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Conserved domains on  [gi|494871827|ref|WP_007597923|]
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tyrosine-protein phosphatase [Rhizobium sp. PDO1-076]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
53-196 2.73e-33

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


The actual alignment was detected with superfamily member cd14529:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 158  Bit Score: 116.70  E-value: 2.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  53 NFHEILPGQYYRSAQLSGDALGQYIDQYKIKTVINLRGEHVGTPWYDGEAAATasrGATLVNFPMSALK-ELKAEDVQRL 131
Cdd:cd14529    5 NFRDVTPYVLYRSAQLSPDEDRALLKKLGIKTVIDLRGADERAASEEAAAKID---GVKYVNLPLSATRpTESDVQSFLL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494871827 132 LGILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEETAEWQLSPIYGHIglPFLGAYAMDDT 196
Cdd:cd14529   82 IMDLKLAPGPVLIHCKHGKDRTGLVSALYR-IVYGGSKEEANEDYRLSNRHL--EGLRSGIALDS 143
 
Name Accession Description Interval E-value
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
53-196 2.73e-33

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: 116.70  E-value: 2.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  53 NFHEILPGQYYRSAQLSGDALGQYIDQYKIKTVINLRGEHVGTPWYDGEAAATasrGATLVNFPMSALK-ELKAEDVQRL 131
Cdd:cd14529    5 NFRDVTPYVLYRSAQLSPDEDRALLKKLGIKTVIDLRGADERAASEEAAAKID---GVKYVNLPLSATRpTESDVQSFLL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494871827 132 LGILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEETAEWQLSPIYGHIglPFLGAYAMDDT 196
Cdd:cd14529   82 IMDLKLAPGPVLIHCKHGKDRTGLVSALYR-IVYGGSKEEANEDYRLSNRHL--EGLRSGIALDS 143
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
61-172 1.28e-14

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 67.55  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  61 QYYRSAQLSGDALGQyIDQYKIKTVINLR--GEHVGTPWYDGEAAATASRGATLVNFPMSAlKELKAEDVQRLLGILKTA 138
Cdd:COG3453    7 RLSVSGQPTPEDLAA-LAAAGFKTVINLRpdGEEPDQPAAADEAAAAEAAGLEYVHIPVTG-GAITDEDVEAFAAALAAA 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494871827 139 QQPVLVHCASGAdRTGLASVIFLQQVAGVDEETA 172
Cdd:COG3453   85 PGPVLAHCRSGT-RSSALWALYQAGKGGMSPEEA 117
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
59-171 6.45e-14

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 68.04  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827   59 PGQYYRSAQLSG--DALGQYIDQYKIKTVINLRGEHvgtpwydgEAAATASR-GATLVNFPMSALKELKAEDVQR----- 130
Cdd:pfam13350  25 WGRLYRSGNLSRltDADLATLADLGIRTVIDLRSPA--------ERAAPGPApDVRYVHLPVADSEASSPELLARraldp 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494871827  131 ------------------------LLGILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEET 171
Cdd:pfam13350  97 ddgeefmaelyrdmvtsaraayraLFEALADNDGPVLFHCTAGKDRTGVAAALLL-SLLGVPEDT 160
 
Name Accession Description Interval E-value
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
53-196 2.73e-33

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: 116.70  E-value: 2.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  53 NFHEILPGQYYRSAQLSGDALGQYIDQYKIKTVINLRGEHVGTPWYDGEAAATasrGATLVNFPMSALK-ELKAEDVQRL 131
Cdd:cd14529    5 NFRDVTPYVLYRSAQLSPDEDRALLKKLGIKTVIDLRGADERAASEEAAAKID---GVKYVNLPLSATRpTESDVQSFLL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494871827 132 LGILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEETAEWQLSPIYGHIglPFLGAYAMDDT 196
Cdd:cd14529   82 IMDLKLAPGPVLIHCKHGKDRTGLVSALYR-IVYGGSKEEANEDYRLSNRHL--EGLRSGIALDS 143
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
61-172 1.28e-14

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 67.55  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  61 QYYRSAQLSGDALGQyIDQYKIKTVINLR--GEHVGTPWYDGEAAATASRGATLVNFPMSAlKELKAEDVQRLLGILKTA 138
Cdd:COG3453    7 RLSVSGQPTPEDLAA-LAAAGFKTVINLRpdGEEPDQPAAADEAAAAEAAGLEYVHIPVTG-GAITDEDVEAFAAALAAA 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494871827 139 QQPVLVHCASGAdRTGLASVIFLQQVAGVDEETA 172
Cdd:COG3453   85 PGPVLAHCRSGT-RSSALWALYQAGKGGMSPEEA 117
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
59-171 6.45e-14

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 68.04  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827   59 PGQYYRSAQLSG--DALGQYIDQYKIKTVINLRGEHvgtpwydgEAAATASR-GATLVNFPMSALKELKAEDVQR----- 130
Cdd:pfam13350  25 WGRLYRSGNLSRltDADLATLADLGIRTVIDLRSPA--------ERAAPGPApDVRYVHLPVADSEASSPELLARraldp 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494871827  131 ------------------------LLGILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEET 171
Cdd:pfam13350  97 ddgeefmaelyrdmvtsaraayraLFEALADNDGPVLFHCTAGKDRTGVAAALLL-SLLGVPEDT 160
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
59-171 6.48e-14

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 68.06  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  59 PGQYYRSAQLSG--DALGQYIDQYKIKTVINLRGEHvgtpwydgEAAATASR---GATLVNFPMSA------LKELKAED 127
Cdd:COG2365   24 WGRLYRSGALSRltDADLARLADLGIRTVIDLRSPA--------EVARAPDRlppGVRYVHLPVLPddaealLEELRDGD 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827 128 -------------------------VQRLLG-ILKTAQQPVLVHCASGADRTGLASVIFLqQVAGVDEET 171
Cdd:COG2365   96 ltpgdaeefmlelyrafvdpdaadaYRAAFRaLADAENGPVLFHCTAGKDRTGVAAALLL-LALGVPRET 164
PTP-bact cd14503
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ...
82-179 6.50e-10

bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown.


Pssm-ID: 350353 [Multi-domain]  Cd Length: 136  Bit Score: 54.94  E-value: 6.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  82 IKTVINLRGEHVGtPWYDGEAAATASRGATLVNFPMSAlKELKAEDVQRLLGILKTAQ-QPVLVHCASGAdRTGlaSVIF 160
Cdd:cd14503   28 FKTVINLRPDGEE-NALPNEAAAVTAAGMEYVHIPVDW-DNPTPEDVERFFEVMDAAQgKPVLVHCASNM-RAS--AFWY 102
                         90       100
                 ....*....|....*....|.
gi 494871827 161 LQQVA--GVDEETAEWQLSPI 179
Cdd:cd14503  103 LYRALdgGVSEEEAIQLMRSA 123
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
53-172 1.89e-08

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


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 51.22  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  53 NFHEILPGqYYRSAQLSGDALGqYIDQYKIKTVINLRGEhvgtPWYDGEAAATASRGATLVNFPMSALKELKAEDVQRLL 132
Cdd:cd18538    5 NFGVVVPG-VYRSSFPKPENFG-FLKSLGLRTILTLVQE----EYSPEFLNFLRENGIQHFHIAMLGNKDPKVSIPDHTM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494871827 133 G-----ILKTAQQPVLVHCASGADRTGLASVIFlQQVAGVDEETA 172
Cdd:cd18538   79 NrilriILDKENHPILVHCNKGKHRTGCVIACF-RKLQGWDVENV 122
BLH_phosphatase pfam04273
Beta-lactamase hydrolase-like protein, phosphatase-like domain; This domain is found ...
83-149 2.13e-06

Beta-lactamase hydrolase-like protein, phosphatase-like domain; This domain is found N-terminal to a beta-lactamase domain, and it may have phosphatase activity. This domain is found in Beta-lactamase hydrolase-like protein from Agrobacterium fabrum, which may play a role in cell adherence or biofilm development.


Pssm-ID: 398110 [Multi-domain]  Cd Length: 110  Bit Score: 44.97  E-value: 2.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494871827   83 KTVINLR--GEHVGTPWYDGEAAATASRGATLVNFPMSAlKELKAEDVQRLLGILKTAQQPVLVHCASG 149
Cdd:pfam04273  29 RSIINNRpdGEEPNQPGNAAEQAAARAAGLAYNHVPVIG-GSITEDDIQAFQAAIAAAEGPVLAHCRSG 96
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
55-156 3.03e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 42.27  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  55 HEILPGQYYRSAQLSGDAlgQYIDQYKIKTVINLRGEHvgtpwyDGEAAATASRGATLVNFPMSALKELKAEDVQRLLGI 134
Cdd:COG2453    1 SWIIPGLLAGGPLPGGGE--ADLKREGIDAVVSLTEEE------ELLLGLLEEAGLEYLHLPIPDFGAPDDEQLQEAVDF 72
                         90       100
                 ....*....|....*....|....*
gi 494871827 135 LKTA---QQPVLVHCASGADRTGLA 156
Cdd:COG2453   73 IDEAlreGKKVLVHCRGGIGRTGTV 97
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
77-156 9.81e-05

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: 41.57  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  77 IDQYK---IKTVINLR--GEHV---------GTPWYDGEAaaTASRGATLVNFPMsalKELKAEDVQRLLGILKTA---- 138
Cdd:cd14506   32 IEQFKekgIKTVINLQepGEHAscgpglepeSGFSYLPEA--FMRAGIYFYNFGW---KDYGVPSLTTILDIVKVMafal 106
                         90       100
                 ....*....|....*....|
gi 494871827 139 --QQPVLVHCASGADRTGLA 156
Cdd:cd14506  107 qeGGKVAVHCHAGLGRTGVL 126
PFA-DSP cd14501
plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical ...
53-155 2.52e-04

plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. The best characterized member is Saccharomyces Siw14, also known as Oca3, which plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7).


Pssm-ID: 350351 [Multi-domain]  Cd Length: 149  Bit Score: 39.97  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  53 NFHEILPGqYYRSAQLSGDALgQYIDQYKIKTVINLRGEHVGTP-----------WYdgEAAATASRGATLVnfpmsALK 121
Cdd:cd14501    5 NFSIVEPG-LYRSAYPTPANF-PFLKTLGLKTIILLSPEPPPKPvlsfltengikLI--HLGMLSSKRADSV-----PWD 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494871827 122 ELKAEDVQR-LLGILKTAQQPVLVHCASGADRTGL 155
Cdd:cd14501   76 PLAYELVKRaLEILLDKTNYPVLVHCSLGEHRTGV 110
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
32-159 2.37e-03

protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2.


Pssm-ID: 350498  Cd Length: 216  Bit Score: 37.84  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494871827  32 IFVAAVCLAYGVYIGVTLLR-GNFHEILPGQYYRSAQLSGDALGQYI-----DQYKIKTVI--NLRGE-------HVGTP 96
Cdd:cd17660   10 VLVEDERLSPDVLSTYKEMKvANFRRVPKMPIYGMAQPSSEALGVVLayltdAKRKHSKVLwvNLREElvleangQTFSP 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494871827  97 WYDGEAAATASRGATLVNFPMSALKELKAEDVQRLLGILKTA----QQPVLV-HCASGADRTGLASVI 159
Cdd:cd17660   90 REPGNLEQLIPVGLTYRRIPIPDFCAPREEDFDRLLEAMKSAlaedSGTAFVfNCLDGKGRTTTAMVI 157
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
82-155 6.47e-03

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: 35.72  E-value: 6.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494871827  82 IKTVINLRGEHVGTPWYDGeaaatasRGATLVNFPMSALKELKAEDVQRLLGILKTAQ---QPVLVHCASGADRTGL 155
Cdd:cd14504   29 IRHVVTLTEEPPPEHSDTC-------PGLRYHHIPIEDYTPPTLEQIDEFLDIVEEANaknEAVLVHCLAGKGRTGT 98
 
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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