ID B6QL54_TALMQ Unreviewed; 872 AA.
AC B6QL54;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=SAM and PH domain protein (Boi1), putative {ECO:0000313|EMBL:EEA21831.1};
GN ORFNames=PMAA_056230 {ECO:0000313|EMBL:EEA21831.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA21831.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995903; EEA21831.1; -; Genomic_DNA.
DR RefSeq; XP_002150440.1; XM_002150404.1.
DR AlphaFoldDB; B6QL54; -.
DR VEuPathDB; FungiDB:PMAA_056230; -.
DR HOGENOM; CLU_009306_0_0_1; -.
DR OrthoDB; 1405875at2759; -.
DR PhylomeDB; B6QL54; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR CDD; cd09535; SAM_BOI-like_fungal; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF42; CONNECTOR ENHANCER OF KSR PROTEIN CNK; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 183..247
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 714..854
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 51..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 97434 MW; 8A24EE306E759740 CRC64;
MATIDNTGYV TLEMLQALSK QSIFRRTTIG RPRSIASDAT EIFDTDFESD CDRSYNDDSS
RRSAGSLVAD SVTTADTPRD VPTPDSGALS AFDFHFDEKP IMGPNGPHLF RSSMSSDEMS
YEVDFMLAKT PTVAIFRRSV TEERRDTPLP GHDDSTEYTP QAQELKSINA AVSALDESEV
RSWSPPDVVR WMQESGFDDS VIEKFFINDI SGAILLDLRS EDLKELDIQS FGKRRHVMNS
IQHLRDSFML PNNETSTSSH DHSSTDCTSS SESASTPTKD SNKKKHRRRR NHRSHKKSLV
AHKDLNPDDS ASIVAIEQFL PKPHRCSKGE NCRKWQKQQR KIARLAKDLP IDVDAARLMS
EDYEDQPPLT SKSLPNMDPM PTPSIVASSD VLGPEQTPVF QISEEKLSEI GPRDPQENVR
QYLNFQHLSK LQPVPQVASK PDLCSSPDID SPDSIRTTTS LADNLRSLPK LTIPVNHHIV
VPGTFSASLS AQRTVTPSIL RRQPNFATNS IDGTLHSALP QPMTYGSCIS PADYVGSPSD
FYRSHDFYQQ TSPLSEIDVP VTAIMSAGPV QRHESQSVPP NMRFGHHLRV IPDPFVRPRS
TKPEIHRAGP TIQILDSVDE ARPSHDTVDV PVTAIPLGPI ERTESQSVPP NMRFGRDFYV
TVDPINRPAS TKANNYRYPS MINSALDRVD ELGPIDTEED FATTPRANPR SANDITHSGW
MRKRKTTRML RHEWEDHHFT LKGTRLAMYE DERASRRDSK AIEYIDVDDY AVACSSIPSS
SKLTAAFKKT VLKRKSSAQD EAAFAFSLIP APSGKTTGVE RRNVFVSNGK SHHFAVKTRD
ERIDWMRELM LAKALKKGKD SGDAVHVNGQ AF
//