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Database: UniProt
Entry: M3IU90_CANMX
LinkDB: M3IU90_CANMX
Original site: M3IU90_CANMX 
ID   M3IU90_CANMX            Unreviewed;       851 AA.
AC   M3IU90;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=CP-type G domain-containing protein {ECO:0000259|PROSITE:PS51721};
GN   ORFNames=G210_4830 {ECO:0000313|EMBL:EMG50156.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50156.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG50156.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the mitochondrial lipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00003269}.
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:EMG50156.1}.
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DR   EMBL; AOGT01000358; EMG50156.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3IU90; -.
DR   STRING; 1245528.M3IU90; -.
DR   eggNOG; KOG0077; Eukaryota.
DR   eggNOG; KOG1424; Eukaryota.
DR   HOGENOM; CLU_011072_2_0_1; -.
DR   OMA; WIFDWIL; -.
DR   OrthoDB; 130417at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   CDD; cd01857; HSR1_MMR1; 1.
DR   CDD; cd00879; Sar1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR45709:SF2; LARGE SUBUNIT GTPASE 1 HOMOLOG; 1.
DR   PANTHER; PTHR45709; LARGE SUBUNIT GTPASE 1 HOMOLOG-RELATED; 1.
DR   Pfam; PF00025; Arf; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51417; ARF; 1.
DR   PROSITE; PS51721; G_CP; 1.
DR   PROSITE; PS51422; SAR1; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..851
FT                   /note="CP-type G domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004035042"
FT   DOMAIN          390..600
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   REGION          820..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..844
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  96947 MW;  4981DC89FF2E13C6 CRC64;
     MWIFDWILSS LGLWNKHAKL LFLGLDNAGK TTLLHMLKND RLATLQPTLH PTSEELAIGS
     VRFTTFDLGG HQQARRLWKD YFPEVNGIVF LVDAADAERF AESKAELESL FKIEELSQVP
     FVILGNKIDV PTAVGEMELK NALGLYNTTG KDTSILMRNG ACQKQNLSHD YTYLTWSDLR
     QLKVIFYSPL SQRNPYTLVI MEGNKVSLHP EQKKWKAPKG PKPVHHKNKN LIGLGRTIAN
     QRSKENAIQY LPDGEMRFTT DKKEANWVKL RSVTQENALD EFLSTAELAD TDFTADKNQQ
     VKIIKVGNTS IVNSNGLLTT DEMLAMRQKH MMFENKLTIP RRPQWSKNQS KLEIDRQENL
     AFLNWRRELA SLTENNDLLL TPFERNLEVW KQLWRVVERC DLVVQIVDAR NPLFFRSVDL
     EKYVNSLSDP ENNKQKNNLL LVNKADMLTR EQRIAWADYF KLKNINYVFF SAAKANELLE
     KEREELELLK NDPNAVASGS ETIEEEIETN ESIRILKIEE LEKLFMDSAP KFEVDPEFPD
     RKLQIGLVGY PNVGKSSTIN ALVGSKKVSV SSTPGKTKHF QTIHLSPDVL LCDCPGLVFP
     NFAYTNGELV CNGVLPIDQL REHIPPVALV CQRVPKFFLE AVYGIHIPIQ KIEDGGNGEY
     PTARELLNAY ARARGYMTQG FGAADEPRAA RYILKDYVNG KLLYVNPPPK EAGDGEWTLP
     NLQESRVFNK NLYTLQHLPE SRQHQIVAAM QSKHIPVDEF NLEKDVQRLN FSQHVGEGKE
     EKGEAKTLFY GGKQAALESA GDDLDREFFA MNNISGKFAT PFHKKSAEKS STKKHNKKNK
     KQDKKVRVVG Y
//
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