ID A0A318ZP36_9EURO Unreviewed; 431 AA.
AC A0A318ZP36;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=SMP-LTD domain-containing protein {ECO:0000259|PROSITE:PS51847};
DE Flags: Fragment;
GN ORFNames=BP01DRAFT_356291 {ECO:0000313|EMBL:PYH45670.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH45670.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH45670.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH45670.1,
RC ECO:0000313|Proteomes:UP000248349};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ821230; PYH45670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZP36; -.
DR STRING; 1450539.A0A318ZP36; -.
DR OrthoDB; 5559at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0032865; C:ERMES complex; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR CDD; cd21672; SMP_Mdm12; 1.
DR HAMAP; MF_03104; Mdm12; 1.
DR InterPro; IPR027532; Mdm12.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR28204; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 12; 1.
DR PANTHER; PTHR28204:SF1; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 12; 1.
DR Pfam; PF10296; MMM1; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 1..431
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 187..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 431
FT /evidence="ECO:0000313|EMBL:PYH45670.1"
SQ SEQUENCE 431 AA; 47519 MW; 02CBAE7662DA2CB9 CRC64;
MSIEVDWGTA TSGPDGEALA ERIRSFIHDK FQQVALPRFI RSVQVHSFDF GTIPPELEIK
DFCEPFADFY EEDEDDEASD VSEELVAGHG TQWVRTGSEL SEPPFQDENA MHQPLRNPFD
ERFQPSPLRS PIALGDHLNP HFLPRAGTPG IPGGTSTLGY HLMSLGGLSG TQTPLAAVAG
GNPFANSWND ASSREPRSRG PLSTSALDGT HPQYPEAELD GSNPTSRPST SSTLPPHPPG
PNTGTGEATA RTEENAHLDV DDDAASTEPL RLPRMRERRP EDFQVLCHVK YRGDVRLSLT
AEILLDYPMP SFVGLPLKLN VTGITFDGVA VIAHIRKRVH FCFLSPEDAD ALLGSDQQDA
AAGTQEDKPR PEPVKRHGGL LEEIRVESEI GRKEDGKQVL KNVGKVERFV LAQVRRIFEE
EFVYPSFWTF L
//
