ID A0A0R3RZM7_9BILA Unreviewed; 392 AA.
AC A0A0R3RZM7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=G2/mitotic-specific cyclin-B3 {ECO:0000256|ARBA:ARBA00021434};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000779101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000779101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR AlphaFoldDB; A0A0R3RZM7; -.
DR STRING; 1147741.A0A0R3RZM7; -.
DR WBParaSite; EEL_0000779101-mRNA-1; EEL_0000779101-mRNA-1; EEL_0000779101.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
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 PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF601; G2_MITOTIC-SPECIFIC CYCLIN-B3; 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.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 153..235
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 244..362
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 248..332
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 45709 MW; C071F1DFE35D5DCE CRC64;
MIPANTKRNI NPTYSDDKNA LPKKNKRTGL TDLSNAISST LHISSKAGEN TEKPRRVRPV
VRAKSEERKS FRVSESTYES DSELPTRLDQ TIWMDPCPDF DYDARNRGDP FQVPEYAVDI
FNYYHNRELK FRPFDYLHRH PQLKKIRRAK VIDWFVRCQE DFEVNHEVLY HSVKMFDLFM
CASRNMEQFD YIGAAAMIVA AKLDQQGPPL PDDFINLPLG QRVKKVNNYE RKILTALKCD
INFPLSYRFL RRYSRTGGLD MQTLTLARFV LETSLLFYEF ICVPDSLMAA AALLLSMRMI
KTGEWSTKLI KYSGYKLEQV EPLMWRLNHM MKMRSKVYPA CISIEEKYSH PIFYNVADIQ
LLPDRRPRNE PVGPPIGLGF ASINKSKLTF ED
//