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Entry: A0AAD7JEJ9_9AGAR
LinkDB: A0AAD7JEJ9_9AGAR
Original site: A0AAD7JEJ9_9AGAR 
ID   A0AAD7JEJ9_9AGAR        Unreviewed;       888 AA.
AC   A0AAD7JEJ9;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=Vacuolar transporter chaperone complex subunit 4 {ECO:0000256|ARBA:ARBA00067464};
DE            EC=2.7.4.1 {ECO:0000256|ARBA:ARBA00012960};
DE   AltName: Full=Polyphosphate kinase {ECO:0000256|ARBA:ARBA00080494};
DE   AltName: Full=SPX-dependent polyphosphate polymerase VTC subunit 4 {ECO:0000256|ARBA:ARBA00075894};
DE   AltName: Full=Vacuolar membrane polyphosphate polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00081313};
DE   Flags: Fragment;
GN   ORFNames=DFH07DRAFT_1020258 {ECO:0000313|EMBL:KAJ7762011.1};
OS   Mycena maculata.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Mycenaceae; Mycena.
OX   NCBI_TaxID=230809 {ECO:0000313|EMBL:KAJ7762011.1, ECO:0000313|Proteomes:UP001215280};
RN   [1] {ECO:0000313|EMBL:KAJ7762011.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBHHK188m {ECO:0000313|EMBL:KAJ7762011.1};
RG   Lawrence Berkeley National Laboratory;
RA   Harder C.B., Miyauchi S., Viragh M., Kuo A., Thoen E., Andreopoulos B.,
RA   Lu D., Skrede I., Drula E., Henrissat B., Morin E., Kohler A., Barry K.,
RA   LaButti K., Morin E., Salamov A., Lipzen A., Mereny Z., Hegedus B.,
RA   Baldrian P., Stursova M., Weitz H., Taylor A., Grigoriev I.V., Nagy L.G.,
RA   Martin F., Kauserud H.;
RT   "Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated
RT   elements and novel gene families across ecological guilds.";
RL   Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC         Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00050204};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19574;
CC         Evidence={ECO:0000256|ARBA:ARBA00050204};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00004128};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
CC   -!- SIMILARITY: Belongs to the VTC4 family.
CC       {ECO:0000256|ARBA:ARBA00061390}.
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:KAJ7762011.1}.
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DR   EMBL; JARJLG010000044; KAJ7762011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD7JEJ9; -.
DR   Proteomes; UP001215280; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:TreeGrafter.
DR   GO; GO:0033254; C:vacuolar transporter chaperone complex; IEA:TreeGrafter.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd07751; PolyPPase_VTC4_like; 1.
DR   CDD; cd14480; SPX_VTC2_like; 1.
DR   FunFam; 3.20.100.30:FF:000001; Vacuolar transporter chaperone 4; 1.
DR   Gene3D; 3.20.100.30; VTC, catalytic tunnel domain; 1.
DR   InterPro; IPR003807; DUF202.
DR   InterPro; IPR004331; SPX_dom.
DR   InterPro; IPR051572; VTC_Complex_Subunit.
DR   InterPro; IPR018966; VTC_domain.
DR   InterPro; IPR042267; VTC_sf.
DR   PANTHER; PTHR46140; VACUOLAR TRANSPORTER CHAPERONE 1-RELATED; 1.
DR   PANTHER; PTHR46140:SF1; VACUOLAR TRANSPORTER CHAPERONE COMPLEX SUBUNIT 4-RELATED; 1.
DR   Pfam; PF02656; DUF202; 1.
DR   Pfam; PF03105; SPX; 1.
DR   Pfam; PF09359; VTC; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP001215280};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        793..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        825..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        865..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..204
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   REGION          95..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..140
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..672
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..751
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAJ7762011.1"
SQ   SEQUENCE   888 AA;  100432 MW;  716B338AF24CF97D CRC64;
     MKFGRKISTD LYNEWRPFYL DYNQLKRELK NRTTGRGWSV ADEKEFTVLL EKELDKIHDF
     QKAKVRSTGS VRTKELSQRI RDAEKDVKRL VAEDAEYGPA SPRHRHRPQS SADPETQLRD
     DSYLDGGSDD DSDTDSDEDI SSMGAESFDA LEARFHGLEE EVANLVADVH DLALYTKLNI
     TGFMKILKKH DKQTNLPLKP TFVQDYLEKR PFYKYNWDAL IVKLSKLYDL VRTRGHPVQG
     DSSAGGSQSA FVRQTTKYWV HPDNLLPLKL AILRNLPVLV FNPDKEFDAK DAAITSIYFD
     NEDLELYLGR LEKTEGAEAI RLRWYGDTDV KTVFVERKTH REDWTGEKSV KARFPIKEHL
     VNAFLRGEYT VDAEFQQLVK KGKKTQQEVD SMIQLANEVQ YAVLTRGLKP VMRSFYNRTA
     FQLPGDARVR ISLDTELTLV REDNWDGRTR AGDNWRRTDI GIDFPFEQLP ADDKELFKYG
     VLEVKLQTQF GQEPPKWVMD LVQSHLVEAV PKFSKFIHGC ATLLPNRVDL VPFWLPQMDT
     DILKPDTGYL TIIERPANAV STAGSSTKAS SEHPTSPTTG MHSPADDEDA AYHEPVSEGE
     EDDDRDLAPA KDEDKWTGLS GQEVAEAIAY REHMLKARSV TDGSPSSSKR NGVQAGPRHQ
     AEDSDADDED EAAVAAGMAA GKGKGIPIMK PRTLSIDPLA PSSAFDETLR DRLKREKEVR
     RGVKHHAEVE EEEEEETRPA TDPDEDEDVD DPLTSRPGDE RHLSREFRAP AGKRISVPVR
     IEPKVYFAAE RTFLKWLNNA VFIGTIATAL LNFTAPEDSR GLMSAALFTL AALLAIAYSA
     TIFVYRAHQL RAHRADGLYY DKYGPTLLCF VLFLALATNI GLRVSQML
//
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