ID A0A0A2KLB9_PENIT Unreviewed; 346 AA.
AC A0A0A2KLB9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Septin {ECO:0000313|EMBL:KGO65140.1};
GN ORFNames=PITC_013990 {ECO:0000313|EMBL:KGO65140.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65140.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65140.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65140.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO65140.1}.
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DR EMBL; JQGA01001535; KGO65140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KLB9; -.
DR STRING; 40296.A0A0A2KLB9; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 2732954at2759; -.
DR PhylomeDB; A0A0A2KLB9; -.
DR Proteomes; UP000030104; 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:SF57; CELL DIVISION CONTROL PROTEIN 10; 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 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:UP000030104}.
FT DOMAIN 37..309
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 314..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 39155 MW; 3F9510F38FA6378C CRC64;
MATATTAASA QQPTVFPHSH VGFDSITSQI ERKLLKRGFQ FNVMCVGQTG LGKSTLVNTI
FASHLIDSKG RLTPSEPVRS TTEIKTESHI IEENGVRLRL NIVDTPGYGD QVNNDRCWDP
IVKYIKDQHS AYLRKELTAQ RERYIQDTRV HCCLFFIQPS GHALKPIDIV VLKKLSDVVN
VVPVIAKSDS LTLEERQAFK ERIKEEFSFH NLKMYPYDND ELDDEERAIN AQIKDIIPFS
IVGSEKTIVV NGKQVRGRQN RWGVINVEDE NHCEFVYLRN FLTRTHLQDL VETTSQIHYE
TFRAKQLLAL KESSTAGGHT GGGRPISPSA DRELSRNSQR AAMNGY
//
