ID A5DH47_PICGU Unreviewed; 347 AA.
AC A5DH47;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000256|RuleBase:RU365059};
GN ORFNames=PGUG_02598 {ECO:0000313|EMBL:EDK38500.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38500.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK38500.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408157; EDK38500.2; -; Genomic_DNA.
DR RefSeq; XP_001484869.1; XM_001484819.1.
DR AlphaFoldDB; A5DH47; -.
DR STRING; 294746.A5DH47; -.
DR GeneID; 5126574; -.
DR KEGG; pgu:PGUG_02598; -.
DR eggNOG; KOG1533; Eukaryota.
DR HOGENOM; CLU_037460_0_2_1; -.
DR InParanoid; A5DH47; -.
DR OMA; ATHNYFL; -.
DR OrthoDB; 168004at2759; -.
DR Proteomes; UP000001997; 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; 1.
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:UP000001997}.
FT REGION 306..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39566 MW; FD2503058A4576C6 CRC64;
MFGQVVIGPP GSGKSTYCYG MYQFMSAIGR KSCVINLDPA NDRLPYPDCA LDIRDILTLD
EIMEELDLGP NGGLMYALEC LSSVEIENFV AKIKKLADEN YYLLIDCPGQ VELFTHHNSL
YQILKLISRK GGIRLCTVSL VDSIYLTSPS QYISILLLSL RSMLQLDLPH VNVISKIDKL
HSYGSLPFKL DYYTEVQDLH YLKPLLEKES NSILGKKFVR LTEAIGELIE DFNLVSFEVL
SVENKRSMIH LLNIIDKANG YMFGTSEIGG DTIWSEATRQ SSLIKDIDVD IHERWIEQKD
TFDRLEETED RRGLNEPNTT GEDEAGEEDE DEAYEEDLRE WERLHSN
//
