ID A0A3P8QMU5_ASTCA Unreviewed; 381 AA.
AC A0A3P8QMU5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=G2/mitotic-specific cyclin-B3 {ECO:0000256|ARBA:ARBA00021434};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000030476.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000030476.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000030476.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8QMU5; -.
DR Ensembl; ENSACLT00000031186.1; ENSACLP00000030476.1; ENSACLG00000020564.1.
DR GeneTree; ENSGT00940000160459; -.
DR Proteomes; UP000265100; Chromosome 3.
DR Bgee; ENSACLG00000020564; Expressed in testis and 2 other cell types or tissues.
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; cd20508; CYCLIN_CCNB3_rpt1; 1.
DR CDD; cd20510; CYCLIN_CCNB3_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 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 Cell cycle {ECO:0000256|ARBA:ARBA00022618};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 161..245
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 254..370
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 258..339
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 43171 MW; DD37FBEA212D8024 CRC64;
MPFPRGRKPT AAAGSKIPKL NATASENQED ATQVKRSSSP PRGAPKKRTA FIDITNAHKV
QISFPGKKKE PGKKTAKKTS STSARCEKLF LSCVSFSFHP SMQIPKEFDI DSENSEDCYM
CPEYAKDIFD YLKNREEKFV LCNYMPTQPS LNSEMRAILI DWLVEVQENF ELYHETLYLA
VKMTDHYLAK TPVHREMLQL VGSTAMLVAS KFEEHSPPCV DDFLYICDDA YKREELISME
ESILQTLSFD INIPIPYRFL RRYAKCVSAS MDTLTLARYY CEMSLMEMDL VPERGSLVAA
ACLLMALVTK DLGGWSPILQ FHSGYQASDL APVVRRIYSM LSAPPDDKLR AIKNKYSHKV
FFEVASLPLL SIDILEKALS S
//
