ID A0A409Y8W4_9AGAR Unreviewed; 1511 AA.
AC A0A409Y8W4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Nucleolar GTP-binding protein 2 {ECO:0000256|ARBA:ARBA00022127, ECO:0000256|RuleBase:RU364023};
GN ORFNames=CVT24_005306 {ECO:0000313|EMBL:PPQ99516.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ99516.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPQ99516.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPQ99516.1,
RC ECO:0000313|Proteomes:UP000284842};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000767};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
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 -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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:PPQ99516.1}.
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DR EMBL; NHTK01001355; PPQ99516.1; -; Genomic_DNA.
DR STRING; 181874.A0A409Y8W4; -.
DR InParanoid; A0A409Y8W4; -.
DR OrthoDB; 2879109at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000284842; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03313; enolase; 2.
DR CDD; cd01858; NGP_1; 1.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 2.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00318; Enolase; 2.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
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 NCBIfam; TIGR01060; eno; 2.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR Pfam; PF00113; Enolase_C; 2.
DR Pfam; PF03952; Enolase_N; 2.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF08153; NGP1NT; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 2.
DR SFLD; SFLDG00178; enolase; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SMART; SM01192; Enolase_C; 2.
DR SMART; SM01193; Enolase_N; 2.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 2.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00164; ENOLASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW GTP-binding {ECO:0000256|RuleBase:RU364023};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364023};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364023};
KW Reference proteome {ECO:0000313|Proteomes:UP000284842}.
FT DOMAIN 219..380
FT /note="CP-type G"
FT /evidence="ECO:0000259|PROSITE:PS51721"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 164588 MW; 5E7CDD3E227E4299 CRC64;
MAPTKKGASP SKSRSSTSSS KISLKKVKGE NFYRNAKQVA RLKMLNGGKA VRDKDGKIIQ
AAAFQKGEDE TKPGRVQPDR RWFGNTRVIS QTALDHFRTS LSEKKDDPYS VLLRRNKLPM
ALLDDAANPN LRKRAHIVET EPFSETFGPK AQRKKPKIDA GTFEELGQLS AAAADEADAA
ATKSGQDIIE PLASTIVDAP THADYNEPIY AKGTSRRIYG ELYKVIDSSD VILHILDARD
PFGTMCESVL EFIKKEKSHK QVVLVINKCD LVPNWVTARY IQHLTPRYPT IAFHASPNHS
FGKGSLIQLL RQFSQLHSDK KQISVGFVGY PNVGKSSVIN TLKSSKVCTV APVPGETKVW
QYITLTKRIY LIDCPGIVPA SARDSQASIV LKGVVRVEAL PTPSEHIPAL MERVKPIYLS
RTYGVPLPNQ DDATQSWEPE DFLDKLARMK GRLLKHGEPD LDAVAKIVLS DWVRGRIPFF
VPPPERSAEL NEAEEKKRKR DLKGKSKAAA QDETEVPGVK QNLKSMMQKN TFLAEDVQRL
DEEFEQPVES GGEEGEESDE EANEVSEGED EDDLKWNDVF EGIDANPVAV SETEEKSAKD
DEETEKAKEQ RMTTNKISLN SFNTTYLSST MSITKVHARQ IFDSRGNPTV EVDLYTAKGR
FRAAVPSGAS TGIHEAVELR DGDKSAYVGK GVTKAVANVN DIIAPALIKS GLSVLNQKDI
DDFLIKLDGT PNKGELGANA ILGVSIAVSE AGAAEKGVPL YQHLAELAGV KPPYVLPTPA
FNVINGGSHA GNKLAFQEFM LLPTGATSFT EAMKIGTETY HTLKKVISAK YGIDAVNVGD
EGGFAPNVSG AEESLELLSD AIKKAGYEGK IKIALDVASS EFYKDGKYDL DFKNPNSDPS
KWITGTELAD LYLGYIEKYP IVSIEDPFDQ DDWEAWTHFT AKSGIQIVGD DLTVTNPLRI
KTAIEKKACN GLLLKVNQIG TISESIQAAQ LAQSDGWGVM ISHRSGETEN TIIADLAVAL
GVGEIKTGAP ARSERVAKYN ALLRIECDVG RNLAAVVQPM QVTRVFPLAL LPQLFSRSKR
SHKPKCNACI PTRHYRASVP SGASTGVHEA VELRDNDKSY GGMGVLKAVA NINNIIKISL
IKSGLNVTQQ EEIDDLMIQL DGTDNKSKLG ANAIVGVSMA VAVAAAAELG IPLYQRLAEL
AGTKPPYILP CPAFNVINGG KHAGNMLAMQ EFMIMPIGAS SFNEAMEMGT ETYHELKKVI
NKKYGLDATN VGDEGGFAPN VSTPQEALDL LVTAINQAGY EGLIKIGIDA AASEFYSDGK
YNLDFKNPKM NPDNRLTGSQ LSDLYLSLLK KYPIIMIEDP FDQDDWDSWT HFRRLANTQI
VADDLTVTNT TRIKTAIQKK CANALLLKAC LLNQIGTVSE SIAAAKLAKA NGWAVMVSHR
SGETDSSFIA DLVVGLGVGE IKSGAPARGE RVAKYNALLR IEEELMSTEQ KPVFARANGF
SRGNAPPSLK N
//
