ID C4JUG3_UNCRE Unreviewed; 1564 AA.
AC C4JUG3;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN ORFNames=UREG_04766 {ECO:0000313|EMBL:EEP79924.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP79924.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001874};
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DR EMBL; CH476617; EEP79924.1; -; Genomic_DNA.
DR RefSeq; XP_002584077.1; XM_002584031.1.
DR STRING; 336963.C4JUG3; -.
DR GeneID; 8440103; -.
DR KEGG; ure:UREG_04766; -.
DR VEuPathDB; FungiDB:UREG_04766; -.
DR eggNOG; KOG0466; Eukaryota.
DR eggNOG; KOG0961; Eukaryota.
DR HOGENOM; CLU_245775_0_0_1; -.
DR InParanoid; C4JUG3; -.
DR OMA; MLHAMEG; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000313|EMBL:EEP79924.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EEP79924.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT DOMAIN 1143..1351
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1019..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1034
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 174190 MW; E9160A0ED77B9E46 CRC64;
MVSQQGSKSY FRQLHKFKTD YSASRFTQYE SERTGMRVVV IDQKGPKVYG YFVLATEIHD
DSGSPHTLEH LCFMGSRNYR YKGFLDKLAT RLYSDTNAWT ATDHTAYTLD TAGWEGFSLI
LPIYLEHIVA PTLTDAGCYT EVYHIDGTGH DAGVVYSEMQ GVQNRSSELI DLRSRRLMYP
EEVGFRYETG GMMEQLRVLT AERIRAFHKD MYQPKNLCLV IIGEVDHVDL LSVLDQFENT
ILDAIPIPDA PFKRPWVEST QPPQLEKSVI DTVEFPEEDE SFGEIEIRFL GPNCNDRVQT
AALNVALMYL AGSSAALLEN VLVEKEQVTT AVYYSTDERP RTEIRFTLTS VATENLRDVE
RRFFEVLTDA MRNEIDMKYM RECIERHRRN WKFSAENSAS SFADYVISDF LFGDKNGSRL
LEIATLKEYE ELESWHDNQW RGFIKQYMAD APHVSVLGVP SAKLAAKIKV DEEARIQERK
EKLGEKGLQL LAEKLTKAKA ENDKPIPREI LAKIQVPDTD SIHFIHTTTA KSGTALKDGR
PDNKFQQLID SDDMNSSLFI HFENISSNFV QFSLVISTQG VPVELLPLLS VYTETFFSLP
IDRDGERISF EQVIVDLERD TVGYTMDTSP GNSEMLAITF QVEVEKYQAA IMYLKELTWS
SVFDPERLVA VTTRLFSDVP DAKRSGSSMV DAVRYMIQYA PESLPRARST LVKAKYLKRV
KRLLAKDPRE VIQRMETIRK TLFQPKNMRI LVIGDLSKLK NPVSSWKPYV DGLDMAKPLE
PVVKLHERLS NAGKKPGQLA YIVPMPTLDS SHVNATTKGL NSYDHPKLPA LMVAIAYMNS
VEGPLWVAVR GTGLAYGASF RHSTDTGLVH FNIYRSPNGF KAFEAAKKVV DDHISGAAVL
DPVMSPEGAI STIVAGFANE QATNILSAQD SYIRQVIRNL PADYKETLLK RVRAVTIDQL
KEALRDIILP VFTPDSSTVV VTCAPVLEER IKTGFESLGF KPEVQSLSYF EDDYGLQLDE
EEEEDEENEE DSGLDSDAGS SLQQYPRLPA IMAPMSDYSD DDSQPGSPTL AADQNGADQD
DFDDLEEDLE ELDAKPLKSA LKQPSSAPSA PAEPKPELPE QPDPETLDLS TLTPLSPEII
ARQATINIGT IGHVAHGKST VVKAISGVQT VRFKNEQERN ITIKLGYANA KIYKCDNPEC
PRPGCYTSFK SEKEVDPPCK REGCAGTYRL QRHVSFVDCP GHDILMSTML SGAAVMDAAL
LLIAGNETCP QPQTSEHLAA IEIMKLNHII ILQNKVDLMR EDGALQHYQS ILKFIRGTVA
DGSPIIPISA QLKYNIDAVN EYLCTHIPVP VRNFAASPHM IIIRSFDVNK PGCEIDSLKG
GVAGGSILTG VLKLGDEIEI RPGIVTRDEQ GKVKCRPIFS RVISLLAEQN DLKFAVPGGL
IGVGTKVDPT LCRADRLLGF VLGHRGKLPA IYSELEVNYF LLRRLLGVKS ADGKQAKVAK
LSKNEVLMVN IGSTATGAKV MGVKADAAKL SLTGPACTEI GEKIALSRRI DKHWRLIGWA
NIVA
//
