ID U1GL27_ENDPU Unreviewed; 385 AA.
AC U1GL27;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Septin-type G domain-containing protein {ECO:0000259|PROSITE:PS51719};
GN ORFNames=EPUS_08365 {ECO:0000313|EMBL:ERF72918.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF72918.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE721013; ERF72918.1; -; Genomic_DNA.
DR RefSeq; XP_007801430.1; XM_007803239.1.
DR AlphaFoldDB; U1GL27; -.
DR GeneID; 19243215; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000019373; 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; 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.
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:UP000019373}.
FT DOMAIN 28..301
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT COILED 318..377
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 385 AA; 44337 MW; AB6E76D75024001D CRC64;
MAPATVESAS PIGIANLPNQ RHKIVAKRGA AFTIMVAGES GLGKTTFINT LFSTTIKNYA
DHKRRHAKQV DKTVEIEITK AELEEKFFKV RLTVIDTPGF GDYVNNRDSW MPVIEFLDDQ
HESYMLQEQQ PRRVDKIDLR VHACLYFIRP TGHTLKPLDI EVMKRLSSRV NLIPVVAKAD
TLSPADLARF KNRIRDVIDA QGIKIYQPPV EEDDEAAASH AKSLMAAMPF SVIGSEKDVK
TADGRIVKGR QYSWGVAEVE NEDHCDFKKL RSILIRTHML DLIHTTEEMH YEAYRAQQME
TRKFGEARPR KLDNPKFKEE EENLRKRFTE QVKVEEQRFR TWEQKLIGER DRLNKDLEST
HAAIKTLEQE LEQMQGSAVR SHGRR
//
