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Database: UniProt
Entry: A1CHK6_ASPCL
LinkDB: A1CHK6_ASPCL
Original site: A1CHK6_ASPCL 
ID   A1CHK6_ASPCL            Unreviewed;       560 AA.
AC   A1CHK6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Nucleolar GTP-binding protein 2 {ECO:0000256|ARBA:ARBA00022127, ECO:0000256|RuleBase:RU364023};
GN   ORFNames=ACLA_048310 {ECO:0000313|EMBL:EAW10361.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10361.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10361.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the
CC       nucleolus and is required for their nuclear export and maturation.
CC       {ECO:0000256|ARBA:ARBA00003892, ECO:0000256|RuleBase:RU364023}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364023}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2
CC       subfamily. {ECO:0000256|RuleBase:RU364023}.
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DR   EMBL; DS027054; EAW10361.1; -; Genomic_DNA.
DR   RefSeq; XP_001271787.1; XM_001271786.1.
DR   AlphaFoldDB; A1CHK6; -.
DR   STRING; 344612.A1CHK6; -.
DR   EnsemblFungi; EAW10361; EAW10361; ACLA_048310.
DR   GeneID; 4704173; -.
DR   KEGG; act:ACLA_048310; -.
DR   VEuPathDB; FungiDB:ACLA_048310; -.
DR   eggNOG; KOG2423; Eukaryota.
DR   HOGENOM; CLU_011106_4_0_1; -.
DR   OMA; RTQGFNH; -.
DR   OrthoDB; 2879109at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   CDD; cd01858; NGP_1; 1.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR024929; GNL2_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR012971; NOG2_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11089; GTP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11089:SF9; NUCLEOLAR GTP-BINDING PROTEIN 2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF08153; NGP1NT; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU364023};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364023};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN          224..385
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51721"
FT   REGION          477..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..560
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  62196 MW;  8C9C3982E8FD4BAB CRC64;
     MGTGKKEANR KVRQGKVGDG MANVKVKGEN FYRDAKKVRT LNRLKDGKPR RDAEGNITVA
     ASYQSRELPT ARIEPNRKWF GNTRVISQDA LTSFRDAVAE RASDPYSVLL KTNKLPMSLI
     KENTTVNGLK QHEAKMAIET SPYGDTFGPK AQRKRVKLGV ASLEDLASET VKMHDAFVEK
     TDQATHEDGT LIVSADVSNE DDTLSTATTA RESVFSKGQS KRIWNELYKV IDSSDVVIHV
     LDARDPEGTR CRSVEKYIRE EAPHKHLIFV LNKCDLVPTN VAASWVRHLS KDYPTLAFHA
     SINNSFGKGS LIQLLRQFSS LHSDRKQISV GLIGYPNTGK SSIINTLRNK KVCTVAPIPG
     ETKVWQYVTL MKRIYLIDCP GVVPPNQNDT ETDILLRGVC RVENVHNPEQ YIPAVLSKVQ
     PKHLERTYGI KGVEGAIEFL SILARKGGRL LRGGEPDLDG VAKMVINDFL RGKIPWFTIP
     PKSTGDGDEK IEGREGRLGE MGRKRKIDET TSEPSDVKQS TSGKEDNETE NGEFEGFGES
     DDDNDSIANL EVSDEESGEE
//
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