ID A0A179G199_METCM Unreviewed; 583 AA.
AC A0A179G199;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Cell division control protein 3 {ECO:0000313|EMBL:OAQ71258.1};
GN ORFNames=VFPPC_03585 {ECO:0000313|EMBL:OAQ71258.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ71258.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ71258.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ71258.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ71258.1}.
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DR EMBL; LSBJ02000002; OAQ71258.1; -; Genomic_DNA.
DR RefSeq; XP_018147795.1; XM_018283074.1.
DR AlphaFoldDB; A0A179G199; -.
DR STRING; 1380566.A0A179G199; -.
DR GeneID; 28847068; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
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 GO; GO:0051301; P:cell division; 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:SF126; SEPTIN; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:OAQ71258.1};
KW Cell division {ECO:0000313|EMBL:OAQ71258.1};
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:UP000078397}.
FT DOMAIN 207..481
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 65343 MW; 40283FB79B8FE41B CRC64;
MATELAKQAK TRTRNTPEEA VLDQSSAAAE PTIASKRTSS IMATQDMTII PSASSSAAPS
ITSTVRHYRS MLDVEDPPKL NPLNPMSFDE LYTPQDQEQP TKNLGKLKDF GELGGASRER
ADDQVKDLGS SNGSDSPTGA PASPPAGKLE SAASAQDVPP SDPAPAVPSQ PAPSSIQDAR
NIVRRKLTGY VGFANLPNQW HRKSVRKGFN FNVMVVGESG LGKSTLVNTL FNTSLYPPRE
RKGPSLDIIP KTVQIQAISA DIEEAGVRLR LTVVDTPGFG DFVNNDESWR PIVDDIERRY
DAYLDAENKV NRMNIVDNRI HACVFFVQPT GHSLKPLDIE VMRRLHTKVN LIPVIAKSDT
LTDEEIASFK ARILADIKHH GIQIFEGPRY ELDDEETIAE NNEIMSKVPF AVVGATNEIK
TADGRAVRGR HYPWGIIEVD NEEHCDFVKL RQMLIRTHME ELKEHTNNTL YENYRTDKLI
AMGVSQDPSV FKEVNPAVKQ EEERALHEQK LAKMEAEMKM VFQQKVAEKE SKLKQSEEEL
YARHREMKEQ LERQRAELED KKQRIESGRP LEKEGKRKGF SLR
//