ID A0A1X2I4N0_9FUNG Unreviewed; 370 AA.
AC A0A1X2I4N0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Septin-domain-containing protein {ECO:0000313|EMBL:ORZ09273.1};
GN ORFNames=BCR42DRAFT_484389 {ECO:0000313|EMBL:ORZ09273.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ09273.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ09273.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ09273.1,
RC ECO:0000313|Proteomes:UP000193560};
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:ORZ09273.1}.
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DR EMBL; MCGE01000028; ORZ09273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2I4N0; -.
DR STRING; 90262.A0A1X2I4N0; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000193560; 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:UP000193560}.
FT DOMAIN 19..294
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 316..368
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 370 AA; 42380 MW; 94A751723C03AE5B CRC64;
MSAAISPARL GGRRKNVKKG FQFTLMVVGA SGTGRTTFVN TLCDSGVLER QVCDNPEEAH
NEPGINIKPV SVELDEDGVR ISLTIVDTPG FGDNIDNERC FQEIVGYLER QYDDILAEES
RIKRNPRFRD NRVHSLLYFI SPTGHALREI DIELMRRLSP RVNVIPVVGR ADSLTPQELK
DFKKRIMEDI EHYNIPIYNF PYDVEEDDED TIEENSELRD LLPFAIIGSD EEIVVNGRTV
RGRQYPWGAV EVDNPQHSDF GRLRSALLSS HLQDLKEITH DFLYENYRTE KLSRTVNGGD
QEDASLNADD MASQSVRLKE EQLRKEEEKL REIELKVQRE IQEKRAELLS KEEALRNLEA
RLAQAQLADE
//
