ID A0A1X2G8N5_9FUNG Unreviewed; 383 AA.
AC A0A1X2G8N5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Septin {ECO:0000313|EMBL:ORX47770.1};
GN ORFNames=DM01DRAFT_1326884 {ECO:0000313|EMBL:ORX47770.1};
OS Hesseltinella vesiculosa.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX47770.1, ECO:0000313|Proteomes:UP000242146};
RN [1] {ECO:0000313|EMBL:ORX47770.1, ECO:0000313|Proteomes:UP000242146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX47770.1,
RC ECO:0000313|Proteomes:UP000242146};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX47770.1}.
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DR EMBL; MCGT01000032; ORX47770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2G8N5; -.
DR STRING; 101127.A0A1X2G8N5; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000242146; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000242146}.
FT DOMAIN 27..299
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 330..375
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 383 AA; 44189 MW; 334659097AE20DDC CRC64;
MSATVVLPDG VGIAHLPNQR HKIVSKRGAR YTIMVCGESG VGKTTFVNTL FTSGIKDPKA
LHLRHKKQTE KTVEIDITKA ELEEKNFSVK LAVIDTPGFG DYVNNRDSWL PIIEFLDDQH
EAYMAQEQQP RRGGIIDMRV HVCLYFVRPN GHTLKPLDIE VMKQLGTRVN LIPVIAKADT
LTPQDLAKFK RNILDVIHAQ GIQVYSCPIE SEDEDVTKTN QQIMDSMPFA VIGSTQDVSV
NGRTVKGRQY SWGVAEVENE DHCDFKKLRN LLIRSHMHDL IDTTEENHYE NYRQVQMETR
KFGEKKVKKY ENPKFKEKEE KLRMAFTEQV KKEESRFRQW EAQLVSERDR LNKDLEAQHA
QIKAMETELE QLHQMAYRGG ARR
//
