ID A0A1Y2VFQ1_9PEZI Unreviewed; 1853 AA.
AC A0A1Y2VFQ1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=M434DRAFT_393864 {ECO:0000313|EMBL:OTA95285.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA95285.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA95285.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA95285.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112444; OTA95285.1; -; Genomic_DNA.
DR STRING; 1001938.A0A1Y2VFQ1; -.
DR Proteomes; UP000194361; 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; IPR045838; DEPDC5_CTD.
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; PF19418; DEPDC5_CTD; 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:UP000194361}.
FT DOMAIN 1321..1416
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1853 AA; 206649 MW; 301037CEF7CCDEC6 CRC64;
MSRNTALSPS APRRATQWTS HLRQFSKSSF DRASTDPPVS PDTAANNPTS RESLPSKRIN
ERICSVTINE SVFRDEVLLN LDLFGGAVQP GMLMSIAPLK SDQDRAQGPQ YGTSRQASYH
RGLGAPTPGD DTSKPDSDTS RRYIFVAKDL PKELKARNPS IEVYVSKQIG IAFNMRKGTQ
VILAPVDHLA PAIEASHVEL TFKDMYLSRA DMWRLAVADL ADRTVYKGQV VYFLGAIKAT
VSTVFVDGRK VQSAFFGRNT RPIFRSESAR YVLFIQMARE MWDFDSDGSG EIMFYKVVNG
FLPALFKKWA LLQVKHLVSI VLFARVEYDT GLTTELANSA LHNDYYTGFQ TSGDRRPFKD
FYRVVVSDMS SGEWTRILHQ LKMEFNVFRR DISLHHRDAM GDTMEIPEDS SAMGTSTNKI
KAQSSLAMYG NFLEAINLAS SLYAHDYVDR DLLRTGISIV VISPGPGVFE VEYESLRRTT
EALVGNGIGI DLICIPNIPL HSVPLFRYRN PHFIEASQRL QTRPIRSHES TPKQPTPLAG
SYTTLGESVS PTKAGDSSSR IDSSSSTMHA DEWAFAVPQW LHISYWTGKS EEALSFQGIT
LSASAQSPKD CQDDFTIRCR LYDLQMRSVL ETNEIETTPL QADPAYSSTI GKLGNDRKLL
GGDNRLSTRI GNRRVPETLF EPVYGFLKFI PDKLTKTGDT LLWKQLQSFD ETRARLPAHR
PLPSTNSYRE LEESAGKQLV EDTNLFGTSV GDSKGASLST GLSSSVVSSS KLVLEGSAST
TASRRNSTAQ SKPPPTRPPK FMRQISLGQR GFGIAAPKIA TAELKMENVG RMETTGPGFH
SPSAPRTTPM TPIKSATRPG SSKAASTGNI LQTINQSDLG IDMVQATPSR PIQIRNPAQA
LDPISTLRSG QIPATPVARS ARPDDRDLRY SNALREEDQK KLYTSKLRAG GVPELPSTLS
PTTAMAPWLV VLNPSNPNVN KVDDSILFSR WQHVFPRPSE MRVMKWKSLS CPAAVPLTTE
YFPTQAQFNT EYQRQPYNIS QEMDDEINDQ PKSRLEFLRE LVSARFSHGF QVVIGPSVAK
AFDQKAVRIA DVFSIDTTVG DGTSIFMSVG NTIHQLSCVN GTEVEVNIYV RKPTESLAQM
DRPSLYKPAI RTLLDDTYHS IDVDIMTLKP ERNWNYIDSY LAGHTDEMTE NLRFWRARFV
LIPMYPRTSS APAPKNEDDE EEVRLEGIKR LAQLWQRYRF LSPSERQFQS AGAKKRDPNP
LDIIYKTEDP SVVITAEMEI LPLFENVETT HRKGLVSDKE RFSKTNFNIA ALAEAIQQPV
ELGGVRMQTR RWHFRIHYHC FIGSDMTTWL LDNFEDLESR EEAVELGNSL MVLEDDKPRD
RDFSKDAKKD RDRGIFVHVE RRHPFRDGQY FYQIVSEYAK PHPVSWFNAR RKDVSVPSTP
LSENPPKDSP RPSQAGIPKP MSIHEENSPI SGSTTPTLAT SGGKKPKVVL SKMMKYDVDP
RKKSYRPERI NLHYDRLHNP DNCYHIRIDW MNVTARLIED ALKSWAAIAA QHGLRLVEVP
IAEACRISEV NPFRRPYRIK LALPPPTQRP VTYYDPNSFG PQAQPGKYYY QKALLRRFDY
VLDVEAASNF PSNVDVSYSW GKPDYKYSQY IHRSGMILAE ITDEGDFLVL ANRLCSNRAA
VMQPTQARAE AVPNERVSRL MNTSAYTNYG LAEPTPISSP MLRPVLFASA ASRAPPEPSS
GSGTGGPQGS PSAINSVGEP ESLKDMLEKF CNDANALETF YKETLERGIT GTPMVGAATM
GPDAVPDANI PTLVLGGNNS SNSELGASAG ASPRGPTPNL AGSLLFRRGS IQH
//
