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Database: UniProt
Entry: A0A177D161_9PLEO
LinkDB: A0A177D161_9PLEO
Original site: A0A177D161_9PLEO 
ID   A0A177D161_9PLEO        Unreviewed;      1390 AA.
AC   A0A177D161;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 28.
DE   RecName: Full=VPS9 domain-containing protein {ECO:0000259|PROSITE:PS51205};
GN   ORFNames=CC84DRAFT_1212361 {ECO:0000313|EMBL:OAG12870.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12870.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG12870.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12870.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UPF0507 family.
CC       {ECO:0000256|ARBA:ARBA00007428}.
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DR   EMBL; KV441548; OAG12870.1; -; Genomic_DNA.
DR   RefSeq; XP_018043235.1; XM_018182445.1.
DR   STRING; 1460663.A0A177D161; -.
DR   GeneID; 28765931; -.
DR   InParanoid; A0A177D161; -.
DR   OrthoDB; 1387097at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036871; PX_dom_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; PF02204; VPS9; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF109993; VPS9 domain; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          343..506
FT                   /note="VPS9"
FT                   /evidence="ECO:0000259|PROSITE:PS51205"
FT   REGION          158..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1390 AA;  154513 MW;  829FDABC660A5346 CRC64;
     MPPVLNPFLR AFFRSTLPSQ CSPVQHHVLL VPTTEVLLTS RDRDTNASYA DLSGSEEFLA
     SHVLRVPGGV GPNNHVKDGS TFRESRGKAK QYSTANGRTV IIKDAFVYSN KGFKTLNQAQ
     LLNDVIFFPD TFEPQPWLVY FISRPLIGTY DATPIIPASL PDPSKERAPK HAPAGPSNSG
     PTASMPRKKD VKSFGDLLNH FPMIARQMQP GLDRLFTEFR KELEKPLPPT PSSTSRASSL
     SSRRRGSVSS AESAPLSLHS SISGPNGFIS TLEIDDEEDL MRRSLETAVI AAIDLFQGVD
     KQQLSLLGAT TDLTGPIVER MIEKYITEQL HAFMFPRLQH IRKSDDAELE MRMRQMVDID
     ISQVGIDIGH GRKGKNELSV RLSKAGEIFK KMGVAGSPQE MVEILLAVQK NITMPEASST
     AAKPLLNGQP YSEKNDHLLT INADTLVSLL LIVVIRSPIK NLQARLSYMR HFIFIDDVES
     GEMGYALSTF EAVLSYLVRD SGGLRKASRR NRTLWQATKS GDLATLQGVL EPERSFHEDA
     WADSDEDEEI RESVRPVRFA PSASELLASA EGPTNGDTGS SYRPGRLSRL RHKDEDGPLS
     HIFPFQRAPT PPIPELPDRP NPKKRVSMDT RSMSSSSAVS FRSHTTLGSR GTGLEGDTSI
     EKLSKTQGSE GDSVLMMAVE NRQDKALQYL LSLSEFYSSD FILDDCNNEG TTLLSAAVQG
     GNAKTTDVLL SWILEVRPPE DILRAYLAKQ DSKGRCMAHY LFNQPLLIDR IGHLVPWRLK
     DKNGQTPMFA LCRSYDHDEY RDMIDRALYA ATRAQNDGQP LHLDEHIDNK GNSLLHIVAD
     PQIAIRLLYR CDSDVNAPND KHFTPLMVAS KYGRTELVRV LFQDPRVDLS VKDVRGLTAV
     ELAKDDEVRN RIDDMVLLSN EPGPDGRTTT VVRSFFVEDG SIRLVLKSGA PNSNATITVT
     TCRRSLHDFE TLAKWLAQEH PASWLPVINN LASPFLIPSR PSRSVLRDIQ LRLDAFLKIL
     LKHPTFATHE MVWEFFLVPD IDIAMLAERS SRKAELLVER IREEYIPVYD VREVELFVQH
     ARESVRSLHH ASKSVLRRTN KLRTTSTDLA DAAKLANTAI HTLKFLPEPH LRAVDRYTKT
     LTQSEASPLA GFYYNVHAIA STINAILSAL NRPSTLINSM SATQKAVDRH SLSMRRSDRW
     PLGLLDDARS RMQRDAQEKM ERATEELSGL GKELRYTQQV VAQELASWQE NRVDMGRRAL
     KEFARKMVVT ERARLESMRR AVRELGLGAA NSQADGKGVA VDRVNGTHPE VGLDTAPPER
     RGSIEDVTDE VDGALAANPE QDMVNGDIDA AEDEPLLPPA SPLQPDGETD GAPEASEEGE
     RLLAPRTGAD
//
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