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Conserved domains on  [gi|767977552|ref|XP_011533334|]
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PAN2-PAN3 deadenylation complex subunit PAN3 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pan3_PK super family cl39491
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
742-795 4.32e-25

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.


The actual alignment was detected with superfamily member pfam18101:

Pssm-ID: 465649  Cd Length: 138  Bit Score: 101.41  E-value: 4.32e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767977552  742 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPD 795
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPE 54
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
493-661 1.32e-08

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 cd08228:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 268  Bit Score: 56.96  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 493 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 568
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 569 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 648
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139
                        170
                 ....*....|...
gi 767977552 649 TGKTRLRVNCVGV 661
Cdd:cd08228  140 TATGVVKLGDLGL 152
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
610-733 5.68e-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: 45.45  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 610 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 681
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767977552 682 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 733
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.20e-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: 1.20e-03
                          10        20
                  ....*....|....*....|....
gi 767977552   45 KLKYCRYYAKDKTCFYGEECQFLH 68
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) ...
742-795 4.32e-25

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: 101.41  E-value: 4.32e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767977552  742 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPD 795
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPE 54
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
493-661 1.32e-08

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: 56.96  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 493 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 568
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 569 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 648
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139
                        170
                 ....*....|...
gi 767977552 649 TGKTRLRVNCVGV 661
Cdd:cd08228  140 TATGVVKLGDLGL 152
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
610-733 5.68e-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: 45.45  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 610 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 681
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767977552 682 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 733
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.20e-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: 1.20e-03
                          10        20
                  ....*....|....*....|....
gi 767977552   45 KLKYCRYYAKDKTCFYGEECQFLH 68
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) ...
742-795 4.32e-25

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: 101.41  E-value: 4.32e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767977552  742 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPD 795
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPE 54
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
493-661 1.32e-08

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: 56.96  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 493 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 568
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 569 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 648
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139
                        170
                 ....*....|...
gi 767977552 649 TGKTRLRVNCVGV 661
Cdd:cd08228  140 TATGVVKLGDLGL 152
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
493-661 1.79e-08

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. 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: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 56.58  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 493 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 568
Cdd:cd08229   27 RIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKaradCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 569 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 648
Cdd:cd08229  107 ---DAGDLSRMIKHF----------------------KKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFI 161
                        170
                 ....*....|...
gi 767977552 649 TGKTRLRVNCVGV 661
Cdd:cd08229  162 TATGVVKLGDLGL 174
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
507-656 1.47e-07

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: 53.43  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 507 YKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFttkaFAEPSLVFAYDFHAGGE-TMMSR 581
Cdd:cd08224   17 YRARCLLDGRLVALKKVQIFEMMDAKarqdCLKEIDLLQQLNHPNIIKYLASF----IENNELNIVLELADAGDlSRLIK 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767977552 582 HFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTaglaCRVM----DPTKILITGKTRLRV 656
Cdd:cd08224   93 HF----------------------KKQKRLIPERTIWKYFVQLCSALEHMHS----KRIMhrdiKPANVFITANGVVKL 145
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
610-733 5.68e-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: 45.45  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977552 610 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 681
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767977552 682 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 733
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.20e-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: 1.20e-03
                          10        20
                  ....*....|....*....|....
gi 767977552   45 KLKYCRYYAKDKTCFYGEECQFLH 68
Cdd:pfam00642   2 KTELCRFFLRTGYCKYGDRCKFAH 25
 
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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