ID A0A165G063_9APHY Unreviewed; 955 AA.
AC A0A165G063;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Utp21-domain-containing protein {ECO:0000313|EMBL:KZT09652.1};
GN ORFNames=LAESUDRAFT_735308 {ECO:0000313|EMBL:KZT09652.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT09652.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT09652.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT09652.1,
RC ECO:0000313|Proteomes:UP000076871};
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; KV427611; KZT09652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165G063; -.
DR STRING; 1314785.A0A165G063; -.
DR InParanoid; A0A165G063; -.
DR OrthoDB; 5477616at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0032040; C:small-subunit processome; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR007319; SSU_processome_Utp21.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22840; WD REPEAT-CONTAINING PROTEIN 36; 1.
DR PANTHER; PTHR22840:SF12; WD REPEAT-CONTAINING PROTEIN 36; 1.
DR Pfam; PF04192; Utp21; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 313..344
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 621..662
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 753..952
FT /note="Small-subunit processome Utp21"
FT /evidence="ECO:0000259|Pfam:PF04192"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 909..936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 105021 MW; DF7D0E365F74371D CRC64;
MSTNSEMEHS HPPPRKRPRV GQTDSKKTST EPRLFAPFRA LGLITNHLPF VLQTRSYKGS
TEGPRLHLVT CLGKAWAMWE GGKMGLLFVG PDAPEPITYM AMEGNSVWTA SGPNVIRYIR
GKETGRLVNP LGTTISFILV FGSQLLALTD DGSRMLAWDV ESEELQATIQ FDTNFIATSI
LHPATYLNKV LVSSSQGDIQ LWNIRTQTRI HTFPVASLLT LPTNSQSSLT NPISALVQSP
AIDVVGIGFA SGEISVYDVR TDERLMRMKM QDGAVRALSF RSDGQAILAS ASSIGHIALW
DLNAGGRLLH LMRGAHDGAV TSVEWVPGQP LLISSGEDNS VKQWVFDSPT SPPRLLKFRS
GHHAPPHLIR YYGEDGKQIL TASRDRSLRC TSVVRDSRSF EFSQGSLSKK ATSQSIPVAS
LKLPPINAVS YSAARARDWD DILTAHADET FARTWSMKEK KIGKYAFGFG NGGKKGAPVG
SVKAVCVSAC GNFGLASSST GAIHMYNMQS GILRKTYSVG PCPPEVTSKF RPTGSTKKKL
EERCITGLAT DALNGSVVAS TLDGTVNFFD FHTAKLEHTL VLPSSAVSIT LHRDSGLLAV
ICDDLLVRIV DIETRRVVRE LGGFRGRVLD VTFSPDSRWL VTTSLDSIIR TFDIPTGRLI
DAFRTASVAT SVTFSPTNDF LATAHVDSVG VYLWANRAQY SEVSFQSVSD EDVQDVSLPS
MQGEAEEEAL DALSSLTLNG QETLPDVFLT QSNLDGDLVT FSLLPRSKWQ TLLNFEVIQQ
RNKPKEPPKE PERAPFFLPT LPGLEPRFAI EEKESDANAP KSTKRLQKAA ASSTSVFYKK
LAAEKPEGDY EEFFAYAKTL SPAALDLELH ELVTLDALRL FLKALHDRLC SHRDFEAVQT
FLNVFLRMHG DVLMENEELH QELEALQEAQ RKESEKLVEL LAWSLGTLSF VRDTL
//