ID A0A2P7YVE8_9ASCO Unreviewed; 1495 AA.
AC A0A2P7YVE8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, 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=C7M61_001732 {ECO:0000313|EMBL:PSK39921.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK39921.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK39921.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK39921.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-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}.
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:PSK39921.1}.
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DR EMBL; PYFQ01000002; PSK39921.1; -; Genomic_DNA.
DR STRING; 418784.A0A2P7YVE8; -.
DR EnsemblFungi; C7M61_001732_t1; PSK39921.1; C7M61_001732.
DR VEuPathDB; FungiDB:C7M61_001732; -.
DR OrthoDB; 946033at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:1990130; C:GATOR1 complex; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IEA:EnsemblFungi.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:EnsemblFungi.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:EnsemblFungi.
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:UP000241107}.
FT DOMAIN 1079..1154
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 171633 MW; 90C7CAB84C3EF70E CRC64;
MQHARWTNGR AKTPVNDNDD LTKYLRKSPE VPMGRLQPKA STLTVGNMSL NTPGSTLTVG
KHKVTTSAGV RHGHNFRSFT DPVAYNKQNA RNINSSQASA SALVDDTTLD DPIQLTVWFH
EPRSYTEDVV IDASAVPGVK EGGIYCLEPV LKDDQRRTKS RRFVFTALKE NIIRDSNAKG
KSNLQISLLS TPLQKLLDIP PRSPVLLQRI RDISEVELDT VEIYLKDVNF PRDSQWGLAS
AFVGKCCYMD QRVLYLGNRV GQIRLTFKDG KKLFRGYVGE KTNIIFRSES AKLVFLVQMS
REMWHFEENG EIMFHKLVNT LFPKIFKKWL SASSHHSITI VLFTSIDLTQ IPWISLGPGE
RPSKSQEYYR VVVDQVSVFS WDKIMASLRL EFANFKRDVL VHLTDNYYKI SGEPCPAVKG
NLLEAVNLTI INHMIVVTPG TGLYDVDYDL MLETSKKMFS LDCALDIVSL SQPPLHTVPL
LRFRDTKGLV GHCVPKWCDI SFYTDTDEWS SQWIPRCKIY ELQMMGVMEN EINEILIDRL
TLRKEMPVVE AMDIYDDDAF KPISRKRTIP VKKTNSGKIL LEKRSTATLS LMGKFPLSTI
NIPQLAPETA KSNVSTTTSA VHGTVLNIPS DTSALSTLYT LNRTVDEPQN RGTPLGRERS
TTPSEASISL AVRVHPARRF EQVIRPKILK PPDNKKRKSK RSSNDGTLEK ISKSKKVSTE
EKEREERLKN NPYWMKISNP SRELASESIR CSRWADVFPP QIKRKLVKWR SLKAPAALPI
ATTLFPTVKE LETEYTFQIY VVSLNFENKL ELRTTHQLMR EMIRLRLATG FQICQGESVR
NAEAERKPSG SPESLIKYMP QGNCTGARIY LSLNDEIHRI FCDYNGTLNV QLYRRSQPQE
APKNTFGRQK HDEASKPLIR TRYADEYTPT AITAQGTKPY TYNWNQFDQL LAGYDDAVGE
TREFHKMKFV VMPGDMPQNA HHIGNDSLSD EEIRVEGLRK LISVIERGRY VRLDEKKPKK
KEEILPEINF YTGNLFDFLN EQAEIFASSG TQPTNSLMVS DAKFNTNIKL STLAERLQSP
GGLKLVDRTW HFKVHPLCFL GQELVSWLIE FFDDIDNREE ATAYGQKIMD EGLFTHVENR
HGFLDGHYFY ELTEGYAKLA SNSKQNSSGW FRKKASIETD KVDTSGQQSP KLTTQVSNTL
GHTRNNSDTI SSLSGIESTS TFRKLIPQFT NNESENLSLT DSQKARKLNK FMISKHVRYD
CDPLKKSFRS ELLDVHYDIV HNPEHCYHIR VQWLNTTNKF IDETIISWSR LCERYGLKLV
ETPWRELCTL PKMNPFHSFV DLKLVVNPVN DAEFNETPEF LNNRFYYHLY LLKKAGFLLD
NRGSNFFLRE NIEIQYSWGL PLFKYAQFIH KTGAYIVELR DSGDFFMAPN NVHILRVNTL
VNAIPEQNNN LKNYSFDSQK VMMDFRELCK DEEYLRNIFR EAKKGDREDY DYNIA
//
