ID A0A319E747_ASPSB Unreviewed; 788 AA.
AC A0A319E747;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Putative SAM and PH domain protein {ECO:0000313|EMBL:PYI05721.1};
GN ORFNames=BO78DRAFT_470347 {ECO:0000313|EMBL:PYI05721.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI05721.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI05721.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI05721.1,
RC ECO:0000313|Proteomes:UP000248423};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ826355; PYI05721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319E747; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:UP000248423};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 164..228
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 632..770
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 230..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 87415 MW; C971A7BB09E75C36 CRC64;
MNYFHMLSDP TVSDTDTTEI LDTDFESDSY DTYSDDSRYL SGHSLATESV TTASTPDDIK
TPDSTGLTAF HFQLDEYPVK GPVGPHLFRV SSDYSDTTTS SFGFDLTIED ISTNATSPLY
QSVTRLEPER KDTPVPIATV ADAQKAPAEA RVRPQPKESE VANWTPKDVV MWMEKHGFDD
SVIEKFFIND ITGTILLELQ AEDLKELEIQ SFGKRHRLMG CIRELRSKAS SVTCDSPSTS
DPISREDTST PKTTAAEVGV DCPCPSPSPS TDDDKSRSKS SQHRRRRRQK RQDGTDIVPE
DSVSIVAIEQ LLPRLHTCSK GENCRKWQKQ QVKLARLAKG LPVEGLGGSV LITGDPGNPA
TAQNLAKTPK SEVTPSVIAS SDALGNNHAA ALQLSQDKLH VVQPRDPQEN VRQFLSFQRL
SKLQPANNPA TPPQEHFSPG SGSPGSARAN PTLSENLRHL PKLRIPSSDA DTSSMLSPNY
SAQRTITPSI LQRRQPFARQ GTKKSLEPLE RGVSPSDFYR IDPHYGQSTP LSEMDVPVTA
IPIGPVARNF SQSVPPDMRF GGDMHRVPDV IPRPASTRPE NSRRNAFFSD GQNMPTLNHL
EKRMLLPPIE TPEDMETTPR AANCKAPITS NSVIHSGWMK KRKTTRFLRH DWEDHHFTLR
GTQLAMHSDE EASHRDSKAL EYIDVDDYAV ACSSFPSNSK LTAAFKKTVL KRKDTLHGEA
AFAFSLIPSP TNSTFDKKLI FTNGPKTHHF AVKTRDERID WMRELMLAKA LRKSREGGVS
VNHNGNFL
//