ID G0SUG1_RHOT2 Unreviewed; 1482 AA.
AC G0SUG1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=PIN domain-containing protein {ECO:0000259|SMART:SM00670};
GN ORFNames=RTG_00068 {ECO:0000313|EMBL:EGU13631.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU13631.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU13631.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU13631.1}.
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DR EMBL; AEVR02000026; EGU13631.1; -; Genomic_DNA.
DR HOGENOM; CLU_003327_1_0_1; -.
DR InParanoid; G0SUG1; -.
DR Proteomes; UP000006141; Unassembled WGS sequence.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:UniProt.
DR CDD; cd09880; PIN_Smg5-6-like; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696:SF39; EST_SMG-LIKE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR15696; SMG-7 SUPPRESSOR WITH MORPHOLOGICAL EFFECT ON GENITALIA PROTEIN 7; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006141}.
FT DOMAIN 1293..1458
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 161663 MW; FC11CDD6BAB93C77 CRC64;
MTTAAPLHPP SLSMRTNDAQ ATAGHASPTK HRARLNNPAA LIDGWRQTLR SRSPAEQATP
TAQPHSPVRG QQEYVQGQYG AAGTCAGAGY GGPRRVPPSV VSSSNRLSTN PSLLSLDRPA
SPSTTVDPYG APPPSSPRYA APSPPTAALP APGYRHSSHA PQPAYQPAFS HSNRSHASLP
PYASGSGGGR HPFAKSHQHA PPAQHPHQRP GRYDADYDRS LPVSAPSATS SGGATAGPSR
ELYDPRSPTF PSPTQAPLPP PVPPIHRSSR TPAAHPSDSA PRHRREREVR EDGGLGSSSS
RRPARSKREA VDPADLGRRA GAGASGSRAD AHAKDSKESL ESVETDFSGR TRSSGRQRRR
RREGDEEAEG DGGAGGAAGR SRQLFDPRKD DPMRFTQAAP APSGRTKDVR SLANGSVLSF
QSSMSDVMAS PAGGSDYTAP GGADDGASIL TGGSARSRSS QHPALAHIKR LYKEITTLEA
QLQEENRAAQ AAASRDAEGE EGKAAGVRIQ GQAKRFDDEY WVKLASRHKQ LVEAHFEFLK
FALDPSHPAS FHSLPQRYNI PTRLWQTAFH QLLERMRHAV LASPFRPDSA SSSSANVLEH
LIEYCQWAYT FYSQLLDEPL VASLQAAWIE QLGDLARYRM AVAGLASRVH AAQQQTLAPA
SLTVAALDAH EKGEAEDAKP PRPADAASIG QAALNDWDLE EQETWREIAK DWYGQGLAEN
PGTGRLQHHL ALLSKGDELR SLYHYCKSLT AAHPYVSARE SILPLFEDEH QARRTQPDVT
KAELFVHLHG MLFTKISLDD FDECLERFVE RLKEEGWALN KAKEDWTSME QDANAPFGDR
EWFMLGIINI AALLQYGAED GVLRKLMNRD SSDAPEAAGS SRRQGQHTSN RHGASASNNK
TRLAPQAIMV KRAEEPVQSS AVSDIGDDTE RASSNGTAIP GEDVVKQLNA PVPTSPEDDP
LPFKLAQRLA FSLLSVALQE PFRRLATTTI VNPYVTVFLT FLAHLSFHPA AFKHIERAVP
WQQLAELFGR IPPVVEIRLE TPAKLVGGKP LPEDWCIRGM DWAGRQLFGR GYWREHRHRS
APEVAGLPPP IEGVEGTTVR VESEMDALKF DLAALDDVTA NSTTDDDYAV GQAAPSGEAY
RSLAAQLAEG RWRRLAICAA WMVRNIPGFD FDVRAMDLEQ RFRVSGVLRD KVERWRQEDE
DAREAERLSR LALEDKVGSA GSAEEDGDES DDEEDFEDEN DSEEVKELKA RRRQLKAIIR
QARSATRSSG KASLKVKLGG KAASQPKVFP GYTILVIDTN VLLTSIKLFS ELVAAECWTI
IVPLAVVTEL DGLKRNSTPL GVAANEVIDY LEQAIRGYSR FLKIQTSRGN YLKDLAIRNE
SIDFRGGADS SYEGGDYGSS NDVARTMDDV ILRAATWQKD HFTNRVALVN PRAIVDRVKI
PSDAAQVVLI TFDRNLRLKA RARGLDVTDE KGLKKSLDAA GG
//
