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Database: UniProt
Entry: A0A0C2FRF7_9BILA
LinkDB: A0A0C2FRF7_9BILA
Original site: A0A0C2FRF7_9BILA 
ID   A0A0C2FRF7_9BILA        Unreviewed;       353 AA.
AC   A0A0C2FRF7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=G2/mitotic-specific cyclin-B3 {ECO:0000256|ARBA:ARBA00021434};
GN   ORFNames=ANCDUO_22458 {ECO:0000313|EMBL:KIH47481.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH47481.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH47481.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH47481.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KN767646; KIH47481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2FRF7; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        246..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..206
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          215..334
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          219..301
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          22..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  40960 MW;  2769A02036BC554D CRC64;
     MRSRDLTQNE AISNVVIDSS KKLHLTKDSR RNGRRSKTQS ENSLPSITES SDSEELKPAV
     EPDPCPAYDY DAESGPDIAN VSEFAFDIFR YYKSREKQFH VPDYLSQHPN LSKQTRAVLA
     DWMVEIQETF ELNHETLYMS VKIVDMYLSK TKGVVKDDLQ LLASAAIFIA CKFEERSPPL
     IDDFMYVCEE MFNREQMIRM EMKVLDTINY DIGFPLSYRN VRRYARVTKT DMPKLTLARY
     ILETSLMFYE FIGVSESLMA AAAILLALKM HDKETTWTPI LQKYSGYKAE DVEPLMWELN
     HMLHKRRVMY DRLETVFSKY SHEVFFSVAA IPLLPDVYTL ERPVQAPPSS SPK
//
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