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Database: UniProt
Entry: A0A068RM00_9FUNG
LinkDB: A0A068RM00_9FUNG
Original site: A0A068RM00_9FUNG 
ID   A0A068RM00_9FUNG        Unreviewed;      1121 AA.
AC   A0A068RM00;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 36.
DE   SubName: Full=Gtp binding protein {ECO:0000313|EMBL:CDH50760.1};
GN   ORFNames=LCOR_02458.1 {ECO:0000313|EMBL:CDH50760.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH50760.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH50760.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
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:CDH50760.1}.
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DR   EMBL; CBTN010000007; CDH50760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RM00; -.
DR   STRING; 1263082.A0A068RM00; -.
DR   VEuPathDB; FungiDB:LCOR_02458.1; -.
DR   OrthoDB; 5478101at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd01882; BMS1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR012948; AARP2CN.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR039761; Bms1/Tsr1.
DR   InterPro; IPR037875; Bms1_N.
DR   InterPro; IPR007034; BMS1_TSR1_C.
DR   InterPro; IPR030387; G_Bms1/Tsr1_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12858; RIBOSOME BIOGENESIS PROTEIN; 1.
DR   PANTHER; PTHR12858:SF2; RIBOSOME BIOGENESIS PROTEIN BMS1 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08142; AARP2CN; 1.
DR   Pfam; PF04950; RIBIOP_C; 1.
DR   SMART; SM00785; AARP2CN; 1.
DR   SMART; SM01362; DUF663; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51714; G_BMS1; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT   DOMAIN          39..203
FT                   /note="Bms1-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51714"
FT   REGION          323..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1067..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..679
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  128783 MW;  CB4784E4540F61F9 CRC64;
     MAFTFASAGR AERSARRNFD LGEKKLHVPL VDRSPIEAPP VVVAVVGPPG CGKSTLIKSL
     VKRYTKHNLA EIKGPITVVS GKKRRLTFIE CNNDINSMID VAKVVDLVLL MIDASFGFEM
     ETFEFLNILQ AHGFPKVMGV LTHLDKFRNN KKLRATKKRL KHRFWTEIYQ GAKLFYLSGV
     INGRYPNQEV QNLSRFISVM KFRPLIWRNT HPYVVADRVE DLTDPELIHT KPNCDRTVTL
     YGYLRGTNLK PNMRIHIPGA GDHTLADVSV LPDPCALPDK ERKRLDEKHK LIYAPMSDVG
     GVMYDKDAVY INVPGHFTKK SALAPAERQE GAEEEHDDTP AGPGEKMVMD LQDAQDTLAA
     RLADSELRIF SGSAPMRSGD VPSDQEDNEG ITESLEQDDT GRTRRRAVFG DEDEDEDMDD
     EDDDEDEDSD QEMLDSDEEM DDDDDAEVPT RGRALTKFDT RNIPRKGDKE DKEERDNGQD
     VQFADSDSDL GFDDEDDQED MVNIDGRQKN EDDDDDELAG ELRWKANLKE KASAMFNATR
     RVNLMSLIYD KTDISPEDIA SGNYNQDDQE NDDNDDEDEE FFTLKREAAD EASETVDTSR
     EQIKMDDLEI WGDDEHLDTI RYRFITGQKT NGEGEEGEEN EEGEEEEEEE EVYGDFEDLE
     DENASGKEDA DENDQEEDSV EAERERIAKR KEELKRKFEE EYEEDEEPQM DFYEQRKAEI
     DRQLKMNVAE FEDDDPHTRA LVEGHRPGTY VRLLIKDMPC EFIQHFDPTY PVLVGGLLTS
     EDQFGIVQVR IKRHRWHRKI LKTNDPLIFS MGWRRFQSIP IYSLNDGTRN RMLKYTPEHM
     HCLATFYGPV HTPNTGFCAV NSVSDNKSAS FRISATGVVV DISKTAEIVK KLKLTGVPAK
     IFKNTAFIKD MFTSALEVAK FEGATIRTVS GIRGQIKKDF ADKVLMSDIV FLRAWYPVKP
     RKYYNPVTSL LLSSKTEWRG MRLTGEVRRE LSMHAPQNID SVYKPIERKT RRFNTLKIPK
     ALQAELPFSS KPKQLKAQRK KTYAAKRAVL LEPEEKKVYT MMQQLNSLRK DKERKRKAKD
     MERRAENIKK KAKLEAEQLE KDKARRKEYF RKEQRNSKSS A
//
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