ID S9VVV2_SCHCR Unreviewed; 323 AA.
AC S9VVV2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000256|RuleBase:RU365059};
GN ORFNames=SPOG_01075 {ECO:0000313|EMBL:EPY50314.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50314.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50314.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE546993; EPY50314.1; -; Genomic_DNA.
DR RefSeq; XP_013024800.1; XM_013169346.1.
DR AlphaFoldDB; S9VVV2; -.
DR STRING; 653667.S9VVV2; -.
DR EnsemblFungi; EPY50314; EPY50314; SPOG_01075.
DR GeneID; 25035406; -.
DR eggNOG; KOG1533; Eukaryota.
DR HOGENOM; CLU_037460_0_2_1; -.
DR OMA; ATHNYFL; -.
DR OrthoDB; 168004at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006606; P:protein import into nucleus; IEA:EnsemblFungi.
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:UP000015464}.
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 36667 MW; 3903A47A304D6B3D CRC64;
MPFGQVVVGP PGSGKSTYCY GMHQFLSAIG RQCIIVNLDP ANDFMRYPCT IDIRKVIDIE
TIQNTYDLGP NGALIFAMET IEYHVDWLCE ELESHKDAYV ILDCPGQVEL FTDHDSLQKI
ISTLSKRIDF RPVVVQLVDS FCCVDPAAYI SALLVCLKGM LQLDLPHINV LSKADLLSTY
GTLPMSLDFY SNVQDLSYLT PLLDRDPRLL RYSELNKTMC ELIEEFGLVS FEVLAVENKA
SMLHLLQKID QAGGYAFGST EIGGDIIWAN AVRQGGDPLQ DVSPQERWID RKEEYDRYER
EMEEKYMSEN KKGEAEEEEE ELM
//
