ID M7X0D3_RHOT1 Unreviewed; 422 AA.
AC M7X0D3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Septin AspB {ECO:0000313|EMBL:EMS23570.1};
GN ORFNames=RHTO_07304 {ECO:0000313|EMBL:EMS23570.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS23570.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS23570.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS23570.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB722647; EMS23570.1; -; Genomic_DNA.
DR RefSeq; XP_016274689.1; XM_016420962.1.
DR AlphaFoldDB; M7X0D3; -.
DR GeneID; 27371317; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF126; SEPTIN; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560}.
FT DOMAIN 44..317
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 388..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48479 MW; 4E86BB0F08FE9B6B CRC64;
MSHDAHQGQL DGAAPAHNVI QKKLGGFVGF ANLPNQYHRR SVRKGFHFTA MVVGESGLGK
STLINTLFNT SLYAKKNVPA PHHERPQTVA IESITADIEE NGVRLRLTVV DTPGYGDFIN
NEDGWKPILD NIEARFDAYL EQENRVNRQK MVDNRVHACL YFIEPTGHSL KPVDIEFMRR
LHTRVNLIPV IAKADTLTDD EIVQFKARIM SDLAHHRIEI YQAPQYELED EETLAENEEI
VRKIPFAVVG SDTVVSTPDG RQARGRAYPW GTIEVDNEDH CDFVKLRQML IRTHMEELKE
HTNGALYENY RTEKLLAMGV AQDHSVFKEV NPAAKMAEER ALHEAKLAKM EAEMKMVFQQ
KVNEKEAKLK QSEEELYARH REMKEALEKQ RIDLEEKKRR LEQGRPLTPE KQQTKKKGFL
RA
//
