ID A0A167RM30_CALVF Unreviewed; 324 AA.
AC A0A167RM30;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cell division/GTP binding protein {ECO:0000313|EMBL:KZP01060.1};
GN ORFNames=CALVIDRAFT_532673 {ECO:0000313|EMBL:KZP01060.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZP01060.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZP01060.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZP01060.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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}.
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DR EMBL; KV417267; KZP01060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167RM30; -.
DR STRING; 1330018.A0A167RM30; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000076738; 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 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: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 Cell cycle {ECO:0000313|EMBL:KZP01060.1};
KW Cell division {ECO:0000313|EMBL:KZP01060.1};
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:UP000076738}.
FT DOMAIN 35..307
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
SQ SEQUENCE 324 AA; 37027 MW; FBC410B2572BB2C3 CRC64;
MASADVMDQP EEIRAASYVG FDSITRQIEH KLLKRGFQFN VMVVGQTGLG KSTMINTIFA
SHLIDSKGRF EADEPVRQTT EIVANSHVIT ENGVKLRLNI VDTPGYGDQV NNEGCWDPIV
KYIKDQHSLY LRKELTAMRD KYILDTRIHC CLYFINPTGH GLRPVDVIVM KKLSEVVNVV
PVIAKADSLT LDERAKFKKR IREELAYHSI KLFPFQSDEY DDEEEKENQI IRDMIPFAVV
GSERNVIVDG KSVRGRKNRW GVINIEDERH CEFVYLRNFL TRTHLQDLIE TTAQLHYEAF
RSKQLLALKD ASNRNAAPSS AAQS
//
