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Conserved domains on  [gi|15220552|ref|NP_174271|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

Protein Classification

dullard-like phosphatase domain-containing protein( domain architecture ID 10020532)

dullard-like phosphatase domain-containing protein similar to Homo sapiens CTD nuclear envelope phosphatase 1( also known as dullard), which functions as a serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 49-210 7.70e-85

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


:

Pssm-ID: 274055  Cd Length: 162  Bit Score: 248.75  E-value: 7.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    49 KRTIILDLDETLVHATTHLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLD- 127
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   128 KNGVISQRLYRDSCTEVNGKYVKDLSLvVGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKDQELLNLVEFLESCYA 207
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSL-VGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGLRF 159


                  ...
gi 15220552   208 YED 210
Cdd:TIGR02251 160 EDD 162
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 49-210 7.70e-85

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 248.75  E-value: 7.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    49 KRTIILDLDETLVHATTHLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLD- 127
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   128 KNGVISQRLYRDSCTEVNGKYVKDLSLvVGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKDQELLNLVEFLESCYA 207
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSL-VGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGLRF 159


                  ...
gi 15220552   208 YED 210
Cdd:TIGR02251 160 EDD 162
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 51-212 2.03e-62

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 191.68  E-value: 2.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    51 TIILDLDETLVHATTHLPGVKHDFmvmVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLDKNG 130
Cdd:pfam03031   2 TLVLDLDETLVHSSFEPPLKSDFI---LPVPGETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   131 V-ISQRLYRDSCTEVNGKYVKDLSLVvGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKDQELLNLVEFLESCYAYE 209
Cdd:pfam03031  79 KlFSHRLYRESCKFEDGVYVKDLSLL-GRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLAGVD 157


                  ...
gi 15220552   210 DMR 212
Cdd:pfam03031 158 DVR 160
CPDc smart00577
catalytic domain of ctd-like phosphatases;
49-192 2.76e-59

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 183.20  E-value: 2.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552     49 KRTIILDLDETLVHAT--THLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKL 126
Cdd:smart00577   2 KKTLVLDLDETLVHSThrSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDLL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220552    127 D-KNGVISQRLYRDSCTEVNGKYVKDLSLvVGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKD 192
Cdd:smart00577  82 DpKKYFGYRRLFRDECVFVKGKYVKDLSL-LNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDD 147
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 49-183 2.32e-54

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 170.08  E-value: 2.32e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552  49 KRTIILDLDETLVHaTTHLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLDK 128
Cdd:cd07521   1 KLTLVLDLDETLVH-STWKPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDP 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15220552 129 NG-VISQRLYRDSCTEVNGKYVKDLSlVVGKDLRSALIVDDNPSSYSLQPENGVPI 183
Cdd:cd07521  80 NGlFIDRRLFRDSCVYVDGNYVKDLS-KLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 49-210 7.70e-85

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 248.75  E-value: 7.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    49 KRTIILDLDETLVHATTHLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLD- 127
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   128 KNGVISQRLYRDSCTEVNGKYVKDLSLvVGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKDQELLNLVEFLESCYA 207
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSL-VGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGLRF 159


                  ...
gi 15220552   208 YED 210
Cdd:TIGR02251 160 EDD 162
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 51-212 2.03e-62

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 191.68  E-value: 2.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    51 TIILDLDETLVHATTHLPGVKHDFmvmVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLDKNG 130
Cdd:pfam03031   2 TLVLDLDETLVHSSFEPPLKSDFI---LPVPGETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   131 V-ISQRLYRDSCTEVNGKYVKDLSLVvGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKDQELLNLVEFLESCYAYE 209
Cdd:pfam03031  79 KlFSHRLYRESCKFEDGVYVKDLSLL-GRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLAGVD 157


                  ...
gi 15220552   210 DMR 212
Cdd:pfam03031 158 DVR 160
CPDc smart00577
catalytic domain of ctd-like phosphatases;
49-192 2.76e-59

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 183.20  E-value: 2.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552     49 KRTIILDLDETLVHAT--THLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKL 126
Cdd:smart00577   2 KKTLVLDLDETLVHSThrSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDLL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220552    127 D-KNGVISQRLYRDSCTEVNGKYVKDLSLvVGKDLRSALIVDDNPSSYSLQPENGVPIKAFVDDLKD 192
Cdd:smart00577  82 DpKKYFGYRRLFRDECVFVKGKYVKDLSL-LNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDD 147
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 49-183 2.32e-54

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 170.08  E-value: 2.32e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552  49 KRTIILDLDETLVHaTTHLPGVKHDFMVMVKMEREIMPIFVVKRPGVTEFLERLGENYKVVVFTAGLEEYASQVLDKLDK 128
Cdd:cd07521   1 KLTLVLDLDETLVH-STWKPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDP 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15220552 129 NG-VISQRLYRDSCTEVNGKYVKDLSlVVGKDLRSALIVDDNPSSYSLQPENGVPI 183
Cdd:cd07521  80 NGlFIDRRLFRDSCVYVDGNYVKDLS-KLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 47-186 2.51e-12

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


Pssm-ID: 131304  Cd Length: 156  Bit Score: 62.30  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    47 NMKRTIILDLDETLVHAT------------------THLPGVKHdfMVMVKMEReimpiFVVKRPGVTEFLERLGENYKV 108
Cdd:TIGR02250   4 EKKLHLVLDLDQTLIHTTkdptlsewekydieepnsETRRDLRK--FNLGTMWY-----LTKLRPFLHEFLKEASKLYEM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   109 VVFTAGLEEYASQVLDKLDKNGVI-SQR-LYRDSCTEVngkYVKDLSLVVGKDLRSALIVDDNPSSYSLQPENGVPIKAF 186
Cdd:TIGR02250  77 HVYTMGTRAYAQAIAKLIDPDGKYfGDRiISRDESGSP---HTKSLLRLFPADESMVVIIDDREDVWPWHKRNLIQIEPY 153
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 52-171 4.38e-04

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 38.53  E-value: 4.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552  52 IILDLDETLVhatthlpgvkhdfmvmvkmereimpifvvkrpgVTEFLERLGE-NYKVVVFTAGLEEYASQVLDKLDKNG 130
Cdd:cd01427   2 VLFDLDGTLL---------------------------------AVELLKRLRAaGIKLAIVTNRSREALRALLEKLGLGD 48

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15220552 131 VISQRLYRDSC--TEVNGKYVKDLSLVVGKDLRSALIVDDNPS 171
Cdd:cd01427  49 LFDGIIGSDGGgtPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91
HAD_IIID1 TIGR02245
HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to ...
 34-213 5.28e-04

HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD.


Pssm-ID: 131299  Cd Length: 195  Bit Score: 39.80  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552    34 KFEKLEDPLTGytnmKRTIILDLDETLVhatthlpgvkhDFMVMVKMEREIMpifvvkRPGVTEFLERLGENYKVVVFTA 113
Cdd:TIGR02245  10 KIKLLNPPREG----KKLLVLDIDYTLF-----------DHRSPAETGEELM------RPYLHEFLTSAYEDYDIVIWSA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220552   114 GLEEYasqVLDKLDKNGVISQRLYR-----DSC------TEVNGKY-VKDLSLVVGK-----DLRSALIVDDNPSSYSLQ 176
Cdd:TIGR02245  69 TSMKW---IEIKMTELGVLTNPNYKitfllDSTamitvhTPRRGKFdVKPLGVIWALlpefySMKNTIMFDDLRRNFLMN 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 15220552   177 PENGVPIKAF----VDDLKDQELLNLVEFLESCYAYEDMRD 213
Cdd:TIGR02245 146 PKNGLKIRPFkkahANRGTDQELLKLTQYLKTIAELEDFSS 186
 
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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