ID   A0A1Z5TFK5_HORWE        Unreviewed;       991 AA.
AC   A0A1Z5TFK5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=GTP-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTJ68_06009 {ECO:0000313|EMBL:OTA34788.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34788.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA34788.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34788.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC       {ECO:0000256|ARBA:ARBA00007756}.
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:OTA34788.1}.
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DR   EMBL; MUNK01000054; OTA34788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TFK5; -.
DR   STRING; 1157616.A0A1Z5TFK5; -.
DR   VEuPathDB; FungiDB:BTJ68_06009; -.
DR   InParanoid; A0A1Z5TFK5; -.
DR   OrthoDB; 1377857at2759; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   CDD; cd10229; HSPA12_like_NBD; 1.
DR   CDD; cd11385; RagC_like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.30.450.190; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR006762; Gtr1_RagA.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039400; RagC/D.
DR   PANTHER; PTHR14187; ALPHA KINASE/ELONGATION FACTOR 2 KINASE; 1.
DR   PANTHER; PTHR14187:SF79; HSP70 FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G15200); 1.
DR   Pfam; PF04670; Gtr1_RagA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  110444 MW;  895BA9FF80F46069 CRC64;
     MNPQQPLGRP PSYQYANTGT GNLGAPHPGQ GRPTSPLPPP PINTGGGHSY APPHQQQMYQ
     QPAPPSYPMQ QQGYGYGAPQ MGGHPAYQNR LAEVEGSNRS KAQLIVGIDF GTTFSGVAFA
     FATNTEAKED IIVEWPGAGT QTKQKIPTVL YYDQHQQVVG WGPDIAEALA PTGYPKPGVQ
     KVEWFKLQLM LSGNTYIDPI NLPPLPPRKS EIDVAADYLF KLRQAMRNQL QKSLGEVFNR
     EERNIRYFLT VPAIWNDAGK AATRAAAIQA GFLRDENDNR LTLISEPEAA AMFCAKTGLL
     NLKVHDAILI VDCGGGTVDL IAYEVEEESP FTVAECTAGS GDSCGSTALN RNFSNILRAK
     IRKMKLPDGS KTAGKVYAKC IMDFENRIKA DFRNNGQKWA VDVGIEAEFP EAGIEEGYMT
     FTNEEILQCF EPVVNRILEL VRNQIIAIQA QNRMLQNVLV VGGFGASEYL FQQIKLHVPP
     QFQNKVVRPM DSVAAIVKGA VTAGITERVI TSRVARRHYL MATLQPFKEG HHPEQYRVPS
     LDGRDRCKYT RQIFVQKGQR VKIGEPVKVS FFRQVAPGAT LMYEDVLYAC DEDVCPEYTK
     DPRIKEVVTL TSDLSRKNLE KDFERMDTPQ GTFYRVYFDI YLTLDGSEFN AELVCQGEVM
     GRCSARFRSG KSSIQKVVFQ KLSPADTLFI EPTSRIETAS MQSFITFESA ELPASYATAA
     AVPAPDFDHH AIFSNAGAVI WILDVQDEYL SSITSMIQTA VFLAEHYPRV NFEVFIHKID
     GLSEEYKYET FREVRQRVQD ELSDLDHGDR TVSYYQTSIF DHSVFEAMSK VVQRLLPQLP
     AMEALLNKLC SSCRIQKAYL FDTMSKIYVA TDASPTFLRD YEVCSDYVDV IVDIKQIYGW
     HHRHSQEAAD SRPVSESGSS LDDGQGSGGG EIGESIVTYD RSGDTYIYAR EINEHLSLLC
     VIGKGSSADK RVLIDYNVGI LHDALLQVFQ V
//