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Conserved domains on  [gi|1720395843|ref|XP_030106943|]
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CWF19-like protein 1 isoform X1 [Mus musculus]

Protein Classification

CWF19 family protein( domain architecture ID 10164532)

CWF19 family protein such as human CWF19-like protein 1

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; ...
 9-91 5.73e-35

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: 126.26  E-value: 5.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843   9 KGVDILLTSPWPKYVGSFGNSSGEVDTKNCGSALISSLAVSLKPRYHFAALEKSYYERLPYRNHVVLqESAQHATRFIAL 88
Cdd:cd07380    68 GGVDILLTSEWPKGISKLSKSPFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGL 146


                  ...
gi 1720395843  89 ANV 91
Cdd:cd07380   147 APV 149
HIT_like super family cl00228
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 189-284 7.11e-35

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: 124.80  E-value: 7.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 189 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLQRFFKSRGKRCVLFE 268
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90
                  ....*....|....*..
gi 1720395843 269 R-NYRSHHLQLQVIPVP 284
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVP 110
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 304-396 3.03e-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: 84.56  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 304 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPEKADWRQCQTSKDEEEA 381
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQ 81

                          90
                  ....*....|....*
gi 1720395843 382 LARRFRKDFEPFDFT 396
Cdd:pfam04676  82 RVEAFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-91 5.73e-35

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: 126.26  E-value: 5.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843   9 KGVDILLTSPWPKYVGSFGNSSGEVDTKNCGSALISSLAVSLKPRYHFAALEKSYYERLPYRNHVVLqESAQHATRFIAL 88
Cdd:cd07380    68 GGVDILLTSEWPKGISKLSKSPFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGL 146


                  ...
gi 1720395843  89 ANV 91
Cdd:cd07380   147 APV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 189-284 7.11e-35

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: 124.80  E-value: 7.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 189 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLQRFFKSRGKRCVLFE 268
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90
                  ....*....|....*..
gi 1720395843 269 R-NYRSHHLQLQVIPVP 284
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVP 110
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 304-396 3.03e-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: 84.56  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 304 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPEKADWRQCQTSKDEEEA 381
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQ 81

                          90
                  ....*....|....*
gi 1720395843 382 LARRFRKDFEPFDFT 396
Cdd:pfam04676  82 RVEAFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 9-91 5.73e-35

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: 126.26  E-value: 5.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843   9 KGVDILLTSPWPKYVGSFGNSSGEVDTKNCGSALISSLAVSLKPRYHFAALEKSYYERLPYRNHVVLqESAQHATRFIAL 88
Cdd:cd07380    68 GGVDILLTSEWPKGISKLSKSPFEPDLLISGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGL 146


                  ...
gi 1720395843  89 ANV 91
Cdd:cd07380   147 APV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 189-284 7.11e-35

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: 124.80  E-value: 7.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 189 CWFCLASPEVEKHLVVNIGTHCYLALAKGGLSDDHVLILPIGHYQSVVELSAEVVEEVEKYKATLQRFFKSRGKRCVLFE 268
Cdd:pfam04677  14 CWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKSQGKDAVFFE 93

                          90
                  ....*....|....*..
gi 1720395843 269 R-NYRSHHLQLQVIPVP 284
Cdd:pfam04677  94 IaSQRRPHLHIQCIPVP 110
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 304-396 3.03e-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: 84.56  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395843 304 QQIELLEIPEHSDIKQIAQPGAAYFYVELDTGEKLFHRI--KKNFPLQFGREVLASeaILNIPEKADWRQCQTSKDEEEA 381
Cdd:pfam04676   4 QHKKLIDTSNKKGFRRSIPKGFPYFHVEFGLDGGYAHVIedEERFPLQFGREVIAG--MLDLPPRVWRKPCRQSKEEEEQ 81

                          90
                  ....*....|....*
gi 1720395843 382 LARRFRKDFEPFDFT 396
Cdd:pfam04676  82 RVEAFKKAWKKYDWT 96
 
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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