ID   GPN2_MACFA              Reviewed;         310 AA.
AC   Q4R579;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=GPN-loop GTPase 2 {ECO:0000250|UniProtKB:Q9H9Y4};
DE   AltName: Full=ATP-binding domain 1 family member B {ECO:0000250|UniProtKB:Q9H9Y4};
GN   Name=GPN2 {ECO:0000250|UniProtKB:Q9H9Y4};
GN   Synonyms=ATPBD1B {ECO:0000250|UniProtKB:Q9H9Y4}; ORFNames=QccE-15365;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q08726}.
CC   -!- SUBUNIT: Heterodimers with GPN1 or GPN3. Binds to RNA polymerase II
CC       (RNAPII). {ECO:0000250|UniProtKB:Q08726, ECO:0000250|UniProtKB:Q9H9Y4}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
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DR   EMBL; AB169665; BAE01746.1; -; mRNA.
DR   RefSeq; NP_001274641.1; NM_001287712.1.
DR   AlphaFoldDB; Q4R579; -.
DR   SMR; Q4R579; -.
DR   STRING; 9541.XP_005544363.1; -.
DR   GeneID; 102133472; -.
DR   CTD; 54707; -.
DR   VEuPathDB; HostDB:ENSMFAG00000036999; -.
DR   eggNOG; KOG1533; Eukaryota.
DR   OMA; YAPLPFN; -.
DR   OrthoDB; 964931at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030231; Gpn2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21231; PTHR21231; 1.
DR   PANTHER; PTHR21231:SF3; PTHR21231:SF3; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; GTP-binding; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9Y4"
FT   CHAIN           2..310
FT                   /note="GPN-loop GTPase 2"
FT                   /id="PRO_0000247830"
FT   MOTIF           76..78
FT                   /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   BINDING         19..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   BINDING         178..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   SITE            78
FT                   /note="Stabilizes the phosphate intermediate; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9Y4"
SQ   SEQUENCE   310 AA;  34462 MW;  F7241F808DA683CA CRC64;
     MAGAAPTTAF GQAVIGPPGS GKTTYCLGMS EFLRALGRRV AVVNLDPANE GLPYECAVDV
     GELVGLGDVM DALRLGPNGG LLYCMEYLEA NLDWLRAKLD PLRGHYFLFD CPGQVELCTH
     HGALRSIFSQ MAQWDLRLTA VHLVDSHYCT DPAKFISVLC TSLATMLHVE LPHINLLSKM
     DLIEHYGKLA FNLDYYTEVL DLSYLLDHLA SDPFFRHYRQ LNEKLVQLIE DYSLVSFIPL
     NIQDKESIQR VLQAVDKANG YCFGAQEQRS LEAMMSAAMG ADFHFSSTLG IQEKYLAPSN
     QSVEQEAMQL