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Conserved domains on  [gi|45550410|ref|NP_610670|]
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uncharacterized protein Dmel_CG7741, isoform A [Drosophila melanogaster]

Protein Classification

CWF19 family protein( domain architecture ID 10164527)

CWF19 family protein contains an N-terminal metallophosphatase domain and may be a cell cycle control protein; similar to Drosophila melanogaster CWF19-like protein 1 homolog

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

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; ...
 29-249 2.75e-52

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: 174.80  E-value: 2.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410  29 LVVGDVRGRFKQLFQRVEQVNKKAGPFEILCCVGDFFGEDKQNEELIAYKNGFKHITVPTYILGPNQrehekyfenltdg 108
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEELEAYKDGSKKVPIPTYFLGGNN------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410 109 eictnltylgrrgvytlssgvkiaylsgleaqgtadsagseheftkadviavrnsclvskncsteyRGVDVLLTSQWPFG 188
Cdd:cd07380  68 ------------------------------------------------------------------GGVDILLTSEWPKG 81

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550410 189 MQEKENA--------TASKLVSFLCREIKPRYHFCAINGTHYESAPFRMPKDEtTQFELCTRFISLAEV 249
Cdd:cd07380  82 ISKLSKSpfepdlliSGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
HIT_like super family cl00228
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 320-428 6.42e-30

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: 113.63  E-value: 6.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   320 GDNNKRDKRPripqieQDKCWFCLSSPDVEKHLIITVGEHFYLALAKGPINKHHVMILSTKHVPCAAQLSPDDWKELNKF 399
Cdd:pfam04677   1 GKDHKRIKIL------PDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNF 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550410   400 KAALRKFFKTLGQVVCFTERH-YKSVHLQI 428
Cdd:pfam04677  75 RKALTLMYKSQGKDAVFFEIAsQRRPHLHI 104
CwfJ_C_2 super family cl04666
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 466-543 7.97e-11

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: 58.76  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   466 KMLPEMGPYFLAELPDDSTL--ITRQMKHFPIHFARDVFCseNLLNCDEKVNWKDCLLDKDEEVAYVEDFRKAFAPFDFT 543
Cdd:pfam04676  19 RSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIA--GMLDLPPRVWRKPCRQSKEEEEQRVEAFKKAWKKYDWT 96
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 29-249 2.75e-52

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: 174.80  E-value: 2.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410  29 LVVGDVRGRFKQLFQRVEQVNKKAGPFEILCCVGDFFGEDKQNEELIAYKNGFKHITVPTYILGPNQrehekyfenltdg 108
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEELEAYKDGSKKVPIPTYFLGGNN------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410 109 eictnltylgrrgvytlssgvkiaylsgleaqgtadsagseheftkadviavrnsclvskncsteyRGVDVLLTSQWPFG 188
Cdd:cd07380  68 ------------------------------------------------------------------GGVDILLTSEWPKG 81

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550410 189 MQEKENA--------TASKLVSFLCREIKPRYHFCAINGTHYESAPFRMPKDEtTQFELCTRFISLAEV 249
Cdd:cd07380  82 ISKLSKSpfepdlliSGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 320-428 6.42e-30

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: 113.63  E-value: 6.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   320 GDNNKRDKRPripqieQDKCWFCLSSPDVEKHLIITVGEHFYLALAKGPINKHHVMILSTKHVPCAAQLSPDDWKELNKF 399
Cdd:pfam04677   1 GKDHKRIKIL------PDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNF 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550410   400 KAALRKFFKTLGQVVCFTERH-YKSVHLQI 428
Cdd:pfam04677  75 RKALTLMYKSQGKDAVFFEIAsQRRPHLHI 104
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 466-543 7.97e-11

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: 58.76  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   466 KMLPEMGPYFLAELPDDSTL--ITRQMKHFPIHFARDVFCseNLLNCDEKVNWKDCLLDKDEEVAYVEDFRKAFAPFDFT 543
Cdd:pfam04676  19 RSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIA--GMLDLPPRVWRKPCRQSKEEEEQRVEAFKKAWKKYDWT 96
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
27-215 2.53e-08

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 54.25  E-value: 2.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410  27 KILVVGDVRGRFKQLFQRVEQVnkKAGPFEILCCVGDF--FGEDKQNEELIAYkngFKHITVPTY-ILGpNqreHEkyFE 103
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELA--RAEDADLVILAGDLtdFGTAEEAREVLEE---LAALGVPVLaVPG-N---HD--DP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410 104 NLTDGEICTNLTYLGRRgVYTLsSGVKIAYLSGleaqGTADSAGSEHEFTKADVIAVRNSCLVskncsteyRGVDVLLTS 183
Cdd:COG2129  70 EVLDALEESGVHNLHGR-VVEI-GGLRIAGLGG----SRPTPFGTPYEYTEEEIEERLAKLRE--------KDVDILLTH 135

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45550410 184 QWPFG-MQEKENATA---SKLVSFLCREIKPRYHFC 215
Cdd:COG2129 136 APPYGtTLDRVEDGPhvgSKALRELIEEFQPKLVLH 171
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 337-408 1.22e-03

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 39.16  E-value: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550410 337 DKCWFCLSSPDVEKHLIITVGEHFYLALAKGPINKHHVMILSTKHVPCAAQLSPDDWKEL----NKFKAALRKFFK 408
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELmrlaQKVAKALRKALG 76
 
Name Accession Description Interval E-value
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 29-249 2.75e-52

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: 174.80  E-value: 2.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410  29 LVVGDVRGRFKQLFQRVEQVNKKAGPFEILCCVGDFFGEDKQNEELIAYKNGFKHITVPTYILGPNQrehekyfenltdg 108
Cdd:cd07380   1 LVCGDVNGRLKALFEKVNTINKKNGPFDALLCVGDFFGDDESDEELEAYKDGSKKVPIPTYFLGGNN------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410 109 eictnltylgrrgvytlssgvkiaylsgleaqgtadsagseheftkadviavrnsclvskncsteyRGVDVLLTSQWPFG 188
Cdd:cd07380  68 ------------------------------------------------------------------GGVDILLTSEWPKG 81

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550410 189 MQEKENA--------TASKLVSFLCREIKPRYHFCAINGTHYESAPFRMPKDEtTQFELCTRFISLAEV 249
Cdd:cd07380  82 ISKLSKSpfepdlliSGSDLIAELAKKLKPRYHFAGLEGVFYEREPYRNDSVL-EKAEHVTRFIGLAPV 149
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 320-428 6.42e-30

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: 113.63  E-value: 6.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   320 GDNNKRDKRPripqieQDKCWFCLSSPDVEKHLIITVGEHFYLALAKGPINKHHVMILSTKHVPCAAQLSPDDWKELNKF 399
Cdd:pfam04677   1 GKDHKRIKIL------PDSCWFCLSNPNLEKHLIVSIGNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNF 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 45550410   400 KAALRKFFKTLGQVVCFTERH-YKSVHLQI 428
Cdd:pfam04677  75 RKALTLMYKSQGKDAVFFEIAsQRRPHLHI 104
CwfJ_C_2 pfam04676
Protein similar to CwfJ C-terminus 2; This region is found in the N terminus of ...
 466-543 7.97e-11

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: 58.76  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410   466 KMLPEMGPYFLAELPDDSTL--ITRQMKHFPIHFARDVFCseNLLNCDEKVNWKDCLLDKDEEVAYVEDFRKAFAPFDFT 543
Cdd:pfam04676  19 RSIPKGFPYFHVEFGLDGGYahVIEDEERFPLQFGREVIA--GMLDLPPRVWRKPCRQSKEEEEQRVEAFKKAWKKYDWT 96
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
27-215 2.53e-08

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 54.25  E-value: 2.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410  27 KILVVGDVRGRFKQLFQRVEQVnkKAGPFEILCCVGDF--FGEDKQNEELIAYkngFKHITVPTY-ILGpNqreHEkyFE 103
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELA--RAEDADLVILAGDLtdFGTAEEAREVLEE---LAALGVPVLaVPG-N---HD--DP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550410 104 NLTDGEICTNLTYLGRRgVYTLsSGVKIAYLSGleaqGTADSAGSEHEFTKADVIAVRNSCLVskncsteyRGVDVLLTS 183
Cdd:COG2129  70 EVLDALEESGVHNLHGR-VVEI-GGLRIAGLGG----SRPTPFGTPYEYTEEEIEERLAKLRE--------KDVDILLTH 135

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45550410 184 QWPFG-MQEKENATA---SKLVSFLCREIKPRYHFC 215
Cdd:COG2129 136 APPYGtTLDRVEDGPhvgSKALRELIEEFQPKLVLH 171
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 337-408 1.22e-03

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 39.16  E-value: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550410 337 DKCWFCLSSPDVEKHLIITVGEHFYLALAKGPINKHHVMILSTKHVPCAAQLSPDDWKEL----NKFKAALRKFFK 408
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELmrlaQKVAKALRKALG 76
 
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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