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Conserved domains on  [gi|62862058|ref|NP_001015176|]
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uncharacterized protein Dmel_CG40191, isoform C [Drosophila melanogaster]

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
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 ...
70-153 9.88e-17

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: 74.62  E-value: 9.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862058  70 AQVHATPCSLIMALIYLDRLNVIDSGYSCRI--TPQQLFVVSLMISTKFYagHDERFYLEDWASDACMTEDRLKAVELEF 147
Cdd:cd20557  11 RRTRLSPSVVLLALVYLERLRRRLPEALLGQegSPYRLFLVALMLASKYL--DDESYSNKSWAEISGLPVRELNAMEREF 88

                ....*.
gi 62862058 148 LSAMGW 153
Cdd:cd20557  89 LEALDW 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 ...
70-153 9.88e-17

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: 74.62  E-value: 9.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862058  70 AQVHATPCSLIMALIYLDRLNVIDSGYSCRI--TPQQLFVVSLMISTKFYagHDERFYLEDWASDACMTEDRLKAVELEF 147
Cdd:cd20557  11 RRTRLSPSVVLLALVYLERLRRRLPEALLGQegSPYRLFLVALMLASKYL--DDESYSNKSWAEISGLPVRELNAMEREF 88

                ....*.
gi 62862058 148 LSAMGW 153
Cdd:cd20557  89 LEALDW 94
PRK13377 PRK13377
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
106-162 3.05e-03

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 184013 [Multi-domain]  Cd Length: 129  Bit Score: 37.47  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862058  106 FVVSLMIS---TKFYAghDERFYLEDWAsdacMTEDRLKAV---ELEFLSAMGWNIYISNELF 162
Cdd:PRK13377  30 FCMSLMKAenrERFKA--DERAYLDEWP----MTEEQKQAVlarDLNRCIALGGNIYFLAKIG 86
 
Name Accession Description Interval E-value
CYCLIN_ScPCL1-like cd20557
cyclin box found in Saccharomyces cerevisiae G1/S-specific cyclin PCL1, PCL2 and similar ...
70-153 9.88e-17

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: 74.62  E-value: 9.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862058  70 AQVHATPCSLIMALIYLDRLNVIDSGYSCRI--TPQQLFVVSLMISTKFYagHDERFYLEDWASDACMTEDRLKAVELEF 147
Cdd:cd20557  11 RRTRLSPSVVLLALVYLERLRRRLPEALLGQegSPYRLFLVALMLASKYL--DDESYSNKSWAEISGLPVRELNAMEREF 88

                ....*.
gi 62862058 148 LSAMGW 153
Cdd:cd20557  89 LEALDW 94
CYCLIN_ScPCL7-like cd20558
cyclin box found in Saccharomyces cerevisiae PHO85 cyclin-7 (ScPCL7) and similar proteins; ...
75-158 7.88e-05

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: 41.39  E-value: 7.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862058  75 TPCS---LIMALIYLDRLnvIDSGYSCRITPQQ---LFVVSLMISTKFyagHDERFY-LEDWASDACMTEDRLKAVELEF 147
Cdd:cd20558  16 CPCSpecFLLALIYIDRL--IATINGFVVTSLNvhrLLITALTLAAKF---LDDRYYsNAYYAKVGGVSVSELNKLELEF 90
                        90
                ....*....|.
gi 62862058 148 LSAMGWNIYIS 158
Cdd:cd20558  91 LFLLDFDLHVS 101
PRK13377 PRK13377
protocatechuate 4,5-dioxygenase subunit alpha; Provisional
106-162 3.05e-03

protocatechuate 4,5-dioxygenase subunit alpha; Provisional


Pssm-ID: 184013 [Multi-domain]  Cd Length: 129  Bit Score: 37.47  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862058  106 FVVSLMIS---TKFYAghDERFYLEDWAsdacMTEDRLKAV---ELEFLSAMGWNIYISNELF 162
Cdd:PRK13377  30 FCMSLMKAenrERFKA--DERAYLDEWP----MTEEQKQAVlarDLNRCIALGGNIYFLAKIG 86
 
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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