ID C6HHY9_AJECH Unreviewed; 1456 AA.
AC C6HHY9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 08-NOV-2023, entry version 63.
DE RecName: Full=VPS9 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCDG_06139 {ECO:0000313|EMBL:EER39917.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER39917.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UPF0507 family.
CC {ECO:0000256|ARBA:ARBA00007428}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000256|ARBA:ARBA00006194}.
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DR EMBL; GG692428; EER39917.1; -; Genomic_DNA.
DR STRING; 544712.C6HHY9; -.
DR VEuPathDB; FungiDB:HCDG_06139; -.
DR eggNOG; ENOG502R3ZQ; Eukaryota.
DR HOGENOM; CLU_002294_0_0_1; -.
DR OMA; HFPMIAR; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 3.30.420.80; Ribosomal protein S11; 1.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR001971; Ribosomal_uS11.
DR InterPro; IPR036967; Ribosomal_uS11_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR24170; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27; 1.
DR PANTHER; PTHR24170:SF1; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G09870)-RELATED; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF53137; Translational machinery components; 1.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 497..658
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT DOMAIN 1068..1200
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 161949 MW; FEBEE5E5E993525C CRC64;
MSTGGPSALS KLSASTRVTR NANNDSASMT FRLNQVVQSG YAIQDPPHHL HVYSHKHNTH
ITLTRPNREP LLSMSCGNIG FRKAQRSKFD AAHQLASFMM GKIQEEGHLL TMKRLEVVLR
GFGPGREAFT KVLLGSEGKN IRNMVCRVTD ATRLKFGGCR SKRNIVDLGA DHVSLFESSV
LLVPVTESLI NGRDRDSNLA YADIVSSEEF LGSHILRVPS PIGSPASKDG PSVRDTRGKA
RQITTVNGRT VVVKETTVFS NKGFKALNQA QLLSDALYYT SNNESQPWLI YYISTPLIGT
FQVVRITPAI TPGLSPKPIE PLKTENRNEN HMSHFSKKEI TSFADLLANF PMIARQMQPG
LDRVFREFGK ELGKPLPPPP SILSPVMSDS EAHVNETEET GSWRSRSPGK GSYINQESLP
FNSSEYFEDD EDLMRRTLET AVTSAIDLFR LVDKQQLSLL GATTDLTGPL VERLIEKHVA
QQVHDSLLFP RLCGYRQAED AELDARIHQM ENIDISQVGI VIEGGRQGKQ ELLRRLGRGV
DEFRKIADAK CPQDMLEILL ATIKLVTVME KSDVRNGEDS YSHSEKQSSV LAINADVLVS
LLLVVIIRSQ VRHLQARLLY MQQYIYTDDV ESGELGYALS TFEAVLTYLS KDSGALRRAS
ARNKRLWTAT KKGRVSDIKA ILDPDSSQDT LTGHNFDEDE CSSFSKDEES GTTSDHADQV
VYVNGSTSNP LNQVSPLSPD TPSLAHVFPF MNWSRVSSSK VEAPPRKKVS MDMRSLSESS
TVSYVSRTTV GSTPSALEGD TSIENLTKTQ DPAGDSVPMM AVEARQPQSL QYLLSRQDYY
PLDSILEDTN SDGTTLLSAA VQLAHTELVD IILDFISQAR DSQLLTSYYA KADQRGRTLA
HYLFSVPTLM SRLECALPWR QRDKNGQTPL FALCRSYDHP DYNPMVHEAL TIAQKAQGDG
KPLRLEDHVD GKGNTLLHVV SDPQIVVRIL KECDCDPNAT NDKRFTPLMM ASKYGRVDLV
RIFFGDPRVD VNVREMRGLT AVELAKDDEV RNRIDDLILF SNASSAPVDP SGRITTVVRS
LFVEDASVRF IIKSGAPNPE RSLQKSSSRG IVTYTITTCR RSIKDFENLI KFLKVEHPAS
YIPELPPFRT PFQIPSRPSR AILHEVQARL DLFLQILLAH PTFATHEMIW EFFLVPEMQT
EMIEDRSRRK AEALAETIED DYEPMTQAEI RDVEQIVSHA QDAVRALSAA TRSLLRRGHI
LQHAYSDLAD SIILCAYALS SLQPPSNSLP TSYVETFVRY AACISTPSID SSPLVQFLTA
LTSSQSTTTA MLNALSRPGK LISNLNAEIR GLTRAHSSLA SSSLPLKFNF PGLEESRQKS
VRDLEQKISA STAEAEHLEK EIAWNKDVVV GELAGWTAWR EKVGKNAIRA FVTTTLVREK
ERGRALERCL RSVKGG
//
