ID A0A2G7FG11_9EURO Unreviewed; 2343 AA.
AC A0A2G7FG11;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AARAC_000335 {ECO:0000313|EMBL:PIG79557.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG79557.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG79557.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG79557.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-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}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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:PIG79557.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NEXV01000676; PIG79557.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7FG11; -.
DR OrthoDB; 946033at2759; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04449; DEP_DEPDC5-like; 1.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06593; GH31_xylosidase_YicI; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR Pfam; PF12257; IML1; 2.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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:UP000231358}.
FT DOMAIN 1173..1248
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 22..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2343 AA; 264853 MW; 4C51C663A6A9E446 CRC64;
MKHSHLRQVS AASLETLSTT RSLALSQTDG QSDKPSTPDE KTIRLSSTGL DRRQCSLWVH
DETFSKEEIL FNQAAFTDMG VEVGDVIEIL PARCPGDGTH SGKTDLGSRS LRDSHVESSS
TLHSDSMSKF KTPLQSRCLF VVKPLPQDIK TRNPKLELSV TTSIANIFGF KNRTTVHISI
VDRAQCAASH VDISFRDQYM VRSDMWRLVM SELAERIVYK GQKIVFTGSI KATVKNIFIR
GKKVLSGFFS PQTIPVFRSE SAKYVLFIQM SREMWDFDSE GTGDILFSRV INGFLPELFK
RHFNYSHSPG SGVFEVSYES LASTTEALTN RGIAIDLVCL SPMPLHSVPL FKYREPAHRP
STAIFGDIQH GGYSPEMRHS FASLSSKTPH LSPKSALLDS FTGISSKSQW SGQSNEWNYG
IPHWLDISYW NPETYRESRR ILKKDPNAPI PFTVTKQSKV FVPRVRMYEI QMMGVMESEQ
SNISIPYLSE GPNISRAASS TLGSSPGSLV PPKATFRRNS PFRHQLSDSL RPEPFLHNMA
SSKDAMLTIS KKTPKTVLSW MDNYDENVFQ SFRKRRHHRK PSKIKRPSEP EVKASNAHER
ISARSISRLR ENESTRSASR QIDIPLSAPK SPVSTKSASP KKPALKSSSK AKLPRISRTI
SFALRGLSST PPRAQASTEV NVEHARGLPT SNSRKLSGVL ADNRSVDSLS ASDSASTVID
LAPSPETPQK PIKNTAITPS KPISIKVPPK QPLQDTEQQG RPAIPESVST TTTEIPLGDD
TRLTAQPRRH GPKFEVTLSS GSRNGSSKSP QSKALAPWVR SVNPCNTPRE VLRDTSWFGR
WQHAYPRPPH VAVVKWKSLK SPAILPLTTE EFPTPSELAS DYLQTPYRVF PNEDSEGIEA
PKTRGVLLRE MISLRLSHGF QIVVGKNVVE ASGQYTLQSP NVFDTHSLER AGATVFLSKG
NSIHRLICVE GAEIEVTRYT HRTSSLLASD QKRKFTLYSP AMRTILSPEY VVKDIKLDST
YEEYNWNYAD NYVAGHRDYL FNPVQQLHFW RVRYVLIPMR LHFKSRRLHG FNEDNEEEIH
LLGINQLTHI WQRHKYIPPE EKRFESSNKK RDQNPLNIMY QTRNPSEVIA AELDRIILVD
PGLDSSPAQL LPESELLERS GISLSSLAQI IQGEKGVRMM DRRWHWRLHY NCFIGFEFTT
WLLQNFRDID SREEAVEFGN ELMKHGLFQH VEKRHNFRDG NYFYQISSEY RVSRPESRGS
WFPQIRPDKS VPSTPAGEAS KGSPISGHTR SDSIEDTQSL TPSTPSKLKN KASITLSKTM
KYDVDPRKRS NRPEVIDLHY DRLHNPENCF HIELSWMNTT PKLIEDTILS WASTAEKFGL
KLVQVPIAEA CAIDKTQPFR KPYCVQLKVP PPKGPIPLQC NSESFSRPVT LDHQYFHKAL
LRKFDFVLDF EARSSYPADV EVSYSWGMPD YQYPQYIHRS GSVLVQITGE GDFLLLANRL
VSTRSAASRD MQRHERLERP DQYRARAGTY DPVDRISPRL SPMARPVHEV HSPLSPQGHA
SIDSANLYRA PEHILTGFAD FCNDPARLEQ FYSEAQEGIR IDWMNNVERL HINNEKVNLL
LNKFQRHRGD TLNSATVTAS VTSPLEGIIG VKLVHWAGQV DNGPHYQLSS STGHTKIDHE
KNVKLNYGSG PLNLAINTAP NELNFVFSGA KGKLTGHSWR SIGYVGDQTT EKSRWDDGIF
FERQGYMLAA LDLGVGEKLY GLGERFGPFV KNGQSVDIWN EDGGTSSELT YKNIPFYISS
KGYGVFVNNP GKVSLELQSE RTTRVNISIA GEELEYFVVY GNTPKEIIRR YTALTGRPSL
VPSWSYNLWL TTSFTTNYDE QTVTGFLDGF RDRDIPLGVF HFDCFWMKSY QWCDFEFDSE
MFPDAGGYLL RLKERDLRIS VWINPYVGQA SPLFDEGKKN GYFIKRTDGS VWQWDYWQAG
MAVVDFTNPA ACTWFSNHLK RLMDMGVDSF KTDFAERIPY RNVQYHDGSD PTRMHNYYTL
LFNKVVYETM TDRYGKSNSL LFARSTSPGG QIYPVHWGGD CESTYEAMAE SLRGGLSLML
SGYIFWASDI GGFEGTPPPA LYKRWVQFGL LSSHSRLHGS SSFRVPWIYG EDCSEVLRDC
VKRKILLTPY LLAEALTGHD QGTPLMRPMF VEFPDDLNTY PLDTQYMFGS NLLVAPVFTD
EGTVTFYVPR TPEESQGKWI SWFDHSKTYE SGQWYTETHG FDTLPILVRP GSVTPINPKL
KGPQDDALDG LELLVNGSLT DEVAVQVVDP SKTHEVLKTV KVAVKGDEVV ADAAGVKVVR
VRH
//
