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Conserved domains on  [gi|42742057|ref|NP_010156|]
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cyclin PCL2 [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 ...
 48-143 1.38e-27

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: 102.74  E-value: 1.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057  48 PLTKFINRLIKHSNVQTPTLMATSVYLAKLRSIIPSNVYGIETTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDglLIL 127
Cdd:cd20557   1 SLRSFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEGSPYRLFLVALMLASKYLDDESYSNKSWAEISG--LPV 78

                        90
                ....*....|....*.
gi 42742057 128 REVNTIERELLEYFDW 143
Cdd:cd20557  79 RELNAMEREFLEALDW 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 ...
 48-143 1.38e-27

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: 102.74  E-value: 1.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057  48 PLTKFINRLIKHSNVQTPTLMATSVYLAKLRSIIPSNVYGIETTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDglLIL 127
Cdd:cd20557   1 SLRSFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEGSPYRLFLVALMLASKYLDDESYSNKSWAEISG--LPV 78

                        90
                ....*....|....*.
gi 42742057 128 REVNTIERELLEYFDW 143
Cdd:cd20557  79 RELNAMEREFLEALDW 94
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a ...
 49-146 2.33e-16

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 459686 [Multi-domain]  Cd Length: 127  Bit Score: 74.09  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057    49 LTKFINRLIKHSNVQTPTLMATSVYLAKLRS--IIPSNvygietTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDGLLI 126
Cdd:pfam00134  34 LIDWLVEVHEKFKLLPETLYLAVNYLDRFLSkkSVPKN------KLQLVGVTCLFIAAKYEEIYPPTVEDLVYITDNAYT 107

                          90       100
                  ....*....|....*....|
gi 42742057   127 LREVNTIERELLEYFDWDVT 146
Cdd:pfam00134 108 REEILRMERLILETLNFDLS 127
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 51-139 7.43e-04

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 37.96  E-value: 7.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057     51 KFINRLIKHSNVQTPTLMaTSVYLAKlRSIIPSNVygIETTRHRIFLGCLILAAKTLNDsSPLNKHWAEYTDGLLIlREV 130
Cdd:smart00385   1 DFLRRVCKALNLDPETLN-LAVNLLD-RFLSDYKF--LKYSPSLIAAAALYLASKTEET-PPWTKELVHYTGYFTE-EEI 74


                   ....*....
gi 42742057    131 NTIERELLE 139
Cdd:smart00385  75 LRMERLLLE 83
 
Name Accession Description Interval E-value
CYCLIN_ScPCL1-like cd20557
cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar ...
 48-143 1.38e-27

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: 102.74  E-value: 1.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057  48 PLTKFINRLIKHSNVQTPTLMATSVYLAKLRSIIPSNVYGIETTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDglLIL 127
Cdd:cd20557   1 SLRSFIARLLRRTRLSPSVVLLALVYLERLRRRLPEALLGQEGSPYRLFLVALMLASKYLDDESYSNKSWAEISG--LPV 78

                        90
                ....*....|....*.
gi 42742057 128 REVNTIERELLEYFDW 143
Cdd:cd20557  79 RELNAMEREFLEALDW 94
Cyclin_N pfam00134
Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a ...
 49-146 2.33e-16

Cyclin, N-terminal domain; Cyclins regulate cyclin dependent kinases (CDKs). Swiss:P22674 is a Uracil-DNA glycosylase that is related to other cyclins. Cyclins contain two domains of similar all-alpha fold, of which this family corresponds with the N-terminal domain.


Pssm-ID: 459686 [Multi-domain]  Cd Length: 127  Bit Score: 74.09  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057    49 LTKFINRLIKHSNVQTPTLMATSVYLAKLRS--IIPSNvygietTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDGLLI 126
Cdd:pfam00134  34 LIDWLVEVHEKFKLLPETLYLAVNYLDRFLSkkSVPKN------KLQLVGVTCLFIAAKYEEIYPPTVEDLVYITDNAYT 107

                          90       100
                  ....*....|....*....|
gi 42742057   127 LREVNTIERELLEYFDWDVT 146
Cdd:pfam00134 108 REEILRMERLILETLNFDLS 127
CYCLIN_ScPCL7-like cd20558
cyclin box found in Saccharomyces cerevisiae PHO85 cyclin-7 (ScPCL7) and similar proteins; ...
 47-148 6.93e-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: 52.56  E-value: 6.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057  47 PPLT--KFINRLIKHSNVQTPTLMATSVYLAKLRSIIPS------NVygiettrHRIFLGCLILAAKTLNDSSPLNKHWA 118
Cdd:cd20558   1 PSISilDYLERIVKYCPCSPECFLLALIYIDRLIATINGfvvtslNV-------HRLLITALTLAAKFLDDRYYSNAYYA 73

                        90       100       110
                ....*....|....*....|....*....|
gi 42742057 119 EYtdGLLILREVNTIERELLEYFDWDVTIS 148
Cdd:cd20558  74 KV--GGVSVSELNKLELEFLFLLDFDLHVS 101
CYCLIN_CCNY_like cd20540
cyclin box found in cyclin-Y (CCNY) family; The CCNY family includes two cyclins, CCNY and ...
 47-143 1.11e-08

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: 51.84  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057  47 PPLTKFINRLIKHSNVQTPTLMATSVYLAKLRSIIPSNVYGieTTRHRIFLGCLILAAKTLNDSSPLNKHWAEYTDgLLI 126
Cdd:cd20540   4 EDIYRFVLTLFSAAQLTAECAIVTLIYIERLIEYAEIDLHP--SNWRRIVLGALLLASKVWDDQAVWNVDFAKILP-ILT 80

                        90
                ....*....|....*..
gi 42742057 127 LREVNTIERELLEYFDW 143
Cdd:cd20540  81 VEDLNRLERSFLELLQF 97
CYCLIN smart00385
domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and ...
 51-139 7.43e-04

domain present in cyclins, TFIIB and Retinoblastoma; A helical domain present in cyclins and TFIIB (twice) and Retinoblastoma (once). A protein recognition domain functioning in cell-cycle and transcription control.


Pssm-ID: 214641 [Multi-domain]  Cd Length: 83  Bit Score: 37.96  E-value: 7.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742057     51 KFINRLIKHSNVQTPTLMaTSVYLAKlRSIIPSNVygIETTRHRIFLGCLILAAKTLNDsSPLNKHWAEYTDGLLIlREV 130
Cdd:smart00385   1 DFLRRVCKALNLDPETLN-LAVNLLD-RFLSDYKF--LKYSPSLIAAAALYLASKTEET-PPWTKELVHYTGYFTE-EEI 74


                   ....*....
gi 42742057    131 NTIERELLE 139
Cdd:smart00385  75 LRMERLLLE 83
 
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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