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Conserved domains on  [gi|530402250|ref|XP_005266390|]
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PAN2-PAN3 deadenylation complex subunit PAN3 isoform X2 [Homo sapiens]

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

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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) ...
 688-825 2.49e-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: 2.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  688 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 767
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250  768 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 825
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 439-607 1.40e-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: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 439 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 514
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 515 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 594
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139

                        170
                 ....*....|...
gi 530402250 595 TGKTRLRVNCVGV 607
Cdd:cd08228  140 TATGVVKLGDLGL 152
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 202-385 4.70e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  202 PYSAHDP--LTSPASSlfndfGALNISQRRKTPNPtasefipkGGSTSRLSNVSQSnmsafsqvfshPSMGSPATAGLAP 279
Cdd:pfam05109 449 PSSTHVPtnLTAPAST-----GPTVSTADVTSPTP--------AGTTSGASPVTPS-----------PSPRDNGTESKAP 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  280 GMSlsAGSSPLHSPkiTPH-TSPAPRRRSHTPNPASYMVPSSASTS-VNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPA 357
Cdd:pfam05109 505 DMT--SPTSAVTTP--TPNaTSPTPAVTTPTPNATSPTLGKTSPTSaVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPT 580

                         170       180
                  ....*....|....*....|....*...
gi 530402250  358 PLTGMVFPNyhiypPTAPHVAYMQPKAN 385
Cdd:pfam05109 581 SAVTTPTPN-----ATSPTVGETSPQAN 603
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 556-679 6.01e-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: 6.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 556 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 627
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250 628 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 679
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.26e-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: 1.26e-03
                          10        20
                  ....*....|....*....|....
gi 530402250   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) ...
 688-825 2.49e-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: 2.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  688 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 767
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250  768 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 825
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 439-607 1.40e-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: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 439 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 514
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 515 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 594
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139

                        170
                 ....*....|...
gi 530402250 595 TGKTRLRVNCVGV 607
Cdd:cd08228  140 TATGVVKLGDLGL 152
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 202-385 4.70e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  202 PYSAHDP--LTSPASSlfndfGALNISQRRKTPNPtasefipkGGSTSRLSNVSQSnmsafsqvfshPSMGSPATAGLAP 279
Cdd:pfam05109 449 PSSTHVPtnLTAPAST-----GPTVSTADVTSPTP--------AGTTSGASPVTPS-----------PSPRDNGTESKAP 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  280 GMSlsAGSSPLHSPkiTPH-TSPAPRRRSHTPNPASYMVPSSASTS-VNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPA 357
Cdd:pfam05109 505 DMT--SPTSAVTTP--TPNaTSPTPAVTTPTPNATSPTLGKTSPTSaVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPT 580

                         170       180
                  ....*....|....*....|....*...
gi 530402250  358 PLTGMVFPNyhiypPTAPHVAYMQPKAN 385
Cdd:pfam05109 581 SAVTTPTPN-----ATSPTVGETSPQAN 603
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 556-679 6.01e-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: 6.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 556 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 627
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250 628 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 679
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 210-358 6.58e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.06  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 210 TSPASS----LFNDFGALNISQRRKTPNPTASEFIPKGGSTSRLSN-------VSQSNMSAFSQVFSHPSMGSPATAGla 278
Cdd:cd21118  203 TNPPPSgsheSFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNggnngssSSNSGNSGGSNGGSSGNSGSGSGGS-- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 279 pGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPASYMVPSSASTSVNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPAP 358
Cdd:cd21118  281 -SSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.26e-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: 1.26e-03
                          10        20
                  ....*....|....*....|....
gi 530402250   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) ...
 688-825 2.49e-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: 2.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  688 VNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQ 767
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250  768 VTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQEL 825
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 439-607 1.40e-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: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 439 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 514
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 515 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 594
Cdd:cd08228   85 ---DAGDLSQMIKYF----------------------KKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI 139

                        170
                 ....*....|...
gi 530402250 595 TGKTRLRVNCVGV 607
Cdd:cd08228  140 TATGVVKLGDLGL 152
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 439-607 1.80e-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: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 439 RIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFA 514
Cdd:cd08229   27 RIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKaradCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 515 ydfHAGGETMMSRHFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILI 594
Cdd:cd08229  107 ---DAGDLSRMIKHF----------------------KKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFI 161

                        170
                 ....*....|...
gi 530402250 595 TGKTRLRVNCVGV 607
Cdd:cd08229  162 TATGVVKLGDLGL 174
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 453-602 1.56e-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: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 453 YKAVNSKDDLPYCLRRIHGFRLVNTK----CMVLVDMWKKIQHSNIVTLREVFttkaFAEPSLVFAYDFHAGGE-TMMSR 527
Cdd:cd08224   17 YRARCLLDGRLVALKKVQIFEMMDAKarqdCLKEIDLLQQLNHPNIIKYLASF----IENNELNIVLELADAGDlSRLIK 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530402250 528 HFndpnadayftkrkwgqhegplpRQHAGLLPESLIWAYIVQLSSALRTIHTaglaCRVM----DPTKILITGKTRLRV 602
Cdd:cd08224   93 HF----------------------KKQKRLIPERTIWKYFVQLCSALEHMHS----KRIMhrdiKPANVFITANGVVKL 145
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 202-385 4.70e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  202 PYSAHDP--LTSPASSlfndfGALNISQRRKTPNPtasefipkGGSTSRLSNVSQSnmsafsqvfshPSMGSPATAGLAP 279
Cdd:pfam05109 449 PSSTHVPtnLTAPAST-----GPTVSTADVTSPTP--------AGTTSGASPVTPS-----------PSPRDNGTESKAP 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250  280 GMSlsAGSSPLHSPkiTPH-TSPAPRRRSHTPNPASYMVPSSASTS-VNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPA 357
Cdd:pfam05109 505 DMT--SPTSAVTTP--TPNaTSPTPAVTTPTPNATSPTLGKTSPTSaVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPT 580

                         170       180
                  ....*....|....*....|....*...
gi 530402250  358 PLTGMVFPNyhiypPTAPHVAYMQPKAN 385
Cdd:pfam05109 581 SAVTTPTPN-----ATSPTVGETSPQAN 603
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 556-679 6.01e-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: 6.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 556 GLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLT--FDNSQN------NNPLALMAQ 627
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLEtsGDVEEGdsrylaPELLNENYT 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530402250 628 Y-QQADLISLGKVVLALACNSL---AGIQRENLQ--KAMELVTINYSSDLKNLILYLL 679
Cdd:cd13997  178 HlPKADIFSLGVTVYEAATGEPlprNGQQWQQLRqgKLPLPPGLVLSQELTRLLKVML 235
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 210-358 6.58e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.06  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 210 TSPASS----LFNDFGALNISQRRKTPNPTASEFIPKGGSTSRLSN-------VSQSNMSAFSQVFSHPSMGSPATAGla 278
Cdd:cd21118  203 TNPPPSgsheSFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNggnngssSSNSGNSGGSNGGSSGNSGSGSGGS-- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402250 279 pGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPASYMVPSSASTSVNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPAP 358
Cdd:cd21118  281 -SSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
45-68 1.26e-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: 1.26e-03
                          10        20
                  ....*....|....*....|....
gi 530402250   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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