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Database: UniProt
Entry: A0A024G8K9_9STRA
LinkDB: A0A024G8K9_9STRA
Original site: A0A024G8K9_9STRA 
ID   A0A024G8K9_9STRA        Unreviewed;       605 AA.
AC   A0A024G8K9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Guanine nucleotide-binding protein-like 1 {ECO:0000256|ARBA:ARBA00039902};
GN   ORFNames=BN9_036540 {ECO:0000313|EMBL:CCI42870.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42870.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI42870.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42870.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible regulatory or functional link with the
CC       histocompatibility cluster. {ECO:0000256|ARBA:ARBA00037770}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the HscB family.
CC       {ECO:0000256|ARBA:ARBA00010476}.
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:CCI42870.1}.
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DR   EMBL; CAIX01000040; CCI42870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G8K9; -.
DR   STRING; 65357.A0A024G8K9; -.
DR   InParanoid; A0A024G8K9; -.
DR   OrthoDB; 130417at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR004640; HscB.
DR   InterPro; IPR036386; HscB_C_sf.
DR   InterPro; IPR009073; HscB_oligo_C.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00714; hscB; 1.
DR   PANTHER; PTHR45709:SF3; GUANINE NUCLEOTIDE-BINDING PROTEIN-LIKE 1; 1.
DR   PANTHER; PTHR45709; LARGE SUBUNIT GTPASE 1 HOMOLOG-RELATED; 1.
DR   Pfam; PF07743; HSCB_C; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          274..340
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
FT   DOMAIN          526..593
FT                   /note="Co-chaperone HscB C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07743"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..28
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  69619 MW;  FF036CDF3234F6E7 CRC64;
     MSERNRRIPF GNKAKKKQLQ LKREKNRARL HKNSSEEEEC DKVAPISEPI PTTTRGLEKD
     LRSIFELESK SVINARKRDA TRPLVEGAES DFQYSLYATY KLHHLSNQAP ILCKPKLNPK
     NMTPDEWHDV EEQSHNCWIN EIKAIQSSRN DSACINLFER NLNTWRELWR VIEQTQILVH
     LVDSRCPLLH LSDQLIQYLL EMKKSVVVIL TKTDLVSLDR VDSWIQYIRN MYASRLPVMT
     YSVPESKVCN NTFFQVIKDI IANDTSHSSP TWNLGFVGEP NVGKSTLLNT LFEKKLVSSS
     QTPGHTKHLQ SHYYPDVSSA LDGINVKVEK LQVFDCPGIV FPRFNVPPSL QILFGSFPIA
     QVREPYSCIR MIAENCRPTL MDVYKLKSIE EEDEWSPWTI AEAYAEQRGF RSKGGKTDVY
     RAANLILRNT LKGEKVVLSF PPPKEQSHSP RKYHIDLKAI EQTYWKLQKR LHPDLFGSKS
     QQLSATNSAL VNDAYRTLKD PIRRIDMLLK LHGINALDET SNATIDPALL METMEIRENI
     ASASLSNLQA FKTQVGNDIS IILQKLQQTY DVERDLKATQ TLMLRLQYLK KSMIEIEKRE
     EQSHG
//
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