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Conserved domains on  [gi|685322953|ref|XP_009151244|]
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mRNA-capping enzyme [Brassica rapa]

Protein Classification

RNA_5'-triphosphatase and Adenylation_mRNA_capping domain-containing protein( domain architecture ID 12998204)

protein containing domains RNA_5'-triphosphatase, Adenylation_mRNA_capping, and mRNA_cap_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 302-495 1.29e-83

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: 260.42  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  302 HPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTR--EGCYLIDRKFRFRRVQ-MRFPCKPHEA--RVHDYTLLDGEMVV 376
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRdpEGCYIIDRDNNVYLVEnLRFPRENDEGleKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  377 DNFldgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRNDEKKvTKGYRYEMEPFGVRVKAFCLLSSVE 456
Cdd:pfam01331  81 DTV----PGQKQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMK-TGRIRTDLEPFSVRRKDFWDLEASA 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 685322953  457 KKVFNELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWK 495
Cdd:pfam01331 156 KLLGNKFIPNLSHESDGLIFQPVDTPYVAGRCSDLLKWK 194
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 50-215 2.80e-63

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: 206.35  E-value: 2.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  50 GWLDCPRFGHEIGP--IIPSKVPLSESYNDHLPPDKRYT---FKQLLTNNKrnKLGLVIDLTNTTRYYNPStDLRREGIE 124
Cdd:cd14502    1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTpsaLAEKFRQDR--KVGLVIDLTNTDRYYDPN-DLDDDGYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 125 YVKIRCsGRDSVPDNVSVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARPPG 204
Cdd:cd14502   78 YYKKVC-VRKEPPDAEEVNKFIELVDKFLAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLG-LTVEQALEAFAQARPPG 155

                        170
                 ....*....|.
gi 685322953 205 IYKSDYIDALY 215
Cdd:cd14502  156 IYKPHYIDELY 166
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
499-593 7.07e-16

mRNA capping enzyme, C-terminal domain;


:

Pssm-ID: 461093  Cd Length: 108  Bit Score: 73.79  E-value: 7.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  499 TIDFLFEV---GRDGRYMLFLCENGRNKLMEGHAVEFRGD------GWEEPGS----YSGKLLECFWDKEdKVWVPMRVR 565
Cdd:pfam03919   2 SVDFRLKLrfpGPTEPPDYDAKPIFELFVWEGGLYEFFGElyvtdeEWEELKSlgepLDGRIVECSWDEE-GRWRFMRFR 80

                          90       100
                  ....*....|....*....|....*...
gi 685322953  566 VDKSQPNGMGTFRGVMKSINDGITKEVL 593
Cdd:pfam03919  81 DDKSNPNHISTVEKVLESIKDGVTEEDL 108
 
Name Accession Description Interval E-value
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 302-495 1.29e-83

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: 260.42  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  302 HPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTR--EGCYLIDRKFRFRRVQ-MRFPCKPHEA--RVHDYTLLDGEMVV 376
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRdpEGCYIIDRDNNVYLVEnLRFPRENDEGleKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  377 DNFldgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRNDEKKvTKGYRYEMEPFGVRVKAFCLLSSVE 456
Cdd:pfam01331  81 DTV----PGQKQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMK-TGRIRTDLEPFSVRRKDFWDLEASA 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 685322953  457 KKVFNELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWK 495
Cdd:pfam01331 156 KLLGNKFIPNLSHESDGLIFQPVDTPYVAGRCSDLLKWK 194
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 293-496 2.22e-76

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: 242.53  E-value: 2.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 293 SSSLQFPGSHPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTREG-CYLIDRKFRFRRVQMR-FPCKPHEARVHDYTLL 370
Cdd:cd07895   17 WERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGeVYLIDRKNDVFKVPGLfFPRRKNLEPHHQGTLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 371 DGEMVVDNfldgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRNDEKKvTKGYRYEMEPFGVRVKAFC 450
Cdd:cd07895   97 DGELVIDK-----VPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLK-KGPIDKAKEPFSVRLKDFF 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 685322953 451 LLSSVEkKVFNELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWKF 496
Cdd:cd07895  171 PLYKIE-KLFEKIIPKLPHENDGLIFTPNDEPYVPGTDKNLLKWKP 215
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 50-215 2.80e-63

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: 206.35  E-value: 2.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  50 GWLDCPRFGHEIGP--IIPSKVPLSESYNDHLPPDKRYT---FKQLLTNNKrnKLGLVIDLTNTTRYYNPStDLRREGIE 124
Cdd:cd14502    1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTpsaLAEKFRQDR--KVGLVIDLTNTDRYYDPN-DLDDDGYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 125 YVKIRCsGRDSVPDNVSVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARPPG 204
Cdd:cd14502   78 YYKKVC-VRKEPPDAEEVNKFIELVDKFLAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLG-LTVEQALEAFAQARPPG 155

                        170
                 ....*....|.
gi 685322953 205 IYKSDYIDALY 215
Cdd:cd14502  156 IYKPHYIDELY 166
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
298-627 3.02e-44

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 162.78  E-value: 3.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 298 FPGSHPVSLDREGFQLLRRRYYYATWKADGTRYMMLLT------REGCYLIDRKFRFRRVQ-MRFPCKPH---EARVHDY 367
Cdd:COG5226   43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVTeepvtgAFRGYFYDRRNNFYEVHtSFPPCSTVlkdGEVLLED 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 368 TLLDGEMVVDNFLdgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRnDEKKVTKGYRYEMEPFGVRVK 447
Cdd:COG5226  123 TLLDGELVFDCLP---YEKVPQLRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPR-ERKRVSIEIDSGSFPFHFSVK 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 448 AFcLLSSVEKKVFnELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWK--FLDTIDFL----FEVGRDGRYML------- 514
Cdd:COG5226  199 QM-LKSYGFWKIY-KKIPELKHGNDGLIFTPADEPYSVGKDGALLKWKpaSLNTIDFRlvlhKKWSEVDDYNYvcspkfg 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 515 -----------FLCEngrNKLMEGHAVEFRGDgwEEPgsYSGKLLECFWDKEDKvWVPMRVRVDKSQPNGMGTFRGVMKS 583
Cdd:COG5226  277 ldvwfgrktyrFFAS---GEVIDGEWCELKYD--CDP--LYWRIVECVLKKEGA-WKLLRFRDDKDTPNHISVVCNVLES 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 685322953 584 INDGITKEVLLEEIKEIVRlpmyverirmdtlAAERRRHGNRRG 627
Cdd:COG5226  349 IRDNVSIEDLSTFYSVIRE-------------NSKRREKAMRRG 379
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
499-593 7.07e-16

mRNA capping enzyme, C-terminal domain;


Pssm-ID: 461093  Cd Length: 108  Bit Score: 73.79  E-value: 7.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  499 TIDFLFEV---GRDGRYMLFLCENGRNKLMEGHAVEFRGD------GWEEPGS----YSGKLLECFWDKEdKVWVPMRVR 565
Cdd:pfam03919   2 SVDFRLKLrfpGPTEPPDYDAKPIFELFVWEGGLYEFFGElyvtdeEWEELKSlgepLDGRIVECSWDEE-GRWRFMRFR 80

                          90       100
                  ....*....|....*....|....*...
gi 685322953  566 VDKSQPNGMGTFRGVMKSINDGITKEVL 593
Cdd:pfam03919  81 DDKSNPNHISTVEKVLESIKDGVTEEDL 108
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
95-218 5.05e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.84  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  95 KRNKLGLVIDLTntTRYYNPSTDLRREGIEYVKIRCSGrDSVPDNVSVNTFVHEVNQFERRNfskKSILVHCTHGHNRTG 174
Cdd:COG2453   22 KREGIDAVVSLT--EEEELLLGLLEEAGLEYLHLPIPD-FGAPDDEQLQEAVDFIDEALREG---KKVLVHCRGGIGRTG 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685322953 175 FMVVHYLMRSSplMSVTQALKTFSDARPPGIYKSDYIDALYSFY 218
Cdd:COG2453   96 TVAAAYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 94-184 7.88e-07

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: 48.41  E-value: 7.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953   94 NKRNKLGLVIDLTNTTRYYNpstdlrrEGIEYvkIRCSGRDSVPDNVS-----VNTFVHEVNQferrnfSKKSILVHCTH 168
Cdd:pfam00782  14 LSKLGITAVINVTREVDLYN-------SGILY--LRIPVEDNHETNISkyleeAVEFIDDARQ------KGGKVLVHCQA 78

                          90
                  ....*....|....*.
gi 685322953  169 GHNRTGFMVVHYLMRS 184
Cdd:pfam00782  79 GISRSATLIIAYLMKT 94
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
74-202 2.11e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 47.66  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953    74 SYNDHLPPDKrytfkqlltnNKRNKLGLVIDLTNTTRYYNPStdlrreGIEYVKIrcsgrdSVPDNVSVNT--FVHEVNQ 151
Cdd:smart00195  12 SYSDALNLAL----------LKKLGITHVINVTNEVPNYNGS------DFTYLGV------PIDDNTETKIspYFPEAVE 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 685322953   152 F-ERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARP 202
Cdd:smart00195  70 FiEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRN-MSLNDAYDFVKDRRP 120
PRK12361 PRK12361
hypothetical protein; Provisional
 135-201 1.52e-03

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 41.53  E-value: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685322953 135 SVPdnvSVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPLMSVTQALKTFSDAR 201
Cdd:PRK12361 154 SVP---TLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIR 217
 
Name Accession Description Interval E-value
mRNA_cap_enzyme pfam01331
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ...
 302-495 1.29e-83

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: 260.42  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  302 HPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTR--EGCYLIDRKFRFRRVQ-MRFPCKPHEA--RVHDYTLLDGEMVV 376
Cdd:pfam01331   1 QPVSLSRENIQLLKQKPYYVSWKADGTRYMMLITRdpEGCYIIDRDNNVYLVEnLRFPRENDEGleKHLDGTLLDGELVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  377 DNFldgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRNDEKKvTKGYRYEMEPFGVRVKAFCLLSSVE 456
Cdd:pfam01331  81 DTV----PGQKQQPRYLIYDIVAINGQTVMQRPFYSRLFIIKREIIKPRNEEMK-TGRIRTDLEPFSVRRKDFWDLEASA 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 685322953  457 KKVFNELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWK 495
Cdd:pfam01331 156 KLLGNKFIPNLSHESDGLIFQPVDTPYVAGRCSDLLKWK 194
Adenylation_mRNA_capping cd07895
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ...
 293-496 2.22e-76

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: 242.53  E-value: 2.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 293 SSSLQFPGSHPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTREG-CYLIDRKFRFRRVQMR-FPCKPHEARVHDYTLL 370
Cdd:cd07895   17 WERGGFPGSQPVSFSRKNLELLKQNDYFVCEKSDGVRYLLLITGRGeVYLIDRKNDVFKVPGLfFPRRKNLEPHHQGTLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 371 DGEMVVDNfldgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRNDEKKvTKGYRYEMEPFGVRVKAFC 450
Cdd:cd07895   97 DGELVIDK-----VPGKKRPRYLIFDILAFNGQSVTEKPLSERLKYIKKEVIEPRNELLK-KGPIDKAKEPFSVRLKDFF 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 685322953 451 LLSSVEkKVFNELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWKF 496
Cdd:cd07895  171 PLYKIE-KLFEKIIPKLPHENDGLIFTPNDEPYVPGTDKNLLKWKP 215
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 50-215 2.80e-63

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: 206.35  E-value: 2.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  50 GWLDCPRFGHEIGP--IIPSKVPLSESYNDHLPPDKRYT---FKQLLTNNKrnKLGLVIDLTNTTRYYNPStDLRREGIE 124
Cdd:cd14502    1 KWLDCPPVGQPVGPtrFIPMKTPLSDDYEHLFAPEIRFTpsaLAEKFRQDR--KVGLVIDLTNTDRYYDPN-DLDDDGYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 125 YVKIRCsGRDSVPDNVSVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARPPG 204
Cdd:cd14502   78 YYKKVC-VRKEPPDAEEVNKFIELVDKFLAEDNPDKLIAVHCTHGFNRTGFMIVSYLVERLG-LTVEQALEAFAQARPPG 155

                        170
                 ....*....|.
gi 685322953 205 IYKSDYIDALY 215
Cdd:cd14502  156 IYKPHYIDELY 166
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 51-215 1.66e-48

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: 167.09  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  51 WLDCPRFGHEI-GPIIPSKVPLSESYNDHLPPDKRYTFKQLL--TNNKRNKLGLVIDLTNTTRYYNPStDLRREGIEYVK 127
Cdd:cd17664    2 WLNCPRKGQPVaGKFLPFKTPLGPRYDDQVPEENRFHPSMLFnyLKSLKVKLGLWIDLTNTNRFYDRN-EVEKEGCKYIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 128 IRCSGRDSVPDNVSVNTFVHEVNQFERRNfSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARPPGIYK 207
Cdd:cd17664   81 LQCKGHGECPSPEQTETFIRLCENFIEKN-PLELIGVHCTHGFNRTGFLICAYLVEKMD-WSVEAAVATFAQARPPGIYK 158


                 ....*...
gi 685322953 208 SDYIDALY 215
Cdd:cd17664  159 GDYLKELF 166
CEG1 COG5226
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification];
298-627 3.02e-44

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


Pssm-ID: 227551 [Multi-domain]  Cd Length: 404  Bit Score: 162.78  E-value: 3.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 298 FPGSHPVSLDREGFQLLRRRYYYATWKADGTRYMMLLT------REGCYLIDRKFRFRRVQ-MRFPCKPH---EARVHDY 367
Cdd:COG5226   43 FPGSQPVSFTLDNIGLLLNNDYLVCEKSDGVRALLLVTeepvtgAFRGYFYDRRNNFYEVHtSFPPCSTVlkdGEVLLED 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 368 TLLDGEMVVDNFLdgqGKPCQARRYLVYDMVAVNGVSVSDRPFSERWSVIDREVIRPRnDEKKVTKGYRYEMEPFGVRVK 447
Cdd:COG5226  123 TLLDGELVFDCLP---YEKVPQLRYLLFDCLAYAGMFVERMEKSERLKTLQKEDEKPR-ERKRVSIEIDSGSFPFHFSVK 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 448 AFcLLSSVEKKVFnELIPSLSHDSDGIILQGWDEPYVYQRNQGLLKWK--FLDTIDFL----FEVGRDGRYML------- 514
Cdd:COG5226  199 QM-LKSYGFWKIY-KKIPELKHGNDGLIFTPADEPYSVGKDGALLKWKpaSLNTIDFRlvlhKKWSEVDDYNYvcspkfg 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 515 -----------FLCEngrNKLMEGHAVEFRGDgwEEPgsYSGKLLECFWDKEDKvWVPMRVRVDKSQPNGMGTFRGVMKS 583
Cdd:COG5226  277 ldvwfgrktyrFFAS---GEVIDGEWCELKYD--CDP--LYWRIVECVLKKEGA-WKLLRFRDDKDTPNHISVVCNVLES 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 685322953 584 INDGITKEVLLEEIKEIVRlpmyverirmdtlAAERRRHGNRRG 627
Cdd:COG5226  349 IRDNVSIEDLSTFYSVIRE-------------NSKRREKAMRRG 379
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 64-216 1.92e-36

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: 133.94  E-value: 1.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  64 IIPSKVPLSESYNDHLPPDKRYTFKQLL-TNNKRN-KLGLVIDLTNTTRYYNPsTDLRREGIEYVKIRCSGRdSVPDNVS 141
Cdd:cd17665   17 FIAFKVPLRKSFFANLPPEQRFTPKDLVeQVEKRGeKLGLVIDLTNTTRYYDP-RDLTNHGVYYKKITCPGH-QVPDDKT 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685322953 142 VNTFVHEVNQFERRNFSK-KSILVHCTHGHNRTGFMVVHYLMrSSPLMSVTQALKTFSDARPPGIYKSDYIDALYS 216
Cdd:cd17665   95 IQSFKDAVKDFLEKNKDNdKLIGVHCTHGLNRTGYLICRYLI-DVDGMSPDDAIEAFEQARGHPIERENYLEDLLK 169
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 299-496 1.73e-18

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: 83.62  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 299 PGSHPVSLDREGFQLLRRRYYYATWKADGTRYMMLLTREGCYLIDRK-FRFRRVQMRFPckPHEARV-HDYTLLDGEMVV 376
Cdd:cd06846    1 PQLLNPILEEALSEYDEQDEYYVQEKYDGKRALIVALNGGVFAISRTgLEVPLPSILIP--GRELLTlKPGFILDGELVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 377 DNFLDGQGKPCqarrYLVYDMVAVNGVSVSDRPFSERWSVIdrevirprndeKKVTKGYRYEMEPFGVRVKAFCLLSSVE 456
Cdd:cd06846   79 ENREVANPKPT----YYAFDVVPLSGVGLRDLPYSDRFAYL-----------KSLLKEFEGLDPVKLVPLENAPSYDETL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 685322953 457 KKVFNELipsLSHDSDGIILQGWDEPY--VYQRNQGLLKWKF 496
Cdd:cd06846  144 DDLLEKL---KKKGKEGLVFKHPDAPYkgRPGSSGNQLKLKP 182
mRNA_cap_C pfam03919
mRNA capping enzyme, C-terminal domain;
499-593 7.07e-16

mRNA capping enzyme, C-terminal domain;


Pssm-ID: 461093  Cd Length: 108  Bit Score: 73.79  E-value: 7.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  499 TIDFLFEV---GRDGRYMLFLCENGRNKLMEGHAVEFRGD------GWEEPGS----YSGKLLECFWDKEdKVWVPMRVR 565
Cdd:pfam03919   2 SVDFRLKLrfpGPTEPPDYDAKPIFELFVWEGGLYEFFGElyvtdeEWEELKSlgepLDGRIVECSWDEE-GRWRFMRFR 80

                          90       100
                  ....*....|....*....|....*...
gi 685322953  566 VDKSQPNGMGTFRGVMKSINDGITKEVL 593
Cdd:pfam03919  81 DDKSNPNHISTVEKVLESIKDGVTEEDL 108
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
95-218 5.05e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.84  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  95 KRNKLGLVIDLTntTRYYNPSTDLRREGIEYVKIRCSGrDSVPDNVSVNTFVHEVNQFERRNfskKSILVHCTHGHNRTG 174
Cdd:COG2453   22 KREGIDAVVSLT--EEEELLLGLLEEAGLEYLHLPIPD-FGAPDDEQLQEAVDFIDEALREG---KKVLVHCRGGIGRTG 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685322953 175 FMVVHYLMRSSplMSVTQALKTFSDARPPGIYKSDYIDALYSFY 218
Cdd:COG2453   96 TVAAAYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 142-215 1.47e-08

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: 53.12  E-value: 1.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685322953 142 VNTFVHEVNQFERRNfskKSILVHCTHGHNRTGFMVVHYLMRSSpLMSVTQALKTFSDARPPGI-YKSDYIDALY 215
Cdd:cd14494   42 VDRFLEVLDQAEKPG---EPVLVHCKAGVGRTGTLVACYLVLLG-GMSAEEAVRIVRLIRPGGIpQTIEQLDFLI 112
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 94-184 7.88e-07

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: 48.41  E-value: 7.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953   94 NKRNKLGLVIDLTNTTRYYNpstdlrrEGIEYvkIRCSGRDSVPDNVS-----VNTFVHEVNQferrnfSKKSILVHCTH 168
Cdd:pfam00782  14 LSKLGITAVINVTREVDLYN-------SGILY--LRIPVEDNHETNISkyleeAVEFIDDARQ------KGGKVLVHCQA 78

                          90
                  ....*....|....*.
gi 685322953  169 GHNRTGFMVVHYLMRS 184
Cdd:pfam00782  79 GISRSATLIIAYLMKT 94
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
74-202 2.11e-06

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 47.66  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953    74 SYNDHLPPDKrytfkqlltnNKRNKLGLVIDLTNTTRYYNPStdlrreGIEYVKIrcsgrdSVPDNVSVNT--FVHEVNQ 151
Cdd:smart00195  12 SYSDALNLAL----------LKKLGITHVINVTNEVPNYNGS------DFTYLGV------PIDDNTETKIspYFPEAVE 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 685322953   152 F-ERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFSDARP 202
Cdd:smart00195  70 FiEDAESKGGKVLVHCQAGVSRSATLIIAYLMKTRN-MSLNDAYDFVKDRRP 120
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 135-219 3.08e-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: 47.27  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 135 SVPDNVSVNTFVHevnQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSpLMSVTQALKTFSDARPPGIYKSDYIDAL 214
Cdd:cd14504   61 TPPTLEQIDEFLD---IVEEANAKNEAVLVHCLAGKGRTGTMLACYLVKTG-KISAVDAINEIRRIRPGSIETSEQEKFV 136


                 ....*
gi 685322953 215 YSFYH 219
Cdd:cd14504  137 IQFAK 141
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 78-182 1.22e-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: 45.83  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  78 HLPPDK-RYTFKQLltnnkrnKLGLVIDLTNT-TRYYNPSTDLRREGIEYVKIRCSGRDSVPDNVsvntfvHEVNQFERR 155
Cdd:cd14529   19 QLSPDEdRALLKKL-------GIKTVIDLRGAdERAASEEAAAKIDGVKYVNLPLSATRPTESDV------QSFLLIMDL 85

                         90       100
                 ....*....|....*....|....*..
gi 685322953 156 NFSKKSILVHCTHGHNRTGFMVVHYLM 182
Cdd:cd14529   86 KLAPGPVLIHCKHGKDRTGLVSALYRI 112
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 95-202 4.34e-05

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: 43.69  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  95 KRNKLGLVIDLTNttryyNPSTDLRREGIEYVKIrcsgrdSVPDNVSVNTFVH--EVNQFERRNFSKK-SILVHCTHGHN 171
Cdd:cd14498   23 KKLGITHILNVAG-----EPPPNKFPDGIKYLRI------PIEDSPDEDILSHfeEAIEFIEEALKKGgKVLVHCQAGVS 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 685322953 172 RTGFMVVHYLMRSSPlMSVTQALKTFSDARP 202
Cdd:cd14498   92 RSATIVIAYLMKKYG-WSLEEALELVKSRRP 121
Adenylation_DNA_ligase_LigD_LigC cd07906
Adenylation domain of Mycobacterium tuberculosis LigD and LigC-like ATP-dependent DNA ligases; ...
 321-413 7.21e-05

Adenylation domain of Mycobacterium tuberculosis LigD and LigC-like ATP-dependent DNA ligases; Bacterial DNA ligases are divided into two broad classes: NAD-dependent and ATP-dependent. All bacterial species have a NAD-dependent DNA ligase (LigA). Some bacterial genomes contain multiple genes for DNA ligases that are predicted to use ATP as their cofactor, including Mycobacterium tuberculosis LigB, LigC, and LigD. This group is composed of ATP-dependent DNA ligases similar to Mycobacterium tuberculosis LigC. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation using nicked nucleic acid substrates with the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. Members of this group contain adenylation and C-terminal oligonucleotide/oligosaccharide binding (OB)-fold domains, comprising a catalytic core unit that is common to all members of the ATP-dependent DNA ligase family. The adenylation domain binds ATP and contains many of the active-site residues. The common catalytic core unit comprises six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases. LigD consists of a central ATP-dependent DNA ligase catalytic core unit fused to a C-terminal polymerase domain and an N-terminal 3'-phosphoesterase (PE) module. LigD catalyzes the end-healing and end-sealing steps during non-homologous end joining.


Pssm-ID: 185715 [Multi-domain]  Cd Length: 190  Bit Score: 44.07  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 321 ATWKADGTRymmLLTREGcylidrkfrfRRVQMRFP--------CKPHEArvhdytLLDGEMVVdnfLDGQGKPC----Q 388
Cdd:cd07906   31 ARVDGGRVR---LYSRNG----------LDWTARFPelaealaaLPVRDA------VLDGEIVV---LDEGGRPDfqalQ 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685322953 389 AR-------------RYLVYDMVAVNGVSVSDRPFSER 413
Cdd:cd07906   89 NRlrlrrrlartvpvVYYAFDLLYLDGEDLRGLPLLER 126
CDC9 COG1793
ATP-dependent DNA ligase [Replication, recombination and repair];
368-515 8.83e-05

ATP-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 441398 [Multi-domain]  Cd Length: 435  Bit Score: 45.30  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 368 TLLDGEMVVdnfLDGQGKP----CQAR----------------RYLVYDMVAVNGVSVSDRPFSERWSVIdREVIRPRND 427
Cdd:COG1793  180 AVLDGEIVA---LDEDGRPpfqaLQQRlgrkrdvaklarevpvVFYAFDLLYLDGEDLRDLPLSERRALL-EELLAGAPP 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 428 EKKVTKgyryemepfgvrvkafcLLSSVE--KKVFNElipSLSHDSDGIILQGWDEPYVY-QRNQGLLKWKFLDTIDFL- 503
Cdd:COG1793  256 PLRLSP-----------------HVIDWGegEALFAA---AREAGLEGVMAKRLDSPYRPgRRSGDWLKVKCPRTQDLVv 315

                        170
                 ....*....|....
gi 685322953 504 --FEVGRDGRYMLF 515
Cdd:COG1793  316 ggATPGKGRRAGGF 329
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
134-202 1.09e-04

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 41.58  E-value: 1.09e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685322953   134 DSVPDNV-SVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTG-FMVVHYLM----RSSPLMSVTQALKTFSDARP 202
Cdd:smart00404  13 HGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLqqleAEAGEVDIFDTVKELRSQRP 87
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 134-202 1.09e-04

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: 41.58  E-value: 1.09e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685322953   134 DSVPDNV-SVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTG-FMVVHYLM----RSSPLMSVTQALKTFSDARP 202
Cdd:smart00012  13 HGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGtFVAIDILLqqleAEAGEVDIFDTVKELRSQRP 87
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 160-214 4.53e-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: 40.72  E-value: 4.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 685322953 160 KSILVHCTHGHNRTGFMVVHYLMRSSPLMSVTQALKTFSDARPPGIYKSDYIDAL 214
Cdd:cd14527   77 GPVLVHCALGYGRSATVVAAWLLAYGRAKSVAEAEALIRAARPQVVLNPAQRKAL 131
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 136-201 6.82e-04

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: 40.81  E-value: 6.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685322953 136 VPDNVSVNTFVHEVNQFERRNfSKKSILVHCTHGHNRTGFMVVHYLMRSSPLMSVTQALKTFSDAR 201
Cdd:cd14510   86 VPTLDEMLSFTAEVREWMAAD-PKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAKEALEYFGERR 150
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 95-202 7.40e-04

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: 40.32  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  95 KRNKLGLVIDLTN---TTRYYNPSTDLRREGIEYvkIRCSGRD--SVPDNVSVNT---FVHEVNQferrnfSKKSILVHC 166
Cdd:cd14524   25 AKENVRGVITMNEeyeTRFFCNSKEEWKALGVEQ--LRLPTVDftGVPSLEDLEKgvdFILKHRE------KGKSVYVHC 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685322953 167 THGHNRTGFMVVHYLMRSSpLMSVTQALKTFSDARP 202
Cdd:cd14524   97 KAGRGRSATIVACYLIQHK-GWSPEEAQEFLRSKRP 131
PRK12361 PRK12361
hypothetical protein; Provisional
 135-201 1.52e-03

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 41.53  E-value: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685322953 135 SVPdnvSVNTFVHEVNQFERRNFSKKSILVHCTHGHNRTGFMVVHYLMRSSPLMSVTQALKTFSDAR 201
Cdd:PRK12361 154 SVP---TLAQLNQAINWIHRQVRANKSVVVHCALGRGRSVLVLAAYLLCKDPDLTVEEVLQQIKQIR 217
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 120-202 3.70e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They 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. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 38.11  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 120 REGIEYVKIRCSgrDSVPDNVS-----VNTFVHEVnqfeRRNfsKKSILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQAL 194
Cdd:cd14519   41 LEDIKYLCIPAA--DTPEQNISqhfreCINFIHEA----RLN--GGNVLVHCLAGVSRSVTIVAAYLMTVTD-LGWRDAL 111


                 ....*...
gi 685322953 195 KTFSDARP 202
Cdd:cd14519  112 KAVRAARP 119
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 159-202 4.24e-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: 38.40  E-value: 4.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 685322953 159 KKSILVHCTHGHNRTGFMVVHYLMRSSPLMSVTQALKTFSDARP 202
Cdd:cd14505  106 GKKVLIHCKGGLGRTGLIAACLLLELGDTLDPEQAIAAVRALRP 149
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 96-202 5.87e-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: 37.81  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953  96 RNKLGLVIDLTNTTryynPSTDLRREGIEYVkiRCSGRDSVPDNVsvNTFVHEVNQF-ERRNFSKKSILVHCTHGHNRTG 174
Cdd:cd14567   24 RLNIGYVLNVTTHL----PLYHEGKGGFRYK--RLPATDSNKQNL--RQYFEEAFEFiEEAHQSGKGVLVHCQAGVSRSA 95

                         90       100
                 ....*....|....*....|....*...
gi 685322953 175 FMVVHYLMRSSPlMSVTQALKTFSDARP 202
Cdd:cd14567   96 TIVIAYLMKHTR-MTMTDAYKFVKNKRP 122
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 122-201 6.82e-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: 37.58  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685322953 122 GIEYVKIRCSGRDSVPDNV---SVNTFVHEVNQFERrnfSKksILVHCTHGHNRTGFMVVHYLMRSSPlMSVTQALKTFS 198
Cdd:cd14515   53 GIIYLGIPASDLPTFDISQyfdEAADFIDKALSDPG---GK--VLVHCVEGVSRSATLVLAYLMIYQN-MTLEEAIRTVR 126


                 ...
gi 685322953 199 DAR 201
Cdd:cd14515  127 KKR 129
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 158-203 8.60e-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: 37.30  E-value: 8.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 685322953 158 SKKSILVHCTHGHNRTGFMVVHYLMRSSPLmSVTQALKTFSDARPP 203
Cdd:cd14518   89 HGGAVLVHCAMGKSRSVTVVIAYLMYKYNL-SVSQALHAVRRKRPI 133
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 158-202 8.74e-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: 37.23  E-value: 8.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 685322953 158 SKKSILVHCTHGHNRTGFMVVHYLMRSSPLmSVTQALKTFSDARP 202
Cdd:cd14520   78 AEGAVLVHCHAGVSRSAAVVTAYLMKTEQL-SFEEALASLRECKP 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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