ID S7ZXQ7_PENO1 Unreviewed; 471 AA.
AC S7ZXQ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS33566.1};
GN ORFNames=PDE_08528 {ECO:0000313|EMBL:EPS33566.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS33566.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS33566.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
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DR EMBL; KB644415; EPS33566.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZXQ7; -.
DR STRING; 933388.S7ZXQ7; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_10_2_1; -.
DR OrthoDB; 5474295at2759; -.
DR PhylomeDB; S7ZXQ7; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR CDD; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
DR CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF587; S-PHASE ENTRY CYCLIN-5-RELATED; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 238..322
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 331..445
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 335..416
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 53315 MW; F708E8B2345CCE7D CRC64;
MPVARSLRSR GAMNENDENG PVTRMTRAKA ALSTEGPTDA IKKPVQAKRS TATGGAQRPR
AALGDVSNVN KTEAAEIKGA KKTATSKAGL TSKATKQTAG IQKLSQTNSS RTGVLQPRNP
NPPAAKANKR PKVDKAEQQE PPRKKEKIEP EEKKIEVEQA KSQKLKDDVV EPVQQEAGLS
EDVADLDTED LDDPLMAAEY VVEIFDYLRD LEQTTLPNPQ YIEHQPDLEW KMRGILVDWL
IEVHTRFRLL PETLFLAVNI IDRFLSVEVV ALDRLQLVGV TAMFIASKYE EVLSPHVANF
SHVADETFTD KEILDAERHV LATLEYNMSF PNPMNFLRRI SKADNYDIQT RTLGKYLMEI
SLLDHRFMSY PQSHIAAAAM YLARLILDRG PWDATLAHYA GYDEKEIDPV FRLMIDYLHR
PVSHEAFFKK YASKKFLKAS ILTRQWAKKY HKLYIDSSDS EPYTFIKDGE Q
//
