ID A0A1W5CT28_9LECA Unreviewed; 1831 AA.
AC A0A1W5CT28;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Vacuolar membrane-associated protein IML1 {ECO:0000256|ARBA:ARBA00018529};
DE AltName: Full=Vacuolar membrane-associated protein iml1 {ECO:0000256|ARBA:ARBA00021881};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM34016.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWEW01000197; SLM34016.1; -; Genomic_DNA.
DR OrthoDB; 946033at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 DNA-binding {ECO:0000313|EMBL:SLM34016.1}.
FT DOMAIN 1341..1416
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1800..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1831 AA; 205270 MW; 8EBEC28C7EDD1439 CRC64;
MTNDPQAEKD IKDISGEMDM SEGPKGTNGT RSSVGRLCPL WIHDDNFSKD QVLLNLALFP
RGTVKVGDLI QVVPQSAGTE NKDYEHRHDA GPRVKRSHRG GEDDEETPGR EPSTPSLEAS
AKEESAFSSG KESDASARYV FKAKEMGSEL LSRNPTLQIS ISSTIASAFG FKNRAQVMVS
AVEESKCSAS HVEINFRDEY LTRADMWRLV ISELARKPVY KGQKLLFMST IKATVHAIYV
EGKIVRSAYF NATTKPIFRS ESARYVLFIQ MSKEMWGFDT NGSGEIMFNK VINGFLPDLF
KRWQEIKARH LVSIILFSRV EYKRDIATGF VHPAVDVEDP SMQTAADNTP YKDFYRVVVS
DMASGQWSTI LQQLKREFKV FLRDVLIRKP TLRGFVANEA ETESAAIEVP KGMIAGHPSS
ATRGNILEAI NLASSQFSND YIDRDLVRTG ISIVVVTPGP GLFEVDYNLL ATTTDILIEN
GIAIDLVCLA PMPLHSVPLF KYKPPQPQSE PANIFAFGTD GSTPKGRDMT FGSYSSRVNN
LSSSNLSRSD RSLPPVASRN KTNPPNDWRY GIPHWIDVSF WVSTTEERGL HVSANKEGLK
KSKLSTKQHK TFVPRVRMYS VQMMGMMENE MSNISIPYLH QPSTFRQDRL ANINHLGSAH
PNRLNTEGTL AAVNADPNAP HNDRTYSERK AETSTSRLDS AALQWMDDYD DKLFRDPRQS
HALDKQSRQL LPARHALQAQ TLRDNYKSLL GTSPHTFQRL PSGLARSSTE SRHTERTMQN
RPVGQGKSKR KESTASTTST ASTNSQTLVK PAMLPWQISF GLRGFGAPAP KALASTEISS
EQAKPTSASN RGLRLQSRTR VKEAGLPAQA KRASQEYNDP RIELLSPRGL EALRASTTRP
IAIRCTTAIR VSGHSHQHSI KAEIEAREPS NEGQPRGRLG ILGKASLRKQ NGPTVNLDHH
YSPQEAPAAL SPGSAMAPWL TVLNPSNPHK MDNDLASRLG RWQHVYPRRL RASTIKWKSL
CSPASIPLTT EQFPTADQLV AEYQESPYRI ALHEEEDLPE MPKSREWLVR ELISFRLSHG
FQIVVGPRLS QAVAKPLSEV FDIFDDKYLS QDGTVIFLSR GSTIHQLSCI EEGEVEVKRY
TRRPMASVDL GSNEEISLAY KPAIRTMLAD TYDPRDMLIA SQRDEYNWHV VDSFIAGHEE
QQAGRFAEHL RFWRARFVLI PVDPPSSARR PLQTLNEDNE EEIRLEGIRK LTQVWQRYRY
IPPDERRFQA PLWTRRDTNP LDIIYQTRNP SSIIATELDR FDSTLLAEND LGGRPVKLLP
DTELYQRSNL NLASLAQTIQ GDRGVRLMDR RWHWRLHYNC FIGSDLTTWL LMNFKDVDTR
EEAIDLGNEL MKGGLFQHVE KRHNFRDGNF FYQIASEYRA PRPESRGGWF GSTRRLDRAV
PPTPVSEHLG KDSPRVSRSR SDSGNNGVSP RNGASAPVGS KQHLAVALSK SLRYDVDHRK
RSYRPEVINL HYDRVHNPDN CYHIQIDWMN VTSKLIEDAI VSWATSAERF GLRLVEVPIG
EASTINGTHP FRAPYLVKLA HHPPNRQPEE DPEASSFTPR PRAEDHYYQT ALLKNFNFVL
DLEAAKDFPL HVEVTYSWGR PDYKYPQYIH RSGVVLAQII DDGNIILLEN KLYNNRSAAA
NDPGKVDSDE FHDRGAGGPK FHQPGRGTGS PFGGSPQVTP FSSPLVRASP DSLGAGYGRP
GLAPAFIRPE TEKIKNELEA FCHNSDTLKK FYEDVLSTAM SPASASPYMD GSIPILGLPP
SLSLREMSSS PSPASSKTRA ENGVTQHSPL A
//
