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Database: UniProt
Entry: A0A135SSF0_9PEZI
LinkDB: A0A135SSF0_9PEZI
Original site: A0A135SSF0_9PEZI 
ID   A0A135SSF0_9PEZI        Unreviewed;       533 AA.
AC   A0A135SSF0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Vacuolar protein sorting-associated protein 4 {ECO:0000313|EMBL:KXH38850.1};
DE   Flags: Fragment;
GN   ORFNames=CNYM01_11339 {ECO:0000313|EMBL:KXH38850.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH38850.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH38850.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH38850.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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:KXH38850.1}.
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DR   EMBL; JEMN01001384; KXH38850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SSF0; -.
DR   Proteomes; UP000070054; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd02678; MIT_VPS4; 1.
DR   CDD; cd19521; RecA-like_VPS4; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   InterPro; IPR045253; VPS4_MIT.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF83; VESICLE-FUSING ATPASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003651}.
FT   DOMAIN          102..180
FT                   /note="MIT"
FT                   /evidence="ECO:0000259|SMART:SM00745"
FT   DOMAIN          263..398
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KXH38850.1"
SQ   SEQUENCE   533 AA;  58369 MW;  0D7CE1E878A98CB7 CRC64;
     ATSQNPRPQV LPQGSSPVQT SNPPPFCARH RRPPRDPTDS SILRRPIPKR LAKDADEHDD
     VHTERAFPAL STSSRNPTSS TPPNRRAPRE TKANPQPTMS GITDFLGRAI STVKQAIDAD
     NAAEYDKAFQ LYTKSLELFV LAVKWEKNPK SKELIRQKTA EYMDRAEKLK TYLNEAESKK
     SGGGGNKPGA VGVNGGGKGK GSADDGDEDN KKLRNALSGA ILQERPNVRW DDVAGLEGAK
     DTLKEAVVLP IKFPSLFQGK RQAWKGILLY GPPGTGKSYL AKAVATEANS TFFSVSSSDL
     VSKWMGESER LVKALFSMAR ENKPSVLFID EIDALCGPRG EGESEASRRI KTELLVQMDG
     VGNDSKGILV LGATNIPWQL DAAIRRRFQR RVHIGLPDVN GRARMFKLAV GDTETHLQAD
     DYRVLAELSE GFSGSDIANV VQQALMGPVR KIIQATHFKP VVHEGQKKLT PCSPGDPQAK
     EMTYHDVDSE ELMAPIIELK DFKQALRDSH PTVSDDDAAK QIEWTNEFGS EGA
//
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