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Database: UniProt
Entry: A0A0G4MHD6_9PEZI
LinkDB: A0A0G4MHD6_9PEZI
Original site: A0A0G4MHD6_9PEZI 
ID   A0A0G4MHD6_9PEZI        Unreviewed;       998 AA.
AC   A0A0G4MHD6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=OBG-type G domain-containing protein {ECO:0000259|PROSITE:PS51710};
GN   ORFNames=BN1708_001078 {ECO:0000313|EMBL:CRK33400.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK33400.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK33400.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK33400.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593}.
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DR   EMBL; CVQH01022527; CRK33400.1; -; Genomic_DNA.
DR   STRING; 100787.A0A0G4MHD6; -.
DR   OrthoDB; 5476718at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd01897; NOG; 1.
DR   Gene3D; 1.20.120.1190; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR041623; NOG1_N.
DR   InterPro; IPR010674; NOG1_Rossman_fold_dom.
DR   InterPro; IPR012973; NOG_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR45759:SF1; GTP-BINDING PROTEIN 4; 1.
DR   PANTHER; PTHR45759; NUCLEOLAR GTP-BINDING PROTEIN 1; 1.
DR   Pfam; PF00996; GDI; 1.
DR   Pfam; PF06858; NOG1; 1.
DR   Pfam; PF17835; NOG1_N; 1.
DR   Pfam; PF08155; NOGCT; 1.
DR   PRINTS; PR00892; RABGDI.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          168..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   REGION          546..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  111698 MW;  8F5566FDDD65C848 CRC64;
     MKTQWKDIPV IPNYSQMTDI ILSSTQRKLP TQIRAGFKIS RIRGFYTRKV KFTQETCSDK
     LGQIIESFPR LNDIHPFHRD LMNTLYDADH LKIALGQIST CKSLIESVGR DYVRLLKYGQ
     SLYQCKQLKR AALGRMATLI KRLKDTFLYL EQVRQHLGRL PSIDPNTRTL VICGFPNVGK
     SSFLESVSRA DVDVQPYAFT TKSLFCGHFD YKYLRFQCID TPGILDHPLE EMSTIEMQSI
     TALAHLRSAV MYFMDLSEQC GYSVEAQINL FASIKPLFSN KLVFLVINKI DITKVEDLDA
     ETQEKLQGLL KSGEVEMLQL SCNTQEGVQD VKNAVCERLI AERVSQKLNA GTTSSGAIGG
     RLADVMSRIH VATPMGGQTL QTFIPEGVKN LKKYDKTDPE RRRLARDVEE EQGGAGVFNV
     DLRADYILAN PEWKYDKIPE IFDGKNVADF IDPDIEAKLA ALEEEEEKLE AEGYYDSDEE
     IDDEEEATVL AQAELIREKQ GQIRNEARMK KRLKNQAIIP RKKVPIPLSK MDDALDQLGV
     DTTDIVSRAR SQSRPRGRSL GRSRAGTEDA DAMDLDATPR ERLRSQSRAR SRSQAAVNRR
     EDGVEDEGNR TKAERMAKLG QKKMNRMARQ GEADRHTTAS LQRHLVAGSY VQQGQGSKAT
     VAKVPSDAAE ALRSPLMGIF EKRRMKSFIE WVGTFDLKNP SSSHKGLDLN TATMKEVYDK
     FSLETGTRDF IGHAMALYTD DDYLTTPGAA PEAIERIRLY GNSVARYGKS PYIYPLYGLG
     ELPQGFARLS AIYGGTYMLN TQIDEILYED GKASGIKATM TGADEMKFET KAKTILGDPS
     YFPNKVKVVG QVLRAICILK HPLSGTNDAD SAQLIIPQSQ VGRKNDIYIA TVSSAHNVCP
     KGYWIAIVST IAETTANHHL ELQPGLERLG KIEEQFMGAP IPIYEPTDDG SKDNVFVSKS
     YDASSHFETT TDDVQNIYRR AAGEALVVEG LRXNVADE
//
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