ID A6QTL1_AJECN Unreviewed; 384 AA.
AC A6QTL1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=HCAG_00717 {ECO:0000313|EMBL:EDN02853.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02853.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476655; EDN02853.1; -; Genomic_DNA.
DR AlphaFoldDB; A6QTL1; -.
DR STRING; 339724.A6QTL1; -.
DR VEuPathDB; FungiDB:HCAG_00717; -.
DR HOGENOM; CLU_017718_7_4_1; -.
DR OMA; TNMYLRS; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000009297; 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:SF123; CELL DIVISION CONTROL PROTEIN 11; 1.
DR PANTHER; PTHR18884; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 18..295
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 295..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43919 MW; B0C249162C03C88A CRC64;
MSSAVNAIKI RRKKNVKKGI QFCLMVCGAS GTGRTTFVNT LCGKKVLQGK DADDAQNAHL
EEGVRIKPIT VELELDEEGT RISLTIVDTP GFGDQIDNEQ SFSEIVGYLE RQYDDILAEE
SRIKRNPRFR DNRVHALLYF ITPTGHGLRE LDIELMKRLS PRVNVIPVIG KADSLTPAEL
AESKKLVMED IEHYRIPVYN FPYDIEEDDE DTVEENAELR GLMPFAIVGS EDVLEIGGRK
VRARQYPWGV VEVDNPRHSD FLAIRSALLH SHLADLKEIT HDFLYENYRT EKLSKSVEGG
AGTNQDSSMN PEDLASQSVR LKEEQLRREE EKLREIEIKV QREIELKRQE LLARESQLKE
IEARMQREHH NHLHQDELNG EVNA
//
