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Conserved domains on  [gi|17559798|ref|NP_504577|]
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CWF19-like protein 1 homolog [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-222 6.63e-58

Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; CWF19 cell cycle control protein (also known as CWF19-like 1 (CWF19L1) in Homo sapiens), N-terminal metallophosphatase domain. CWF19 contains C-terminal domains similar to that found in the CwfJ cell cycle control protein. The metallophosphatase domain 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: 277326  Cd Length: 149  Bit Score: 189.43  E-value: 6.63e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   9 LCCGDVNGNFVELIKKISTTEKKNGPFDSLFCVGEFFGDDDDSNE--KVINGNIEFPIPTYILGPANPrysylypeesie 86
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEEleAYKDGSKKVPIPTYFLGGNNG------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798  87 fssnltylgkkgllntasglqiaylsgvegsskdlscfdkadveelliplgtqvgfsGTDILLTSVWPADIARHSHN--Q 164
Cdd:cd07380  69 ---------------------------------------------------------GVDILLTSEWPKGISKLSKSpfE 91

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559798 165 PSKPQPGSVLLSKLAAHLKPRYHFAGL-GVHYERQPYRNHRVlLEPARHTTRFIGLAAI 222
Cdd:cd07380  92 PDLLISGSDLIAELAKKLKPRYHFAGLeGVFYEREPYRNDSV-LEKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 309-417 1.11e-51

Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


:

Pssm-ID: 428062  Cd Length: 122  Bit Score: 172.18  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   309 GNDGPRNKQPVGPCWFCLSNVDAEKHLVVAIGNKCYAAMPKGPLTEDHVMVLSVGHIQSQVSAPVEVRDEIEKFKSAFTL 388
Cdd:pfam04677   1 GKDHKRIKILPDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 17559798   389 MANKQGKALVTFER-NFRTQHLQVQMVMID 417
Cdd:pfam04677  81 MYKSQGKDAVFFEIaSQRRPHLHIQCIPVP 110
CwfJ_C_2 super family cl04666
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 438-527 4.52e-12

Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


The actual alignment was detected with superfamily member pfam04676:

Pssm-ID: 461388  Cd Length: 96  Bit Score: 62.22  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   438 ELVTMGPDESLLDMVNEGCPYFVAELPDGSKL--FTRSMKGFPLHFGREVLAStpILDCEDKVDWKACVLAKEKEVELVN 515
Cdd:pfam04676   7 KLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQRVE 84

                          90
                  ....*....|..
gi 17559798   516 KLKSDFKPFDFT 527
Cdd:pfam04676  85 AFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-222 6.63e-58

Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; CWF19 cell cycle control protein (also known as CWF19-like 1 (CWF19L1) in Homo sapiens), N-terminal metallophosphatase domain. CWF19 contains C-terminal domains similar to that found in the CwfJ cell cycle control protein. The metallophosphatase domain 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: 277326  Cd Length: 149  Bit Score: 189.43  E-value: 6.63e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   9 LCCGDVNGNFVELIKKISTTEKKNGPFDSLFCVGEFFGDDDDSNE--KVINGNIEFPIPTYILGPANPrysylypeesie 86
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEEleAYKDGSKKVPIPTYFLGGNNG------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798  87 fssnltylgkkgllntasglqiaylsgvegsskdlscfdkadveelliplgtqvgfsGTDILLTSVWPADIARHSHN--Q 164
Cdd:cd07380  69 ---------------------------------------------------------GVDILLTSEWPKGISKLSKSpfE 91

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559798 165 PSKPQPGSVLLSKLAAHLKPRYHFAGL-GVHYERQPYRNHRVlLEPARHTTRFIGLAAI 222
Cdd:cd07380  92 PDLLISGSDLIAELAKKLKPRYHFAGLeGVFYEREPYRNDSV-LEKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 309-417 1.11e-51

Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 428062  Cd Length: 122  Bit Score: 172.18  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   309 GNDGPRNKQPVGPCWFCLSNVDAEKHLVVAIGNKCYAAMPKGPLTEDHVMVLSVGHIQSQVSAPVEVRDEIEKFKSAFTL 388
Cdd:pfam04677   1 GKDHKRIKILPDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 17559798   389 MANKQGKALVTFER-NFRTQHLQVQMVMID 417
Cdd:pfam04677  81 MYKSQGKDAVFFEIaSQRRPHLHIQCIPVP 110
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 438-527 4.52e-12

Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 461388  Cd Length: 96  Bit Score: 62.22  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   438 ELVTMGPDESLLDMVNEGCPYFVAELPDGSKL--FTRSMKGFPLHFGREVLAStpILDCEDKVDWKACVLAKEKEVELVN 515
Cdd:pfam04676   7 KLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQRVE 84

                          90
                  ....*....|..
gi 17559798   516 KLKSDFKPFDFT 527
Cdd:pfam04676  85 AFKKAWKKYDWT 96
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
7-190 1.99e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 42.69  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   7 KILCCGDVNGNFvELIKKIsTTEKKNGPFDSLFCVG--EFFGDDDDSnEKVINGNIEFPIPTY-ILGPANPRYSylypEE 83
Cdd:COG2129   1 KILAVSDLHGNF-DLLEKL-LELARAEDADLVILAGdlTDFGTAEEA-REVLEELAALGVPVLaVPGNHDDPEV----LD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798  84 SIEfSSNLTYLGKKGLlnTASGLQIAYLSGVEGSS-KDLSCFDKADVEELLIPLGTQvgfsGTDILLTSVWPADIarHSH 162
Cdd:COG2129  74 ALE-ESGVHNLHGRVV--EIGGLRIAGLGGSRPTPfGTPYEYTEEEIEERLAKLREK----DVDILLTHAPPYGT--TLD 144

                       170       180
                ....*....|....*....|....*...
gi 17559798 163 NQPSKPQPGSVLLSKLAAHLKPRYHFAG 190
Cdd:COG2129 145 RVEDGPHVGSKALRELIEEFQPKLVLHG 172
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-222 6.63e-58

Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; CWF19 cell cycle control protein (also known as CWF19-like 1 (CWF19L1) in Homo sapiens), N-terminal metallophosphatase domain. CWF19 contains C-terminal domains similar to that found in the CwfJ cell cycle control protein. The metallophosphatase domain 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: 277326  Cd Length: 149  Bit Score: 189.43  E-value: 6.63e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   9 LCCGDVNGNFVELIKKISTTEKKNGPFDSLFCVGEFFGDDDDSNE--KVINGNIEFPIPTYILGPANPrysylypeesie 86
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEEleAYKDGSKKVPIPTYFLGGNNG------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798  87 fssnltylgkkgllntasglqiaylsgvegsskdlscfdkadveelliplgtqvgfsGTDILLTSVWPADIARHSHN--Q 164
Cdd:cd07380  69 ---------------------------------------------------------GVDILLTSEWPKGISKLSKSpfE 91

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17559798 165 PSKPQPGSVLLSKLAAHLKPRYHFAGL-GVHYERQPYRNHRVlLEPARHTTRFIGLAAI 222
Cdd:cd07380  92 PDLLISGSDLIAELAKKLKPRYHFAGLeGVFYEREPYRNDSV-LEKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 309-417 1.11e-51

Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 428062  Cd Length: 122  Bit Score: 172.18  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   309 GNDGPRNKQPVGPCWFCLSNVDAEKHLVVAIGNKCYAAMPKGPLTEDHVMVLSVGHIQSQVSAPVEVRDEIEKFKSAFTL 388
Cdd:pfam04677   1 GKDHKRIKILPDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 17559798   389 MANKQGKALVTFER-NFRTQHLQVQMVMID 417
Cdd:pfam04677  81 MYKSQGKDAVFFEIaSQRRPHLHIQCIPVP 110
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 438-527 4.52e-12

Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 461388  Cd Length: 96  Bit Score: 62.22  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   438 ELVTMGPDESLLDMVNEGCPYFVAELPDGSKL--FTRSMKGFPLHFGREVLAStpILDCEDKVDWKACVLAKEKEVELVN 515
Cdd:pfam04676   7 KLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQRVE 84

                          90
                  ....*....|..
gi 17559798   516 KLKSDFKPFDFT 527
Cdd:pfam04676  85 AFKKAWKKYDWT 96
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
7-190 1.99e-04

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 42.69  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798   7 KILCCGDVNGNFvELIKKIsTTEKKNGPFDSLFCVG--EFFGDDDDSnEKVINGNIEFPIPTY-ILGPANPRYSylypEE 83
Cdd:COG2129   1 KILAVSDLHGNF-DLLEKL-LELARAEDADLVILAGdlTDFGTAEEA-REVLEELAALGVPVLaVPGNHDDPEV----LD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559798  84 SIEfSSNLTYLGKKGLlnTASGLQIAYLSGVEGSS-KDLSCFDKADVEELLIPLGTQvgfsGTDILLTSVWPADIarHSH 162
Cdd:COG2129  74 ALE-ESGVHNLHGRVV--EIGGLRIAGLGGSRPTPfGTPYEYTEEEIEERLAKLREK----DVDILLTHAPPYGT--TLD 144

                       170       180
                ....*....|....*....|....*...
gi 17559798 163 NQPSKPQPGSVLLSKLAAHLKPRYHFAG 190
Cdd:COG2129 145 RVEDGPHVGSKALRELIEEFQPKLVLHG 172
 
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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