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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//