ID A0A3Q7XX93_CICAR Unreviewed; 663 AA.
AC A0A3Q7XX93;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=B-like cyclin {ECO:0000256|ARBA:ARBA00032263};
GN Name=LOC101488392 {ECO:0000313|RefSeq:XP_027188711.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_027188711.1};
RN [1] {ECO:0000313|RefSeq:XP_027188711.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_027188711.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Interacts with the CDC2 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:ARBA00011177}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR RefSeq; XP_027188711.1; XM_027332910.1.
DR AlphaFoldDB; A0A3Q7XX93; -.
DR STRING; 3827.A0A3Q7XX93; -.
DR PaxDb; 3827-XP_004493703-1; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000087171; Chromosome Ca3.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20567; CYCLIN_AtCycB-like_rpt1; 1.
DR CDD; cd20511; CYCLIN_AtCycB-like_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:SF615; G2_MITOTIC-SPECIFIC CYCLIN-B; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 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:UP000087171}.
FT DOMAIN 432..516
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 525..651
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 529..620
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 72163 MW; A0C1903DEE929EA4 CRC64;
MASRPIVPQQ QQPRGDAALG GGKQHQKKNG VAGGDGRNRG ALRDIGNVVT LRGVEVKPNR
PITRSFCAQL LANAQAAAVN ENNKKQACAN VAPARPVAPA KPAPPVLDGV AVARRVATKP
AQKKVTAKPK PVEVIDISSE ESANEEDKSV HKKKEVDVNS KKKSRTLTSV LTARSKEQCD
CDFEMASRPI VPQQQQPRGD AALGGGKQHQ KKNGVAGGDG RNRGALRDIG NVVTLRGVEV
KPNRPITRSF CAQLLANAQA AAVNENNKKQ ACANVAPARP VAPARPVAPA KPAPPVLDGV
AVARRVATKP AQKKVTAKPK PVEVIDISSE ESANEEDKSV HKKKEVDVNS KKKSRTLTSV
LTARSKAACG LTNKPKEIVD IDAGDANNEL AAVEYIEDIY KFYKIIENES RPHDYMDSQP
EINERMRAIL VDWLVDVHTK FELSPETLYL TINIVDRFLA INLVSRRELQ LVGISAMLMA
SKYEEIWPPE VNDFVCLSDR AYTHEQILMM EKTILGKLEW TLTVPTPFVF LVRFIKASVS
ASLSVPSEQD DALENMSHFL SELGMMHYES LRYCPSMVAA SAVFAARCTL NKVPVWNETL
KVHTGYSEEQ LMDCARMLVS FHSSVGNGKL KVVFKKYSDL QRGAVAVIPP AKNLVAVVGG
GSF
//
