ID A0A183LKY1_9TREM Unreviewed; 361 AA.
AC A0A183LKY1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=GPN-loop GTPase {ECO:0000256|RuleBase:RU365059};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU365059};
GN ORFNames=SMRZ_LOCUS4456 {ECO:0000313|EMBL:VDO61766.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000445701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000445701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO61766.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO61766.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAI01001421; VDO61766.1; -; Genomic_DNA.
DR STRING; 48269.A0A183LKY1; -.
DR WBParaSite; SMRZ_0000445701-mRNA-1; SMRZ_0000445701-mRNA-1; SMRZ_0000445701.
DR Proteomes; UP000277204; 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 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 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 PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000277204}.
FT REGION 279..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 40382 MW; 4B111C450E1D6085 CRC64;
MNQLEQDLRT KPICLIVLGM AGSGKTTFVK KLTEYLTVSS NSSYTINLDP AVYHIPYNPN
IEVMKQYGYG PNGAIMTSLN FFASQFHKVV DIVNSNSGKV SYVIIDTPGQ IEVFTWSASG
TIITELLGNS FPTLIIYVMD TPRSHNPITF MSNMLYACSV LYKMRLPFIL VLNKTDIIDC
DFAIQWMRDF ETFQDALAGH QSTDGPSEME GDNPCPGTSP YMNSLVHSMS LVLDEFYSTL
RCCGISSITG EGMTKFVEEI DEAKEEYFKI NLPSLYAKQE KNKQDSSDKS SKSHSSKHGS
MLLDLAGNDD EAENDPLPDV DGIEIRPHSD SDDNDDDDEF LESKDLTSIQ SRFQLTNQNF
K
//
