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Conserved domains on  [gi|300797289|ref|NP_001179014|]
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CWF19-like protein 1 [Bos taurus]

Protein Classification

CWF19 family protein( domain architecture ID 10164532)

CWF19 family protein contains an N-terminal metallophosphatase domain and may be a cell cycle control protein; such as human CWF19-like protein 1

CATH:  3.60.21.10
Gene Ontology:  GO:0046872
PubMed:  8003970|25837850

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; ...
 9-229 8.78e-63

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: 202.15  E-value: 8.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289   9 LACGDVEGKFDALFNRVRAIQKKSGNFDLLLCVGNFFG-STPDAEWEEYKTGVKKAPIQTYVLGANNQetvkyfqdvdgc 87
Cdd:cd07380    1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGdDESDEELEAYKDGSKKVPIPTYFLGGNNG------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  88 elaenitylgrkgvftgssglqivylsgteslnepvpgysfspkdvsslrtmlcstpqfkGVDILLTSPWPKYVGNFGNS 167
Cdd:cd07380   69 ------------------------------------------------------------GVDILLTSEWPKGISKLSKS 88

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797289 168 SGEVDTKKCGSALISSLATGLKPRYHFASLEKTYYERLPYRNHIVLqENAQHATRFIALANV 229
Cdd:cd07380   89 PFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
HIT_like super family cl00228
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 328-426 2.37e-34

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


The actual alignment was detected with superfamily member pfam04677:

Pssm-ID: 469672  Cd Length: 122  Bit Score: 125.95  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  328 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLRRFFRSRGKRCVLFE 407
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90       100
                  ....*....|....*....|
gi 300797289  408 R-NYKSHHLQLQVIPVPLSS 426
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVPKSI 113
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 443-535 3.94e-20

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: 85.33  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  443 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPdKSDWRK-CQMSKEEEE 519
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLP-PRVWRKpCRQSKEEEE 80

                          90
                  ....*....|....*.
gi 300797289  520 TLARRFRKDFEPFDFT 535
Cdd:pfam04676  81 QRVEAFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-229 8.78e-63

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: 202.15  E-value: 8.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289   9 LACGDVEGKFDALFNRVRAIQKKSGNFDLLLCVGNFFG-STPDAEWEEYKTGVKKAPIQTYVLGANNQetvkyfqdvdgc 87
Cdd:cd07380    1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGdDESDEELEAYKDGSKKVPIPTYFLGGNNG------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  88 elaenitylgrkgvftgssglqivylsgteslnepvpgysfspkdvsslrtmlcstpqfkGVDILLTSPWPKYVGNFGNS 167
Cdd:cd07380   69 ------------------------------------------------------------GVDILLTSEWPKGISKLSKS 88

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797289 168 SGEVDTKKCGSALISSLATGLKPRYHFASLEKTYYERLPYRNHIVLqENAQHATRFIALANV 229
Cdd:cd07380   89 PFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 328-426 2.37e-34

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: 125.95  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  328 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLRRFFRSRGKRCVLFE 407
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90       100
                  ....*....|....*....|
gi 300797289  408 R-NYKSHHLQLQVIPVPLSS 426
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVPKSI 113
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 443-535 3.94e-20

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: 85.33  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  443 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPdKSDWRK-CQMSKEEEE 519
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLP-PRVWRKpCRQSKEEEE 80

                          90
                  ....*....|....*.
gi 300797289  520 TLARRFRKDFEPFDFT 535
Cdd:pfam04676  81 QRVEAFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-229 8.78e-63

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: 202.15  E-value: 8.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289   9 LACGDVEGKFDALFNRVRAIQKKSGNFDLLLCVGNFFG-STPDAEWEEYKTGVKKAPIQTYVLGANNQetvkyfqdvdgc 87
Cdd:cd07380    1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGdDESDEELEAYKDGSKKVPIPTYFLGGNNG------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  88 elaenitylgrkgvftgssglqivylsgteslnepvpgysfspkdvsslrtmlcstpqfkGVDILLTSPWPKYVGNFGNS 167
Cdd:cd07380   69 ------------------------------------------------------------GVDILLTSEWPKGISKLSKS 88

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797289 168 SGEVDTKKCGSALISSLATGLKPRYHFASLEKTYYERLPYRNHIVLqENAQHATRFIALANV 229
Cdd:cd07380   89 PFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 328-426 2.37e-34

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: 125.95  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  328 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLRRFFRSRGKRCVLFE 407
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90       100
                  ....*....|....*....|
gi 300797289  408 R-NYKSHHLQLQVIPVPLSS 426
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVPKSI 113
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 443-535 3.94e-20

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: 85.33  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  443 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPdKSDWRK-CQMSKEEEE 519
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLP-PRVWRKpCRQSKEEEE 80

                          90
                  ....*....|....*.
gi 300797289  520 TLARRFRKDFEPFDFT 535
Cdd:pfam04676  81 QRVEAFKKAWKKYDWT 96
MPP_Dbr1_N cd00844
Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA ...
 16-196 1.48e-13

Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This 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: 277322 [Multi-domain]  Cd Length: 271  Bit Score: 71.13  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  16 GKFDALFNRVRAIQKKSG-NFDLLLCVGNFFG----------STPD-----AEWEEYKTGVKKAPIQTYVLGANNqETVK 79
Cdd:cd00844    9 GELDKIYETLEKYEKKNGtKVDLLICCGDFQAvrneadlkcmAVPPkykkmGDFHKYYSGEKKAPILTIFIGGNH-EASN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797289  80 YFQDV-DGCELAENITYLGRKGVFTgSSGLQIVYLSGTES----LNEPVPGYSFSPKDVSS---------LRTMLCSTPq 145
Cdd:cd00844   88 YLWELpYGGWVAPNIYYLGYAGVVN-FGGLRIGGISGIYKshdyKKGHFERPPYNPSTIRSayhvrnidvFKLKQLKHP- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300797289 146 fkgVDILLTSPWPKYVGNFGNSSG----------EVDTKKCGSALISSLATGLKPRYHFAS 196
Cdd:cd00844  166 ---IDIFLSHDWPRGIEKHGDKKQllrrkpffrqDIESGTLGSPAAEELLEHLKPRYWFSA 223
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 9-73 7.51e-06

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: 45.72  E-value: 7.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300797289   9 LACGDVEGKFDALFNRVRAIQKKSGNFDLLLCVGNFFGSTPDAEWEEYK-TGVKKAPIQTYVLGAN 73
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKaLRLLLAGIPVYVVPGN 66
 
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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