ID F4X3B6_ACREC Unreviewed; 391 AA.
AC F4X3B6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN ORFNames=G5I_12810 {ECO:0000313|EMBL:EGI59097.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI59097.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR EMBL; GL888609; EGI59097.1; -; Genomic_DNA.
DR AlphaFoldDB; F4X3B6; -.
DR STRING; 103372.F4X3B6; -.
DR EnsemblMetazoa; XM_011066406.1; XP_011064708.1; LOC105152246.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; F4X3B6; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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; SEPTIN; 1.
DR PANTHER; PTHR18884:SF126; 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:UP000007755}.
FT DOMAIN 1..263
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 45169 MW; A3DC8BE0BA699564 CRC64;
MVVGESGLGK STLINSMFLA DIYSAEYPGP SLRIKKTVAV ETSKVLLKEK GVNLTLTVVD
TPGFGDAVDN SNCWVPVIDY IESKYEEFLN AESRVTRRQI PDSRVHCCLY FVAPSGHGLK
PLDVEFMQRL HDKVNIIPVI AKADTMTPDE CAHFKKQILN EIAQHKIKIY EFPEVEEEED
TKLHKLLRDR VPFAVVGANT VIEHDGKKIR GRKYPWGIAE VENLEHCDFI ALRNMVVRTH
VQDLKDVTNN VHYENFRCRT LAGLGVDGKP TKASNKNPLA QLEEEKREHD NKMKKMETEM
EQVFEMKVRE KRQKLKDSET DLQRRHEQMR RSLEQQVREL EEKRRAFEAE KTAWEQQTGH
SIEELRRRSL EANSKETVDG KDKKNKKKGL F
//
