ID A0A2U9CRQ1_SCOMX Unreviewed; 314 AA.
AC A0A2U9CRQ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative G1/S-specific cyclin-D2-like {ECO:0000313|EMBL:AWP19261.1};
GN ORFNames=SMAX5B_011148 {ECO:0000313|EMBL:AWP19261.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP19261.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP19261.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with the CDK1 protein kinase to form a
CC serine/threonine kinase holoenzyme complex also known as maturation
CC promoting factor (MPF). The cyclin subunit imparts substrate
CC specificity to the complex. {ECO:0000256|ARBA:ARBA00025821}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; CP026261; AWP19261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CRQ1; -.
DR STRING; 52904.ENSSMAP00000013180; -.
DR Proteomes; UP000246464; Chromosome 19.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20516; CYCLIN_CCND_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 PANTHER; PTHR10177:SF262; CYCLIN DX; 1.
DR PANTHER; PTHR10177; CYCLINS; 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.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022618};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 81..165
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 174..309
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 34521 MW; C2466B3802D2DA6C CRC64;
MSVSLWCEEV EDEQSRERGQ AEAPAQGHTG GPSQVRAAWD PTVSGHRVIQ RLLHVEERYI
PSTLYVALIQ RDPERREELA KWALEVCCEC GCDEAVFPLS VSLLDRFLSA SLSVPVSPYC
LAAGCILIAS KLTECDNVTA DTLCAAAEYS FQPSNLRDME RVILATLRWD TAAVTPQDFL
PHFLASVEQS GVWEGGESEE RLSTLRRHSD TLAAMCVCDS RFLGAPPSLV AAASLNCALR
GLGDKGPSQL ALMSEVLAEL CQTDLVVLQC YSEMIEYGLH QRLRSGLQQA PTEKGEEVEN
ERAGTPTDMR EIDF
//
