ID M9MCR2_PSEA3 Unreviewed; 442 AA.
AC M9MCR2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000256|RuleBase:RU365059};
GN ORFNames=PANT_9d00255 {ECO:0000313|EMBL:GAC73763.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC73763.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC step prior to nuclear import. {ECO:0000256|RuleBase:RU365059}.
CC -!- SUBUNIT: Binds to RNA polymerase II (RNAPII).
CC {ECO:0000256|RuleBase:RU365059}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290, ECO:0000256|RuleBase:RU365059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF196775; GAC73763.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MCR2; -.
DR STRING; 1151754.M9MCR2; -.
DR OrthoDB; 168004at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17871; GPN2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030231; Gpn2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU365059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365059};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT REGION 215..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49377 MW; 19E1057C12360A74 CRC64;
MPFAQLVIGP PGSGKTTYCF GQYQFLSLLS RPCSVINLDP ANDRLPYPCA VDINRLISVR
DVMAELSLGP NAAMLYCIEY LEKNVDWLIQ ELKRVMDEQR QGKTGQIAGR GDQETPIGPV
SPGFEYLIFD LPGQVELSTN HPALKRILAT LEKQLGLRFV AVHLTDATHI TDASRYVSIL
ILALRAMLTL ELPHVNVLSK VDLLGQSFIS RSKRSLDRYG PDSDTDGDDD EDMEDASADR
PGNSADMGLQ SDLAFNLDFY TQVQDLSYLR DLLSQPSGPG SSLRNEKYGE LNEAICELVE
DFGLVSFETL AVEDRRSMFR LLQVLDKAVG YIYVSASSNA YDYGDEENEG LYEPGRASAT
AGVALRGQMG ADAHSLFSVA DRGDPLGWGD ALEVQERYID HRELYEEAEA EERKQMHEKE
WEQKVWSEVR KATEEQKQKQ GK
//