ID L5MII5_MYODS Unreviewed; 535 AA.
AC L5MII5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=G1/S-specific cyclin-E2 {ECO:0000313|EMBL:ELK38191.1};
GN ORFNames=MDA_GLEAN10013301 {ECO:0000313|EMBL:ELK38191.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK38191.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; KB099299; ELK38191.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MII5; -.
DR eggNOG; KOG0655; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20580; CYCLIN_CCNE2_rpt1; 1.
DR CDD; cd20582; CYCLIN_CCNE2_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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF70; G1_S-SPECIFIC CYCLIN-E2; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
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:UP000010556}.
FT DOMAIN 278..363
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 372..494
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT REGION 112..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 60303 MW; 3E4C9E77739ED2FA CRC64;
MACLPSTGPP LVCSPPTAPT PITSLIIRNS PSTSLITHNC HPILAWSPTT ALSSWPLTAS
TLAPPPWLCP EDVRSARPPL RGGSAALRVL RITNSPELPE VDCCQWQQCS LPNSQDGSRR
ASTEPGTQTS AAPAHSRLQA KQQPQPSQTD SPQEAQIIQA KKRKTAQDVR KRREEKVAQK
HQYEIRNCWP PALSGGISPC IIIETPHKEI ETSDFSRFTN YRFKNLFINP SPLPDLSWGC
SNDVWLNMLK KETRYVHDKH FEVLHSDLEP QMRSILLDWL LEVCEVYTLH RETFYLAQDF
FDRFMLTQKD INKNMLQLIG ITSLFIASKL EEIYAPKLQE FAYVTDGACS EEDILRMELI
ILKALKWELC PVTVISWLNL FLQVDALKDA PKVLLPQYSQ EKFIQIAQLL DLCILAIDSL
EFQYRVLAAA ALCHFTSIEV VKKASGLEWE SISECVEWMV PFASVVKSTG PVKLKMFNKI
SMEDRHNIQT HTNYLPMLEE VSYVNTLRNG GQLSPVCNGG LMTPPKSTEK PSGKH
//
