ID A0A0P1BMI2_9BASI Unreviewed; 943 AA.
AC A0A0P1BMI2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=CELL DIVISION CONTROL PROTEIN 11 {ECO:0000313|EMBL:CEH17532.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17532.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH17532.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; CCYA01000265; CEH17532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BMI2; -.
DR STRING; 401625.A0A0P1BMI2; -.
DR OrthoDB; 1699019at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18884:SF57; CELL DIVISION CONTROL PROTEIN 10; 1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR Pfam; PF00735; Septin; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:CEH17532.1};
KW Cell division {ECO:0000313|EMBL:CEH17532.1};
KW GTP-binding {ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT DOMAIN 521..583
FT /note="Septin-type G"
FT /evidence="ECO:0000259|Pfam:PF00735"
FT DOMAIN 870..924
FT /note="Septin-type G"
FT /evidence="ECO:0000259|Pfam:PF00735"
FT REGION 43..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 100105 MW; 2C0EF0F41159EACA CRC64;
MPLFRRRSIP KVSKAAPALP DLALPGLESV ADLNAAYGMA APASTDSDLA QSDRNPKTQQ
VLPASLPNSL AQTPAPRQTP QAEPHKSELS SDHPPSKTSA ASMLGNSPSV PQYHRPWTRE
GVTDYASSSP LAAPNAGTPL VKSAISPTAQ HRPPPSAYKP SRASPASEQD FRNSPNAVSQ
QSPQARRAAI EAGRRRSLRR SKAPTPLNIL VAGAAGTGKT SWIRTLIASC EKEGSVQSLD
PQLIGHGLSL NPTHRTRLHN PPIPLPTRAV INLPAFDLAS DAILPLPAAP GSGVSRGSRG
RRPTSIASTA AGLPTSRILV SITDTPGLDF APAKEWETER KVRSLLREIE SRLSRTLAEE
TKISRAPQSL ADSHIDCVIY IIDPLSLSRS YGPKLDSVLA RNGSAAGSVS ADSKRDLEGG
SYESAGYKRT KSISEGIAAR DAILSGLRKS ATVGRAAGQG QSLASMTNGS PDPAYGLSAR
QARSSGGLGS PFAEHKETFQ NAGGDSDGID EEATAERELA LSPTELRAIS RLAKHATIIP
VIGKADLLTA TALVEVREAV RSSLMRAGIG LGPFDIREES EDQDGALGPG QFRTNGHSHD
SYEDEERDGT TNQSGEAAPS SRDAPVKRIR IRSRRTYSIA GQRTSIDSQS PGDERSEHGS
PIELKQTPPI FDDLPTNAAL GTLSAQQLAS IIPFAIFGPE SVPLQLPAAL RREPNPESSA
SLMRRPSAGN LRKAPPPAAL DEEFSLMTPL DSAIPRTQDV PPVPPLPTNL TGVASPGSNS
TGSPFVRARE NSSDLAISST PGTAEQMGTS NGTGLSELGL LNLTDASARP ATAGRSTMRP
LTQTEMTKLA RLKRDAEIGA IQRDTAPRFE RSYFWGDASV LDPVHSDFSA MRYALLFTHL
KTLKESSRAL YEEHRARALE ARRVTLSMPA NEQRRLITSI GAL
//