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Conserved domains on  [gi|1444527163|ref|XP_025940286|]
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mRNA-capping enzyme isoform X2 [Apteryx rowi]

Protein Classification

dual specificity protein phosphatase family protein; protein-tyrosine phosphatase family protein( domain architecture ID 13026128)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases; protein-tyrosine phosphatase family protein, similar to Saccharomyces cerevisiae OCA6 that is required for replication of Brome mosaic virus, but may be inactive as a protein-tyrosine phosphatase as it lacks the CxxxxxR catalytic motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 1-146 4.38e-111

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: 325.40  E-value: 4.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163   1 MLGPRYDEQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHGECPTPENTETFIRV 80
Cdd:cd17664    22 PLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163  81 CEHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGIYKGDYLKELFR 146
Cdd:cd17664   102 CENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 222-435 8.28e-111

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: 326.51  E-value: 8.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 222 PKLGGIQQKCQQFC-GWEGSGFPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNEVYMIDRDNSIFHVSNLE 300
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 301 FPFRKDLRSHLANTLLDGEMIIDKVNGQVVPRYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQE 380
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163 381 PFSVRNKPFFDIYTARKLLEGSFaREVSHEVDGLIFQPTG-KYKPGRCDDILKWKP 435
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKII-PKLPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
 
Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 1-146 4.38e-111

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: 325.40  E-value: 4.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163   1 MLGPRYDEQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHGECPTPENTETFIRV 80
Cdd:cd17664    22 PLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163  81 CEHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGIYKGDYLKELFR 146
Cdd:cd17664   102 CENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 222-435 8.28e-111

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: 326.51  E-value: 8.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 222 PKLGGIQQKCQQFC-GWEGSGFPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNEVYMIDRDNSIFHVSNLE 300
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 301 FPFRKDLRSHLANTLLDGEMIIDKVNGQVVPRYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQE 380
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163 381 PFSVRNKPFFDIYTARKLLEGSFaREVSHEVDGLIFQPTG-KYKPGRCDDILKWKP 435
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKII-PKLPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 246-434 6.61e-97

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: 290.46  E-value: 6.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 246 QPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNE-VYMIDRDNSIFHVSNLEFPFRKD--LRSHLANTLLDGEMII 322
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 323 DKVNGQ-VVPRYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQEPFSVRNKPFFDIYTARKLLEG 401
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKLLGN 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1444527163 402 SFAREVSHEVDGLIFQPTG-KYKPGRCDDILKWK 434
Cdd:pfam01331 161 KFIPNLSHESDGLIFQPVDtPYVAGRCSDLLKWK 194
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
242-447 1.83e-33

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 130.81  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 242 FPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLI-----DGKNEVYMIDRDNSIFHVsNLEFPFR----KDLRSHLA 312
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 313 NTLLDGEMIIDKVNGQVVP--RYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQEPFSVRNKPFF 390
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQML 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444527163 391 DIYTARKLLEGsfAREVSHEVDGLIFQPTGK-YKPGRCDDILKWKPPSLNSVDFRLKI 447
Cdd:COG5226   202 KSYGFWKIYKK--IPELKHGNDGLIFTPADEpYSVGKDGALLKWKPASLNTIDFRLVL 257
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-132 6.51e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.73  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  35 LVDLTnTTRFYDRNDIEKEGIKYIKLQCKGHGeCPTPENTETFIR-VCEHFSDKNPselIGVHCTHGFNRTGFLICAFLV 113
Cdd:COG2453    29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDfIDEALREGKK---VLVHCRGGIGRTGTVAAAYLV 103

                          90
                  ....*....|....*....
gi 1444527163 114 EKlDWSVEAAVATFAQARP 132
Cdd:COG2453   104 LL-GLSAEEALARVRAARP 121
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 18-114 6.78e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 46.17  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  18 PSMLSNYLKSLKvKMGL--LVDLTNTTrfYDRNDIEKEGIKyIKLQCKGHGECPTPENTETFIRVCEHF--SDKNPSELI 93
Cdd:PTZ00242   26 PSNLPLYIKELQ-RYNVthLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLDQEfaKQSTPPETI 101

                          90       100
                  ....*....|....*....|.
gi 1444527163  94 GVHCTHGFNRTGFLICAFLVE 114
Cdd:PTZ00242  102 AVHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 29-132 1.14e-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: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  29 KVKMGLLVDLTNTTRFYdrndieKEGIKYIKlqckghgeCPTPENTETFIrvCEHFSD--------KNPSELIGVHCTHG 100
Cdd:pfam00782  16 KLGITAVINVTREVDLY------NSGILYLR--------IPVEDNHETNI--SKYLEEavefiddaRQKGGKVLVHCQAG 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1444527163 101 FNRTGFLICAFLVEKLDWSVEAAVATFAQARP 132
Cdd:pfam00782  80 ISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
93-132 1.96e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.50  E-value: 1.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1444527163   93 IGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARP 132
Cdd:smart00195  81 VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
 
Name Accession Description Interval E-value
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 1-146 4.38e-111

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: 325.40  E-value: 4.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163   1 MLGPRYDEQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHGECPTPENTETFIRV 80
Cdd:cd17664    22 PLGPRYDDQVPEENRFHPSMLFNYLKSLKVKLGLWIDLTNTNRFYDRNEVEKEGCKYIKLQCKGHGECPSPEQTETFIRL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163  81 CEHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGIYKGDYLKELFR 146
Cdd:cd17664   102 CENFIEKNPLELIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIYKGDYLKELFR 167
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 222-435 8.28e-111

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: 326.51  E-value: 8.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 222 PKLGGIQQKCQQFC-GWEGSGFPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNEVYMIDRDNSIFHVSNLE 300
Cdd:cd07895     1 EKLSELRRKVAELCpGWERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGEVYLIDRKNDVFKVPGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 301 FPFRKDLRSHLANTLLDGEMIIDKVNGQVVPRYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQE 380
Cdd:cd07895    81 FPRRKNLEPHHQGTLLDGELVIDKVPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLKKGPIDKAKE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1444527163 381 PFSVRNKPFFDIYTARKLLEGSFaREVSHEVDGLIFQPTG-KYKPGRCDDILKWKP 435
Cdd:cd07895   161 PFSVRLKDFFPLYKIEKLFEKII-PKLPHENDGLIFTPNDePYVPGTDKNLLKWKP 215
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 246-434 6.61e-97

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: 290.46  E-value: 6.61e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 246 QPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLIDGKNE-VYMIDRDNSIFHVSNLEFPFRKD--LRSHLANTLLDGEMII 322
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRDPEgCYIIDRDNNVYLVENLRFPRENDegLEKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 323 DKVNGQ-VVPRYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQEPFSVRNKPFFDIYTARKLLEG 401
Cdd:pfam01331  81 DTVPGQkQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMKTGRIRTDLEPFSVRRKDFWDLEASAKLLGN 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1444527163 402 SFAREVSHEVDGLIFQPTG-KYKPGRCDDILKWK 434
Cdd:pfam01331 161 KFIPNLSHESDGLIFQPVDtPYVAGRCSDLLKWK 194
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 1-146 2.71e-61

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: 197.50  E-value: 2.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163   1 MLGPRYDEQVAEENRFHPSMLSNYLKSLKvKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKgHGECPTPENTETFIRV 80
Cdd:cd14502    23 PLSDDYEHLFAPEIRFTPSALAEKFRQDR-KVGLVIDLTNTDRYYDPNDLDDDGYVYYKKVCV-RKEPPDAEEVNKFIEL 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444527163  81 C-EHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGIYKGDYLKELFR 146
Cdd:cd14502   101 VdKFLAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIYKPHYIDELYR 167
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 9-144 8.64e-39

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: 138.56  E-value: 8.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163   9 QVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHgECPTPENTETFIRVCEHFSDKN 88
Cdd:cd17665    31 NLPPEQRFTPKDLVEQVEKRGEKLGLVIDLTNTTRYYDPRDLTNHGVYYKKITCPGH-QVPDDKTIQSFKDAVKDFLEKN 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444527163  89 --PSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGIYKGDYLKEL 144
Cdd:cd17665   110 kdNDKLIGVHCTHGLNRTGYLICRYLIDVDGMSPDDAIEAFEQARGHPIERENYLEDL 167
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
242-447 1.83e-33

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 130.81  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 242 FPGAQPVSMDKQNIKFLEQKPYKVSWKADGTRYMMLI-----DGKNEVYMIDRDNSIFHVsNLEFPFR----KDLRSHLA 312
Cdd:COG5226    43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVteepvTGAFRGYFYDRRNNFYEV-HTSFPPCstvlKDGEVLLE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 313 NTLLDGEMIIDKVNGQVVP--RYLIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKMKTGLIDKAQEPFSVRNKPFF 390
Cdd:COG5226   122 DTLLDGELVFDCLPYEKVPqlRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPRERKRVSIEIDSGSFPFHFSVKQML 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444527163 391 DIYTARKLLEGsfAREVSHEVDGLIFQPTGK-YKPGRCDDILKWKPPSLNSVDFRLKI 447
Cdd:COG5226   202 KSYGFWKIYKK--IPELKHGNDGLIFTPADEpYSVGKDGALLKWKPASLNTIDFRLVL 257
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 68-146 4.37e-15

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: 71.23  E-value: 4.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  68 CPTPENTETFIRVCEHFsdKNPSELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGI-YKGDYLKELFR 146
Cdd:cd14494    36 DLTLAMVDRFLEVLDQA--EKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 256-435 1.24e-14

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: 72.07  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 256 KFLEQKPYKVSWKADGTRYMM-LIDGKneVYMIDRDNSIFHVSNLEFPFRKDLRSHLaNTLLDGEMIIDKVNG-QVVPRY 333
Cdd:cd06846    14 EYDEQDEYYVQEKYDGKRALIvALNGG--VFAISRTGLEVPLPSILIPGRELLTLKP-GFILDGELVVENREVaNPKPTY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 334 LIYDIIKFNGQPVGDCDFNVRLACIEKEIIFPRHEKmktglidkaqePFSVRNKPFFDIYTarKLLEGSFAREVSHEVDG 413
Cdd:cd06846    91 YAFDVVPLSGVGLRDLPYSDRFAYLKSLLKEFEGLD-----------PVKLVPLENAPSYD--ETLDDLLEKLKKKGKEG 157

                         170       180
                  ....*....|....*....|....*
gi 1444527163 414 LIF-QPTGKYK--PGRCDDILKWKP 435
Cdd:cd06846   158 LVFkHPDAPYKgrPGSSGNQLKLKP 182
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 14-125 4.83e-09

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: 55.54  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  14 NRFHPSMLSNYLKSLKVKmgLLVDLTNTTrfYDRNDIEKEGIKYIKLQCKgHGECPTPENTETFIRVCEhfsdkNPSELI 93
Cdd:cd14499    43 PTHTPEDYIPYFKKLGVT--TVVRLNKKL--YDAKRFTDAGIRHYDLYFP-DGSTPSDDIVKKFLDICE-----NEKGAI 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1444527163  94 GVHCTHGFNRTGFLICAFLVEKLDWSVEAAVA 125
Cdd:cd14499   113 AVHCKAGLGRTGTLIACYLMKHYGFTAREAIA 144
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
35-132 6.51e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.73  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  35 LVDLTnTTRFYDRNDIEKEGIKYIKLQCKGHGeCPTPENTETFIR-VCEHFSDKNPselIGVHCTHGFNRTGFLICAFLV 113
Cdd:COG2453    29 VVSLT-EEEELLLGLLEEAGLEYLHLPIPDFG-APDDEQLQEAVDfIDEALREGKK---VLVHCRGGIGRTGTVAAAYLV 103

                          90
                  ....*....|....*....
gi 1444527163 114 EKlDWSVEAAVATFAQARP 132
Cdd:COG2453   104 LL-GLSAEEALARVRAARP 121
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 18-114 6.78e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 46.17  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  18 PSMLSNYLKSLKvKMGL--LVDLTNTTrfYDRNDIEKEGIKyIKLQCKGHGECPTPENTETFIRVCEHF--SDKNPSELI 93
Cdd:PTZ00242   26 PSNLPLYIKELQ-RYNVthLVRVCGPT--YDAELLEKNGIE-VHDWPFDDGAPPPKAVIDNWLRLLDQEfaKQSTPPETI 101

                          90       100
                  ....*....|....*....|.
gi 1444527163  94 GVHCTHGFNRTGFLICAFLVE 114
Cdd:PTZ00242  102 AVHCVAGLGRAPILVALALVE 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 29-132 1.14e-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: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  29 KVKMGLLVDLTNTTRFYdrndieKEGIKYIKlqckghgeCPTPENTETFIrvCEHFSD--------KNPSELIGVHCTHG 100
Cdd:pfam00782  16 KLGITAVINVTREVDLY------NSGILYLR--------IPVEDNHETNI--SKYLEEavefiddaRQKGGKVLVHCQAG 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1444527163 101 FNRTGFLICAFLVEKLDWSVEAAVATFAQARP 132
Cdd:pfam00782  80 ISRSATLIIAYLMKTRNLSLNEAYSFVKERRP 111
DSP_laforin-like cd14526
dual specificity phosphatase domain of laforin and similar domains; This family is composed of ...
 49-137 4.55e-05

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: 43.34  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  49 DIEKEGIKY--IKLQCKGHG----ECPTPE-NTETFIR-----VCEHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKL 116
Cdd:cd14526    41 DMEYWGVDIdsIRKACKESGiryvRLPIRDfDTEDLRQklpqaVALLYRLLKNGGTVYVHCTAGLGRAPATVIAYLYWVL 120

                          90       100
                  ....*....|....*....|.
gi 1444527163 117 DWSVEAAVATFAQARPPGIYK 137
Cdd:cd14526   121 GYSLDEAYYLLTSKRPCGPDE 141
Snurportin-1_C cd09232
C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 ...
 271-435 9.16e-05

C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 or SNUPN) is a nuclear import adaptor for m3G-capped spliceosomal U small nucleoproteins (snRNPs), which are assembled in the cytoplasm. After capping and assembly, the U snRNPs are transported into the nucleus by SPN1 and importin beta; SPN1 is then returned to the cytoplasm by exportin 1 (CRM1), which also transports the non-capped U snRNPs. The U snRNPs are essential elements of the spliceosome, which catalyzes the excision of introns and the ligation of exons to form a mature mRNA. SPN1 contains two domains, an N-terminal importin beta-binding (IBB) domain and a C-terminal m3G cap-binding domain.


Pssm-ID: 185717  Cd Length: 186  Bit Score: 43.40  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 271 GTRYMMLI-DGKNEVYmiDRDNSIFH--VSNLefPFRKDLRSHLANTLLDGemIIDKVNGQvvprYLIYDIIKFNGQPVG 347
Cdd:cd09232    31 GKRCLVVAsKGKTVAR--SKNGRTLHrfSSAL--PGGSRKTSNSGYTILDC--IYNEDDRT----YYVLDVLCWNGHPLY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 348 DCDFNVRLACIEKEIifprhEKMKTGLIDKAQEPFSVRNKPFFDIYTA--RKLLEGSFaREVSHEVDGLIF-QPTGKYKP 424
Cdd:cd09232   101 DCETEFRFFWLRSKL-----EELPELDEPSEKNPFRFVPLPYFPCTKEslQSAYSGPL-NDDPYELDGLLFyHKESHYTP 174

                         170
                  ....*....|.
gi 1444527163 425 GRCDDILKWKP 435
Cdd:cd09232   175 GSTPLVLWLKD 185
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
93-132 1.96e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.50  E-value: 1.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1444527163   93 IGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARP 132
Cdd:smart00195  81 VLVHCQAGVSRSATLIIAYLMKTRNMSLNDAYDFVKDRRP 120
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 69-135 2.83e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 2.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444527163  69 PTPENTETFIRVCEHFSDKNpsELIGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGI 135
Cdd:cd14504    63 PTLEQIDEFLDIVEEANAKN--EAVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRPGSI 127
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 45-114 4.62e-04

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: 40.67  E-value: 4.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444527163  45 YDRNDIEKEGIKYIKLQCKgHGECPTPENTETFIRVCE-HFSDK-NPSELIGVHCTHGFNRTGFLICAFLVE 114
Cdd:cd14500    49 YDKEPLEKAGIKVHDWPFD-DGSPPPDDVVDDWLDLLKtRFKEEgKPGACIAVHCVAGLGRAPVLVAIALIE 119
PTP_auxilin-like cd14511
protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily ...
 67-135 1.28e-03

protein tyrosine phosphatase-like domain of auxilin and similar proteins; This subfamily contains proteins similar to auxilin, characterized by also containing a J domain. It includes auxilin, also called auxilin-1, and cyclin-G-associated kinase (GAK), also called auxilin-2. Auxilin-1 and -2 facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, while auxilin-1 which is nerve-specific. Both proteins contain a protein tyrosine phosphatase (PTP)-like domain similar to the PTP-like domain of PTEN (a phosphoinositide 3-phosphatase), and a C-terminal region with clathrin-binding and J domains. In addition, GAK contains an N-terminal protein kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2.


Pssm-ID: 350361 [Multi-domain]  Cd Length: 164  Bit Score: 39.64  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444527163  67 ECPTPENT----ETFIRVCEH---FSDKNPSELIGVHCTHGFNRTGFLICAFLVE-KLDWSVEAAVATFAQAR-PPGI 135
Cdd:cd14511    73 ECSWPYRRapslHALYALCRDiyqWLNKDPKNVIVIHCTDGKAASATVVCALLVYcGLFKTPEDALQMFAVKRcPPGL 150
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 95-132 1.65e-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: 38.68  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1444527163  95 VHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARP 132
Cdd:cd14498    84 VHCQAGVSRSATIVIAYLMKKYGWSLEEALELVKSRRP 121
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 24-147 2.17e-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: 38.89  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  24 YLKSLKVKmgLLVDLtnttRFYDRNDIEKE------GIKYIKLqcKGHGECPTPENTETFIRVcehFSDKNPSELIGVHC 97
Cdd:cd14529    28 LLKKLGIK--TVIDL----RGADERAASEEaaakidGVKYVNL--PLSATRPTESDVQSFLLI---MDLKLAPGPVLIHC 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444527163  98 THGFNRTGfLICAFLVEKLDWSVEAAVATFAQ-ARPPGIY------------KGDYLKELFRR 147
Cdd:cd14529    97 KHGKDRTG-LVSALYRIVYGGSKEEANEDYRLsNRHLEGLrsgialdskggvKGRYLAAYFER 158
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 68-131 2.98e-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: 38.34  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444527163  68 CPTPENTETFIRVCEHFSDKNPSELIGVHCTHGFNRTGFLICAFLVEKLDW-SVEAAVATFAQAR 131
Cdd:cd14509    72 PPPLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICCYLLYLGKFpSAKEALDFYGAKR 136
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 93-135 6.61e-03

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: 38.10  E-value: 6.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1444527163  93 IGVHCTHGFNRTGFLICAFLVEKLDWSVEAAVATFAQARPPGI 135
Cdd:cd14506   112 VAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRPNSI 154
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
70-113 7.50e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 36.18  E-value: 7.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1444527163   70 TPENTETFIRVCEHF----SDKNPSELIGVHCTHGFNRTGFLICAFLV 113
Cdd:smart00404  15 VPESPDSILELLRAVkknlNQSESSGPVVVHCSAGVGRTGTFVAIDIL 62
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 70-113 7.50e-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: 36.18  E-value: 7.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1444527163   70 TPENTETFIRVCEHF----SDKNPSELIGVHCTHGFNRTGFLICAFLV 113
Cdd:smart00012  15 VPESPDSILELLRAVkknlNQSESSGPVVVHCSAGVGRTGTFVAIDIL 62
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 18-131 8.52e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 37.89  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163  18 PSMLSNYLKSLKVKMGLLVDLTntTRFYDRNDIEKEGIKYIK-LQCKG---HGECPTPENTETFIRVCEHFSDKNPselI 93
Cdd:cd14597    96 TTMVDNRLQLTLVRMQQLKNFV--IRVLELEDIQTREVRHIThLNFTAwpdHDTPSQPEQLLTFISYMRHIHKSGP---I 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1444527163  94 GVHCTHGFNRTGFLIC-----AFLVEKLDWSVEAAVATFAQAR 131
Cdd:cd14597   171 ITHCSAGIGRSGTLICidvvlGLISKDLDFDISDIVRTMRLQR 213
DNA_ligase_A_M pfam01068
ATP dependent DNA ligase domain; This domain belongs to a more diverse superfamily, including ...
 245-434 9.07e-03

ATP dependent DNA ligase domain; This domain belongs to a more diverse superfamily, including pfam01331 and pfam01653.


Pssm-ID: 426028 [Multi-domain]  Cd Length: 203  Bit Score: 37.65  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 245 AQPVSMDKQNIKFLEQKPYkVSWKADGTRYMMLIDGkNEVYMIDRdnsifhvsNLE---------FPFRKDLRSHLANTL 315
Cdd:pfam01068   4 AKSFKSIEEALKKFGGAFI-AEYKYDGERAQIHKDG-DEVKLFSR--------NLEnitrhypeiVEALKEAFKPDEKSF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444527163 316 -LDGEMI-IDKVNGQVVPR-----------------------YLIYDIIKFNGQPVGDCDFNVRLACIEK-----EIIFP 365
Cdd:pfam01068  74 iLDGEIVaVDPETGEILPFqvladrkkkkvdveelaekvpvcLFVFDLLYLDGEDLTDLPLRERRKLLEEifkeiPGRIQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444527163 366 RHEKMKTGLIDKAQEpfsvrnkpFFDIytarkllegsfAREVSHEvdGLIF-QPTGKYKPG-RCDDILKWK 434
Cdd:pfam01068 154 LAESIVTKDVEEAQE--------FLEE-----------AISEGLE--GLVVkDPDSTYEPGkRGKNWLKIK 203
 
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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