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Database: UniProt
Entry: A0A197JLV5_9FUNG
LinkDB: A0A197JLV5_9FUNG
Original site: A0A197JLV5_9FUNG 
ID   A0A197JLV5_9FUNG        Unreviewed;       168 AA.
AC   A0A197JLV5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN   ORFNames=K457DRAFT_116570 {ECO:0000313|EMBL:OAQ25354.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ25354.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ25354.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ25354.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC       kinases and is essential for their biological function.
CC       {ECO:0000256|RuleBase:RU311113}.
CC   -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|ARBA:ARBA00007782,
CC       ECO:0000256|RuleBase:RU311113}.
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DR   EMBL; KV442079; OAQ25354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197JLV5; -.
DR   STRING; 1314771.A0A197JLV5; -.
DR   OrthoDB; 204504at2759; -.
DR   Proteomes; UP000078512; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR   InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR   InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR   PANTHER; PTHR23415:SF48; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT 2; 1.
DR   PANTHER; PTHR23415; CYCLIN-DEPENDENT KINASES REGULATORY SUBUNIT/60S RIBOSOME SUBUNIT BIOGENESIS PROTEIN NIP7; 1.
DR   Pfam; PF01111; CKS; 1.
DR   PRINTS; PR00296; CYCLINKINASE.
DR   SMART; SM01084; CKS; 1.
DR   SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR   PROSITE; PS00945; CKS_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU311113};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   ECO:0000256|RuleBase:RU311113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  19720 MW;  317901F7430F03D3 CRC64;
     MLSSNAGVNN GGDPTLNNHH THQQQHNGGA ANNNIAHMQP HGHTQQDHHH LHTQPSHHSH
     HHSRQDEEKA RLRAEQRAKD IAKNQEHIFY STRYYDDVWE YRHVSLPKPI ARHVPNELMT
     EEEWRSLGVK QSQGWEHYMI HSPEPHVLLF KREKDYQIKY LNAPPPKP
//
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