVNEVNQFvLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIY 243
Cdd:cd14502  80 KKVCV-RKEPPDAEEVNKFIELVDKF-LAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIY 157


                ....*....
gi 30680771 244 KPDYIDALY 252
Cdd:cd14502 158 KPHYIDELY 166
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 354-460 2.84e-49

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: 166.81  E-value: 2.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771   354 HPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTD--GCYIVDRSFRFRRVQ-MRFPFRHPTEgiSDKVHHFTLLDGEM 430
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDpeGCYIIDRDNNVYLVEnLRFPRENDEG--LEKHLDGTLLDGEL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 30680771   431 IIDTLPdKQKQERRYLIYDMVAINGQSVVE 460
Cdd:pfam01331  79 VIDTVP-GQKQQPRYLIYDIVAINGQTVMQ 107
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 336-460 3.32e-49

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: 167.42  E-value: 3.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 336 RMLSLNIGGRGCSQFPGSHPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTT-DGCYIVDRSFRFRRVQMRFPFRHPte 414
Cdd:cd07895   8 RKVAELCPGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGrGEVYLIDRKNDVFKVPGLFFPRRK-- 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30680771 415 gISDKVHHFTLLDGEMIIDTLPDKQKqeRRYLIYDMVAINGQSVVE 460
Cdd:cd07895  86 -NLEPHHQGTLLDGELVIDKVPGKKR--PRYLIFDILAFNGQSVTE 128
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
317-455 4.14e-23

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 100.76  E-value: 4.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 317 VLGDEIPPDQEEGYRQFFYRMLSLNiggRGCSQFPGSHPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTD------G 390
Cdd:COG5226  13 RPGNKVPPDIAEALKTKIYKLLCIT---EPRETFPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVTEEpvtgafR 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30680771 391 CYIVDRSFRFRRVQMRFPFRHPTEGISDKVHHFTLLDGEMIIDTLPDKQKQERRYLIYDMVAING 455
Cdd:COG5226  90 GYFYDRRNNFYEVHTSFPPCSTVLKDGEVLLEDTLLDGELVFDCLPYEKVPQLRYLLFDCLAYAG 154
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
140-255 3.52e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 60.75  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 140 VIDLTnTTRYYSTTDLKKEGIKHVKIACKGRDAvPDNVSVNAFVNEVNQfvlNLKHSKKyILVHCTHGHNRTGFMIVHYL 219
Cdd:COG2453  29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFGA-PDDEQLQEAVDFIDE---ALREGKK-VLVHCRGGIGRTGTVAAAYL 102

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30680771 220 MRSGpMNVTQALKIFSDARPPGIYKPDYIDALYSFY 255
Cdd:COG2453 103 VLLG-LSAEEALARVRAARPGAVETPAQRAFLERFA 137
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
121-239 1.21e-09

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 56.52  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771    121 YSFKQVIHNQRIAGRKLGLVIDLTNTTRYYSTTDLKkegIKHVKIackgrdavPDNVSVN--AFVNEVNQFVLNLKHSKK 198
Cdd:smart00195  11 GSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFT---YLGVPI--------DDNTETKisPYFPEAVEFIEDAESKGG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 30680771    199 YILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARP 239
Cdd:smart00195  80 KVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 136-239 2.53e-09

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: 55.35  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771   136 KLGLVIDLTNTTryysttDLKKEGIKHvkIACKGRDAVPDNVSvnAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMI 215
Cdd:pfam00782  18 GITAVINVTREV------DLYNSGILY--LRIPVEDNHETNIS--KYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLI 87

                          90       100
                  ....*....|....*....|....
gi 30680771   216 VHYLMRSGPMNVTQALKIFSDARP 239
Cdd:pfam00782  88 IAYLMKTRNLSLNEAYSFVKERRP 111
 
Name Accession Description Interval E-value
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 86-252 2.61e-68

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: 215.60  E-value: 2.61e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771  86 GWLDCPPSGNEIGF--LVPSKVPLNESYNNHVPPGSRYSFKQVIhNQRIAGRKLGLVIDLTNTTRYYSTTDLKKEGIKHV 163
Cdd:cd14502   1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTPSALA-EKFRQDRKVGLVIDLTNTDRYYDPNDLDDDGYVYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 164 KIACKgRDAVPDNVSVNAFVNEVNQFvLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIY 243
Cdd:cd14502  80 KKVCV-RKEPPDAEEVNKFIELVDKF-LAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIY 157


                ....*....
gi 30680771 244 KPDYIDALY 252
Cdd:cd14502 158 KPHYIDELY 166
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 87-252 4.36e-51

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: 170.94  E-value: 4.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771  87 WLDCPPSGNEI-GFLVPSKVPLNESYNNHVPPGSRYSFKQVIHNQRIAGRKLGLVIDLTNTTRYYSTTDLKKEGIKHVKI 165
Cdd:cd17664   2 WLNCPRKGQPVaGKFLPFKTPLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIKL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 166 ACKGRDAVPDNVSVNAFVNEVNQFVLnlKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIYKP 245
Cdd:cd17664  82 QCKGHGECPSPEQTETFIRLCENFIE--KNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKG 159


                ....*..
gi 30680771 246 DYIDALY 252
Cdd:cd17664 160 DYLKELF 166
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 354-460 2.84e-49

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: 166.81  E-value: 2.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771   354 HPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTD--GCYIVDRSFRFRRVQ-MRFPFRHPTEgiSDKVHHFTLLDGEM 430
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDpeGCYIIDRDNNVYLVEnLRFPRENDEG--LEKHLDGTLLDGEL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 30680771   431 IIDTLPdKQKQERRYLIYDMVAINGQSVVE 460
Cdd:pfam01331  79 VIDTVP-GQKQQPRYLIYDIVAINGQTVMQ 107
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 336-460 3.32e-49

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: 167.42  E-value: 3.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 336 RMLSLNIGGRGCSQFPGSHPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTT-DGCYIVDRSFRFRRVQMRFPFRHPte 414
Cdd:cd07895   8 RKVAELCPGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGrGEVYLIDRKNDVFKVPGLFFPRRK-- 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30680771 415 gISDKVHHFTLLDGEMIIDTLPDKQKqeRRYLIYDMVAINGQSVVE 460
Cdd:cd07895  86 -NLEPHHQGTLLDGELVIDKVPGKKR--PRYLIFDILAFNGQSVTE 128
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 87-253 9.46e-40

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: 140.87  E-value: 9.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771  87 WLDCPPSGNEI--GFLVPSKVPLNESYNNHVPPGSRYSFKQVIHNQRIAGRKLGLVIDLTNTTRYYSTTDLKKEGIKHVK 164
Cdd:cd17665   2 WIDYLPVGQRIpgTRFIAFKVPLRKSFFANLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYKK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 165 IACkGRDAVPDNVSVNAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIYK 244
Cdd:cd17665  82 ITC-PGHQVPDDKTIQSFKDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIER 160


                ....*....
gi 30680771 245 PDYIDALYS 253
Cdd:cd17665 161 ENYLEDLLK 169
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
317-455 4.14e-23

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 100.76  E-value: 4.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 317 VLGDEIPPDQEEGYRQFFYRMLSLNiggRGCSQFPGSHPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTD------G 390
Cdd:COG5226  13 RPGNKVPPDIAEALKTKIYKLLCIT---EPRETFPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVTEEpvtgafR 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30680771 391 CYIVDRSFRFRRVQMRFPFRHPTEGISDKVHHFTLLDGEMIIDTLPDKQKQERRYLIYDMVAING 455
Cdd:COG5226  90 GYFYDRRNNFYEVHTSFPPCSTVLKDGEVLLEDTLLDGELVFDCLPYEKVPQLRYLLFDCLAYAG 154
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
140-255 3.52e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 60.75  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 140 VIDLTnTTRYYSTTDLKKEGIKHVKIACKGRDAvPDNVSVNAFVNEVNQfvlNLKHSKKyILVHCTHGHNRTGFMIVHYL 219
Cdd:COG2453  29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFGA-PDDEQLQEAVDFIDE---ALREGKK-VLVHCRGGIGRTGTVAAAYL 102

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30680771 220 MRSGpMNVTQALKIFSDARPPGIYKPDYIDALYSFY 255
Cdd:COG2453 103 VLLG-LSAEEALARVRAARPGAVETPAQRAFLERFA 137
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
121-239 1.21e-09

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 56.52  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771    121 YSFKQVIHNQRIAGRKLGLVIDLTNTTRYYSTTDLKkegIKHVKIackgrdavPDNVSVN--AFVNEVNQFVLNLKHSKK 198
Cdd:smart00195  11 GSYSDALNLALLKKLGITHVINVTNEVPNYNGSDFT---YLGVPI--------DDNTETKisPYFPEAVEFIEDAESKGG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 30680771    199 YILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARP 239
Cdd:smart00195  80 KVLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 155-256 1.27e-09

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 55.82  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 155 LKKEGIKHVKIACKgrdavpdnvsvnAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIF 234
Cdd:cd14494  26 LKQLGVTTIVDLTL------------AMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIV 93

                        90       100
                ....*....|....*....|..
gi 30680771 235 SDARPPGIykPDYIDALYSFYH 256
Cdd:cd14494  94 RLIRPGGI--PQTIEQLDFLIK 113
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 351-460 1.38e-09

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: 57.43  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 351 PGSHPVSLNRENLQLLRQRYYYATWKADGTRYMMLLTTDGCYIVDRS-FRFRRVQMRFPFRHPTegisdKVHHFTLLDGE 429
Cdd:cd06846   1 PQLLNPILEEALSEYDEQDEYYVQEKYDGKRALIVALNGGVFAISRTgLEVPLPSILIPGRELL-----TLKPGFILDGE 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 30680771 430 MIIDTLPDKQKQErRYLIYDMVAINGQSVVE 460
Cdd:cd06846  76 LVVENREVANPKP-TYYAFDVVPLSGVGLRD 105
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 136-239 2.53e-09

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: 55.35  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771   136 KLGLVIDLTNTTryysttDLKKEGIKHvkIACKGRDAVPDNVSvnAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMI 215
Cdd:pfam00782  18 GITAVINVTREV------DLYNSGILY--LRIPVEDNHETNIS--KYLEEAVEFIDDARQKGGKVLVHCQAGISRSATLI 87

                          90       100
                  ....*....|....*....|....
gi 30680771   216 VHYLMRSGPMNVTQALKIFSDARP 239
Cdd:pfam00782  88 IAYLMKTRNLSLNEAYSFVKERRP 111
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 155-239 1.18e-07

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: 50.62  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 155 LKKEGIKHVKIACKGRDA-------------VPDNVSVN--AFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYL 219
Cdd:cd14498  22 LKKLGITHILNVAGEPPPnkfpdgikylripIEDSPDEDilSHFEEAIEFIEEALKKGGKVLVHCQAGVSRSATIVIAYL 101

                        90       100
                ....*....|....*....|
gi 30680771 220 MRSGPMNVTQALKIFSDARP 239
Cdd:cd14498 102 MKKYGWSLEEALELVKSRRP 121
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 181-256 2.50e-06

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.89  E-value: 2.50e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680771 181 AFVNEVNQFvlNLKhskkyILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIYKPDYIDALYSFYH 256
Cdd:cd14504  73 DIVEEANAK--NEA-----VLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRPGSIETSEQEKFVIQFAK 141
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 104-235 1.57e-05

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 44.67  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 104 KVPLNesYNNHVPPGSRYSFKQVIHNQRIagRKLGLVIDLTNTTRYYSTTD---LKKEGIKHVKIACKGRDAVPDNVsVN 180
Cdd:cd18538   1 GLPPN--FGVVVPGVYRSSFPKPENFGFL--KSLGLRTILTLVQEEYSPEFlnfLRENGIQHFHIAMLGNKDPKVSI-PD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30680771 181 AFVNEVNQFVLNLKHSKkyILVHCTHGHNRTGFMI--VHYLMRSGPMNVTQALKIFS 235
Cdd:cd18538  76 HTMNRILRIILDKENHP--ILVHCNKGKHRTGCVIacFRKLQGWDVENVLEEYLSYA 130
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 129-239 3.93e-05

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 43.79  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 129 NQRIAGRKLGLVIDLTN--TTRYY--STTDLKKEGIKHVKIACKGRDAVPDNVSVNAFVnevnQFVLNLKHSKKYILVHC 204
Cdd:cd14524  21 VALVAKENVRGVITMNEeyETRFFcnSKEEWKALGVEQLRLPTVDFTGVPSLEDLEKGV----DFILKHREKGKSVYVHC 96

                        90       100       110
                ....*....|....*....|....*....|....*
gi 30680771 205 THGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARP 239
Cdd:cd14524  97 KAGRGRSATIVACYLIQHKGWSPEEAQEFLRSKRP 131
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 135-223 7.27e-05

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: 43.13  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 135 RKLGL--VIDL--TNTTRYYSTTDLKKEGIKHVKIACKGRDAVPDNVsvnafvnEVNQFVLNLKHSKKYILVHCTHGHNR 210
Cdd:cd14529  30 KKLGIktVIDLrgADERAASEEAAAKIDGVKYVNLPLSATRPTESDV-------QSFLLIMDLKLAPGPVLIHCKHGKDR 102

                        90
                ....*....|...
gi 30680771 211 TGFMIVHYLMRSG 223
Cdd:cd14529 103 TGLVSALYRIVYG 115
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 200-251 1.11e-04

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: 41.88  E-value: 1.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 30680771 200 ILVHCTHGHNRTGFMIVHYLMRSGPM-NVTQALKIFSDARPPGIYKPDYIDAL 251
Cdd:cd14527  79 VLVHCALGYGRSATVVAAWLLAYGRAkSVAEAEALIRAARPQVVLNPAQRKAL 131
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 155-254 4.59e-04

dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs 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. IBR5 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. It has been shown to target MPK12, which is a negative regulator of auxin signaling.


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 40.21  E-value: 4.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 155 LKKEGIKHVkiackgRDAVPDNVSV--NAFV------------NEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYLM 220
Cdd:cd18534  23 LKAQGITRI------LNTVPDCQNLykNSFTyhvlseektvpfAEAVDFIEQCRKDKARVLVHCMSGQSRSPAVVIAYLM 96

                        90       100       110
                ....*....|....*....|....*....|....
gi 30680771 221 RSGPMNVTQALKIFSDARPPGIYKPDYIDALYSF 254
Cdd:cd18534  97 KHKGWRLAESYQWVKERRPSINLSPAVAKQLQEF 130
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 137-239 5.21e-04

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They 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. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 40.16  E-value: 5.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 137 LGLVIDLTNTTryystTDLKKEGIKHVKiackgRDAVPDNVSVN--AFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFM 214
Cdd:cd14512  27 IGYVLNVSNTC-----PNPDFIGLFHYK-----RIPVNDSFCQNisPWFDEAIEFIEEAKASNGGVLVHCLAGISRSATI 96

                        90       100
                ....*....|....*....|....*
gi 30680771 215 IVHYLMRSGPMNVTQALKIFSDARP 239
Cdd:cd14512  97 AIAYLMKRMRMSLDEAYDFVKEKRP 121
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 149-242 6.64e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 40.80  E-value: 6.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 149 YYSTTDLKKEGIKHVKIACKGRDAVP-----DNVSVNAFVnevnqfvlnLKHSKKyILVHCTHGHNRTGFMIVHYLMRSG 223
Cdd:cd14506  66 SYLPEAFMRAGIYFYNFGWKDYGVPSlttilDIVKVMAFA---------LQEGGK-VAVHCHAGLGRTGVLIACYLVYAL 135

                        90
                ....*....|....*....
gi 30680771 224 PMNVTQALKIFSDARPPGI 242
Cdd:cd14506 136 RMSADQAIRLVRSKRPNSI 154
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 171-239 2.00e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 38.78  E-value: 2.00e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 171 DAVPDNVsvnAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYLMRSGP-MNVTQALKIFSDARP 239
Cdd:cd14505  83 GGVPSDI---AQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAACLLLELGDtLDPEQAIAAVRALRP 149
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
182-239 2.35e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 37.72  E-value: 2.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680771    182 FVNEVNQFvLNLKHSKKYILVHCTHGHNRTGFMIVHYLM------RSGPMNVTQALKIFSDARP 239
Cdd:smart00404  25 LLRAVKKN-LNQSESSGPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRP 87
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 182-239 2.35e-03

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 37.72  E-value: 2.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680771    182 FVNEVNQFvLNLKHSKKYILVHCTHGHNRTGFMIVHYLM------RSGPMNVTQALKIFSDARP 239
Cdd:smart00012  25 LLRAVKKN-LNQSESSGPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRP 87
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 155-239 2.41e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It 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. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 38.10  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 155 LKKEGIKHV-KIACKGRDAVPDN-------------VSVNAFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFMIVHYLM 220
Cdd:cd14523  23 LKKHKVTHIlNVAYGVENAFPDDftyktisildlpeTDITSYFPECFEFIDEAKSQDGVVLVHCNAGVSRSASIVIGYLM 102

                        90
                ....*....|....*....
gi 30680771 221 RSGPMNVTQALKIFSDARP 239
Cdd:cd14523 103 ATENLSFEDAFSLVKNARP 121
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 137-239 4.88e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 37.42  E-value: 4.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 137 LGLVIDLTNTTRYYsttDLKKEGIKhvkiaCKgRDAVPDNVSVN--AFVNEVNQFVLNLKHSKKYILVHCTHGHNRTGFM 214
Cdd:cd14567  27 IGYVLNVTTHLPLY---HEGKGGFR-----YK-RLPATDSNKQNlrQYFEEAFEFIEEAHQSGKGVLVHCQAGVSRSATI 97

                        90       100
                ....*....|....*....|....*
gi 30680771 215 IVHYLMRSGPMNVTQALKIFSDARP 239
Cdd:cd14567  98 VIAYLMKHTRMTMTDAYKFVKNKRP 122
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 173-238 5.41e-03

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


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 37.73  E-value: 5.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30680771 173 VPDNVSVNAFVNEVNQFVLnlKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQ-ALKIFSDAR 238
Cdd:cd14510  86 VPTLDEMLSFTAEVREWMA--ADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKeALEYFGERR 150
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 193-238 5.58e-03

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 37.19  E-value: 5.58e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30680771 193 LKHSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDAR 238
Cdd:cd14515  84 LSDPGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKR 129
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 178-238 7.80e-03

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


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.18  E-value: 7.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30680771 178 SVNAFVNEVNQFvlnLK-HSKKYILVHCTHGHNRTGFMIVHYLMRSGPMNVTQ-ALKIFSDAR 238
Cdd:cd14509  77 LIKPFCEDVDEW---LKeDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSAKeALDFYGAKR 136
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 200-259 8.09e-03

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 36.91  E-value: 8.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680771 200 ILVHCTHGHNRTGFMIVHYLMRSGPMNVTQALKIFSDARPPGIYKPDYIDALySFYHEIK 259
Cdd:cd14518  93 VLVHCAMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRPIAEPNDGFMEQL-ELYHEMG 151
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 200-239 9.09e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, 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. DUSP12 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 targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 36.84  E-value: 9.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 30680771 200 ILVHCTHGHNRTGFMIVHYLMRSGPMNVTQAL----KIFSDARP 239
Cdd:cd14520  82 VLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALaslrECKPDVKP 125
 
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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