ID NOP12_YARLI Reviewed; 509 AA. AC Q6C2Q7; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 22-FEB-2023, entry version 95. DE RecName: Full=Nucleolar protein 12; GN Name=NOP12; OrderedLocusNames=YALI0F05918g; OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=284591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Involved in pre-25S rRNA processing. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RRM RBM34 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR382132; CAG77862.1; -; Genomic_DNA. DR RefSeq; XP_505055.1; XM_505055.1. DR AlphaFoldDB; Q6C2Q7; -. DR SMR; Q6C2Q7; -. DR STRING; 4952.CAG77862; -. DR EnsemblFungi; CAG77862; CAG77862; YALI0_F05918g. DR GeneID; 2908470; -. DR KEGG; yli:YALI0F05918g; -. DR VEuPathDB; FungiDB:YALI0_F05918g; -. DR HOGENOM; CLU_006468_0_0_1; -. DR InParanoid; Q6C2Q7; -. DR OMA; QFHDENA; -. DR OrthoDB; 36980at2759; -. DR Proteomes; UP000001300; Chromosome F. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR CDD; cd12669; RRM1_Nop12p_like; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR034777; Nop12_RRM1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23236; EUKARYOTIC TRANSLATION INITIATION FACTOR 4B/4H; 1. DR PANTHER; PTHR23236:SF25; RNA-BINDING PROTEIN 34; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. PE 3: Inferred from homology; KW Coiled coil; Nucleus; Reference proteome; Repeat; Ribosome biogenesis; KW RNA-binding; rRNA processing. FT CHAIN 1..509 FT /note="Nucleolar protein 12" FT /id="PRO_0000081674" FT DOMAIN 168..266 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 274..359 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 345..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 419..509 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 33..114 FT /evidence="ECO:0000255" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..84 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 85..133 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..393 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 475..502 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 509 AA; 57053 MW; BBF37FDB0FB732E9 CRC64; MTTTKDNSGL AALFANSSGP RQKPQRAGKV DPVRDQQEDK MEVEDEEEDE EEDEEDEEED EEDEEDEEEK EEDDDDDDDE EEIEEPVIKK SKKNKKSKEE SADLEDQYMA KLAEEVAEEK PMVAETSAEE IKVDEPESDS EDEPELDVDE ETKKKLEATN KELDKADYTI FVGNVSSEVI TDKTVYNNFK ALFAAIGTVA SVRFRSISFS KLLPRKVAFI SQQFHSKRDT VNAYIVFKNV KSVKGALTLN GSVFKGFHMR VDSVAHPGAQ DHKRCVFVGA LDFEEQEESL WEAFSSCGDV EYVRIVRDPK TNVGKGFAYV QFKDVNSVEQ ALLLNGKGIN ELSKSTTNKR KLRVSRAKSQ HSQERAKQAD MKNIRNAKTE GLSRDEKSHF GRAQSRLGKA GKAQLQSIVQ EGLRAKKEDG KVNLARSKRR GVKPNKNRVE KPGQSRAEKR KAMFGTPTNG APGAGGKKKR LTTRSQKFKQ DGGVKKDGDA KKDGPKKERD GSKKGSKKN //