ID A0A061HBK8_9BASI Unreviewed; 379 AA.
AC A0A061HBK8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=PFL1_02532 {ECO:0000313|EMBL:EPQ29859.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29859.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29859.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29859.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361629; EPQ29859.1; -; Genomic_DNA.
DR RefSeq; XP_007878240.1; XM_007880049.1.
DR AlphaFoldDB; A0A061HBK8; -.
DR GeneID; 19316652; -.
DR KEGG; pfp:PFL1_02532; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000053664; 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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF109; SEPTIN-1; 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.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 22..295
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
SQ SEQUENCE 379 AA; 43460 MW; 8529C114E087C7AE CRC64;
MAANGIGIAN LPNQRHKIVA KAGGHFTLMV VGESGVGKTT LINTLFSTEL ATGKDHTKRH
IKQLDKTVEI DIIKAELEEK QFKVKLTVID TPGFGDYVNN RDSWTPIVDF IDDQHELYMR
QEQQPERKEK TDLRVHACLY FIRPTGHTLK PLDIETMKRL GTRVNLIPVI AKADTLTQND
LAVFKQRIRE VINTQGITIY NPPIEADDEA SAEHAKTLMG AMPFSIIGST QDVQTADGRT
VKGRDYLWGV AEVENEEHCD FKKLRSLLIR THMLDLISTT EETHYENYRQ AQMETRKFGE
PKVKKLDNPK FKEEEELLRK RFTEQVKLEE ARFRQWEQHL IAERDRLNKD LETAHGSIKG
LEAELDAMQN GYGRGSQRR
//
