ID A0A165TFT1_9AGAM Unreviewed; 1541 AA.
AC A0A165TFT1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Vacuolar membrane-associated protein IML1 {ECO:0000256|ARBA:ARBA00018529};
DE AltName: Full=Vacuolar membrane-associated protein iml1 {ECO:0000256|ARBA:ARBA00021881};
GN ORFNames=NEOLEDRAFT_1062935 {ECO:0000313|EMBL:KZT26603.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT26603.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT26603.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT26603.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00004148};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004148}.
CC -!- SIMILARITY: Belongs to the IML1 family.
CC {ECO:0000256|ARBA:ARBA00005643}.
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DR EMBL; KV425566; KZT26603.1; -; Genomic_DNA.
DR STRING; 1314782.A0A165TFT1; -.
DR InParanoid; A0A165TFT1; -.
DR OrthoDB; 946033at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04449; DEP_DEPDC5-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027244; IML1.
DR InterPro; IPR048255; IML1_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13179; DEP DOMAIN CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR13179:SF8; GATOR COMPLEX PROTEIN DEPDC5; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF12257; IML1; 1.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076761}.
FT DOMAIN 1174..1249
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1541 AA; 174708 MW; 63784EF9D4BF9CF7 CRC64;
MSSSRAESQH PQYTRRRSNT ATSLFKGPVT PLKVGDKKTF TIWVHDPKDS PNVLFNHSLW
PGIAEGDMLS VRSPGAEDSA GFFFVASKEE GNVKPQLQIS IPRFMADTFG LRNNGEIVLT
KVEKEKCSAD HVEFIFQDQY LGRNDMWRLG KQLVDQCVYV EQEVSFIGAP AAKIQGIFID
GKKVSAAYVT SATKAIYRSL TARTTIFIQV CKELWEFAGD GERYTEKIIH SFLPALFNKW
REAGTNHIVT IVLISRVYYD TSETEYAAGP LRRDDDGKWY KDFYKVITDL EVIYDWKPTL
LILKDSFVAF QRDILLTHHY HRALVGFPSQ SSEDPLDQVR LVGRLSCAHD GPILEAINLG
LNPTETHYID RSLSQTGAAT ILITPGTGYY RVSKQLLRLT TVRMLDQGFG LDLVSLAKPP
LHQSPIFSFQ SIEPEPRFER EGRLGSRIMD PLWDGDDEQE ESPGRERTTF WWDPFWMSVS
FWDKQMDLPF REDRFIARAK MYEIEMLGLL DHDVLSSIEV PYMPEQRTEA ATPSSEIGPD
NRLTKREADL FDQNVFSFHR EPKPTTTGRN SLASSASGTI VAPSSLRSSI VSYRSSMVSQ
VTLSSPNKIH PIEESPLRAT RDLPVEQPSE SERPLSMISF RGLSSSPSQS SILSNRSTTS
TSTMSSVNPD GRPRRPGSAR SVLSARLSAP SWLFNPFRSG PSHPQTSPIS ASGISSTHNG
TPTLTALDPT STTPTAATPI SRPPRPVTIR NPPTRRLQAN RTLEEDGIGP QRKHTSPINT
PPARDDTSFG ARRSTALSLS MPPISSSPNF RTNPSRPRSS VAPSQATLAR RWEHMFAHPL
YKHDIKWKSM TTPGCLPLTT EYFPSGSDLE ALYDVHEYGI YIDPTEIRSF LVKSPNMSGS
PDQERRAWAL MIMRVMAAVR LAQGFQFILQ PKQVYGENDR NPLRRTQSFM TDEEMVPKFG
GASQVLESPD DPVYISMSNE IHRISYNREG ETVQIRRYVR RMPSLRPFQY QCLIWPKLGV
GYTELKTSFI SHGLENYLWN RLDMVVAGVE PQFNESLRYW RTRFVVIPTA ESPSATIGPA
GEKLNEEEIR LLGMDKLAEL FTRLRWRPLE ERTNPVIPVR FLPTDLGPTT CLFDEHLMAQ
LDEIHAKGPL KKKVKSDKDI ANMSLANIAR AMREDDGVPI KDRRWHTKRY TSVFTGAEFV
SWLVREFRDV STREQGVEVG QKLLDQGLFE HSRGMHGFLD GHYFYQLKGE FAVHTTPKTG
GWFRSSRHVS NAEDNMPRSG YYPSSSAKAS SPRKPKRQLI LSQSMAIDID PVKRSDQAEC
VVLHHDIIHN PATCFHFELH WMGTTARCIE DTLRQWSRTI ERYGLKLVEA YVGQIADIRD
RNAFQSCFPI RLAIPPPVVM DLEKRVPEGT QTSYYFEYAL LKRFGFILDI EAAHLYPEQV
DVNYSYRRAP FSYSQFIHRS GVAFVQVLPN GNGFLFLTNR LLAPGRMGAL KSKEQRPAIA
AEELRVKLHA FCDDGEQLMK FYDEELIQLR DAPEEPPPLN I
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