ID A0A098VLP1_9MICR Unreviewed; 380 AA.
AC A0A098VLP1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=DI09_96p20 {ECO:0000313|EMBL:KGG49988.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG49988.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG49988.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG49988.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG49988.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small GTPase required for proper nuclear import of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000256|RuleBase:RU365059}.
CC -!- SUBUNIT: Binds to RNA polymerase II. {ECO:0000256|RuleBase:RU365059}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365059}.
CC Nucleus {ECO:0000256|RuleBase:RU365059}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290, ECO:0000256|RuleBase:RU365059}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGG49988.1}.
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DR EMBL; JMKJ01000608; KGG49988.1; -; Genomic_DNA.
DR RefSeq; XP_013236424.1; XM_013380970.1.
DR AlphaFoldDB; A0A098VLP1; -.
DR GeneID; 25261120; -.
DR VEuPathDB; MicrosporidiaDB:DI09_96p20; -.
DR HOGENOM; CLU_037460_1_0_1; -.
DR OrthoDB; 5475185at2759; -.
DR Proteomes; UP000029725; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd17870; GPN1; 1.
DR CDD; cd20908; SUF4-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21231:SF8; GPN-LOOP GTPASE 1; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365059};
KW GTP-binding {ECO:0000256|RuleBase:RU365059};
KW Hydrolase {ECO:0000256|RuleBase:RU365059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365059};
KW Reference proteome {ECO:0000313|Proteomes:UP000029725}.
FT DOMAIN 322..343
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT DOMAIN 346..367
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
SQ SEQUENCE 380 AA; 43037 MW; 6DB959AA7A334240 CRC64;
MDPTVLIVVG MAGSGKTTFT QRLYSHASYI QKRTPFVINL DPAVLEVPFP CDVDIRDTLE
YKDVMESARF DLVLEQLASL STASTQVEKN NPIKGDVAIE EHKAVDGGDA IEKNHFEDDG
SGYENPRHVS LAIVDTPGQI EVFTWSASGT IITESIAANH PTVLVYVVDT PRCVSNPATF
MSNMLYACSI LYKTRLPLLV VLNKTDEQSD APIREWMLDY EAFQDALRHP SNVERSSDSF
MNSMLHSMSL VLEEFYSTLN VIGLSSYSGD GFDGFMDAVD RAKEEYFSGY RSILDARKAE
QQLINRMSKK RKIEQALKRP WCWFCERDFD DEKVLILHQK AKHFKCPTCH RKLNTAQGMF
VHMAQVHKET ITKFGLKSFF
//
