ID A0A395H471_9EURO Unreviewed; 1836 AA.
AC A0A395H471;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=BO80DRAFT_43201 {ECO:0000313|EMBL:RAL02249.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL02249.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL02249.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL02249.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ824432; RAL02249.1; -; Genomic_DNA.
DR STRING; 1448316.A0A395H471; -.
DR VEuPathDB; FungiDB:BO80DRAFT_43201; -.
DR OrthoDB; 946033at2759; -.
DR Proteomes; UP000249402; 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:UP000249402}.
FT DOMAIN 1338..1413
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 726..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1836 AA; 206435 MW; D8186B5CC5884F4B CRC64;
MSLRGPMKRS HLRQVSAASI DTLSSSRTLE LPPRGTPRER DRDRSSTPDE KVPRLASTGL
DRRQCSLWVH DETFSREEIL FNQAAFSDTG VQVGDIIEIL PARFAGDAPH SAKAELGARS
LRGSHVDLTS LLPADPRSKF KTPLQGRCLF VVKPLPQEIK SRHSKLELSV TSSVANIFGF
KNRSAVHISI VERAQCSASH VDISFRDQYL VRSDMWRLVM SELSEKIVYK GQKIVFMGSI
KATVKNIFIR GKKVLSGFFS PQTIPVFRSE SAKYVLFIQM SREMWDFDSE GTGDILFSRV
INGFLPELFK RWASSDARHL VTIVLFTRVE YDPSAIGPSS SLNTDSWTNE FTPNGAPTRD
FYRVVVNDMA SGHWTTILDE LKKDFRTFLR DVSILKTTDD VKTPTIDGVK VAPKAQSATI
AGRPSTALRG NILEAIHLAS SHLAYDHIDR DMVHTGTSII VITPGSGVFE VSYESLASTT
EALTNRGIAI DLVCLSPMPL HSVPLFKYRE PVQKSPSPSY GADIQAGGYS PEARLSFASL
ASRGSHLSPK STLHSSFPGI SARHWSSRLS EWNYGIPHWL DISYWNPETY REARRILKKD
PNAPIPFTVT KQSKVFVPRV RMYEIQMMGV MESEQSNISI PYLLEGQGVT RRSNPAMGLS
PASLSPANMP LTRNTSFRHQ LSDSLRPEPF LQNIASSKDA ILAKSRKSSN SALTWMDHYD
EAVFQPFPHR RQRRKPPKQK RTSEPEVQVS NAHDRLSARS VTRLRENESN SSERAQSTFS
APRNIDATLP VPKNPVSTRT VSPKKPALKA PSATRMPRIS RTISFALRGL SATPPRAQAS
TEVNVEHAKG QSTSNPKKIA GMLADSRSVD SLSISDSAST KTVIDLSSTP TTPQKQAHGS
TITPSRPISI KVPPKQPSQD PEQAERPITE SFSTTTTEIP ISDEARPESR TKRPNPRVTL
TVNGSSRDAA SKSPQSKALA PWVRSINPCN TPKDVLRDTS WFGRWQHAYP RPPHVAVVKW
KSLKSPAILP LTTEEFPTAS ELASDYFQTP YRVFPNDDAE GIEPPRTRGV LLREMISLRL
SHGFQIVVGK HVVEVSGQYS LEAPNVFDTH SLERDGATVF LSKGNTIHRL VCIDGAEIEV
TRYTHRNASV LASPQINNFT LYSPAMRTIL SPQYEVKHIR LDSTMEEYNW NYADNYVAGH
REYLFSPAQQ LQFWRARYVL IPMHLQVNAR RQLQSFNEDN EEEIHLLGIN QLTHIWQRHK
YVPPEEKLFD TSSKKREQNP LNIMYQTRNS SEVVAAELDR ILLTDPGLDN SPAQLLPESE
LLERSSIGLS SLAQLIQGDK GVRMMDRRWH WRLHYNCFIG FELTTWLLHN FRDIDSREEA
VEFGNELMKH GLFQHVEKRH NFRDGNYFYQ ISSEFRASRP ESRGGWFPQI RPDKPIASTP
AGDNPRDSPI SGHSRSESLD EAAPQPVPHT PSKLKNKAAI MLSKTMKYDV DPRKRSNRPE
VIDLHYDRLH NPDNCFHIEL SWMNTTAKLI EDAVLSWAST AEKFGLKLVQ VPIAEACAID
ETQPFRKPYR VQLKVPPPKG PVPSLFQAAT FTQPVAPDRH YFQKALLRKF DFVLDFEARS
AFPADVEVSY SWGIPDYRYP QYIHRSGSIL AQITDEGDFL FLANRLVSTR TTPSRDIPRH
ERLERDQFRT RAGTYDPGDR LSPRLSPMAR PVHDVGSPRF QGQPTLDSAN LYRAPEHILN
GFVDFCRDPV RLDQFYSESH ARPTSTRVEP TSLLEASIPS LELPASVVSH HITLPPGLTS
RASHSGTLPT VESRTRSRDE GSVGRSPRSG ALRPLI
//