ID A0A068S053_9FUNG Unreviewed; 365 AA.
AC A0A068S053;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Related to septin 3 {ECO:0000313|EMBL:CDH55763.1};
GN ORFNames=LCOR_06877.1 {ECO:0000313|EMBL:CDH55763.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55763.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH55763.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH55763.1}.
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DR EMBL; CBTN010000032; CDH55763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S053; -.
DR STRING; 1263082.A0A068S053; -.
DR VEuPathDB; FungiDB:LCOR_06877.1; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000027586; 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 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:UP000027586}.
FT DOMAIN 14..289
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 311..363
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 365 AA; 41934 MW; F01CDC80EED4B3C6 CRC64;
MAHRLGGRRK NVKKGFQFTL MVVGASGTGR TTFVNTLCGS NVLAKKVCDN PEEAHNEPGI
TIKPMSVELD EDGVRISLTI VDTPGFGDNI DNERCFQEIV GYLERQYDDI LAEESRIKRN
PRFRDNRVHA LLYFISPTGH ALREIDIELM RRLSPRVNVI PVVGRADSLT PQELHDFKRR
IMEDVEHYNI PIYNFPYDVE EDDEDTIEEN SELRALLPFS IIGSDEEIVV NGRTVRGRQY
PWGAVEVDNP QHSDFARLRS ALLSSHLQDL KEITHDFLYE NYRTEKLSRT VDGGEQEDAS
LNADDMASQS VRLKEEQLRK EEEKLREIEL KVQREIQEKR AELLSKEEAL RSLEARLAQA
QISEE
//
