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Conserved domains on  [gi|6321862|ref|NP_011938|]
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Pcl5p [Saccharomyces cerevisiae S288C]

Protein Classification

cyclin family protein( domain architecture ID 15334467)

cyclin family protein may associate with and activate its cognate cyclin-dependent kinase (CDK); similar to Homo sapiens protein CNPPD1 and Saccharomyces cerevisiae PHO85 cyclins

CATH:  1.10.472.10
Gene Ontology:  GO:0000079|GO:0019901|GO:0007049
PubMed:  30185601|15840440|15269391
SCOP:  4001102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYCLIN_ScPCL1-like cd20557
cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar ...
 82-176 4.47e-22

cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar proteins; The family includes a group of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase, such as Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2, PCL9 and their vertebrate counterparts, cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1). PCL1 (also called PHO85 cyclin-1, or cyclin HCS26) and PCL2 (also called PHO85 cyclin-1, or cyclin HCS26 homolog) are G1/S-specific cyclin partners of the cyclin-dependent kinase (CDK) PHO85. They are essential for the control of the cell cycle at the G1/S (start) transition. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. Together with cyclin PCL2, it positively controls degradation of sphingoid long chain base kinase LCB4. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton. PCL9 is an M/G1-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. It may have a role in bud site selection in the G1 phase. The family also includes cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1) and similar proteins. Their biological functions remain unclear. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


:

Pssm-ID: 410260  Cd Length: 94  Bit Score: 86.56  E-value: 4.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321862   82 KFLNEVLKRSKCSKENAVLATFYFQKIHQSRGVRDESSLPefshCSRRIFLCCLILSHKFLNDNTYSMKNWQIISGLHAK 161
Cdd:cd20557   4 SFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEG----SPYRLFLVALMLASKYLDDESYSNKSWAEISGLPVR 79

                        90
                ....*....|....*
gi 6321862  162 DLSLMERWCLGKLNY 176
Cdd:cd20557  80 ELNAMEREFLEALDW 94
 
Name Accession Description Interval E-value
CYCLIN_ScPCL1-like cd20557
cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar ...
 82-176 4.47e-22

cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar proteins; The family includes a group of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase, such as Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2, PCL9 and their vertebrate counterparts, cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1). PCL1 (also called PHO85 cyclin-1, or cyclin HCS26) and PCL2 (also called PHO85 cyclin-1, or cyclin HCS26 homolog) are G1/S-specific cyclin partners of the cyclin-dependent kinase (CDK) PHO85. They are essential for the control of the cell cycle at the G1/S (start) transition. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. Together with cyclin PCL2, it positively controls degradation of sphingoid long chain base kinase LCB4. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton. PCL9 is an M/G1-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. It may have a role in bud site selection in the G1 phase. The family also includes cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1) and similar proteins. Their biological functions remain unclear. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410260  Cd Length: 94  Bit Score: 86.56  E-value: 4.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321862   82 KFLNEVLKRSKCSKENAVLATFYFQKIHQSRGVRDESSLPefshCSRRIFLCCLILSHKFLNDNTYSMKNWQIISGLHAK 161
Cdd:cd20557   4 SFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEG----SPYRLFLVALMLASKYLDDESYSNKSWAEISGLPVR 79

                        90
                ....*....|....*
gi 6321862  162 DLSLMERWCLGKLNY 176
Cdd:cd20557  80 ELNAMEREFLEALDW 94
 
Name Accession Description Interval E-value
CYCLIN_ScPCL1-like cd20557
cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar ...
 82-176 4.47e-22

cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar proteins; The family includes a group of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase, such as Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2, PCL9 and their vertebrate counterparts, cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1). PCL1 (also called PHO85 cyclin-1, or cyclin HCS26) and PCL2 (also called PHO85 cyclin-1, or cyclin HCS26 homolog) are G1/S-specific cyclin partners of the cyclin-dependent kinase (CDK) PHO85. They are essential for the control of the cell cycle at the G1/S (start) transition. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. Together with cyclin PCL2, it positively controls degradation of sphingoid long chain base kinase LCB4. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton. PCL9 is an M/G1-specific cyclin partner of the cyclin-dependent kinase (CDK) PHO85. It may have a role in bud site selection in the G1 phase. The family also includes cyclin Pas1/PHO80 domain-containing protein 1 (CNPPD1) and similar proteins. Their biological functions remain unclear. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410260  Cd Length: 94  Bit Score: 86.56  E-value: 4.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321862   82 KFLNEVLKRSKCSKENAVLATFYFQKIHQSRGVRDESSLPefshCSRRIFLCCLILSHKFLNDNTYSMKNWQIISGLHAK 161
Cdd:cd20557   4 SFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEG----SPYRLFLVALMLASKYLDDESYSNKSWAEISGLPVR 79

                        90
                ....*....|....*
gi 6321862  162 DLSLMERWCLGKLNY 176
Cdd:cd20557  80 ELNAMEREFLEALDW 94
CYCLIN_ScPCL7-like cd20558
cyclin box found in Saccharomyces cerevisiae PHO85 cyclin-7 (ScPCL7) and similar proteins; ...
 80-181 2.43e-09

cyclin box found in Saccharomyces cerevisiae PHO85 cyclin-7 (ScPCL7) and similar proteins; ScPCL7, also called PHO85-associated protein 1, is a cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL6, ScPCL7 controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. This family also includes Schizosaccharomyces pombe PHO85 cyclin-like protein Psl1 (SpPsl1) and Arabidopsis thaliana PHO80-like proteins, P-type cyclins (CYCPs). SpPsl1 is the cyclin partner of the CDK pef1 (PHO85 homolog). CYCPs may be involved in cell division, cell differentiation, and the nutritional status of the cell in Arabidopsis thaliana. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410261  Cd Length: 101  Bit Score: 52.95  E-value: 2.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321862   80 ILKFLNEVLKRSKCSKENAVLATFYFQKIHQSRGVRDESSLpefshCSRRIFLCCLILSHKFLNDNTYSMKNWQIISGLH 159
Cdd:cd20558   5 ILDYLERIVKYCPCSPECFLLALIYIDRLIATINGFVVTSL-----NVHRLLITALTLAAKFLDDRYYSNAYYAKVGGVS 79

                        90       100
                ....*....|....*....|..
gi 6321862  160 AKDLSLMERWCLGKLNYELAIP 181
Cdd:cd20558  80 VSELNKLELEFLFLLDFDLHVS 101
CYCLIN_CCNY_like cd20540
cyclin box found in cyclin-Y (CCNY) family; The CCNY family includes two cyclins, CCNY and ...
 76-176 2.31e-06

cyclin box found in cyclin-Y (CCNY) family; The CCNY family includes two cyclins, CCNY and CCNY-like protein 1 (CCNYL1). They can enhance Wnt/beta-catenin signaling in mitosis. CCNY, also called Cyc-Y, cyclin box protein 1 (CBCP1), cyclin fold protein 1 (CFP1), or cyclin-X (CCNX), is a key cell cycle regulator that acts as a growth factor sensor to integrate extracellular signals with the cell cycle machinery. It is a positive regulatory subunit of the cyclin-dependent kinases CDK14/PFTK1 and CDK16. It acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410243  Cd Length: 97  Bit Score: 44.52  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321862   76 STHNILKFLNEVLKRSKCSKENAVLATFYFQKIHQSRGVRdesslpeFSHCS-RRIFLCCLILSHKFLNDNTYSMKNW-Q 153
Cdd:cd20540   2 SHEDIYRFVLTLFSAAQLTAECAIVTLIYIERLIEYAEID-------LHPSNwRRIVLGALLLASKVWDDQAVWNVDFaK 74

                        90       100
                ....*....|....*....|...
gi 6321862  154 IISGLHAKDLSLMERWCLGKLNY 176
Cdd:cd20540  75 ILPILTVEDLNRLERSFLELLQF 97
 
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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