ID A0A0M8MT34_9BASI Unreviewed; 404 AA.
AC A0A0M8MT34;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Cell division control gtp binding protein {ECO:0000313|EMBL:KOS13230.1};
GN ORFNames=Malapachy_1662 {ECO:0000313|EMBL:KOS13230.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS13230.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS13230.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS13230.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS13230.1}.
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DR EMBL; LGAV01000007; KOS13230.1; -; Genomic_DNA.
DR RefSeq; XP_017990862.1; XM_018136164.1.
DR AlphaFoldDB; A0A0M8MT34; -.
DR STRING; 77020.A0A0M8MT34; -.
DR GeneID; 28728039; -.
DR VEuPathDB; FungiDB:Malapachy_1662; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000037751; 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 GO; GO:0051301; P:cell division; 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 Cell cycle {ECO:0000313|EMBL:KOS13230.1};
KW Cell division {ECO:0000313|EMBL:KOS13230.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 43..315
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 45953 MW; 371B14838ACAFFAF CRC64;
MASAPAATPA AVPAVPAVPR KKLTNYVGFA NLPNQVHRAS IRKGFTFTAM VVGETGLGKS
TLINTLFNTN LVPSGEERVV GREPTQTVGI ETISADIEEN EVRLRLNLID TPGFGDFVNN
ENAWEPILQT IRARFDAYLE QENRTSRSKI VDNRVHALLY FIQPTGHALR QIDLEFLTRL
HKLVNVIPII AKSDTVAESD MQTYKQRILR DLEFHGIDIV KLSTLGYEDE EMIAEVNEIQ
NRLPFAIVGS NDLVKTVDGR VVRGRAYPWG VIEVDNEEHC DFVKLRQMLI RSNMEDLREL
TEVLYENYRA SKLQELGISQ DDSVFSDVNP SAKQAEARAV HEAKLAKMES DMKAVFQRKV
AEKESKLKQS EEELYARHRQ MRAALDQQRQ ELEERKRRLQ NSLR
//
