NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039772632|ref|XP_017176602|]
View 

PAN2-PAN3 deadenylation complex subunit Pan3 isoform X6 [Mus musculus]

Protein Classification

PAN2-PAN3 deadenylation complex subunit PAN3( domain architecture ID 15848462)

PAN2-PAN3 deadenylation complex subunit PAN3 is a regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover; contains a catalytically inactive pseudokinase domain

CATH:  1.10.510.10
Gene Symbol:  PAN3
Gene Ontology:  GO:0005524|GO:0031251|GO:0046872|GO:0006397
PubMed:  24880344|16244704|17210253
SCOP:  4003661

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Pan3_PK pfam18101
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
 703-840 3.55e-91

Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal domain (C-term). The PAN3 PK domain has retained its ATP binding capacity, and this function is required for mRNA degradation in vivo. Analysis of Pan3 amino acids sequences show that, despite of retaining the general structural characteriztics of protein kinases, the PK domain has substitutions in all the conserved motifs that are critical for kinase activity, such as in the catalytic VAIK and HRD motifs and in the Mg2+ binding DFG motif. However, the PAN3 PK domain has been shown to bind ATP. Furthermore, similar to other kinases, the ATP-binding site is located in the cleft between the N- and C-lobes of the kinase fold, however, the ATP-binding pocket is wider than that of typical kinases.


:

Pssm-ID: 465649  Cd Length: 138  Bit Score: 283.22  E-value: 3.55e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 703 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 782
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 783 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 840
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 571-694 1.85e-05

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd13997:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 252  Bit Score: 46.99  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 571 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITSKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 642
Cdd:cd13997    98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 643 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 694
Cdd:cd13997   178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
51-74 1.29e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.79  E-value: 1.29e-03
                          10        20
                  ....*....|....*....|....
gi 1039772632  51 KLKYCRYYAKDKTCFYGEECQFLH 74
Cdd:pfam00642   2 KTELCRFFLRTGYCKYGDRCKFAH 25
 
Name Accession Description Interval E-value
Pan3_PK pfam18101
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
 703-840 3.55e-91

Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal domain (C-term). The PAN3 PK domain has retained its ATP binding capacity, and this function is required for mRNA degradation in vivo. Analysis of Pan3 amino acids sequences show that, despite of retaining the general structural characteriztics of protein kinases, the PK domain has substitutions in all the conserved motifs that are critical for kinase activity, such as in the catalytic VAIK and HRD motifs and in the Mg2+ binding DFG motif. However, the PAN3 PK domain has been shown to bind ATP. Furthermore, similar to other kinases, the ATP-binding site is located in the cleft between the N- and C-lobes of the kinase fold, however, the ATP-binding pocket is wider than that of typical kinases.


Pssm-ID: 465649  Cd Length: 138  Bit Score: 283.22  E-value: 3.55e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 703 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 782
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 783 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 840
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 571-694 1.85e-05

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 46.99  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 571 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITSKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 642
Cdd:cd13997    98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 643 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 694
Cdd:cd13997   178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
51-74 1.29e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.79  E-value: 1.29e-03
                          10        20
                  ....*....|....*....|....
gi 1039772632  51 KLKYCRYYAKDKTCFYGEECQFLH 74
Cdd:pfam00642   2 KTELCRFFLRTGYCKYGDRCKFAH 25
 
Name Accession Description Interval E-value
Pan3_PK pfam18101
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
 703-840 3.55e-91

Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A)-specific ribonuclease subunit pan3. PAN3 proteins contain three prominent regions: an unstructured N-terminal region (N-term), a central PK domain, and a highly conserved C-terminal domain (C-term). The PAN3 PK domain has retained its ATP binding capacity, and this function is required for mRNA degradation in vivo. Analysis of Pan3 amino acids sequences show that, despite of retaining the general structural characteriztics of protein kinases, the PK domain has substitutions in all the conserved motifs that are critical for kinase activity, such as in the catalytic VAIK and HRD motifs and in the Mg2+ binding DFG motif. However, the PAN3 PK domain has been shown to bind ATP. Furthermore, similar to other kinases, the ATP-binding site is located in the cleft between the N- and C-lobes of the kinase fold, however, the ATP-binding pocket is wider than that of typical kinases.


Pssm-ID: 465649  Cd Length: 138  Bit Score: 283.22  E-value: 3.55e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 703 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 782
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 783 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 840
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 571-694 1.85e-05

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 46.99  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772632 571 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITSKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 642
Cdd:cd13997    98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772632 643 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 694
Cdd:cd13997   178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
51-74 1.29e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.79  E-value: 1.29e-03
                          10        20
                  ....*....|....*....|....
gi 1039772632  51 KLKYCRYYAKDKTCFYGEECQFLH 74
Cdd:pfam00642   2 KTELCRFFLRTGYCKYGDRCKFAH 25
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 567-617 1.74e-03

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 41.10  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039772632 567 RQHAGLLPESLIWAYIVQLSSALRTIHTaglaCRVM----DPTKILITSKTRLRV 617
Cdd:cd08224    95 KKQKRLIPERTIWKYFVQLCSALEHMHS----KRIMhrdiKPANVFITANGVVKL 145
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 572-622 2.84e-03

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 40.40  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039772632 572 LLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITSKTRLRVNCVGV 622
Cdd:cd08228   102 LIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL 152
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH