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Database: UniProt
Entry: M9MCR2_PSEA3
LinkDB: M9MCR2_PSEA3
Original site: M9MCR2_PSEA3 
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}.
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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
//
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