ID A0A1E4RD74_9ASCO Unreviewed; 1142 AA.
AC A0A1E4RD74;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=SMP-LTD domain-containing protein {ECO:0000259|PROSITE:PS51847};
GN ORFNames=HYPBUDRAFT_168653 {ECO:0000313|EMBL:ODV65201.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV65201.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV454545; ODV65201.1; -; Genomic_DNA.
DR RefSeq; XP_020074268.1; XM_020222813.1.
DR AlphaFoldDB; A0A1E4RD74; -.
DR STRING; 984485.A0A1E4RD74; -.
DR GeneID; 30997362; -.
DR OrthoDB; 25272at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd21675; SMP_TEX2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR13466:SF0; SMP-LTD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13466; TEX2 PROTEIN-RELATED; 1.
DR Pfam; PF10296; MMM1; 1.
DR Pfam; PF15413; PH_11; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095085};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 595..784
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 129647 MW; 28359CB45F96AD20 CRC64;
MSTIQSPALK KRRLNDEDDH DKIDPVEKLL SLTTFNNDIL LDIDQEQQQQ QEEEDGEESD
SEDSEYESEE ESSNISLNFS KILNENIRNY YSNLKRCPIE IYNDNSSFAL LNKQQQPQEQ
PKQPPQQQEV PFFKNVNFNP KPQSAYTFDE YLSYDDDEPT TPSTPTVLPN NKMSFHYRHH
DNLNLSTTNH STNEPQDIFK ILNKRSVLSG KASEMVCSLQ VSTIILMLTW FGHGSSFTTL
FGYNRFCFNV ELKIVPAASR DHTGKGGVPV GFCFFPPYFE GTEKGLNMGL TLLIYTYLIG
GLTFLPGLVI IFVYLHPIFQ EEQEEEQEQE FIGKKLKAGE IEELNQLGLD TYKVGWITVT
QEYLESIDEI TSSTQSISDS TSNKSAYSSL YKLVKDSEDP INNSSNSSIK EQPNTTTNTT
TNTNKSSNQK KHRYYAILKH GNLFLYKNEK LKDVKHVIVL SNHMISIWPK GLTDAQLFTK
YTSISIMKKN WSRNRRLSDN YESNLSHDEF NDSPKKLNIL DVLDPNNKLK PPPGSFFIYC
DNNSDKEDWY FALIRATKID DDSNKLIDPR IHAKTLHFET SNMMDLIQTL YSSEGQLNTK
WLNALIGRIF LSLQKTELLS NFLKKRIDKK LNKIKTPGFL DKFQIVDLTT GNSAPFITFP
ELKEINPNGE VLVSSYIHYF GSMSLKIKTK LNINLGFKPR EVDVLLKITL VKLQGPLIIK
FKPPPSNRLW YTFEKEPLIN LKIEPIISSR QLTYNIITNT IEKKFKEAIK ESLVLPFWDD
FAYYDTENEF FRGGIWDKTE RENLNTNNNS TEENLEVYDS NSIDNASMKS SLKTDDSSIN
LDKASSTTEL SSSKPSNSRL KISNTFNDIS KKLKKPRSQT QLNANLDEES ELSTEPISSS
PSIKSSSTIP SKSKDLSGDT ASSKKSISTL KKIGKWYFKD DKALTTTSDQ EITYTPPEMI
SNRRSSPRKS SFSSNKSTQD VAFKSNSMSP TYDFGSRFPL NGFISGNFDG GSNSSETTNE
NDIEPDLKSR PTSIELKSTF HQNDTQIPIS KNDDNSTFDS DLSKTEKADL ISNLKILPPD
EDSDVTQGST PATEEPPSVN ISPANSSNET HGPIPKNLYR KPPPNDTPPL APTNERDLIE
DI
//
