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Conserved domains on  [gi|2980795|emb|CAA18171|]
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putative protein [Arabidopsis thaliana]

Protein Classification

cleavage and polyadenylation specificity factor subunit 5( domain architecture ID 19109046)

cleavage and polyadenylation specificity factor subunit 5 is a component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs.

CATH:  3.90.79.10
EC:  3.6.1.-
Gene Ontology:  GO:0046872|GO:0016818
SCOP:  3000098

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NUDIX_Cfim25_Nudt21 cd18871
25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also ...
10-198 1.17e-108

25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also called NUDIX (nucleoside diphosphate linked moiety X))-type motif 21) is a oligomer composed of a small 25 kDa subunit (CF I(m)25) and a variable larger subunit of either 59, 68 or 72 kDa and plays an important role in pre-mRNA 3'-end cleavage and the selection of poly(A) sites in a 3'-untranslated region (3'-UTR) of mRNA, producing mRNAs with variable 3' ends. The small subunit also interacts with RNA, poly(A) polymerase, and the nuclear poly(A)-binding protein and belongs to the NUDIX hydrolase superfamily. NUDIX hydrolases are found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes.


:

Pssm-ID: 467583  Cd Length: 184  Bit Score: 309.16  E-value: 1.17e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   10 YPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPGENgiq 89
Cdd:cd18871   2 YPLTNYTFGTKEAKVEKDSSVAARLQRLKEEYEKDGMRRTVEGVLLVHEHGHPHVLLLQLGNSFFKLPGGRLRPGED--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   90 lppfwvyyvvsaEADGLKRKLTSKLGGNSAALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKvvkkhnECKRLYIV 169
Cdd:cd18871  79 ------------EVEGLKRKLTEKLSPEDSEVLNDWEIGDCLGVWWRPNFETPMYPYLPAHITKPK------ECKKLYLV 140
                       170       180
                ....*....|....*....|....*....
gi 2980795  170 HLSEKEYFAVPKNLKLLAVPLFELYDNVQ 198
Cdd:cd18871 141 QLPEKCLFAVPKNYKLLAVPLFELYDNAA 169
 
Name Accession Description Interval E-value
NUDIX_Cfim25_Nudt21 cd18871
25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also ...
10-198 1.17e-108

25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also called NUDIX (nucleoside diphosphate linked moiety X))-type motif 21) is a oligomer composed of a small 25 kDa subunit (CF I(m)25) and a variable larger subunit of either 59, 68 or 72 kDa and plays an important role in pre-mRNA 3'-end cleavage and the selection of poly(A) sites in a 3'-untranslated region (3'-UTR) of mRNA, producing mRNAs with variable 3' ends. The small subunit also interacts with RNA, poly(A) polymerase, and the nuclear poly(A)-binding protein and belongs to the NUDIX hydrolase superfamily. NUDIX hydrolases are found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes.


Pssm-ID: 467583  Cd Length: 184  Bit Score: 309.16  E-value: 1.17e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   10 YPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPGENgiq 89
Cdd:cd18871   2 YPLTNYTFGTKEAKVEKDSSVAARLQRLKEEYEKDGMRRTVEGVLLVHEHGHPHVLLLQLGNSFFKLPGGRLRPGED--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   90 lppfwvyyvvsaEADGLKRKLTSKLGGNSAALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKvvkkhnECKRLYIV 169
Cdd:cd18871  79 ------------EVEGLKRKLTEKLSPEDSEVLNDWEIGDCLGVWWRPNFETPMYPYLPAHITKPK------ECKKLYLV 140
                       170       180
                ....*....|....*....|....*....
gi 2980795  170 HLSEKEYFAVPKNLKLLAVPLFELYDNVQ 198
Cdd:cd18871 141 QLPEKCLFAVPKNYKLLAVPLFELYDNAA 169
NUDIX_2 pfam13869
Nucleotide hydrolase; Nudix hydrolases are found in all classes of organizm and hydrolyse a ...
5-198 2.04e-102

Nucleotide hydrolase; Nudix hydrolases are found in all classes of organizm and hydrolyse a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, di-nucleoside and diphospho-inositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity.


Pssm-ID: 433540  Cd Length: 188  Bit Score: 293.42  E-value: 2.04e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795      5 QVVNTYPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPG 84
Cdd:pfam13869   1 PTWLLYPLSNYTFGTKEALVEKDISVAERLKRLKDNYEKNGMRRTVEGVILVHRHGHPHVLLLQIGNSFFKLPGGRLKPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795     85 ENgiqlppfwvyyvvsaEADGLKRKLTSKLGGNSaALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKvvkkhnECK 164
Cdd:pfam13869  81 EN---------------EIEGLKRKLAKKLSPEK-GVVETWEVGECLGEWWRPNFETSMYPYLPAHITRPK------ECI 138
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2980795    165 RLYIVHLSEKEYFAVPKNLKLLAVPLFELYDNVQ 198
Cdd:pfam13869 139 KLYLVTLPEKCKFAVPKNMKLLAVPLFELYDNAA 172
 
Name Accession Description Interval E-value
NUDIX_Cfim25_Nudt21 cd18871
25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also ...
10-198 1.17e-108

25 kDa subunit of cleavage factor Im; Precursor mRNA (pre-mRNA) cleavage factor I(m) (also called NUDIX (nucleoside diphosphate linked moiety X))-type motif 21) is a oligomer composed of a small 25 kDa subunit (CF I(m)25) and a variable larger subunit of either 59, 68 or 72 kDa and plays an important role in pre-mRNA 3'-end cleavage and the selection of poly(A) sites in a 3'-untranslated region (3'-UTR) of mRNA, producing mRNAs with variable 3' ends. The small subunit also interacts with RNA, poly(A) polymerase, and the nuclear poly(A)-binding protein and belongs to the NUDIX hydrolase superfamily. NUDIX hydrolases are found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes.


Pssm-ID: 467583  Cd Length: 184  Bit Score: 309.16  E-value: 1.17e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   10 YPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPGENgiq 89
Cdd:cd18871   2 YPLTNYTFGTKEAKVEKDSSVAARLQRLKEEYEKDGMRRTVEGVLLVHEHGHPHVLLLQLGNSFFKLPGGRLRPGED--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795   90 lppfwvyyvvsaEADGLKRKLTSKLGGNSAALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKvvkkhnECKRLYIV 169
Cdd:cd18871  79 ------------EVEGLKRKLTEKLSPEDSEVLNDWEIGDCLGVWWRPNFETPMYPYLPAHITKPK------ECKKLYLV 140
                       170       180
                ....*....|....*....|....*....
gi 2980795  170 HLSEKEYFAVPKNLKLLAVPLFELYDNVQ 198
Cdd:cd18871 141 QLPEKCLFAVPKNYKLLAVPLFELYDNAA 169
NUDIX_2 pfam13869
Nucleotide hydrolase; Nudix hydrolases are found in all classes of organizm and hydrolyse a ...
5-198 2.04e-102

Nucleotide hydrolase; Nudix hydrolases are found in all classes of organizm and hydrolyse a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, di-nucleoside and diphospho-inositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity.


Pssm-ID: 433540  Cd Length: 188  Bit Score: 293.42  E-value: 2.04e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795      5 QVVNTYPLSNYSFGTKEPKLEKDTSVADRLARMKINYMKEGMRTSVEGILLVQEHNHPHILLLQIGNTFCKLPGGRLKPG 84
Cdd:pfam13869   1 PTWLLYPLSNYTFGTKEALVEKDISVAERLKRLKDNYEKNGMRRTVEGVILVHRHGHPHVLLLQIGNSFFKLPGGRLKPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2980795     85 ENgiqlppfwvyyvvsaEADGLKRKLTSKLGGNSaALVPDWTVGECVATWWRPNFETMMYPYCPPHITKPKvvkkhnECK 164
Cdd:pfam13869  81 EN---------------EIEGLKRKLAKKLSPEK-GVVETWEVGECLGEWWRPNFETSMYPYLPAHITRPK------ECI 138
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2980795    165 RLYIVHLSEKEYFAVPKNLKLLAVPLFELYDNVQ 198
Cdd:pfam13869 139 KLYLVTLPEKCKFAVPKNMKLLAVPLFELYDNAA 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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