ID A0A165T546_9APHY Unreviewed; 1120 AA.
AC A0A165T546;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=SMP-LTD domain-containing protein {ECO:0000259|PROSITE:PS51847};
GN ORFNames=DAEQUDRAFT_704734 {ECO:0000313|EMBL:KZT72943.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72943.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72943.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72943.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429039; KZT72943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165T546; -.
DR STRING; 1314783.A0A165T546; -.
DR OrthoDB; 25272at2759; -.
DR Proteomes; UP000076727; 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 InterPro; IPR019411; MMM1_dom.
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 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:UP000076727};
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 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..482
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 47..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 120326 MW; 54126B176F4A8F33 CRC64;
MSLKALLYAY VLGGITFIPL LVLGAIFYTI YTAVPVEEVE AKKAPQSAEV SEPLDLPSTT
AAPSPSEIND APRVRKGWLT VRRTFEEQPS DSSYVNMVRG FLDARSKDAR RSRPKDMWYV
VLKGKVLYLY EDESMTECEA AIELSGHEVV VYPEGLLDGE LFSRRNAICL KPKVPPPSKE
MPSVTKEMKL GGEDVDEKLD EASGSSRSKQ RQREQILETE RRREDARTQA LDLATPWFIF
VKNVVDMEDW YHTFIHASDN PANAGTLSPL EQVFRPEDMS HLVSTLDEQP DVIPMRWLNA
LLGRIFFSYY RTQALESYII GRLMKKISKV KRPGFLSDIN VREVSVGNKA PTLSKPMLKE
LTKEGDASFE IHVHYKGEVR ITVEATATIN LGARFKTYTV KLVLALVVRE VEGNLLVKVK
RPPSSRIWYA FTQMPRMVMA VEPVVSDRQI TWGMILSTIE SRVREVIQDS VVLPNMDDIS
FFESVKYLRR GGIWADASRM RGDAPYGQGE DDGDDTSSTV SASGAELSKP MPTDPEHPPV
QRSYSAEQAK TEAKIVSDAQ EIFVNLRREA TAVSLPSSPA ANISSDSRRR TWFGTLNEDD
ADALKLGSGG EADRRGRTPD SEHTLTRRSS STPIASSDDT TTQPTETQQL REDYLAPSVA
RRSSSQHSQS SSRGTSSSAT DDESAGGAGD SSSSSRRSKS PGIGNSSGRS NTTSSTAAFL
QTLKSRAGDK QALSNTAKEA MRKWGVNWSG LRKDSVNSGT SEDVADGASA PQDETRLRAN
SAAHRSRPSY AEVRAAVEQR KHHDGTLGAD LRSDPISIPQ SGKGKERARS VSPSQVGGGG
NSSGGGSPYL APPLPTSPRP EARSPSPTFP LERTASGRSV QGLVVDEPEE RPPAPIHTQP
PQAKSMTIPG IHASHRGEVM SMGYAPPPRA SPPEKKPAIQ SVYRLWKNPG AAGGQTPRGT
ESPAVAQMQT DFPGHDHESA SAGVAAAPVV PSTSDAQAQP EVVSPRPIPP PLPPRIISGT
LRKASGGGAA TAEQNASAAS AALQSIVSKD RSKRASLEPA PPPGSGEANT AVSNGAAAGS
PAANAGPDSG GGEGGSLRAP KPVPPALPPR RTPAATPAPA
//
