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Conserved domains on  [gi|491198765|ref|WP_005057109|]
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metallophosphoesterase [Mycobacteroides abscessus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11444094)

metallophosphatase family protein containing an active site consisting of two metal ions

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0016787|GO:0046872|GO:0042578
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
8-252 1.34e-17

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.12  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   8 TLWAISDLHVGQSANKSVLEELH------PASPEDWLIVAGDVAER--SDDIRAALDLLRRRFTKVIWVPGNHELWTtar 79
Cdd:COG1409    2 RFAHISDLHLGAPDGSDTAEVLAaaladiNAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  80 dpmqifgqsryDYLVNMCDEMGVITPEHPYPVwveqggpativpmFVLYDYTFLpeganskaeglkiardrnvvatdeFL 159
Cdd:COG1409   79 -----------AMAEAYREYFGDLPPGGLYYS-------------FDYGGVRFI------------------------GL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765 160 LSSEPFATRDAWCRDRLRYTRKRLEDLDwMTPTVLVNHFPLVREPCDalfyPEFSLWCGTTETADWHTRYNAACSVYGHL 239
Cdd:COG1409  111 DSNVPGRSSGELGPEQLAWLEEELAAAP-AKPVIVFLHHPPYSTGSG----SDRIGLRNAEELLALLARYGVDLVLSGHV 185

                        250
                 ....*....|...
gi 491198765 240 HIPRTTWYDDVRF 252
Cdd:COG1409  186 HRYERTRRDGVPY 198
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
8-252 1.34e-17

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.12  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   8 TLWAISDLHVGQSANKSVLEELH------PASPEDWLIVAGDVAER--SDDIRAALDLLRRRFTKVIWVPGNHELWTtar 79
Cdd:COG1409    2 RFAHISDLHLGAPDGSDTAEVLAaaladiNAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  80 dpmqifgqsryDYLVNMCDEMGVITPEHPYPVwveqggpativpmFVLYDYTFLpeganskaeglkiardrnvvatdeFL 159
Cdd:COG1409   79 -----------AMAEAYREYFGDLPPGGLYYS-------------FDYGGVRFI------------------------GL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765 160 LSSEPFATRDAWCRDRLRYTRKRLEDLDwMTPTVLVNHFPLVREPCDalfyPEFSLWCGTTETADWHTRYNAACSVYGHL 239
Cdd:COG1409  111 DSNVPGRSSGELGPEQLAWLEEELAAAP-AKPVIVFLHHPPYSTGSG----SDRIGLRNAEELLALLARYGVDLVLSGHV 185

                        250
                 ....*....|...
gi 491198765 240 HIPRTTWYDDVRF 252
Cdd:COG1409  186 HRYERTRRDGVPY 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 8-105 2.61e-11

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 59.92  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765    8 TLWAISDLHVGQSAN--KSVLEELHPASPEDWLIVAGDVAERSDDIRAALDLLRR--RFTKVIWVPGNHELWTTARDPMQ 83
Cdd:pfam00149   2 RILVIGDLHLPGQLDdlLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERliKYVPVYLVRGNHDFDYGECLRLY 81

                          90       100
                  ....*....|....*....|..
gi 491198765   84 IFgQSRYDYLVNMCDEMGVITP 105
Cdd:pfam00149  82 PY-LGLLARPWKRFLEVFNFLP 102
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 11-75 1.65e-07

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 49.57  E-value: 1.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491198765  11 AISDLHVGQSANKSVLEELHPASPE-DWLIVAGDVAERSDDIRAALDLLRR---RFTKVIWVPGNHELW 75
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAKAEKpDLVICLGDLVDYGPDPEEVELKALRlllAGIPVYVVPGNHDIL 70
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
8-252 1.34e-17

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 80.12  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   8 TLWAISDLHVGQSANKSVLEELH------PASPEDWLIVAGDVAER--SDDIRAALDLLRRRFTKVIWVPGNHELWTtar 79
Cdd:COG1409    2 RFAHISDLHLGAPDGSDTAEVLAaaladiNAPRPDFVVVTGDLTDDgePEEYAAAREILARLGVPVYVVPGNHDIRA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  80 dpmqifgqsryDYLVNMCDEMGVITPEHPYPVwveqggpativpmFVLYDYTFLpeganskaeglkiardrnvvatdeFL 159
Cdd:COG1409   79 -----------AMAEAYREYFGDLPPGGLYYS-------------FDYGGVRFI------------------------GL 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765 160 LSSEPFATRDAWCRDRLRYTRKRLEDLDwMTPTVLVNHFPLVREPCDalfyPEFSLWCGTTETADWHTRYNAACSVYGHL 239
Cdd:COG1409  111 DSNVPGRSSGELGPEQLAWLEEELAAAP-AKPVIVFLHHPPYSTGSG----SDRIGLRNAEELLALLARYGVDLVLSGHV 185

                        250
                 ....*....|...
gi 491198765 240 HIPRTTWYDDVRF 252
Cdd:COG1409  186 HRYERTRRDGVPY 198
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 8-105 2.61e-11

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 59.92  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765    8 TLWAISDLHVGQSAN--KSVLEELHPASPEDWLIVAGDVAERSDDIRAALDLLRR--RFTKVIWVPGNHELWTTARDPMQ 83
Cdd:pfam00149   2 RILVIGDLHLPGQLDdlLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERliKYVPVYLVRGNHDFDYGECLRLY 81

                          90       100
                  ....*....|....*....|..
gi 491198765   84 IFgQSRYDYLVNMCDEMGVITP 105
Cdd:pfam00149  82 PY-LGLLARPWKRFLEVFNFLP 102
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
9-263 8.24e-09

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 54.64  E-value: 8.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   9 LWAISDLHVGQSANKSVLEELHPASPeDWLIVAGDVAE--RSDDIRAALDLLRRRFTKVIWVPGNHElwttardpmqifg 86
Cdd:COG2129    2 ILAVSDLHGNFDLLEKLLELARAEDA-DLVILAGDLTDfgTAEEAREVLEELAALGVPVLAVPGNHD------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  87 qsrYDYLVNMCDEMGVItpehpypvWVEqGGPATIvpmfvlydytflpeganskaEGLKIARDRNVVATdefllssePFA 166
Cdd:COG2129   68 ---DPEVLDALEESGVH--------NLH-GRVVEI--------------------GGLRIAGLGGSRPT--------PFG 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765 167 TRDAWCRDRLRYTRKRLEDLDwmtPTVLVNHFPLVREPCDalfYPEFSLWCGTTETADWHTRYNAACSVYGHLHIPR-TT 245
Cdd:COG2129  108 TPYEYTEEEIEERLAKLREKD---VDILLTHAPPYGTTLD---RVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRgVD 181

                        250
                 ....*....|....*...
gi 491198765 246 WYDDVRFeeVSVGYPREW 263
Cdd:COG2129  182 KIGGTRV--VNPGSLAEG 197
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 11-75 1.65e-07

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 49.57  E-value: 1.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491198765  11 AISDLHVGQSANKSVLEELHPASPE-DWLIVAGDVAERSDDIRAALDLLRR---RFTKVIWVPGNHELW 75
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAKAEKpDLVICLGDLVDYGPDPEEVELKALRlllAGIPVYVVPGNHDIL 70
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 13-85 3.46e-05

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 43.86  E-value: 3.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491198765  13 SDLHVGQSANKSVLEELHPASPEDWLIVAGDVAERSDDI--RAALDLLRRRFTKVIWVPGNHELWTTARDPMQIF 85
Cdd:cd07404    5 SDLHLEVEQNLAKLKFFPKVPDADILILAGDIGRLTDAEawDNFLDLQSFQFEPVYYVPGNHEFYGGSLDITLDA 79
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 12-72 5.08e-05

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 42.28  E-value: 5.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491198765  12 ISDLHVGQSANKSVLE--------ELHPaspeDWLIVAGDVAERSDD-----IRAALDLLRRRftKVIWVPGNH 72
Cdd:cd07400    4 ISDLHFGEERKPEVLElnlldeinALKP----DLVVVTGDLTQRARPaefeeAREFLDALEPE--PVVVVPGNH 71
DR1119 COG1768
Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function ...
 8-75 6.57e-05

Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function prediction only];


Pssm-ID: 441374 [Multi-domain]  Cd Length: 230  Bit Score: 43.27  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   8 TLWAISDLHVGQSANKS--VLEEL---HPA----------SPEDWLIVAGDV--AERSDDIRAALDLLRRR-FTKVIwVP 69
Cdd:COG1768    2 RIYAIGDLHLSFAPDKPmdVFGERwenHPEkiaenwretvGPDDTVLIPGDIswAMKLEEALPDLDWIDALpGRKVL-IK 80


                 ....*.
gi 491198765  70 GNHELW 75
Cdd:COG1768   81 GNHDYW 86
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
12-95 1.42e-04

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 42.86  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  12 ISDLHVGQSANKSVLE-------ELHPaspeDWLIVAGD-VAERSDDIRAALDLLrRRFTK---VIWVPGNHELWTTARD 80
Cdd:COG1408   48 LSDLHLGPFIGGERLErlvekinALKP----DLVVLTGDlVDGSVAELEALLELL-KKLKAplgVYAVLGNHDYYAGLEE 122

                         90
                 ....*....|....*
gi 491198765  81 PMQIFGQSRYDYLVN 95
Cdd:COG1408  123 LRAALEEAGVRVLRN 137
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 12-82 2.57e-03

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 38.41  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765  12 ISDLHVGQSANKSVLE-------ELHPaspeDWLIVAGDVAERS-DDIRAALDLLRRRFTK--VIWVPGNHELWTTARDP 81
Cdd:cd07385    7 LSDIHLGPFVGRTRLQkvvrkvnELNP----DLIVITGDLVDGDvSVLRLLASPLSKLKAPlgVYFVLGNHDYYSGDVEV 82


                 .
gi 491198765  82 M 82
Cdd:cd07385   83 W 83
COG1407 COG1407
Metallophosphoesterase superfamily enzyme [General function prediction only];
4-72 3.42e-03

Metallophosphoesterase superfamily enzyme [General function prediction only];


Pssm-ID: 441017  Cd Length: 224  Bit Score: 38.32  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491198765   4 EREPTLwAISDLHVGQSAN--------------------KSVLEELHPaspeDWLIVAGDV----AERSDDIRAALDLLR 59
Cdd:COG1407   21 PAERTL-VVADLHLGKESAfrrrgiplppydtretlerlEALIERTGP----DRLIILGDLfhdfGGPSRQEWEELERLL 95

                         90
                 ....*....|....*
gi 491198765  60 R--RFTKVIWVPGNH 72
Cdd:COG1407   96 AlhAGVEVILVRGNH 110
MPP_YbbF-LpxH cd07398
Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an ...
 12-75 6.57e-03

Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain; YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277343 [Multi-domain]  Cd Length: 217  Bit Score: 37.34  E-value: 6.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491198765  12 ISDLHVGQSANKSV--LEEL--HPASPEDWLIVAGD-----------VAERSDDIRAALDLLRRRFTKVIWVPGNHELW 75
Cdd:cd07398    3 ISDLHLGLRGCRADrlLDFLlvEELDEADALYLLGDifdlwigddsvVWPGAHRALARLLRLADRGTEVIYVPGNHDFL 81
 
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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