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Conserved domains on  [gi|161080921|ref|NP_001097488|]
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Poly(A) specific ribonuclease subunit PAN3, isoform Q [Drosophila melanogaster]

Protein Classification

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) ...
 645-782 2.35e-87

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: 272.05  E-value: 2.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921  645 VTDLMPMIGARFYTQLDALQSKIDMQEDELAKEMENGRLYRILVKLNSINERPDFNLDCTWSETGDRYMLKLFRDYLFHS 724
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161080921  725 VTEDGRPWLDHAHIVQCLNKLDAGSIERVQLMSRDEQSVLIVSYAELKNCLENAFSEL 782
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
DUF4797 super family cl24576
Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. ...
 243-282 1.43e-08

Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 40 amino acids in length. There is a conserved SGLPT sequence motif. There are two completely conserved residues (P and G) that may be functionally important.


The actual alignment was detected with superfamily member pfam16051:

Pssm-ID: 435100  Cd Length: 44  Bit Score: 51.06  E-value: 1.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 161080921  243 KSPPHGMTPHGASPIPSALPTSvHQENVGGTIYFYPTANA 282
Cdd:pfam16051   6 RSPVHYMYVRGLSGLPTQRVPR-SQENVGGTSYSCQYARG 44
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 407-541 9.26e-06

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 smart00220:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 254  Bit Score: 47.91  E-value: 9.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921   407 YRATHNTTGYKYCLRRIHGFRLQSTKCMTLVE--MWKKLQHTNVVQLREVFTTkafgDNSLVLVYDYHPGSQtlLAKYFt 484
Cdd:smart00220  16 YLARDKKTGKLVAIKVIKKKKIKKDRERILREikILKKLKHPNIVRLYDVFED----EDKLYLVMEYCEGGD--LFDLL- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161080921   485 papetngytdpfqgearpfshksnmqrTSNGPlLPEATIWSIIMQLTAGLKAIHHAG 541
Cdd:smart00220  89 ---------------------------KKRGR-LSEDEARFYLRQILSALEYLHSKG 117
 
Name Accession Description Interval E-value
Pan3_PK pfam18101
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
 645-782 2.35e-87

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: 272.05  E-value: 2.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921  645 VTDLMPMIGARFYTQLDALQSKIDMQEDELAKEMENGRLYRILVKLNSINERPDFNLDCTWSETGDRYMLKLFRDYLFHS 724
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161080921  725 VTEDGRPWLDHAHIVQCLNKLDAGSIERVQLMSRDEQSVLIVSYAELKNCLENAFSEL 782
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
DUF4797 pfam16051
Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. ...
 243-282 1.43e-08

Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 40 amino acids in length. There is a conserved SGLPT sequence motif. There are two completely conserved residues (P and G) that may be functionally important.


Pssm-ID: 435100  Cd Length: 44  Bit Score: 51.06  E-value: 1.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 161080921  243 KSPPHGMTPHGASPIPSALPTSvHQENVGGTIYFYPTANA 282
Cdd:pfam16051   6 RSPVHYMYVRGLSGLPTQRVPR-SQENVGGTSYSCQYARG 44
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 407-541 9.26e-06

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 47.91  E-value: 9.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921   407 YRATHNTTGYKYCLRRIHGFRLQSTKCMTLVE--MWKKLQHTNVVQLREVFTTkafgDNSLVLVYDYHPGSQtlLAKYFt 484
Cdd:smart00220  16 YLARDKKTGKLVAIKVIKKKKIKKDRERILREikILKKLKHPNIVRLYDVFED----EDKLYLVMEYCEGGD--LFDLL- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161080921   485 papetngytdpfqgearpfshksnmqrTSNGPlLPEATIWSIIMQLTAGLKAIHHAG 541
Cdd:smart00220  89 ---------------------------KKRGR-LSEDEARFYLRQILSALEYLHSKG 117
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 433-559 2.57e-05

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily 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: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 46.76  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 433 CMTL--VEMWKKLQ-HTNVVQLREVFTTKafgdNSLVLVYDYHPGsqtllakyftpapetNGYtdpfqgearpfshksNM 509
Cdd:cd07830   42 CMNLreVKSLRKLNeHPNIVKLKEVFREN----DELYFVFEYMEG---------------NLY---------------QL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 161080921 510 QRTSNGPLLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVTGKRV 559
Cdd:cd07830   88 MKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV 137
Pkinase pfam00069
Protein kinase domain;
404-474 1.05e-03

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 41.08  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161080921  404 ATTYRATHNTTGYKYCLRRIHGFRLQSTKCMTL---VEMWKKLQHTNVVQLREVFTTKafgdNSLVLVYDYHPG 474
Cdd:pfam00069  13 GTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNIlreIKILKKLNHPNIVRLYDAFEDK----DNLYLVLEYVEG 82
 
Name Accession Description Interval E-value
Pan3_PK pfam18101
Pan3 Pseudokinase domain; This is a pseudokinase (PK) domain found in PAB-dependent poly(A) ...
 645-782 2.35e-87

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: 272.05  E-value: 2.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921  645 VTDLMPMIGARFYTQLDALQSKIDMQEDELAKEMENGRLYRILVKLNSINERPDFNLDCTWSETGDRYMLKLFRDYLFHS 724
Cdd:pfam18101   1 IDELLPMIGARLLTELDAALHYNDELESELSRELENGRLFRLLCKLGFINERPEFEGDPRWSETGDRYMLKLFRDYVFHQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 161080921  725 VTEDGRPWLDHAHIVQCLNKLDAGSIERVQLMSRDEQSVLIVSYAELKNCLENAFSEL 782
Cdd:pfam18101  81 VDEQGRPVLDLGHVLSCLNKLDAGVDEKIMLTSRDEQSCLVVSYKELKKCIESAFGEL 138
DUF4797 pfam16051
Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. ...
 243-282 1.43e-08

Domain of unknown function (DUF4797); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 40 amino acids in length. There is a conserved SGLPT sequence motif. There are two completely conserved residues (P and G) that may be functionally important.


Pssm-ID: 435100  Cd Length: 44  Bit Score: 51.06  E-value: 1.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 161080921  243 KSPPHGMTPHGASPIPSALPTSvHQENVGGTIYFYPTANA 282
Cdd:pfam16051   6 RSPVHYMYVRGLSGLPTQRVPR-SQENVGGTSYSCQYARG 44
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 407-541 9.26e-06

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 47.91  E-value: 9.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921   407 YRATHNTTGYKYCLRRIHGFRLQSTKCMTLVE--MWKKLQHTNVVQLREVFTTkafgDNSLVLVYDYHPGSQtlLAKYFt 484
Cdd:smart00220  16 YLARDKKTGKLVAIKVIKKKKIKKDRERILREikILKKLKHPNIVRLYDVFED----EDKLYLVMEYCEGGD--LFDLL- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 161080921   485 papetngytdpfqgearpfshksnmqrTSNGPlLPEATIWSIIMQLTAGLKAIHHAG 541
Cdd:smart00220  89 ---------------------------KKRGR-LSEDEARFYLRQILSALEYLHSKG 117
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 433-559 2.57e-05

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily 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: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 46.76  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 433 CMTL--VEMWKKLQ-HTNVVQLREVFTTKafgdNSLVLVYDYHPGsqtllakyftpapetNGYtdpfqgearpfshksNM 509
Cdd:cd07830   42 CMNLreVKSLRKLNeHPNIVKLKEVFREN----DELYFVFEYMEG---------------NLY---------------QL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 161080921 510 QRTSNGPLLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVTGKRV 559
Cdd:cd07830   88 MKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV 137
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 404-538 3.34e-05

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: 46.11  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 404 ATTYRATHNTTGYKYCLRRIHGFRLQSTK----CMTLVEMWKKLQHTNVVQLREVFttkaFGDNSLVLVYDYHP-GSQTL 478
Cdd:cd08224   14 SVVYRARCLLDGRLVALKKVQIFEMMDAKarqdCLKEIDLLQQLNHPNIIKYLASF----IENNELNIVLELADaGDLSR 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 479 LAKYFtpapetngytdpfqgearpfshksnmqrTSNGPLLPEATIWSIIMQLTAGLKAIH 538
Cdd:cd08224   90 LIKHF----------------------------KKQKRLIPERTIWKYFVQLCSALEHMH 121
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 407-471 1.70e-04

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily 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: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 44.48  E-value: 1.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161080921 407 YRATHNTTGYKYCLRRIhgfRLQSTKC------MTLVEMWKKLQHTNVVQLREVFTTKAFGD--NSLVLVYDY 471
Cdd:cd07840   16 YKARNKKTGELVALKKI---RMENEKEgfpitaIREIKLLQKLDHPNVVRLKEIVTSKGSAKykGSIYMVFEY 85
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 405-555 1.89e-04

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. 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: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 43.92  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 405 TTYRATHNTTGYKYCLRRIHgFRLQSTK----CMTLVEMWKKLQHTNVVQLREVFttkaFGDNSLVLVYDYHPGSQtlLA 480
Cdd:cd08530   15 SVYKVKRLSDNQVYALKEVN-LGSLSQKeredSVNEIRLLASVNHPNIIRYKEAF----LDGNRLCIVMEYAPFGD--LS 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161080921 481 KYFTpapetngytdpfqgearpfshKSNMQRTsngpLLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVT 555
Cdd:cd08530   88 KLIS---------------------KRKKKRR----LFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLS 137
Pkinase pfam00069
Protein kinase domain;
404-474 1.05e-03

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 41.08  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161080921  404 ATTYRATHNTTGYKYCLRRIHGFRLQSTKCMTL---VEMWKKLQHTNVVQLREVFTTKafgdNSLVLVYDYHPG 474
Cdd:pfam00069  13 GTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNIlreIKILKKLNHPNIVRLYDAFEDK----DNLYLVLEYVEG 82
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 407-471 1.09e-03

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily 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: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 41.70  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161080921 407 YRATHNTTGYKYCLRRIH------GFrlQSTkcmTLVEM--WKKLQHTNVVQLREVFTTKafgdNSLVLVYDY 471
Cdd:cd07829   16 YKAKDKKTGEIVALKKIRldneeeGI--PST---ALREIslLKELKHPNIVKLLDVIHTE----NKLYLVFEY 79
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 404-474 4.53e-03

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 39.77  E-value: 4.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161080921 404 ATTYRATHNTTGYKYCLRRIHGFRLQSTKCMTL---VEMWKKLQHTNVVQLREVFTTkafgDNSLVLVYDYHPG 474
Cdd:cd05117   14 GVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLrreIEILKRLDHPNIVKLYEVFED----DKNLYLVMELCTG 83
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
 417-557 5.58e-03

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 39.67  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161080921 417 KYCLRRIHGFRLQSTKCMTlVEMWKKLQHTNVVQLREVFTTKAfgDNSLVLVYDYHPGSQTLLAKyFTPAPETNgytdpf 496
Cdd:cd07867   31 EYALKQIEGTGISMSACRE-IALLRELKHPNVIALQKVFLSHS--DRKVWLLFDYAEHDLWHIIK-FHRASKAN------ 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161080921 497 qgearpfshKSNMQrtsngplLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVTGK 557
Cdd:cd07867  101 ---------KKPMQ-------LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGE 145
 
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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